pdb_id release_class protein_name species construct mutation focal_ligand focal_component_ids selected_annotation_index source_metric primary_metric source_qualifier qualifier value unit normalized_value_nM normalized_lower_nM normalized_upper_nM replicate_values_nM normalization_method p_activity normalization_status numeric_ready assay_type assay_context evidence_page evidence_statement selection_status selection_basis equivalent_candidate_indices activity_measurement_count source_structure_metadata label_kind protein_pdb pocket_pdb ligand_sdf ligand_pdb ligand_cif complex_pdb complex_cif 21OM classic human indoleamine 2,3-dioxygenase 2 (IDO2) human N-terminal MBP-tagged human IDO2, residues 11-420 wild-type 5-hydroxy-L-Trp (5HTP) "[""4PQ""]" 1 Kd Kd = = 1920 ± 71 μM 1920000.0 [] unit_conversion 2.7166987712964508 success True direct_binding Absorption-titration binding assay of purified IDO2 WT with tryptophan analogs. 10 Table 4 prints IDO2 Kd = 1920 ± 71 μM for 5HTP. auto_single_measurement only accepted activity measurement [1] 1 structures\21OM\21OM_metadata.json point structures/21OM/21om_protein.pdb structures/21OM/21om_pocket.pdb structures/21OM/21om_ligand.sdf structures/21OM/21om_ligand.pdb structures/21OM/21om_ligand.cif structures/21OM/21om_complex.pdb structures/21OM/21om_complex.cif 22MJ classic INPP5K human delta-INPP5K-cd, human INPP5K catalytic domain loop-substituted/deletion construct; residues 1-322 with Δ285-290 Human INPP5K residues 280-299 replaced by rat INPP5K residues 283-296, resulting in deletion of six residues (Δ285-290) CPD-1 "[""A1MDP""]" 1 IC50 IC50 = = 2.9 µM 2900.0 [] unit_conversion 5.537602002101044 success True biochemical_inhibition Fluorescence-polarization phosphatase-inhibition assay; Figure 2 reports ΔINPP5K-cd IC50 = 2.9 µM. The methods define the loop-substituted deletion construct used for crystallization. 4 Figure 2 caption: “delta-INPP5K-cd (light green curve, IC50 = 2.9 µM) by CPD-1, determined using a fluorescence polarization assay.” auto_single_measurement only accepted activity measurement [1] 1 structures\22MJ\22MJ_metadata.json point structures/22MJ/22mj_protein.pdb structures/22MJ/22mj_pocket.pdb structures/22MJ/22mj_ligand.sdf structures/22MJ/22mj_ligand.pdb structures/22MJ/22mj_ligand.cif structures/22MJ/22mj_complex.pdb structures/22MJ/22mj_complex.cif 3IX2 classic purine nucleoside phosphorylase (PNP) Mycobacterium tuberculosis Na Na acyclovir (ACY) "[""AC2""]" 1 Ki Ki = = 150 ± 46 nM 150.0 [] unit_conversion 6.823908740944319 success True biochemical_inhibition Initial-rate phosphorolysis assay at 25 °C; competitive inhibition versus inosine, with inosine 40 μM and PO4 600 μM. 9 Section 3.8 states that ACY is a competitive inhibitor of MtPNP with respect to inosine, yielding Ki = 150 ± 46 nM. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\3IX2\3IX2_metadata.json point structures/3IX2/3ix2_protein.pdb structures/3IX2/3ix2_pocket.pdb structures/3IX2/3ix2_ligand.sdf structures/3IX2/3ix2_ligand.pdb structures/3IX2/3ix2_ligand.cif structures/3IX2/3ix2_complex.pdb structures/3IX2/3ix2_complex.cif 5S3W classic SARS-CoV-2 Nsp3 macrodomain SARS-CoV-2 Na Na POB0135 "[""W2S""]" 1 IC50 IC50 = = 881 μM 881000.0 [] unit_conversion 3.055024091587952 success True biochemical_inhibition HTRF-based ADP-ribosylated peptide displacement/competition assay. 20 Figure 9H visibly reports POB0135 | 5S3W with IC50 = 881 μM in the peptide-displacement assay. auto_single_measurement only accepted activity measurement [1] 1 structures\5S3W\5S3W_metadata.json point structures/5S3W/5s3w_protein.pdb structures/5S3W/5s3w_pocket.pdb structures/5S3W/5s3w_ligand.sdf structures/5S3W/5s3w_ligand.pdb structures/5S3W/5s3w_ligand.cif structures/5S3W/5s3w_complex.pdb structures/5S3W/5s3w_complex.cif 5S4G classic SARS-CoV-2 Nsp3 macrodomain SARS-CoV-2 Na Na SF005 "[""W3S""]" 1 IC50 IC50 = = 568 μM 568000.0 [] unit_conversion 3.2456516642889808 success True biochemical_inhibition HTRF-based ADP-ribosylated-peptide displacement assay; Figure 9H. 20 Figure 9H labels “SF005 | 5S4G” with IC50 = 568 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\5S4G\5S4G_metadata.json point structures/5S4G/5s4g_protein.pdb structures/5S4G/5s4g_pocket.pdb structures/5S4G/5s4g_ligand.sdf structures/5S4G/5s4g_ligand.pdb structures/5S4G/5s4g_ligand.cif structures/5S4G/5s4g_complex.pdb structures/5S4G/5s4g_complex.cif 5S9P classic BRD4 human His-TVMV-hBRD4(44-168) Na compound 11; 9-benzyl-2-(3,5-dimethyl-1,2-oxazol-4-yl)-7-(2-hydroxypropan-2-yl)-9H-carbazole-4-carboxamide "[""YW4""]" 1 IC50 IC50 = = 4.4 nM 4.4 [] unit_conversion 8.356547323513812 success True direct_binding Time-resolved fluorescence energy transfer binding assay; N = 3. 4 Table 2 reports compound 11 BRD4 IC50 = 4.4 nM. Its footnote identifies a TR-FRET binding assay with BRD4 BD1; Figure 3 identifies compound 11 in the BRD4 (BD1) structure, PDB 5S9P. auto_single_measurement only accepted activity measurement [1] 1 structures\5S9P\5S9P_metadata.json point structures/5S9P/5s9p_protein.pdb structures/5S9P/5s9p_pocket.pdb structures/5S9P/5s9p_ligand.sdf structures/5S9P/5s9p_ligand.pdb structures/5S9P/5s9p_ligand.cif structures/5S9P/5s9p_complex.pdb structures/5S9P/5s9p_complex.cif 5S9Q classic BRD4 human His-TVMV-hBRD4(44-168) Na compound 15; 2-(3,5-dimethyl-1,2-oxazol-4-yl)-7-(2-hydroxypropan-2-yl)-9-[(S)-(oxan-4-yl)(phenyl)methyl]-9H-carbazole-4-carboxamide "[""YW7""]" 1 IC50 IC50 = = 1.0 nM 1.0 [] unit_conversion 9.0 success True direct_binding Time-resolved fluorescence energy transfer binding assay; N = 3. 4 Table 2 reports compound 15 BRD4 IC50 = 1.0 nM. Its footnote identifies a TR-FRET binding assay with BRD4 BD1; Figure 4 identifies compound 15 in the BRD4 (BD1) structure, PDB 5S9Q. auto_single_measurement only accepted activity measurement [1] 1 structures\5S9Q\5S9Q_metadata.json point structures/5S9Q/5s9q_protein.pdb structures/5S9Q/5s9q_pocket.pdb structures/5S9Q/5s9q_ligand.sdf structures/5S9Q/5s9q_ligand.pdb structures/5S9Q/5s9q_ligand.cif structures/5S9Q/5s9q_complex.pdb structures/5S9Q/5s9q_complex.cif 5S9R classic BRD4 human His-TVMV-hBRD4(44-168) Na compound 18 (BMS-986158); 2-{3-(1,4-dimethyl-1H-1,2,3-triazol-5-yl)-5-[(S)-(oxan-4-yl)(phenyl)methyl]-5H-pyrido[3,2-b]indol-7-yl}propan-2-ol "[""YWA""]" 1 IC50 IC50 = = 1.1 nM 1.1 [] unit_conversion 8.958607314841775 success True direct_binding Time-resolved fluorescence energy transfer binding assay; N = 3. Table 3 gives BRD2/3/4 IC50 values of 0.8/1.4/1.1 nM, respectively. 7 Table 3 reports compound 18 BRD2/3/4 IC50 values of 0.8/1.4/1.1 nM, respectively; the BRD4 value is 1.1 nM. The footnote identifies a TR-FRET binding assay with BRD4 BD1, and Figure 5 identifies compound 18 in BRD4 (BD1), PDB 5S9R. auto_single_measurement only accepted activity measurement [1] 1 structures\5S9R\5S9R_metadata.json point structures/5S9R/5s9r_protein.pdb structures/5S9R/5s9r_pocket.pdb structures/5S9R/5s9r_ligand.sdf structures/5S9R/5s9r_ligand.pdb structures/5S9R/5s9r_ligand.cif structures/5S9R/5s9r_complex.pdb structures/5S9R/5s9r_complex.cif 5SB7 classic Tubulin Na Na Na Todalam (compound 18) "[""4I2""]" 1 IC50 IC50 = = 48 ± 17 μM 48000.0 [] unit_conversion 4.318758762624412 success True biochemical_inhibition In vitro tubulin polymerization assay with 30 μM tubulin under polymerizing conditions. 7 Todalam fully inhibited microtubule formation at 100 μM, with an IC50 of 48±17 μM in the tubulin polymerization assay. auto_single_measurement only accepted activity measurement [1] 1 structures\5SB7\5SB7_metadata.json point structures/5SB7/5sb7_protein.pdb structures/5SB7/5sb7_pocket.pdb structures/5SB7/5sb7_ligand.sdf structures/5SB7/5sb7_ligand.pdb structures/5SB7/5sb7_ligand.cif structures/5SB7/5sb7_complex.pdb structures/5SB7/5sb7_complex.cif 5SB8 classic beta-tubulin Na T2R-TTL protein complex containing two alpha,beta-tubulin dimers, RB3, and TTL Na maytansinoid 3 "[""5IS""]" 1 Kd Kd = = 830 ± 20 nM 830.0 [] unit_conversion 6.080921907623926 success True direct_binding Binding affinity determined by competition/displacement against fluorescent Fc-maytansine. 4 Table 4 reports maytansinoid 3 Kd = 830 ± 20 nM; Table 6 maps compound 3 to PDB 5SB8. auto_single_measurement only accepted activity measurement [1] 1 structures\5SB8\5SB8_metadata.json point structures/5SB8/5sb8_protein.pdb structures/5SB8/5sb8_pocket.pdb structures/5SB8/5sb8_ligand.sdf structures/5SB8/5sb8_ligand.pdb structures/5SB8/5sb8_ligand.cif structures/5SB8/5sb8_complex.pdb structures/5SB8/5sb8_complex.cif 5SB9 classic beta-tubulin Na T2R-TTL protein complex containing two alpha,beta-tubulin dimers, RB3, and TTL Na maytansinoid 4a "[""5IX""]" 1 Kd Kd = = 51 ± 3 nM 51.0 [] unit_conversion 7.292429823902063 success True direct_binding Binding affinity determined by competition/displacement against fluorescent Fc-maytansine. 4 Table 4 reports maytansinoid 4a Kd = 51 ± 3 nM; Table 6 maps compound 4a to PDB 5SB9. auto_single_measurement only accepted activity measurement [1] 1 structures\5SB9\5SB9_metadata.json point structures/5SB9/5sb9_protein.pdb structures/5SB9/5sb9_pocket.pdb structures/5SB9/5sb9_ligand.sdf structures/5SB9/5sb9_ligand.pdb structures/5SB9/5sb9_ligand.cif structures/5SB9/5sb9_complex.pdb structures/5SB9/5sb9_complex.cif 5SBA classic beta-tubulin Na T2R-TTL protein complex containing two alpha,beta-tubulin dimers, RB3, and TTL Na maytansinoid 4b "[""5IJ""]" 1 Kd Kd = = 11 ± 1 nM 11.0 [] unit_conversion 7.958607314841775 success True direct_binding Binding affinity determined by competition/displacement against fluorescent Fc-maytansine. 4 Table 4 reports maytansinoid 4b Kd = 11 ± 1 nM; Table 6 maps compound 4b to PDB 5SBA. auto_single_measurement only accepted activity measurement [1] 1 structures\5SBA\5SBA_metadata.json point structures/5SBA/5sba_protein.pdb structures/5SBA/5sba_pocket.pdb structures/5SBA/5sba_ligand.sdf structures/5SBA/5sba_ligand.pdb structures/5SBA/5sba_ligand.cif structures/5SBA/5sba_complex.pdb structures/5SBA/5sba_complex.cif 5SBB classic beta-tubulin Na T2R-TTL protein complex containing two alpha,beta-tubulin dimers, RB3, and TTL Na maytansinoid 4c "[""5JH""]" 1 Kd Kd = = 20 ± 2 nM 20.0 [] unit_conversion 7.698970004336019 success True direct_binding Binding affinity determined by competition/displacement against fluorescent Fc-maytansine. 4 Table 4 reports maytansinoid 4c Kd = 20 ± 2 nM; Table 6 maps compound 4c to PDB 5SBB. auto_single_measurement only accepted activity measurement [1] 1 structures\5SBB\5SBB_metadata.json point structures/5SBB/5sbb_protein.pdb structures/5SBB/5sbb_pocket.pdb structures/5SBB/5sbb_ligand.sdf structures/5SBB/5sbb_ligand.pdb structures/5SBB/5sbb_ligand.cif structures/5SBB/5sbb_complex.pdb structures/5SBB/5sbb_complex.cif 5SBC classic beta-tubulin Na T2R-TTL protein complex containing two alpha,beta-tubulin dimers, RB3, and TTL Na maytansinoid 5a "[""5JS""]" 1 Kd Kd = = 1090 ± 40 nM 1090.0 [] unit_conversion 5.962573502059376 success True direct_binding Binding affinity determined by competition/displacement against fluorescent Fc-maytansine. 4 Table 4 reports maytansinoid 5a Kd = 1090 ± 40 nM; Table 6 maps compound 5a to PDB 5SBC. auto_single_measurement only accepted activity measurement [1] 1 structures\5SBC\5SBC_metadata.json point structures/5SBC/5sbc_protein.pdb structures/5SBC/5sbc_pocket.pdb structures/5SBC/5sbc_ligand.sdf structures/5SBC/5sbc_ligand.pdb structures/5SBC/5sbc_ligand.cif structures/5SBC/5sbc_complex.pdb structures/5SBC/5sbc_complex.cif 5SBD classic beta-tubulin Na T2R-TTL protein complex containing two alpha,beta-tubulin dimers, RB3, and TTL Na maytansinoid 5b "[""5KI""]" 1 Kd Kd = = 860 ± 30 nM 860.0 [] unit_conversion 6.065501548756432 success True direct_binding Binding affinity determined by competition/displacement against fluorescent Fc-maytansine. 4 Table 4 reports maytansinoid 5b Kd = 860 ± 30 nM; Table 6 maps compound 5b to PDB 5SBD. auto_single_measurement only accepted activity measurement [1] 1 structures\5SBD\5SBD_metadata.json point structures/5SBD/5sbd_protein.pdb structures/5SBD/5sbd_pocket.pdb structures/5SBD/5sbd_ligand.sdf structures/5SBD/5sbd_ligand.pdb structures/5SBD/5sbd_ligand.cif structures/5SBD/5sbd_complex.pdb structures/5SBD/5sbd_complex.cif 5SBE classic beta-tubulin Na T2R-TTL protein complex containing two alpha,beta-tubulin dimers, RB3, and TTL Na maytansinoid 5c "[""5L5""]" 1 Kd Kd = = 1800 ± 120 nM 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding Binding affinity determined by competition/displacement against fluorescent Fc-maytansine. 4 Table 4 reports maytansinoid 5c Kd = 1800 ± 120 nM; Table 6 maps compound 5c to PDB 5SBE. auto_single_measurement only accepted activity measurement [1] 1 structures\5SBE\5SBE_metadata.json point structures/5SBE/5sbe_protein.pdb structures/5SBE/5sbe_pocket.pdb structures/5SBE/5sbe_ligand.sdf structures/5SBE/5sbe_ligand.pdb structures/5SBE/5sbe_ligand.cif structures/5SBE/5sbe_complex.pdb structures/5SBE/5sbe_complex.cif 5SDU classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1oc(-c2ccccc2)nc1CCc1nc(-c2ccccc2)cn1C "[""I9Z""]" 1 pIC50 IC50 = = 7.33 46.77351412871981 [] p_metric_transform 7.33 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SDU to this ligand and reports PDE10A pIC50 7.33. auto_single_measurement only accepted activity measurement [1] 1 structures\5SDU\5SDU_metadata.json point structures/5SDU/5sdu_protein.pdb structures/5SDU/5sdu_pocket.pdb structures/5SDU/5sdu_ligand.sdf structures/5SDU/5sdu_ligand.pdb structures/5SDU/5sdu_ligand.cif structures/5SDU/5sdu_complex.pdb structures/5SDU/5sdu_complex.cif 5SDV classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1ncc(C(=O)NCc2cocn2)c1C(=O)Nc1ccn2cc(-c3ccccc3)nc2n1 "[""IAI""]" 1 pIC50 IC50 = = 8.90 1.2589254117941662 [] p_metric_transform 8.9 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SDV to this ligand and reports PDE10A pIC50 8.90. auto_single_measurement only accepted activity measurement [1] 1 structures\5SDV\5SDV_metadata.json point structures/5SDV/5sdv_protein.pdb structures/5SDV/5sdv_pocket.pdb structures/5SDV/5sdv_ligand.sdf structures/5SDV/5sdv_ligand.pdb structures/5SDV/5sdv_ligand.cif structures/5SDV/5sdv_complex.pdb structures/5SDV/5sdv_complex.cif 5SDW classic human phosphodiesterase 10 (PDE10A) human Na Na CN(C)C(=O)c1cnn(C)c1C(=O)Nc1ccc2[nH]c(-c3ccccc3)nc2c1 "[""IAL""]" 1 pIC50 IC50 = = 9.44 0.36307805477010174 [] p_metric_transform 9.44 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SDW to this ligand and reports PDE10A pIC50 9.44. auto_single_measurement only accepted activity measurement [1] 1 structures\5SDW\5SDW_metadata.json point structures/5SDW/5sdw_protein.pdb structures/5SDW/5sdw_pocket.pdb structures/5SDW/5sdw_ligand.sdf structures/5SDW/5sdw_ligand.pdb structures/5SDW/5sdw_ligand.cif structures/5SDW/5sdw_complex.pdb structures/5SDW/5sdw_complex.cif 5SDX classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1cc(-c2ccccc2)nc1CCc1cccc(N2CCOCC2)n1 "[""IAY""]" 1 pIC50 IC50 = = 5.50 3162.2776601683795 [] p_metric_transform 5.5 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SDX to this ligand and reports PDE10A pIC50 5.50. auto_single_measurement only accepted activity measurement [1] 1 structures\5SDX\5SDX_metadata.json point structures/5SDX/5sdx_protein.pdb structures/5SDX/5sdx_pocket.pdb structures/5SDX/5sdx_ligand.sdf structures/5SDX/5sdx_ligand.pdb structures/5SDX/5sdx_ligand.cif structures/5SDX/5sdx_complex.pdb structures/5SDX/5sdx_complex.cif 5SDY classic human phosphodiesterase 10 (PDE10A) human Na Na COCCn1ncc(NC(=O)c2nc(C3CC3)ccc2Nc2cncnc2)c1C(=O)N(C)C "[""IB4""]" 1 pIC50 IC50 = = 7.90 12.589254117941662 [] p_metric_transform 7.9 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SDY to this ligand and reports PDE10A pIC50 7.90. auto_single_measurement only accepted activity measurement [1] 1 structures\5SDY\5SDY_metadata.json point structures/5SDY/5sdy_protein.pdb structures/5SDY/5sdy_pocket.pdb structures/5SDY/5sdy_ligand.sdf structures/5SDY/5sdy_ligand.pdb structures/5SDY/5sdy_ligand.cif structures/5SDY/5sdy_complex.pdb structures/5SDY/5sdy_complex.cif 5SDZ classic human phosphodiesterase 10 (PDE10A) human Na Na CN(CC(O)CO)C(=O)c1nn(C)cc1NC(=O)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IB7""]" 1 pIC50 IC50 = = 7.71 19.498445997580454 [] p_metric_transform 7.71 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SDZ to this ligand and reports PDE10A pIC50 7.71. auto_single_measurement only accepted activity measurement [1] 1 structures\5SDZ\5SDZ_metadata.json point structures/5SDZ/5sdz_protein.pdb structures/5SDZ/5sdz_pocket.pdb structures/5SDZ/5sdz_ligand.sdf structures/5SDZ/5sdz_ligand.pdb structures/5SDZ/5sdz_ligand.cif structures/5SDZ/5sdz_complex.pdb structures/5SDZ/5sdz_complex.cif 5SE0 classic human phosphodiesterase 10 (PDE10A) human Na Na O=C(Nc1cc(-c2ccccn2)nn1CCO)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IBJ""]" 1 pIC50 IC50 = = 8.65 2.2387211385683377 [] p_metric_transform 8.65 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE0 to this ligand and reports PDE10A pIC50 8.65. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE0\5SE0_metadata.json point structures/5SE0/5se0_protein.pdb structures/5SE0/5se0_pocket.pdb structures/5SE0/5se0_ligand.sdf structures/5SE0/5se0_ligand.pdb structures/5SE0/5se0_ligand.cif structures/5SE0/5se0_complex.pdb structures/5SE0/5se0_complex.cif 5SE1 classic human phosphodiesterase 10 (PDE10A) human Na Na CN(C)C(=O)c1nn(C)cc1NC(=O)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IBV""]" 1 pIC50 IC50 = = 7.50 31.622776601683793 [] p_metric_transform 7.5 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE1 to this ligand and reports PDE10A pIC50 7.50. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE1\5SE1_metadata.json point structures/5SE1/5se1_protein.pdb structures/5SE1/5se1_pocket.pdb structures/5SE1/5se1_ligand.sdf structures/5SE1/5se1_ligand.pdb structures/5SE1/5se1_ligand.cif structures/5SE1/5se1_complex.pdb structures/5SE1/5se1_complex.cif 5SE2 classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1cc(-c2ccccc2)nc1CCc1ccc2ccccc2n1 "[""IBY""]" 1 pIC50 IC50 = = 7.03 93.32543007969905 [] p_metric_transform 7.03 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE2 to this ligand and reports PDE10A pIC50 7.03. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE2\5SE2_metadata.json point structures/5SE2/5se2_protein.pdb structures/5SE2/5se2_pocket.pdb structures/5SE2/5se2_ligand.sdf structures/5SE2/5se2_ligand.pdb structures/5SE2/5se2_ligand.cif structures/5SE2/5se2_complex.pdb structures/5SE2/5se2_complex.cif 5SE3 classic human phosphodiesterase 10 (PDE10A) human Na Na O=C(Nc1ccn2nc(-c3ccccc3)nc2c1)c1ccnc(Cl)c1 "[""ICK""]" 1 pIC50 IC50 = = 7.35 44.668359215096345 [] p_metric_transform 7.35 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE3 to this ligand and reports PDE10A pIC50 7.35. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE3\5SE3_metadata.json point structures/5SE3/5se3_protein.pdb structures/5SE3/5se3_pocket.pdb structures/5SE3/5se3_ligand.sdf structures/5SE3/5se3_ligand.pdb structures/5SE3/5se3_ligand.cif structures/5SE3/5se3_complex.pdb structures/5SE3/5se3_complex.cif 5SE4 classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1cc(C2CC2)nc2nc(CCc3nc(-c4ccccc4)cn3C)nn12 "[""ICW""]" 1 pIC50 IC50 = = 8.87 1.348962882591656 [] p_metric_transform 8.87 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE4 to this ligand and reports PDE10A pIC50 8.87. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE4\5SE4_metadata.json point structures/5SE4/5se4_protein.pdb structures/5SE4/5se4_pocket.pdb structures/5SE4/5se4_ligand.sdf structures/5SE4/5se4_ligand.pdb structures/5SE4/5se4_ligand.cif structures/5SE4/5se4_complex.pdb structures/5SE4/5se4_complex.cif 5SE5 classic human phosphodiesterase 10 (PDE10A) human Na Na CNC(=O)c1c(NC(=O)c2nc(C3CC3)cnc2Nc2cncnc2)cnn1C "[""IEH""]" 1 pIC50 IC50 = = 8.24 5.754399373371567 [] p_metric_transform 8.24 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE5 to this ligand and reports PDE10A pIC50 8.24. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE5\5SE5_metadata.json point structures/5SE5/5se5_protein.pdb structures/5SE5/5se5_pocket.pdb structures/5SE5/5se5_ligand.sdf structures/5SE5/5se5_ligand.pdb structures/5SE5/5se5_ligand.cif structures/5SE5/5se5_complex.pdb structures/5SE5/5se5_complex.cif 5SE6 classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1nc(OCc2nc(-c3ccccc3)cn2C)c2ncn(C)c2n1 "[""IEB""]" 1 pIC50 IC50 = = 7.00 100.0 [] p_metric_transform 7.0 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE6 to this ligand and reports PDE10A pIC50 7.00. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE6\5SE6_metadata.json point structures/5SE6/5se6_protein.pdb structures/5SE6/5se6_pocket.pdb structures/5SE6/5se6_ligand.sdf structures/5SE6/5se6_ligand.pdb structures/5SE6/5se6_ligand.cif structures/5SE6/5se6_complex.pdb structures/5SE6/5se6_complex.cif 5SE7 classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1ncc(C(=O)N2CCC2)c1C(=O)Nc1ccn2nc(-c3ccccc3)nc2c1 "[""IE7""]" 1 pIC50 IC50 = = 9.56 0.27542287033381635 [] p_metric_transform 9.56 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE7 to this ligand and reports PDE10A pIC50 9.56. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE7\5SE7_metadata.json point structures/5SE7/5se7_protein.pdb structures/5SE7/5se7_pocket.pdb structures/5SE7/5se7_ligand.sdf structures/5SE7/5se7_ligand.pdb structures/5SE7/5se7_ligand.cif structures/5SE7/5se7_complex.pdb structures/5SE7/5se7_complex.cif 5SE8 classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1nc(-c2ccccc2)nc1CCNC(=O)c1c(C(=O)N2CCC2)cnn1C "[""IE1""]" 1 pIC50 IC50 = = 7.67 21.379620895022324 [] p_metric_transform 7.67 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE8 to this ligand and reports PDE10A pIC50 7.67. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE8\5SE8_metadata.json point structures/5SE8/5se8_protein.pdb structures/5SE8/5se8_pocket.pdb structures/5SE8/5se8_ligand.sdf structures/5SE8/5se8_ligand.pdb structures/5SE8/5se8_ligand.cif structures/5SE8/5se8_complex.pdb structures/5SE8/5se8_complex.cif 5SE9 classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1nc2ccc(OCc3nc(-c4ccccc4)cn3C)nn2c1C "[""ID9""]" 1 pIC50 IC50 = = 8.14 7.244359600749891 [] p_metric_transform 8.14 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SE9 to this ligand and reports PDE10A pIC50 8.14. auto_single_measurement only accepted activity measurement [1] 1 structures\5SE9\5SE9_metadata.json point structures/5SE9/5se9_protein.pdb structures/5SE9/5se9_pocket.pdb structures/5SE9/5se9_ligand.sdf structures/5SE9/5se9_ligand.pdb structures/5SE9/5se9_ligand.cif structures/5SE9/5se9_complex.pdb structures/5SE9/5se9_complex.cif 5SEA classic human phosphodiesterase 10 human Na Na O=C(Nc1ccnn1-c1ccccc1)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IF5""]" 1 pIC50 IC50 = = 9.06 0.8709635899560796 [] p_metric_transform 9.06 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEA to this ligand and reports PDE10A pIC50 9.06. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEA\5SEA_metadata.json point structures/5SEA/5sea_protein.pdb structures/5SEA/5sea_pocket.pdb structures/5SEA/5sea_ligand.sdf structures/5SEA/5sea_ligand.pdb structures/5SEA/5sea_ligand.cif structures/5SEA/5sea_complex.pdb structures/5SEA/5sea_complex.cif 5SEB classic human phosphodiesterase 10 human Na Na Cc1nc2ccccc2nc1CCc1nc(N2CCCC2)nn1C "[""IF2""]" 1 pIC50 IC50 = = 7.21 61.65950018614822 [] p_metric_transform 7.21 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEB to this ligand and reports PDE10A pIC50 7.21. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEB\5SEB_metadata.json point structures/5SEB/5seb_protein.pdb structures/5SEB/5seb_pocket.pdb structures/5SEB/5seb_ligand.sdf structures/5SEB/5seb_ligand.pdb structures/5SEB/5seb_ligand.cif structures/5SEB/5seb_complex.pdb structures/5SEB/5seb_complex.cif 5SEC classic human phosphodiesterase 10 human Na Na Cc1nc2ccccc2nc1CCc1nc(-c2ccccc2)cn1-c1ccccc1 "[""IEX""]" 1 pIC50 IC50 = = 9.48 0.3311311214825908 [] p_metric_transform 9.48 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEC to this ligand and reports PDE10A pIC50 9.48. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEC\5SEC_metadata.json point structures/5SEC/5sec_protein.pdb structures/5SEC/5sec_pocket.pdb structures/5SEC/5sec_ligand.sdf structures/5SEC/5sec_ligand.pdb structures/5SEC/5sec_ligand.cif structures/5SEC/5sec_complex.pdb structures/5SEC/5sec_complex.cif 5SED classic human phosphodiesterase 10 human Na Na Cn1cc(-c2ccccc2)nc1COc1nc(N2CCOCC2)c2cc(Cl)ccc2n1 "[""IEU""]" 1 pIC50 IC50 = = 8.67 2.1379620895022327 [] p_metric_transform 8.67 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SED to this ligand and reports PDE10A pIC50 8.67. auto_single_measurement only accepted activity measurement [1] 1 structures\5SED\5SED_metadata.json point structures/5SED/5sed_protein.pdb structures/5SED/5sed_pocket.pdb structures/5SED/5sed_ligand.sdf structures/5SED/5sed_ligand.pdb structures/5SED/5sed_ligand.cif structures/5SED/5sed_complex.pdb structures/5SED/5sed_complex.cif 5SEE classic human phosphodiesterase 10 human Na Na O=C(Nc1ccnn1-c1ccccn1)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IEN""]" 1 pIC50 IC50 = = 8.46 3.4673685045253095 [] p_metric_transform 8.46 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEE to this ligand and reports PDE10A pIC50 8.46. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEE\5SEE_metadata.json point structures/5SEE/5see_protein.pdb structures/5SEE/5see_pocket.pdb structures/5SEE/5see_ligand.sdf structures/5SEE/5see_ligand.pdb structures/5SEE/5see_ligand.cif structures/5SEE/5see_complex.pdb structures/5SEE/5see_complex.cif 5SEF classic human phosphodiesterase 10 human Na Na Cc1nc(C)n2nc(CCc3nc(N4CCCC4)nn3C)nc2c1C "[""IFR""]" 1 pIC50 IC50 = = 7.87 13.489628825916533 [] p_metric_transform 7.87 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEF to this ligand and reports PDE10A pIC50 7.87. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEF\5SEF_metadata.json point structures/5SEF/5sef_protein.pdb structures/5SEF/5sef_pocket.pdb structures/5SEF/5sef_ligand.sdf structures/5SEF/5sef_ligand.pdb structures/5SEF/5sef_ligand.cif structures/5SEF/5sef_complex.pdb structures/5SEF/5sef_complex.cif 5SEG classic human phosphodiesterase 10 human Na Na Cn1cc(Br)cc(C(=O)Nc2cc3nc(-c4ccccc4)[nH]c3cc2C(=O)NC2COC2)c1=O "[""IFN""]" 1 pIC50 IC50 = = 8.17 6.760829753919819 [] p_metric_transform 8.17 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEG to this ligand and reports PDE10A pIC50 8.17. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEG\5SEG_metadata.json point structures/5SEG/5seg_protein.pdb structures/5SEG/5seg_pocket.pdb structures/5SEG/5seg_ligand.sdf structures/5SEG/5seg_ligand.pdb structures/5SEG/5seg_ligand.cif structures/5SEG/5seg_complex.pdb structures/5SEG/5seg_complex.cif 5SEH classic human phosphodiesterase 10 human Na Na Cn1ncc(C(=O)N2CCC2)c1C(=O)Nc1ccn2nc(N3CCOCC3)nc2c1 "[""IFI""]" 1 pIC50 IC50 = = 8.69 2.041737944669532 [] p_metric_transform 8.69 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEH to this ligand and reports PDE10A pIC50 8.69. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEH\5SEH_metadata.json point structures/5SEH/5seh_protein.pdb structures/5SEH/5seh_pocket.pdb structures/5SEH/5seh_ligand.sdf structures/5SEH/5seh_ligand.pdb structures/5SEH/5seh_ligand.cif structures/5SEH/5seh_complex.pdb structures/5SEH/5seh_complex.cif 5SEI classic human phosphodiesterase 10 human Na Na Cn1nc(N2CCCC2)nc1/C=C/c1nc2ccc(Cl)cn2n1 "[""IFE""]" 1 pIC50 IC50 = = 6.88 131.82567385564073 [] p_metric_transform 6.88 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEI to this ligand and reports PDE10A pIC50 6.88. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEI\5SEI_metadata.json point structures/5SEI/5sei_protein.pdb structures/5SEI/5sei_pocket.pdb structures/5SEI/5sei_ligand.sdf structures/5SEI/5sei_ligand.pdb structures/5SEI/5sei_ligand.cif structures/5SEI/5sei_complex.pdb structures/5SEI/5sei_complex.cif 5SEJ classic human phosphodiesterase 10 human Na Na Cn1nc(N2CCCC2)nc1CCc1nc2ccc(Cl)cn2n1 "[""IFV""]" 1 pIC50 IC50 = = 7.20 63.0957344480193 [] p_metric_transform 7.2 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEJ to this ligand and reports PDE10A pIC50 7.20. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEJ\5SEJ_metadata.json point structures/5SEJ/5sej_protein.pdb structures/5SEJ/5sej_pocket.pdb structures/5SEJ/5sej_ligand.sdf structures/5SEJ/5sej_ligand.pdb structures/5SEJ/5sej_ligand.cif structures/5SEJ/5sej_complex.pdb structures/5SEJ/5sej_complex.cif 5SEK classic human phosphodiesterase 10 human Na Na Cc1nc2ccccc2nc1CCc1nc(-c2ccccc2)cn1C "[""IFY""]" 1 pIC50 IC50 = = 8.29 5.128613839913658 [] p_metric_transform 8.29 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEK to this ligand and reports PDE10A pIC50 8.29. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEK\5SEK_metadata.json point structures/5SEK/5sek_protein.pdb structures/5SEK/5sek_pocket.pdb structures/5SEK/5sek_ligand.sdf structures/5SEK/5sek_ligand.pdb structures/5SEK/5sek_ligand.cif structures/5SEK/5sek_complex.pdb structures/5SEK/5sek_complex.cif 5SEL classic human phosphodiesterase 10 human Na Na Cn1nc(-c2ccccn2)cc1NC(=O)c1c(C(=O)N2CCC2)cnn1C "[""IG1""]" 1 pIC50 IC50 = = 8.10 7.943282347242821 [] p_metric_transform 8.1 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEL to this ligand and reports PDE10A pIC50 8.10. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEL\5SEL_metadata.json point structures/5SEL/5sel_protein.pdb structures/5SEL/5sel_pocket.pdb structures/5SEL/5sel_ligand.sdf structures/5SEL/5sel_ligand.pdb structures/5SEL/5sel_ligand.cif structures/5SEL/5sel_complex.pdb structures/5SEL/5sel_complex.cif 5SEM classic human phosphodiesterase 10 human Na Na Cc1c(C(F)(F)F)nc2ccc(CCc3nc(-c4ccccc4)cn3C)nn12 "[""IG6""]" 1 pIC50 IC50 = = 8.75 1.7782794100389228 [] p_metric_transform 8.75 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEM to this ligand and reports PDE10A pIC50 8.75. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEM\5SEM_metadata.json point structures/5SEM/5sem_protein.pdb structures/5SEM/5sem_pocket.pdb structures/5SEM/5sem_ligand.sdf structures/5SEM/5sem_ligand.pdb structures/5SEM/5sem_ligand.cif structures/5SEM/5sem_complex.pdb structures/5SEM/5sem_complex.cif 5SEN classic human phosphodiesterase 10 human Na Na Cn1ncc(C(=O)N2CCC2)c1C(=O)Nc1cn(-c2ccc3ccccc3n2)cn1 "[""IG9""]" 1 pIC50 IC50 = = 9.16 0.6918309709189363 [] p_metric_transform 9.16 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEN to this ligand and reports PDE10A pIC50 9.16. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEN\5SEN_metadata.json point structures/5SEN/5sen_protein.pdb structures/5SEN/5sen_pocket.pdb structures/5SEN/5sen_ligand.sdf structures/5SEN/5sen_ligand.pdb structures/5SEN/5sen_ligand.cif structures/5SEN/5sen_complex.pdb structures/5SEN/5sen_complex.cif 5SEO classic human phosphodiesterase 10 human Na Na Cc1[nH]c(-c2ccccc2)nc1CCN1C(=O)c2ccccc2C1=O "[""IGE""]" 1 pIC50 IC50 = = 7.06 87.09635899560814 [] p_metric_transform 7.06 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEO to this ligand and reports PDE10A pIC50 7.06. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEO\5SEO_metadata.json point structures/5SEO/5seo_protein.pdb structures/5SEO/5seo_pocket.pdb structures/5SEO/5seo_ligand.sdf structures/5SEO/5seo_ligand.pdb structures/5SEO/5seo_ligand.cif structures/5SEO/5seo_complex.pdb structures/5SEO/5seo_complex.cif 5SEP classic human phosphodiesterase 10 human Na Na Cc1ncc(C)n2nc(CCc3nc(C4CCCC4)cn3C)nc12 "[""IGI""]" 1 pIC50 IC50 = = 6.99 102.32929922807536 [] p_metric_transform 6.99 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEP to this ligand and reports PDE10A pIC50 6.99. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEP\5SEP_metadata.json point structures/5SEP/5sep_protein.pdb structures/5SEP/5sep_pocket.pdb structures/5SEP/5sep_ligand.sdf structures/5SEP/5sep_ligand.pdb structures/5SEP/5sep_ligand.cif structures/5SEP/5sep_complex.pdb structures/5SEP/5sep_complex.cif 5SEQ classic phosphodiesterase 10 human Na Na Cc1nc(C)c2nc(CCc3nc(N4CCCC4)nn3C)nn2c1C "[""IGO""]" 1 pIC50 IC50 = = 7.43 37.15352290971728 [] p_metric_transform 7.43 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEQ to this ligand and reports PDE10A pIC50 7.43. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEQ\5SEQ_metadata.json point structures/5SEQ/5seq_protein.pdb structures/5SEQ/5seq_pocket.pdb structures/5SEQ/5seq_ligand.sdf structures/5SEQ/5seq_ligand.pdb structures/5SEQ/5seq_ligand.cif structures/5SEQ/5seq_complex.pdb structures/5SEQ/5seq_complex.cif 5SER classic phosphodiesterase 10 human Na Na CN(CCF)C(=O)c1cnn(C)c1C(=O)Nc1ccn2nc(-c3ccccc3)nc2c1 "[""IGW""]" 1 pIC50 IC50 = = 9.07 0.8511380382023759 [] p_metric_transform 9.07 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SER to this ligand and reports PDE10A pIC50 9.07. auto_single_measurement only accepted activity measurement [1] 1 structures\5SER\5SER_metadata.json point structures/5SER/5ser_protein.pdb structures/5SER/5ser_pocket.pdb structures/5SER/5ser_ligand.sdf structures/5SER/5ser_ligand.pdb structures/5SER/5ser_ligand.cif structures/5SER/5ser_complex.pdb structures/5SER/5ser_complex.cif 5SES classic phosphodiesterase 10 human Na Na Cn1ncc(C(=O)N2CCC2)c1C(=O)NC1CCn2cc(-c3ccccc3)nc2C1 "[""IGZ""]" 1 pIC50 IC50 = = 8.54 2.8840315031266117 [] p_metric_transform 8.54 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SES to this ligand and reports PDE10A pIC50 8.54. auto_single_measurement only accepted activity measurement [1] 1 structures\5SES\5SES_metadata.json point structures/5SES/5ses_protein.pdb structures/5SES/5ses_pocket.pdb structures/5SES/5ses_ligand.sdf structures/5SES/5ses_ligand.pdb structures/5SES/5ses_ligand.cif structures/5SES/5ses_complex.pdb structures/5SES/5ses_complex.cif 5SET classic phosphodiesterase 10 human Na Na Cn1nc(-c2ccccn2)cc1NC(=O)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IH8""]" 1 pIC50 IC50 = = 8.49 3.235936569296281 [] p_metric_transform 8.49 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SET to this ligand and reports PDE10A pIC50 8.49. auto_single_measurement only accepted activity measurement [1] 1 structures\5SET\5SET_metadata.json point structures/5SET/5set_protein.pdb structures/5SET/5set_pocket.pdb structures/5SET/5set_ligand.sdf structures/5SET/5set_ligand.pdb structures/5SET/5set_ligand.cif structures/5SET/5set_complex.pdb structures/5SET/5set_complex.cif 5SEU classic phosphodiesterase 10 human Na Na Cn1nc(N2CCCC2)nc1CCc1nc2ccc(C(F)(F)F)cn2n1 "[""IHL""]" 1 pIC50 IC50 = = 6.27 537.0317963702532 [] p_metric_transform 6.27 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEU to this ligand and reports PDE10A pIC50 6.27. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEU\5SEU_metadata.json point structures/5SEU/5seu_protein.pdb structures/5SEU/5seu_pocket.pdb structures/5SEU/5seu_ligand.sdf structures/5SEU/5seu_ligand.pdb structures/5SEU/5seu_ligand.cif structures/5SEU/5seu_complex.pdb structures/5SEU/5seu_complex.cif 5SEV classic phosphodiesterase 10 human Na Na Cc1nc(C)c(CCc2nc(-c3ccccc3)cn2C)nc1C "[""IHV""]" 1 pIC50 IC50 = = 7.09 81.28305161640995 [] p_metric_transform 7.09 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEV to this ligand and reports PDE10A pIC50 7.09. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEV\5SEV_metadata.json point structures/5SEV/5sev_protein.pdb structures/5SEV/5sev_pocket.pdb structures/5SEV/5sev_ligand.sdf structures/5SEV/5sev_ligand.pdb structures/5SEV/5sev_ligand.cif structures/5SEV/5sev_complex.pdb structures/5SEV/5sev_complex.cif 5SEW classic phosphodiesterase 10 human Na Na CNC(=O)c1c(NC(=O)c2nc(C3CC3)ccc2Nc2cncnc2)cnn1CCOC "[""II5""]" 1 pIC50 IC50 = = 9.08 0.8317637711026709 [] p_metric_transform 9.08 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEW to this ligand and reports PDE10A pIC50 9.08. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEW\5SEW_metadata.json point structures/5SEW/5sew_protein.pdb structures/5SEW/5sew_pocket.pdb structures/5SEW/5sew_ligand.sdf structures/5SEW/5sew_ligand.pdb structures/5SEW/5sew_ligand.cif structures/5SEW/5sew_complex.pdb structures/5SEW/5sew_complex.cif 5SEX classic phosphodiesterase 10 human Na Na CNC(=O)c1cc2[nH]c(-c3ccccc3)nc2cc1NC(=O)c1cccc(C)n1 "[""II9""]" 1 pIC50 IC50 = = 7.45 35.481338923357534 [] p_metric_transform 7.45 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEX to this ligand and reports PDE10A pIC50 7.45. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEX\5SEX_metadata.json point structures/5SEX/5sex_protein.pdb structures/5SEX/5sex_pocket.pdb structures/5SEX/5sex_ligand.sdf structures/5SEX/5sex_ligand.pdb structures/5SEX/5sex_ligand.cif structures/5SEX/5sex_complex.pdb structures/5SEX/5sex_complex.cif 5SEY classic phosphodiesterase 10 human Na Na Cn1cc(-c2ccccc2)nc1C#Cc1ccc2nc(C3CC3)c(CO)n2n1 "[""IIR""]" 1 pIC50 IC50 = = 7.33 46.77351412871981 [] p_metric_transform 7.33 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEY to this ligand and reports PDE10A pIC50 7.33. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEY\5SEY_metadata.json point structures/5SEY/5sey_protein.pdb structures/5SEY/5sey_pocket.pdb structures/5SEY/5sey_ligand.sdf structures/5SEY/5sey_ligand.pdb structures/5SEY/5sey_ligand.cif structures/5SEY/5sey_complex.pdb structures/5SEY/5sey_complex.cif 5SEZ classic phosphodiesterase 10 human Na Na CCc1cc(C(=O)Nc2ccn3nc(-c4ccccc4)nc3c2)cc(Cl)n1 "[""IIU""]" 1 pIC50 IC50 = = 7.99 10.232929922807536 [] p_metric_transform 7.99 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SEZ to this ligand and reports PDE10A pIC50 7.99. auto_single_measurement only accepted activity measurement [1] 1 structures\5SEZ\5SEZ_metadata.json point structures/5SEZ/5sez_protein.pdb structures/5SEZ/5sez_pocket.pdb structures/5SEZ/5sez_ligand.sdf structures/5SEZ/5sez_ligand.pdb structures/5SEZ/5sez_ligand.cif structures/5SEZ/5sez_complex.pdb structures/5SEZ/5sez_complex.cif 5SF0 classic phosphodiesterase 10 human Na Na Cn1ncc(C(=O)N2CCC2)c1C(=O)Nc1cc(-c2ccccn2)n[nH]1 "[""IIX""]" 1 pIC50 IC50 = = 8.08 8.317637711026709 [] p_metric_transform 8.08 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF0 to this ligand and reports PDE10A pIC50 8.08. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF0\5SF0_metadata.json point structures/5SF0/5sf0_protein.pdb structures/5SF0/5sf0_pocket.pdb structures/5SF0/5sf0_ligand.sdf structures/5SF0/5sf0_ligand.pdb structures/5SF0/5sf0_ligand.cif structures/5SF0/5sf0_complex.pdb structures/5SF0/5sf0_complex.cif 5SF1 classic phosphodiesterase 10 human Na Na Cc1c(C(F)F)nc2ccc(C#Cc3nc(-c4ccccc4)cn3C)nn12 "[""IJ0""]" 1 pIC50 IC50 = = 9.01 0.9772372209558111 [] p_metric_transform 9.01 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF1 to this ligand and reports PDE10A pIC50 9.01. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF1\5SF1_metadata.json point structures/5SF1/5sf1_protein.pdb structures/5SF1/5sf1_pocket.pdb structures/5SF1/5sf1_ligand.sdf structures/5SF1/5sf1_ligand.pdb structures/5SF1/5sf1_ligand.cif structures/5SF1/5sf1_complex.pdb structures/5SF1/5sf1_complex.cif 5SF2 classic phosphodiesterase 10 human Na Na O=C1NCc2ccc(NC(=O)c3nc(C4CC4)ccc3Nc3cncnc3)cc21 "[""IJ7""]" 1 pIC50 IC50 = = 7.71 19.498445997580454 [] p_metric_transform 7.71 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF2 to this ligand and reports PDE10A pIC50 7.71. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF2\5SF2_metadata.json point structures/5SF2/5sf2_protein.pdb structures/5SF2/5sf2_pocket.pdb structures/5SF2/5sf2_ligand.sdf structures/5SF2/5sf2_ligand.pdb structures/5SF2/5sf2_ligand.cif structures/5SF2/5sf2_complex.pdb structures/5SF2/5sf2_complex.cif 5SF3 classic phosphodiesterase 10 human Na Na Cn1ncc(C(=O)NCc2ccn[nH]2)c1C(=O)Nc1ccn2cc(-c3ccccc3)nc2n1 "[""IJA""]" 1 pIC50 IC50 = = 8.60 2.5118864315095824 [] p_metric_transform 8.6 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF3 to this ligand and reports PDE10A pIC50 8.60. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF3\5SF3_metadata.json point structures/5SF3/5sf3_protein.pdb structures/5SF3/5sf3_pocket.pdb structures/5SF3/5sf3_ligand.sdf structures/5SF3/5sf3_ligand.pdb structures/5SF3/5sf3_ligand.cif structures/5SF3/5sf3_complex.pdb structures/5SF3/5sf3_complex.cif 5SF4 classic phosphodiesterase 10 human Na Na CN(C)CCn1nc(-c2ccccn2)cc1NC(=O)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IJD""]" 1 pIC50 IC50 = = 8.98 1.0471285480508985 [] p_metric_transform 8.98 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF4 to this ligand and reports PDE10A pIC50 8.98. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF4\5SF4_metadata.json point structures/5SF4/5sf4_protein.pdb structures/5SF4/5sf4_pocket.pdb structures/5SF4/5sf4_ligand.sdf structures/5SF4/5sf4_ligand.pdb structures/5SF4/5sf4_ligand.cif structures/5SF4/5sf4_complex.pdb structures/5SF4/5sf4_complex.cif 5SF5 classic phosphodiesterase 10 human Na Na Cc1nc2ccc(CCc3nc(-c4ccccc4)cn3C)nn2c1C "[""IJH""]" 1 pIC50 IC50 = = 8.47 3.3884415613920207 [] p_metric_transform 8.47 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF5 to this ligand and reports PDE10A pIC50 8.47. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF5\5SF5_metadata.json point structures/5SF5/5sf5_protein.pdb structures/5SF5/5sf5_pocket.pdb structures/5SF5/5sf5_ligand.sdf structures/5SF5/5sf5_ligand.pdb structures/5SF5/5sf5_ligand.cif structures/5SF5/5sf5_complex.pdb structures/5SF5/5sf5_complex.cif 5SF6 classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1nc2c(NC(C)C)nc(CCc3nc(N4CCCC4)nn3C)nn2c1C "[""IJK""]" 1 pIC50 IC50 = = 8.56 2.754228703338163 [] p_metric_transform 8.56 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF6 to this ligand and reports PDE10A pIC50 8.56. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF6\5SF6_metadata.json point structures/5SF6/5sf6_protein.pdb structures/5SF6/5sf6_pocket.pdb structures/5SF6/5sf6_ligand.sdf structures/5SF6/5sf6_ligand.pdb structures/5SF6/5sf6_ligand.cif structures/5SF6/5sf6_complex.pdb structures/5SF6/5sf6_complex.cif 5SF7 classic human phosphodiesterase 10 (PDE10A) human Na Na COc1ccc2c(=O)n(C)c3c(C)nc(-c4ccccc4Cl)n3c2c1 "[""IJN""]" 1 pIC50 IC50 = = 8.14 7.244359600749891 [] p_metric_transform 8.14 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF7 to this ligand and reports PDE10A pIC50 8.14. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF7\5SF7_metadata.json point structures/5SF7/5sf7_protein.pdb structures/5SF7/5sf7_pocket.pdb structures/5SF7/5sf7_ligand.sdf structures/5SF7/5sf7_ligand.pdb structures/5SF7/5sf7_ligand.cif structures/5SF7/5sf7_complex.pdb structures/5SF7/5sf7_complex.cif 5SF8 classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1ncc(C(=O)N2CCC2)c1C(=O)NCCc1nc(-c2ccccc2)nn1-c1ccccn1 "[""IJQ""]" 1 pIC50 IC50 = = 9.32 0.47863009232263803 [] p_metric_transform 9.32 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF8 to this ligand and reports PDE10A pIC50 9.32. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF8\5SF8_metadata.json point structures/5SF8/5sf8_protein.pdb structures/5SF8/5sf8_pocket.pdb structures/5SF8/5sf8_ligand.sdf structures/5SF8/5sf8_ligand.pdb structures/5SF8/5sf8_ligand.cif structures/5SF8/5sf8_complex.pdb structures/5SF8/5sf8_complex.cif 5SF9 classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1nc2ccccc2nc1OCc1nc(-c2ccccc2)cn1C "[""IJT""]" 1 pIC50 IC50 = = 8.38 4.168693834703347 [] p_metric_transform 8.38 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SF9 to this ligand and reports PDE10A pIC50 8.38. auto_single_measurement only accepted activity measurement [1] 1 structures\5SF9\5SF9_metadata.json point structures/5SF9/5sf9_protein.pdb structures/5SF9/5sf9_pocket.pdb structures/5SF9/5sf9_ligand.sdf structures/5SF9/5sf9_ligand.pdb structures/5SF9/5sf9_ligand.cif structures/5SF9/5sf9_complex.pdb structures/5SF9/5sf9_complex.cif 5SFA classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1cc(-c2ccccc2)nc1COc1ncc(C2CC2)nc1C(=O)NC1CCOC1 "[""IJW""]" 1 pIC50 IC50 = = 6.82 151.3561248436207 [] p_metric_transform 6.82 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFA to this ligand and reports PDE10A pIC50 6.82. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFA\5SFA_metadata.json point structures/5SFA/5sfa_protein.pdb structures/5SFA/5sfa_pocket.pdb structures/5SFA/5sfa_ligand.sdf structures/5SFA/5sfa_ligand.pdb structures/5SFA/5sfa_ligand.cif structures/5SFA/5sfa_complex.pdb structures/5SFA/5sfa_complex.cif 5SFB classic human phosphodiesterase 10 (PDE10A) human Na Na CNC(=O)c1cc(CCc2nc(N3CCCC3)nn2C)nn2c(C)c(C)nc12 "[""IK0""]" 1 pIC50 IC50 = = 8.68 2.089296130854041 [] p_metric_transform 8.68 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFB to this ligand and reports PDE10A pIC50 8.68. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFB\5SFB_metadata.json point structures/5SFB/5sfb_protein.pdb structures/5SFB/5sfb_pocket.pdb structures/5SFB/5sfb_ligand.sdf structures/5SFB/5sfb_ligand.pdb structures/5SFB/5sfb_ligand.cif structures/5SFB/5sfb_complex.pdb structures/5SFB/5sfb_complex.cif 5SFC classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1ncc(C(=O)Nc2ccn3cc(-c4ccccc4)nc3n2)c1C(=O)N1CCC1 "[""IK6""]" 1 pIC50 IC50 = = 5.66 2187.761623949552 [] p_metric_transform 5.66 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFC to this ligand and reports PDE10A pIC50 5.66. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFC\5SFC_metadata.json point structures/5SFC/5sfc_protein.pdb structures/5SFC/5sfc_pocket.pdb structures/5SFC/5sfc_ligand.sdf structures/5SFC/5sfc_ligand.pdb structures/5SFC/5sfc_ligand.cif structures/5SFC/5sfc_complex.pdb structures/5SFC/5sfc_complex.cif 5SFD classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1ncc(C)n2nc(CCc3nc(N4CCCCC4)nn3C)nc12 "[""IKB""]" 1 pIC50 IC50 = = 7.50 31.622776601683793 [] p_metric_transform 7.5 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFD to this ligand and reports PDE10A pIC50 7.50. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFD\5SFD_metadata.json point structures/5SFD/5sfd_protein.pdb structures/5SFD/5sfd_pocket.pdb structures/5SFD/5sfd_ligand.sdf structures/5SFD/5sfd_ligand.pdb structures/5SFD/5sfd_ligand.cif structures/5SFD/5sfd_complex.pdb structures/5SFD/5sfd_complex.cif 5SFF classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1nc2ccc(C#Cc3nc(-c4ccccc4)cn3C)nn2c1CO "[""IKH""]" 1 pIC50 IC50 = = 8.99 1.0232929922807537 [] p_metric_transform 8.99 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFF to this ligand and reports PDE10A pIC50 8.99. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFF\5SFF_metadata.json point structures/5SFF/5sff_protein.pdb structures/5SFF/5sff_pocket.pdb structures/5SFF/5sff_ligand.sdf structures/5SFF/5sff_ligand.pdb structures/5SFF/5sff_ligand.cif structures/5SFF/5sff_complex.pdb structures/5SFF/5sff_complex.cif 5SFG classic human phosphodiesterase 10 (PDE10A) human Na Na O=C(N[C@@H]1CCN(c2ccc(Cl)cn2)C1)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IKK""]" 1 pIC50 IC50 = = 8.22 6.025595860743569 [] p_metric_transform 8.22 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFG to this ligand and reports PDE10A pIC50 8.22. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFG\5SFG_metadata.json point structures/5SFG/5sfg_protein.pdb structures/5SFG/5sfg_pocket.pdb structures/5SFG/5sfg_ligand.sdf structures/5SFG/5sfg_ligand.pdb structures/5SFG/5sfg_ligand.cif structures/5SFG/5sfg_complex.pdb structures/5SFG/5sfg_complex.cif 5SFH classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1ncc(C)n2nc(CCc3nc(N(C)C4CC4)nn3C)nc12 "[""IKO""]" 1 pIC50 IC50 = = 7.37 42.65795188015925 [] p_metric_transform 7.37 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFH to this ligand and reports PDE10A pIC50 7.37. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFH\5SFH_metadata.json point structures/5SFH/5sfh_protein.pdb structures/5SFH/5sfh_pocket.pdb structures/5SFH/5sfh_ligand.sdf structures/5SFH/5sfh_ligand.pdb structures/5SFH/5sfh_ligand.cif structures/5SFH/5sfh_complex.pdb structures/5SFH/5sfh_complex.cif 5SFI classic human phosphodiesterase 10 (PDE10A) human Na Na Cc1ncc(C)n2nc(CCc3nc(N4CCCC4C)nn3C)nc12 "[""IKU""]" 1 pIC50 IC50 = = 7.55 28.18382931264455 [] p_metric_transform 7.55 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFI to this ligand and reports PDE10A pIC50 7.55. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFI\5SFI_metadata.json point structures/5SFI/5sfi_protein.pdb structures/5SFI/5sfi_pocket.pdb structures/5SFI/5sfi_ligand.sdf structures/5SFI/5sfi_ligand.pdb structures/5SFI/5sfi_ligand.cif structures/5SFI/5sfi_complex.pdb structures/5SFI/5sfi_complex.cif 5SFJ classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1ncc(C(=O)NCc2ccccn2)c1C(=O)Nc1ccn2cc(-c3ccccc3)nc2n1 "[""IKZ""]" 1 pIC50 IC50 = = 7.93 11.748975549395302 [] p_metric_transform 7.93 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFJ to this ligand and reports PDE10A pIC50 7.93. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFJ\5SFJ_metadata.json point structures/5SFJ/5sfj_protein.pdb structures/5SFJ/5sfj_pocket.pdb structures/5SFJ/5sfj_ligand.sdf structures/5SFJ/5sfj_ligand.pdb structures/5SFJ/5sfj_ligand.cif structures/5SFJ/5sfj_complex.pdb structures/5SFJ/5sfj_complex.cif 5SFK classic human phosphodiesterase 10 (PDE10A) human Na Na O=C(Nc1ccn(CC(F)(F)F)n1)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IL6""]" 1 pIC50 IC50 = = 8.19 6.456542290346563 [] p_metric_transform 8.19 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFK to this ligand and reports PDE10A pIC50 8.19. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFK\5SFK_metadata.json point structures/5SFK/5sfk_protein.pdb structures/5SFK/5sfk_pocket.pdb structures/5SFK/5sfk_ligand.sdf structures/5SFK/5sfk_ligand.pdb structures/5SFK/5sfk_ligand.cif structures/5SFK/5sfk_complex.pdb structures/5SFK/5sfk_complex.cif 5SFL classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1ncc(NC(=O)c2nc(C3CC3)cnc2Nc2cncnc2)c1C(=O)NCC(C)(C)O "[""IL9""]" 1 pIC50 IC50 = = 8.51 3.090295432513592 [] p_metric_transform 8.51 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFL to this ligand and reports PDE10A pIC50 8.51. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFL\5SFL_metadata.json point structures/5SFL/5sfl_protein.pdb structures/5SFL/5sfl_pocket.pdb structures/5SFL/5sfl_ligand.sdf structures/5SFL/5sfl_ligand.pdb structures/5SFL/5sfl_ligand.cif structures/5SFL/5sfl_complex.pdb structures/5SFL/5sfl_complex.cif 5SFM classic human phosphodiesterase 10 (PDE10A) human Na Na Cn1ncc(C(=O)N2CCOCC2)c1C(=O)Nc1cc2nc(-c3ccccc3)nn2cn1 "[""ILN""]" 1 pIC50 IC50 = = 9.06 0.8709635899560796 [] p_metric_transform 9.06 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFM to this ligand and reports PDE10A pIC50 9.06. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFM\5SFM_metadata.json point structures/5SFM/5sfm_protein.pdb structures/5SFM/5sfm_pocket.pdb structures/5SFM/5sfm_ligand.sdf structures/5SFM/5sfm_ligand.pdb structures/5SFM/5sfm_ligand.cif structures/5SFM/5sfm_complex.pdb structures/5SFM/5sfm_complex.cif 5SFN classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na Cn1ncc(C(=O)N2CCC2)c1C(=O)NCCc1nc2ccccc2n1C "[""ILS""]" 1 pIC50 IC50 = = 7.80 15.848931924611142 [] p_metric_transform 7.8 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFN to this ligand and reports PDE10A pIC50 7.80. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFN\5SFN_metadata.json point structures/5SFN/5sfn_protein.pdb structures/5SFN/5sfn_pocket.pdb structures/5SFN/5sfn_ligand.sdf structures/5SFN/5sfn_ligand.pdb structures/5SFN/5sfn_ligand.cif structures/5SFN/5sfn_complex.pdb structures/5SFN/5sfn_complex.cif 5SFO classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na Cn1cc(-c2ccccc2)nc1CCNC(=O)c1c(C(=O)N2CCC2)cnn1C "[""ILZ""]" 1 pIC50 IC50 = = 8.55 2.8183829312644493 [] p_metric_transform 8.55 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFO to this ligand and reports PDE10A pIC50 8.55. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFO\5SFO_metadata.json point structures/5SFO/5sfo_protein.pdb structures/5SFO/5sfo_pocket.pdb structures/5SFO/5sfo_ligand.sdf structures/5SFO/5sfo_ligand.pdb structures/5SFO/5sfo_ligand.cif structures/5SFO/5sfo_complex.pdb structures/5SFO/5sfo_complex.cif 5SFP classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na O=C(Nc1ccnc(Cl)c1)c1ccc2cc(-c3ccccc3)nn2c1 "[""IO4""]" 1 pIC50 IC50 = = 7.43 37.15352290971728 [] p_metric_transform 7.43 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFP to this ligand and reports PDE10A pIC50 7.43. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFP\5SFP_metadata.json point structures/5SFP/5sfp_protein.pdb structures/5SFP/5sfp_pocket.pdb structures/5SFP/5sfp_ligand.sdf structures/5SFP/5sfp_ligand.pdb structures/5SFP/5sfp_ligand.cif structures/5SFP/5sfp_complex.pdb structures/5SFP/5sfp_complex.cif 5SFQ classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na Cn1ncc(C(=O)N2CCC2)c1C(=O)Nc1ccn(CC(F)F)n1 "[""IO7""]" 1 pIC50 IC50 = = 6.56 275.4228703338169 [] p_metric_transform 6.56 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFQ to this ligand and reports PDE10A pIC50 6.56. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFQ\5SFQ_metadata.json point structures/5SFQ/5sfq_protein.pdb structures/5SFQ/5sfq_pocket.pdb structures/5SFQ/5sfq_ligand.sdf structures/5SFQ/5sfq_ligand.pdb structures/5SFQ/5sfq_ligand.cif structures/5SFQ/5sfq_complex.pdb structures/5SFQ/5sfq_complex.cif 5SFR classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na CCN(C)C(=O)c1cnn(C)c1C(=O)Nc1ccn2cc(-c3cccc(OCCF)c3)nc2n1 "[""IOI""]" 1 pIC50 IC50 = = 8.21 6.16595001861481 [] p_metric_transform 8.21 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFR to this ligand and reports PDE10A pIC50 8.21. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFR\5SFR_metadata.json point structures/5SFR/5sfr_protein.pdb structures/5SFR/5sfr_pocket.pdb structures/5SFR/5sfr_ligand.sdf structures/5SFR/5sfr_ligand.pdb structures/5SFR/5sfr_ligand.cif structures/5SFR/5sfr_complex.pdb structures/5SFR/5sfr_complex.cif 5SFS classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na Cc1ncc(C)n2nc(CCc3nc(N4CC[C@H](C)C4)nn3C)nc12 "[""IOU""]" 1 pIC50 IC50 = = 7.94 11.481536214968818 [] p_metric_transform 7.94 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFS to this ligand and reports PDE10A pIC50 7.94. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFS\5SFS_metadata.json point structures/5SFS/5sfs_protein.pdb structures/5SFS/5sfs_pocket.pdb structures/5SFS/5sfs_ligand.sdf structures/5SFS/5sfs_ligand.pdb structures/5SFS/5sfs_ligand.cif structures/5SFS/5sfs_complex.pdb structures/5SFS/5sfs_complex.cif 5SFT classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na Cc1ncc(C)n2nc(CCc3nc(N4CCCC4)n(C)n3)nc12 "[""IOZ""]" 1 pIC50 IC50 = = 8.55 2.8183829312644493 [] p_metric_transform 8.55 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFT to this ligand and reports PDE10A pIC50 8.55. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFT\5SFT_metadata.json point structures/5SFT/5sft_protein.pdb structures/5SFT/5sft_pocket.pdb structures/5SFT/5sft_ligand.sdf structures/5SFT/5sft_ligand.pdb structures/5SFT/5sft_ligand.cif structures/5SFT/5sft_complex.pdb structures/5SFT/5sft_complex.cif 5SFU classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na O=C(Nc1cnccc1C(=O)N1CCCC1)c1nc(C2CC2)ccc1Nc1cncnc1 "[""IQ3""]" 1 pIC50 IC50 = = 7.73 18.620871366628656 [] p_metric_transform 7.73 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFU to this ligand and reports PDE10A pIC50 7.73. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFU\5SFU_metadata.json point structures/5SFU/5sfu_protein.pdb structures/5SFU/5sfu_pocket.pdb structures/5SFU/5sfu_ligand.sdf structures/5SFU/5sfu_ligand.pdb structures/5SFU/5sfu_ligand.cif structures/5SFU/5sfu_complex.pdb structures/5SFU/5sfu_complex.cif 5SFV classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na Cn1ncc(C(=O)N2CCC2)c1C(=O)Nc1ccn(C2CCCC2)n1 "[""IQ9""]" 1 pIC50 IC50 = = 7.12 75.85775750291836 [] p_metric_transform 7.12 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFV to this ligand and reports PDE10A pIC50 7.12. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFV\5SFV_metadata.json point structures/5SFV/5sfv_protein.pdb structures/5SFV/5sfv_pocket.pdb structures/5SFV/5sfv_ligand.sdf structures/5SFV/5sfv_ligand.pdb structures/5SFV/5sfv_ligand.cif structures/5SFV/5sfv_complex.pdb structures/5SFV/5sfv_complex.cif 5SFW classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na CCc1ncc(C)c2nc(CCc3nc(N4CCCC4)nn3C)nn12 "[""IQF""]" 1 pIC50 IC50 = = 8.31 4.897788193684456 [] p_metric_transform 8.31 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFW to this ligand and reports PDE10A pIC50 8.31. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFW\5SFW_metadata.json point structures/5SFW/5sfw_protein.pdb structures/5SFW/5sfw_pocket.pdb structures/5SFW/5sfw_ligand.sdf structures/5SFW/5sfw_ligand.pdb structures/5SFW/5sfw_ligand.cif structures/5SFW/5sfw_complex.pdb structures/5SFW/5sfw_complex.cif 5SFX classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na CC(=O)Nc1nc2cc(NC(=O)c3c(C(=O)N4CCC4)cnn3C)ccc2s1 "[""IQJ""]" 1 pIC50 IC50 = = 7.93 11.748975549395302 [] p_metric_transform 7.93 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFX to this ligand and reports PDE10A pIC50 7.93. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFX\5SFX_metadata.json point structures/5SFX/5sfx_protein.pdb structures/5SFX/5sfx_pocket.pdb structures/5SFX/5sfx_ligand.sdf structures/5SFX/5sfx_ligand.pdb structures/5SFX/5sfx_ligand.cif structures/5SFX/5sfx_complex.pdb structures/5SFX/5sfx_complex.cif 5SFY classic human phosphodiesterase 10 (PDE10A) human catalytic domain, residues 439-779, N-terminal His6 fusion with thrombin recognition sequence Na Cc1ncc(C)n2nc(/C=C/c3nc(-c4cn[nH]c4)nn3C)nc12 "[""IQV""]" 1 pIC50 IC50 = = 6.65 223.87211385683378 [] p_metric_transform 6.65 success True biochemical_inhibition Human PDE10A biochemical inhibition assay. 0 Supplementary Table S3 maps PDB 5SFY to this ligand and reports PDE10A pIC50 6.65. auto_single_measurement only accepted activity measurement [1] 1 structures\5SFY\5SFY_metadata.json point structures/5SFY/5sfy_protein.pdb structures/5SFY/5sfy_pocket.pdb structures/5SFY/5sfy_ligand.sdf structures/5SFY/5sfy_ligand.pdb structures/5SFY/5sfy_ligand.cif structures/5SFY/5sfy_complex.pdb structures/5SFY/5sfy_complex.cif 5SOJ classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na ZINC000642067873 (R) isomer "[""RWQ""]" 1 IC50 IC50 = = 90.3 µM 90300.0 [] unit_conversion 4.044312249686494 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay. 7 Fig. 5D prints “Z7873 (PDB 5SOJ) IC50 = 90.3 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\5SOJ\5SOJ_metadata.json point structures/5SOJ/5soj_protein.pdb structures/5SOJ/5soj_pocket.pdb structures/5SOJ/5soj_ligand.sdf structures/5SOJ/5soj_ligand.pdb structures/5SOJ/5soj_ligand.cif structures/5SOJ/5soj_complex.pdb structures/5SOJ/5soj_complex.cif 5SOL classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na ZINC000910475722 (S,R) isomer "[""WVM""]" 1 IC50 IC50 = = 464 µM 464000.0 [] unit_conversion 3.3334820194451193 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay. 7 Fig. 5D prints “Z5722 (PDB 5SOL) IC50 = 464 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\5SOL\5SOL_metadata.json point structures/5SOL/5sol_protein.pdb structures/5SOL/5sol_pocket.pdb structures/5SOL/5sol_ligand.sdf structures/5SOL/5sol_ligand.pdb structures/5SOL/5sol_ligand.cif structures/5SOL/5sol_complex.pdb structures/5SOL/5sol_complex.cif 5SOP classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na ZINC001364194305 (R) isomer "[""RYI""]" 1 IC50 IC50 = = 170 µM 170000.0 [] unit_conversion 3.769551078621726 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay. 7 Fig. 5D prints “Z4305 (PDB 5SOP) IC50 = 170 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\5SOP\5SOP_metadata.json point structures/5SOP/5sop_protein.pdb structures/5SOP/5sop_pocket.pdb structures/5SOP/5sop_ligand.sdf structures/5SOP/5sop_ligand.pdb structures/5SOP/5sop_ligand.cif structures/5SOP/5sop_complex.pdb structures/5SOP/5sop_complex.cif 5SOQ classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na ZINC000896845531 (R) isomer "[""WWJ""]" 1 IC50 IC50 = = 148 µM 148000.0 [] unit_conversion 3.8297382846050425 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay. 7 Fig. 5D prints “Z5531 (PDB 5SOQ) IC50 = 148 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\5SOQ\5SOQ_metadata.json point structures/5SOQ/5soq_protein.pdb structures/5SOQ/5soq_pocket.pdb structures/5SOQ/5soq_ligand.sdf structures/5SOQ/5soq_ligand.pdb structures/5SOQ/5soq_ligand.cif structures/5SOQ/5soq_complex.pdb structures/5SOQ/5soq_complex.cif 5SP3 classic SARS-CoV-2 NSP3 SARS-CoV-2 Na Na ZINC000450476923 - (S,R) isomer; Z6923 "[""WYJ""]" 1 IC50 IC50 = = 416 µM 416000.0 [] unit_conversion 3.3809066693732577 success True direct_binding HTRF-based ADPr-conjugated peptide displacement assay 7 Fig. 5D prints “Z6923 (PDB 5SP3) IC50 = 416 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\5SP3\5SP3_metadata.json point structures/5SP3/5sp3_protein.pdb structures/5SP3/5sp3_pocket.pdb structures/5SP3/5sp3_ligand.sdf structures/5SP3/5sp3_ligand.pdb structures/5SP3/5sp3_ligand.cif structures/5SP3/5sp3_complex.pdb structures/5SP3/5sp3_complex.cif 5SPE classic SARS-CoV-2 NSP3 SARS-CoV-2 Na Na Z4718398531 - (S,S) isomer; Z8531 "[""S1F""]" 1 IC50 IC50 > > 250 µM 250000.0 [] unit_conversion 3.6020599913279625 success True direct_binding HTRF-based ADPr-conjugated peptide displacement assay 4 Fig. 2D prints “Z8531 (PDB 5SPE) IC50 > 250 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\5SPE\5SPE_metadata.json point structures/5SPE/5spe_protein.pdb structures/5SPE/5spe_pocket.pdb structures/5SPE/5spe_ligand.sdf structures/5SPE/5spe_ligand.pdb structures/5SPE/5spe_ligand.cif structures/5SPE/5spe_complex.pdb structures/5SPE/5spe_complex.cif 5SPT classic SARS-CoV-2 NSP3 SARS-CoV-2 Na Na ZINC000850008207 (Z8207) "[""S6U""]" 1 IC50 IC50 = = 55.3 µM 55300.0 [] unit_conversion 4.257274868695302 success True direct_binding HTRF-based ADPr-conjugated peptide displacement assay. 7 Fig. 5D explicitly labels “Z8207 (PDB 5SPT) IC50 = 55.3 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\5SPT\5SPT_metadata.json point structures/5SPT/5spt_protein.pdb structures/5SPT/5spt_pocket.pdb structures/5SPT/5spt_ligand.sdf structures/5SPT/5spt_ligand.pdb structures/5SPT/5spt_ligand.cif structures/5SPT/5spt_complex.pdb structures/5SPT/5spt_complex.cif 5SPW classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na FRESH00004674769 - (R,S,R) isomer; F4769 "[""S5O""]" 1 IC50 IC50 = = 113 µM 113000.0 [] unit_conversion 3.94692155651658 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay 7 Fig. 5D prints: F4769 (PDB 5SPW), IC50 = 113 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\5SPW\5SPW_metadata.json point structures/5SPW/5spw_protein.pdb structures/5SPW/5spw_pocket.pdb structures/5SPW/5spw_ligand.sdf structures/5SPW/5spw_ligand.pdb structures/5SPW/5spw_ligand.cif structures/5SPW/5spw_complex.pdb structures/5SPW/5spw_complex.cif 5SPY extended SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na REAL300019621104 "[""QJ0""]" 1 IC50 IC50 = = 55.3 µM 55300.0 [] unit_conversion 4.257274868695302 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay 7 Fig. 5D prints: R1104 (PDB 5SPY), IC50 = 55.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\5SPY\5SPY_metadata.json point structures/5SPY/5spy_protein.pdb structures/5SPY/5spy_pocket.pdb structures/5SPY/5spy_ligand.pdb structures/5SPY/5spy_ligand.cif structures/5SPY/5spy_complex.pdb structures/5SPY/5spy_complex.cif 5SQ3 classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na Z5028367848 - (R) isomer; LL1_0014 "[""QK6""]" 1 IC50 IC50 range range 16.4–28.7 µM 16400.0 28700.0 [] range_unit_conversion success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay 9 Fig. 7C–D prints: LL1_0014 (PDB 5SQ3), IC50 = 16.4–28.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\5SQ3\5SQ3_metadata.json interval structures/5SQ3/5sq3_protein.pdb structures/5SQ3/5sq3_pocket.pdb structures/5SQ3/5sq3_ligand.sdf structures/5SQ3/5sq3_ligand.pdb structures/5SQ3/5sq3_ligand.cif structures/5SQ3/5sq3_complex.pdb structures/5SQ3/5sq3_complex.cif 5SQ6 classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na Z5010894406; Z8539_0027 "[""QL6""]" 1 IC50 IC50 = = 7.6 µM 7600.0 [] unit_conversion 5.119186407719209 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay 5 Fig. 3E–F prints: Z8539_0027 (PDB 5SQ6), IC50 = 7.6 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\5SQ6\5SQ6_metadata.json point structures/5SQ6/5sq6_protein.pdb structures/5SQ6/5sq6_pocket.pdb structures/5SQ6/5sq6_ligand.sdf structures/5SQ6/5sq6_ligand.pdb structures/5SQ6/5sq6_ligand.cif structures/5SQ6/5sq6_complex.pdb structures/5SQ6/5sq6_complex.cif 5SQ7 classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na Z1445235880; Z8539_0026 "[""QM6""]" 1 IC50 IC50 = = 83.8 µM 83800.0 [] unit_conversion 4.076755981369724 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay 5 Fig. 3E–F prints: Z8539_0026 (PDB 5SQ7), IC50 = 83.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\5SQ7\5SQ7_metadata.json point structures/5SQ7/5sq7_protein.pdb structures/5SQ7/5sq7_pocket.pdb structures/5SQ7/5sq7_ligand.sdf structures/5SQ7/5sq7_ligand.pdb structures/5SQ7/5sq7_ligand.cif structures/5SQ7/5sq7_complex.pdb structures/5SQ7/5sq7_complex.cif 5SQ8 classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na Z1445261766; Z8539_0025 "[""QMF""]" 1 IC50 IC50 = = 20.4 µM 20400.0 [] unit_conversion 4.690369832574102 success True biochemical_inhibition HTRF-based ADPr-conjugated peptide displacement assay 5 Fig. 3E–G prints: Z8539_0025 (PDB 5SQ8), IC50 = 20.4 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\5SQ8\5SQ8_metadata.json point structures/5SQ8/5sq8_protein.pdb structures/5SQ8/5sq8_pocket.pdb structures/5SQ8/5sq8_ligand.sdf structures/5SQ8/5sq8_ligand.pdb structures/5SQ8/5sq8_ligand.cif structures/5SQ8/5sq8_complex.pdb structures/5SQ8/5sq8_complex.cif 5SQU classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na REAL250004627335 (R7335) "[""QVL""]" 1 IC50 IC50 = = 42.2 µM 42200.0 [] unit_conversion 4.374687549038327 success True direct_binding HTRF-based ADPr-peptide displacement assay. 7 Fig. 5D labels R7335 (PDB 5SQU) with IC50 = 42.2 µM; the figure caption identifies HTRF-based peptide-displacement dose-response curves. auto_single_measurement only accepted activity measurement [1] 1 structures\5SQU\5SQU_metadata.json point structures/5SQU/5squ_protein.pdb structures/5SQU/5squ_pocket.pdb structures/5SQU/5squ_ligand.sdf structures/5SQU/5squ_ligand.pdb structures/5SQU/5squ_ligand.cif structures/5SQU/5squ_complex.pdb structures/5SQU/5squ_complex.cif 5UMB classic PfGRP78-NBD Plasmodium falciparum NBD, residues I26-G404 Na ADP "[""ADP""]" 1 Kd Kd = = 16.2 ± 2.8 μM 16200.0 [] unit_conversion 4.790484985457369 success True direct_binding Biacore SPR affinity measurement; buffer contained 2 mM MgCl2. 6 Table 2 reports PfGRP78-NBD ADP Kd = 16.2 ± 2.8 μM; the caption identifies these as SPR-derived affinity constants. auto_single_measurement only accepted activity measurement [1] 1 structures\5UMB\5UMB_metadata.json point structures/5UMB/5umb_protein.pdb structures/5UMB/5umb_pocket.pdb structures/5UMB/5umb_ligand.sdf structures/5UMB/5umb_ligand.pdb structures/5UMB/5umb_ligand.cif structures/5UMB/5umb_complex.pdb structures/5UMB/5umb_complex.cif 6L3Y classic Plasmodium falciparum lysyl-tRNA synthetase (PfKRS) Plasmodium falciparum Na Na Clado-C "[""E5C""]" 1 IC50 IC50 = = 7.9 µM 7900.0 [] unit_conversion 5.102372908709558 success True biochemical_inhibition In vitro PfKRS aminoacylation inhibition assay; L-lysine is included in the reported assay conditions. 10 Table 1 lists Clado-C: Pf IC50 7.9 µM. The text identifies 6L3Y as the PfKRS–L-lysine–Cla-C structure. auto_single_measurement only accepted activity measurement [1] 1 structures\6L3Y\6L3Y_metadata.json point structures/6L3Y/6l3y_protein.pdb structures/6L3Y/6l3y_pocket.pdb structures/6L3Y/6l3y_ligand.sdf structures/6L3Y/6l3y_ligand.pdb structures/6L3Y/6l3y_ligand.cif structures/6L3Y/6l3y_complex.pdb structures/6L3Y/6l3y_complex.cif 6L4Q classic Plasmodium falciparum lysyl-tRNA synthetase (PfKRS) Plasmodium falciparum Na Na Clado-B "[""E5R""]" 1 IC50 IC50 = = 6.2 µM 6200.0 [] unit_conversion 5.207608310501746 success True biochemical_inhibition In vitro PfKRS aminoacylation inhibition assay; L-lysine is included in the reported assay conditions. 10 Table 1 lists Clado-B: Pf IC50 6.2 µM. The text identifies 6L4Q as the PfKRS–L-lysine–Cla-B structure. auto_single_measurement only accepted activity measurement [1] 1 structures\6L4Q\6L4Q_metadata.json point structures/6L4Q/6l4q_protein.pdb structures/6L4Q/6l4q_pocket.pdb structures/6L4Q/6l4q_ligand.sdf structures/6L4Q/6l4q_ligand.pdb structures/6L4Q/6l4q_ligand.cif structures/6L4Q/6l4q_complex.pdb structures/6L4Q/6l4q_complex.cif 6LD0 classic Bifidobacterium dentium beta-glucuronidase Bifidobacterium dentium Na Na C6-hexyl uronic isofagomine (compound 3) "[""E8X""]" 1 Ki Ki = = 0.86 ± 0.2 μM 860.0 [] unit_conversion 6.065501548756432 success True biochemical_inhibition Purified BdGUS inhibition; Table 1 inhibition constants. 3 Table 1 reports BdGUS Ki for inhibitor 3 as 0.86 ± 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6LD0\6LD0_metadata.json point structures/6LD0/6ld0_protein.pdb structures/6LD0/6ld0_pocket.pdb structures/6LD0/6ld0_ligand.sdf structures/6LD0/6ld0_ligand.pdb structures/6LD0/6ld0_ligand.cif structures/6LD0/6ld0_complex.pdb structures/6LD0/6ld0_complex.cif 6LDB classic Bifidobacterium dentium beta-glucuronidase Bifidobacterium dentium Na Na uronic isofagomine (compound 1) "[""SJ5""]" 1 Ki Ki = = 0.0074 ± 0.002 μM 7.4 [] unit_conversion 8.130768280269024 success True biochemical_inhibition Purified BdGUS inhibition; Table 1 inhibition constants. 3 Table 1 reports BdGUS Ki for inhibitor 1 as 0.0074 ± 0.002 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6LDB\6LDB_metadata.json point structures/6LDB/6ldb_protein.pdb structures/6LDB/6ldb_pocket.pdb structures/6LDB/6ldb_ligand.sdf structures/6LDB/6ldb_ligand.pdb structures/6LDB/6ldb_ligand.cif structures/6LDB/6ldb_complex.pdb structures/6LDB/6ldb_complex.cif 6LDC classic Bifidobacterium dentium beta-glucuronidase Bifidobacterium dentium Na Na C6-nonyl uronic isofagomine (compound 4) "[""E9O""]" 1 Ki Ki = = 0.44 ± 0.02 μM 440.0 [] unit_conversion 6.356547323513812 success True biochemical_inhibition Purified BdGUS inhibition; Table 1 inhibition constants. 3 Table 1 reports BdGUS Ki for inhibitor 4 as 0.44 ± 0.02 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6LDC\6LDC_metadata.json point structures/6LDC/6ldc_protein.pdb structures/6LDC/6ldc_pocket.pdb structures/6LDC/6ldc_ligand.sdf structures/6LDC/6ldc_ligand.pdb structures/6LDC/6ldc_ligand.cif structures/6LDC/6ldc_complex.pdb structures/6LDC/6ldc_complex.cif 6LDD classic Bifidobacterium dentium beta-glucuronidase Bifidobacterium dentium Na Na C6-propyl uronic isofagomine (compound 2) "[""CKX""]" 1 Ki Ki = = 4.9 ± 1.2 μM 4900.0 [] unit_conversion 5.309803919971486 success True biochemical_inhibition Purified BdGUS inhibition; Table 1 inhibition constants. 3 Table 1 reports BdGUS Ki for inhibitor 2 as 4.9 ± 1.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6LDD\6LDD_metadata.json point structures/6LDD/6ldd_protein.pdb structures/6LDD/6ldd_pocket.pdb structures/6LDD/6ldd_ligand.sdf structures/6LDD/6ldd_ligand.pdb structures/6LDD/6ldd_ligand.cif structures/6LDD/6ldd_complex.pdb structures/6LDD/6ldd_complex.cif 6LEG classic E. coli beta-glucuronidase E. coli Na Na uronic isofagomine (compound 1) "[""SJ5""]" 1 Ki Ki = = 0.016 ± 0.002 μM 16.0 [] unit_conversion 7.795880017344075 success True biochemical_inhibition Purified EcGUS inhibition; Table 1 inhibition constants. 3 Table 1 reports EcGUS Ki for inhibitor 1 as 0.016 ± 0.002 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6LEG\6LEG_metadata.json point structures/6LEG/6leg_protein.pdb structures/6LEG/6leg_pocket.pdb structures/6LEG/6leg_ligand.sdf structures/6LEG/6leg_ligand.pdb structures/6LEG/6leg_ligand.cif structures/6LEG/6leg_complex.pdb structures/6LEG/6leg_complex.cif 6LEJ classic E. coli beta-glucuronidase E. coli Na Na C6-propyl uronic isofagomine (compound 2) "[""CKX""]" 1 Ki Ki = = 0.035 ± 0.009 μM 35.0 [] unit_conversion 7.455931955649724 success True biochemical_inhibition Purified EcGUS inhibition; Table 1 inhibition constants. 3 Table 1 reports EcGUS Ki for inhibitor 2 as 0.035 ± 0.009 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6LEJ\6LEJ_metadata.json point structures/6LEJ/6lej_protein.pdb structures/6LEJ/6lej_pocket.pdb structures/6LEJ/6lej_ligand.sdf structures/6LEJ/6lej_ligand.pdb structures/6LEJ/6lej_ligand.cif structures/6LEJ/6lej_complex.pdb structures/6LEJ/6lej_complex.cif 6LEL classic E. coli beta-glucuronidase E. coli Na Na C6-hexyl uronic isofagomine (compound 3) "[""E8X""]" 1 Ki Ki = = 0.003 ± 0.0006 μM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Purified EcGUS inhibition; Table 1 inhibition constants. 3 Table 1 reports EcGUS Ki for inhibitor 3 as 0.003 ± 0.0006 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6LEL\6LEL_metadata.json point structures/6LEL/6lel_protein.pdb structures/6LEL/6lel_pocket.pdb structures/6LEL/6lel_ligand.sdf structures/6LEL/6lel_ligand.pdb structures/6LEL/6lel_ligand.cif structures/6LEL/6lel_complex.pdb structures/6LEL/6lel_complex.cif 6LEM classic E. coli beta-glucuronidase E. coli Na Na C6-nonyl uronic isofagomine (compound 4) "[""E9O""]" 1 Ki Ki = = 0.0045 ± 0.0007 μM 4.5 [] unit_conversion 8.346787486224656 success True biochemical_inhibition Purified EcGUS inhibition; Table 1 inhibition constants. 3 Table 1 reports EcGUS Ki for inhibitor 4 as 0.0045 ± 0.0007 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6LEM\6LEM_metadata.json point structures/6LEM/6lem_protein.pdb structures/6LEM/6lem_pocket.pdb structures/6LEM/6lem_ligand.sdf structures/6LEM/6lem_ligand.pdb structures/6LEM/6lem_ligand.cif structures/6LEM/6lem_complex.pdb structures/6LEM/6lem_complex.cif 6LN1 classic dual-specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A) Na Na Na desmethylbellidifolin (DMB; compound 1) "[""EKU""]" 1 Kd Kd = = 5.11 ± 0.33 µM 5110.0 [] unit_conversion 5.291579099865287 success True direct_binding Microscale thermophoresis measurement of DMB binding to DYRK1A. 1 “The equilibrium dissociation constant (Kd) of DMB (compound 1, 5.11 ± 0.33 μM) with DYRK1A (Figure 1A)…” auto_single_measurement only accepted activity measurement [1] 1 structures\6LN1\6LN1_metadata.json point structures/6LN1/6ln1_protein.pdb structures/6LN1/6ln1_pocket.pdb structures/6LN1/6ln1_ligand.sdf structures/6LN1/6ln1_ligand.pdb structures/6LN1/6ln1_ligand.cif structures/6LN1/6ln1_complex.pdb structures/6LN1/6ln1_complex.cif 6LNN classic MERS-CoV nucleocapsid protein N MERS-CoV MERS-CoV N39-165 protein with a histidine tag Na P4-1; 5-(Propoxy)-1H-indole "[""EJC""]" 1 Kd Kd = = 23.4 ± 4.94 μM 23400.0 [] unit_conversion 4.6307841425898575 success True direct_binding Fluorescent quenching assay of purified MERS-CoV N-NTD with P4-1. 7 “The values of binding constant (Kd) for MERS-CoV-N-NTD to P4-1 ... is found to be 23.4 ± 4.94 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\6LNN\6LNN_metadata.json point structures/6LNN/6lnn_protein.pdb structures/6LNN/6lnn_pocket.pdb structures/6LNN/6lnn_ligand.sdf structures/6LNN/6lnn_ligand.pdb structures/6LNN/6lnn_ligand.cif structures/6LNN/6lnn_complex.pdb structures/6LNN/6lnn_complex.cif 6LRM classic PDE4D Na Na Na arctigenin "[""EQC""]" 2 Kd Kd = = 6.275E-6 ± 1.754E-6 M 6275.0 [] unit_conversion 5.202386269846924 success True direct_binding Isothermal titration calorimetry binding profile of arctigenin to the PDE4D catalytic domain (Fig. 1C). 5 Fig. 1C's printed one-site ITC fit reports Kd = 6.275E-6 ± 1.754E-6 M; the legend identifies it as binding to the PDE4D catalytic domain. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\6LRM\6LRM_metadata.json point structures/6LRM/6lrm_protein.pdb structures/6LRM/6lrm_pocket.pdb structures/6LRM/6lrm_ligand.sdf structures/6LRM/6lrm_ligand.pdb structures/6LRM/6lrm_ligand.cif structures/6LRM/6lrm_complex.pdb structures/6LRM/6lrm_complex.cif 6LTK classic Hsp90 Homo sapiens Hsp90N residues 9-236; artificially synthesized gene cloned into pET-28a and expressed in E. coli BL21(DE3) Na SNX-2112 "[""E0G""]" 1 Kd Kd = = 14.10 ± 1.60 nM 14.1 [] unit_conversion 7.85078088734462 success True direct_binding Isothermal titration calorimetry (ITC), 25 °C; purified Hsp90N titrated with SNX-2112; bimolecular binding fit. 7 Table 1 reports Kd 14.10 ± 1.60 nM for the Hsp90N–SNX-2112 binding process at 25 °C. The main text identifies the crystallographic complex as Hsp90N–SNX-2112, PDB ID 6LTK. auto_single_measurement only accepted activity measurement [1] 1 structures\6LTK\6LTK_metadata.json point structures/6LTK/6ltk_protein.pdb structures/6LTK/6ltk_pocket.pdb structures/6LTK/6ltk_ligand.sdf structures/6LTK/6ltk_ligand.pdb structures/6LTK/6ltk_ligand.cif structures/6LTK/6ltk_complex.pdb structures/6LTK/6ltk_complex.cif 6M0P classic Hydroxylamine oxidoreductase (NeHAO) Nitrosomonas europaea Na Na juglone "[""JUG""]" 1 IC50 IC50 = = 5.5 nM 5.5 [] unit_conversion 8.259637310505756 success True biochemical_inhibition Inhibition of NeHAO-coupled electron transfer to resazurin during hydroxylamine oxidation; IC50 fitted to a dose-dependent sigmoidal curve. 7 The text states that juglone, plumbagin, and 1,4-NQ inhibited the reaction in a dose-dependent manner with IC50 values of 5.5 nM, 23.7 nM, and 9.8 nM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\6M0P\6M0P_metadata.json point structures/6M0P/6m0p_protein.pdb structures/6M0P/6m0p_pocket.pdb structures/6M0P/6m0p_ligand.sdf structures/6M0P/6m0p_ligand.pdb structures/6M0P/6m0p_ligand.cif structures/6M0P/6m0p_complex.pdb structures/6M0P/6m0p_complex.cif 6M0T classic Lysyl-tRNA synthetase (PfKRS) Plasmodium falciparum Na Na CL-2 "[""EZ3""]" 1 IC50 IC50 = = 0.1 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition PfKRS aminoacylation/ATP-hydrolysis inhibition assay. 8 Table 1 reports CL-2 IC50 = 0.1 µM against P. falciparum; the same page's Figure 3 caption identifies the PfKRS+CL-2+L-lys crystal structure as PDB ID 6M0T. auto_single_measurement only accepted activity measurement [1] 1 structures\6M0T\6M0T_metadata.json point structures/6M0T/6m0t_protein.pdb structures/6M0T/6m0t_pocket.pdb structures/6M0T/6m0t_ligand.sdf structures/6M0T/6m0t_ligand.pdb structures/6M0T/6m0t_ligand.cif structures/6M0T/6m0t_complex.pdb structures/6M0T/6m0t_complex.cif 6M63 classic G-Flamp1 Na cAMP-bound G-Flamp1 without RSET tag P285N; D173G; S308V cAMP "[""CMP""]" 1 Kd Kd = = 2.17 μM 2170.0 [] unit_conversion 5.66354026615147 success True direct_binding Binding titration of purified G-Flamp1 with cAMP in HEPES buffer (pH 7.15); fluorescence change fitted by a sigmoidal binding function. 2 “The concentration-response curves showed that Kd values of G-Flamp1 for cAMP and cGMP were 2.17 and 30.09 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\6M63\6M63_metadata.json point structures/6M63/6m63_protein.pdb structures/6M63/6m63_pocket.pdb structures/6M63/6m63_ligand.sdf structures/6M63/6m63_ligand.pdb structures/6M63/6m63_ligand.cif structures/6M63/6m63_complex.pdb structures/6M63/6m63_complex.cif 6M6D classic Arabidopsis thaliana 4-hydroxyphenylpyruvate dioxygenase (AtHPPD) Arabidopsis thaliana Na Na compound 60 "[""NJX""]" 2 Ki Ki = = 0.86 ± 0.023 nM 0.86 [] unit_conversion 9.065501548756432 success True biochemical_inhibition Time-dependent inhibitory kinetics; Ki calculated from k−0/k+0. 10 The text reports compound 60 Ki = 0.86 ± 0.023 nM from the fitted kinetic equations. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\6M6D\6M6D_metadata.json point structures/6M6D/6m6d_protein.pdb structures/6M6D/6m6d_pocket.pdb structures/6M6D/6m6d_ligand.sdf structures/6M6D/6m6d_ligand.pdb structures/6M6D/6m6d_ligand.cif structures/6M6D/6m6d_complex.pdb structures/6M6D/6m6d_complex.cif 6PLO classic zebra fish alpha-1 glycine receptor YGF mutant zebra fish full-length zebrafish alpha1 glycine receptor in SMA F175Y/Y177F GABA "[""ABU""]" 1 Ki Ki = = 0.18 ± 0.07 mM 180000.0 [] unit_conversion 3.7447274948966935 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; YGF mutant in SMA. 7 Figure 4 caption: Ki of GABA to YGF mutant was 0.18 ± 0.07 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLO\6PLO_metadata.json point structures/6PLO/6plo_protein.pdb structures/6PLO/6plo_pocket.pdb structures/6PLO/6plo_ligand.sdf structures/6PLO/6plo_ligand.pdb structures/6PLO/6plo_ligand.cif structures/6PLO/6plo_complex.pdb structures/6PLO/6plo_complex.cif 6PLP classic zebra fish alpha-1 glycine receptor YGF mutant zebra fish full-length zebrafish alpha1 glycine receptor in SMA F175Y/Y177F GABA "[""ABU""]" 1 Ki Ki = = 0.18 ± 0.07 mM 180000.0 [] unit_conversion 3.7447274948966935 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; YGF mutant in SMA. 7 Figure 4 caption: Ki of GABA to YGF mutant was 0.18 ± 0.07 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLP\6PLP_metadata.json point structures/6PLP/6plp_protein.pdb structures/6PLP/6plp_pocket.pdb structures/6PLP/6plp_ligand.sdf structures/6PLP/6plp_ligand.pdb structures/6PLP/6plp_ligand.cif structures/6PLP/6plp_complex.pdb structures/6PLP/6plp_complex.cif 6PLQ classic zebra fish alpha-1 glycine receptor YGF mutant zebra fish full-length zebrafish alpha1 glycine receptor in SMA F175Y/Y177F GABA "[""ABU""]" 1 Ki Ki = = 0.18 ± 0.07 mM 180000.0 [] unit_conversion 3.7447274948966935 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; YGF mutant in SMA. 7 Figure 4 caption: Ki of GABA to YGF mutant was 0.18 ± 0.07 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLQ\6PLQ_metadata.json point structures/6PLQ/6plq_protein.pdb structures/6PLQ/6plq_pocket.pdb structures/6PLQ/6plq_ligand.sdf structures/6PLQ/6plq_ligand.pdb structures/6PLQ/6plq_ligand.cif structures/6PLQ/6plq_complex.pdb structures/6PLQ/6plq_complex.cif 6PLU classic zebra fish alpha-1 glycine receptor zebra fish full-length zebrafish alpha1 glycine receptor reconstituted in nanodisc Na GABA "[""ABU""]" 1 Ki Ki = = 1.41 ± 0.94 mM 1410000.0 [] unit_conversion 2.8507808873446203 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; full-length receptor in SMA. 7 Figure 4 caption: Ki of GABA to FL was 1.41 ± 0.94 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLU\6PLU_metadata.json point structures/6PLU/6plu_protein.pdb structures/6PLU/6plu_pocket.pdb structures/6PLU/6plu_ligand.sdf structures/6PLU/6plu_ligand.pdb structures/6PLU/6plu_ligand.cif structures/6PLU/6plu_complex.pdb structures/6PLU/6plu_complex.cif 6PLV classic zebra fish alpha-1 glycine receptor zebra fish full-length zebrafish alpha1 glycine receptor reconstituted in nanodisc Na GABA "[""ABU""]" 1 Ki Ki = = 1.41 ± 0.94 mM 1410000.0 [] unit_conversion 2.8507808873446203 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; full-length receptor in SMA. 7 Figure 4 caption: Ki of GABA to FL was 1.41 ± 0.94 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLV\6PLV_metadata.json point structures/6PLV/6plv_protein.pdb structures/6PLV/6plv_pocket.pdb structures/6PLV/6plv_ligand.sdf structures/6PLV/6plv_ligand.pdb structures/6PLV/6plv_ligand.cif structures/6PLV/6plv_complex.pdb structures/6PLV/6plv_complex.cif 6PLW classic zebra fish alpha-1 glycine receptor zebra fish full-length zebrafish alpha1 glycine receptor in SMA Na GABA "[""ABU""]" 1 Ki Ki = = 1.41 ± 0.94 mM 1410000.0 [] unit_conversion 2.8507808873446203 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; full-length receptor in SMA. 7 Figure 4 caption: Ki of GABA to FL was 1.41 ± 0.94 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLW\6PLW_metadata.json point structures/6PLW/6plw_protein.pdb structures/6PLW/6plw_pocket.pdb structures/6PLW/6plw_ligand.sdf structures/6PLW/6plw_ligand.pdb structures/6PLW/6plw_ligand.cif structures/6PLW/6plw_complex.pdb structures/6PLW/6plw_complex.cif 6PLX classic zebra fish alpha-1 glycine receptor zebra fish full-length zebrafish alpha1 glycine receptor in SMA Na GABA "[""ABU""]" 1 Ki Ki = = 1.41 ± 0.94 mM 1410000.0 [] unit_conversion 2.8507808873446203 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; full-length receptor in SMA. 7 Figure 4 caption: Ki of GABA to FL was 1.41 ± 0.94 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLX\6PLX_metadata.json point structures/6PLX/6plx_protein.pdb structures/6PLX/6plx_pocket.pdb structures/6PLX/6plx_ligand.sdf structures/6PLX/6plx_ligand.pdb structures/6PLX/6plx_ligand.cif structures/6PLX/6plx_complex.pdb structures/6PLX/6plx_complex.cif 6PLY classic zebra fish alpha-1 glycine receptor zebra fish full-length zebrafish alpha1 glycine receptor in SMA Na GABA "[""ABU""]" 1 Ki Ki = = 1.41 ± 0.94 mM 1410000.0 [] unit_conversion 2.8507808873446203 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; full-length receptor in SMA. 7 Figure 4 caption: Ki of GABA to FL was 1.41 ± 0.94 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLY\6PLY_metadata.json point structures/6PLY/6ply_protein.pdb structures/6PLY/6ply_pocket.pdb structures/6PLY/6ply_ligand.sdf structures/6PLY/6ply_ligand.pdb structures/6PLY/6ply_ligand.cif structures/6PLY/6ply_complex.pdb structures/6PLY/6ply_complex.cif 6PLZ classic zebra fish alpha-1 glycine receptor zebra fish full-length zebrafish alpha1 glycine receptor in SMA Na GABA "[""ABU""]" 1 Ki Ki = = 1.41 ± 0.94 mM 1410000.0 [] unit_conversion 2.8507808873446203 success True direct_binding Competition ligand-binding experiment using [3H]-strychnine; full-length receptor in SMA. 7 Figure 4 caption: Ki of GABA to FL was 1.41 ± 0.94 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6PLZ\6PLZ_metadata.json point structures/6PLZ/6plz_protein.pdb structures/6PLZ/6plz_pocket.pdb structures/6PLZ/6plz_ligand.sdf structures/6PLZ/6plz_ligand.pdb structures/6PLZ/6plz_ligand.cif structures/6PLZ/6plz_complex.pdb structures/6PLZ/6plz_complex.cif 6PZ0 classic TnIYD (iodotyrosine deiodinase) Thermotoga neapolitana TnIYD with a C-terminal (His)6 tag Na L-Tyrosine (Tyr) "[""TYR""]" 1 Kd Kd = = 0.45 ± 0.07 µM 450.0 [] unit_conversion 6.346787486224656 success True direct_binding Ligand-dependent quenching of oxidized FMN fluorescence; 25 °C. Table 3 reports binding affinity of Tyr to WT TnIYD. 7 Table 3, “Binding affinity of I-Tyr and Tyr as a function of side chain substitution (25 °C),” reports for TnIYD wt: Tyr Kd = 0.45 ± 0.07 µM. The binding-affinity method is described as ligand-dependent FMN fluorescence quenching. auto_single_measurement only accepted activity measurement [1] 1 structures\6PZ0\6PZ0_metadata.json point structures/6PZ0/6pz0_protein.pdb structures/6PZ0/6pz0_pocket.pdb structures/6PZ0/6pz0_ligand.sdf structures/6PZ0/6pz0_ligand.pdb structures/6PZ0/6pz0_ligand.cif structures/6PZ0/6pz0_complex.pdb structures/6PZ0/6pz0_complex.cif 6Q1L classic TnIYD (iodotyrosine deiodinase) Thermotoga neapolitana TnIYD with a C-terminal (His)6 tag Na 3-iodo-L-tyrosine (I-Tyr) "[""IYR""]" 1 Kd Kd = = 0.05 ± 0.02 µM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding Ligand-dependent quenching of oxidized FMN fluorescence; 25 °C. Table 3 reports binding affinity of I-Tyr to WT TnIYD. 7 Table 3, “Binding affinity of I-Tyr and Tyr as a function of side chain substitution (25 °C),” reports for TnIYD wt: I-Tyr Kd = 0.05 ± 0.02 µM. The binding-affinity method is described as ligand-dependent FMN fluorescence quenching. auto_single_measurement only accepted activity measurement [1] 1 structures\6Q1L\6Q1L_metadata.json point structures/6Q1L/6q1l_protein.pdb structures/6Q1L/6q1l_pocket.pdb structures/6Q1L/6q1l_ligand.sdf structures/6Q1L/6q1l_ligand.pdb structures/6Q1L/6q1l_ligand.cif structures/6Q1L/6q1l_complex.pdb structures/6Q1L/6q1l_complex.cif 6QSU classic Helicobacter pylori urease Helicobacter pylori Recombinant urease expressed in E. coli BL21(DE3) using pHP808 and pHP902; pHP808 contains the entire urease gene cluster and pHP902 contains ureA and ureB Na BME (beta-mercaptoethanol) "[""BME""]" 2 Ki Ki = = 435 µM 435000.0 [] unit_conversion 3.361510743045363 success True biochemical_inhibition Competitive-inhibition Ki derived using the Cheng-Prusoff equation from the BME IC50 assay, with 6 mM urea and reported Km of 0.2 mM. 4 Fig. 3 caption states that the BME IC50 corresponds to Ki = 435 µM; page 3 also explicitly reports this Ki value. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\6QSU\6QSU_metadata.json point structures/6QSU/6qsu_protein.pdb structures/6QSU/6qsu_pocket.pdb structures/6QSU/6qsu_ligand.sdf structures/6QSU/6qsu_ligand.pdb structures/6QSU/6qsu_ligand.cif structures/6QSU/6qsu_complex.pdb structures/6QSU/6qsu_complex.cif 6R6A extended Major aspartyl peptidase 1 (May1) Cryptococcus neoformans var. grubii H99 May1(17-434)-Avi Na PepA (pepstatin A) "[""CHAIN:D""]" 1 Ki Ki = = 1.3 ± 0.1 nM 1.3 [] unit_conversion 8.886056647693163 success True biochemical_inhibition May1(17-434)-Avi inhibition assay; PepA is identified as pepstatin A. 5 “May1(17-434)-Avi is inhibited by both PepA and acetyl pepstatin with Ki values of 1.3 ± 0.1 and 3.3 ± 0.1 nM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\6R6A\6R6A_metadata.json point structures/6R6A/6r6a_protein.pdb structures/6R6A/6r6a_pocket.pdb structures/6R6A/6r6a_ligand.pdb structures/6R6A/6r6a_ligand.cif structures/6R6A/6r6a_complex.pdb structures/6R6A/6r6a_complex.cif 6SQU classic human SHIP2 catalytic domain human Na Na 1,2,4-dimer (5); 5,5'-ethane-1,2-diylbis(oxy)bis(benzene-1,2,4-trisphosphate) "[""D7I""]" 4 Ki Ki = = 4.9 µM 4900.0 [] unit_conversion 5.309803919971486 success True biochemical_inhibition Mixed-inhibition kinetic analysis of SHIP2cd with Ins(1,3,4,5)P4 substrate. 8 The text states that the Ki determined for 1,2,4-dimer (5) is 4.9 µM. auto_metric_priority unique highest-priority metric family: Ki [4] 5 structures\6SQU\6SQU_metadata.json point structures/6SQU/6squ_protein.pdb structures/6SQU/6squ_pocket.pdb structures/6SQU/6squ_ligand.sdf structures/6SQU/6squ_ligand.pdb structures/6SQU/6squ_ligand.cif structures/6SQU/6squ_complex.pdb structures/6SQU/6squ_complex.cif 6TCJ extended BCL6 (B-cell lymphoma 6) Human BCL6 BTB domain residues 6-129, BCL6 BTB-TM construct C8Q; C67R; C84N Hybrid BTB-binding peptide, HBP (PGGFLCWDGRSIHEIPR) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 6.51 ± 2.10 µM 6510.0 [] unit_conversion 5.186419011431807 success True direct_binding ITC titration of HBP into BCL6 BTB-TM; N = 0.92 ± 0.13. 7 “The interaction of the HBP and BCL6BTB-TM was determined by ITC, and had a Kd of 6.51 ± 2.10 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\6TCJ\6TCJ_metadata.json point structures/6TCJ/6tcj_protein.pdb structures/6TCJ/6tcj_pocket.pdb structures/6TCJ/6tcj_ligand.pdb structures/6TCJ/6tcj_ligand.cif structures/6TCJ/6tcj_complex.pdb structures/6TCJ/6tcj_complex.cif 6TE7 classic CYP121 Mycobacterium tuberculosis Recombinant CYP121 expressed from pET21; C-terminal His6 tag removed before crystallization Na S2 "[""N55""]" 1 Kd Kd = = 8.3 ± 1.7 µM 8300.0 [] unit_conversion 5.080921907623926 success True direct_binding UV/Vis heme-binding assay; concentration-dependent titration of CYP121 with S2. 8 Table 2 lists co-crystallized compound S2 with K_D ± STD of 8.3 ± 1.7 µM; the paper describes the K_D determinations as UV/Vis heme-binding measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\6TE7\6TE7_metadata.json point structures/6TE7/6te7_protein.pdb structures/6TE7/6te7_pocket.pdb structures/6TE7/6te7_ligand.sdf structures/6TE7/6te7_ligand.pdb structures/6TE7/6te7_ligand.cif structures/6TE7/6te7_complex.pdb structures/6TE7/6te7_complex.cif 6TES classic Lysyl Hydroxylase LH3 human full-length Na UDP-Glucuronic Acid "[""UGA""]" 1 IC50 IC50 = = 1130 ± 370 µM 1130000.0 [] unit_conversion 2.94692155651658 success True biochemical_inhibition Competitive inhibition in the presence of UDP-Gal and acceptor substrates. 14 Table 2 reports wild-type + UDP-GlcA, UDP-Gal (IC50, µM): 1130 ± 370. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\6TES\6TES_metadata.json point structures/6TES/6tes_protein.pdb structures/6TES/6tes_pocket.pdb structures/6TES/6tes_ligand.sdf structures/6TES/6tes_ligand.pdb structures/6TES/6tes_ligand.cif structures/6TES/6tes_complex.pdb structures/6TES/6tes_complex.cif 6TET classic CYP121 Mycobacterium tuberculosis Recombinant CYP121 expressed from pET21; C-terminal His6 tag removed before crystallization Na L21 "[""N5Z""]" 1 Kd Kd = = 5.9 ± 0.6 µM 5900.0 [] unit_conversion 5.229147988357855 success True direct_binding UV/Vis heme-binding assay; concentration-dependent titration of CYP121 with L21. 8 Table 2 lists co-crystallized compound L21 with K_D ± STD of 5.9 ± 0.6 µM; the paper describes the K_D determinations as UV/Vis heme-binding measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\6TET\6TET_metadata.json point structures/6TET/6tet_protein.pdb structures/6TET/6tet_pocket.pdb structures/6TET/6tet_ligand.sdf structures/6TET/6tet_ligand.pdb structures/6TET/6tet_ligand.cif structures/6TET/6tet_complex.pdb structures/6TET/6tet_complex.cif 6TEV classic CYP121 Mycobacterium tuberculosis Recombinant CYP121 expressed from pET21; C-terminal His6 tag removed before crystallization Na L44 "[""N5W""]" 1 Kd Kd = = 5.6 ± 0.9 µM 5600.0 [] unit_conversion 5.251811972993799 success True direct_binding UV/Vis heme-binding assay; concentration-dependent titration of CYP121 with L44. 8 Table 2 lists co-crystallized compound L44 with K_D ± STD of 5.6 ± 0.9 µM; the paper describes the K_D determinations as UV/Vis heme-binding measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\6TEV\6TEV_metadata.json point structures/6TEV/6tev_protein.pdb structures/6TEV/6tev_pocket.pdb structures/6TEV/6tev_ligand.sdf structures/6TEV/6tev_ligand.pdb structures/6TEV/6tev_ligand.cif structures/6TEV/6tev_complex.pdb structures/6TEV/6tev_complex.cif 6TGW classic Aldehyde dehydrogenase 1A3 (ALDH1A3) human Full-length human ALDH1A3 with an N-terminal 6xHis tag Na MCI-INI-3 "[""N98""]" 2 Ki Ki = = 0.55 ± 0.11 µM 550.0 [] unit_conversion 6.259637310505756 success True biochemical_inhibition Steady-state enzyme kinetics of purified recombinant human ALDH1A3 with MCI-INI-3; competitive inhibition for the aldehyde substrate. 6 “Michaelis-Menten kinetics ... MCI-INI-3 to be a competitive inhibitor ... with Ki values of 0.55 ± 0.11 µM for ALDH1A3.” auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\6TGW\6TGW_metadata.json point structures/6TGW/6tgw_protein.pdb structures/6TGW/6tgw_pocket.pdb structures/6TGW/6tgw_ligand.sdf structures/6TGW/6tgw_ligand.pdb structures/6TGW/6tgw_ligand.cif structures/6TGW/6tgw_complex.pdb structures/6TGW/6tgw_complex.cif 6TNQ extended human Arc human hArc-NL residues 207-277; cleavable His-MBP tag removed by TEV; N-terminal GAMG sequence Na GKAP-R4 (GKAP repeat 4 peptide) "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F""]" 1 Kd Kd = = 714 ± 19 µM 714000.0 [] unit_conversion 3.146301788223826 success True direct_binding Isothermal titration calorimetry; hArc-NL with GKAP-R4. 3 Table 2 reports hArc-NL–GKAP-R4 Kd 714 ± 19 µM; Table 3 maps hArc-NL + GKAP-R4 to PDB 6TNQ. auto_single_measurement only accepted activity measurement [1] 1 structures\6TNQ\6TNQ_metadata.json point structures/6TNQ/6tnq_protein.pdb structures/6TNQ/6tnq_pocket.pdb structures/6TNQ/6tnq_ligand.pdb structures/6TNQ/6tnq_ligand.cif structures/6TNQ/6tnq_complex.pdb structures/6TNQ/6tnq_complex.cif 6TQ0 extended human Arc human hArc-NL residues 207-277; cleavable His-MBP tag removed by TEV; N-terminal GAMG sequence Na GKAP-R5 (GKAP repeat 5 peptide) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 2390 ± 314 µM 2390000.0 [] unit_conversion 2.621602099051862 success True direct_binding Isothermal titration calorimetry; hArc-NL with GKAP-R5. 3 Table 2 reports hArc-NL–GKAP-R5 Kd 2390 ± 314 µM; Table 3 maps hArc-NL + GKAP-R5 to PDB 6TQ0. auto_single_measurement only accepted activity measurement [1] 1 structures\6TQ0\6TQ0_metadata.json point structures/6TQ0/6tq0_protein.pdb structures/6TQ0/6tq0_pocket.pdb structures/6TQ0/6tq0_ligand.pdb structures/6TQ0/6tq0_ligand.cif structures/6TQ0/6tq0_complex.pdb structures/6TQ0/6tq0_complex.cif 6TTA classic NDM-1 Na Na Na quercetin "[""QUE""]" 1 IC50 IC50 range range 5–10 µM 5000.0 10000.0 [] range_unit_conversion success True biochemical_inhibition Purified NDM-1 inhibition assay; quercetin IC50 could only be estimated because of solubility problems. The IC50 assay used 50 µM ZnSO4 and 100 µM imipenem. 4 “IC50 values for quercetin could only be estimated between 5 and 10 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\6TTA\6TTA_metadata.json interval structures/6TTA/6tta_protein.pdb structures/6TTA/6tta_pocket.pdb structures/6TTA/6tta_ligand.sdf structures/6TTA/6tta_ligand.pdb structures/6TTA/6tta_ligand.cif structures/6TTA/6tta_complex.pdb structures/6TTA/6tta_complex.cif 6TTC classic NDM-1 Na Na Na myricetin "[""MYC""]" 1 IC50 IC50 = = 3.3 µM 3300.0 [] unit_conversion 5.481486060122112 success True biochemical_inhibition Purified NDM-1 biochemical inhibition assay. The IC50 determination used 50 µM ZnSO4 and 100 µM imipenem. 4 “The IC50 for myricetin was determined as 3.3 µM (Figure 5c).” auto_single_measurement only accepted activity measurement [1] 1 structures\6TTC\6TTC_metadata.json point structures/6TTC/6ttc_protein.pdb structures/6TTC/6ttc_pocket.pdb structures/6TTC/6ttc_ligand.sdf structures/6TTC/6ttc_ligand.pdb structures/6TTC/6ttc_ligand.cif structures/6TTC/6ttc_complex.pdb structures/6TTC/6ttc_complex.cif 6ULT extended BRD2 Na Na Na 4.2C; 4.2_3 "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L""]" 1 Kd Kd = = 22 ± 26 nM 22.0 [] unit_conversion 7.657577319177793 success True direct_binding SPR; geometric mean and SD of two to five measurements. 8 Fig. 5D reports BRD2-BD2–4.2C K_D = 22 ± 26 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\6ULT\6ULT_metadata.json point structures/6ULT/6ult_protein.pdb structures/6ULT/6ult_pocket.pdb structures/6ULT/6ult_ligand.pdb structures/6ULT/6ult_ligand.cif structures/6ULT/6ult_complex.pdb structures/6ULT/6ult_complex.cif 6UVD classic BCL-XL human C-terminally truncated, loop-deleted human BCL-XL (Delta27-82, DeltaC24) Na compound 2 "[""XOU""]" 1 IC50 IC50 = = 0.51 ± 0.07 µM 510.0 [] unit_conversion 6.292429823902063 success True direct_binding AlphaSCREEN (AS) solution competition assay using GST-BCL-XL. 3 Table 1 reports compound 2 AS IC50 for BCL-XL as 0.51 ± 0.07 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\6UVD\6UVD_metadata.json point structures/6UVD/6uvd_protein.pdb structures/6UVD/6uvd_pocket.pdb structures/6UVD/6uvd_ligand.sdf structures/6UVD/6uvd_ligand.pdb structures/6UVD/6uvd_ligand.cif structures/6UVD/6uvd_complex.pdb structures/6UVD/6uvd_complex.cif 6UVE classic BCL-XL human C-terminally truncated, loop-deleted human BCL-XL (Delta27-82, DeltaC24) Na compound 7 "[""QHV""]" 1 IC50 IC50 = = 0.24 ± 0.02 µM 240.0 [] unit_conversion 6.619788758288394 success True direct_binding AlphaSCREEN (AS) solution competition assay using GST-BCL-XL. 3 Table 1 reports compound 7 AS IC50 for BCL-XL as 0.24 ± 0.02 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\6UVE\6UVE_metadata.json point structures/6UVE/6uve_protein.pdb structures/6UVE/6uve_pocket.pdb structures/6UVE/6uve_ligand.sdf structures/6UVE/6uve_ligand.pdb structures/6UVE/6uve_ligand.cif structures/6UVE/6uve_complex.pdb structures/6UVE/6uve_complex.cif 6VBA classic human Uracil DNA Glycosylase (UDG) human Na Na Aurintricarboxylic acid (ATA) "[""QU4""]" 2 Kd Kd = = 679 ± 250 nM 679.0 [] unit_conversion 6.168130225719498 success True direct_binding Microscale thermophoresis of purified, fluorescently labelled full-length human UDG titrated with ATA tri-ammonium salt (Fig. 3A). 9 Fig. 3A prints “Kd = 679 ± 250 nM.” auto_metric_priority unique highest-priority metric family: Kd [2] 4 structures\6VBA\6VBA_metadata.json point structures/6VBA/6vba_protein.pdb structures/6VBA/6vba_pocket.pdb structures/6VBA/6vba_ligand.sdf structures/6VBA/6vba_ligand.pdb structures/6VBA/6vba_ligand.cif structures/6VBA/6vba_complex.pdb structures/6VBA/6vba_complex.cif 6VGL classic JAK2 human JAK2 KD/JH1, residues 840-1132, His8 N-terminal affinity tag Na ruxolitinib "[""RXT""]" 1 IC50 IC50 = = 0.40 ± 0.005 nM 0.4 [] unit_conversion 9.397940008672037 success True biochemical_inhibition Radiometric enzymatic JAK2 inhibition assay (Reaction Biology Corp.). 4 Table 1 lists ruxolitinib biochemical inhibition IC50 = 0.40 ± 0.005 nM; the PDB list assigns 6VGL to JAK2/ruxolitinib. auto_single_measurement only accepted activity measurement [1] 1 structures\6VGL\6VGL_metadata.json point structures/6VGL/6vgl_protein.pdb structures/6VGL/6vgl_pocket.pdb structures/6VGL/6vgl_ligand.sdf structures/6VGL/6vgl_ligand.pdb structures/6VGL/6vgl_ligand.cif structures/6VGL/6vgl_complex.pdb structures/6VGL/6vgl_complex.cif 6VN8 classic JAK2 human JAK2 KD/JH1, residues 840-1132, His8 N-terminal affinity tag Na baricitinib "[""3JW""]" 1 IC50 IC50 = = 0.29 ± 0.13 nM 0.29 [] unit_conversion 9.537602002101044 success True biochemical_inhibition Radiometric enzymatic JAK2 inhibition assay (Reaction Biology Corp.). 4 Table 1 lists baricitinib biochemical inhibition IC50 = 0.29 ± 0.13 nM; the PDB list assigns 6VN8 to JAK2/baricitinib. auto_single_measurement only accepted activity measurement [1] 1 structures\6VN8\6VN8_metadata.json point structures/6VN8/6vn8_protein.pdb structures/6VN8/6vn8_pocket.pdb structures/6VN8/6vn8_ligand.sdf structures/6VN8/6vn8_ligand.pdb structures/6VN8/6vn8_ligand.cif structures/6VN8/6vn8_complex.pdb structures/6VN8/6vn8_complex.cif 6VNE classic JAK2 human JAK2 KD/JH1, residues 840-1132, His8 N-terminal affinity tag Na Fedratinib "[""2TA""]" 1 IC50 IC50 = = 0.75 ± 0.39 nM 0.75 [] unit_conversion 9.1249387366083 success True biochemical_inhibition Radiometric enzymatic JAK2 inhibition assay (Reaction Biology Corp.). 4 Table 1 lists fedratinib biochemical inhibition IC50 = 0.75 ± 0.39 nM; the PDB list assigns 6VNE to JAK2/fedratinib. auto_single_measurement only accepted activity measurement [1] 1 structures\6VNE\6VNE_metadata.json point structures/6VNE/6vne_protein.pdb structures/6VNE/6vne_pocket.pdb structures/6VNE/6vne_ligand.sdf structures/6VNE/6vne_ligand.pdb structures/6VNE/6vne_ligand.cif structures/6VNE/6vne_complex.pdb structures/6VNE/6vne_complex.cif 6VVH extended AtDHDPS1 (dihydrodipicolinate synthase isoform 1) Arabidopsis thaliana AtDHDPS1 construct lacking the first 48 amino acids; purification fusion tag removed before crystallization Na L-lysine "[""LYS""]" 2 Kd Kd = = 5.7 ± 0.6 μM 5700.0 [] unit_conversion 5.2441251443275085 success True direct_binding Microscale thermophoresis lysine-binding assay fitted to a Hill coefficient model. 7 “Kd values were of 5.7 ± 0.6 and 36 ± 1.2 μM for AtDHDPS1 and AtDHDPS2, respectively.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\6VVH\6VVH_metadata.json point structures/6VVH/6vvh_ligand.sdf structures/6VVH/6vvh_ligand.cif structures/6VVH/6vvh_complex.cif 6VZL classic PPARgamma human PPARgamma LBD residues 203-477, isoform 1 numbering Na GW1929 "[""EDK""]" 1 Ki Ki = = 100 pM 0.1 [] unit_conversion 10.0 success True biochemical_inhibition TR-FRET fluorescent tracer ligand-displacement assay; Figure 1 reports the inhibitory binding constant for GW1929 binding to PPARγ LBD. 3 “GW1929 ... displays a 100 pM inhibitory binding constant (Ki) (Figure 1B).” auto_single_measurement only accepted activity measurement [1] 1 structures\6VZL\6VZL_metadata.json point structures/6VZL/6vzl_protein.pdb structures/6VZL/6vzl_pocket.pdb structures/6VZL/6vzl_ligand.sdf structures/6VZL/6vzl_ligand.pdb structures/6VZL/6vzl_ligand.cif structures/6VZL/6vzl_complex.pdb structures/6VZL/6vzl_complex.cif 6W11 extended Csa3a (Sso1445) Sulfolobus solfataricus Csa3a (Sso1445), expressed from pEXP14-6xHis-Sso1445; modeled with the native, nontagged protein sequence Na cyclic tetra-adenylate (cA4) "[""CHAIN:C""]" 2 Kd Kd = = 1.09 (0.10) µM 1090.0 [] unit_conversion 5.962573502059376 success True direct_binding ITC at 25 °C; 250 µM cA4 titrated into 25 µM Csa3a dimer. 9 Figure 2 reports Kd = 1.09 (0.10) µM for titration of 250 µM cA4 into 25 µM Csa3a dimer. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\6W11\6W11_metadata.json point structures/6W11/6w11_protein.pdb structures/6W11/6w11_pocket.pdb structures/6W11/6w11_ligand.pdb structures/6W11/6w11_ligand.cif structures/6W11/6w11_complex.pdb structures/6W11/6w11_complex.cif 6W2J classic carbamoyl phosphate synthetase 1 (CPS1) Na Na Na H3B-374 (compound 12) "[""374""]" 1 IC50 IC50 = = 0.36 μM 360.0 [] unit_conversion 6.443697499232712 success True biochemical_inhibition ADPGlo biochemical assay measuring ADP formation from CPS1 in the presence of inhibitor; reported value is an average of at least two experimental replicates (N = 2). 2 Table 1 lists compound 12 with ADPGlo IC50 = 0.36 μM. Figure 2 identifies H3B-374 (12) bound to CPS1 as PDB code 6W2J. auto_single_measurement only accepted activity measurement [1] 1 structures\6W2J\6W2J_metadata.json point structures/6W2J/6w2j_protein.pdb structures/6W2J/6w2j_pocket.pdb structures/6W2J/6w2j_ligand.sdf structures/6W2J/6w2j_ligand.pdb structures/6W2J/6w2j_ligand.cif structures/6W2J/6w2j_complex.pdb structures/6W2J/6w2j_complex.cif 6W30 classic Protein Tyrosine Phosphatase 1B Na Na Na amorphadiene "[""SJA""]" 1 IC50 IC50 = = 53 ± 8 μM 53000.0 [] unit_conversion 4.275724130399211 success True biochemical_inhibition Purified PTP1B-catalyzed p-nitrophenyl phosphate hydrolysis; 10% DMSO. 5 “The IC50s for amorphadiene and α-bisabolene were 53 ± 8 μM and 13 ± 2 μM, respectively, in 10% DMSO.” Figure 3 identifies the PTP1B–amorphadiene crystal structure as PDB 6W30. auto_single_measurement only accepted activity measurement [1] 1 structures\6W30\6W30_metadata.json point structures/6W30/6w30_protein.pdb structures/6W30/6w30_pocket.pdb structures/6W30/6w30_ligand.sdf structures/6W30/6w30_ligand.pdb structures/6W30/6w30_ligand.cif structures/6W30/6w30_complex.pdb structures/6W30/6w30_complex.cif 6W44 classic HAO1 human Residues 1-168; N-terminal 6xHis tag with TEV cleavage site, expressed in Escherichia coli Na Compound 4 "[""SLJ""]" 1 IC50 IC50 = = 510 nM 510.0 [] unit_conversion 6.292429823902063 success True biochemical_inhibition Fluorescence-based HAO1 activity assay detecting hydrogen peroxide via coupled HRP reaction; purified recombinant human HAO1. 5 “Compound 4 less potent (HAO1 IC50 = 510 nM)”. The assay is described as a fluorescence-based HAO1 activity assay. auto_single_measurement only accepted activity measurement [1] 1 structures\6W44\6W44_metadata.json point structures/6W44/6w44_protein.pdb structures/6W44/6w44_pocket.pdb structures/6W44/6w44_ligand.sdf structures/6W44/6w44_ligand.pdb structures/6W44/6w44_ligand.cif structures/6W44/6w44_complex.pdb structures/6W44/6w44_complex.cif 6W45 classic HAO1 human Residues 1-168; N-terminal 6xHis tag with TEV cleavage site, expressed in Escherichia coli Na Compound 3 "[""SLG""]" 1 IC50 IC50 = = 110 nM 110.0 [] unit_conversion 6.958607314841775 success True biochemical_inhibition Fluorescence-based HAO1 activity assay detecting hydrogen peroxide via coupled HRP reaction; purified recombinant human HAO1. 5 “Biaryl acid Compound 3 from Series 1 gave an IC50 = 110 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\6W45\6W45_metadata.json point structures/6W45/6w45_protein.pdb structures/6W45/6w45_pocket.pdb structures/6W45/6w45_ligand.sdf structures/6W45/6w45_ligand.pdb structures/6W45/6w45_ligand.cif structures/6W45/6w45_complex.pdb structures/6W45/6w45_complex.cif 6W4C classic HAO1 human Residues 1-168; N-terminal 6xHis tag with TEV cleavage site, expressed in Escherichia coli Na Compound 5 "[""SL7""]" 2 Kd Kd = = 160 nM 160.0 [] unit_conversion 6.795880017344075 success True direct_binding SPR (Biacore), 1:1 binding of FMN-loaded HAO1. 4 “Target engagement was confirmed for both series using SPR (Biacore) with Compound 5 determined to have a KD of 160 nM with 1:1 binding of FMN (Flavin mononucleotide)-loaded HAO1”. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\6W4C\6W4C_metadata.json point structures/6W4C/6w4c_protein.pdb structures/6W4C/6w4c_pocket.pdb structures/6W4C/6w4c_ligand.sdf structures/6W4C/6w4c_ligand.pdb structures/6W4C/6w4c_ligand.cif structures/6W4C/6w4c_complex.pdb structures/6W4C/6w4c_complex.cif 6WE2 classic Human PARP14 (ARTD8) Homo sapiens Catalytic fragment, residues 1611-1801, with an N-terminal hexahistidine tag and TEV cleavage site; His6 tag cleaved for crystallization Na RBN012759 "[""XBA""]" 3 Kd Kd = = 0.002 µM 2.0 [] unit_conversion 8.698970004336019 success True direct_binding SPR using immobilized human PARP14 catalytic domain. 4 “The PARP14 binding affinity of RBN012759 (Kd = 0.002 µM) was determined by surface plasmon resonance (SPR) using the immobilized catalytic domain of PARP14.” auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\6WE2\6WE2_metadata.json point structures/6WE2/6we2_protein.pdb structures/6WE2/6we2_pocket.pdb structures/6WE2/6we2_ligand.sdf structures/6WE2/6we2_ligand.pdb structures/6WE2/6we2_ligand.cif structures/6WE2/6we2_complex.pdb structures/6WE2/6we2_complex.cif 6WE3 classic Human PARP14 (ARTD8) Homo sapiens Catalytic fragment, residues 1611-1801, with an N-terminal hexahistidine tag and TEV cleavage site; His6 tag cleaved for crystallization Na Compound 3 "[""TZ7""]" 1 IC50 IC50 = = 0.3 µM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition PARP14 TR-FRET active-site probe displacement assay. 4 “The trans-cyclohexanol-containing compound 3 was prepared … and it provided a 3-fold improvement in PARP14 potency (IC50 = 0.3 µM) versus 2.” auto_single_measurement only accepted activity measurement [1] 1 structures\6WE3\6WE3_metadata.json point structures/6WE3/6we3_protein.pdb structures/6WE3/6we3_pocket.pdb structures/6WE3/6we3_ligand.sdf structures/6WE3/6we3_ligand.pdb structures/6WE3/6we3_ligand.cif structures/6WE3/6we3_complex.pdb structures/6WE3/6we3_complex.cif 6WH5 extended pduO-type ATP:cobalamin adenosyltransferase Mycobacterium tuberculosis Na Na cob(II)alamin "[""B12""]" 1 Kd Kd <= <= 0.2 µM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Cob(II)alamin binding to Mtb ATR in the presence of PPPi. 3 “In the presence of PPPi, Mtb ATR binds cob(II)alamin stoichiometrically (KD ≤ 0.2 µM).” auto_single_measurement only accepted activity measurement [1] 1 structures\6WH5\6WH5_metadata.json point structures/6WH5/6wh5_protein.pdb structures/6WH5/6wh5_pocket.pdb structures/6WH5/6wh5_ligand.pdb structures/6WH5/6wh5_ligand.cif structures/6WH5/6wh5_complex.pdb structures/6WH5/6wh5_complex.cif 6WHO extended Human histone deacetylase 2 (HDAC2) Homo sapiens C-terminally truncated HDAC2 Na des1.1.0 "[""POLYMER_ENTITY:2""]" 1 IC50 IC50 = = 289 nM 289.0 [] unit_conversion 6.539102157243452 success True biochemical_inhibition HDAC2 fluorogenic enzymatic inhibition assay; Figure 2 caption identifies the des1.1.0 HDAC2 crystal structure as PDB 6WHO. 4 “des1.1.0 inhibits HDAC2 with an IC50 of 289 nM”; the caption maps its crystal structure to PDB ID 6WHO. auto_single_measurement only accepted activity measurement [1] 1 structures\6WHO\6WHO_metadata.json point structures/6WHO/6who_protein.pdb structures/6WHO/6who_pocket.pdb structures/6WHO/6who_ligand.pdb structures/6WHO/6who_ligand.cif structures/6WHO/6who_complex.pdb structures/6WHO/6who_complex.cif 6WKA classic human carbonic anhydrase II human Na Na compound 3b "[""U4V""]" 1 Ki Ki = = 32.9 nM 32.9 [] unit_conversion 7.482804102050026 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay of hCA II. 5 Table 2 reports Ki = 32.9 nM for compound 3b against hCA II. Figure 5 (PDF page 7) identifies PDB 6WKA as hCA II bound to inhibitor 3b. auto_single_measurement only accepted activity measurement [1] 1 structures\6WKA\6WKA_metadata.json point structures/6WKA/6wka_protein.pdb structures/6WKA/6wka_pocket.pdb structures/6WKA/6wka_ligand.sdf structures/6WKA/6wka_ligand.pdb structures/6WKA/6wka_ligand.cif structures/6WKA/6wka_complex.pdb structures/6WKA/6wka_complex.cif 6WMQ extended Human REV-ERBbeta Homo sapiens REV-ERBbeta ligand-binding domain (LBD) Na heme "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 2.4 (95% CI: 1.0 to 5.7) µM 2400.0 [] unit_conversion 5.619788758288394 success True direct_binding ITC, heme-bound LBD; ternary heme–LBD–ID1-peptide binding. 2 Table 1 reports Kd = 2.4 µM (95% CI: 1.0 to 5.7) for NCoR ID1 peptide binding to heme LBD. Figure 2 maps the heme/ID1 structure to PDB 6WMQ. auto_single_measurement only accepted activity measurement [1] 1 structures\6WMQ\6WMQ_metadata.json point structures/6WMQ/6wmq_protein.pdb structures/6WMQ/6wmq_pocket.pdb structures/6WMQ/6wmq_ligand.pdb structures/6WMQ/6wmq_ligand.cif structures/6WMQ/6wmq_complex.pdb structures/6WMQ/6wmq_complex.cif 6WMS extended Human REV-ERBbeta Homo sapiens REV-ERBbeta ligand-binding domain (LBD) Na heme "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 2.2 (95% CI: 1.6 to 3.1) µM 2200.0 [] unit_conversion 5.657577319177793 success True direct_binding ITC, heme-bound LBD; ternary heme–LBD–ID2-peptide binding. 2 Table 1 reports Kd = 2.2 µM (95% CI: 1.6 to 3.1) for NCoR ID2 peptide binding to heme LBD. Figure 2 maps the heme/ID2 structure to PDB 6WMS. auto_single_measurement only accepted activity measurement [1] 1 structures\6WMS\6WMS_metadata.json point structures/6WMS/6wms_protein.pdb structures/6WMS/6wms_pocket.pdb structures/6WMS/6wms_ligand.pdb structures/6WMS/6wms_ligand.cif structures/6WMS/6wms_complex.pdb structures/6WMS/6wms_complex.cif 6WNK classic Mtb20SOG proteasome Mycobacterium tuberculosis Na Na TDI5575 (macrocycle 6) "[""U5Y""]" 3 Ki Ki = = 12.1 nM 12.1 [] unit_conversion 7.91721462968355 success True biochemical_inhibition Time-dependent inhibition kinetics, following peptide LLVY hydrolysis by Mtb20S. 5 The inhibition-kinetics text reports that macrocycle 6 yielded “a Ki of 12.1 nM”. auto_metric_priority unique highest-priority metric family: Ki [3] 3 structures\6WNK\6WNK_metadata.json point structures/6WNK/6wnk_protein.pdb structures/6WNK/6wnk_pocket.pdb structures/6WNK/6wnk_ligand.sdf structures/6WNK/6wnk_ligand.pdb structures/6WNK/6wnk_ligand.cif structures/6WNK/6wnk_complex.pdb structures/6WNK/6wnk_complex.cif 6WR1 classic steroidogenic cytochrome P450 17A1 (CYP17A1) Human pCWOri+ construct with a 19-residue N-terminal truncation, modification of the first five residues, a C-terminal 4xHis tag, and the N52Y substitution N52Y abiraterone "[""AER""]" 1 IC50 IC50 = = 51 ± 2 nM 51.0 [] unit_conversion 7.292429823902063 success True biochemical_inhibition Inhibition of progesterone hydroxylation by CYP17A1 N52Y; the paper states the IC50 for abiraterone was 51 ± 2 nM. 6 “there was very little difference in the IC50 value between WT enzyme (69 ± 5 nM) and the N52Y mutant (51 ± 2 nM).” The preceding sentence specifies abiraterone inhibition of progesterone hydroxylation. auto_single_measurement only accepted activity measurement [1] 1 structures\6WR1\6WR1_metadata.json point structures/6WR1/6wr1_protein.pdb structures/6WR1/6wr1_pocket.pdb structures/6WR1/6wr1_ligand.sdf structures/6WR1/6wr1_ligand.pdb structures/6WR1/6wr1_ligand.cif structures/6WR1/6wr1_complex.pdb structures/6WR1/6wr1_complex.cif 6WTA classic MSMEG_2027 Mycobacterium smegmatis Full-length recombinant MSMEG_2027 Na F420 "[""UBM""]" 1 Kd Kd = = 486 (68.3% CI 378–611) nM 486.0 [] unit_conversion 6.313363730737707 success True direct_binding Isothermal titration calorimetry of F420 into MSMEG_2027; one-site binding model. 5 ITC data were fit with a one-site binding model, giving an apparent Kd of 486 nM (68.3% CI 378–611 nM). auto_single_measurement only accepted activity measurement [1] 1 structures\6WTA\6WTA_metadata.json point structures/6WTA/6wta_protein.pdb structures/6WTA/6wta_pocket.pdb structures/6WTA/6wta_ligand.sdf structures/6WTA/6wta_ligand.pdb structures/6WTA/6wta_ligand.cif structures/6WTA/6wta_complex.pdb structures/6WTA/6wta_complex.cif 6WU8 classic human SHP2 human SHP2 residues 1-530 Na IACS-13909 "[""U9Y""]" 1 Kd Kd ~ ~ 32 nM 32.0 [] unit_conversion 7.494850021680094 success True direct_binding Isothermal titration calorimetry measurement of IACS-13909 binding to SHP2. 6 “The Kd of IACS-13909 binding to SHP2 is ~ 32 nM, as determined by isothermal titration calorimetry analysis.” PDB=6WU8 is explicitly assigned to the IACS-13909:SHP2 structure on the same page. auto_single_measurement only accepted activity measurement [1] 1 structures\6WU8\6WU8_metadata.json point structures/6WU8/6wu8_protein.pdb structures/6WU8/6wu8_pocket.pdb structures/6WU8/6wu8_ligand.sdf structures/6WU8/6wu8_ligand.pdb structures/6WU8/6wu8_ligand.cif structures/6WU8/6wu8_complex.pdb structures/6WU8/6wu8_complex.cif 6WWC extended Vaccine-elicited mouse FP-targeting neutralizing antibody vFP16.02 mouse Fab fragment S48K in the light chain HIV fusion peptide, residues 512-519; FP8v1 (AVGIGAVF) "[""CHAIN:C"", ""CHAIN:F""]" 1 Kd Kd < < 0.001 nM 0.001 [] unit_conversion 12.0 success True direct_binding Surface plasmon resonance binding against soluble FP8v1 peptide. 5 The text states binding affinities were assessed against soluble FP8v1 peptide (Fig. 4C); the VL-S48K panel prints K_D < 0.001 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\6WWC\6WWC_metadata.json point structures/6WWC/6wwc_protein.pdb structures/6WWC/6wwc_pocket.pdb structures/6WWC/6wwc_ligand.pdb structures/6WWC/6wwc_ligand.cif structures/6WWC/6wwc_complex.pdb structures/6WWC/6wwc_complex.cif 6WX2 extended Vaccine-elicited mouse FP-targeting neutralizing antibody vFP16.02 mouse Fab fragment F60P in the light chain HIV fusion peptide, residues 512-519; FP8v1 (AVGIGAVF) "[""POLYMER_ENTITY:3""]" 1 Kd Kd = = 0.001 nM 0.001 [] unit_conversion 12.0 success True direct_binding Surface plasmon resonance binding against soluble FP8v1 peptide. 5 The text states binding affinities were assessed against soluble FP8v1 peptide (Fig. 4C); the VL-F60P panel prints K_D = 0.001 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\6WX2\6WX2_metadata.json point structures/6WX2/6wx2_protein.pdb structures/6WX2/6wx2_pocket.pdb structures/6WX2/6wx2_ligand.pdb structures/6WX2/6wx2_ligand.cif structures/6WX2/6wx2_complex.pdb structures/6WX2/6wx2_complex.cif 6WXQ extended CRISPR-associated transcription factor Csa3 (Csa3Sso) Saccharolobus solfataricus Full-length N-terminally His6-tagged Csa3Sso Na cA4 (cyclic tetra-adenylate) "[""CHAIN:E""]" 1 Kd Kd = = 5.8 ± 0.03 μM 5800.0 [] unit_conversion 5.236572006437063 success True direct_binding Microscale thermophoresis binding-affinity analysis of purified recombinant N-terminally His6-tagged Csa3Sso against cA4. 2 Only cA4 exhibited specific low-micromolar binding to His6-Csa3Sso, with an apparent dissociation constant (KD) of 5.8 ± 0.03 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6WXQ\6WXQ_metadata.json point structures/6WXQ/6wxq_protein.pdb structures/6WXQ/6wxq_pocket.pdb structures/6WXQ/6wxq_ligand.pdb structures/6WXQ/6wxq_ligand.cif structures/6WXQ/6wxq_complex.pdb structures/6WXQ/6wxq_complex.cif 6X10 extended acetyltransferase Eis Mycobacterium tuberculosis Na Na haloperidol (1) "[""GMJ""]" 2 Ki Ki = = 0.39 ± 0.02 μM 390.0 [] unit_conversion 6.4089353929735005 success True biochemical_inhibition Eis Michaelis–Menten/Lineweaver–Burk inhibition kinetics; competitive with kanamycin. 9 The analysis yielded Ki values of 0.39 ± 0.02 μM for inhibitor 1; the inhibitors occupied the aminoglycoside binding site. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\6X10\6X10_metadata.json point structures/6X10/6x10_protein.pdb structures/6X10/6x10_pocket.pdb structures/6X10/6x10_ligand.pdb structures/6X10/6x10_ligand.cif structures/6X10/6x10_complex.pdb structures/6X10/6x10_complex.cif 6X5W extended MpIBP_RIII1-4 Marinomonas primoryensis MpPBD truncated by 12 amino acids, ending at N507 instead of D519 Na AGYTD "[""CHAIN:B""]" 1 Kd Kd = = 67.1 ± 3.0 nM 67.1 [] unit_conversion 7.1732774798310075 success True direct_binding Isothermal titration calorimetry of unlabeled AGYTD binding MpPBD. 8 ITC of AGYTD with MpPBD gave a calculated Kd of 67.1 ± 3.0 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\6X5W\6X5W_metadata.json point structures/6X5W/6x5w_protein.pdb structures/6X5W/6x5w_pocket.pdb structures/6X5W/6x5w_ligand.pdb structures/6X5W/6x5w_ligand.cif structures/6X5W/6x5w_complex.pdb structures/6X5W/6x5w_complex.cif 6X6G extended acetyltransferase Eis Mycobacterium tuberculosis Na Na droperidol (DPD) "[""USS""]" 1 IC50 IC50 = = 12.2 ± 0.9 μM 12200.0 [] unit_conversion 4.913640169325252 success True biochemical_inhibition Eis-catalyzed aminoglycoside acetylation inhibition assay. 2 DPD exhibited weak Eis inhibition with an IC50 = 12.2 ± 0.9 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\6X6G\6X6G_metadata.json point structures/6X6G/6x6g_ligand.sdf structures/6X6G/6x6g_ligand.cif structures/6X6G/6x6g_complex.cif 6X6I extended acetyltransferase Eis Mycobacterium tuberculosis Na Na inhibitor SGT543 "[""USG""]" 2 Ki Ki = = 0.91 ± 0.22 μM 910.0 [] unit_conversion 6.040958607678906 success True biochemical_inhibition Eis Michaelis–Menten/Lineweaver–Burk inhibition kinetics; competitive with kanamycin. 9 The analysis yielded Ki values of 0.91 ± 0.22 μM for inhibitor 10; Fig. 3 identifies compound 10 as SGT543 in PDB 6X6I. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\6X6I\6X6I_metadata.json point structures/6X6I/6x6i_ligand.cif structures/6X6I/6x6i_complex.cif 6X6Y extended acetyltransferase Eis Mycobacterium tuberculosis Na Na inhibitor SGT1264 "[""USY""]" 1 IC50 IC50 = = 1.1 ± 0.1 μM 1100.0 [] unit_conversion 5.958607314841775 success True biochemical_inhibition Dose-response Eis-catalyzed aminoglycoside acetylation assay. 4 Table 1 reports compound 35 IC50 = 1.1 ± 0.1 μM against Eis; Fig. 4 identifies the Eis-35 (SGT1264) complex as PDB ID 6X6Y. auto_single_measurement only accepted activity measurement [1] 1 structures\6X6Y\6X6Y_metadata.json point structures/6X6Y/6x6y_ligand.sdf structures/6X6Y/6x6y_ligand.cif structures/6X6Y/6x6y_complex.cif 6X7A extended acetyltransferase Eis Mycobacterium tuberculosis Na Na inhibitor SGT572 "[""UTD""]" 1 IC50 IC50 = = 0.56 ± 0.05 μM 560.0 [] unit_conversion 6.251811972993799 success True biochemical_inhibition Dose-response Eis-catalyzed aminoglycoside acetylation assay. 4 Table 1 reports compound 30 IC50 = 0.56 ± 0.05 μM against Eis; Fig. 3 identifies the Eis-30 (SGT572) complex as PDB ID 6X7A. auto_single_measurement only accepted activity measurement [1] 1 structures\6X7A\6X7A_metadata.json point structures/6X7A/6x7a_ligand.cif structures/6X7A/6x7a_complex.cif 6X7Z classic MpPA14 Marinomonas primoryensis Na Na myo-inositol (inositol) "[""INS""]" 1 Kd Kd = = 2.7 mM 2700000.0 [] unit_conversion 2.568636235841013 success True direct_binding Dextran-resin comparative competition binding assay; reported as Kdapp. 5 Table 1 reports inositol Kdapp of 2.7 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6X7Z\6X7Z_metadata.json point structures/6X7Z/6x7z_protein.pdb structures/6X7Z/6x7z_pocket.pdb structures/6X7Z/6x7z_ligand.sdf structures/6X7Z/6x7z_ligand.pdb structures/6X7Z/6x7z_ligand.cif structures/6X7Z/6x7z_complex.pdb structures/6X7Z/6x7z_complex.cif 6X81 classic TNFalpha human TNFalpha residues 77-233 Na isoquinoline compound 2 "[""UTJ""]" 1 Kd Kd = = 2.7 μM 2700.0 [] unit_conversion 5.568636235841012 success True direct_binding Surface plasmon resonance (SPR) kinetic measurement. 3 Compound 2 showed an equilibrium dissociation constant (KD) of 2.70 μM for the TNFα trimer by SPR. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\6X81\6X81_metadata.json point structures/6X81/6x81_protein.pdb structures/6X81/6x81_pocket.pdb structures/6X81/6x81_ligand.sdf structures/6X81/6x81_ligand.pdb structures/6X81/6x81_ligand.cif structures/6X81/6x81_complex.pdb structures/6X81/6x81_complex.cif 6X83 classic TNFalpha human TNFalpha residues 77-233 Na fragment compound 6 "[""UTS""]" 1 Kd Kd = = 300,000 nM 300000.0 [] unit_conversion 3.5228787452803374 success True direct_binding SPR kinetic data, Table 1. 7 Table 1 reports SPR KD = 300,000 nM for compound 6. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\6X83\6X83_metadata.json point structures/6X83/6x83_protein.pdb structures/6X83/6x83_pocket.pdb structures/6X83/6x83_ligand.sdf structures/6X83/6x83_ligand.pdb structures/6X83/6x83_ligand.cif structures/6X83/6x83_complex.pdb structures/6X83/6x83_complex.cif 6X85 classic TNFalpha human TNFalpha residues 77-233 Na indolinone compound 9 "[""UTV""]" 1 Kd Kd = = 19,000 nM 19000.0 [] unit_conversion 4.721246399047171 success True direct_binding SPR kinetic data, Table 1. 7 Table 1 reports SPR KD = 19,000 nM for compound 9. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\6X85\6X85_metadata.json point structures/6X85/6x85_protein.pdb structures/6X85/6x85_pocket.pdb structures/6X85/6x85_ligand.sdf structures/6X85/6x85_ligand.pdb structures/6X85/6x85_ligand.cif structures/6X85/6x85_complex.pdb structures/6X85/6x85_complex.cif 6X86 classic TNFalpha human TNFalpha residues 77-233 Na indolinone compound 11 "[""UTY""]" 1 Kd Kd = = 7.3 nM 7.3 [] unit_conversion 8.136677139879545 success True direct_binding SPR kinetic data, Table 1. 7 Table 1 reports SPR KD = 7.3 nM for compound 11. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\6X86\6X86_metadata.json point structures/6X86/6x86_protein.pdb structures/6X86/6x86_pocket.pdb structures/6X86/6x86_ligand.sdf structures/6X86/6x86_ligand.pdb structures/6X86/6x86_ligand.cif structures/6X86/6x86_complex.pdb structures/6X86/6x86_complex.cif 6X8D classic MpPA14 Marinomonas primoryensis Na Na L-arabinose "[""ARA""]" 1 Kd Kd = = 2.2 mM 2200000.0 [] unit_conversion 2.6575773191777934 success True direct_binding Dextran-resin comparative competition binding assay; reported as Kdapp. 5 Table 1 reports L-arabinose Kdapp of 2.2 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6X8D\6X8D_metadata.json point structures/6X8D/6x8d_protein.pdb structures/6X8D/6x8d_pocket.pdb structures/6X8D/6x8d_ligand.sdf structures/6X8D/6x8d_ligand.pdb structures/6X8D/6x8d_ligand.cif structures/6X8D/6x8d_complex.pdb structures/6X8D/6x8d_complex.cif 6X8Y classic MpPA14 Marinomonas primoryensis Na Na ribose "[""RIP""]" 1 Kd Kd = = 6.8 mM 6800000.0 [] unit_conversion 2.1674910872937634 success True direct_binding Dextran-resin comparative competition binding assay; reported as Kdapp. 5 Table 1 reports ribose Kdapp of 6.8 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6X8Y\6X8Y_metadata.json point structures/6X8Y/6x8y_protein.pdb structures/6X8Y/6x8y_pocket.pdb structures/6X8Y/6x8y_ligand.sdf structures/6X8Y/6x8y_ligand.pdb structures/6X8Y/6x8y_ligand.cif structures/6X8Y/6x8y_complex.pdb structures/6X8Y/6x8y_complex.cif 6X95 classic MpPA14 Marinomonas primoryensis Na Na 2-deoxy-D-glucose "[""Z61""]" 1 Kd Kd = = 1.4 mM 1400000.0 [] unit_conversion 2.853871964321762 success True direct_binding Dextran-resin comparative competition binding assay; reported as Kdapp. 5 Table 1 reports 2-deoxy-glucose Kdapp of 1.4 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6X95\6X95_metadata.json point structures/6X95/6x95_protein.pdb structures/6X95/6x95_pocket.pdb structures/6X95/6x95_ligand.sdf structures/6X95/6x95_ligand.pdb structures/6X95/6x95_ligand.cif structures/6X95/6x95_complex.pdb structures/6X95/6x95_complex.cif 6X9M classic MpPA14 Marinomonas primoryensis Na Na 3-O-methyl-glucose "[""3MG""]" 1 Kd Kd = = 5.7 mM 5700000.0 [] unit_conversion 2.2441251443275085 success True direct_binding Dextran-resin comparative competition binding assay; reported as Kdapp. 5 Table 1 reports 3-O-methyl-glucose Kdapp of 5.7 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6X9M\6X9M_metadata.json point structures/6X9M/6x9m_protein.pdb structures/6X9M/6x9m_pocket.pdb structures/6X9M/6x9m_ligand.sdf structures/6X9M/6x9m_ligand.pdb structures/6X9M/6x9m_ligand.cif structures/6X9M/6x9m_complex.pdb structures/6X9M/6x9m_complex.cif 6X9P classic MpPA14 Marinomonas primoryensis Na Na 2-deoxy-D-ribose "[""UZJ""]" 1 Kd Kd = = 18 mM 18000000.0 [] unit_conversion 1.7447274948966935 success True direct_binding Dextran-resin comparative competition binding assay; reported as Kdapp. 5 Table 1 reports 2-deoxy-ribose Kdapp of 18 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6X9P\6X9P_metadata.json point structures/6X9P/6x9p_protein.pdb structures/6X9P/6x9p_pocket.pdb structures/6X9P/6x9p_ligand.sdf structures/6X9P/6x9p_ligand.pdb structures/6X9P/6x9p_ligand.cif structures/6X9P/6x9p_complex.pdb structures/6X9P/6x9p_complex.cif 6XA6 extended Human Scribble human Human Scribble PDZ3 domain, residues 1002-1094 Na Human Vangl2 C-terminal 8-mer PBM peptide RLQSETSV "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 40.16 ± 3.92 μM 40160.0 [] unit_conversion 4.3962062958630375 success True direct_binding Isothermal titration calorimetry; purified protein and Vangl2 peptide; pH 7.5, 25°C; 1:1 binding model. 6 Table 1 reports Scribble PDZ3 WT binding to Vangl2: K_D 40.16 ± 3.92 μM. The ITC method identifies the human Vangl2 C-terminal 8-mer RLQSETSV. auto_single_measurement only accepted activity measurement [1] 1 structures\6XA6\6XA6_metadata.json point structures/6XA6/6xa6_protein.pdb structures/6XA6/6xa6_pocket.pdb structures/6XA6/6xa6_ligand.pdb structures/6XA6/6xa6_ligand.cif structures/6XA6/6xa6_complex.pdb structures/6XA6/6xa6_complex.cif 6XA7 extended Human Scribble human Human Scribble PDZ2 domain, residues 860-950 Na Human Vangl2 C-terminal 8-mer PBM peptide RLQSETSV "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 45.13 ± 4.92 μM 45130.0 [] unit_conversion 4.345534666479854 success True direct_binding Isothermal titration calorimetry; purified protein and Vangl2 peptide; pH 7.5, 25°C; 1:1 binding model. 6 Table 1 reports Scribble PDZ2 WT binding to Vangl2: K_D 45.13 ± 4.92 μM. The ITC method identifies the human Vangl2 C-terminal 8-mer RLQSETSV. auto_single_measurement only accepted activity measurement [1] 1 structures\6XA7\6XA7_metadata.json point structures/6XA7/6xa7_protein.pdb structures/6XA7/6xa7_pocket.pdb structures/6XA7/6xa7_ligand.pdb structures/6XA7/6xa7_ligand.cif structures/6XA7/6xa7_complex.pdb structures/6XA7/6xa7_complex.cif 6XAC classic MpPA14 Marinomonas primoryensis Na Na galactose "[""GAL""]" 1 Kd Kd = = 4.1 mM 4099999.9999999995 [] unit_conversion 2.3872161432802645 success True direct_binding Dextran-resin comparative competition binding assay; reported as Kdapp. 5 Table 1 reports galactose Kdapp of 4.1 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6XAC\6XAC_metadata.json point structures/6XAC/6xac_protein.pdb structures/6XAC/6xac_pocket.pdb structures/6XAC/6xac_ligand.sdf structures/6XAC/6xac_ligand.pdb structures/6XAC/6xac_ligand.cif structures/6XAC/6xac_complex.pdb structures/6XAC/6xac_complex.cif 6XAQ classic MpPA14 Marinomonas primoryensis Na Na alpha-methyl-glucose "[""GYP""]" 1 Kd Kd = = 2.1 mM 2100000.0 [] unit_conversion 2.6777807052660805 success True direct_binding Dextran-resin comparative competition binding assay; reported as Kdapp. 5 Table 1 reports methyl-α-glucose Kdapp of 2.1 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\6XAQ\6XAQ_metadata.json point structures/6XAQ/6xaq_protein.pdb structures/6XAQ/6xaq_pocket.pdb structures/6XAQ/6xaq_ligand.sdf structures/6XAQ/6xaq_ligand.pdb structures/6XAQ/6xaq_ligand.cif structures/6XAQ/6xaq_complex.pdb structures/6XAQ/6xaq_complex.cif 6XB9 classic Azotobacter vinelandii 3-mercaptopropionic acid dioxygenase Azotobacter vinelandii Na Na 3-hydroxypropionic acid (3HPA) "[""3OH""]" 1 Ki Ki = = 280 ± 26 µM 280000.0 [] unit_conversion 3.5528419686577806 success True biochemical_inhibition Steady-state Av3MDO-catalyzed 3MPA reactions; 3HPA behaved as a classic competitive inhibitor. 5 “A Lineweaver–Burk plot of the activity data revealed an inhibition constant (Ki) of 280 ± 26 μM … consistent with the behavior of a classic competitive inhibitor.” auto_single_measurement only accepted activity measurement [1] 1 structures\6XB9\6XB9_metadata.json point structures/6XB9/6xb9_protein.pdb structures/6XB9/6xb9_pocket.pdb structures/6XB9/6xb9_ligand.sdf structures/6XB9/6xb9_ligand.pdb structures/6XB9/6xb9_ligand.cif structures/6XB9/6xb9_complex.pdb structures/6XB9/6xb9_complex.cif 6XBE extended New Delhi metallo-beta-lactamase 1 (NDM-1) Na Na Na NDM1i-1F "[""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I""]" 1 IC50 IC50 = = 2.6 ± 0.2 μM 2600.0 [] unit_conversion 5.585026652029182 success True biochemical_inhibition Purified NDM-1 nitrocefin hydrolysis inhibition assay; IC50 fitted using a modified Hill equation. 4 Fig. 2F prints IC50 = 2.6 ± 0.2 μM for NDM1i-1F. The Fig. 2 caption identifies experimentally measured NDM-1 activity in the presence of peptide; page 8 describes the purified-enzyme nitrocefin assay. auto_single_measurement only accepted activity measurement [1] 1 structures\6XBE\6XBE_metadata.json point structures/6XBE/6xbe_protein.pdb structures/6XBE/6xbe_pocket.pdb structures/6XBE/6xbe_ligand.pdb structures/6XBE/6xbe_ligand.cif structures/6XBE/6xbe_complex.pdb structures/6XBE/6xbe_complex.cif 6XBF extended New Delhi metallo-beta-lactamase 1 (NDM-1) Na Na Na NDM1i-1G "[""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I""]" 1 IC50 IC50 = = 1.2 ± 0.1 μM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition Purified NDM-1 nitrocefin hydrolysis inhibition assay; IC50 fitted using a modified Hill equation. 4 Fig. 2G prints IC50 = 1.2 ± 0.1 μM for NDM1i-1G. The Fig. 2 caption identifies experimentally measured NDM-1 activity in the presence of peptide; page 8 describes the purified-enzyme nitrocefin assay. auto_single_measurement only accepted activity measurement [1] 1 structures\6XBF\6XBF_metadata.json point structures/6XBF/6xbf_protein.pdb structures/6XBF/6xbf_pocket.pdb structures/6XBF/6xbf_ligand.pdb structures/6XBF/6xbf_ligand.cif structures/6XBF/6xbf_complex.pdb structures/6XBF/6xbf_complex.cif 6XCI extended New Delhi metallo-beta-lactamase 1 (NDM-1) Na Na Na NDM1i-3D "[""CHAIN:H""]" 1 IC50 IC50 = = 3.1 ± 0.3 μM 3100.0 [] unit_conversion 5.508638306165727 success True biochemical_inhibition Purified NDM-1 nitrocefin hydrolysis inhibition assay; IC50 fitted using a modified Hill equation. 6 The main text states that NDM1i-3D had an IC50 of 3.1 ± 0.3 μM. Page 8 maps NDM1i-3D to PDB 6XCI and describes the purified-enzyme nitrocefin assay. auto_single_measurement only accepted activity measurement [1] 1 structures\6XCI\6XCI_metadata.json point structures/6XCI/6xci_protein.pdb structures/6XCI/6xci_pocket.pdb structures/6XCI/6xci_ligand.pdb structures/6XCI/6xci_ligand.cif structures/6XCI/6xci_complex.pdb structures/6XCI/6xci_complex.cif 6XF3 classic STING human Na WT (wild-type) E7766 "[""V5V""]" 1 Kd Kd = = 0.04 ± 0.01 μM 40.0 [] unit_conversion 7.3979400086720375 success True direct_binding Isothermal titration calorimetry (ITC), n=4, mean ± SD. 3 Table 1 reports E7766 Kd (WT) = 0.04 ± 0.01 μM; the text states Kd was measured by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\6XF3\6XF3_metadata.json point structures/6XF3/6xf3_protein.pdb structures/6XF3/6xf3_pocket.pdb structures/6XF3/6xf3_ligand.sdf structures/6XF3/6xf3_ligand.pdb structures/6XF3/6xf3_ligand.cif structures/6XF3/6xf3_complex.pdb structures/6XF3/6xf3_complex.cif 6XL2 classic ArrX Chrysiogenes arsenatis residues 30-310 Na arsenate (AsO4^3-) "[""ART""]" 1 Kd Kd = = 1.00 ± 0.17 μM 1000.0 [] unit_conversion 6.0 success True direct_binding ITC; Table 2 reports thermodynamic parameters for ligand binding. Measurements were performed in triplicate. 5 Table 2 reports WT ArrX–arsenate KD = 1.00 ± 0.17 μM. The methods identify binding-affinity measurements as ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\6XL2\6XL2_metadata.json point structures/6XL2/6xl2_protein.pdb structures/6XL2/6xl2_pocket.pdb structures/6XL2/6xl2_ligand.sdf structures/6XL2/6xl2_ligand.pdb structures/6XL2/6xl2_ligand.cif structures/6XL2/6xl2_complex.pdb structures/6XL2/6xl2_complex.cif 6XNC classic tryptophan synthase Salmonella enterica serovar typhimurium Na Na L-tryptophan "[""TRP""]" 1 Ki Ki = = 42 ± 22 μM 42000.0 [] unit_conversion 4.376750709602099 success True biochemical_inhibition Steady-state kinetic inhibition; 0.05 M disodium D,L-α-glycerophosphate (GP), 37 °C; Ki fitted from initial rates. 4 Table 2 reports L-tryptophan Ki = 42 ± 22 μM; the methods state that Ki values were determined by fitting initial rates for steady-state kinetic inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\6XNC\6XNC_metadata.json point structures/6XNC/6xnc_protein.pdb structures/6XNC/6xnc_pocket.pdb structures/6XNC/6xnc_ligand.sdf structures/6XNC/6xnc_ligand.pdb structures/6XNC/6xnc_ligand.cif structures/6XNC/6xnc_complex.pdb structures/6XNC/6xnc_complex.cif 6XND classic avidin Na Na Na biotin-phenol (7) "[""V8M""]" 1 Kd Kd = = 2.25 × 10⁻⁷ M 225.0 [] unit_conversion 6.647817481888637 success True direct_binding Isothermal titration calorimetry (ITC) measurement of ligand (7) binding to avidin. 3 “Isothermal titration calorimetry (ITC) shows the dissociation constant of the ligand to be Kd = 2.25 × 10⁻⁷ M (Figure S5).” auto_single_measurement only accepted activity measurement [1] 1 structures\6XND\6XND_metadata.json point structures/6XND/6xnd_protein.pdb structures/6XND/6xnd_pocket.pdb structures/6XND/6xnd_ligand.sdf structures/6XND/6xnd_ligand.pdb structures/6XND/6xnd_ligand.cif structures/6XND/6xnd_complex.pdb structures/6XND/6xnd_complex.cif 6XRN classic human PI3K-gamma human Na Na Compound 17 "[""V84""]" 1 IC50 IC50 = = 1.9 nM 1.9 [] unit_conversion 8.721246399047171 success True biochemical_inhibition Enzymatic kinase activity assay; Table 1 reports PI3Kγ IC50 for compound 17. The paper maps compound 17 bound to hPI3Kγ to PDB 6XRN. 4 Table 1 lists compound 17 with “PI3Kγ IC50 (nM)” of 1.9; its footnote identifies this as an enzymatic kinase activity assay. The following text states that the X-ray crystal structure of 17 bound to hPI3Kγ has PDB code 6XRN. auto_single_measurement only accepted activity measurement [1] 1 structures\6XRN\6XRN_metadata.json point structures/6XRN/6xrn_protein.pdb structures/6XRN/6xrn_pocket.pdb structures/6XRN/6xrn_ligand.sdf structures/6XRN/6xrn_ligand.pdb structures/6XRN/6xrn_ligand.cif structures/6XRN/6xrn_complex.pdb structures/6XRN/6xrn_complex.cif 6XS5 extended Vps29 Homo sapiens Na Na RT-D1 "[""CHAIN:B""]" 1 Kd Kd = = 95.4 nM 95.4 [] unit_conversion 7.020451625295905 success True direct_binding ITC titration of cyclic peptide with Vps29 alone. 3 Fig. 1C prints for RT-D1 binding Vps29: Kd = 95.4 nM; the caption identifies the measurements as ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\6XS5\6XS5_metadata.json point structures/6XS5/6xs5_protein.pdb structures/6XS5/6xs5_pocket.pdb structures/6XS5/6xs5_ligand.pdb structures/6XS5/6xs5_ligand.cif structures/6XS5/6xs5_complex.pdb structures/6XS5/6xs5_complex.cif 6XS7 extended Vps29 Homo sapiens Na Na RT-D2 "[""CHAIN:B""]" 1 Kd Kd = = 64.4 nM 64.4 [] unit_conversion 7.1911141326401875 success True direct_binding ITC titration of cyclic peptide with Vps29 alone. 3 Fig. 1C prints for RT-D2 binding Vps29: Kd = 64.4 nM; the caption identifies the measurements as ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\6XS7\6XS7_metadata.json point structures/6XS7/6xs7_protein.pdb structures/6XS7/6xs7_pocket.pdb structures/6XS7/6xs7_ligand.pdb structures/6XS7/6xs7_ligand.cif structures/6XS7/6xs7_complex.pdb structures/6XS7/6xs7_complex.cif 6XS9 extended Vps29 Homo sapiens Na Na RT-L1 "[""CHAIN:C"", ""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 64.0 nM 64.0 [] unit_conversion 7.1938200260161125 success True direct_binding ITC titration of cyclic peptide with Vps29 alone. 3 Fig. 1C prints for RT-L1 binding Vps29: Kd = 64.0 nM; the caption identifies the measurements as ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\6XS9\6XS9_metadata.json point structures/6XS9/6xs9_protein.pdb structures/6XS9/6xs9_pocket.pdb structures/6XS9/6xs9_ligand.pdb structures/6XS9/6xs9_ligand.cif structures/6XS9/6xs9_complex.pdb structures/6XS9/6xs9_complex.cif 6XSA extended Vps29 Homo sapiens Na Na RT-L2 "[""CHAIN:B""]" 1 Kd Kd = = 783.5 nM 783.5 [] unit_conversion 6.105960999195391 success True direct_binding ITC titration of cyclic peptide with Vps29 alone. 3 Fig. 1C prints for RT-L2 binding Vps29: Kd = 783.5 nM; the caption identifies the measurements as ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\6XSA\6XSA_metadata.json point structures/6XSA/6xsa_protein.pdb structures/6XSA/6xsa_pocket.pdb structures/6XSA/6xsa_ligand.pdb structures/6XSA/6xsa_ligand.cif structures/6XSA/6xsa_complex.pdb structures/6XSA/6xsa_complex.cif 6XXF extended Calmodulin (CaM) Homo sapiens (human) Ca2+/CaM bound to RyR2_3583-3603 peptide WT (wild type) RyR2_3583-3603 peptide "[""CHAIN:BBB""]" 1 Kd Kd = = 51±9 nM 51.0 [] unit_conversion 7.292429823902063 success True direct_binding Isothermal titration calorimetry of Ca2+/CaM binding to RyR2_3583-3603 peptide in 5 mM CaCl2 at 25°C. 2 “in the presence of Ca2+, the affinity for RyR2_3583-3603 was significantly reduced ... from 51±9 nM (CaM-WT)” (Fig. 1D). auto_single_measurement only accepted activity measurement [1] 1 structures\6XXF\6XXF_metadata.json point structures/6XXF/6xxf_ligand.cif structures/6XXF/6xxf_complex.cif 6XXX extended Calmodulin (CaM) Homo sapiens (human) Ca2+/CaM-A102V bound to RyR2_3583-3603 peptide A102V RyR2_3583-3603 peptide "[""CHAIN:BBB""]" 1 Kd Kd = = 349±72 nM 349.0 [] unit_conversion 6.45717457304082 success True direct_binding Isothermal titration calorimetry of Ca2+/CaM binding to RyR2_3583-3603 peptide in 5 mM CaCl2 at 25°C. 2 “in the presence of Ca2+, the affinity for RyR2_3583-3603 was significantly reduced ... to ... 349±72 nM (CaM-A102V)” (Fig. 1D). auto_single_measurement only accepted activity measurement [1] 1 structures\6XXX\6XXX_metadata.json point structures/6XXX/6xxx_ligand.cif structures/6XXX/6xxx_complex.cif 6XY3 extended Calmodulin (CaM) Homo sapiens (human) Ca2+/CaM-N53I bound to RyR2_3583-3603 peptide N53I RyR2_3583-3603 peptide "[""CHAIN:BBB""]" 1 Kd Kd = = 146±40 nM 146.0 [] unit_conversion 6.835647144215563 success True direct_binding Isothermal titration calorimetry of Ca2+/CaM binding to RyR2_3583-3603 peptide in 5 mM CaCl2 at 25°C. 2 “in the presence of Ca2+, the affinity for RyR2_3583-3603 was significantly reduced ... to 146±40 nM (CaM-N53I)” (Fig. 1D). auto_single_measurement only accepted activity measurement [1] 1 structures\6XY3\6XY3_metadata.json point structures/6XY3/6xy3_ligand.cif structures/6XY3/6xy3_complex.cif 6Y4K extended 14-3-3 gamma human 14-3-3 gamma residues 1-235 lacking the C-terminal 12-residue flexible tail; CaMKK2 pSer100 peptide pepS100, sequence RKLpSLQER Na Fusicoccin A; CaMKK2 pSer100 14-3-3 binding motif peptide (pepS100) "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 17.1 ± 0.5 µM 17100.0 [] unit_conversion 4.767003889607846 success True direct_binding Fluorescence-polarization binding affinity of FAM-pepS100 to 14-3-3γ in 500 µM FC-A. 3 Table 1 reports Kd = 17.1 ± 0.5 µM for FAM-pepS100 with FC-A; the caption states apparent peptide:14-3-3γ Kd values were determined by FP in 500 µM study fusicoccane. auto_single_measurement only accepted activity measurement [1] 1 structures\6Y4K\6Y4K_metadata.json point structures/6Y4K/6y4k_protein.pdb structures/6Y4K/6y4k_pocket.pdb structures/6Y4K/6y4k_ligand.pdb structures/6Y4K/6y4k_ligand.cif structures/6Y4K/6y4k_complex.pdb structures/6Y4K/6y4k_complex.cif 6Y6B extended 14-3-3 gamma human 14-3-3 gamma residues 1-235 lacking the C-terminal 12-residue flexible tail; CaMKK2 pSer100 peptide pepS100, sequence RKLpSLQER Na 16-OMe-Fusicoccin H (16-O-Me-FC-H); CaMKK2 pSer100 14-3-3 binding motif peptide (pepS100) "[""OD8"", ""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.5 ± 0.05 µM 500.0 [] unit_conversion 6.301029995663981 success True direct_binding Fluorescence-polarization binding affinity of FAM-pepS100 to 14-3-3γ in 500 µM 16-O-Me-FC-H. 3 Table 1 reports Kd = 0.5 ± 0.05 µM for FAM-pepS100 with 16-O-Me-FC-H; the caption states these apparent peptide:14-3-3γ Kd values were determined by FP in 500 µM study fusicoccane. auto_single_measurement only accepted activity measurement [1] 1 structures\6Y6B\6Y6B_metadata.json point structures/6Y6B/6y6b_protein.pdb structures/6Y6B/6y6b_pocket.pdb structures/6Y6B/6y6b_ligand.pdb structures/6Y6B/6y6b_ligand.cif structures/6Y6B/6y6b_complex.pdb structures/6Y6B/6y6b_complex.cif 6Y6S classic Mouse galactocerebrosidase (GALC) mouse Na Na GNS (galacto-noeurostegine; compound 5) "[""ODW""]" 1 Ki Ki = = 7 µM 7000.0 [] unit_conversion 5.154901959985743 success True biochemical_inhibition Competitive inhibition of GALC by GNS (5), measured at pH 4.6. 2 “5 is a competitive inhibitor of GALC at 7 μM (pH 4.6).” auto_single_measurement only accepted activity measurement [1] 1 structures\6Y6S\6Y6S_metadata.json point structures/6Y6S/6y6s_protein.pdb structures/6Y6S/6y6s_pocket.pdb structures/6Y6S/6y6s_ligand.sdf structures/6Y6S/6y6s_ligand.pdb structures/6Y6S/6y6s_ligand.cif structures/6Y6S/6y6s_complex.pdb structures/6Y6S/6y6s_complex.cif 6Y6T classic Mouse galactocerebrosidase (GALC) mouse Na Na GNS (galacto-noeurostegine; compound 5) "[""ODW""]" 1 Ki Ki = = 7 µM 7000.0 [] unit_conversion 5.154901959985743 success True biochemical_inhibition Competitive inhibition of GALC by GNS (5), measured at pH 4.6. 2 “5 is a competitive inhibitor of GALC at 7 μM (pH 4.6).” auto_single_measurement only accepted activity measurement [1] 1 structures\6Y6T\6Y6T_metadata.json point structures/6Y6T/6y6t_protein.pdb structures/6Y6T/6y6t_pocket.pdb structures/6Y6T/6y6t_ligand.sdf structures/6Y6T/6y6t_ligand.pdb structures/6Y6T/6y6t_ligand.cif structures/6Y6T/6y6t_complex.pdb structures/6Y6T/6y6t_complex.cif 6YD2 extended furin Na Na Na compound 5; 4-aminomethyl-phenylacetyl-canavanine-Tle-Arg-Amba "[""CHAIN:611""]" 1 Ki Ki = = 114 ± 23.9 pM 0.114 [] unit_conversion 9.943095148663527 success True biochemical_inhibition Enzyme kinetic assay using fluorogenic substrate Phac-Arg-Val-Arg-Arg-AMC; Table 1. 2 Table 1 lists inhibitor 5 with Ki 114 ± 23.9 pM; footnote states the assay used recombinant soluble human furin and fluorogenic substrate. auto_single_measurement only accepted activity measurement [1] 1 structures\6YD2\6YD2_metadata.json point structures/6YD2/6yd2_protein.pdb structures/6YD2/6yd2_pocket.pdb structures/6YD2/6yd2_ligand.cif structures/6YD2/6yd2_complex.cif 6YD3 extended furin Na Na Na compound 6; 4-guanidinomethyl-phenylacetyl-Canavanine-Tle-Arg-Amba "[""CHAIN:611""]" 1 Ki Ki = = 36.3 ± 11.2 pM 0.0363 [] unit_conversion 10.440093374963887 success True biochemical_inhibition Enzyme kinetic assay using fluorogenic substrate Phac-Arg-Val-Arg-Arg-AMC; Table 1. 2 Table 1 lists inhibitor 6 with Ki 36.3 ± 11.2 pM; footnote states the assay used recombinant soluble human furin and fluorogenic substrate. auto_single_measurement only accepted activity measurement [1] 1 structures\6YD3\6YD3_metadata.json point structures/6YD3/6yd3_protein.pdb structures/6YD3/6yd3_pocket.pdb structures/6YD3/6yd3_ligand.cif structures/6YD3/6yd3_complex.cif 6YD4 extended furin Na Na Na compound 8; 4-guanidinomethyl-phenylacetyl-Canavanine-Tle-Canavanine-Amba "[""CHAIN:B""]" 1 Ki Ki = = 10.1 ± 3.2 pM 0.0101 [] unit_conversion 10.995678626217357 success True biochemical_inhibition Enzyme kinetic assay using fluorogenic substrate Phac-Arg-Val-Arg-Arg-AMC; Table 1. 2 Table 1 lists inhibitor 8 with Ki 10.1 ± 3.2 pM; footnote states the assay used recombinant soluble human furin and fluorogenic substrate. auto_single_measurement only accepted activity measurement [1] 1 structures\6YD4\6YD4_metadata.json point structures/6YD4/6yd4_protein.pdb structures/6YD4/6yd4_pocket.pdb structures/6YD4/6yd4_ligand.pdb structures/6YD4/6yd4_ligand.cif structures/6YD4/6yd4_complex.pdb structures/6YD4/6yd4_complex.cif 6YD7 extended furin Na Na Na compound 4; 4-guanidinomethyl-phenylacetyl-Arg-Tle-Canavanine-Amba "[""CHAIN:B""]" 1 Ki Ki = = 13.1 ± 1.6 pM 0.0131 [] unit_conversion 10.882728704344236 success True biochemical_inhibition Enzyme kinetic assay using fluorogenic substrate Phac-Arg-Val-Arg-Arg-AMC; Table 1. 2 Table 1 lists inhibitor 4 with Ki 13.1 ± 1.6 pM; footnote states the assay used recombinant soluble human furin and fluorogenic substrate. auto_single_measurement only accepted activity measurement [1] 1 structures\6YD7\6YD7_metadata.json point structures/6YD7/6yd7_protein.pdb structures/6YD7/6yd7_pocket.pdb structures/6YD7/6yd7_ligand.pdb structures/6YD7/6yd7_ligand.cif structures/6YD7/6yd7_complex.pdb structures/6YD7/6yd7_complex.cif 6YE0 classic PotF (putrescine receptor) Escherichia coli PotF lacking the N-terminal signal peptide and carrying a C-terminal His6-tag Na Putrescine (PUT) "[""PUT""]" 1 Kd Kd = = 0.068 ± 0.040 μM 68.0 [] unit_conversion 7.167491087293763 success True direct_binding Isothermal titration calorimetry (ITC), n = 2. 3 Table 1 reports PotF–putrescine Kd = 0.068 ± 0.040 μM; the page text identifies these as ITC binding-affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\6YE0\6YE0_metadata.json point structures/6YE0/6ye0_protein.pdb structures/6YE0/6ye0_pocket.pdb structures/6YE0/6ye0_ligand.sdf structures/6YE0/6ye0_ligand.pdb structures/6YE0/6ye0_ligand.cif structures/6YE0/6ye0_complex.pdb structures/6YE0/6ye0_complex.cif 6YE2 classic human ecto-5'-nucleotidase (CD73) human Na Na A1202; compound 4a "[""OO5""]" 1 IC50 IC50 = = 0.86 nM 0.86 [] unit_conversion 9.065501548756432 success True biochemical_inhibition Soluble hCD73 inhibition assay. 5 Table 5 reports potency against hCD73 (soluble), IC50 = 0.86 nM, for 4a. auto_single_measurement only accepted activity measurement [1] 1 structures\6YE2\6YE2_metadata.json point structures/6YE2/6ye2_protein.pdb structures/6YE2/6ye2_pocket.pdb structures/6YE2/6ye2_ligand.sdf structures/6YE2/6ye2_ligand.pdb structures/6YE2/6ye2_ligand.cif structures/6YE2/6ye2_complex.pdb structures/6YE2/6ye2_complex.cif 6YE6 classic PotF (putrescine receptor) Escherichia coli PotF lacking the N-terminal signal peptide and carrying a C-terminal His6-tag Na Agmatine (AGM) "[""AG2""]" 1 Kd Kd = = 0.22 ± 0.08 μM 220.0 [] unit_conversion 6.657577319177793 success True direct_binding Isothermal titration calorimetry (ITC), n = 2. 3 Table 1 reports PotF–agmatine Kd = 0.22 ± 0.08 μM; the page text identifies these as ITC binding-affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\6YE6\6YE6_metadata.json point structures/6YE6/6ye6_protein.pdb structures/6YE6/6ye6_pocket.pdb structures/6YE6/6ye6_ligand.sdf structures/6YE6/6ye6_ligand.pdb structures/6YE6/6ye6_ligand.cif structures/6YE6/6ye6_complex.pdb structures/6YE6/6ye6_complex.cif 6YE7 classic PotF (putrescine receptor) Escherichia coli PotF lacking the N-terminal signal peptide and carrying a C-terminal His6-tag Na Cadaverine (CDV) "[""N2P""]" 1 Kd Kd = = 1.95 ± 0.16 μM 1950.0 [] unit_conversion 5.709965388637482 success True direct_binding Isothermal titration calorimetry (ITC), n = 2. 3 Table 1 reports PotF–cadaverine Kd = 1.95 ± 0.16 μM; the page text identifies these as ITC binding-affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\6YE7\6YE7_metadata.json point structures/6YE7/6ye7_protein.pdb structures/6YE7/6ye7_pocket.pdb structures/6YE7/6ye7_ligand.sdf structures/6YE7/6ye7_ligand.pdb structures/6YE7/6ye7_ligand.cif structures/6YE7/6ye7_complex.pdb structures/6YE7/6ye7_complex.cif 6YE8 classic PotF (putrescine receptor) Escherichia coli PotF lacking the N-terminal signal peptide and carrying a C-terminal His6-tag Na Spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 29.71 ± 1.15 μM 29710.0 [] unit_conversion 4.527097348196336 success True direct_binding Isothermal titration calorimetry (ITC), n = 2. 3 Table 1 reports PotF–spermidine Kd = 29.71 ± 1.15 μM; the page text identifies these as ITC binding-affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\6YE8\6YE8_metadata.json point structures/6YE8/6ye8_protein.pdb structures/6YE8/6ye8_pocket.pdb structures/6YE8/6ye8_ligand.sdf structures/6YE8/6ye8_ligand.pdb structures/6YE8/6ye8_ligand.cif structures/6YE8/6ye8_complex.pdb structures/6YE8/6ye8_complex.cif 6YH6 classic chimeric carbonic anhydrase XII (chCA XII) human CA II-based chimeric carbonic anhydrase XII A65S, N67K, I91T, F130A, V134S, L203N compound 44 (VD12-36); 2-(cyclooctylamino)-3,5,6-trifluorobenzenesulfonamide "[""OQW""]" 1 Kd Kd = = 4000 nM 4000.0 [] unit_conversion 5.3979400086720375 success True direct_binding Fluorescent thermal shift assay (pH 7.0, 37 °C); recombinant human chCA XII. 9 Table 2 reports compound 44 Kd = 4000 nM for chCA XII; Figure 7A maps compound 44 to chCA XII PDB 6YH6. auto_single_measurement only accepted activity measurement [1] 1 structures\6YH6\6YH6_metadata.json point structures/6YH6/6yh6_protein.pdb structures/6YH6/6yh6_pocket.pdb structures/6YH6/6yh6_ligand.sdf structures/6YH6/6yh6_ligand.pdb structures/6YH6/6yh6_ligand.cif structures/6YH6/6yh6_complex.pdb structures/6YH6/6yh6_complex.cif 6YH7 classic chimeric carbonic anhydrase XII (chCA XII) human CA II-based chimeric carbonic anhydrase XII A65S, N67K, I91T, F130A, V134S, L203N compound 50 (VD12-34); 3-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide "[""5EF""]" 1 Kd Kd = = 12.5 nM 12.5 [] unit_conversion 7.903089986991944 success True direct_binding Fluorescent thermal shift assay (pH 7.0, 37 °C); recombinant human chCA XII. 9 Table 2 reports compound 50 Kd = 12.5 nM for chCA XII; Figure 7C maps compound 50 to chCA XII PDB 6YH7. auto_single_measurement only accepted activity measurement [1] 1 structures\6YH7\6YH7_metadata.json point structures/6YH7/6yh7_protein.pdb structures/6YH7/6yh7_pocket.pdb structures/6YH7/6yh7_ligand.sdf structures/6YH7/6yh7_ligand.pdb structures/6YH7/6yh7_ligand.cif structures/6YH7/6yh7_complex.pdb structures/6YH7/6yh7_complex.cif 6YH8 classic chimeric carbonic anhydrase XII (chCA XII) human CA II-based chimeric carbonic anhydrase XII A65S, N67K, I91T, F130A, V134S, L203N compound 43 (VD12-29-2); 2-[(1S)-1,2,3,4-tetrahydronaphthalen-1-ylamino]-3,5,6-trifluorobenzenesulfonamide "[""OQT""]" 1 Kd Kd = = 12500 nM 12500.0 [] unit_conversion 4.903089986991944 success True direct_binding Fluorescent thermal shift assay (pH 7.0, 37 °C); recombinant human chCA XII. 9 Table 2 reports compound 43 Kd = 12500 nM for chCA XII; Figure 7A maps compound 43 to chCA XII PDB 6YH8. auto_single_measurement only accepted activity measurement [1] 1 structures\6YH8\6YH8_metadata.json point structures/6YH8/6yh8_protein.pdb structures/6YH8/6yh8_pocket.pdb structures/6YH8/6yh8_ligand.sdf structures/6YH8/6yh8_ligand.pdb structures/6YH8/6yh8_ligand.cif structures/6YH8/6yh8_complex.pdb structures/6YH8/6yh8_complex.cif 6YH9 classic chimeric carbonic anhydrase XII (chCA XII) human CA II-based chimeric carbonic anhydrase XII A65S, N67K, I91T, F130A, V134S, L203N compound 48 (VD12-25-2); 2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide "[""WWX""]" 1 Kd Kd = = 46 nM 46.0 [] unit_conversion 7.337242168318426 success True direct_binding Fluorescent thermal shift assay (pH 7.0, 37 °C); recombinant human chCA XII. 9 Table 2 reports compound 48 Kd = 46 nM for chCA XII; Figure 7B maps compound 48 to chCA XII PDB 6YH9. auto_single_measurement only accepted activity measurement [1] 1 structures\6YH9\6YH9_metadata.json point structures/6YH9/6yh9_protein.pdb structures/6YH9/6yh9_pocket.pdb structures/6YH9/6yh9_ligand.sdf structures/6YH9/6yh9_ligand.pdb structures/6YH9/6yh9_ligand.cif structures/6YH9/6yh9_complex.pdb structures/6YH9/6yh9_complex.cif 6YHC classic chimeric carbonic anhydrase XII (chCA XII) human CA II-based chimeric carbonic anhydrase XII A65S, N67K, I91T, F130A, V134S, L203N compound 52 (VD10-39b); 3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide "[""WWO""]" 1 Kd Kd = = 40 nM 40.0 [] unit_conversion 7.3979400086720375 success True direct_binding Fluorescent thermal shift assay (pH 7.0, 37 °C); recombinant human chCA XII. 9 Table 2 reports compound 52 Kd = 40 nM for chCA XII; Figure 7D maps compound 52 to chCA XII PDB 6YHC. auto_single_measurement only accepted activity measurement [1] 1 structures\6YHC\6YHC_metadata.json point structures/6YHC/6yhc_protein.pdb structures/6YHC/6yhc_pocket.pdb structures/6YHC/6yhc_ligand.sdf structures/6YHC/6yhc_ligand.pdb structures/6YHC/6yhc_ligand.cif structures/6YHC/6yhc_complex.pdb structures/6YHC/6yhc_complex.cif 6YK1 classic mouse pyridoxal kinase mouse Na Na artesunate "[""D95""]" 1 Ki Ki = = 1,250 ± 4.7 µM 1250000.0 [] unit_conversion 2.9030899869919438 success True biochemical_inhibition Dixon-plot analysis of enzymatic PDXK activity; assays used pyridoxal concentrations of 50 and 150 µM. 3 “Ki values of 120 ± 24 and 1250 ± 4.7 µM were derived for artemisinin and artesunate, respectively.” auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\6YK1\6YK1_metadata.json point structures/6YK1/6yk1_protein.pdb structures/6YK1/6yk1_pocket.pdb structures/6YK1/6yk1_ligand.sdf structures/6YK1/6yk1_ligand.pdb structures/6YK1/6yk1_ligand.cif structures/6YK1/6yk1_complex.pdb structures/6YK1/6yk1_complex.cif 6YLD extended Trichoplax adhaerens trBcl-2L2 Trichoplax adhaerens trBcl-2L2 residues 34-182 Na trBak BH3 "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 563 ± 30 nM 563.0 [] unit_conversion 6.249491605148654 success True direct_binding Isothermal titration calorimetry of recombinant trBcl-2L2 with a peptide spanning the trBak BH3 motif. 6 trBcl-2L2 bound trBak with nanomolar affinity (K_D of 563 nM); Fig. 4A prints 563 ± 30 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\6YLD\6YLD_metadata.json point structures/6YLD/6yld_protein.pdb structures/6YLD/6yld_pocket.pdb structures/6YLD/6yld_ligand.pdb structures/6YLD/6yld_ligand.cif structures/6YLD/6yld_complex.pdb structures/6YLD/6yld_complex.cif 6YLI extended Human Bcl-xL human Bcl-xL residues 1-209 Deltaop45 Trichoplax adhaerens trBak BH3 "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 197 ± 23 nM 197.0 [] unit_conversion 6.7055337738384075 success True direct_binding Isothermal titration calorimetry of recombinant human Bcl-xL with a peptide spanning the trBak BH3 motif. 8 Fig. 5A prints the human Bcl-xL affinity for trBak as K_D = 197 ± 23 nM. Methods specify the Bcl-xL residues 1–209 Deltaop45 construct. auto_single_measurement only accepted activity measurement [1] 1 structures\6YLI\6YLI_metadata.json point structures/6YLI/6yli_protein.pdb structures/6YLI/6yli_pocket.pdb structures/6YLI/6yli_ligand.pdb structures/6YLI/6yli_ligand.cif structures/6YLI/6yli_complex.pdb structures/6YLI/6yli_complex.cif 6YPW classic human carbonic anhydrase II human Na Na compound 7: 4-((1-(2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl)-1H-1,2,3-triazol-4-yl)methoxy)benzenesulfonamide "[""P75""]" 1 Ki Ki = = 1.3 nM 1.3 [] unit_conversion 8.886056647693163 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay. 2 Table 1 reports compound 7 Ki = 1.3 nM for hCA II. auto_single_measurement only accepted activity measurement [1] 1 structures\6YPW\6YPW_metadata.json point structures/6YPW/6ypw_protein.pdb structures/6YPW/6ypw_pocket.pdb structures/6YPW/6ypw_ligand.sdf structures/6YPW/6ypw_ligand.pdb structures/6YPW/6ypw_ligand.cif structures/6YPW/6ypw_complex.pdb structures/6YPW/6ypw_complex.cif 6YR5 extended 14-3-3 sigma Na 14-3-3 sigma DeltaC, with the C-terminus truncated for crystallography Na hDMX361-374 pSer367 peptide "[""CHAIN:O"", ""CHAIN:P"", ""CHAIN:Q"", ""CHAIN:R""]" 1 Kd Kd = = 3.6 ± 0.4 µM 3600.0 [] unit_conversion 5.443697499232712 success True direct_binding Fluorescence anisotropy; Table 2. 7 Table 2 reports Kd = 3.6 ± 0.4 µM for hDMX361-374 pSer367 binding to 14-3-3σ. auto_single_measurement only accepted activity measurement [1] 1 structures\6YR5\6YR5_metadata.json point structures/6YR5/6yr5_protein.pdb structures/6YR5/6yr5_pocket.pdb structures/6YR5/6yr5_ligand.pdb structures/6YR5/6yr5_ligand.cif structures/6YR5/6yr5_complex.pdb structures/6YR5/6yr5_complex.cif 6YR6 extended 14-3-3 sigma Na 14-3-3 sigma DeltaC, with the C-terminus truncated for crystallography Na hDM2 180-192 pSer186 peptide "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H""]" 1 Kd Kd > > 170 µM 170000.0 [] unit_conversion 3.769551078621726 success True direct_binding Fluorescence anisotropy; Table 2. 7 Table 2 reports Kd >170 µM for hDM2 180-192 pSer186 binding to 14-3-3σ. auto_single_measurement only accepted activity measurement [1] 1 structures\6YR6\6YR6_metadata.json point structures/6YR6/6yr6_protein.pdb structures/6YR6/6yr6_pocket.pdb structures/6YR6/6yr6_ligand.pdb structures/6YR6/6yr6_ligand.cif structures/6YR6/6yr6_complex.pdb structures/6YR6/6yr6_complex.cif 6YRI classic HCAII Na Na Na caffeic acid (CFA; compound 2) "[""DHC""]" 1 Ki Ki = = 1.61 µM 1610.0 [] unit_conversion 5.79317412396815 success True biochemical_inhibition Inhibition assay of hCA II with CFA; incubation time 15 min; stopped-flow technique. 2 Table 1 lists CFA Ki = 1.61 µM at incubation time 15 min. auto_single_measurement only accepted activity measurement [1] 1 structures\6YRI\6YRI_metadata.json point structures/6YRI/6yri_protein.pdb structures/6YRI/6yri_pocket.pdb structures/6YRI/6yri_ligand.sdf structures/6YRI/6yri_ligand.pdb structures/6YRI/6yri_ligand.cif structures/6YRI/6yri_complex.pdb structures/6YRI/6yri_complex.cif 6YUH classic SMYD3 Na Full-length SMYD3 expressed from pET15b with an N-terminal hexahistidine tag and thrombin cleavage site Na (R)-diperodon "[""POW""]" 1 Kd Kd = = 84 ± 12 μM 84000.0 [] unit_conversion 4.075720713938118 success True direct_binding SPR biosensor steady-state analysis using immobilized SMYD3; concentration series up to 100 μM. 4 The paper reports K_D values of 42 ± 8 μM for (S)-diperodon and 84 ± 12 μM for (R)-diperodon. It identifies 6YUH as the SMYD3-(R)-diperodon co-crystal structure. auto_single_measurement only accepted activity measurement [1] 1 structures\6YUH\6YUH_metadata.json point structures/6YUH/6yuh_protein.pdb structures/6YUH/6yuh_pocket.pdb structures/6YUH/6yuh_ligand.sdf structures/6YUH/6yuh_ligand.pdb structures/6YUH/6yuh_ligand.cif structures/6YUH/6yuh_complex.pdb structures/6YUH/6yuh_complex.cif 6YUR classic Staphylococcus aureus enoyl-ACP reductase (saFabI/FabI) Staphylococcus aureus Na Na SKTS1 "[""F9T""]" 1 Ki Ki = = 46 nM 46.0 [] unit_conversion 7.337242168318426 success True biochemical_inhibition Kinetic inhibition experiment at 37 °C; Table 1 reports SKTS1 Kiapp for saFabI. 4 Table 1, “Kinetic Parameters for SKTS1 Inhibition of InhA and saFabI at 37 °C,” reports Kiapp = 46 nM for saFabI. auto_single_measurement only accepted activity measurement [1] 1 structures\6YUR\6YUR_metadata.json point structures/6YUR/6yur_protein.pdb structures/6YUR/6yur_pocket.pdb structures/6YUR/6yur_ligand.sdf structures/6YUR/6yur_ligand.pdb structures/6YUR/6yur_ligand.cif structures/6YUR/6yur_complex.pdb structures/6YUR/6yur_complex.cif 6YUU classic Mycobacterium tuberculosis enoyl-ACP reductase (InhA) Mycobacterium tuberculosis Na Na SKTS1 "[""F9T""]" 1 Ki Ki = = 90 ± 14 nM 90.0 [] unit_conversion 7.045757490560675 success True biochemical_inhibition Kinetic inhibition experiment at 37 °C; Table 1 reports SKTS1 Kiapp for InhA. 4 Table 1, “Kinetic Parameters for SKTS1 Inhibition of InhA and saFabI at 37 °C,” reports Kiapp = 90 ± 14 nM for InhA. auto_single_measurement only accepted activity measurement [1] 1 structures\6YUU\6YUU_metadata.json point structures/6YUU/6yuu_protein.pdb structures/6YUU/6yuu_pocket.pdb structures/6YUU/6yuu_ligand.sdf structures/6YUU/6yuu_ligand.pdb structures/6YUU/6yuu_ligand.cif structures/6YUU/6yuu_complex.pdb structures/6YUU/6yuu_complex.cif 6YVI classic EED Na Na Na compound 19 (R1 = CN) "[""PV5""]" 1 Kd Kd = = 15 nM 15.0 [] unit_conversion 7.823908740944319 success True direct_binding EED SPR affinity; geometric mean of at least two Kd determinations per compound. 2 Table 1 lists compound 19 (R1 = CN): EED SPR Kd = 15; table footnote states nanomolar affinity. auto_single_measurement only accepted activity measurement [1] 1 structures\6YVI\6YVI_metadata.json point structures/6YVI/6yvi_protein.pdb structures/6YVI/6yvi_pocket.pdb structures/6YVI/6yvi_ligand.sdf structures/6YVI/6yvi_ligand.pdb structures/6YVI/6yvi_ligand.cif structures/6YVI/6yvi_complex.pdb structures/6YVI/6yvi_complex.cif 6YZH extended CK2alpha Na Na Na P8C9 "[""CHAIN:D""]" 1 IC50 IC50 = = 1.7 ± 0.3 μM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding Fluorescence-polarisation assay of cyclic peptides against CK2α; Table 2 reports IC50 ± SEM. 3 Table 2 lists P8C9 with IC50 1.7 ± 0.3 μM; the text states the cyclic peptides were tested in an FP assay and identifies P8C9 as binding CK2α. auto_single_measurement only accepted activity measurement [1] 1 structures\6YZH\6YZH_metadata.json point structures/6YZH/6yzh_protein.pdb structures/6YZH/6yzh_pocket.pdb structures/6YZH/6yzh_ligand.pdb structures/6YZH/6yzh_ligand.cif structures/6YZH/6yzh_complex.pdb structures/6YZH/6yzh_complex.cif 6Z19 extended CK2alpha Na Na Na P8C9 "[""CHAIN:C""]" 1 IC50 IC50 = = 1.7 ± 0.3 μM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding Fluorescence-polarisation assay of cyclic peptides against CK2α; Table 2 reports IC50 ± SEM. 3 Table 2 lists P8C9 with IC50 1.7 ± 0.3 μM; the text states the cyclic peptides were tested in an FP assay and identifies P8C9 as binding CK2α. auto_single_measurement only accepted activity measurement [1] 1 structures\6Z19\6Z19_metadata.json point structures/6Z19/6z19_protein.pdb structures/6Z19/6z19_pocket.pdb structures/6Z19/6z19_ligand.pdb structures/6Z19/6z19_ligand.cif structures/6Z19/6z19_complex.pdb structures/6Z19/6z19_complex.cif 6Z61 classic NAD kinase 1 (LmNADK1) Listeria monocytogenes Na Na compound 2 "[""Q9H""]" 1 Ki Ki = = 347 µM 347000.0 [] unit_conversion 3.459670525209126 success True biochemical_inhibition Competitive inhibition of recombinant LmNADK1; activity measured at 30 °C with NAD varied and inhibitor concentrations of 0, 10, 25, or 50 µM. 6 Figure 5 reports the Ki bar for compound 2 as 347 µM; the text identifies compounds 2–5 as inhibitors of recombinant LmNADK1 in vitro. Figure 4 maps compound 2 to PDB 6Z61. auto_single_measurement only accepted activity measurement [1] 1 structures\6Z61\6Z61_metadata.json point structures/6Z61/6z61_protein.pdb structures/6Z61/6z61_pocket.pdb structures/6Z61/6z61_ligand.sdf structures/6Z61/6z61_ligand.pdb structures/6Z61/6z61_ligand.cif structures/6Z61/6z61_complex.pdb structures/6Z61/6z61_complex.cif 6Z64 classic NAD kinase 1 (LmNADK1) Listeria monocytogenes Na Na compound 5 "[""Q9K""]" 1 Ki Ki = = 5.6 µM 5600.0 [] unit_conversion 5.251811972993799 success True biochemical_inhibition Competitive inhibition of recombinant LmNADK1; activity measured at 30 °C with NAD varied and inhibitor concentrations of 0, 10, 25, or 50 µM. 6 Figure 5 reports the Ki bar for compound 5 as 5.6 µM; the text identifies compounds 2–5 as inhibitors of recombinant LmNADK1 in vitro. Figure 4 maps compound 5 to PDB 6Z64. auto_single_measurement only accepted activity measurement [1] 1 structures\6Z64\6Z64_metadata.json point structures/6Z64/6z64_protein.pdb structures/6Z64/6z64_pocket.pdb structures/6Z64/6z64_ligand.sdf structures/6Z64/6z64_ligand.pdb structures/6Z64/6z64_ligand.cif structures/6Z64/6z64_complex.pdb structures/6Z64/6z64_complex.cif 6Z65 classic NAD kinase 1 (LmNADK1) Listeria monocytogenes Na Na compound 4 "[""Q9N""]" 1 Ki Ki = = 23.8 µM 23800.0 [] unit_conversion 4.623423042943488 success True biochemical_inhibition Competitive inhibition of recombinant LmNADK1; activity measured at 30 °C with NAD varied and inhibitor concentrations of 0, 10, 25, or 50 µM. 6 Figure 5 reports the Ki bar for compound 4 as 23.8 µM; the text identifies compounds 2–5 as inhibitors of recombinant LmNADK1 in vitro. Figure 4 maps compound 4 to PDB 6Z65. auto_single_measurement only accepted activity measurement [1] 1 structures\6Z65\6Z65_metadata.json point structures/6Z65/6z65_protein.pdb structures/6Z65/6z65_pocket.pdb structures/6Z65/6z65_ligand.sdf structures/6Z65/6z65_ligand.pdb structures/6Z65/6z65_ligand.cif structures/6Z65/6z65_complex.pdb structures/6Z65/6z65_complex.cif 6Z6C extended FleA lectin Aspergillus fumigatus Na Na compound 8 "[""Q9Q""]" 1 Kd Kd = = 18.5 ± 0.6 μM 18500.0 [] unit_conversion 4.732828271596986 success True direct_binding Isothermal titration calorimetry (ITC) of monovalent compound 8 toward FleA. 3 Table 1 reports compound 8 Kd = 18.5 ± 0.6 μM toward FleA by ITC; the text identifies ligand 8 as the crystallized FleA complex. auto_single_measurement only accepted activity measurement [1] 1 structures\6Z6C\6Z6C_metadata.json point structures/6Z6C/6z6c_ligand.cif structures/6Z6C/6z6c_complex.cif 6Z81 classic EcTsaBD heterodimer Escherichia coli Na Na BK951 "[""QCB""]" 1 Kd Kd = = 3.4 ± 0.6 µM 3400.0 [] unit_conversion 5.468521082957745 success True direct_binding Microscale thermophoresis measurement of BK951 binding to fluorescently labelled EcTsaBD heterodimer, with 1 mM ATP. 7 Table 2 reports Kd = 3.4 ± 0.6 µM, obtained by MST with fluorescently labelled EcTsaBD; Figure 5D identifies this as BK951 binding to labelled TsaBD heterodimer. auto_single_measurement only accepted activity measurement [1] 1 structures\6Z81\6Z81_metadata.json point structures/6Z81/6z81_protein.pdb structures/6Z81/6z81_pocket.pdb structures/6Z81/6z81_ligand.sdf structures/6Z81/6z81_ligand.pdb structures/6Z81/6z81_ligand.cif structures/6Z81/6z81_complex.pdb structures/6Z81/6z81_complex.cif 6ZC9 extended 14-3-3 gamma human 14-3-3 gamma DeltaC, C-terminally truncated by removal of the 15 flexible C-terminal residues Na pep-S448, Nedd4-2 phosphopeptide containing pSer448 "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 Kd Kd = = 7.2 ± 0.7 µM 7200.0 [] unit_conversion 5.142667503568731 success True direct_binding Fluorescence-polarization titration of FITC-labeled pep-S448 with human 14-3-3 isoforms; Table 1 reports the γ-isoform value. 5 Table 1 lists 14-3-3γ with pep-S448: K_D = 7.2 ± 0.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZC9\6ZC9_metadata.json point structures/6ZC9/6zc9_protein.pdb structures/6ZC9/6zc9_pocket.pdb structures/6ZC9/6zc9_ligand.pdb structures/6ZC9/6zc9_ligand.cif structures/6ZC9/6zc9_complex.pdb structures/6ZC9/6zc9_complex.cif 6ZFZ classic M1 muscarinic acetylcholine receptor (M1 mAChR) human M1-StaR-T4L thermostabilized receptor construct with T4 lysozyme inserted in ICL3, terminal truncations, GP64 signal sequence, and C-terminal decahistidine tag F27A, T32A, V46L, L64A, T95A, W101A, S112A, A143L, A196T, K362A, A364L, S411A, C435A 77-LH-28-1 "[""QJT""]" 1 Kd Kd = = 3.7 ± 1.1 (3) nM 3.7 [] unit_conversion 8.431798275933005 success True direct_binding Saturation radioligand binding using [3H]-77-LH-28-1. 56 Supplementary Table S2 reports for M1-StaR-T4L with radioligand 77-LH-28-1: Kd 3.7 ± 1.1 (3) nM. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZFZ\6ZFZ_metadata.json point structures/6ZFZ/6zfz_protein.pdb structures/6ZFZ/6zfz_pocket.pdb structures/6ZFZ/6zfz_ligand.sdf structures/6ZFZ/6zfz_ligand.pdb structures/6ZFZ/6zfz_ligand.cif structures/6ZFZ/6zfz_complex.pdb structures/6ZFZ/6zfz_complex.cif 6ZHL classic RsgA Staphylococcus aureus 291-residue S. aureus RsgA with an N-terminal 20-residue tag MGSSHHHHHHSSGLVPRGSH; 311 residues total Na ppGpp "[""G4P""]" 1 Kd Kd = = 2.2 ± 0.2 µM 2200.0 [] unit_conversion 5.657577319177793 success True direct_binding DRaCALA binding assay using recombinant 6×His-tagged RsgA. 4 Table 1 reports RsgA binding affinity for ppGpp as Kd 2.2 ± 0.2 µM; the accompanying Results text describes DRaCALA with recombinant RsgA. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZHL\6ZHL_metadata.json point structures/6ZHL/6zhl_protein.pdb structures/6ZHL/6zhl_pocket.pdb structures/6ZHL/6zhl_ligand.sdf structures/6ZHL/6zhl_ligand.pdb structures/6ZHL/6zhl_ligand.cif structures/6ZHL/6zhl_complex.pdb structures/6ZHL/6zhl_complex.cif 6ZHM classic RsgA Staphylococcus aureus Na Na GDP "[""GDP""]" 1 Kd Kd = = 1.8 ± 0.2 µM 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding DRaCALA binding assay using recombinant 6×His-tagged RsgA. 4 Table 1 reports RsgA binding affinity for GDP as Kd 1.8 ± 0.2 µM; the Results text describes DRaCALA with recombinant RsgA. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZHM\6ZHM_metadata.json point structures/6ZHM/6zhm_protein.pdb structures/6ZHM/6zhm_pocket.pdb structures/6ZHM/6zhm_ligand.sdf structures/6ZHM/6zhm_ligand.pdb structures/6ZHM/6zhm_ligand.cif structures/6ZHM/6zhm_complex.pdb structures/6ZHM/6zhm_complex.cif 6ZL4 classic glutamate transporter homologue GltTk Thermococcus kodakarensis His8-tagged wild-type GltTk wild-type p-OMe-azo-TBOA, cis "[""QM5""]" 1 IC50 IC50 = = 9.1 ± 1.5 µM 9100.0 [] unit_conversion 5.040958607678906 success True biochemical_inhibition Transport assay of purified, reconstituted GltTk; cis p-OMe-azo-TBOA is the weaker inhibitor. 3 Figure 2 explicitly prints for cis p-OMe-azo-TBOA: “weaker inhibitor IC50 = 9.1 ± 1.5 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\6ZL4\6ZL4_metadata.json point structures/6ZL4/6zl4_protein.pdb structures/6ZL4/6zl4_pocket.pdb structures/6ZL4/6zl4_ligand.sdf structures/6ZL4/6zl4_ligand.pdb structures/6ZL4/6zl4_ligand.cif structures/6ZL4/6zl4_complex.pdb structures/6ZL4/6zl4_complex.cif 6ZLH classic glutamate transporter homologue GltTk Thermococcus kodakarensis His8-tagged wild-type GltTk wild-type p-OMe-azo-TBOA, trans "[""QM5""]" 1 IC50 IC50 = = 2.5 ± 0.4 µM 2500.0 [] unit_conversion 5.6020599913279625 success True biochemical_inhibition Transport assay of purified, reconstituted GltTk; trans p-OMe-azo-TBOA is the stronger inhibitor. 3 Figure 2 explicitly prints for trans p-OMe-azo-TBOA: “stronger inhibitor IC50 = 2.5 ± 0.4 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\6ZLH\6ZLH_metadata.json point structures/6ZLH/6zlh_protein.pdb structures/6ZLH/6zlh_pocket.pdb structures/6ZLH/6zlh_ligand.sdf structures/6ZLH/6zlh_ligand.pdb structures/6ZLH/6zlh_ligand.cif structures/6ZLH/6zlh_complex.pdb structures/6ZLH/6zlh_complex.cif 6ZN2 classic tyrosine hydroxylase (TH) human Coordinates for residues 40-57 and 163-497 Na dopamine (DA) "[""LDP""]" 1 IC50 IC50 = = 0.49 ± 0.04 μM 490.0 [] unit_conversion 6.309803919971486 success True biochemical_inhibition Purified full-length TH activity inhibition by dopamine; IC50 from four-parameter logistic fitting of triplicate curves. 8 “The calculated IC50 for TH (0.49 ± 0.04 μM)”; Fig. 5 identifies IC50 values from TH activity versus DA concentration. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZN2\6ZN2_metadata.json point structures/6ZN2/6zn2_protein.pdb structures/6ZN2/6zn2_pocket.pdb structures/6ZN2/6zn2_ligand.sdf structures/6ZN2/6zn2_ligand.pdb structures/6ZN2/6zn2_ligand.cif structures/6ZN2/6zn2_complex.pdb structures/6ZN2/6zn2_complex.cif 6ZNG classic MaeB full-length enzyme Bdellovibrio bacteriovorus strain HD100 Full-length MaeB, residues Met1-Lys780 Na acetyl-CoA "[""ACO""]" 1 IC50 IC50 = = 0.453 ± 0.019 μM 453.0 [] unit_conversion 6.343901797987169 success True biochemical_inhibition Dose-response inhibition of full-length MaeB oxidative L-malate decarboxylation; L-malate and NADP+ concentrations fixed. 4 Fig. 2E explicitly reports “IC50 = 0.453 ± 0.019 μM” for acetyl-CoA. The text on page 3 identifies the dose-response assay as full-length MaeB activity. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZNG\6ZNG_metadata.json point structures/6ZNG/6zng_protein.pdb structures/6ZNG/6zng_pocket.pdb structures/6ZNG/6zng_ligand.sdf structures/6ZNG/6zng_ligand.pdb structures/6ZNG/6zng_ligand.cif structures/6ZNG/6zng_complex.pdb structures/6ZNG/6zng_complex.cif 6ZOR classic estrogen receptor alpha Na estrogen receptor alpha ligand binding domain construct Na compound 28 "[""QNH""]" 1 pIC50 IC50 = = 8.6 2.5118864315095824 [] p_metric_transform 8.6 success True direct_binding ER binding assay; Table 5, compound 28 (n = 1 as marked by footnote b). 11 Table 5 lists compound 28 with “ER bind pIC50” of 8.6. The table legend identifies the binding metric and footnote b states n = 1. The paper maps 6ZOR to compound 28 bound to the ERα ligand-binding-domain construct. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZOR\6ZOR_metadata.json point structures/6ZOR/6zor_protein.pdb structures/6ZOR/6zor_pocket.pdb structures/6ZOR/6zor_ligand.sdf structures/6ZOR/6zor_ligand.pdb structures/6ZOR/6zor_ligand.cif structures/6ZOR/6zor_complex.pdb structures/6ZOR/6zor_complex.cif 6ZQR classic fibrinogen C domain-containing protein 1 (FIBCD1) human FIBCD1-FReD residues 236-461; Sf9 insect-cell expressed Na GlcNAc "[""NAG""]" 1 Kd Kd = = 27 ± 9 mM 27000000.0 [] unit_conversion 1.568636235841013 success True direct_binding Microscale thermophoresis of Sf9-expressed recombinant FIBCD1-FReD with GlcNAc. 4 MST analysis reports GlcNAc Kd = 27 ± 9 mM; methods specify the MST protein was Sf9-expressed FIBCD1-FReD residues 236–461. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZQR\6ZQR_metadata.json point structures/6ZQR/6zqr_protein.pdb structures/6ZQR/6zqr_pocket.pdb structures/6ZQR/6zqr_ligand.sdf structures/6ZQR/6zqr_ligand.pdb structures/6ZQR/6zqr_ligand.cif structures/6ZQR/6zqr_complex.pdb structures/6ZQR/6zqr_complex.cif 6ZTC classic Prostaglandin D2 synthase (H-PGDS) Na Na Na fragment 1a "[""QPN""]" 1 IC50 IC50 = = 2.8 µM 2800.0 [] unit_conversion 5.552841968657781 success True biochemical_inhibition Fluorescence-polarization assay; compound 1a is described as a weak, competitive, reversible inhibitor of human H-PGDS. 3 “hit molecule 1a (H-PGDS IC50 = 2.8 μM) … a weak, competitive, reversible inhibitor of human H-PGDS in a fluorescence polarization (FP) assay.” auto_single_measurement only accepted activity measurement [1] 1 structures\6ZTC\6ZTC_metadata.json point structures/6ZTC/6ztc_protein.pdb structures/6ZTC/6ztc_pocket.pdb structures/6ZTC/6ztc_ligand.sdf structures/6ZTC/6ztc_ligand.pdb structures/6ZTC/6ztc_ligand.cif structures/6ZTC/6ztc_complex.pdb structures/6ZTC/6ztc_complex.cif 6ZVP classic tyrosine hydroxylase (TH) human Residues 40-497; regulatory domain residues 40-165 modeled with backbone atoms only Na dopamine (DA) "[""LDP""]" 1 IC50 IC50 = = 0.49 ± 0.04 μM 490.0 [] unit_conversion 6.309803919971486 success True biochemical_inhibition Purified full-length TH activity inhibition by dopamine; IC50 from four-parameter logistic fitting of triplicate curves. 8 “The calculated IC50 for TH (0.49 ± 0.04 μM)”; Fig. 5 identifies IC50 values from TH activity versus DA concentration. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZVP\6ZVP_metadata.json point structures/6ZVP/6zvp_protein.pdb structures/6ZVP/6zvp_pocket.pdb structures/6ZVP/6zvp_ligand.sdf structures/6ZVP/6zvp_ligand.pdb structures/6ZVP/6zvp_ligand.cif structures/6ZVP/6zvp_complex.pdb structures/6ZVP/6zvp_complex.cif 6ZWE classic human acetylcholinesterase (hAChE) human Na Na compound 3; ((6-((2E,4E)-5-(benzo[d][1,3]dioxol-5-yl)penta-2,4-dienamido)hexyl)triphenylphosphonium bromide) "[""QRH""]" 1 IC50 IC50 = = 2.0 ± 0.2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition Recombinant hAChE inhibition measured spectrophotometrically at 412 nm and 25 °C using Ellman buffer; IC50 determined by nonlinear fitting. 10 Table 2 reports compound 3 hAChE IC50 = 2.0 ± 0.2 µM. The paper maps 6ZWE to hAChE in complex with compound 3. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZWE\6ZWE_metadata.json point structures/6ZWE/6zwe_protein.pdb structures/6ZWE/6zwe_pocket.pdb structures/6ZWE/6zwe_ligand.sdf structures/6ZWE/6zwe_ligand.pdb structures/6ZWE/6zwe_ligand.cif structures/6ZWE/6zwe_complex.pdb structures/6ZWE/6zwe_complex.cif 6ZWI extended human butyrylcholinesterase (hBChE) human Na Na compound 3; ((6-((2E,4E)-5-(benzo[d][1,3]dioxol-5-yl)penta-2,4-dienamido)hexyl)triphenylphosphonium bromide) "[""QRH""]" 1 IC50 IC50 = = 3.0 ± 0.4 µM 3000.0 [] unit_conversion 5.522878745280337 success True biochemical_inhibition Recombinant hBChE inhibition measured spectrophotometrically at 412 nm and 25 °C using Ellman buffer; IC50 determined by nonlinear fitting. 10 Table 2 reports compound 3 hBChE IC50 = 3.0 ± 0.4 µM. The paper maps 6ZWI to hBChE in complex with compound 3. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZWI\6ZWI_metadata.json point structures/6ZWI/6zwi_protein.pdb structures/6ZWI/6zwi_pocket.pdb structures/6ZWI/6zwi_ligand.pdb structures/6ZWI/6zwi_ligand.cif structures/6ZWI/6zwi_complex.pdb structures/6ZWI/6zwi_complex.cif 6ZWK extended C6 gammaXbody (C6 nanobody) Lama pacos (alpaca) C6 VHH nanobody Na Phosphorylated H2AX C-terminal tail peptide CKATQA(p)SQEY (ApSQEY) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 11 +/- 4 nM 11.0 [] unit_conversion 7.958607314841775 success True direct_binding Surface plasmon resonance using purified monovalent C6 and immobilized phosphopeptide; K_D determined from equilibrium response versus concentration. 9 “To calculate the affinity of C6 for the antigen (K_D value) we used purified monovalent molecules and found that it lies in the low nanomolar range (11 +/− 4 nM; Figure S3C).” auto_single_measurement only accepted activity measurement [1] 1 structures\6ZWK\6ZWK_metadata.json point structures/6ZWK/6zwk_protein.pdb structures/6ZWK/6zwk_pocket.pdb structures/6ZWK/6zwk_ligand.pdb structures/6ZWK/6zwk_ligand.cif structures/6ZWK/6zwk_complex.pdb structures/6ZWK/6zwk_complex.cif 6ZXM classic DgcR diguanylate cyclase Leptospira biflexa Full-length DgcR, residues 1-298 Na c-di-GMP "[""C2E""]" 1 Ki Ki ~ ~ 30 μM 30000.0 [] unit_conversion 4.522878745280337 success True biochemical_inhibition Kinetic model of non-competitive feedback product inhibition of native wild-type DgcR by c-di-GMP. 10 The native DgcR progress curve is described as consistent with a classical model having “a relatively large Ki of about 30 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\6ZXM\6ZXM_metadata.json point structures/6ZXM/6zxm_protein.pdb structures/6ZXM/6zxm_pocket.pdb structures/6ZXM/6zxm_ligand.sdf structures/6ZXM/6zxm_ligand.pdb structures/6ZXM/6zxm_ligand.cif structures/6ZXM/6zxm_complex.pdb structures/6ZXM/6zxm_complex.cif 6ZXR extended KDEL receptor 2 (KDEL2R) Chicken (Gallus gallus) Na Na RDEL peptide (TAERDEL) "[""CHAIN:B""]" 1 Kd Kd = = 2.71 μM 2710.0 [] unit_conversion 5.567030709125595 success True direct_binding Purified-receptor retrieval-signal binding; apparent Kd reported for RDEL. 2 “HDEL has the highest affinity for the receptor KD 0.24 μM, followed by KDEL KD 1.94 μM and RDEL KD 2.71 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZXR\6ZXR_metadata.json point structures/6ZXR/6zxr_protein.pdb structures/6ZXR/6zxr_pocket.pdb structures/6ZXR/6zxr_ligand.pdb structures/6ZXR/6zxr_ligand.cif structures/6ZXR/6zxr_complex.pdb structures/6ZXR/6zxr_complex.cif 6ZYN extended VIM-2 Na Na Na 2-Mercaptomethyl-thiazolidine L-anti-1b "[""QT2""]" 1 Ki Ki = = 0.75 ± 0.09 µM 750.0 [] unit_conversion 6.1249387366083 success True biochemical_inhibition Steady-state inhibition of imipenem hydrolysis by purified VIM-2. 4 Table 1 reports L-anti-1b Ki = 0.75 ± 0.09 µM for VIM-2; text states Ki values were obtained by fitting to a competitive inhibition model. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZYN\6ZYN_metadata.json point structures/6ZYN/6zyn_protein.pdb structures/6ZYN/6zyn_pocket.pdb structures/6ZYN/6zyn_ligand.pdb structures/6ZYN/6zyn_ligand.cif structures/6ZYN/6zyn_complex.pdb structures/6ZYN/6zyn_complex.cif 6ZYO extended VIM-2 Na Na Na 2-Mercaptomethyl-thiazolidine D-syn-1b "[""QST""]" 1 Ki Ki = = 1.9 ± 0.1 µM 1900.0 [] unit_conversion 5.721246399047171 success True biochemical_inhibition Steady-state inhibition of imipenem hydrolysis by purified VIM-2. 4 Table 1 reports D-syn-1b Ki = 1.9 ± 0.1 µM for VIM-2; text states Ki values were obtained by fitting to a competitive inhibition model. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZYO\6ZYO_metadata.json point structures/6ZYO/6zyo_protein.pdb structures/6ZYO/6zyo_pocket.pdb structures/6ZYO/6zyo_ligand.pdb structures/6ZYO/6zyo_ligand.cif structures/6ZYO/6zyo_complex.pdb structures/6ZYO/6zyo_complex.cif 6ZYP classic NDM-1 Na Na Na 2-Mercaptomethyl-thiazolidine L-anti-1b "[""QT2""]" 1 Ki Ki = = 0.44 ± 0.06 µM 440.0 [] unit_conversion 6.356547323513812 success True biochemical_inhibition Steady-state inhibition of imipenem hydrolysis by purified NDM-1. 4 Table 1 reports L-anti-1b Ki = 0.44 ± 0.06 µM for NDM-1; text states Ki values were obtained by fitting to a competitive inhibition model. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZYP\6ZYP_metadata.json point structures/6ZYP/6zyp_protein.pdb structures/6ZYP/6zyp_pocket.pdb structures/6ZYP/6zyp_ligand.sdf structures/6ZYP/6zyp_ligand.pdb structures/6ZYP/6zyp_ligand.cif structures/6ZYP/6zyp_complex.pdb structures/6ZYP/6zyp_complex.cif 6ZYQ classic NDM-1 Na Na Na 2-Mercaptomethyl-thiazolidine D-syn-1b "[""QST""]" 1 Ki Ki = = 0.60 ± 0.05 µM 600.0 [] unit_conversion 6.221848749616356 success True biochemical_inhibition Steady-state inhibition of imipenem hydrolysis by purified NDM-1. 4 Table 1 reports D-syn-1b Ki = 0.60 ± 0.05 µM for NDM-1; text states Ki values were obtained by fitting to a competitive inhibition model. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZYQ\6ZYQ_metadata.json point structures/6ZYQ/6zyq_protein.pdb structures/6ZYQ/6zyq_pocket.pdb structures/6ZYQ/6zyq_ligand.sdf structures/6ZYQ/6zyq_ligand.pdb structures/6ZYQ/6zyq_ligand.cif structures/6ZYQ/6zyq_complex.pdb structures/6ZYQ/6zyq_complex.cif 6ZYR classic IMP-1 Na Na Na 2-Mercaptomethyl-thiazolidine L-anti-1b "[""QT2""]" 1 Ki Ki = = 0.46 ± 0.05 µM 460.0 [] unit_conversion 6.337242168318426 success True biochemical_inhibition Steady-state inhibition of imipenem hydrolysis by purified IMP-1. 4 Table 1 reports L-anti-1b Ki = 0.46 ± 0.05 µM for IMP-1; text states Ki values were obtained by fitting to a competitive inhibition model. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZYR\6ZYR_metadata.json point structures/6ZYR/6zyr_protein.pdb structures/6ZYR/6zyr_pocket.pdb structures/6ZYR/6zyr_ligand.sdf structures/6ZYR/6zyr_ligand.pdb structures/6ZYR/6zyr_ligand.cif structures/6ZYR/6zyr_complex.pdb structures/6ZYR/6zyr_complex.cif 6ZYS classic IMP-1 Na Na Na 2-Mercaptomethyl-thiazolidine D-syn-1b "[""QST""]" 1 Ki Ki = = 2.0 ± 0.2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition Steady-state inhibition of imipenem hydrolysis by purified IMP-1. 4 Table 1 reports D-syn-1b Ki = 2.0 ± 0.2 µM for IMP-1; text states Ki values were obtained by fitting to a competitive inhibition model. auto_single_measurement only accepted activity measurement [1] 1 structures\6ZYS\6ZYS_metadata.json point structures/6ZYS/6zys_protein.pdb structures/6ZYS/6zys_pocket.pdb structures/6ZYS/6zys_ligand.sdf structures/6ZYS/6zys_ligand.pdb structures/6ZYS/6zys_ligand.cif structures/6ZYS/6zys_complex.pdb structures/6ZYS/6zys_complex.cif 7A00 extended Shank1 PDZ Na SHANK1 PDZ domain L6F (Leu-to-Phe substitution) in the GKAP peptide Ac-Glu-Ala-Gln-Thr-Arg-Phe-CO2H (L6F GKAP peptide) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 5 (±0.5) μM 5000.0 [] unit_conversion 5.301029995663981 success True direct_binding Isothermal titration calorimetry of L6F GKAP peptide binding to SHANK1 PDZ. 4 Fig. 3f prints “L6F GKAP Kd = 5(±0.5) μM”; the caption identifies this as binding of the L6F GKAP peptide to SHANK1 PDZ monitored by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7A00\7A00_metadata.json point structures/7A00/7a00_protein.pdb structures/7A00/7a00_pocket.pdb structures/7A00/7a00_ligand.pdb structures/7A00/7a00_ligand.cif structures/7A00/7a00_complex.pdb structures/7A00/7a00_complex.cif 7A4Q classic CK2alpha Na Na Na RO4613269; RO4613269-000 "[""QY2""]" 1 IC50 IC50 = = 116 nM 116.0 [] unit_conversion 6.935542010773082 success True biochemical_inhibition Recombinant kinase activity assay; table reports activity IC50 for CK2 inhibitors. 19 Extended Data Fig. 6 table reports RO4613269-000 activity IC50 of 116 nM for CSNK2A1; the caption identifies recombinant kinase activity assays. auto_single_measurement only accepted activity measurement [1] 1 structures\7A4Q\7A4Q_metadata.json point structures/7A4Q/7a4q_protein.pdb structures/7A4Q/7a4q_pocket.pdb structures/7A4Q/7a4q_ligand.sdf structures/7A4Q/7a4q_ligand.pdb structures/7A4Q/7a4q_ligand.cif structures/7A4Q/7a4q_complex.pdb structures/7A4Q/7a4q_complex.cif 7A4R classic DYRK1A Na His-Thrombin-DYRK1A(148-479-Ala-Ala) Na compound 1 "[""QY8""]" 1 Ki Ki = = 1.5 µM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter assay; ligand-efficiency-ranked fragment-hit table. 3 Table 1 prints DYRK1A cKi 1.5 µM (LE 0.73) for fragment/compound 1. auto_single_measurement only accepted activity measurement [1] 1 structures\7A4R\7A4R_metadata.json point structures/7A4R/7a4r_protein.pdb structures/7A4R/7a4r_pocket.pdb structures/7A4R/7a4r_ligand.sdf structures/7A4R/7a4r_ligand.pdb structures/7A4R/7a4r_ligand.cif structures/7A4R/7a4r_complex.pdb structures/7A4R/7a4r_complex.cif 7A4S classic DYRK1A Na His-Thrombin-DYRK1A(148-485) Na compound 2 "[""QYE""]" 1 Ki Ki = = 4.4 µM 4400.0 [] unit_conversion 5.356547323513812 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter assay; ligand-efficiency-ranked fragment-hit table. 3 Table 1 prints DYRK1A cKi 4.4 µM (LE 0.67) for fragment/compound 2. auto_single_measurement only accepted activity measurement [1] 1 structures\7A4S\7A4S_metadata.json point structures/7A4S/7a4s_protein.pdb structures/7A4S/7a4s_pocket.pdb structures/7A4S/7a4s_ligand.sdf structures/7A4S/7a4s_ligand.pdb structures/7A4S/7a4s_ligand.cif structures/7A4S/7a4s_complex.pdb structures/7A4S/7a4s_complex.cif 7A4W classic DYRK1A Na His-TEV-DYRK1A(127-485) Na compound 3 "[""QYH""]" 1 Ki Ki = = 0.1 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter assay; ligand-efficiency-ranked fragment-hit table. 3 Table 1 prints DYRK1A cKi 0.1 µM (LE 0.59) for fragment/compound 3. auto_single_measurement only accepted activity measurement [1] 1 structures\7A4W\7A4W_metadata.json point structures/7A4W/7a4w_protein.pdb structures/7A4W/7a4w_pocket.pdb structures/7A4W/7a4w_ligand.sdf structures/7A4W/7a4w_ligand.pdb structures/7A4W/7a4w_ligand.cif structures/7A4W/7a4w_complex.pdb structures/7A4W/7a4w_complex.cif 7A4Z classic DYRK1A Na His-Thrombin-DYRK1A(148-485) Na compound 4 "[""6SD""]" 1 Ki Ki = = 6.1 µM 6100.0 [] unit_conversion 5.214670164989233 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter assay; ligand-efficiency-ranked fragment-hit table. 3 Table 1 prints DYRK1A cKi 6.1 µM (LE 0.51) for fragment/compound 4. auto_single_measurement only accepted activity measurement [1] 1 structures\7A4Z\7A4Z_metadata.json point structures/7A4Z/7a4z_protein.pdb structures/7A4Z/7a4z_pocket.pdb structures/7A4Z/7a4z_ligand.sdf structures/7A4Z/7a4z_ligand.pdb structures/7A4Z/7a4z_ligand.cif structures/7A4Z/7a4z_complex.pdb structures/7A4Z/7a4z_complex.cif 7A51 classic DYRK1A Na His-Thrombin-DYRK1A(148-485) Na compound 5 "[""QYK""]" 2 Ki Ki = = 6.4 µM 6400.0 [] unit_conversion 5.1938200260161125 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter biochemical inhibition assay. 5 Table 2 prints ADP DYRK1A cKi 6.4 µM for compound 5. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7A51\7A51_metadata.json point structures/7A51/7a51_protein.pdb structures/7A51/7a51_pocket.pdb structures/7A51/7a51_ligand.sdf structures/7A51/7a51_ligand.pdb structures/7A51/7a51_ligand.cif structures/7A51/7a51_complex.pdb structures/7A51/7a51_complex.cif 7A52 classic DYRK1A Na His-Thrombin-DYRK1A(148-479-Ala-Ala) Na compound 6 "[""QYB""]" 1 Ki Ki = = 2.3 µM 2300.0 [] unit_conversion 5.638272163982407 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter assay; ligand-efficiency-ranked fragment-hit table. 3 Table 1 prints DYRK1A cKi 2.3 µM (LE 0.48) for fragment/compound 6. auto_single_measurement only accepted activity measurement [1] 1 structures\7A52\7A52_metadata.json point structures/7A52/7a52_protein.pdb structures/7A52/7a52_pocket.pdb structures/7A52/7a52_ligand.sdf structures/7A52/7a52_ligand.pdb structures/7A52/7a52_ligand.cif structures/7A52/7a52_complex.pdb structures/7A52/7a52_complex.cif 7A53 classic DYRK1A Na His-Thrombin-DYRK1A(148-485) Na compound 7 "[""QYZ""]" 1 Ki Ki = = 1.5 µM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter assay; ligand-efficiency-ranked fragment-hit table. 3 Table 1 prints DYRK1A cKi 1.5 µM (LE 0.47) for fragment/compound 7. auto_single_measurement only accepted activity measurement [1] 1 structures\7A53\7A53_metadata.json point structures/7A53/7a53_protein.pdb structures/7A53/7a53_pocket.pdb structures/7A53/7a53_ligand.sdf structures/7A53/7a53_ligand.pdb structures/7A53/7a53_ligand.cif structures/7A53/7a53_complex.pdb structures/7A53/7a53_complex.cif 7A55 classic DYRK1A Na His-TEV-DYRK1A(127-485) Na compound 8 "[""QZ2""]" 1 Ki Ki > > 200 µM 200000.0 [] unit_conversion 3.6989700043360187 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter assay; ligand-efficiency-ranked fragment-hit table. 3 Table 1 prints DYRK1A cKi >200 µM for fragment/compound 8. auto_single_measurement only accepted activity measurement [1] 1 structures\7A55\7A55_metadata.json point structures/7A55/7a55_protein.pdb structures/7A55/7a55_pocket.pdb structures/7A55/7a55_ligand.sdf structures/7A55/7a55_ligand.pdb structures/7A55/7a55_ligand.cif structures/7A55/7a55_complex.pdb structures/7A55/7a55_complex.cif 7A5D classic DYRK1A Na His-Thrombin-DYRK1A(148-485) Na compound 16 "[""QYW""]" 2 Ki Ki = = 0.032 µM 32.0 [] unit_conversion 7.494850021680094 success True biochemical_inhibition Corrected Ki (cKi) from the ADP Hunter biochemical inhibition assay. 5 Table 2 prints ADP DYRK1A cKi 0.032 µM for compound 16. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7A5D\7A5D_metadata.json point structures/7A5D/7a5d_protein.pdb structures/7A5D/7a5d_pocket.pdb structures/7A5D/7a5d_ligand.sdf structures/7A5D/7a5d_ligand.pdb structures/7A5D/7a5d_ligand.cif structures/7A5D/7a5d_complex.pdb structures/7A5D/7a5d_complex.cif 7A5N classic DYRK1A Na His-Thrombin-DYRK1A(148-485) Na compound 34 "[""R05""]" 1 Kd Kd = = 0.24 nM 0.24 [] unit_conversion 9.619788758288394 success True direct_binding DiscoverX KINOMEscan binding assay. 6 The text states that Kd values for compound 34 binding to DYRK1A, DYRK1B, CLK1, CLK2, and CLK4 were 0.24, 0.05, 2.6, 0.9, and 0.8 nM, respectively. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7A5N\7A5N_metadata.json point structures/7A5N/7a5n_protein.pdb structures/7A5N/7a5n_pocket.pdb structures/7A5N/7a5n_ligand.sdf structures/7A5N/7a5n_ligand.pdb structures/7A5N/7a5n_ligand.cif structures/7A5N/7a5n_complex.pdb structures/7A5N/7a5n_complex.cif 7A6R extended 14-3-3 gamma human 14-3-3 gamma DeltaC bound to ctDAPK2-pT369 peptide (RRRSpT369S); DeltaC is C-terminally truncated and lacks the flexible approximately 13-residue tail Na ctDAPK2-pT369 peptide (RRRSpT369S) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:L""]" 1 Kd Kd = = 161 ± 7 nM 161.0 [] unit_conversion 6.79317412396815 success True direct_binding Fluorescence-polarization binding assay of 14-3-3γΔC with FAM-ctDAPK2-pT369 peptide. 3 “14-3-3γΔC binds to FAM-ctDAPK2-pT369 with a binding affinity similar to that of 14-3-3γ (KD = 161 ± 7 nM, Fig. 1b).” auto_single_measurement only accepted activity measurement [1] 1 structures\7A6R\7A6R_metadata.json point structures/7A6R/7a6r_protein.pdb structures/7A6R/7a6r_pocket.pdb structures/7A6R/7a6r_ligand.pdb structures/7A6R/7a6r_ligand.cif structures/7A6R/7a6r_complex.pdb structures/7A6R/7a6r_complex.cif 7A6T classic Deoxyhypusine synthase Homo sapiens Full-length DHS, residues 1-369 Asn173Ser (N173S) Spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 40.96 ± 3.75 µM 40960.0 [] unit_conversion 4.387640052032226 success True direct_binding FRET-based SPD binding assay; N173S value tabulated in Fig. 5h. 8 Fig. 5h reports SPD K_D for DHS N173S as 40.96 ± 3.75 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7A6T\7A6T_metadata.json point structures/7A6T/7a6t_protein.pdb structures/7A6T/7a6t_pocket.pdb structures/7A6T/7a6t_ligand.sdf structures/7A6T/7a6t_ligand.pdb structures/7A6T/7a6t_ligand.cif structures/7A6T/7a6t_complex.pdb structures/7A6T/7a6t_complex.cif 7A6V classic Human Carbonic Anhydrase II Human Na Na Compound 9; 4-(3-(3-phenoxypropyl)thioureido)benzenesulfonamide "[""R2W""]" 1 Ki Ki = = 0.008 ± 0.00003 μM 8.0 [] unit_conversion 8.096910013008056 success True biochemical_inhibition Stopped-flow CO₂ hydrase inhibition assay; Ki values obtained by nonlinear least-squares analysis. 4 Table 1 reports compound 9 against hCA II: Ki = 0.008 ± 0.00003 μM. The text identifies compounds as inhibitors of human carbonic anhydrase isoforms assayed by stopped-flow technique. auto_single_measurement only accepted activity measurement [1] 1 structures\7A6V\7A6V_metadata.json point structures/7A6V/7a6v_protein.pdb structures/7A6V/7a6v_pocket.pdb structures/7A6V/7a6v_ligand.sdf structures/7A6V/7a6v_ligand.pdb structures/7A6V/7a6v_ligand.cif structures/7A6V/7a6v_complex.pdb structures/7A6V/7a6v_complex.cif 7A6Y extended 14-3-3 gamma human 14-3-3 gamma DeltaC bound to ctDAPK2-pT369 peptide (RRRSpT369S) with FC-A; DeltaC is C-terminally truncated and lacks the flexible approximately 13-residue tail Na ctDAPK2-pT369 peptide (RRRSpT369S) "[""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L"", ""CHAIN:M""]" 1 Kd Kd = = 4.4 ± 0.2 nM 4.4 [] unit_conversion 8.356547323513812 success True direct_binding Fluorescence-polarization binding assay of FAM-ctDAPK2-pT369 peptide with 14-3-3γΔC in the presence of FC-A (10 μM). 3 “10 μM FC-A increased the apparent binding affinity of FAM-ctDAPK2-pT369 ~26-fold to a KD of 4.4 ± 0.2 nM (Fig. 1b).” auto_single_measurement only accepted activity measurement [1] 1 structures\7A6Y\7A6Y_metadata.json point structures/7A6Y/7a6y_protein.pdb structures/7A6Y/7a6y_pocket.pdb structures/7A6Y/7a6y_ligand.pdb structures/7A6Y/7a6y_ligand.cif structures/7A6Y/7a6y_complex.pdb structures/7A6Y/7a6y_complex.cif 7A9Z extended cellular retinoic acid-binding protein I (CRABPI) Homo sapiens CRABPI-L29C expressed from a pET28a-hCRABPI-L29C construct; His-tagged L29C DC645 "[""R62""]" 1 Kd Kd = = 1.94 ± 0.11 µM 1940.0 [] unit_conversion 5.7121982700697735 success True direct_binding Competitive displacement of DC271 from purified CRABPI-L29C by DC645; curve fitting by least-squares regression using DynaFit (n = 6, α = 0.05). 8 “CRABPI-L29C interacts less favourably with DC645, with a Kd value of 1.94 ± 0.11 µM being determined for this pair.” auto_single_measurement only accepted activity measurement [1] 1 structures\7A9Z\7A9Z_metadata.json point structures/7A9Z/7a9z_ligand.sdf structures/7A9Z/7a9z_ligand.cif structures/7A9Z/7a9z_complex.cif 7AA1 extended cellular retinoic acid-binding protein II (CRABPII) Na GST-tagged CRABPII expressed from a pGEX4T1-hCRABPII construct Na DC645 "[""R62""]" 1 Kd Kd = = 0.25 ± 0.06 µM 250.0 [] unit_conversion 6.6020599913279625 success True direct_binding Competitive displacement of DC271 from purified CRABPII by DC645; curve fitting by least-squares regression using DynaFit (n = 3). 8 “Using DynaFit to fit the data (Fig. 5b), a Kd value of 0.25 ± 0.06 µM was determined for the binding of DC645 to CRABPII.” auto_single_measurement only accepted activity measurement [1] 1 structures\7AA1\7AA1_metadata.json point structures/7AA1/7aa1_ligand.sdf structures/7AA1/7aa1_ligand.cif structures/7AA1/7aa1_complex.cif 7AA4 extended ClpC1 Mycobacterium smegmatis ClpC1 NTD residues 1-148 with a C-terminal hexahistidine tag Na sCym-1 "[""CHAIN:B""]" 1 Kd Kd = = 0.81 ± 0.05 µM 810.0 [] unit_conversion 6.09151498112135 success True direct_binding ITC measurement of sCym-1 binding to ClpC1 NTD; the co-crystal structure is identified as PDB 7AA4. 7 The text states that sCym-1 has high affinity for ClpC1 NTD (KD = 0.81 µM), and that the co-crystal structure is PDB 7AA4; Figure S4 reports KD = 0.81 ± 0.05 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7AA4\7AA4_metadata.json point structures/7AA4/7aa4_protein.pdb structures/7AA4/7aa4_pocket.pdb structures/7AA4/7aa4_ligand.pdb structures/7AA4/7aa4_ligand.cif structures/7AA4/7aa4_complex.pdb structures/7AA4/7aa4_complex.cif 7AAM extended PSTPIP1 human F-BAR domain, residues 1-289 wild type LYP C-terminal homology (CTH) peptide, residues 787-807, GFANRFSKPKGPRNPPPTWNI "[""CHAIN:C""]" 1 Kd Kd = = 253 ± 21 nM 253.0 [] unit_conversion 6.596879478824182 success True direct_binding Isothermal titration calorimetry of unlabeled LYP-CTH binding to purified PSTPIP1 F-BAR; one-binding-site fit. 11 “ITC ... revealed a N of 0.48 ± 0.02 molecules of LYP-CTH for each PSTPIP1 (Fig. 4D and Table S2). The binding affinity determined by ITC (kd = 253 ± 21 nM) ...” auto_single_measurement only accepted activity measurement [1] 1 structures\7AAM\7AAM_metadata.json point structures/7AAM/7aam_protein.pdb structures/7AAM/7aam_pocket.pdb structures/7AAM/7aam_ligand.pdb structures/7AAM/7aam_ligand.cif structures/7AAM/7aam_complex.pdb structures/7AAM/7aam_complex.cif 7ABT extended PPIA human PPIA expressed from a modified pET28a vector with a TEV-cleaved His tag Na PR20 peptide "[""CHAIN:B""]" 1 Kd Kd = = 23 ± 7 µM 23000.0 [] unit_conversion 4.638272163982407 success True direct_binding NMR signal-broadening titration of PPIA with increasing PR20 concentrations; dissociation constant derived from catalytic-residue Arg55 data. 2 “The dissociation constant 23 ± 7 µM.” auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\7ABT\7ABT_metadata.json point structures/7ABT/7abt_protein.pdb structures/7ABT/7abt_pocket.pdb structures/7ABT/7abt_ligand.pdb structures/7ABT/7abt_ligand.cif structures/7ABT/7abt_complex.pdb structures/7ABT/7abt_complex.cif 7ACK classic CDK2/cyclin A2 Na Thr160-phosphorylated CDK2 with cyclin A2 fragment residues 175-432 Na compound 3b "[""R7B""]" 1 IC50 IC50 = = 0.68 ± 0.05 µM 680.0 [] unit_conversion 6.167491087293763 success True biochemical_inhibition CDK selectivity panel; biochemical CDK/cyclin kinase inhibition assay, measured at least in triplicate. 7 Table 5 reports compound 3b IC50 = 0.68 ± 0.05 µM against CDK2/A2. auto_single_measurement only accepted activity measurement [1] 1 structures\7ACK\7ACK_metadata.json point structures/7ACK/7ack_protein.pdb structures/7ACK/7ack_pocket.pdb structures/7ACK/7ack_ligand.sdf structures/7ACK/7ack_ligand.pdb structures/7ACK/7ack_ligand.cif structures/7ACK/7ack_complex.pdb structures/7ACK/7ack_complex.cif 7AGN classic Human carbonic anhydrase II Human Na Na 11b; 4-(2-aminoethylsulfanyl)-2,3,5,6-tetrafluoro-N-methyl-benzenesulfonamide "[""RAK""]" 1 Kd Kd = = 0.11 µM 110.0 [] unit_conversion 6.958607314841775 success True direct_binding Intrinsic dissociation constant calculated from FTSA observed dissociation constants. 4 Table S2 lists intrinsic Kd,int values for human recombinant CA isoforms; CA II–11b is 0.11 µM. Table S5 maps CA II–11b to PDB 7AGN. auto_single_measurement only accepted activity measurement [1] 1 structures\7AGN\7AGN_metadata.json point structures/7AGN/7agn_protein.pdb structures/7AGN/7agn_pocket.pdb structures/7AGN/7agn_ligand.sdf structures/7AGN/7agn_ligand.pdb structures/7AGN/7agn_ligand.cif structures/7AGN/7agn_complex.pdb structures/7AGN/7agn_complex.cif 7AH0 extended 4D2 Na 112-amino-acid four-helix bundle formed from four 25-residue D2 helices linked by loops Na heme B "[""HEM""]" 1 Kd Kd = = 5.7 ± 2 nM 5.7 [] unit_conversion 8.244125144327509 success True direct_binding Heme B binding isotherm of apo-4D2 (1.5 µM, 20 mM CHES, 100 mM KCl, pH 8.6) versus hemin in DMSO; triplicate data with SD error bars. 3 “4D2 binds two molecules of heme B with high affinity, with an observed dissociation constant (K_D) of <5 nM,” and Fig. 2B prints “K_D = 5.7 ± 2 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7AH0\7AH0_metadata.json point structures/7AH0/7ah0_protein.pdb structures/7AH0/7ah0_pocket.pdb structures/7AH0/7ah0_ligand.pdb structures/7AH0/7ah0_ligand.cif structures/7AH0/7ah0_complex.pdb structures/7AH0/7ah0_complex.cif 7AH8 classic NF-YB/NF-YC heterodimer (NF-Yd) Na Minimal functional NF-Y HFD dimer comprising NF-YB residues 49-141 and NF-YC residues 27-120 Na suramin "[""SVR""]" 1 Kd Kd = = 2.9 ± 0.7 μM 2900.0 [] unit_conversion 5.537602002101044 success True direct_binding Isothermal titration calorimetry of suramin binding to purified NF-Yd; first binding event in the double-dependent-sites model. 8 “The proposed model ... yield[ed] two mean dissociation constants (Kd) values of 2.9 ± 0.7 μM ... for the first (NF-Yd + suramin) ... binding event.” auto_single_measurement only accepted activity measurement [1] 1 structures\7AH8\7AH8_metadata.json point structures/7AH8/7ah8_protein.pdb structures/7AH8/7ah8_pocket.pdb structures/7AH8/7ah8_ligand.sdf structures/7AH8/7ah8_ligand.pdb structures/7AH8/7ah8_ligand.cif structures/7AH8/7ah8_complex.pdb structures/7AH8/7ah8_complex.cif 7AJR extended Pseudomonas aeruginosa elastase B (LasB) Pseudomonas aeruginosa Na Na compound 29 "[""RJB""]" 1 Ki Ki = = 0.16 µM 160.0 [] unit_conversion 6.795880017344075 success True biochemical_inhibition Purified LasB biochemical inhibition; Table 3 reports LasB Ki for regioisomer-B compound 29. 6 Table 3 lists compound (29) with LasB Ki = 0.16 µM. The paper identifies the LasB–29 crystal structure as PDB 7AJR. auto_single_measurement only accepted activity measurement [1] 1 structures\7AJR\7AJR_metadata.json point structures/7AJR/7ajr_ligand.sdf structures/7AJR/7ajr_ligand.cif structures/7AJR/7ajr_complex.cif 7AL2 extended Cell division protein SepF Methanobrevibacter smithii MsSepFcore, residues 54-149 Na FtsZ-CTD (FtsZ_CTD) peptide "[""CHAIN:B""]" 1 Kd Kd = = 84.0 ± 8.5 µM 84000.0 [] unit_conversion 4.075720713938118 success True direct_binding Surface plasmon resonance measurement of the MsSepFcore–MsFtsZCTD peptide interaction. 3 “The apparent Kd value for this interaction is 84.0 ± 8.5 µM as determined by surface plasmon resonance (SPR)”. auto_single_measurement only accepted activity measurement [1] 1 structures\7AL2\7AL2_metadata.json point structures/7AL2/7al2_protein.pdb structures/7AL2/7al2_pocket.pdb structures/7AL2/7al2_ligand.pdb structures/7AL2/7al2_ligand.cif structures/7AL2/7al2_complex.pdb structures/7AL2/7al2_complex.cif 7AMA classic IL-17A human Na Na PPIm 23; compound 23 "[""RMK""]" 1 Kd Kd = = 32 nM 32.0 [] unit_conversion 7.494850021680094 success True direct_binding SPR assay of compound 23 with IL-17A; the paper reports koff and KD. 8 “compound 23 ... showed a koff of 5.7 × 10−5 s−1 in an IL-17A SPR assay (KD = 32 nM).” Pages 8–9 identify compound 23 as bound in PDB 7AMA; page 13 identifies 7AMA as a complex of human IL-17A with compound 23. auto_single_measurement only accepted activity measurement [1] 1 structures\7AMA\7AMA_metadata.json point structures/7AMA/7ama_protein.pdb structures/7AMA/7ama_pocket.pdb structures/7AMA/7ama_ligand.sdf structures/7AMA/7ama_ligand.pdb structures/7AMA/7ama_ligand.cif structures/7AMA/7ama_complex.pdb structures/7AMA/7ama_complex.cif 7AOP classic NUDT15 Na Full-length NUDT15 Na TH8321 "[""RTW""]" 1 IC50 IC50 = = 35 nM 35.0 [] unit_conversion 7.455931955649724 success True biochemical_inhibition Enzyme-coupled malachite green assay of recombinant human NUDT15; Figure 3 reports TH8321 inhibition of NUDT15 dGTPase activity. 6 Figure 3A visibly prints “TH8321 IC50 35 nM”; its legend states that TH8321 potently inhibited the dGTPase activity of NUDT15 using the enzyme-coupled MG assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7AOP\7AOP_metadata.json point structures/7AOP/7aop_protein.pdb structures/7AOP/7aop_pocket.pdb structures/7AOP/7aop_ligand.sdf structures/7AOP/7aop_ligand.pdb structures/7AOP/7aop_ligand.cif structures/7AOP/7aop_complex.pdb structures/7AOP/7aop_complex.cif 7APU classic adenylate kinase (AdK) Escherichia coli Na Na ADP;ADP "[""ADP""]" 1 Kd Kd = = 9 µM 9000.0 [] unit_conversion 5.045757490560675 success True direct_binding Isothermal calorimetry of ADP binding to AdK; the data fit a single Kd, suggesting the two ADP molecules bind the two sites with the same affinity. 6 “Here, binding of ADP to AdK is quantified via isothermal titration calorimetry ... The data can be fitted well with a single Kd value of 9 µM, suggesting that the two ADP molecules bind with the same binding affinity for the two binding sites.” auto_single_measurement only accepted activity measurement [1] 1 structures\7APU\7APU_metadata.json point structures/7APU/7apu_protein.pdb structures/7APU/7apu_pocket.pdb structures/7APU/7apu_ligand.sdf structures/7APU/7apu_ligand.pdb structures/7APU/7apu_ligand.cif structures/7APU/7apu_complex.pdb structures/7APU/7apu_complex.cif 7AS0 classic Influenza A virus polymerase basic protein 2 (PB2) Influenza A virus (A/California/07/2009) PB2 cap-binding domain residues 318-483; expressed as His6-SUMO-PB2 fusion with tag cleaved before crystallization wild-type VX-787 (pimodivir) "[""21G""]" 1 Kd Kd = = 2.2 ± 0.5 nM 2.2 [] unit_conversion 8.657577319177793 success True direct_binding Isothermal titration calorimetry; 20 mM PIPES (or Tris-HCl), pH 7.5, 150 mM NaCl, 1% DMSO, 25 °C; Table 1 reports mean ± s.d. of two independent experiments. 4 Table 1 reports pimodivir binding to PB2 wild-type with Kd 2.2 ± 0.5 nM; Table 4 maps PB2-WT to PDB 7AS0. auto_single_measurement only accepted activity measurement [1] 1 structures\7AS0\7AS0_metadata.json point structures/7AS0/7as0_protein.pdb structures/7AS0/7as0_pocket.pdb structures/7AS0/7as0_ligand.sdf structures/7AS0/7as0_ligand.pdb structures/7AS0/7as0_ligand.cif structures/7AS0/7as0_complex.pdb structures/7AS0/7as0_complex.cif 7AS1 classic Influenza A virus polymerase basic protein 2 (PB2) Influenza A virus (A/California/07/2009) PB2 cap-binding domain residues 318-483; expressed as His6-SUMO-PB2 fusion with tag cleaved before crystallization F404Y VX-787 (pimodivir) "[""21G""]" 1 Kd Kd = = 610 ± 100 nM 610.0 [] unit_conversion 6.214670164989233 success True direct_binding Isothermal titration calorimetry; 20 mM PIPES (or Tris-HCl), pH 7.5, 150 mM NaCl, 1% DMSO, 25 °C; Table 1 reports mean ± s.d. of two independent experiments. 4 Table 1 reports pimodivir binding to PB2-F404Y with Kd 610 ± 100 nM; Table 4 maps PB2-F404Y to PDB 7AS1. auto_single_measurement only accepted activity measurement [1] 1 structures\7AS1\7AS1_metadata.json point structures/7AS1/7as1_protein.pdb structures/7AS1/7as1_pocket.pdb structures/7AS1/7as1_ligand.sdf structures/7AS1/7as1_ligand.pdb structures/7AS1/7as1_ligand.cif structures/7AS1/7as1_complex.pdb structures/7AS1/7as1_complex.cif 7AS2 classic Influenza A virus polymerase basic protein 2 (PB2) Influenza A virus (A/California/07/2009) PB2 cap-binding domain residues 318-483; expressed as His6-SUMO-PB2 fusion with tag cleaved before crystallization M431I VX-787 (pimodivir) "[""21G""]" 1 Kd Kd = = 14 ± 1 nM 14.0 [] unit_conversion 7.853871964321762 success True direct_binding Isothermal titration calorimetry; 20 mM PIPES (or Tris-HCl), pH 7.5, 150 mM NaCl, 1% DMSO, 25 °C; Table 1 reports mean ± s.d. of two independent experiments. 4 Table 1 reports pimodivir binding to PB2-M431I with Kd 14 ± 1 nM; Table 4 maps PB2-M431I to PDB 7AS2. auto_single_measurement only accepted activity measurement [1] 1 structures\7AS2\7AS2_metadata.json point structures/7AS2/7as2_protein.pdb structures/7AS2/7as2_pocket.pdb structures/7AS2/7as2_ligand.sdf structures/7AS2/7as2_ligand.pdb structures/7AS2/7as2_ligand.cif structures/7AS2/7as2_complex.pdb structures/7AS2/7as2_complex.cif 7AS3 classic Influenza A virus polymerase basic protein 2 (PB2) Influenza A virus (A/California/07/2009) PB2 cap-binding domain residues 318-483; expressed as His6-SUMO-PB2 fusion with tag cleaved before crystallization H357N VX-787 (pimodivir) "[""21G""]" 1 Kd Kd = = 290 ± 20 nM 290.0 [] unit_conversion 6.537602002101044 success True direct_binding Isothermal titration calorimetry; 20 mM PIPES (or Tris-HCl), pH 7.5, 150 mM NaCl, 1% DMSO, 25 °C; Table 1 reports mean ± s.d. of two independent experiments. 4 Table 1 reports pimodivir binding to PB2-H357N with Kd 290 ± 20 nM; Table 4 maps PB2-H357N to PDB 7AS3. auto_single_measurement only accepted activity measurement [1] 1 structures\7AS3\7AS3_metadata.json point structures/7AS3/7as3_protein.pdb structures/7AS3/7as3_pocket.pdb structures/7AS3/7as3_ligand.sdf structures/7AS3/7as3_ligand.pdb structures/7AS3/7as3_ligand.cif structures/7AS3/7as3_complex.pdb structures/7AS3/7as3_complex.cif 7ASJ classic human carbonic anhydrase II human Na Na 11f; 3-(3-methyl-3-phenethylureido)benzenesulfonamide "[""RWH""]" 1 Ki Ki = = 489.5 nM 489.5 [] unit_conversion 6.3102473038608435 success True biochemical_inhibition Stopped-flow CO2 hydrase assay. 4 Table 1 reports compound 11f with a Ki of 489.5 nM against hCA II. Figure 2 maps 11f to PDB 7ASJ; the isolated page-11 accession/ligand inconsistency is resolved by the supplied sibling mapping. auto_single_measurement only accepted activity measurement [1] 1 structures\7ASJ\7ASJ_metadata.json point structures/7ASJ/7asj_protein.pdb structures/7ASJ/7asj_pocket.pdb structures/7ASJ/7asj_ligand.sdf structures/7ASJ/7asj_ligand.pdb structures/7ASJ/7asj_ligand.cif structures/7ASJ/7asj_complex.pdb structures/7ASJ/7asj_complex.cif 7AU4 classic SARS-CoV-2 main protease (Nsp5) SARS-CoV-2 Residues S1-Q306; N-terminal GST tag followed by an Mpro recognition sequence; C-terminal 6x His tag preceded by an HRV Mpro recognition sequence Na compound 3 "[""RY5""]" 1 Kd Kd = = 61 ± 5 μM 61000.0 [] unit_conversion 4.214670164989233 success True direct_binding SPR biosensor assay of purified Mpro; Table 1 reports Kd values. 4 Table 1 maps compound 3 to PDB 7AU4 and reports Kd = 61 ± 5 μM; the footnote states Kd values were determined by SPR biosensor analysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7AU4\7AU4_metadata.json point structures/7AU4/7au4_protein.pdb structures/7AU4/7au4_pocket.pdb structures/7AU4/7au4_ligand.sdf structures/7AU4/7au4_ligand.pdb structures/7AU4/7au4_ligand.cif structures/7AU4/7au4_complex.pdb structures/7AU4/7au4_complex.cif 7AUZ classic leukotriene A4 hydrolase (LTA4H) Na Na Na LYS006; (S)-22 "[""RZE""]" 2 IC50 IC50 = = 0.12 ± 0.01 nM 0.12 [] unit_conversion 9.920818753952375 success True biochemical_inhibition Biochemical LTA4H inhibition assay at reduced enzyme concentration; Table 4 reports the exact biochemical potency. 6 The text states that LYS006 “delivered a remarkable biochemical IC50 of 0.12 ± 0.01 nM (Table 4),” and Table 4 lists biochemical IC50 0.12 ± 0.01 nM for LYS006. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\7AUZ\7AUZ_metadata.json point structures/7AUZ/7auz_protein.pdb structures/7AUZ/7auz_pocket.pdb structures/7AUZ/7auz_ligand.sdf structures/7AUZ/7auz_ligand.pdb structures/7AUZ/7auz_ligand.cif structures/7AUZ/7auz_complex.pdb structures/7AUZ/7auz_complex.cif 7AV0 classic leukotriene A4 hydrolase (LTA4H) Na Na Na R(13); (R)-13 "[""RZB""]" 1 IC50 IC50 < < 3.0 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition LTA4H enzyme inhibition assay using Arg-AMC substrate. 4 Table 2, “Head Group Modifications,” reports LTA4H IC50 <3.0 nM for (R)-13; the table footnote defines the LTA4H enzyme inhibition assay using Arg-AMC. auto_single_measurement only accepted activity measurement [1] 1 structures\7AV0\7AV0_metadata.json point structures/7AV0/7av0_protein.pdb structures/7AV0/7av0_pocket.pdb structures/7AV0/7av0_ligand.sdf structures/7AV0/7av0_ligand.pdb structures/7AV0/7av0_ligand.cif structures/7AV0/7av0_complex.pdb structures/7AV0/7av0_complex.cif 7AV1 classic leukotriene A4 hydrolase (LTA4H) Na Na Na fragment2; fragment 2 "[""RZK""]" 1 IC50 IC50 = = 8.8 μM 8800.0 [] unit_conversion 5.055517327849831 success True biochemical_inhibition Biochemical peptide assay; fragment 2 inhibition was characterized as measurable but weak. 3 The text states that fragment 2 showed weak inhibition in the biochemical peptide assay with IC50 8.8 μM; Table 1 also lists compound 2 biochemical IC50 = 8.8 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7AV1\7AV1_metadata.json point structures/7AV1/7av1_protein.pdb structures/7AV1/7av1_pocket.pdb structures/7AV1/7av1_ligand.sdf structures/7AV1/7av1_ligand.pdb structures/7AV1/7av1_ligand.cif structures/7AV1/7av1_complex.pdb structures/7AV1/7av1_complex.cif 7AV2 classic leukotriene A4 hydrolase (LTA4H) Na Na Na fragment1; fragment 1 "[""RZN""]" 1 IC50 IC50 = = 4.5 μM 4500.0 [] unit_conversion 5.346787486224656 success True biochemical_inhibition Biochemical peptide assay; fragment 1 inhibition was characterized as measurable but weak. 3 The text states that fragment 1 showed weak inhibition in the biochemical peptide assay with IC50 4.5 μM; Table 1 also lists compound 1 biochemical IC50 = 4.5 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7AV2\7AV2_metadata.json point structures/7AV2/7av2_protein.pdb structures/7AV2/7av2_pocket.pdb structures/7AV2/7av2_ligand.sdf structures/7AV2/7av2_ligand.pdb structures/7AV2/7av2_ligand.cif structures/7AV2/7av2_complex.pdb structures/7AV2/7av2_complex.cif 7AVA classic FAST Na Na Na N871b "[""S1Q""]" 1 Kd Kd = = 0.25 µM 250.0 [] unit_conversion 6.6020599913279625 success True direct_binding Table 1 reports the dissociation constant for the FAST:N871b fluorogen complex. 2 Table 1 lists FAST:N871b with Kd = 0.25 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVA\7AVA_metadata.json point structures/7AVA/7ava_protein.pdb structures/7AVA/7ava_pocket.pdb structures/7AVA/7ava_ligand.sdf structures/7AVA/7ava_ligand.pdb structures/7AVA/7ava_ligand.cif structures/7AVA/7ava_complex.pdb structures/7AVA/7ava_complex.cif 7AVI classic SOS1 Na Na Na compound 2 "[""S2Q""]" 1 Kd Kd = = 937 ± 476 nM 937.0 [] unit_conversion 6.028260409112222 success True direct_binding SPR biophysical assay 2 Table 1 reports SOS1 KD (SPR) 937 ± 476 nM for compound 2. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVI\7AVI_metadata.json point structures/7AVI/7avi_protein.pdb structures/7AVI/7avi_pocket.pdb structures/7AVI/7avi_ligand.sdf structures/7AVI/7avi_ligand.pdb structures/7AVI/7avi_ligand.cif structures/7AVI/7avi_complex.pdb structures/7AVI/7avi_complex.cif 7AVL classic SOS1 Na Na Na compound 4 "[""S2Z""]" 1 Kd Kd = = 469 ± 26 nM 469.0 [] unit_conversion 6.328827157284916 success True direct_binding SPR biophysical assay 5 Table 2 reports SOS1 KD (SPR) 469 ± 26 nM for compound 4. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVL\7AVL_metadata.json point structures/7AVL/7avl_protein.pdb structures/7AVL/7avl_pocket.pdb structures/7AVL/7avl_ligand.sdf structures/7AVL/7avl_ligand.pdb structures/7AVL/7avl_ligand.cif structures/7AVL/7avl_complex.pdb structures/7AVL/7avl_complex.cif 7AVS classic SOS1 Na Na Na compound 6 "[""S3Q""]" 1 Kd Kd = = 104 ± 5 nM 104.0 [] unit_conversion 6.982966660701219 success True direct_binding SPR biophysical assay 5 Table 2 reports SOS1 KD (SPR) 104 ± 5 nM for compound 6. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVS\7AVS_metadata.json point structures/7AVS/7avs_protein.pdb structures/7AVS/7avs_pocket.pdb structures/7AVS/7avs_ligand.sdf structures/7AVS/7avs_ligand.pdb structures/7AVS/7avs_ligand.cif structures/7AVS/7avs_complex.pdb structures/7AVS/7avs_complex.cif 7AVT classic SOS1 Na Na Na compound 7 "[""S3T""]" 1 Kd Kd = = 123 ± 12 nM 123.0 [] unit_conversion 6.910094888560602 success True direct_binding SPR biophysical assay 5 Table 2 reports SOS1 KD (SPR) 123 ± 12 nM for compound 7. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVT\7AVT_metadata.json point structures/7AVT/7avt_protein.pdb structures/7AVT/7avt_pocket.pdb structures/7AVT/7avt_ligand.sdf structures/7AVT/7avt_ligand.pdb structures/7AVT/7avt_ligand.cif structures/7AVT/7avt_complex.pdb structures/7AVT/7avt_complex.cif 7AVU classic SOS1 Na Na Na compound 8 "[""S3Z""]" 1 Kd Kd = = 16 ± 2 nM 16.0 [] unit_conversion 7.795880017344075 success True direct_binding SPR biophysical assay 5 Table 2 reports SOS1 KD (SPR) 16 ± 2 nM for compound 8. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVU\7AVU_metadata.json point structures/7AVU/7avu_protein.pdb structures/7AVU/7avu_pocket.pdb structures/7AVU/7avu_ligand.sdf structures/7AVU/7avu_ligand.pdb structures/7AVU/7avu_ligand.cif structures/7AVU/7avu_complex.pdb structures/7AVU/7avu_complex.cif 7AVV classic SOS1 Na Na Na compound 9 "[""S2W""]" 1 Kd Kd = = 350 ± 32 nM 350.0 [] unit_conversion 6.455931955649724 success True direct_binding SPR biophysical assay 7 Table 3 reports SOS1 KD (SPR) 350 ± 32 nM for compound 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVV\7AVV_metadata.json point structures/7AVV/7avv_protein.pdb structures/7AVV/7avv_pocket.pdb structures/7AVV/7avv_ligand.sdf structures/7AVV/7avv_ligand.pdb structures/7AVV/7avv_ligand.cif structures/7AVV/7avv_complex.pdb structures/7AVV/7avv_complex.cif 7AVX classic MerTK Na Na Na NPS-1034 (compound 1) "[""S4K""]" 1 pIC50 IC50 = = 8.8 1.584893192461111 [] p_metric_transform 8.8 success True biochemical_inhibition Mer biochemical activity assay; Table 1 reports Mer pIC50. 3 Table 1 lists compound 1 with Mer pIC50 8.8; Figure 2 maps compound 1 to PDB 7AVX. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVX\7AVX_metadata.json point structures/7AVX/7avx_protein.pdb structures/7AVX/7avx_pocket.pdb structures/7AVX/7avx_ligand.sdf structures/7AVX/7avx_ligand.pdb structures/7AVX/7avx_ligand.cif structures/7AVX/7avx_complex.pdb structures/7AVX/7avx_complex.cif 7AVY classic MerTK Na Na Na compound 2 (quinazoline-based inhibitor) "[""S4E""]" 1 pIC50 IC50 = = 6.6 251.18864315095823 [] p_metric_transform 6.6 success True biochemical_inhibition Mer biochemical activity assay; Table 1 reports Mer pIC50. 3 Table 1 lists compound 2 with Mer pIC50 6.6; Figure 2 maps compound 2 to PDB 7AVY. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVY\7AVY_metadata.json point structures/7AVY/7avy_protein.pdb structures/7AVY/7avy_pocket.pdb structures/7AVY/7avy_ligand.sdf structures/7AVY/7avy_ligand.pdb structures/7AVY/7avy_ligand.cif structures/7AVY/7avy_complex.pdb structures/7AVY/7avy_complex.cif 7AVZ classic MerTK Na Na Na compound 5 (bisaminopyrimidine inhibitor) "[""S4N""]" 1 pIC50 IC50 = = 7.3 50.11872336272725 [] p_metric_transform 7.3 success True biochemical_inhibition Mer biochemical activity assay; Table 3 reports Mer pIC50. 6 Table 3 lists compound 5 with Mer pIC50 7.3; Figure 4 maps compound 5 to PDB 7AVZ. auto_single_measurement only accepted activity measurement [1] 1 structures\7AVZ\7AVZ_metadata.json point structures/7AVZ/7avz_protein.pdb structures/7AVZ/7avz_pocket.pdb structures/7AVZ/7avz_ligand.sdf structures/7AVZ/7avz_ligand.pdb structures/7AVZ/7avz_ligand.cif structures/7AVZ/7avz_complex.pdb structures/7AVZ/7avz_complex.cif 7AW0 classic MerTK Na Na Na compound 9 (purine inhibitor) "[""S4Q""]" 1 pIC50 IC50 = = 6.9 125.89254117941663 [] p_metric_transform 6.9 success True biochemical_inhibition Mer biochemical activity assay; Table 4 reports Mer pIC50. 6 Table 4 lists compound 9 with Mer pIC50 6.9; Figure 4 maps compound 9 to PDB 7AW0. auto_single_measurement only accepted activity measurement [1] 1 structures\7AW0\7AW0_metadata.json point structures/7AW0/7aw0_protein.pdb structures/7AW0/7aw0_pocket.pdb structures/7AW0/7aw0_ligand.sdf structures/7AW0/7aw0_ligand.pdb structures/7AW0/7aw0_ligand.cif structures/7AW0/7aw0_complex.pdb structures/7AW0/7aw0_complex.cif 7AW1 classic MerTK Na Na Na compound 11 (type-II inhibitor) "[""S4T""]" 1 pIC50 IC50 = = 8.2 6.309573444801943 [] p_metric_transform 8.2 success True biochemical_inhibition Mer biochemical activity assay; Table 5 reports Mer pIC50. 7 Table 5 lists compound 11 with Mer pIC50 8.2; Figure 5 maps compound 11 to PDB 7AW1. auto_single_measurement only accepted activity measurement [1] 1 structures\7AW1\7AW1_metadata.json point structures/7AW1/7aw1_protein.pdb structures/7AW1/7aw1_pocket.pdb structures/7AW1/7aw1_ligand.sdf structures/7AW1/7aw1_ligand.pdb structures/7AW1/7aw1_ligand.cif structures/7AW1/7aw1_complex.pdb structures/7AW1/7aw1_complex.cif 7AW2 classic MerTK Na Na Na compound 14 (oxadiazole inhibitor) "[""S4W""]" 1 pIC50 IC50 = = 8.3 5.011872336272715 [] p_metric_transform 8.3 success True biochemical_inhibition Mer biochemical activity assay; Table 6 reports Mer pIC50. 8 Table 6 lists compound 14 with Mer pIC50 8.3; Figure 8 maps compound 14 to PDB 7AW2. auto_single_measurement only accepted activity measurement [1] 1 structures\7AW2\7AW2_metadata.json point structures/7AW2/7aw2_protein.pdb structures/7AW2/7aw2_pocket.pdb structures/7AW2/7aw2_ligand.sdf structures/7AW2/7aw2_ligand.pdb structures/7AW2/7aw2_ligand.cif structures/7AW2/7aw2_complex.pdb structures/7AW2/7aw2_complex.cif 7AW3 classic MerTK Na Na Na compound 12 (azaindole inhibitor) "[""S4Z""]" 1 pIC50 IC50 = = 7.6 25.11886431509582 [] p_metric_transform 7.6 success True biochemical_inhibition Mer biochemical activity assay; Table 6 reports Mer pIC50. 8 Table 6 lists compound 12 with Mer pIC50 7.6; Figure 6 maps compound 12 to PDB 7AW3. auto_single_measurement only accepted activity measurement [1] 1 structures\7AW3\7AW3_metadata.json point structures/7AW3/7aw3_protein.pdb structures/7AW3/7aw3_pocket.pdb structures/7AW3/7aw3_ligand.sdf structures/7AW3/7aw3_ligand.pdb structures/7AW3/7aw3_ligand.cif structures/7AW3/7aw3_complex.pdb structures/7AW3/7aw3_complex.cif 7AW4 classic MerTK Na Na Na compound 13 (DNA-encoded-library inhibitor) "[""S5E""]" 1 pIC50 IC50 = = 8.3 5.011872336272715 [] p_metric_transform 8.3 success True biochemical_inhibition Mer biochemical activity assay; Table 6 reports Mer pIC50. 8 Table 6 lists compound 13 with Mer pIC50 8.3; Figure 7 maps compound 13 to PDB 7AW4. auto_single_measurement only accepted activity measurement [1] 1 structures\7AW4\7AW4_metadata.json point structures/7AW4/7aw4_protein.pdb structures/7AW4/7aw4_pocket.pdb structures/7AW4/7aw4_ligand.sdf structures/7AW4/7aw4_ligand.pdb structures/7AW4/7aw4_ligand.cif structures/7AW4/7aw4_complex.pdb structures/7AW4/7aw4_complex.cif 7AWM classic EAAT1 (excitatory amino acid transporter 1) Human Thermostabilized EAAT1CRYST Na L-ASP; UCPH101 "[""ASP""]" 1 Kd Kd = = 0.9 ± 0.1 mM 900000.0 [] unit_conversion 3.045757490560675 success True direct_binding Intrinsic-tryptophan fluorescence transmitter-binding determination in the presence of UCPH101. 2 “transmitter KD values in the presence (0.9 ± 0.1 mM) ... of UCPH101”. auto_single_measurement only accepted activity measurement [1] 1 structures\7AWM\7AWM_metadata.json point structures/7AWM/7awm_protein.pdb structures/7AWM/7awm_pocket.pdb structures/7AWM/7awm_ligand.sdf structures/7AWM/7awm_ligand.pdb structures/7AWM/7awm_ligand.cif structures/7AWM/7awm_complex.pdb structures/7AWM/7awm_complex.cif 7AY6 classic PDE4D Na PDE4D catalytic domain, amino acids 244-578, with a C-terminal 6His-tag Na GEBR-41b; compound 1b "[""S8Q""]" 1 IC50 IC50 = = 2.5 ± 0.2 µM 2500.0 [] unit_conversion 5.6020599913279625 success True biochemical_inhibition NADH-coupled biochemical inhibition assay against purified PDE4D catalytic domain. 6 Table 2 reports compound 1b IC50 = 2.5 ± 0.2 µM against PDE4D Cat; Figure 6 identifies the crystallized 7AY6 ligand as GEBR-41b/1b. auto_single_measurement only accepted activity measurement [1] 1 structures\7AY6\7AY6_metadata.json point structures/7AY6/7ay6_protein.pdb structures/7AY6/7ay6_pocket.pdb structures/7AY6/7ay6_ligand.sdf structures/7AY6/7ay6_ligand.pdb structures/7AY6/7ay6_ligand.cif structures/7AY6/7ay6_complex.pdb structures/7AY6/7ay6_complex.cif 7AYH classic Aurora A Na recombinant kinase domain Na compound 2c "[""S9H""]" 1 IC50 IC50 = = 1.8 µM 1800.0 [] unit_conversion 5.7447274948966935 success True biochemical_inhibition Radiometric 33P-Panginase protein-kinase inhibition assay using recombinant kinases; Table 3 reports the compound series against Aurora A. 7 Table 3 lists compound 2c (R = 4-OCH3) with Aurora A IC50 = 1.8 µM. The paper’s Table 1 maps PDB 7AYH to Aurora A complexed with 2c. auto_single_measurement only accepted activity measurement [1] 1 structures\7AYH\7AYH_metadata.json point structures/7AYH/7ayh_protein.pdb structures/7AYH/7ayh_pocket.pdb structures/7AYH/7ayh_ligand.sdf structures/7AYH/7ayh_ligand.pdb structures/7AYH/7ayh_ligand.cif structures/7AYH/7ayh_complex.pdb structures/7AYH/7ayh_complex.cif 7AYI classic Aurora A Na recombinant kinase domain Na compound 2a "[""S9K""]" 1 IC50 IC50 = = 2.4 µM 2400.0 [] unit_conversion 5.619788758288394 success True biochemical_inhibition Radiometric 33P-Panginase protein-kinase inhibition assay using recombinant kinases; Table 3 reports the compound series against Aurora A. 7 Table 3 lists compound 2a (R = H) with Aurora A IC50 = 2.4 µM. The paper’s Table 1 maps PDB 7AYI to Aurora A complexed with 2a. auto_single_measurement only accepted activity measurement [1] 1 structures\7AYI\7AYI_metadata.json point structures/7AYI/7ayi_protein.pdb structures/7AYI/7ayi_pocket.pdb structures/7AYI/7ayi_ligand.sdf structures/7AYI/7ayi_ligand.pdb structures/7AYI/7ayi_ligand.cif structures/7AYI/7ayi_complex.pdb structures/7AYI/7ayi_complex.cif 7AYJ classic VIM-1 Na Na Na compound 6 (NSPC sulfamoyl inhibitor) "[""S9N""]" 1 pIC50 IC50 = = 6.9 125.89254117941663 [] p_metric_transform 6.9 success True biochemical_inhibition Fluorogenic assay against clinically relevant B1 MBLs; Table 1 reports pIC50 values (pIC50 = −log10 IC50), repeated in quadruplicate. 3 Table 1 lists compound 6a (compound 6) pIC50 = 6.9 against VIM-1. The text states NSPCs were screened against VIM-1 using a fluorogenic assay. Figure 2 identifies VIM-1:Zn2:6 as PDB 7AYJ. auto_single_measurement only accepted activity measurement [1] 1 structures\7AYJ\7AYJ_metadata.json point structures/7AYJ/7ayj_protein.pdb structures/7AYJ/7ayj_pocket.pdb structures/7AYJ/7ayj_ligand.sdf structures/7AYJ/7ayj_ligand.pdb structures/7AYJ/7ayj_ligand.cif structures/7AYJ/7ayj_complex.pdb structures/7AYJ/7ayj_complex.cif 7AZ6 extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 36 "[""CHAIN:H""]" 1 Kd Kd = = 278 (± 44) nM 278.0 [] unit_conversion 6.555955204081924 success True direct_binding ITC at 25 °C; Table 4. 7 Table 4 reports Kd 278 (±44) nM for compound/peptide 36; Figure 4 assigns peptide 36 to PDB 7AZ6. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZ6\7AZ6_metadata.json point structures/7AZ6/7az6_protein.pdb structures/7AZ6/7az6_pocket.pdb structures/7AZ6/7az6_ligand.pdb structures/7AZ6/7az6_ligand.cif structures/7AZ6/7az6_complex.pdb structures/7AZ6/7az6_complex.cif 7AZ7 extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 37 "[""CHAIN:H""]" 1 Kd Kd = = 92 (± 44) nM 92.0 [] unit_conversion 7.036212172654444 success True direct_binding ITC at 25 °C; Table 4. 7 Table 4 reports Kd 92 (±44) nM for compound/peptide 37; Figure 4 assigns peptide 37 to PDB 7AZ7. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZ7\7AZ7_metadata.json point structures/7AZ7/7az7_protein.pdb structures/7AZ7/7az7_pocket.pdb structures/7AZ7/7az7_ligand.pdb structures/7AZ7/7az7_ligand.cif structures/7AZ7/7az7_complex.pdb structures/7AZ7/7az7_complex.cif 7AZ8 extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 43 "[""CHAIN:H"", ""CHAIN:I""]" 1 Kd Kd = = 132 (± 44) nM 132.0 [] unit_conversion 6.8794260687941495 success True direct_binding ITC at 25 °C; Table 4. 7 Table 4 reports Kd 132 (±44) nM for compound/peptide 43; Figure 5 assigns peptide 43 to PDB 7AZ8. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZ8\7AZ8_metadata.json point structures/7AZ8/7az8_protein.pdb structures/7AZ8/7az8_pocket.pdb structures/7AZ8/7az8_ligand.pdb structures/7AZ8/7az8_ligand.cif structures/7AZ8/7az8_complex.pdb structures/7AZ8/7az8_complex.cif 7AZC extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 22 "[""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K""]" 1 Kd Kd = = 73 (± 24) nM 73.0 [] unit_conversion 7.136677139879544 success True direct_binding ITC at 25 °C; Table 2. 4 Table 2 reports Kd 73 (±24) nM for compound/peptide 22; Figure 3 assigns peptide 22 to PDB 7AZC. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZC\7AZC_metadata.json point structures/7AZC/7azc_protein.pdb structures/7AZC/7azc_pocket.pdb structures/7AZC/7azc_ligand.pdb structures/7AZC/7azc_ligand.cif structures/7AZC/7azc_complex.pdb structures/7AZC/7azc_complex.cif 7AZD extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 20 "[""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K""]" 1 Kd Kd = = 89 (± 21) nM 89.0 [] unit_conversion 7.050609993355087 success True direct_binding ITC at 25 °C; Table 2. 4 Table 2 reports Kd 89 (±21) nM for compound/peptide 20; Figure 3 assigns peptide 20 to PDB 7AZD. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZD\7AZD_metadata.json point structures/7AZD/7azd_protein.pdb structures/7AZD/7azd_pocket.pdb structures/7AZD/7azd_ligand.pdb structures/7AZD/7azd_ligand.cif structures/7AZD/7azd_complex.pdb structures/7AZD/7azd_complex.cif 7AZE extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 18 "[""CHAIN:H"", ""CHAIN:I""]" 1 Kd Kd = = 144 (± 38) nM 144.0 [] unit_conversion 6.84163750790475 success True direct_binding ITC at 25 °C; Table 2. 4 Table 2 reports Kd 144 (±38) nM for compound/peptide 18; Figure 3 assigns peptide 18 to PDB 7AZE. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZE\7AZE_metadata.json point structures/7AZE/7aze_protein.pdb structures/7AZE/7aze_pocket.pdb structures/7AZE/7aze_ligand.pdb structures/7AZE/7aze_ligand.cif structures/7AZE/7aze_complex.pdb structures/7AZE/7aze_complex.cif 7AZF extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 8 "[""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K""]" 1 Kd Kd = = 172 (± 29) nM 172.0 [] unit_conversion 6.764471553092451 success True direct_binding ITC at 25 °C; Table 2. 4 Table 2 reports Kd 172 (±29) nM for compound/peptide 8; Figure 3 assigns peptide 8 to PDB 7AZF. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZF\7AZF_metadata.json point structures/7AZF/7azf_protein.pdb structures/7AZF/7azf_pocket.pdb structures/7AZF/7azf_ligand.pdb structures/7AZF/7azf_ligand.cif structures/7AZF/7azf_complex.pdb structures/7AZF/7azf_complex.cif 7AZG extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 4 "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L"", ""CHAIN:M"", ""CHAIN:N"", ""CHAIN:O"", ""CHAIN:P""]" 1 Kd Kd = = 114 (± 31) nM 114.0 [] unit_conversion 6.943095148663527 success True direct_binding ITC at 298.15 K; Table 1. 2 Table 1 reports Kd 114 (±31) nM for compound/peptide 4; Figure 2 assigns peptide 4 to PDB 7AZG. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZG\7AZG_metadata.json point structures/7AZG/7azg_protein.pdb structures/7AZG/7azg_pocket.pdb structures/7AZG/7azg_ligand.pdb structures/7AZG/7azg_ligand.cif structures/7AZG/7azg_complex.pdb structures/7AZG/7azg_complex.cif 7AZK extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 35 "[""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K""]" 1 Kd Kd = = 41 (± 26) nM 41.0 [] unit_conversion 7.3872161432802645 success True direct_binding ITC at 25 °C; Table 4. 7 Table 4 reports Kd 41 (±26) nM for compound/peptide 35; the Notes identify PDB 7AZK as peptide 35. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZK\7AZK_metadata.json point structures/7AZK/7azk_protein.pdb structures/7AZK/7azk_pocket.pdb structures/7AZK/7azk_ligand.pdb structures/7AZK/7azk_ligand.cif structures/7AZK/7azk_complex.pdb structures/7AZK/7azk_complex.cif 7AZL extended DNA polymerase sliding clamp Escherichia coli Na Na peptide 38 "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 Kd Kd = = 46 (± 30) nM 46.0 [] unit_conversion 7.337242168318426 success True direct_binding ITC at 25 °C; Table 4. 7 Table 4 reports Kd 46 (±30) nM for compound/peptide 38; the Notes identify PDB 7AZL as peptide 38. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZL\7AZL_metadata.json point structures/7AZL/7azl_protein.pdb structures/7AZL/7azl_pocket.pdb structures/7AZL/7azl_ligand.pdb structures/7AZL/7azl_ligand.cif structures/7AZL/7azl_complex.pdb structures/7AZL/7azl_complex.cif 7AZN classic Aster-C (GramD1c) mouse Aster-C residues 296-517 Na AI-1l "[""YK8""]" 1 IC50 IC50 = = 0.85 µM 850.0 [] unit_conversion 6.070581074285707 success True direct_binding Purified Aster-C296-517 competition binding assay with 22-NBD-cholesterol; dose-response curve for AI-1l. 5 Fig. 3E explicitly reports “Aster-C IC50: 0.85 µM” for AI-1l; the caption states this value was measured for 1l binding to Aster-C296-517. auto_single_measurement only accepted activity measurement [1] 1 structures\7AZN\7AZN_metadata.json point structures/7AZN/7azn_protein.pdb structures/7AZN/7azn_pocket.pdb structures/7AZN/7azn_ligand.sdf structures/7AZN/7azn_ligand.pdb structures/7AZN/7azn_ligand.cif structures/7AZN/7azn_complex.pdb structures/7AZN/7azn_complex.cif 7B0T classic MLLT1 YEATS domain Na YEATS domain residues 1-148 with a C-terminal His6-tag T3 mutant benzimidazole-amide based compound 1 "[""GKT""]" 1 Kd Kd = = 4.7 μM 4700.0 [] unit_conversion 5.327902142064282 success True direct_binding Isothermal titration calorimetry (ITC), Figure 4C; T3 mutant. 5 Figure 4C reports compound 1 Kd values: WT 2.6, T1 4.8, and T3 4.7 μM. The Figure 4 caption identifies compound 1 as a benzimidazole-amide based MLLT1 inhibitor and states that panel C summarizes ITC binding constants. auto_single_measurement only accepted activity measurement [1] 1 structures\7B0T\7B0T_metadata.json point structures/7B0T/7b0t_protein.pdb structures/7B0T/7b0t_pocket.pdb structures/7B0T/7b0t_ligand.sdf structures/7B0T/7b0t_ligand.pdb structures/7B0T/7b0t_ligand.cif structures/7B0T/7b0t_complex.pdb structures/7B0T/7b0t_complex.cif 7B0V classic human monoamine oxidase B human Na Na compound 13; (E)-3-phenyl-1-(3-(trifluoromethyl)phenyl)prop-2-en-1-one "[""SKB""]" 1 Ki Ki = = 5.0 ± 0.5 nM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition Ki determined for human recombinant MAO-B using kynuramine as substrate; competitive reversible inhibition. 4 Table 2 reports compound 13 Ki for MAO-B as 5.0 ± 0.5 nM; text identifies it as a competitive reversible MAO-B inhibitor. auto_single_measurement only accepted activity measurement [1] 1 structures\7B0V\7B0V_metadata.json point structures/7B0V/7b0v_protein.pdb structures/7B0V/7b0v_pocket.pdb structures/7B0V/7b0v_ligand.sdf structures/7B0V/7b0v_ligand.pdb structures/7B0V/7b0v_ligand.cif structures/7B0V/7b0v_complex.pdb structures/7B0V/7b0v_complex.cif 7B0Z classic human monoamine oxidase B human Na Na compound 14; (E)-3-phenyl-1-(4-(trifluoromethyl)phenyl)prop-2-en-1-one "[""SK5""]" 1 Ki Ki = = 14.6 ± 0.1 nM 14.6 [] unit_conversion 7.835647144215563 success True biochemical_inhibition Ki determined for human recombinant MAO-B using kynuramine as substrate; competitive reversible inhibition. 4 Table 2 reports compound 14 Ki for MAO-B as 14.6 ± 0.1 nM; the text states the same competitive behavior for compounds 13 and 14. auto_single_measurement only accepted activity measurement [1] 1 structures\7B0Z\7B0Z_metadata.json point structures/7B0Z/7b0z_protein.pdb structures/7B0Z/7b0z_pocket.pdb structures/7B0Z/7b0z_ligand.sdf structures/7B0Z/7b0z_ligand.pdb structures/7B0Z/7b0z_ligand.cif structures/7B0Z/7b0z_complex.pdb structures/7B0Z/7b0z_complex.cif 7B10 classic MLLT1 YEATS domain Na YEATS domain residues 1-148 with a C-terminal His6-tag T1 mutant benzimidazole-amide based compound 1 "[""GKT""]" 1 Kd Kd = = 4.8 μM 4800.0 [] unit_conversion 5.318758762624412 success True direct_binding Isothermal titration calorimetry (ITC), Figure 4C; T1 mutant. 5 Figure 4C reports compound 1 Kd values: WT 2.6, T1 4.8, and T3 4.7 μM. The Figure 4 caption identifies compound 1 as a benzimidazole-amide based MLLT1 inhibitor and states that panel C summarizes ITC binding constants. auto_single_measurement only accepted activity measurement [1] 1 structures\7B10\7B10_metadata.json point structures/7B10/7b10_protein.pdb structures/7B10/7b10_pocket.pdb structures/7B10/7b10_ligand.sdf structures/7B10/7b10_ligand.pdb structures/7B10/7b10_ligand.cif structures/7B10/7b10_complex.pdb structures/7B10/7b10_complex.cif 7B1F extended Mad1 C-terminal domain (Mad1CTD) Human (Homo sapiens) Mad1 residues 597-718 bound to a Bub1CD1 peptide spanning residues 455-479 Na Doubly phosphorylated Bub1CD1 peptide (pSer459 and pThr461) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 2.7 ± 1.20 µM 2700.0 [] unit_conversion 5.568636235841012 success True direct_binding Isothermal titration calorimetry of Mad1CTD binding the doubly phosphorylated Bub1CD1 peptide; 1:1 Mad1CTD dimer:peptide stoichiometry. 6 Figure 4B reports WT Mad1CTD with pSpT CD1 peptide, Kd 2.7 ± 1.20 µM. The text identifies this as the doubly phosphorylated pSer459-pThr461 Bub1 peptide, and page 3 identifies 7B1F as this complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7B1F\7B1F_metadata.json point structures/7B1F/7b1f_protein.pdb structures/7B1F/7b1f_pocket.pdb structures/7B1F/7b1f_ligand.pdb structures/7B1F/7b1f_ligand.cif structures/7B1F/7b1f_complex.pdb structures/7B1F/7b1f_complex.cif 7B1H extended Mad1 C-terminal domain (Mad1CTD) Human (Homo sapiens) Mad1 C-terminal domain bound to a Bub1CD1 peptide Na Doubly phosphorylated Bub1CD1 peptide (pSer459 and pThr461) "[""CHAIN:C"", ""CHAIN:D"", ""CHAIN:G"", ""CHAIN:H""]" 1 Kd Kd = = 2.7 ± 1.20 µM 2700.0 [] unit_conversion 5.568636235841012 success True direct_binding Isothermal titration calorimetry of Mad1CTD binding the doubly phosphorylated Bub1CD1 peptide; 1:1 Mad1CTD dimer:peptide stoichiometry. 6 Figure 4B reports WT Mad1CTD with pSpT CD1 peptide, Kd 2.7 ± 1.20 µM. Page 14 maps 7B1H to deposited Mad1CTD-Bub1CD1 coordinates; the paper describes the phosphorylated peptide complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7B1H\7B1H_metadata.json point structures/7B1H/7b1h_protein.pdb structures/7B1H/7b1h_pocket.pdb structures/7B1H/7b1h_ligand.pdb structures/7B1H/7b1h_ligand.cif structures/7B1H/7b1h_complex.pdb structures/7B1H/7b1h_complex.cif 7B1J extended Mad1 C-terminal domain (Mad1CTD) Human (Homo sapiens) Mad1 C-terminal domain bound to a Bub1CD1 peptide Na Doubly phosphorylated Bub1CD1 peptide (pSer459 and pThr461) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 2.7 ± 1.20 µM 2700.0 [] unit_conversion 5.568636235841012 success True direct_binding Isothermal titration calorimetry of Mad1CTD binding the doubly phosphorylated Bub1CD1 peptide; 1:1 Mad1CTD dimer:peptide stoichiometry. 6 Figure 4B reports WT Mad1CTD with pSpT CD1 peptide, Kd 2.7 ± 1.20 µM. Page 14 maps 7B1J to deposited Mad1CTD-Bub1CD1 coordinates; the paper describes the phosphorylated peptide complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7B1J\7B1J_metadata.json point structures/7B1J/7b1j_protein.pdb structures/7B1J/7b1j_pocket.pdb structures/7B1J/7b1j_ligand.pdb structures/7B1J/7b1j_ligand.cif structures/7B1J/7b1j_complex.pdb structures/7B1J/7b1j_complex.cif 7B1O classic indoleamine 2,3-dioxygenase 1 (IDO1) human Na Na compound 22 "[""SLW""]" 1 IC50 IC50 > > 50,000 nM 50000.0 [] unit_conversion 4.301029995663981 success True biochemical_inhibition hIDO1 RFMS enzymatic assay; Table 1. 3 Table 1 reports compound 22 hIDO1 RFMS IC50 as >50,000 nM; footnote identifies this as an enzymatic RFMS assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7B1O\7B1O_metadata.json point structures/7B1O/7b1o_protein.pdb structures/7B1O/7b1o_pocket.pdb structures/7B1O/7b1o_ligand.sdf structures/7B1O/7b1o_ligand.pdb structures/7B1O/7b1o_ligand.cif structures/7B1O/7b1o_complex.pdb structures/7B1O/7b1o_complex.cif 7B1Q classic BACE1 human Na Na compound 54 (NB-360) "[""SLK""]" 1 IC50 IC50 = = 0.005 µM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition BACE1 IC50 reported in Table 3. 9 Table 3 lists compound 54 with BACE1 IC50 = 0.005 µM. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\7B1Q\7B1Q_metadata.json point structures/7B1Q/7b1q_protein.pdb structures/7B1Q/7b1q_pocket.pdb structures/7B1Q/7b1q_ligand.sdf structures/7B1Q/7b1q_ligand.pdb structures/7B1Q/7b1q_ligand.cif structures/7B1Q/7b1q_complex.pdb structures/7B1Q/7b1q_complex.cif 7B2J classic SARS-CoV-2 main protease (Nsp5) SARS-CoV-2 Residues S1-Q306; N-terminal GST tag followed by an Mpro recognition sequence; C-terminal 6x His tag preceded by an HRV Mpro recognition sequence Na compound 5 "[""SQ2""]" 2 Kd Kd = = 7.2 ± 1 μM 7200.0 [] unit_conversion 5.142667503568731 success True direct_binding SPR biosensor assay of purified Mpro. 4 Table 1 maps compound 5 to PDB 7B2J and reports Kd = 7.2 ± 1 μM; the footnote specifies SPR biosensor analysis. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7B2J\7B2J_metadata.json point structures/7B2J/7b2j_protein.pdb structures/7B2J/7b2j_pocket.pdb structures/7B2J/7b2j_ligand.sdf structures/7B2J/7b2j_ligand.pdb structures/7B2J/7b2j_ligand.cif structures/7B2J/7b2j_complex.pdb structures/7B2J/7b2j_complex.cif 7B2U classic SARS-CoV-2 main protease (Nsp5) SARS-CoV-2 Residues S1-Q306; N-terminal GST tag followed by an Mpro recognition sequence; C-terminal 6x His tag preceded by an HRV Mpro recognition sequence Na compound 1 "[""SQ5""]" 2 Kd Kd = = 23 ± 2 μM 23000.0 [] unit_conversion 4.638272163982407 success True direct_binding SPR biosensor assay of purified Mpro. 4 Table 1 maps compound 1 to PDB 7B2U and reports Kd = 23 ± 2 μM; the footnote specifies SPR biosensor analysis. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7B2U\7B2U_metadata.json point structures/7B2U/7b2u_protein.pdb structures/7B2U/7b2u_pocket.pdb structures/7B2U/7b2u_ligand.sdf structures/7B2U/7b2u_ligand.pdb structures/7B2U/7b2u_ligand.cif structures/7B2U/7b2u_complex.pdb structures/7B2U/7b2u_complex.cif 7B37 classic Notum human enzyme core residues S81-T451; deglycosylated for crystallization C330S ARUK3003718; compound 2 "[""SRK""]" 1 IC50 IC50 = = 3100 ± 920 nM 3100.0 [] unit_conversion 5.508638306165727 success True biochemical_inhibition Notum OPTS activity assay; values are mean ± s.d. (n = 4). 5 Table 1 reports compound 2, R = H (acid), Notum OPTS IC50 = 3100 ± 920 nM; Figure 4 and the accessions map compound 2 to PDB 7B37. auto_single_measurement only accepted activity measurement [1] 1 structures\7B37\7B37_metadata.json point structures/7B37/7b37_protein.pdb structures/7B37/7b37_pocket.pdb structures/7B37/7b37_ligand.sdf structures/7B37/7b37_ligand.pdb structures/7B37/7b37_ligand.cif structures/7B37/7b37_complex.pdb structures/7B37/7b37_complex.cif 7B3G classic Notum Na Na Na ARUK3003902; paper compound 4e "[""SSQ""]" 1 IC50 IC50 = = 30 nM 30.0 [] unit_conversion 7.522878745280337 success True biochemical_inhibition Notum OPTS biochemical assay; Table 3 aryl-ring SAR. 6 Table 3 lists compound 4e (R = 2-Cl) with Notum (OPTS) IC50 30 nM; Figure 5 maps 4e to PDB 7B3G. auto_single_measurement only accepted activity measurement [1] 1 structures\7B3G\7B3G_metadata.json point structures/7B3G/7b3g_protein.pdb structures/7B3G/7b3g_pocket.pdb structures/7B3G/7b3g_ligand.sdf structures/7B3G/7b3g_ligand.pdb structures/7B3G/7b3g_ligand.cif structures/7B3G/7b3g_complex.pdb structures/7B3G/7b3g_complex.cif 7B3P classic Notum Na Na Na ARUK3003775; paper compound 4g "[""SUQ""]" 1 IC50 IC50 = = 21 nM 21.0 [] unit_conversion 7.6777807052660805 success True biochemical_inhibition Notum OPTS biochemical assay; Table 3 aryl-ring SAR. 6 Table 3 lists compound 4g (R = 4-Cl) with Notum (OPTS) IC50 21 nM; Figure 5 maps 4g to PDB 7B3P. auto_single_measurement only accepted activity measurement [1] 1 structures\7B3P\7B3P_metadata.json point structures/7B3P/7b3p_protein.pdb structures/7B3P/7b3p_pocket.pdb structures/7B3P/7b3p_ligand.sdf structures/7B3P/7b3p_ligand.pdb structures/7B3P/7b3p_ligand.cif structures/7B3P/7b3p_complex.pdb structures/7B3P/7b3p_complex.cif 7B3X classic Notum Na Na Na ARUK3003748; paper compound 4c "[""SUT""]" 1 IC50 IC50 = = 9 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition Notum OPTS biochemical assay; Table 3 aryl-ring SAR. 6 Table 3 lists compound 4c (R = 3-Me) with Notum (OPTS) IC50 9 nM; Figure 5 maps 4c to PDB 7B3X. auto_single_measurement only accepted activity measurement [1] 1 structures\7B3X\7B3X_metadata.json point structures/7B3X/7b3x_protein.pdb structures/7B3X/7b3x_pocket.pdb structures/7B3X/7b3x_ligand.sdf structures/7B3X/7b3x_ligand.pdb structures/7B3X/7b3x_ligand.cif structures/7B3X/7b3x_complex.pdb structures/7B3X/7b3x_complex.cif 7B45 classic Notum Na Na Na ARUK3003934; paper compound 4r "[""SWQ""]" 1 IC50 IC50 = = 24 nM 24.0 [] unit_conversion 7.619788758288394 success True biochemical_inhibition Notum OPTS biochemical assay; Table 3 aryl-ring SAR. 6 Table 3 lists compound 4r (R = 3-SMe) with Notum (OPTS) IC50 24 nM; Figure 5 maps 4r to PDB 7B45. auto_single_measurement only accepted activity measurement [1] 1 structures\7B45\7B45_metadata.json point structures/7B45/7b45_protein.pdb structures/7B45/7b45_pocket.pdb structures/7B45/7b45_ligand.sdf structures/7B45/7b45_ligand.pdb structures/7B45/7b45_ligand.cif structures/7B45/7b45_complex.pdb structures/7B45/7b45_complex.cif 7B5Z classic SARS-CoV-2 main protease (Nsp5) SARS-CoV-2 Residues S1-Q306; N-terminal GST tag followed by an Mpro recognition sequence; C-terminal 6x His tag preceded by an HRV Mpro recognition sequence Na compound 6 "[""SYH""]" 1 Kd Kd = = 39 ± 4 μM 39000.0 [] unit_conversion 4.4089353929735005 success True direct_binding SPR biosensor assay of purified Mpro. 4 Table 1 maps compound 6 to PDB 7B5Z and reports Kd = 39 ± 4 μM; the footnote specifies SPR biosensor analysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7B5Z\7B5Z_metadata.json point structures/7B5Z/7b5z_protein.pdb structures/7B5Z/7b5z_pocket.pdb structures/7B5Z/7b5z_ligand.sdf structures/7B5Z/7b5z_ligand.pdb structures/7B5Z/7b5z_ligand.cif structures/7B5Z/7b5z_complex.pdb structures/7B5Z/7b5z_complex.cif 7B63 classic NUDT15 human pCold II expression construct with an N-terminal His tag; expressed in E. coli BL21 WT TH7755 "[""SYW""]" 3 Ki Ki = = 10.2 ± 0.9 nM 10.2 [] unit_conversion 7.991399828238082 success True biochemical_inhibition Initial-rate enzymatic assay with 6-thio-dGTP; competitive-inhibition model fitted to determine Ki. 3 “The Ki for TH7755 was determined to be 10.2 ±” (continued as “0.9 nM” on page 4). auto_metric_priority unique highest-priority metric family: Ki [3] 3 structures\7B63\7B63_metadata.json point structures/7B63/7b63_protein.pdb structures/7B63/7b63_pocket.pdb structures/7B63/7b63_ligand.sdf structures/7B63/7b63_ligand.pdb structures/7B63/7b63_ligand.cif structures/7B63/7b63_complex.pdb structures/7B63/7b63_complex.cif 7B6S extended Sheep polyomavirus VP1 sheep Recombinant His6-tagged VP1; His6 tag cleaved before crystallization Na Forssman antigen pentaose (Forssman pentaose, FP) "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 3.6 nM 3.6 [] unit_conversion 8.443697499232712 success True direct_binding Surface plasmon resonance of purified ShPyV VP1 binding a Forssman-pentaose-decorated surface; kinetic-parameter table in Figure 3a. 26 Figure 3a reports VP1 K_D = 3.6 nM for binding toward a Forssman-decorated surface. auto_single_measurement only accepted activity measurement [1] 1 structures\7B6S\7B6S_metadata.json point structures/7B6S/7b6s_ligand.cif structures/7B6S/7b6s_complex.cif 7B77 classic SARS-CoV-2 main protease (Nsp5) SARS-CoV-2 Residues S1-Q306; N-terminal GST tag followed by an Mpro recognition sequence; C-terminal 6x His tag preceded by an HRV Mpro recognition sequence Na compound 8 "[""T0W""]" 1 Kd Kd = = 79 ± 6 μM 79000.0 [] unit_conversion 4.102372908709558 success True direct_binding SPR biosensor assay of purified Mpro. 4 Table 1 maps compound 8 to PDB 7B77 and reports Kd = 79 ± 6 μM; the footnote specifies SPR biosensor analysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7B77\7B77_metadata.json point structures/7B77/7b77_protein.pdb structures/7B77/7b77_pocket.pdb structures/7B77/7b77_ligand.sdf structures/7B77/7b77_ligand.pdb structures/7B77/7b77_ligand.cif structures/7B77/7b77_complex.pdb structures/7B77/7b77_complex.cif 7B9H classic PDE4D Na PDE4D catalytic domain, amino acids 244-578, with a C-terminal 6His-tag Na GEBR-42a; compound 2a "[""T3K""]" 1 IC50 IC50 = = 33.1 ± 4.6 µM 33100.0 [] unit_conversion 4.480172006224281 success True biochemical_inhibition NADH-coupled biochemical inhibition assay against purified PDE4D catalytic domain. 6 Table 2 reports compound 2a IC50 = 33.1 ± 4.6 µM against PDE4D Cat; Figure 7 identifies the crystallized 7B9H ligand as GEBR-42a/2a. auto_single_measurement only accepted activity measurement [1] 1 structures\7B9H\7B9H_metadata.json point structures/7B9H/7b9h_protein.pdb structures/7B9H/7b9h_pocket.pdb structures/7B9H/7b9h_ligand.sdf structures/7B9H/7b9h_ligand.pdb structures/7B9H/7b9h_ligand.cif structures/7B9H/7b9h_complex.pdb structures/7B9H/7b9h_complex.cif 7BAG extended C3b Human C3 purified from human plasma and converted to C3b Na Cp40 "[""CHAIN:C""]" 1 Kd Kd = = 0.8 ± 0.2 nM 0.8 [] unit_conversion 9.096910013008056 success True direct_binding SPR on amine-reactive immobilized C3b; average ± standard deviation from three independent experiments. 7 Table 1 lists Cp40 K_D = 0.8 ± 0.2 nM; its footnote specifies three independent SPR experiments on amine-reactive immobilized C3b. auto_single_measurement only accepted activity measurement [1] 1 structures\7BAG\7BAG_metadata.json point structures/7BAG/7bag_protein.pdb structures/7BAG/7bag_pocket.pdb structures/7BAG/7bag_ligand.pdb structures/7BAG/7bag_ligand.cif structures/7BAG/7bag_complex.pdb structures/7BAG/7bag_complex.cif 7BBM classic mutant nitrobindin (NB4H) Arabidopsis thaliana NB4H nitrobindin variant M75L/H76L/Q96C/M148L MnPPIX "[""MNH""]" 1 Kd Kd = = 195 nM 195.0 [] unit_conversion 6.709965388637482 success True direct_binding Cofactor-binding determination for MnPPIX@NB4H. 3 “For MnPPIX@NB4H a Kd = 195 nM was observed.” auto_single_measurement only accepted activity measurement [1] 1 structures\7BBM\7BBM_metadata.json point structures/7BBM/7bbm_protein.pdb structures/7BBM/7bbm_pocket.pdb structures/7BBM/7bbm_ligand.sdf structures/7BBM/7bbm_ligand.pdb structures/7BBM/7bbm_ligand.cif structures/7BBM/7bbm_complex.pdb structures/7BBM/7bbm_complex.cif 7BCE classic Human Notum human Notum_core S81-T451 C330S compound 38 (DSPL fragment 718) "[""LDV""]" 1 IC50 IC50 = = 120 ± 49 μM 120000.0 [] unit_conversion 3.920818753952375 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 5 Table 1 reports compound 38 / PDB 7BCE: IC50 120 ± 49 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BCE\7BCE_metadata.json point structures/7BCE/7bce_protein.pdb structures/7BCE/7bce_pocket.pdb structures/7BCE/7bce_ligand.sdf structures/7BCE/7bce_ligand.pdb structures/7BCE/7bce_ligand.cif structures/7BCE/7bce_complex.pdb structures/7BCE/7bce_complex.cif 7BCF classic Human Notum human Notum_core S81-T451 C330S compound 39 (DSPL fragment 722) "[""T9W""]" 1 IC50 IC50 > > 1000 μM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 5 Table 1 reports compound 39 / PDB 7BCF: IC50 >1000 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BCF\7BCF_metadata.json point structures/7BCF/7bcf_protein.pdb structures/7BCF/7bcf_pocket.pdb structures/7BCF/7bcf_ligand.sdf structures/7BCF/7bcf_ligand.pdb structures/7BCF/7bcf_ligand.cif structures/7BCF/7bcf_complex.pdb structures/7BCF/7bcf_complex.cif 7BCH classic Human Notum human Notum_core S81-T451 C330S compound 41 (DSPL fragment 772) "[""T9Q""]" 1 IC50 IC50 = = 68 ± 5.4 μM 68000.0 [] unit_conversion 4.167491087293763 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 5 Table 1 reports compound 41 / PDB 7BCH: IC50 68 ± 5.4 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BCH\7BCH_metadata.json point structures/7BCH/7bch_protein.pdb structures/7BCH/7bch_pocket.pdb structures/7BCH/7bch_ligand.sdf structures/7BCH/7bch_ligand.pdb structures/7BCH/7bch_ligand.cif structures/7BCH/7bch_complex.pdb structures/7BCH/7bch_complex.cif 7BCI classic Human Notum human Notum_core S81-T451 C330S compound 42 (DSPL fragment 784) "[""GVV""]" 1 IC50 IC50 > > 1000 μM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 5 Table 1 reports compound 42 / PDB 7BCI: IC50 >1000 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BCI\7BCI_metadata.json point structures/7BCI/7bci_protein.pdb structures/7BCI/7bci_pocket.pdb structures/7BCI/7bci_ligand.sdf structures/7BCI/7bci_ligand.pdb structures/7BCI/7bci_ligand.cif structures/7BCI/7bci_complex.pdb structures/7BCI/7bci_complex.cif 7BCK classic Human Notum human Notum_core S81-T451 C330S compound 43 (DSPL fragment 791) "[""T9B""]" 1 IC50 IC50 = = 87 ± 47 μM 87000.0 [] unit_conversion 4.060480747381382 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 5 Table 1 reports compound 43 / PDB 7BCK: IC50 87 ± 47 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BCK\7BCK_metadata.json point structures/7BCK/7bck_protein.pdb structures/7BCK/7bck_pocket.pdb structures/7BCK/7bck_ligand.sdf structures/7BCK/7bck_ligand.pdb structures/7BCK/7bck_ligand.cif structures/7BCK/7bck_complex.pdb structures/7BCK/7bck_complex.cif 7BCL classic Human Notum human Notum_core S81-T451 C330S compound 44 (DSPL fragment 792) "[""T9K""]" 1 IC50 IC50 = = 410 ± 63 μM 410000.0 [] unit_conversion 3.3872161432802645 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 44 / PDB 7BCL: IC50 410 ± 63 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BCL\7BCL_metadata.json point structures/7BCL/7bcl_protein.pdb structures/7BCL/7bcl_pocket.pdb structures/7BCL/7bcl_ligand.sdf structures/7BCL/7bcl_ligand.pdb structures/7BCL/7bcl_ligand.cif structures/7BCL/7bcl_complex.pdb structures/7BCL/7bcl_complex.cif 7BCQ classic ASCT2 (SLC1A5) human (Homo sapiens) Na Na Lc-BPE (L-cis hydroxyproline biphenyl ester) "[""TG2""]" 1 IC50 IC50 = = 20.0 µM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition Glutamine-uptake assay in proteoliposomes reconstituted with purified hASCT2; 5 µM L-glutamine. 5 Fig. 2 caption: inhibition of glutamine uptake in proteoliposomes reconstituted with purified hASCT2 gave a half-maximum inhibitory concentration (IC50) of 20.0 µM for Lc-BPE in the presence of 5 µM glutamine. auto_single_measurement only accepted activity measurement [1] 1 structures\7BCQ\7BCQ_metadata.json point structures/7BCQ/7bcq_protein.pdb structures/7BCQ/7bcq_pocket.pdb structures/7BCQ/7bcq_ligand.sdf structures/7BCQ/7bcq_ligand.pdb structures/7BCQ/7bcq_ligand.cif structures/7BCQ/7bcq_complex.pdb structures/7BCQ/7bcq_complex.cif 7BCS classic ASCT2 (SLC1A5) human (Homo sapiens) Na Na Lc-BPE (L-cis hydroxyproline biphenyl ester) "[""TJ5""]" 1 IC50 IC50 = = 20.0 µM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition Glutamine-uptake assay in proteoliposomes reconstituted with purified hASCT2; 5 µM L-glutamine. 5 Fig. 2 caption: inhibition of glutamine uptake in proteoliposomes reconstituted with purified hASCT2 gave a half-maximum inhibitory concentration (IC50) of 20.0 µM for Lc-BPE in the presence of 5 µM glutamine. auto_single_measurement only accepted activity measurement [1] 1 structures\7BCS\7BCS_metadata.json point structures/7BCS/7bcs_protein.pdb structures/7BCS/7bcs_pocket.pdb structures/7BCS/7bcs_ligand.sdf structures/7BCS/7bcs_ligand.pdb structures/7BCS/7bcs_ligand.cif structures/7BCS/7bcs_complex.pdb structures/7BCS/7bcs_complex.cif 7BD2 classic Human Notum human Notum_core S81-T451 C330S compound 45 (DSPL fragment 810) "[""NUM""]" 1 IC50 IC50 = = 720 ± 18 μM 720000.0 [] unit_conversion 3.142667503568732 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 45 / PDB 7BD2: IC50 720 ± 18 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BD2\7BD2_metadata.json point structures/7BD2/7bd2_protein.pdb structures/7BD2/7bd2_pocket.pdb structures/7BD2/7bd2_ligand.sdf structures/7BD2/7bd2_ligand.pdb structures/7BD2/7bd2_ligand.cif structures/7BD2/7bd2_complex.pdb structures/7BD2/7bd2_complex.cif 7BD3 classic Human Notum human Notum_core S81-T451 C330S compound 46 (DSPL fragment 823) "[""TE5""]" 1 IC50 IC50 = = 380 ± 130 μM 380000.0 [] unit_conversion 3.42021640338319 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 46 / PDB 7BD3: IC50 380 ± 130 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BD3\7BD3_metadata.json point structures/7BD3/7bd3_protein.pdb structures/7BD3/7bd3_pocket.pdb structures/7BD3/7bd3_ligand.sdf structures/7BD3/7bd3_ligand.pdb structures/7BD3/7bd3_ligand.cif structures/7BD3/7bd3_complex.pdb structures/7BD3/7bd3_complex.cif 7BD5 classic Human Notum human Notum_core S81-T451 C330S compound 48 (DSPL fragment 830) "[""YI6""]" 1 IC50 IC50 > > 1000 μM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 48 / PDB 7BD5: IC50 >1000 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BD5\7BD5_metadata.json point structures/7BD5/7bd5_protein.pdb structures/7BD5/7bd5_pocket.pdb structures/7BD5/7bd5_ligand.sdf structures/7BD5/7bd5_ligand.pdb structures/7BD5/7bd5_ligand.cif structures/7BD5/7bd5_complex.pdb structures/7BD5/7bd5_complex.cif 7BD8 classic Human Notum human Notum_core S81-T451 C330S compound 50 (DSPL fragment 872) "[""QL5""]" 1 IC50 IC50 = = 36 ± 2.7 μM 36000.0 [] unit_conversion 4.443697499232713 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 50 / PDB 7BD8: IC50 36 ± 2.7 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BD8\7BD8_metadata.json point structures/7BD8/7bd8_protein.pdb structures/7BD8/7bd8_pocket.pdb structures/7BD8/7bd8_ligand.sdf structures/7BD8/7bd8_ligand.pdb structures/7BD8/7bd8_ligand.cif structures/7BD8/7bd8_complex.pdb structures/7BD8/7bd8_complex.cif 7BD9 classic Human Notum human Notum_core S81-T451 C330S compound 51 (DSPL fragment 886) "[""GW1""]" 1 IC50 IC50 > > 1000 μM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 51 / PDB 7BD9: IC50 >1000 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BD9\7BD9_metadata.json point structures/7BD9/7bd9_protein.pdb structures/7BD9/7bd9_pocket.pdb structures/7BD9/7bd9_ligand.sdf structures/7BD9/7bd9_ligand.pdb structures/7BD9/7bd9_ligand.cif structures/7BD9/7bd9_complex.pdb structures/7BD9/7bd9_complex.cif 7BDA classic Human Notum human Notum_core S81-T451 C330S compound 52 (DSPL fragment 900) "[""O1J""]" 1 IC50 IC50 > > 1000 μM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 52 / PDB 7BDA: IC50 >1000 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BDA\7BDA_metadata.json point structures/7BDA/7bda_protein.pdb structures/7BDA/7bda_pocket.pdb structures/7BDA/7bda_ligand.sdf structures/7BDA/7bda_ligand.pdb structures/7BDA/7bda_ligand.cif structures/7BDA/7bda_complex.pdb structures/7BDA/7bda_complex.cif 7BDB classic Human Notum human Notum_core S81-T451 C330S compound 53 (DSPL fragment 916) "[""NW7""]" 1 IC50 IC50 = = 980 ± 17 μM 980000.0 [] unit_conversion 3.008773924307505 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 53 / PDB 7BDB: IC50 980 ± 17 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BDB\7BDB_metadata.json point structures/7BDB/7bdb_protein.pdb structures/7BDB/7bdb_pocket.pdb structures/7BDB/7bdb_ligand.sdf structures/7BDB/7bdb_ligand.pdb structures/7BDB/7bdb_ligand.cif structures/7BDB/7bdb_complex.pdb structures/7BDB/7bdb_complex.cif 7BDC classic Human Notum human Notum_core S81-T451 C330S compound 54 (DSPL fragment 923) "[""WNA""]" 1 IC50 IC50 = = 78 ± 8.2 μM 78000.0 [] unit_conversion 4.107905397309519 success True biochemical_inhibition OPTS-substrate biochemical Notum inhibition assay; Table 1 value. 6 Table 1 reports compound 54 / PDB 7BDC: IC50 78 ± 8.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BDC\7BDC_metadata.json point structures/7BDC/7bdc_protein.pdb structures/7BDC/7bdc_pocket.pdb structures/7BDC/7bdc_ligand.sdf structures/7BDC/7bdc_ligand.pdb structures/7BDC/7bdc_ligand.cif structures/7BDC/7bdc_complex.pdb structures/7BDC/7bdc_complex.cif 7BE3 extended Human Galectin-3 human carbohydrate recognition domain, residues L114-L250 Na LacdiNAc (LDN; GalNAc beta 1-4 GlcNAc) "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 18.3 ± 2.2 μM 18300.0 [] unit_conversion 4.73754891026957 success True direct_binding Isothermal titration calorimetry of hGal-3 with LDN; single-site binding model, 298 K. 2 Figure 2A reports hGal-3/LDN K_D (μM) = 18.3 ± 2.2. The text states that ITC measurements for LDN in the presence of hGal-3 were performed and that the resulting dissociation constants are shown in Figure 2A. auto_single_measurement only accepted activity measurement [1] 1 structures\7BE3\7BE3_metadata.json point structures/7BE3/7be3_protein.pdb structures/7BE3/7be3_pocket.pdb structures/7BE3/7be3_ligand.pdb structures/7BE3/7be3_ligand.cif structures/7BE3/7be3_complex.pdb structures/7BE3/7be3_complex.cif 7BF6 classic SARS-CoV-2 macrodomain SARS-CoV-2 Na Na remdesivir metabolite GS-441524 "[""U08""]" 1 Kd Kd = = 10.8 ± 1.8 μM 10800.0 [] unit_conversion 4.966576244513051 success True direct_binding Isothermal titration calorimetry; binding parameters averaged from duplicates. 4 Figure 4 maps GS-441524 to PDB ID 7BF6 and reports its ITC K_D = 10.8 ± 1.8 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BF6\7BF6_metadata.json point structures/7BF6/7bf6_protein.pdb structures/7BF6/7bf6_pocket.pdb structures/7BF6/7bf6_ligand.sdf structures/7BF6/7bf6_ligand.pdb structures/7BF6/7bf6_ligand.cif structures/7BF6/7bf6_complex.pdb structures/7BF6/7bf6_complex.cif 7BFA extended human carbonic anhydrase II (hCA II) human native hCA II crystals Na compound 23; 4-(2-(3-(4-iodophenyl)thioureido)ethyl)benzenesulfonamide "[""TKE""]" 1 Ki Ki = = 7.6 nM 7.6 [] unit_conversion 8.119186407719209 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay; Table 1. 3 Table 1 reports Ki = 7.6 nM for compound 23 against hCA II; the text states these compounds were tested by stopped-flow CO2-hydration assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7BFA\7BFA_metadata.json point structures/7BFA/7bfa_ligand.sdf structures/7BFA/7bfa_ligand.cif structures/7BFA/7bfa_complex.cif 7BFZ classic human prostate-specific membrane antigen (PSMA) human extracellular domain of human PSMA, amino acids 44-750 Na Glu-490 "[""TKZ""]" 1 IC50 IC50 = = 63.1 pM 0.0631 [] unit_conversion 10.199970640755865 success True biochemical_inhibition Established NAAG-hydrolyzing inhibition assay using recombinant human PSMA; the paper reports IC50 values for Glu-490, ODAP-490, and ODAP-436. 2 “The IC50 values of the probes were determined using an established NAAG-hydrolyzing assay… Inhibition constants for Glu-490, ODAP-490, and ODAP-436 were 63.1, 99.6, and 118.4 pM (Fig. 1d), respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7BFZ\7BFZ_metadata.json point structures/7BFZ/7bfz_protein.pdb structures/7BFZ/7bfz_pocket.pdb structures/7BFZ/7bfz_ligand.sdf structures/7BFZ/7bfz_ligand.pdb structures/7BFZ/7bfz_ligand.cif structures/7BFZ/7bfz_complex.pdb structures/7BFZ/7bfz_complex.cif 7BG5 extended human carbonic anhydrase II (hCA II) human native hCA II crystals Na compound 27; 4-(2-(3-(4-iodophenyl)ureido)ethyl)benzenesulfonamide "[""TKQ""]" 1 Ki Ki = = 7.8 nM 7.8 [] unit_conversion 8.10790539730952 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay; Table 1. 3 Table 1 reports Ki = 7.8 nM for compound 27 against hCA II; the text states these compounds were tested by stopped-flow CO2-hydration assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7BG5\7BG5_metadata.json point structures/7BG5/7bg5_ligand.sdf structures/7BG5/7bg5_ligand.cif structures/7BG5/7bg5_complex.cif 7BGN classic MtHISN2 Medicago truncatula N-terminally truncated construct starting at Val49 with a Ser-Asn-Ala linker Na AMP "[""AMP""]" 1 Kd Kd = = 47 ± 6 μM 47000.0 [] unit_conversion 4.327902142064283 success True direct_binding Isothermal titration calorimetry of AMP against MtHISN2 protein; stoichiometry N = 1. 12 “AMP binding to MtHISN2 … is characterized by the Kd value of 47 ± 6 μM and stoichiometry N = 1.” auto_single_measurement only accepted activity measurement [1] 1 structures\7BGN\7BGN_metadata.json point structures/7BGN/7bgn_protein.pdb structures/7BGN/7bgn_pocket.pdb structures/7BGN/7bgn_ligand.sdf structures/7BGN/7bgn_ligand.pdb structures/7BGN/7bgn_ligand.cif structures/7BGN/7bgn_complex.pdb structures/7BGN/7bgn_complex.cif 7BHD extended FimH fimbrial adhesin Escherichia coli FimH lectin domain, residues Phe1-Thr158 Na alpha1,6 core-fucosylated oligomannose-3 (Man3Gn2F1[6]) "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 118 nM 118.0 [] unit_conversion 6.928117992693874 success True direct_binding SPR binding to immobilized glycan ligand; Langmuir 1:1 fit. 5 Table 1 reports Kd = 118 nM for glycan Man3Gn2F1[6]; Figure 2 identifies the FimH–Man3Gn2F1[6] crystal as PDB 7BHD. auto_single_measurement only accepted activity measurement [1] 1 structures\7BHD\7BHD_metadata.json point structures/7BHD/7bhd_protein.pdb structures/7BHD/7bhd_pocket.pdb structures/7BHD/7bhd_ligand.pdb structures/7BHD/7bhd_ligand.cif structures/7BHD/7bhd_complex.pdb structures/7BHD/7bhd_complex.cif 7BHH classic human carbonic anhydrase II (hCA II) human native hCA II crystals Na compound 18; 4-(2-(3-(4-iodophenyl)selenoureido)ethyl)benzenesulfonamide "[""TN8""]" 1 Ki Ki = = 57.6 nM 57.6 [] unit_conversion 7.239577516576788 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay; Table 1. 3 Table 1 reports Ki = 57.6 nM for compound 18 against hCA II; the text states these compounds were tested by stopped-flow CO2-hydration assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7BHH\7BHH_metadata.json point structures/7BHH/7bhh_protein.pdb structures/7BHH/7bhh_pocket.pdb structures/7BHH/7bhh_ligand.sdf structures/7BHH/7bhh_ligand.pdb structures/7BHH/7bhh_ligand.cif structures/7BHH/7bhh_complex.pdb structures/7BHH/7bhh_complex.cif 7BHR classic MAT2a Na Na Na compound 1 (triazinone fragment) "[""TQE""]" 1 Kd Kd = = 250 µM 250000.0 [] unit_conversion 3.6020599913279625 success True direct_binding SPR binding assay 3 Table 1 reports compound 1 Kd = 250 µM; the text identifies fragment affinities as determined by SPR. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7BHR\7BHR_metadata.json point structures/7BHR/7bhr_protein.pdb structures/7BHR/7bhr_pocket.pdb structures/7BHR/7bhr_ligand.sdf structures/7BHR/7bhr_ligand.pdb structures/7BHR/7bhr_ligand.cif structures/7BHR/7bhr_complex.pdb structures/7BHR/7bhr_complex.cif 7BHS classic MAT2a Na Na Na compound 2 (quinazoline fragment) "[""TNZ""]" 1 Kd Kd = = 6.2 µM 6200.0 [] unit_conversion 5.207608310501746 success True direct_binding SPR binding assay 3 Table 1 reports compound 2 Kd = 6.2 µM; the text identifies fragment affinities as determined by SPR. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7BHS\7BHS_metadata.json point structures/7BHS/7bhs_protein.pdb structures/7BHS/7bhs_pocket.pdb structures/7BHS/7bhs_ligand.sdf structures/7BHS/7bhs_ligand.pdb structures/7BHS/7bhs_ligand.cif structures/7BHS/7bhs_complex.pdb structures/7BHS/7bhs_complex.cif 7BHT classic MAT2a Na Na Na compound 5 (quinazolinone fragment) "[""TO8""]" 1 Kd Kd = = 4.9 µM 4900.0 [] unit_conversion 5.309803919971486 success True direct_binding Direct binding measurement shown with the fragment-merging series 4 Figure 3 explicitly prints compound 5 Kd = 4.9 µM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7BHT\7BHT_metadata.json point structures/7BHT/7bht_protein.pdb structures/7BHT/7bht_pocket.pdb structures/7BHT/7bht_ligand.sdf structures/7BHT/7bht_ligand.pdb structures/7BHT/7bht_ligand.cif structures/7BHT/7bht_complex.pdb structures/7BHT/7bht_complex.cif 7BHU classic MAT2a Na Na Na compound 26 "[""TOW""]" 1 IC50 IC50 = = 7.2 µM 7200.0 [] unit_conversion 5.142667503568731 success True biochemical_inhibition MAT2a enzymatic functional assay measuring free phosphate release 6 Table 4 reports compound 26 IC50 = 7.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BHU\7BHU_metadata.json point structures/7BHU/7bhu_protein.pdb structures/7BHU/7bhu_pocket.pdb structures/7BHU/7bhu_ligand.sdf structures/7BHU/7bhu_ligand.pdb structures/7BHU/7bhu_ligand.cif structures/7BHU/7bhu_complex.pdb structures/7BHU/7bhu_complex.cif 7BHV classic MAT2a Na Na Na compound 28 (in vivo tool compound) "[""TQB""]" 1 IC50 IC50 = = 0.022 µM 22.0 [] unit_conversion 7.657577319177793 success True biochemical_inhibition MAT2a enzymatic functional assay measuring free phosphate release 6 Table 4 reports compound 28 IC50 = 0.022 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BHV\7BHV_metadata.json point structures/7BHV/7bhv_protein.pdb structures/7BHV/7bhv_pocket.pdb structures/7BHV/7bhv_ligand.sdf structures/7BHV/7bhv_ligand.pdb structures/7BHV/7bhv_ligand.cif structures/7BHV/7bhv_complex.pdb structures/7BHV/7bhv_complex.cif 7BHW classic MAT2a Na Na Na compound 29 "[""TNW""]" 1 IC50 IC50 = = 0.016 µM 16.0 [] unit_conversion 7.795880017344075 success True biochemical_inhibition MAT2a enzymatic functional assay measuring free phosphate release 6 Table 4 reports compound 29 IC50 = 0.016 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BHW\7BHW_metadata.json point structures/7BHW/7bhw_protein.pdb structures/7BHW/7bhw_pocket.pdb structures/7BHW/7bhw_ligand.sdf structures/7BHW/7bhw_ligand.pdb structures/7BHW/7bhw_ligand.cif structures/7BHW/7bhw_complex.pdb structures/7BHW/7bhw_complex.cif 7BHX classic MAT2a Na Na Na compound 31 "[""TO5""]" 1 IC50 IC50 = = 0.021 µM 21.0 [] unit_conversion 7.6777807052660805 success True biochemical_inhibition MAT2a enzymatic functional assay measuring free phosphate release 6 Table 4 reports compound 31 IC50 = 0.021 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BHX\7BHX_metadata.json point structures/7BHX/7bhx_protein.pdb structures/7BHX/7bhx_pocket.pdb structures/7BHX/7bhx_ligand.sdf structures/7BHX/7bhx_ligand.pdb structures/7BHX/7bhx_ligand.cif structures/7BHX/7bhx_complex.pdb structures/7BHX/7bhx_complex.cif 7BI9 classic PI3KC2alpha mouse PI3KC2alpha core construct HBD residues 550-665 replaced by SGAGSGA PIK-90 "[""090""]" 1 IC50 IC50 = = 78 nM 78.0 [] unit_conversion 7.107905397309519 success True biochemical_inhibition In vitro kinase inhibition measurement of PI3KC2α with PIK-90; the paper states that the PI3KC2α core structure was determined in complex with PIK-90 and reports its IC50 for PI3KC2α. 3 “PIK-90, which also displays profound off-target activity toward PI3KC2α (IC50 = 78 nM)” and the adjacent section identifies the PI3KC2αcore–PIK-90 structure. auto_single_measurement only accepted activity measurement [1] 1 structures\7BI9\7BI9_metadata.json point structures/7BI9/7bi9_protein.pdb structures/7BI9/7bi9_pocket.pdb structures/7BI9/7bi9_ligand.sdf structures/7BI9/7bi9_ligand.pdb structures/7BI9/7bi9_ligand.cif structures/7BI9/7bi9_complex.pdb structures/7BI9/7bi9_complex.cif 7BIR classic MDM2 human MDM2 residues 17–109 E69A; K70A compound 23 "[""TUZ""]" 1 IC50 IC50 = = 0.010 µM 10.0 [] unit_conversion 8.0 success True biochemical_inhibition MDM2-p53 ELISA inhibition assay. 47 The official Supporting Information maps 7BIR to compound 23 and its crystallization construct; the main-text table reports ELISA IC50 0.010 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BIR\7BIR_metadata.json point structures/7BIR/7bir_protein.pdb structures/7BIR/7bir_pocket.pdb structures/7BIR/7bir_ligand.sdf structures/7BIR/7bir_ligand.pdb structures/7BIR/7bir_ligand.cif structures/7BIR/7bir_complex.pdb structures/7BIR/7bir_complex.cif 7BIT classic MDM2 human MDM2 residues 17–125 K51A compound 21 (AT31188; PDB ligand TV5) "[""TV5""]" 1 IC50 IC50 = = 0.0087 µM 8.7 [] unit_conversion 8.060480747381382 success True biochemical_inhibition MDM2-p53 ELISA inhibition assay. 47 The official Supporting Information maps 7BIT to compound 21 (AT31188; PDB ligand TV5) and its crystallization construct; the main-text table reports ELISA IC50 0.0087 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BIT\7BIT_metadata.json point structures/7BIT/7bit_protein.pdb structures/7BIT/7bit_pocket.pdb structures/7BIT/7bit_ligand.sdf structures/7BIT/7bit_ligand.pdb structures/7BIT/7bit_ligand.cif structures/7BIT/7bit_complex.pdb structures/7BIT/7bit_complex.cif 7BJ0 classic MDM2 human MDM2 residues 17–125 E69A; K70A compound 1 "[""TVH""]" 1 IC50 IC50 = = 0.040 µM 40.0 [] unit_conversion 7.3979400086720375 success True biochemical_inhibition MDM2-p53 ELISA inhibition assay. 44 The official Supporting Information maps 7BJ0 to compound 1 and its crystallization construct; the main-text table reports ELISA IC50 0.040 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BJ0\7BJ0_metadata.json point structures/7BJ0/7bj0_protein.pdb structures/7BJ0/7bj0_pocket.pdb structures/7BJ0/7bj0_ligand.sdf structures/7BJ0/7bj0_ligand.pdb structures/7BJ0/7bj0_ligand.cif structures/7BJ0/7bj0_complex.pdb structures/7BJ0/7bj0_complex.cif 7BJ8 classic L1 Stenotrophomonas maltophilia Na Na 2-mercaptomethyl thiazolidine D-syn-1b "[""QST""]" 1 Ki Ki = = 4.0 ± 0.6 µM 4000.0 [] unit_conversion 5.3979400086720375 success True biochemical_inhibition Purified, recombinant L1; steady-state imipenem-hydrolysis competitive-inhibition assay at 30 °C. 3 Table 1 reports D-syn-1b against B3 MBL L1: Ki 4.0 ± 0.6 µM. Figure 4 maps L1:D-syn-1b to PDB 7BJ8. auto_single_measurement only accepted activity measurement [1] 1 structures\7BJ8\7BJ8_metadata.json point structures/7BJ8/7bj8_protein.pdb structures/7BJ8/7bj8_pocket.pdb structures/7BJ8/7bj8_ligand.sdf structures/7BJ8/7bj8_ligand.pdb structures/7BJ8/7bj8_ligand.cif structures/7BJ8/7bj8_complex.pdb structures/7BJ8/7bj8_complex.cif 7BJ9 classic Sfh-I Serratia fonticola Na Na 2-mercaptomethyl thiazolidine L-anti-1a "[""TWW""]" 1 Ki Ki = = 0.16 ± 0.03 µM 160.0 [] unit_conversion 6.795880017344075 success True biochemical_inhibition Purified, recombinant Sfh-I; steady-state imipenem-hydrolysis competitive-inhibition assay at 30 °C. 3 Table 1 reports L-anti-1a against B2 MBL Sfh-I: Ki 0.16 ± 0.03 µM. Figure 4 maps Sfh-I:L-anti-1a to PDB 7BJ9. auto_single_measurement only accepted activity measurement [1] 1 structures\7BJ9\7BJ9_metadata.json point structures/7BJ9/7bj9_protein.pdb structures/7BJ9/7bj9_pocket.pdb structures/7BJ9/7bj9_ligand.sdf structures/7BJ9/7bj9_ligand.pdb structures/7BJ9/7bj9_ligand.cif structures/7BJ9/7bj9_complex.pdb structures/7BJ9/7bj9_complex.cif 7BLA classic BAZ2A Na Na Na TP-238 "[""WCS""]" 1 Kd Kd = = 108 ± 6 µM 108000.0 [] unit_conversion 3.9665762445130506 success True direct_binding Isothermal titration calorimetry; thermodynamic binding parameters in Table 2. 9 Table 2 prints TP-238 KD BAZ2A as 108 ± 6 µM; the preceding text identifies the measurement as ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7BLA\7BLA_metadata.json point structures/7BLA/7bla_protein.pdb structures/7BLA/7bla_pocket.pdb structures/7BLA/7bla_ligand.sdf structures/7BLA/7bla_ligand.pdb structures/7BLA/7bla_ligand.cif structures/7BLA/7bla_complex.pdb structures/7BLA/7bla_complex.cif 7BLB classic BAZ2A Na Na Na GSK4027 "[""9ST""]" 1 Kd Kd = = 165 ± 8 µM 165000.0 [] unit_conversion 3.7825160557860933 success True direct_binding Isothermal titration calorimetry; thermodynamic binding parameters in Table 2. 9 Table 2 prints GSK4027 KD BAZ2A as 165 ± 8 µM; the preceding text identifies the measurement as ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7BLB\7BLB_metadata.json point structures/7BLB/7blb_protein.pdb structures/7BLB/7blb_pocket.pdb structures/7BLB/7blb_ligand.sdf structures/7BLB/7blb_ligand.pdb structures/7BLB/7blb_ligand.cif structures/7BLB/7blb_complex.pdb structures/7BLB/7blb_complex.cif 7BLC classic BAZ2A Na Na Na UP39 "[""U2E""]" 1 IC50 IC50 = = 61 ± 4 µM 61000.0 [] unit_conversion 4.214670164989233 success True biochemical_inhibition Binding-competition activity tested by AlphaScreen (Table 1). 6 Table 1 prints UP39 IC50 for BAZ2A as 61 ± 4 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BLC\7BLC_metadata.json point structures/7BLC/7blc_protein.pdb structures/7BLC/7blc_pocket.pdb structures/7BLC/7blc_ligand.sdf structures/7BLC/7blc_ligand.pdb structures/7BLC/7blc_ligand.cif structures/7BLC/7blc_complex.pdb structures/7BLC/7blc_complex.cif 7BLD classic BAZ2A Na Na Na UZH23 "[""U2K""]" 1 IC50 IC50 = = 86 ± 9 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Binding-competition activity tested by AlphaScreen (Table 1). 6 Table 1 prints UZH23 IC50 for BAZ2A as 86 ± 9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BLD\7BLD_metadata.json point structures/7BLD/7bld_protein.pdb structures/7BLD/7bld_pocket.pdb structures/7BLD/7bld_ligand.sdf structures/7BLD/7bld_ligand.pdb structures/7BLD/7bld_ligand.cif structures/7BLD/7bld_complex.pdb structures/7BLD/7bld_complex.cif 7BM4 classic alpha carbonic anhydrase from Schistosoma mansoni (SmCA) Schistosoma mansoni recombinant SmCA Na compound 8; 1-(4-fluorophenyl)-3-(4-sulfamoylphenyl)selenourea "[""U3N""]" 1 Ki Ki = = 76.8 nM 76.8 [] unit_conversion 7.114638779968488 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay using recombinant SmCA; Table 1. 3 Table 1 reports Ki = 76.8 nM for compound 8 against SmCA; the text identifies recombinant SmCA and the stopped-flow assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7BM4\7BM4_metadata.json point structures/7BM4/7bm4_protein.pdb structures/7BM4/7bm4_pocket.pdb structures/7BM4/7bm4_ligand.sdf structures/7BM4/7bm4_ligand.pdb structures/7BM4/7bm4_ligand.cif structures/7BM4/7bm4_complex.pdb structures/7BM4/7bm4_complex.cif 7BMG classic MDM2 human MDM2 residues 17–109 E69A; K70A compound 5 "[""U3Z""]" 1 IC50 IC50 = = 0.011 µM 11.0 [] unit_conversion 7.958607314841775 success True biochemical_inhibition MDM2-p53 ELISA inhibition assay. 44 The official Supporting Information maps 7BMG to compound 5 and its crystallization construct; the main-text table reports ELISA IC50 0.011 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BMG\7BMG_metadata.json point structures/7BMG/7bmg_protein.pdb structures/7BMG/7bmg_pocket.pdb structures/7BMG/7bmg_ligand.sdf structures/7BMG/7bmg_ligand.pdb structures/7BMG/7bmg_ligand.cif structures/7BMG/7bmg_complex.pdb structures/7BMG/7bmg_complex.cif 7BN1 extended Clathrin heavy chain N-terminal domain Na Clathrin heavy chain N-terminal domain Na mu-NS705-720 peptide from Reovirus type 1 (MRV1) "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 32 μM 32000.0 [] unit_conversion 4.494850021680094 success True direct_binding Fluorescence-polarization monitored affinity measurement of peptide binding to CLTC NTD. 8 Fig. 5D lists mu-NS705-720 (MRV1) with Kd 32 μM; the figure legend identifies FP-monitored affinity measurements. Page 14 identifies mu-NS705-720 as one of the CLTC NTD crystallization peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7BN1\7BN1_metadata.json point structures/7BN1/7bn1_protein.pdb structures/7BN1/7bn1_pocket.pdb structures/7BN1/7bn1_ligand.pdb structures/7BN1/7bn1_ligand.cif structures/7BN1/7bn1_complex.pdb structures/7BN1/7bn1_complex.cif 7BN2 extended Clathrin heavy chain N-terminal domain Na Clathrin heavy chain N-terminal domain Na Nsp3 1765-1780 peptide from Eastern equine encephalitis virus (EEEV) "[""CHAIN:CCC"", ""CHAIN:DDD""]" 1 Kd Kd = = 27 μM 27000.0 [] unit_conversion 4.568636235841013 success True direct_binding Fluorescence-polarization monitored affinity measurement of peptide binding to CLTC NTD. 8 Fig. 5D lists Nsp3 1765-1780 (EEEV) with Kd 27 μM; the figure legend identifies FP-monitored affinity measurements. Page 14 identifies Nsp3 1765-1780 as one of the CLTC NTD crystallization peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7BN2\7BN2_metadata.json point structures/7BN2/7bn2_ligand.cif structures/7BN2/7bn2_complex.cif 7BN3 extended PABPC1 (PABP1) C-terminal domain Human C-terminal domain of PABPC1 Na N351-366 peptide from Human coronavirus 229E nucleoprotein (HCoV 229E) "[""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 23 μM 23000.0 [] unit_conversion 4.638272163982407 success True direct_binding Fluorescence-polarization monitored affinity measurement of peptide binding to PABP1 PABC. 10 Fig. 6C lists N351-366 (HCoV 229E) with Kd 23 μM; the legend identifies FP-monitored affinity measurements. Page 14 states that the PABPC1 PABC domain was crystallized with the N351-366 peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7BN3\7BN3_metadata.json point structures/7BN3/7bn3_protein.pdb structures/7BN3/7bn3_pocket.pdb structures/7BN3/7bn3_ligand.pdb structures/7BN3/7bn3_ligand.cif structures/7BN3/7bn3_complex.pdb structures/7BN3/7bn3_complex.cif 7BO3 classic Human butyrylcholinesterase (hBChE) Human Recombinant hBChE devoid of its C-terminal end and engineered to remove four N-glycosylation sites, produced in Chinese hamster ovary cells Na Compound 17; N-(2-(1H-indol-3-yl)ethyl)-2-cycloheptyl-N-methylethan-1-amine "[""IA4""]" 1 IC50 IC50 = = 1.9 ± 0.3 nM 1.9 [] unit_conversion 8.721246399047171 success True biochemical_inhibition In vitro ChE inhibition assay; Table 1. 6 Table 1 reports compound 17 hBChE IC50 = 1.9 ± 0.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7BO3\7BO3_metadata.json point structures/7BO3/7bo3_protein.pdb structures/7BO3/7bo3_pocket.pdb structures/7BO3/7bo3_ligand.sdf structures/7BO3/7bo3_ligand.pdb structures/7BO3/7bo3_ligand.cif structures/7BO3/7bo3_complex.pdb structures/7BO3/7bo3_complex.cif 7BPH extended GNAS (G alpha s) Homo sapiens (human) Short isoform, residues 7-380 Wild type (WT) GN13 "[""CHAIN:B""]" 1 Kd Kd = = 0.19 ± 0.02 µM 190.0 [] unit_conversion 6.721246399047171 success True direct_binding Bio-layer interferometry of GN13 binding to Gαs/GNP. 3 “GN13 binds to Gαs/GNP with a KD value of 0.19 ± 0.02 µM.” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7BPH\7BPH_metadata.json point structures/7BPH/7bph_protein.pdb structures/7BPH/7bph_pocket.pdb structures/7BPH/7bph_ligand.pdb structures/7BPH/7bph_ligand.cif structures/7BPH/7bph_complex.pdb structures/7BPH/7bph_complex.cif 7BPI classic PDE10A Na Na Na 14 "[""DZU""]" 1 IC50 IC50 = = 2.8 ± 0.1 nmol/L 2.8 [] unit_conversion 8.55284196865778 success True biochemical_inhibition In vitro enzymatic inhibition assay using purified PDE10A catalytic domain (449–770); Table 1 values are means ± SD (n=3). 4 Table 1 reports compound 14 with PDE10A IC50 = 2.8 ± 0.1 nmol/L. The paper maps PDB 7BPI to the PDE10A–14 crystal complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7BPI\7BPI_metadata.json point structures/7BPI/7bpi_protein.pdb structures/7BPI/7bpi_pocket.pdb structures/7BPI/7bpi_ligand.sdf structures/7BPI/7bpi_ligand.pdb structures/7BPI/7bpi_ligand.cif structures/7BPI/7bpi_complex.pdb structures/7BPI/7bpi_complex.cif 7C2Z classic Bromodomain-containing 4 (BRD4) human BRD4-BD1 with an N-terminal His-tag and thrombin cleavage site Na 3478 (3',4',7,8-tetrahydroxyflavone) "[""SQH""]" 1 IC50 IC50 = = 17.9 µM 17900.0 [] unit_conversion 4.747146969020107 success True biochemical_inhibition 10-dose AlphaScreen compound–protein interaction assay using recombinant human N-terminal His-tagged BRD4-BD1 and a biotinylated histone H4 peptide ligand. 6 Figure 1(C) and Results state that 3478 was tested by 10-dose AlphaScreen against BRD4-BD1 and BD2, with IC50=17.9 µM for BRD4-BD1. auto_single_measurement only accepted activity measurement [1] 1 structures\7C2Z\7C2Z_metadata.json point structures/7C2Z/7c2z_protein.pdb structures/7C2Z/7c2z_pocket.pdb structures/7C2Z/7c2z_ligand.sdf structures/7C2Z/7c2z_ligand.pdb structures/7C2Z/7c2z_ligand.cif structures/7C2Z/7c2z_complex.pdb structures/7C2Z/7c2z_complex.cif 7CA0 classic dihydroorotase (ScDHOase) Saccharomyces cerevisiae ScDHOase expressed from pET21b-ScDHOase Na 5-fluoroorotic acid (5-FOA) "[""FOT""]" 1 Kd Kd = = 83.8 ± 1.5 μM 83800.0 [] unit_conversion 4.076755981369724 success True direct_binding Purified ScDHOase fluorescence-quenching titration with 5-FOA; intrinsic fluorescence measured at 324 nm upon 280 nm excitation. 7 Table 2 reports the Kd value for ScDHOase binding to 5-FOA as 83.8 ± 1.5 μM; the text identifies fluorescence quenching as the method used to determine ScDHOase binding to 5-FOA. auto_single_measurement only accepted activity measurement [1] 1 structures\7CA0\7CA0_metadata.json point structures/7CA0/7ca0_protein.pdb structures/7CA0/7ca0_pocket.pdb structures/7CA0/7ca0_ligand.sdf structures/7CA0/7ca0_ligand.pdb structures/7CA0/7ca0_ligand.cif structures/7CA0/7ca0_complex.pdb structures/7CA0/7ca0_complex.cif 7CA1 classic dihydroorotase (ScDHOase) Saccharomyces cerevisiae Na Na plumbagin (PLU) "[""90R""]" 1 Kd Kd = = 64.8 ± 1.6 µM 64800.0 [] unit_conversion 4.188424994129407 success True direct_binding Fluorescence-quenching titration of purified ScDHOase with PLU. 9 “The Kd value of ScDHOase bound to PLU was 64.8 ± 1.6 µM,” with Table 3 listing ScDHOase–PLU Kd 64.8 ± 1.6 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7CA1\7CA1_metadata.json point structures/7CA1/7ca1_protein.pdb structures/7CA1/7ca1_pocket.pdb structures/7CA1/7ca1_ligand.sdf structures/7CA1/7ca1_ligand.pdb structures/7CA1/7ca1_ligand.cif structures/7CA1/7ca1_complex.pdb structures/7CA1/7ca1_complex.cif 7CBJ classic PDE4D human Catalytic domain, residues 86-413, with an N-terminal 6x His tag Na compound 36 "[""FTX""]" 1 IC50 IC50 = = 0.36 ± 0.02 µM 360.0 [] unit_conversion 6.443697499232712 success True biochemical_inhibition PDE4D inhibition measured by scintillation proximity assay (SPA). 20 Table 3 reports compound 36 PDE4D IC50 = 0.36 ± 0.02 µM. The paper maps the PDE4D–compound 36 crystal complex to PDB 7CBJ. auto_single_measurement only accepted activity measurement [1] 1 structures\7CBJ\7CBJ_metadata.json point structures/7CBJ/7cbj_protein.pdb structures/7CBJ/7cbj_pocket.pdb structures/7CBJ/7cbj_ligand.sdf structures/7CBJ/7cbj_ligand.pdb structures/7CBJ/7cbj_ligand.cif structures/7CBJ/7cbj_complex.pdb structures/7CBJ/7cbj_complex.cif 7CBQ classic PDE4D human Catalytic domain, residues 86-413, with an N-terminal 6x His tag Na Apremilast "[""A9L""]" 1 IC50 IC50 = = 0.077 µM 77.0 [] unit_conversion 7.113509274827518 success True biochemical_inhibition PDE4D inhibition; the paper states the apremilast IC50 while comparing enzymatic inhibition with compounds 1 and 36. 24 The paper states that compound 36 was weaker against PDE4D than compound 1 and apremilast, giving IC50 values of 0.14 µM and 0.077 µM, respectively, for compound 1 and apremilast. It maps the PDE4D–apremilast complex to PDB 7CBQ. auto_single_measurement only accepted activity measurement [1] 1 structures\7CBQ\7CBQ_metadata.json point structures/7CBQ/7cbq_protein.pdb structures/7CBQ/7cbq_pocket.pdb structures/7CBQ/7cbq_ligand.sdf structures/7CBQ/7cbq_ligand.pdb structures/7CBQ/7cbq_ligand.cif structures/7CBQ/7cbq_complex.pdb structures/7CBQ/7cbq_complex.cif 7CCT classic Quinolone synthase (QNS) Aegle marmelos Correa Na Na N-Methylanthraniloyl-CoA (MANT-CoA) "[""FWC""]" 1 Kd Kd = = 2.04 nM 2.04 [] unit_conversion 8.6903698325741 success True direct_binding Surface plasmon resonance (SPR)-based assay of AmQNS with acyl-CoA substrates; Kd stated for N-methylanthraniloyl-CoA. 2 The paper states that SPR-based assays measured AmQNS binding and reports Kd values of 2.04 nM, 9.83 nM, and 7.30 nM for N-methylanthraniloyl-CoA, feruloyl-CoA, and hexanoyl-CoA, respectively. The paper maps MANT-CoA-bound AmQNS to PDB 7CCT. auto_single_measurement only accepted activity measurement [1] 1 structures\7CCT\7CCT_metadata.json point structures/7CCT/7cct_protein.pdb structures/7CCT/7cct_pocket.pdb structures/7CCT/7cct_ligand.sdf structures/7CCT/7cct_ligand.pdb structures/7CCT/7cct_ligand.cif structures/7CCT/7cct_complex.pdb structures/7CCT/7cct_complex.cif 7CCY classic hydroxymethylbilane synthase (HMBS) human Na Na 2-I-PBG (2-iodoporphobilinogen) "[""FWL""]" 1 Ki Ki = = 5.4 ± 0.3 μM 5400.0 [] unit_conversion 5.267606240177031 success True biochemical_inhibition Enzyme kinetic study measuring HMB formation as uroporphyrin I formation; Cornish–Bowden analysis reported noncompetitive inhibition of HMBS by 2-I-PBG (n=4). 7 “2-I-PBG inhibited the HMBS reaction in a noncompetitive manner, with a Ki value of 5.4 ± 0.3 μM (n = 4).” auto_single_measurement only accepted activity measurement [1] 1 structures\7CCY\7CCY_metadata.json point structures/7CCY/7ccy_protein.pdb structures/7CCY/7ccy_pocket.pdb structures/7CCY/7ccy_ligand.sdf structures/7CCY/7ccy_ligand.pdb structures/7CCY/7ccy_ligand.cif structures/7CCY/7ccy_complex.pdb structures/7CCY/7ccy_complex.cif 7CDC extended LSD1-CoREST Na Na Na peptide 3 (PRSFLVRRP) "[""CHAIN:C""]" 1 Ki Ki = = 0.18 ± 0.033 µM 180.0 [] unit_conversion 6.7447274948966935 success True biochemical_inhibition Peroxidase-coupled LSD1/CoREST inhibition assay; fitted with steady-state kinetics. 2 Table 1 reports peptide 3 (PRSFLVRRP), Ki = 0.18 ± 0.033 µM; the text states these Ki values for LSD1/CoREST inhibition were measured by a peroxidase-coupled reaction assay. Figure 2 identifies peptide 3 as PDB 7CDC. auto_single_measurement only accepted activity measurement [1] 1 structures\7CDC\7CDC_metadata.json point structures/7CDC/7cdc_protein.pdb structures/7CDC/7cdc_pocket.pdb structures/7CDC/7cdc_ligand.pdb structures/7CDC/7cdc_ligand.cif structures/7CDC/7cdc_complex.pdb structures/7CDC/7cdc_complex.cif 7CDD extended LSD1-CoREST Na Na Na peptide 4 (PRSFLVRR) "[""CHAIN:C""]" 1 Ki Ki = = 0.10 ± 0.0081 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition Peroxidase-coupled LSD1/CoREST inhibition assay; fitted with steady-state kinetics. 2 Table 1 reports peptide 4 (PRSFLVRR), Ki = 0.10 ± 0.0081 µM; the text states these Ki values for LSD1/CoREST inhibition were measured by a peroxidase-coupled reaction assay. Figure 2 identifies peptide 4 as PDB 7CDD. auto_single_measurement only accepted activity measurement [1] 1 structures\7CDD\7CDD_metadata.json point structures/7CDD/7cdd_protein.pdb structures/7CDD/7cdd_pocket.pdb structures/7CDD/7cdd_ligand.pdb structures/7CDD/7cdd_ligand.cif structures/7CDD/7cdd_complex.pdb structures/7CDD/7cdd_complex.cif 7CDE extended LSD1-CoREST Na Na Na peptide 5 (PRSFLVRKR) "[""CHAIN:C""]" 1 Ki Ki = = 0.10 ± 0.0046 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition Peroxidase-coupled LSD1/CoREST inhibition assay; fitted with steady-state kinetics. 2 Table 1 reports peptide 5 (PRSFLVRKR), Ki = 0.10 ± 0.0046 µM; the text states these Ki values for LSD1/CoREST inhibition were measured by a peroxidase-coupled reaction assay. Figure 2 identifies peptide 5 as PDB 7CDE. auto_single_measurement only accepted activity measurement [1] 1 structures\7CDE\7CDE_metadata.json point structures/7CDE/7cde_protein.pdb structures/7CDE/7cde_pocket.pdb structures/7CDE/7cde_ligand.pdb structures/7CDE/7cde_ligand.cif structures/7CDE/7cde_complex.pdb structures/7CDE/7cde_complex.cif 7CDF extended LSD1-CoREST Na Na Na peptide 6 (PRSFLVRRK) "[""CHAIN:C""]" 1 Ki Ki = = 0.0078 ± 0.0018 µM 7.8 [] unit_conversion 8.10790539730952 success True biochemical_inhibition Peroxidase-coupled LSD1/CoREST inhibition assay; fitted with steady-state kinetics. 2 Table 1 reports peptide 6 (PRSFLVRRK), Ki = 0.0078 ± 0.0018 µM; the text states these Ki values for LSD1/CoREST inhibition were measured by a peroxidase-coupled reaction assay. Figure 2 identifies peptide 6 as PDB 7CDF. auto_single_measurement only accepted activity measurement [1] 1 structures\7CDF\7CDF_metadata.json point structures/7CDF/7cdf_protein.pdb structures/7CDF/7cdf_pocket.pdb structures/7CDF/7cdf_ligand.pdb structures/7CDF/7cdf_ligand.cif structures/7CDF/7cdf_complex.pdb structures/7CDF/7cdf_complex.cif 7CDG extended LSD1-CoREST Na Na Na peptide 7 (PRSFLVRRR) "[""CHAIN:C""]" 1 Ki Ki = = 0.0053 ± 0.0013 µM 5.3 [] unit_conversion 8.275724130399212 success True biochemical_inhibition Peroxidase-coupled LSD1/CoREST inhibition assay; fitted with steady-state kinetics. 2 Table 1 reports peptide 7 (PRSFLVRRR), Ki = 0.0053 ± 0.0013 µM; the text states these Ki values for LSD1/CoREST inhibition were measured by a peroxidase-coupled reaction assay. Figure 2 identifies peptide 7 as PDB 7CDG. auto_single_measurement only accepted activity measurement [1] 1 structures\7CDG\7CDG_metadata.json point structures/7CDG/7cdg_protein.pdb structures/7CDG/7cdg_pocket.pdb structures/7CDG/7cdg_ligand.pdb structures/7CDG/7cdg_ligand.cif structures/7CDG/7cdg_complex.pdb structures/7CDG/7cdg_complex.cif 7CDW classic Mycobacterium tuberculosis elongation factor G1 (Mtb EF-G1) Mycobacterium tuberculosis Recombinant Mtb EF-G1 with a C-terminal His tag Na GDP "[""GDP""]" 1 Kd Kd = = 11.5 ± 0.3 μM 11500.0 [] unit_conversion 4.939302159646388 success True direct_binding Isothermal titration calorimetry (ITC), 25 °C; Mtb EF-G1 titrated with GDP. 3 “Mtb EF-G1 binds GDP with an apparent dissociation constant (Kd) of 11.5 ± 0.3 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7CDW\7CDW_metadata.json point structures/7CDW/7cdw_protein.pdb structures/7CDW/7cdw_pocket.pdb structures/7CDW/7cdw_ligand.sdf structures/7CDW/7cdw_ligand.pdb structures/7CDW/7cdw_ligand.cif structures/7CDW/7cdw_complex.pdb structures/7CDW/7cdw_complex.cif 7CFC extended Krimper Drosophila melanogaster eTud1 (residues 272-512) Na Ago3-2 peptide "[""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I""]" 1 Kd Kd = = 62.8 µM 62800.0 [] unit_conversion 4.2020403562628035 success True direct_binding Isothermal titration calorimetry (ITC) of purified Krimper eTud1 with Ago3-2 peptide. 3 “eTud1 binds to the Ago3-2 peptide ... with a binding affinity of 62.8 μM (Fig. 1f).” auto_single_measurement only accepted activity measurement [1] 1 structures\7CFC\7CFC_metadata.json point structures/7CFC/7cfc_protein.pdb structures/7CFC/7cfc_pocket.pdb structures/7CFC/7cfc_ligand.pdb structures/7CFC/7cfc_ligand.cif structures/7CFC/7cfc_complex.pdb structures/7CFC/7cfc_complex.cif 7CFI classic TpCorC Thermus parvatiensis TpCorC CBS domain, residues 202-361 Na ATP "[""ATP""]" 1 Kd Kd = = 0.46 ± 0.04 μM 460.0 [] unit_conversion 6.337242168318426 success True direct_binding Isothermal titration calorimetry (ITC) of the TpCorC CBS domain with ATP. 8 Fig. 8B prints Kd = 0.46 ± 0.04 μM for WT; the text identifies this as ATP binding by the TpCorC CBS domain. auto_single_measurement only accepted activity measurement [1] 1 structures\7CFI\7CFI_metadata.json point structures/7CFI/7cfi_protein.pdb structures/7CFI/7cfi_pocket.pdb structures/7CFI/7cfi_ligand.sdf structures/7CFI/7cfi_ligand.pdb structures/7CFI/7cfi_ligand.cif structures/7CFI/7cfi_complex.pdb structures/7CFI/7cfi_complex.cif 7CFK classic TpCorC (CorC) Thermus parvatensis CBS domain residues 183-361 C282A; T336I IGN95a "[""FX6""]" 1 Kd Kd = = 147.28 ± 18.35 µM 147280.0 [] unit_conversion 3.8318562245040413 success True direct_binding ITC measurement of TpCorC CBS-domain T336I mutant with IGN95a; the CBS constructs use C282A and the crystallized C282A/T336I construct is specified for 7CFK. 23 Table S1 reports for “T336I” TpCorC CBS with IGN95a: K_D 147.28 ± 18.35 µM. The resource table identifies the TpCorC 183–361 C282A/T336I CBS construct, and the crystallization methods specify the C282A/T336I construct with IGN95a. auto_single_measurement only accepted activity measurement [1] 1 structures\7CFK\7CFK_metadata.json point structures/7CFK/7cfk_protein.pdb structures/7CFK/7cfk_pocket.pdb structures/7CFK/7cfk_ligand.sdf structures/7CFK/7cfk_ligand.pdb structures/7CFK/7cfk_ligand.cif structures/7CFK/7cfk_complex.pdb structures/7CFK/7cfk_complex.cif 7CFP extended WDR5 human WDR5 residues 22-334, truncated construct Na H3Q5ser peptide "[""CHAIN:B""]" 1 Kd Kd = = 4.02 ± 0.39 μM 4019.9999999999995 [] unit_conversion 5.39577394691553 success True direct_binding Isothermal titration calorimetry (ITC) of recombinant WDR5^22–334 with H3Q5ser peptide. 3 Table 1 reports K_D = 4.02 ± 0.39 μM for WT WDR5^22–334 with the H3Q5ser H3_1–14 peptide; the text identifies the 7CFP structure as WDR5/H3Q5ser. auto_single_measurement only accepted activity measurement [1] 1 structures\7CFP\7CFP_metadata.json point structures/7CFP/7cfp_protein.pdb structures/7CFP/7cfp_pocket.pdb structures/7CFP/7cfp_ligand.pdb structures/7CFP/7cfp_ligand.cif structures/7CFP/7cfp_complex.pdb structures/7CFP/7cfp_complex.cif 7CFQ extended WDR5 human WDR5 residues 22-334, truncated construct Na H3K4me3Q5ser peptide "[""CHAIN:B""]" 1 Kd Kd = = 4.33 ± 0.30 μM 4330.0 [] unit_conversion 5.363512103646634 success True direct_binding Isothermal titration calorimetry (ITC) of recombinant WDR5^22–334 with H3K4me3Q5ser peptide. 3 Table 1 reports K_D = 4.33 ± 0.30 μM for WT WDR5^22–334 with the H3K4me3Q5ser H3_1–14 peptide; the text and Table 2 map the WDR5/H3K4me3Q5ser structure to 7CFQ. auto_single_measurement only accepted activity measurement [1] 1 structures\7CFQ\7CFQ_metadata.json point structures/7CFQ/7cfq_protein.pdb structures/7CFQ/7cfq_pocket.pdb structures/7CFQ/7cfq_ligand.pdb structures/7CFQ/7cfq_ligand.cif structures/7CFQ/7cfq_complex.pdb structures/7CFQ/7cfq_complex.cif 7CHM classic monopolar spindle kinase 1 (MPS1; TTK) kinase domain human MPS1 kinase domain spanning residues 515-795 Na compound 8 "[""FZF""]" 1 IC50 IC50 = = 3.2 ± 1.2 nM 3.2 [] unit_conversion 8.494850021680094 success True biochemical_inhibition MPS1 enzyme assay; Table 4 reports in vitro and PK profiles. 7 Table 4 lists compound 8 with MPS1 enzyme IC50 of 3.2 ± 1.2 nM. The experimental section identifies human TTK kinase for the kinase assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7CHM\7CHM_metadata.json point structures/7CHM/7chm_protein.pdb structures/7CHM/7chm_pocket.pdb structures/7CHM/7chm_ligand.sdf structures/7CHM/7chm_ligand.pdb structures/7CHM/7chm_ligand.cif structures/7CHM/7chm_complex.pdb structures/7CHM/7chm_complex.cif 7CHN classic monopolar spindle kinase 1 (MPS1; TTK) kinase domain human MPS1 kinase domain spanning residues 515-795 Na compound 9 "[""FZL""]" 1 IC50 IC50 = = 6.4 ± 0.7 nM 6.4 [] unit_conversion 8.193820026016112 success True biochemical_inhibition MPS1 enzyme assay; Table 4 reports in vitro and PK profiles. 7 Table 4 lists compound 9 with MPS1 enzyme IC50 of 6.4 ± 0.7 nM. The experimental section identifies human TTK kinase for the kinase assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7CHN\7CHN_metadata.json point structures/7CHN/7chn_protein.pdb structures/7CHN/7chn_pocket.pdb structures/7CHN/7chn_ligand.sdf structures/7CHN/7chn_ligand.pdb structures/7CHN/7chn_ligand.cif structures/7CHN/7chn_complex.pdb structures/7CHN/7chn_complex.cif 7CJG classic Porphyromonas gingivalis glutaminyl cyclase (PgQC) Porphyromonas gingivalis Na Na 5,6-dimethylbenzimidazole (56BI) "[""DMD""]" 2 Ki Ki = = 1.937 ± 0.231 µM 1937.0 [] unit_conversion 5.712870379280889 success True biochemical_inhibition Inhibition-constant measurement for 5,6-dimethylbenzimidazole with wild-type PgQC. 7 The text reports wild-type PgQC Ki = 1.937 ± 0.231 µM for 5,6-dimethylbenzimidazole. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7CJG\7CJG_metadata.json point structures/7CJG/7cjg_protein.pdb structures/7CJG/7cjg_pocket.pdb structures/7CJG/7cjg_ligand.sdf structures/7CJG/7cjg_ligand.pdb structures/7CJG/7cjg_ligand.cif structures/7CJG/7cjg_complex.pdb structures/7CJG/7cjg_complex.cif 7CKK classic FTO human FTO DeltaN31, with the N-terminal 31 residues truncated Na Dac51 "[""B6C""]" 1 IC50 IC50 = = 0.4 ± 0.1 μM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition HPLC-based inhibition assay of FTO-mediated demethylation of an m6A-containing 15-mer ssRNA using purified human FTO with the N-terminal 31 residues truncated. 9 Figure 5B visibly prints “IC50 = 0.4 ± 0.1 μM” for Dac51 inhibition of FTO. The methods specify the FTO demethylation assay and the matching truncated human FTO construct. auto_single_measurement only accepted activity measurement [1] 1 structures\7CKK\7CKK_metadata.json point structures/7CKK/7ckk_protein.pdb structures/7CKK/7ckk_pocket.pdb structures/7CKK/7ckk_ligand.sdf structures/7CKK/7ckk_ligand.pdb structures/7CKK/7ckk_ligand.cif structures/7CKK/7ckk_complex.pdb structures/7CKK/7ckk_complex.cif 7CMF classic human P-cadherin human REC12 (EC12 construct; monomer) arginine insertion at the N terminus of EC12 Hit 1; 2-(5-chloro-2-methyl-1H-indol-3-yl)ethan-1-amine "[""G60""]" 1 Kd Kd = = 916 µM 916000.0 [] unit_conversion 3.03810452633215 success True direct_binding SPR direct-binding dose-response assay using immobilized REC12 monomer mutant; approximate Kd calculated by Scatchard method. 3 “The approximate KD value of Hit 1 (Fig. 1d) for the monomer mutant was calculated to be 916 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7CMF\7CMF_metadata.json point structures/7CMF/7cmf_protein.pdb structures/7CMF/7cmf_pocket.pdb structures/7CMF/7cmf_ligand.sdf structures/7CMF/7cmf_ligand.pdb structures/7CMF/7cmf_ligand.cif structures/7CMF/7cmf_complex.pdb structures/7CMF/7cmf_complex.cif 7CNA extended Spindlin1/C11orf84 complex Na Spindlin1 residues 50-262 and C11orf84 residues 253-295 Na histone H3K4me3K9me3 peptide (A1-G12) "[""CHAIN:C""]" 1 Kd Kd = = 20 nM 20.0 [] unit_conversion 7.698970004336019 success True direct_binding ITC, Fig. 1f 3 Fig. 1f lists Kd = 20 nM for Spindlin1/C11orf84 binding to H3K4me3K9me3. auto_single_measurement only accepted activity measurement [1] 1 structures\7CNA\7CNA_metadata.json point structures/7CNA/7cna_protein.pdb structures/7CNA/7cna_pocket.pdb structures/7CNA/7cna_ligand.pdb structures/7CNA/7cna_ligand.cif structures/7CNA/7cna_complex.pdb structures/7CNA/7cna_complex.cif 7CPZ classic Streptavidin C1 Streptomyces cinnamonensis mature form, 191 amino acids Na D-biotin "[""BTN""]" 1 Kd Kd = = 3.06 ± 0.498 pM 0.0030600000000000002 [] unit_conversion 11.51427857351842 success True direct_binding Microscale thermophoresis dose–response measurement of recombinant fluorescently labelled streptavidin C1 binding D-biotin. 9 “The Kd of biotin binding to recombinant streptavidin C1 was about 3.06 ± 0.498 pM.” Figure 6(a) labels the same value for Streptavidin C1. auto_single_measurement only accepted activity measurement [1] 1 structures\7CPZ\7CPZ_metadata.json point structures/7CPZ/7cpz_protein.pdb structures/7CPZ/7cpz_pocket.pdb structures/7CPZ/7cpz_ligand.sdf structures/7CPZ/7cpz_ligand.pdb structures/7CPZ/7cpz_ligand.cif structures/7CPZ/7cpz_complex.pdb structures/7CPZ/7cpz_complex.cif 7CQH extended Drosophila TRP CBS2 and calmodulin C-lobe Drosophila Drosophila TRP CBS2 aa M899-D940; calmodulin C-lobe aa T79-K148 Na Drosophila TRP CBS2 peptide "[""CHAIN:A""]" 1 Kd Kd = = 0.25±0.03 μM 250.0 [] unit_conversion 6.6020599913279625 success True direct_binding ITC assay; CBS2 bound Ca2+-CaM with 1:1 stoichiometry. 8 “CBS2 also binds to Ca2+-CaM with a 1:1 stoichiometry and a Kd of 0.25±0.03 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7CQH\7CQH_metadata.json point structures/7CQH/7cqh_protein.pdb structures/7CQH/7cqh_pocket.pdb structures/7CQH/7cqh_ligand.pdb structures/7CQH/7cqh_ligand.cif structures/7CQH/7cqh_complex.pdb structures/7CQH/7cqh_complex.cif 7CQS classic 4-Hydroxyphenylpyruvate dioxygenase (AtHPPD) Arabidopsis thaliana Na Na Topramezone "[""GJL""]" 1 IC50 IC50 = = 0.140 μM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition HPPD activity/inhibition assay; the paper states Topramezone efficiency towards AtHPPD. 2 “Topramezone, with high efficiency towards AtHPPD (IC50 = 0.140 μM)”. auto_single_measurement only accepted activity measurement [1] 1 structures\7CQS\7CQS_metadata.json point structures/7CQS/7cqs_protein.pdb structures/7CQS/7cqs_pocket.pdb structures/7CQS/7cqs_ligand.sdf structures/7CQS/7cqs_ligand.pdb structures/7CQS/7cqs_ligand.cif structures/7CQS/7cqs_complex.pdb structures/7CQS/7cqs_complex.cif 7CQV extended Drosophila TRP CBS1 and calmodulin N-lobe Drosophila Drosophila TRP CBS1 aa T802-K862; calmodulin N-lobe aa A1-D78 Na Drosophila TRP CBS1 peptide "[""CHAIN:B""]" 1 Kd Kd = = 0.35±0.09 μM 350.0 [] unit_conversion 6.455931955649724 success True direct_binding ITC assay; CBS1 bound Ca2+-CaM with 1:1 stoichiometry. 8 “ITC-based assays showed that CBS1 binds to Ca2+-CaM with a Kd of 0.35±0.09 μM, and with a 1:1 stoichiometry.” auto_single_measurement only accepted activity measurement [1] 1 structures\7CQV\7CQV_metadata.json point structures/7CQV/7cqv_protein.pdb structures/7CQV/7cqv_pocket.pdb structures/7CQV/7cqv_ligand.pdb structures/7CQV/7cqv_ligand.cif structures/7CQV/7cqv_complex.pdb structures/7CQV/7cqv_complex.cif 7CRU extended hnRNPK Na NLS of hnRNPK Na Na "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 115 nM 115.0 [] unit_conversion 6.939302159646388 success True direct_binding ITC titration of Impα1 into the isolated hnRNPK NLS. 5 The text states that the isolated NLS (18–38) bound tightly to Impα1, and Fig. 3C prints Kd: 115 nM for “Impα1 to hnRNPK NLS.” auto_single_measurement only accepted activity measurement [1] 1 structures\7CRU\7CRU_metadata.json point structures/7CRU/7cru_protein.pdb structures/7CRU/7cru_pocket.pdb structures/7CRU/7cru_ligand.pdb structures/7CRU/7cru_ligand.cif structures/7CRU/7cru_complex.pdb structures/7CRU/7cru_complex.cif 7CTW classic Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) Plasmodium falciparum wild-type PfDHFR-TS wild-type fragment 820 "[""GEX""]" 1 IC50 IC50 = = 84 ± 5 µM 84000.0 [] unit_conversion 4.075720713938118 success True biochemical_inhibition PfDHFR activity assay with NADPH; IC50 determined from variable inhibitor concentrations fitted using the Hill equation. 6 Figure 5B reports fragment 820: IC50 84 ± 5 µM against WT PfDHFR. auto_single_measurement only accepted activity measurement [1] 1 structures\7CTW\7CTW_metadata.json point structures/7CTW/7ctw_protein.pdb structures/7CTW/7ctw_pocket.pdb structures/7CTW/7ctw_ligand.sdf structures/7CTW/7ctw_ligand.pdb structures/7CTW/7ctw_ligand.cif structures/7CTW/7ctw_complex.pdb structures/7CTW/7ctw_complex.cif 7CTY classic Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) Plasmodium falciparum wild-type PfDHFR-TS wild-type fragment 263 "[""GF3""]" 1 IC50 IC50 = = 28 ± 2 µM 28000.0 [] unit_conversion 4.552841968657781 success True biochemical_inhibition PfDHFR activity assay with NADPH; IC50 determined from variable inhibitor concentrations fitted using the Hill equation. 6 Figure 5B reports fragment 263: IC50 28 ± 2 µM against WT PfDHFR. auto_single_measurement only accepted activity measurement [1] 1 structures\7CTY\7CTY_metadata.json point structures/7CTY/7cty_protein.pdb structures/7CTY/7cty_pocket.pdb structures/7CTY/7cty_ligand.sdf structures/7CTY/7cty_ligand.pdb structures/7CTY/7cty_ligand.cif structures/7CTY/7cty_complex.pdb structures/7CTY/7cty_complex.cif 7CTZ classic Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) Plasmodium falciparum wild-type PfDHFR-TS wild-type fragment 148 "[""GF6""]" 1 IC50 IC50 = = 464 ± 32 µM 464000.0 [] unit_conversion 3.3334820194451193 success True biochemical_inhibition PfDHFR activity assay with NADPH; IC50 determined from variable inhibitor concentrations fitted using the Hill equation. 6 Figure 5B reports fragment 148: IC50 464 ± 32 µM against WT PfDHFR. auto_single_measurement only accepted activity measurement [1] 1 structures\7CTZ\7CTZ_metadata.json point structures/7CTZ/7ctz_protein.pdb structures/7CTZ/7ctz_pocket.pdb structures/7CTZ/7ctz_ligand.sdf structures/7CTZ/7ctz_ligand.pdb structures/7CTZ/7ctz_ligand.cif structures/7CTZ/7ctz_complex.pdb structures/7CTZ/7ctz_complex.cif 7CWA classic PDE8A Na PDE8A1 catalytic domain, residues 480-820, in pET15b expression construct Na clofarabine "[""CFB""]" 1 IC50 IC50 = = 0.12 µM 120.0 [] unit_conversion 6.920818753952375 success True biochemical_inhibition PDE8A inhibition; Figure 1 identifies the clofarabine-bound PDE8A structure as PDB 7CWA. 2 Figure 1 labels clofarabine “PDE8A: IC50 = 0.12 µM” and states that PDB ID 7CWA is the PDE8A–clofarabine crystal structure. auto_single_measurement only accepted activity measurement [1] 1 structures\7CWA\7CWA_metadata.json point structures/7CWA/7cwa_protein.pdb structures/7CWA/7cwa_pocket.pdb structures/7CWA/7cwa_ligand.sdf structures/7CWA/7cwa_ligand.pdb structures/7CWA/7cwa_ligand.cif structures/7CWA/7cwa_complex.pdb structures/7CWA/7cwa_complex.cif 7CWF classic PDE8A Na PDE8A1 catalytic domain, residues 480-820, in pET15b expression construct Na 2c "[""GJR""]" 1 IC50 IC50 = = 0.36 ± 0.01 µM 360.0 [] unit_conversion 6.443697499232712 success True biochemical_inhibition PDE8A inhibition; Table 1 reports targeted-compound inhibitory affinities. Figure 1 maps compound 2c to PDB 7CWF. 3 Table 1 reports for 2c, “IC50 (µM) 0.36 ± 0.01”; Figure 1 identifies 7CWF as the crystal structure of the PDE8A–2c complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7CWF\7CWF_metadata.json point structures/7CWF/7cwf_protein.pdb structures/7CWF/7cwf_pocket.pdb structures/7CWF/7cwf_ligand.sdf structures/7CWF/7cwf_ligand.pdb structures/7CWF/7cwf_ligand.cif structures/7CWF/7cwf_complex.pdb structures/7CWF/7cwf_complex.cif 7CWG classic PDE8A Na PDE8A1 catalytic domain, residues 480-820, in pET15b expression construct Na 3a "[""GJU""]" 1 IC50 IC50 = = 0.010 ± 0.001 µM 10.0 [] unit_conversion 8.0 success True biochemical_inhibition PDE8A inhibition; Table 1 reports targeted-compound inhibitory affinities. Figure 3 maps compound 3a to PDB 7CWG. 3 Table 1 reports for 3a/(S)-3, “IC50 (µM) 0.010 ± 0.001”; the paper identifies the 3a cocrystal as PDE8A–3a, PDB ID 7CWG. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\7CWG\7CWG_metadata.json point structures/7CWG/7cwg_protein.pdb structures/7CWG/7cwg_pocket.pdb structures/7CWG/7cwg_ligand.sdf structures/7CWG/7cwg_ligand.pdb structures/7CWG/7cwg_ligand.cif structures/7CWG/7cwg_complex.pdb structures/7CWG/7cwg_complex.cif 7CWH extended RACK7 PHD domain Na RACK7 PHD domain in complex with H3.3G34R(22-44) peptide H3.3G34R H3.3G34R peptide (residues 22-44) "[""CHAIN:A""]" 1 Kd Kd = = 5.67 ± 0.49 µM 5670.0 [] unit_conversion 5.246416941107094 success True direct_binding MST analysis of GST-tagged RACK7 PHD binding the H3.3G34R peptide; reported in the current work. 3 “PHD^RACK7 binds to H3.3G34R peptide with a dissociation constant (Kd) of 5.67 ± 0.49 µM (Fig 2a, supplemental table S3).” auto_single_measurement only accepted activity measurement [1] 1 structures\7CWH\7CWH_metadata.json point structures/7CWH/7cwh_protein.pdb structures/7CWH/7cwh_pocket.pdb structures/7CWH/7cwh_ligand.pdb structures/7CWH/7cwh_ligand.cif structures/7CWH/7cwh_complex.pdb structures/7CWH/7cwh_complex.cif 7CYL extended Karyopherin-beta2 Na Kapbeta2DeltaLoop with residues 337-367 replaced by a linker, in complex with FUS PY-NLS residues 475-526 P525L Na "[""CHAIN:B""]" 1 Kd Kd = = 180 [130–240] nM 180.0 [] unit_conversion 6.7447274948966935 success True direct_binding Isothermal titration calorimetry (ITC) measurement of Kapβ2 binding to FUS fragments. 3 Table 1 reports FUS PY-NLS (P525L), residues 475–526: K_D 180 [130–240] nM; the Results state the Kapβ2–FUS(P525L) PY-NLS complex has K_D = 180 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7CYL\7CYL_metadata.json point structures/7CYL/7cyl_protein.pdb structures/7CYL/7cyl_pocket.pdb structures/7CYL/7cyl_ligand.pdb structures/7CYL/7cyl_ligand.cif structures/7CYL/7cyl_complex.pdb structures/7CYL/7cyl_complex.cif 7CZM extended FIP200 human FIP200 residues 1490-1594 Na p-Optineurin LIR (SSEDpSFVEIRMAE) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 11.55±1.74 μM 11550.0 [] unit_conversion 4.937418015771837 success True direct_binding Fluorescence-polarization binding assay; one-site binding-model fit. 6 Fig. 3e reports: “p-Optineurin LIR, Kd = 11.55±1.74 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7CZM\7CZM_metadata.json point structures/7CZM/7czm_protein.pdb structures/7CZM/7czm_pocket.pdb structures/7CZM/7czm_ligand.pdb structures/7CZM/7czm_ligand.cif structures/7CZM/7czm_complex.pdb structures/7CZM/7czm_complex.cif 7D0E extended FIP200 human FIP200 residues 1490-1594 Na p-CCPG1 FIR2 (SDDpSDIVTLEPPK) "[""CHAIN:B""]" 1 Kd Kd = = 0.72±0.10 μM 720.0 [] unit_conversion 6.142667503568731 success True direct_binding Fluorescence-polarization binding assay; one-site binding-model fit. 3 Fig. 1b reports: “p-CCPG1 FIR2, Kd = 0.72±0.10 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7D0E\7D0E_metadata.json point structures/7D0E/7d0e_protein.pdb structures/7D0E/7d0e_pocket.pdb structures/7D0E/7d0e_ligand.pdb structures/7D0E/7d0e_ligand.cif structures/7D0E/7d0e_complex.pdb structures/7D0E/7d0e_complex.cif 7D1D classic glutaminyl cyclase Bacteroides thetaiotaomicron 4FUU construct, residues G23-K331 Na 1-benzylimidazole "[""1BN""]" 1 Ki Ki = = 2.1 ± 0.14 µM 2100.0 [] unit_conversion 5.6777807052660805 success True biochemical_inhibition Enzyme inhibition assay; Table 1 column BeI (1-benzylimidazole). 5 Table 1 reports B. thetaiotaomicron QC (PDB: 4FUU) Ki for BeI as 2.1 ± 0.14 µM; BeI is defined as 1-benzylimidazole. auto_single_measurement only accepted activity measurement [1] 1 structures\7D1D\7D1D_metadata.json point structures/7D1D/7d1d_protein.pdb structures/7D1D/7d1d_pocket.pdb structures/7D1D/7d1d_ligand.sdf structures/7D1D/7d1d_ligand.pdb structures/7D1D/7d1d_ligand.cif structures/7D1D/7d1d_complex.pdb structures/7D1D/7d1d_complex.cif 7D1E classic glutaminyl cyclase Bacteroides thetaiotaomicron 4FUU construct, residues G23-K331 Na N-acetylhistamine (N-omega-acetylhistamine) "[""AHN""]" 1 Ki Ki = = 59.3 ± 4.67 µM 59300.0 [] unit_conversion 4.226945306635737 success True biochemical_inhibition Enzyme inhibition assay; Table 1 column ACh (N-ω-acetylhistamine). 5 Table 1 reports B. thetaiotaomicron QC (PDB: 4FUU) Ki for ACh as 59.3 ± 4.67 µM; ACh is defined as N-ω-acetylhistamine. auto_single_measurement only accepted activity measurement [1] 1 structures\7D1E\7D1E_metadata.json point structures/7D1E/7d1e_protein.pdb structures/7D1E/7d1e_pocket.pdb structures/7D1E/7d1e_ligand.sdf structures/7D1E/7d1e_ligand.pdb structures/7D1E/7d1e_ligand.cif structures/7D1E/7d1e_complex.pdb structures/7D1E/7d1e_complex.cif 7D1V classic Hsp90 alpha mouse mHsp90ND, Hsp90alpha residues 9-225, N-terminal His6 tag Na 6c "[""GOU""]" 1 Kd Kd = = 0.68 µM 680.0 [] unit_conversion 6.167491087293763 success True direct_binding ITC, mHsp90ND at 25 °C; one-site binding model. 8 Table 3 reports K_D = 0.68 µM for compound 6c with mHsp90ND; the text identifies 6c as an ITC-tested compound. auto_single_measurement only accepted activity measurement [1] 1 structures\7D1V\7D1V_metadata.json point structures/7D1V/7d1v_protein.pdb structures/7D1V/7d1v_pocket.pdb structures/7D1V/7d1v_ligand.sdf structures/7D1V/7d1v_ligand.pdb structures/7D1V/7d1v_ligand.cif structures/7D1V/7d1v_complex.pdb structures/7D1V/7d1v_complex.cif 7D22 classic Hsp90 alpha mouse mHsp90ND, Hsp90alpha residues 9-225, N-terminal His6 tag Na 6b "[""GQ0""]" 1 Kd Kd = = 0.44 µM 440.0 [] unit_conversion 6.356547323513812 success True direct_binding ITC, mHsp90ND at 25 °C; one-site binding model. 8 Table 3 reports K_D = 0.44 µM for compound 6b with mHsp90ND. auto_single_measurement only accepted activity measurement [1] 1 structures\7D22\7D22_metadata.json point structures/7D22/7d22_protein.pdb structures/7D22/7d22_pocket.pdb structures/7D22/7d22_ligand.sdf structures/7D22/7d22_ligand.pdb structures/7D22/7d22_ligand.cif structures/7D22/7d22_complex.pdb structures/7D22/7d22_complex.cif 7D24 classic Hsp90 alpha mouse mHsp90ND, Hsp90alpha residues 9-225, N-terminal His6 tag Na 4b "[""GQ3""]" 1 Kd Kd = = 15.6 µM 15600.0 [] unit_conversion 4.806875401645539 success True direct_binding ITC, mHsp90ND at 25 °C; one-site binding model. 8 Table 3 reports K_D = 15.6 µM for compound 4b with mHsp90ND. auto_single_measurement only accepted activity measurement [1] 1 structures\7D24\7D24_metadata.json point structures/7D24/7d24_protein.pdb structures/7D24/7d24_pocket.pdb structures/7D24/7d24_ligand.sdf structures/7D24/7d24_ligand.pdb structures/7D24/7d24_ligand.cif structures/7D24/7d24_complex.pdb structures/7D24/7d24_complex.cif 7D25 classic Hsp90 alpha mouse mHsp90ND, Hsp90alpha residues 9-225, N-terminal His6 tag Na 14 "[""GQ6""]" 1 Kd Kd = = 0.41 µM 410.0 [] unit_conversion 6.3872161432802645 success True direct_binding ITC, mHsp90ND at 25 °C; one-site binding model. 8 Table 3 reports K_D = 0.41 µM for compound 14 with mHsp90ND. auto_single_measurement only accepted activity measurement [1] 1 structures\7D25\7D25_metadata.json point structures/7D25/7d25_protein.pdb structures/7D25/7d25_pocket.pdb structures/7D25/7d25_ligand.sdf structures/7D25/7d25_ligand.pdb structures/7D25/7d25_ligand.cif structures/7D25/7d25_complex.pdb structures/7D25/7d25_complex.cif 7D2V classic BACE1 Na Na Na compound 1 (verubecestat); N-{3-[(5R)-3-amino-2,5-dimethyl-1,1-dioxo-5,6-dihydro-2H-1lambda6,2,4-thiadiazin-5-yl]-4-fluorophenyl}-5-fluoropyridine-2-carboxamide "[""66F""]" 1 IC50 IC50 = = 1.9 nM 1.9 [] unit_conversion 8.721246399047171 success True biochemical_inhibition BACE1 FRET assay using APP-derived peptides. 2 Chart 1 prints “BACE1 FRET IC50: 1.9 nM” for compound 1 (verubecestat). auto_single_measurement only accepted activity measurement [1] 1 structures\7D2V\7D2V_metadata.json point structures/7D2V/7d2v_protein.pdb structures/7D2V/7d2v_pocket.pdb structures/7D2V/7d2v_ligand.sdf structures/7D2V/7d2v_ligand.pdb structures/7D2V/7d2v_ligand.cif structures/7D2V/7d2v_complex.pdb structures/7D2V/7d2v_complex.cif 7D2X classic BACE1 Na Na Na compound 3; N-{3-[(4R)-2-amino-4-(prop-1-yn-1-yl)-5,6-dihydro-4H-1,3-oxazin-4-yl]-4-fluorophenyl}-5-cyanopyridine-2-carboxamide "[""GTU""]" 1 IC50 IC50 = = 71 nM 71.0 [] unit_conversion 7.1487416512809245 success True biochemical_inhibition Biochemical FRET assay using APP-derived peptides. 3 Table 1 prints compound 3 BACE1 FRET IC50 of 71 nM; its footnote identifies a biochemical FRET assay using APP-derived peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7D2X\7D2X_metadata.json point structures/7D2X/7d2x_protein.pdb structures/7D2X/7d2x_pocket.pdb structures/7D2X/7d2x_ligand.sdf structures/7D2X/7d2x_ligand.pdb structures/7D2X/7d2x_ligand.cif structures/7D2X/7d2x_complex.pdb structures/7D2X/7d2x_complex.cif 7D35 extended human dynein light chain 8 (LC8) human recombinant human LC8 protein; homodimeric LC8 protomer Na Ebola virus VP35(67-76) peptide, K67TRNSQTQTD76 "[""CHAIN:B""]" 1 Kd Kd = = 3.91 µM 3910.0 [] unit_conversion 5.407823242604133 success True direct_binding ITC measurement of human LC8 with EBOV VP35(67–76) peptide; measurements performed at 25°C. 4 “The VP35(67–76) peptide that forms a stable complex with LC8 ... was shown to interact with the human protein with a dissociation constant (KD) of 3.91 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7D35\7D35_metadata.json point structures/7D35/7d35_protein.pdb structures/7D35/7d35_pocket.pdb structures/7D35/7d35_ligand.pdb structures/7D35/7d35_ligand.cif structures/7D35/7d35_complex.pdb structures/7D35/7d35_complex.cif 7D36 classic BACE1 human Na Na compound 11; N-{3-[(3S)-1-amino-5-fluoro-3-methyl-3,4-dihydro-2,6-naphthyridin-3-yl]-4-fluorophenyl}-5-cyano-3-methylpyridine-2-carboxamide "[""GUC""]" 1 IC50 IC50 = = 9.1 nM 9.1 [] unit_conversion 8.040958607678906 success True biochemical_inhibition Biochemical BACE1 IC50 determined by HTRF using an APP-derived peptide; values are mean values of at least two determinations. 3 Table 1 reports compound 11 (chiral, S) with BACE1 IC50 = 9.1 nM. The same page states that the X-ray cocrystal structure of compound 11 bound to BACE1 is PDB code 7D36. auto_single_measurement only accepted activity measurement [1] 1 structures\7D36\7D36_metadata.json point structures/7D36/7d36_protein.pdb structures/7D36/7d36_pocket.pdb structures/7D36/7d36_ligand.sdf structures/7D36/7d36_ligand.pdb structures/7D36/7d36_ligand.cif structures/7D36/7d36_complex.pdb structures/7D36/7d36_complex.cif 7D54 classic MsGATase Mycobacterium smegmatis Na Na glutamine (Gln) "[""GLN""]" 1 Kd Kd = = 3.1 ± 0.89 mM 3100000.0 [] unit_conversion 2.508638306165727 success True direct_binding Microscale thermophoresis direct-binding assay of MsGATase and glutamine. 8 The Results text reports MsGATase glutamine Kd 3.1 ± 0.89 mM, while the article header explicitly maps 7D54 to the MsGATase-glutamine complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7D54\7D54_metadata.json point structures/7D54/7d54_protein.pdb structures/7D54/7d54_pocket.pdb structures/7D54/7d54_ligand.sdf structures/7D54/7d54_ligand.pdb structures/7D54/7d54_ligand.cif structures/7D54/7d54_complex.pdb structures/7D54/7d54_complex.cif 7D5O classic C-Src chicken SRC residues 251-533 with an N-terminal 6xHis tag followed by a PreScission or TEV cleavage site Na TAS-120 "[""TZ0""]" 1 IC50 IC50 = = 1673 nM 1673.0 [] unit_conversion 5.776504059037606 success True biochemical_inhibition In vitro kinase assay against SRC; mean of n = 3 independent experiments. 4 Fig. 3a reports TAS-120 against SRC with IC50 = 1673 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7D5O\7D5O_metadata.json point structures/7D5O/7d5o_protein.pdb structures/7D5O/7d5o_pocket.pdb structures/7D5O/7d5o_ligand.sdf structures/7D5O/7d5o_ligand.pdb structures/7D5O/7d5o_ligand.cif structures/7D5O/7d5o_complex.pdb structures/7D5O/7d5o_complex.cif 7D6R extended Stx2a holotoxin Na Na Na MMA betaAla peptide (MMβA-mono) "[""CHAIN:G""]" 1 Kd Kd = = 0.05 µM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding AlphaScreen assay examining binding of MMβA-mono to the Stx2a A-subunit; reported as apparent Kd. 3 “The apparent Kd value of MMβA-mono for the A-subunit of Stx1a or Stx2a (0.032 or 0.05 µM, respectively)” auto_single_measurement only accepted activity measurement [1] 1 structures\7D6R\7D6R_metadata.json point structures/7D6R/7d6r_protein.pdb structures/7D6R/7d6r_pocket.pdb structures/7D6R/7d6r_ligand.pdb structures/7D6R/7d6r_ligand.cif structures/7D6R/7d6r_complex.pdb structures/7D6R/7d6r_complex.cif 7D87 extended zebrafish PHF14-PZP zebrafish PZP domain, residues 278-487 Na H3(1-25) "[""CHAIN:E""]" 1 Kd Kd = = 2.20 µM 2200.0 [] unit_conversion 5.657577319177793 success True direct_binding ITC binding of PHF14-PZP to H3(1-25). 5 “The H3(1–25)-PHF14PZP complex was successfully crystallized” after H3(1–25) “displayed decent binding with PHF14PZP at an affinity of 2.20 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7D87\7D87_metadata.json point structures/7D87/7d87_protein.pdb structures/7D87/7d87_pocket.pdb structures/7D87/7d87_ligand.pdb structures/7D87/7d87_ligand.cif structures/7D87/7d87_complex.pdb structures/7D87/7d87_complex.cif 7D9O classic recombinant human acetylcholinesterase human Na Na Compound 2 "[""H0L""]" 2 Kd Kd = = 2.78E-09 M 2.78 [] unit_conversion 8.555955204081924 success True direct_binding Surface plasmon resonance binding at 298.15 K; Table in Figure 2A. 5 Figure 2A reports for Compound 2: KD 2.78E-09 M; Figure 2 caption identifies SPR sensorgrams for compound binding to rhAChE. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7D9O\7D9O_metadata.json point structures/7D9O/7d9o_protein.pdb structures/7D9O/7d9o_pocket.pdb structures/7D9O/7d9o_ligand.sdf structures/7D9O/7d9o_ligand.pdb structures/7D9O/7d9o_ligand.cif structures/7D9O/7d9o_complex.pdb structures/7D9O/7d9o_complex.cif 7D9P classic recombinant human acetylcholinesterase human Na Na Compound 12 "[""H0R""]" 2 Kd Kd = = 3.50E-09 M 3.5 [] unit_conversion 8.455931955649724 success True direct_binding Surface plasmon resonance binding at 298.15 K; Table in Figure 2A. 5 Figure 2A reports for Compound 12: KD 3.50E-09 M; Figure 2 caption identifies SPR sensorgrams for compound binding to rhAChE. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7D9P\7D9P_metadata.json point structures/7D9P/7d9p_protein.pdb structures/7D9P/7d9p_pocket.pdb structures/7D9P/7d9p_ligand.sdf structures/7D9P/7d9p_ligand.pdb structures/7D9P/7d9p_ligand.cif structures/7D9P/7d9p_complex.pdb structures/7D9P/7d9p_complex.cif 7D9Q classic recombinant human acetylcholinesterase human Na Na Compound 7 "[""H1R""]" 2 Kd Kd = = 5.02E-09 M 5.02 [] unit_conversion 8.29929628285498 success True direct_binding Surface plasmon resonance binding at 298.15 K; Table in Figure 2A. 5 Figure 2A reports for Compound 7: KD 5.02E-09 M; Figure 2 caption identifies SPR sensorgrams for compound binding to rhAChE. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7D9Q\7D9Q_metadata.json point structures/7D9Q/7d9q_protein.pdb structures/7D9Q/7d9q_pocket.pdb structures/7D9Q/7d9q_ligand.sdf structures/7D9Q/7d9q_ligand.pdb structures/7D9Q/7d9q_ligand.cif structures/7D9Q/7d9q_complex.pdb structures/7D9Q/7d9q_complex.cif 7DAX classic Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14) Drosophila melanogaster Na Na TDP013 "[""H1X""]" 1 IC50 IC50 = = 8.94 ± 1.65 µM 8940.0 [] unit_conversion 5.048662481204082 success True biochemical_inhibition In vitro inhibition of DmNobo GSH-conjugation activity using 3,4-DNADCF; assay contained 1 mM GSH and was performed in duplicate. 3 Results explicitly report TDP013 IC50 = 8.94 ± 1.65 µM for DmNobo; the assay method specifies in vitro GSH-conjugation inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7DAX\7DAX_metadata.json point structures/7DAX/7dax_protein.pdb structures/7DAX/7dax_pocket.pdb structures/7DAX/7dax_ligand.sdf structures/7DAX/7dax_ligand.pdb structures/7DAX/7dax_ligand.cif structures/7DAX/7dax_complex.pdb structures/7DAX/7dax_complex.cif 7DAY classic Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14) Drosophila melanogaster Na Na TDP013 "[""H1X""]" 1 IC50 IC50 = = 8.94 ± 1.65 µM 8940.0 [] unit_conversion 5.048662481204082 success True biochemical_inhibition In vitro inhibition of DmNobo GSH-conjugation activity using 3,4-DNADCF; assay contained 1 mM GSH and was performed in duplicate. 3 Results explicitly report TDP013 IC50 = 8.94 ± 1.65 µM for DmNobo; the assay method specifies in vitro GSH-conjugation inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7DAY\7DAY_metadata.json point structures/7DAY/7day_protein.pdb structures/7DAY/7day_pocket.pdb structures/7DAY/7day_ligand.sdf structures/7DAY/7day_ligand.pdb structures/7DAY/7day_ligand.cif structures/7DAY/7day_complex.pdb structures/7DAY/7day_complex.cif 7DAZ classic Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14) Drosophila melanogaster Na Na TDP015 "[""H29""]" 1 IC50 IC50 = = 3.32 ± 0.81 µM 3320.0 [] unit_conversion 5.478861916295964 success True biochemical_inhibition In vitro inhibition of DmNobo GSH-conjugation activity using 3,4-DNADCF; assay contained 1 mM GSH and was performed in duplicate. 3 Results explicitly report TDP015 IC50 = 3.32 ± 0.81 µM for DmNobo. auto_single_measurement only accepted activity measurement [1] 1 structures\7DAZ\7DAZ_metadata.json point structures/7DAZ/7daz_protein.pdb structures/7DAZ/7daz_pocket.pdb structures/7DAZ/7daz_ligand.sdf structures/7DAZ/7daz_ligand.pdb structures/7DAZ/7daz_ligand.cif structures/7DAZ/7daz_complex.pdb structures/7DAZ/7daz_complex.cif 7DB0 classic Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14) Drosophila melanogaster Na Na dimedone (TDP045) "[""DC1""]" 1 IC50 IC50 > > 1000 µM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition In vitro inhibition of DmNobo GSH-conjugation activity using 3,4-DNADCF; assay contained 1 mM GSH and was performed in duplicate. 5 Figure 2 explicitly labels TDP045 IC50 > 1000 µM; Table 1 likewise reports >1000 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DB0\7DB0_metadata.json point structures/7DB0/7db0_protein.pdb structures/7DB0/7db0_pocket.pdb structures/7DB0/7db0_ligand.sdf structures/7DB0/7db0_ligand.pdb structures/7DB0/7db0_ligand.cif structures/7DB0/7db0_complex.pdb structures/7DB0/7db0_complex.cif 7DC7 classic D12 Fab anti-ATP antibody human Fab fragment of D12 Na ATP "[""ATP""]" 1 Kd Kd = = 31.6 ± 2.5 µM 31600.0 [] unit_conversion 4.5003129173815966 success True direct_binding Surface plasmon resonance measurement of clone D12 binding to ATP. 3 “surface plasmon resonance (SPR) showed that ... clone D12, bound to ATP with 31.6 ± 2.5 µM KD.” auto_single_measurement only accepted activity measurement [1] 1 structures\7DC7\7DC7_metadata.json point structures/7DC7/7dc7_protein.pdb structures/7DC7/7dc7_pocket.pdb structures/7DC7/7dc7_ligand.sdf structures/7DC7/7dc7_ligand.pdb structures/7DC7/7dc7_ligand.cif structures/7DC7/7dc7_complex.pdb structures/7DC7/7dc7_complex.cif 7DCF classic EHMT2 (G9a) Na Na Na compound 10 (DS79932728) "[""H30""]" 1 IC50 IC50 = = 12.6 ± 0.228 nM 12.6 [] unit_conversion 7.899629454882437 success True biochemical_inhibition G9a enzymatic inhibition; Table 2 reports mean of four technical replicates ± SEM. 3 Table 2 lists compound 10 (DS79932728): G9a IC50 = 12.6 ± 0.228 nM. Figure 2 identifies compound 10 bound to G9a as PDB 7DCF. auto_single_measurement only accepted activity measurement [1] 1 structures\7DCF\7DCF_metadata.json point structures/7DCF/7dcf_protein.pdb structures/7DCF/7dcf_pocket.pdb structures/7DCF/7dcf_ligand.sdf structures/7DCF/7dcf_ligand.pdb structures/7DCF/7dcf_ligand.cif structures/7DCF/7dcf_complex.pdb structures/7DCF/7dcf_complex.cif 7DCZ classic BACE1 (beta-site amyloid precursor protein cleaving enzyme 1) human Na Na N-{3-[(4S)-2-amino-4-methyl-4H-1,3-thiazin-4-yl]-4-fluorophenyl}-5-cyanopyridine-2-carboxamide (compound 1, atabecestat, JNJ-54861911) "[""H3C""]" 1 IC50 IC50 = = 9.8 ± 1.6 nM 9.8 [] unit_conversion 8.008773924307505 success True biochemical_inhibition Biochemical homogeneous time-resolved fluorescence (HTRF) BACE1 assay; Table 1, mean ± SD from triplicate data for compound 1. 3 Table 1 lists compound 1 with BACE1 (HTRF) IC50 of 9.8 ± 1.6 nM; footnote states BACE1 IC50 values were determined using a biochemical HTRF-based assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7DCZ\7DCZ_metadata.json point structures/7DCZ/7dcz_protein.pdb structures/7DCZ/7dcz_pocket.pdb structures/7DCZ/7dcz_ligand.sdf structures/7DCZ/7dcz_ligand.pdb structures/7DCZ/7dcz_ligand.cif structures/7DCZ/7dcz_complex.pdb structures/7DCZ/7dcz_complex.cif 7DD1 extended SRPK1 Na SRPK1DeltaNS3; residues 67-236 and 475-655 modeled Na 7-mer peptide (R-E-R-A-R-T-R) "[""CHAIN:B""]" 1 Kd Kd = = 112 ± 9.9 µM 112000.0 [] unit_conversion 3.950781977329818 success True direct_binding Isothermal titration calorimetry of the 7-mer peptide binding SRPK1. 4 “ITC experiments determined that the 7-mer peptide binds SRPK1 with a dissociation constant (Kd) of 112 ± 9.9 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7DD1\7DD1_metadata.json point structures/7DD1/7dd1_protein.pdb structures/7DD1/7dd1_pocket.pdb structures/7DD1/7dd1_ligand.pdb structures/7DD1/7dd1_ligand.cif structures/7DD1/7dd1_complex.pdb structures/7DD1/7dd1_complex.cif 7DDC classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na Tafenoquine (TFQ) "[""H3F""]" 1 IC50 IC50 = = 31.8 μM 31800.0 [] unit_conversion 4.497572880015567 success True biochemical_inhibition FRET dose-response assay of purified SARS-CoV-2 Mpro; TFQ was preincubated with 4 μM Mpro for 30 min at room temperature before fluorescent substrate addition. 3 Figure 1 caption explicitly states: “Dose–response curve of TFQ against SARS-CoV-2 Mpro with an IC50 value of 31.8 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7DDC\7DDC_metadata.json point structures/7DDC/7ddc_protein.pdb structures/7DDC/7ddc_pocket.pdb structures/7DDC/7ddc_ligand.sdf structures/7DDC/7ddc_ligand.pdb structures/7DDC/7ddc_ligand.cif structures/7DDC/7ddc_complex.pdb structures/7DDC/7ddc_complex.cif 7DDH classic Na+,K+-ATPase pig Na Na digoxin (DGX) "[""DGX""]" 1 Ki Ki = = 0.126 ± 0.003 µM 126.0 [] unit_conversion 6.899629454882437 success True biochemical_inhibition E2PPi·Mg2+ condition; Table 1 apparent inhibitor affinity. 3 Table 1 reports DGX Ki 0.126 ± 0.003 µM in E2PPi·Mg2+. auto_single_measurement only accepted activity measurement [1] 1 structures\7DDH\7DDH_metadata.json point structures/7DDH/7ddh_protein.pdb structures/7DDH/7ddh_pocket.pdb structures/7DDH/7ddh_ligand.sdf structures/7DDH/7ddh_ligand.pdb structures/7DDH/7ddh_ligand.cif structures/7DDH/7ddh_complex.pdb structures/7DDH/7ddh_complex.cif 7DDI classic Na+,K+-ATPase pig Na Na digitoxin (DTX) "[""F9R""]" 1 Ki Ki = = 0.17 ± 0.01 µM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition E2PPi·Mg2+ condition; Table 1 apparent inhibitor affinity. 3 Table 1 reports DTX Ki 0.17 ± 0.01 µM in E2PPi·Mg2+. auto_single_measurement only accepted activity measurement [1] 1 structures\7DDI\7DDI_metadata.json point structures/7DDI/7ddi_protein.pdb structures/7DDI/7ddi_pocket.pdb structures/7DDI/7ddi_ligand.sdf structures/7DDI/7ddi_ligand.pdb structures/7DDI/7ddi_ligand.cif structures/7DDI/7ddi_complex.pdb structures/7DDI/7ddi_complex.cif 7DDK classic Na+,K+-ATPase pig Na Na rostafuroxin (ROS) "[""E4R""]" 1 Ki Ki = = 234 ± 10 µM 234000.0 [] unit_conversion 3.6307841425898575 success True biochemical_inhibition E2PPi·Mg2+ condition; Table 1 apparent inhibitor affinity. 3 Table 1 reports ROS Ki 234 ± 10 µM in E2PPi·Mg2+. auto_single_measurement only accepted activity measurement [1] 1 structures\7DDK\7DDK_metadata.json point structures/7DDK/7ddk_protein.pdb structures/7DDK/7ddk_pocket.pdb structures/7DDK/7ddk_ligand.sdf structures/7DDK/7ddk_ligand.pdb structures/7DDK/7ddk_ligand.cif structures/7DDK/7ddk_complex.pdb structures/7DDK/7ddk_complex.cif 7DDL classic Na+,K+-ATPase pig Na Na bufalin (BUF) "[""BUF""]" 1 Ki Ki = = 0.125 ± 0.006 µM 125.0 [] unit_conversion 6.903089986991944 success True biochemical_inhibition E2PPi·Mg2+ condition; Table 1 apparent inhibitor affinity. 3 Table 1 reports BUF Ki 0.125 ± 0.006 µM in E2PPi·Mg2+. auto_single_measurement only accepted activity measurement [1] 1 structures\7DDL\7DDL_metadata.json point structures/7DDL/7ddl_protein.pdb structures/7DDL/7ddl_pocket.pdb structures/7DDL/7ddl_ligand.sdf structures/7DDL/7ddl_ligand.pdb structures/7DDL/7ddl_ligand.cif structures/7DDL/7ddl_complex.pdb structures/7DDL/7ddl_complex.cif 7DF5 classic Human Galectin-3 CRD human Na Na compound 45 "[""H5O""]" 1 IC50 IC50 = = 0.019 ± 0.005 μM 19.0 [] unit_conversion 7.721246399047171 success True biochemical_inhibition His-tagged recombinant human Gal-3 homogeneous time-resolved fluorescence (HTRF) competition/binding assay using biotin-ASF ligand. 7 Table 1 and Table 2 report compound 45 hGal-3 IC50 = 0.019 ± 0.005 μM; Figure 5 maps compound 45 bound to human Gal-3 to PDB 7DF5. auto_single_measurement only accepted activity measurement [1] 1 structures\7DF5\7DF5_metadata.json point structures/7DF5/7df5_protein.pdb structures/7DF5/7df5_pocket.pdb structures/7DF5/7df5_ligand.sdf structures/7DF5/7df5_ligand.pdb structures/7DF5/7df5_ligand.cif structures/7DF5/7df5_complex.pdb structures/7DF5/7df5_complex.cif 7DF6 classic Mouse Galectin-3 CRD mouse Na Na compound 45 "[""H5O""]" 1 IC50 IC50 = = 0.229 ± 0.067 μM 229.0 [] unit_conversion 6.6401645176601125 success True biochemical_inhibition His-tagged recombinant mouse Gal-3 homogeneous time-resolved fluorescence (HTRF) competition/binding assay using biotin-ASF ligand. 7 Table 1 and Table 2 report compound 45 mGal-3 IC50 = 0.229 ± 0.067 μM; Figure 5 maps compound 45 bound to mouse Gal-3 to PDB 7DF6. auto_single_measurement only accepted activity measurement [1] 1 structures\7DF6\7DF6_metadata.json point structures/7DF6/7df6_protein.pdb structures/7DF6/7df6_pocket.pdb structures/7DF6/7df6_ligand.sdf structures/7DF6/7df6_ligand.pdb structures/7DF6/7df6_ligand.cif structures/7DF6/7df6_complex.pdb structures/7DF6/7df6_complex.cif 7DFZ classic human NPC1L1 human N-terminally truncated hNPC1L1 (deltaN-hNPC1L1) Na ezetimibe (EZE) "[""H56""]" 1 Kd Kd = = 2.77 ± 0.68 μM 2770.0 [] unit_conversion 5.557520230935552 success True direct_binding Fluorescence-quenching EZE-binding affinity measurement. 6 Figure 3E explicitly reports Kd = 2.77 ± 0.68 μM for ΔN-NPC1L1; the Figure 3 caption identifies the ΔN-hNPC1L1-CLR-EZE structure as EZE-bound. auto_single_measurement only accepted activity measurement [1] 1 structures\7DFZ\7DFZ_metadata.json point structures/7DFZ/7dfz_protein.pdb structures/7DFZ/7dfz_pocket.pdb structures/7DFZ/7dfz_ligand.sdf structures/7DFZ/7dfz_ligand.pdb structures/7DFZ/7dfz_ligand.cif structures/7DFZ/7dfz_complex.pdb structures/7DFZ/7dfz_complex.cif 7DG4 classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 6 "[""H5R""]" 1 IC50 IC50 = = 20 ± 3 nM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 4 Table 1 reports compound 6 DYRK2 IC50 = 20 ± 3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DG4\7DG4_metadata.json point structures/7DG4/7dg4_protein.pdb structures/7DG4/7dg4_pocket.pdb structures/7DG4/7dg4_ligand.sdf structures/7DG4/7dg4_ligand.pdb structures/7DG4/7dg4_ligand.cif structures/7DG4/7dg4_complex.pdb structures/7DG4/7dg4_complex.cif 7DH9 classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 7 "[""H7F""]" 1 IC50 IC50 = = 13 ± 1 nM 13.0 [] unit_conversion 7.886056647693163 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 4 Table 1 reports compound 7 DYRK2 IC50 = 13 ± 1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DH9\7DH9_metadata.json point structures/7DH9/7dh9_protein.pdb structures/7DH9/7dh9_pocket.pdb structures/7DH9/7dh9_ligand.sdf structures/7DH9/7dh9_ligand.pdb structures/7DH9/7dh9_ligand.cif structures/7DH9/7dh9_complex.pdb structures/7DH9/7dh9_complex.cif 7DHC classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 10 "[""H99""]" 1 IC50 IC50 = = 522 ± 210 nM 522.0 [] unit_conversion 6.282329496997738 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 4 Table 1 reports compound 10 DYRK2 IC50 = 522 ± 210 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DHC\7DHC_metadata.json point structures/7DHC/7dhc_protein.pdb structures/7DHC/7dhc_pocket.pdb structures/7DHC/7dhc_ligand.sdf structures/7DHC/7dhc_ligand.pdb structures/7DHC/7dhc_ligand.cif structures/7DHC/7dhc_complex.pdb structures/7DHC/7dhc_complex.cif 7DHH classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 19 "[""H7L""]" 1 IC50 IC50 = = 23 ± 3 nM 23.0 [] unit_conversion 7.638272163982407 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 5 Table 1 reports compound 19 DYRK2 IC50 = 23 ± 3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DHH\7DHH_metadata.json point structures/7DHH/7dhh_protein.pdb structures/7DHH/7dhh_pocket.pdb structures/7DHH/7dhh_ligand.sdf structures/7DHH/7dhh_ligand.pdb structures/7DHH/7dhh_ligand.cif structures/7DHH/7dhh_complex.pdb structures/7DHH/7dhh_complex.cif 7DHK classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 13 "[""H7O""]" 1 IC50 IC50 = = 124 ± 27 nM 124.0 [] unit_conversion 6.906578314837764 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 5 Table 1 reports compound 13 DYRK2 IC50 = 124 ± 27 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DHK\7DHK_metadata.json point structures/7DHK/7dhk_protein.pdb structures/7DHK/7dhk_pocket.pdb structures/7DHK/7dhk_ligand.sdf structures/7DHK/7dhk_ligand.pdb structures/7DHK/7dhk_ligand.cif structures/7DHK/7dhk_complex.pdb structures/7DHK/7dhk_complex.cif 7DHL classic FGFR3 Na Na Na compound 11 "[""H6X""]" 1 IC50 IC50 = = 24 nM 24.0 [] unit_conversion 7.619788758288394 success True biochemical_inhibition Off-chip mobility shift enzyme inhibition assay against FGFR3. 6 Table 3 reports compound 11 enzyme FGFR3 IC50 = 24 nM; Fig. 5 identifies the FGFR3–compound 11 crystal structure as PDB 7DHL. auto_single_measurement only accepted activity measurement [1] 1 structures\7DHL\7DHL_metadata.json point structures/7DHL/7dhl_protein.pdb structures/7DHL/7dhl_pocket.pdb structures/7DHL/7dhl_ligand.sdf structures/7DHL/7dhl_ligand.pdb structures/7DHL/7dhl_ligand.cif structures/7DHL/7dhl_complex.pdb structures/7DHL/7dhl_complex.cif 7DHN classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 20 "[""H7R""]" 1 IC50 IC50 = = 1498 ± 104 nM 1498.0 [] unit_conversion 5.824488186636552 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 5 Table 1 reports compound 20 DYRK2 IC50 = 1498 ± 104 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DHN\7DHN_metadata.json point structures/7DHN/7dhn_protein.pdb structures/7DHN/7dhn_pocket.pdb structures/7DHN/7dhn_ligand.sdf structures/7DHN/7dhn_ligand.pdb structures/7DHN/7dhn_ligand.cif structures/7DHN/7dhn_complex.pdb structures/7DHN/7dhn_complex.cif 7DHO classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 14 "[""H7U""]" 1 IC50 IC50 = = 85 ± 17 nM 85.0 [] unit_conversion 7.070581074285707 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 5 Table 1 reports compound 14 DYRK2 IC50 = 85 ± 17 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DHO\7DHO_metadata.json point structures/7DHO/7dho_protein.pdb structures/7DHO/7dho_pocket.pdb structures/7DHO/7dho_ligand.sdf structures/7DHO/7dho_ligand.pdb structures/7DHO/7dho_ligand.cif structures/7DHO/7dho_complex.pdb structures/7DHO/7dho_complex.cif 7DHV classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 8 "[""H7X""]" 1 IC50 IC50 = = 342 ± 77 nM 342.0 [] unit_conversion 6.465973893943865 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 4 Table 1 reports compound 8 DYRK2 IC50 = 342 ± 77 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DHV\7DHV_metadata.json point structures/7DHV/7dhv_protein.pdb structures/7DHV/7dhv_pocket.pdb structures/7DHV/7dhv_ligand.sdf structures/7DHV/7dhv_ligand.pdb structures/7DHV/7dhv_ligand.cif structures/7DHV/7dhv_complex.pdb structures/7DHV/7dhv_complex.cif 7DJO classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 17 "[""H80""]" 1 IC50 IC50 = = 9 ± 2 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 5 Table 1 reports compound 17 DYRK2 IC50 = 9 ± 2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DJO\7DJO_metadata.json point structures/7DJO/7djo_protein.pdb structures/7DJO/7djo_pocket.pdb structures/7DJO/7djo_ligand.sdf structures/7DJO/7djo_ligand.pdb structures/7DJO/7djo_ligand.cif structures/7DJO/7djo_complex.pdb structures/7DJO/7djo_complex.cif 7DL6 classic DYRK2 Na DYRK2^208-552 with an N-terminal 6 x His affinity tag and TEV protease cleavage site Na compound 18 "[""H96""]" 1 IC50 IC50 = = 18 ± 2 nM 18.0 [] unit_conversion 7.7447274948966935 success True biochemical_inhibition In vitro ADP-Glo kinase assay with purified active DYRK2; Table 1 molecular-level IC50. 5 Table 1 reports compound 18 DYRK2 IC50 = 18 ± 2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DL6\7DL6_metadata.json point structures/7DL6/7dl6_protein.pdb structures/7DL6/7dl6_pocket.pdb structures/7DL6/7dl6_ligand.sdf structures/7DL6/7dl6_ligand.pdb structures/7DL6/7dl6_ligand.cif structures/7DL6/7dl6_complex.pdb structures/7DL6/7dl6_complex.cif 7DML classic OXA-48 carbapenemase Na Na Na (R)-4a; (R)-2-(1-hydroxy-1,3-dihydrobenzo[c][1,2]oxaborol-3-yl)acrylic acid "[""H9O""]" 1 IC50 IC50 = = 15.84 μM 15840.0 [] unit_conversion 4.800244822746525 success True biochemical_inhibition Purified recombinant β-lactamase inhibition; Table 2, Class D OXA-48. 3 Table 2 prints an IC50 of 15.84 μM for (R)-4a against Class D OXA-48. Page 4 maps the OXA-48:(R)-4a complex to PDB 7DML. auto_single_measurement only accepted activity measurement [1] 1 structures\7DML\7DML_metadata.json point structures/7DML/7dml_protein.pdb structures/7DML/7dml_pocket.pdb structures/7DML/7dml_ligand.sdf structures/7DML/7dml_ligand.pdb structures/7DML/7dml_ligand.cif structures/7DML/7dml_complex.pdb structures/7DML/7dml_complex.cif 7DMY classic BPTF bromodomain human BPTF bromodomain residues 2916-3037 with an N-terminal 6xHis tag and TEV cleavage site Na Cpd7 "[""HAF""]" 1 Kd Kd = = 750 nM 750.0 [] unit_conversion 6.1249387366083 success True direct_binding Isothermal titration calorimetry (ITC) with BPTF BRD. 2 Fig. 1 caption: “ITC curve of Cpd7 with BPTF BRD (KD = 750 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7DMY\7DMY_metadata.json point structures/7DMY/7dmy_protein.pdb structures/7DMY/7dmy_pocket.pdb structures/7DMY/7dmy_ligand.sdf structures/7DMY/7dmy_ligand.pdb structures/7DMY/7dmy_ligand.cif structures/7DMY/7dmy_complex.pdb structures/7DMY/7dmy_complex.cif 7DN4 classic BPTF bromodomain human BPTF bromodomain residues 2916-3037 with an N-terminal 6xHis tag and TEV cleavage site Na Cpd8 "[""JC3""]" 1 Kd Kd = = 428 nM 428.0 [] unit_conversion 6.368556230986828 success True direct_binding Isothermal titration calorimetry (ITC) with BPTF BRD. 2 Fig. 1 caption: “ITC analysis of Cpd8 with BPTF BRD (KD = 428 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7DN4\7DN4_metadata.json point structures/7DN4/7dn4_protein.pdb structures/7DN4/7dn4_pocket.pdb structures/7DN4/7dn4_ligand.sdf structures/7DN4/7dn4_ligand.pdb structures/7DN4/7dn4_ligand.cif structures/7DN4/7dn4_complex.pdb structures/7DN4/7dn4_complex.cif 7DNO extended WDR5 Na WDR5 residues 23-483; purification tag removed for crystallization Na D206115 (CRTLPFHEC) "[""CHAIN:C"", ""CHAIN:D""]" 1 Ki Ki = = 1.2 ± 0.04 µM 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding Fluorescence-polarization direct competitive binding assay against WDR5; results presented as mean ± standard error. 5 Table 4 reports Ki = 1.2 ± 0.04 µM for D206115-CRTLPFHEC targeting WDR5. The same page identifies D206115 as CRTLPFHEC; page 6 identifies the WDR5–D206115 cocrystal as PDB 7DNO. auto_single_measurement only accepted activity measurement [1] 1 structures\7DNO\7DNO_metadata.json point structures/7DNO/7dno_protein.pdb structures/7DNO/7dno_pocket.pdb structures/7DNO/7dno_ligand.pdb structures/7DNO/7dno_ligand.cif structures/7DNO/7dno_complex.pdb structures/7DNO/7dno_complex.cif 7DNU classic mRNA-decapping enzyme g5Rp African swine fever virus (ASFV) Recombinant wild-type g5Rp, residues 1-250, with an N-terminal His6 tag wild-type (WT) InsP6 "[""IHP""]" 1 Kd Kd = = 22.48 ± 9.27 µM 22480.0 [] unit_conversion 4.648203693102976 success True direct_binding Microscale thermophoresis (MST) measurement of g5Rp binding to InsP6; dissociation constant calculated from three independent replicates (mean ± standard deviation). 10 Figure 6A visibly reports “K_D = 22.48 ± 9.27 µM” for g5Rp with InsP6 measured by MST. auto_single_measurement only accepted activity measurement [1] 1 structures\7DNU\7DNU_metadata.json point structures/7DNU/7dnu_protein.pdb structures/7DNU/7dnu_pocket.pdb structures/7DNU/7dnu_ligand.sdf structures/7DNU/7dnu_ligand.pdb structures/7DNU/7dnu_ligand.cif structures/7DNU/7dnu_complex.pdb structures/7DNU/7dnu_complex.cif 7DNY classic human ABCB6 human ABCB6-DeltaTMD0, core residues 206-842 DeltaTMD0, deletion of the N-terminal TMD0 coproporphyrin III (CPIII) "[""HT9""]" 1 Kd Kd = = 8.2 ± 0.1 µM 8200.0 [] unit_conversion 5.086186147616283 success True direct_binding Microscale thermophoresis (MST) binding assay of CPIII with ABCB6-ΔTMD0. 9 “dissociation constant (14.1 ± 0.9 µM) for CPIII relative to ABCB6-ΔTMD0 (8.2 ± 0.1 µM)” auto_single_measurement only accepted activity measurement [1] 1 structures\7DNY\7DNY_metadata.json point structures/7DNY/7dny_protein.pdb structures/7DNY/7dny_pocket.pdb structures/7DNY/7dny_ligand.sdf structures/7DNY/7dny_ligand.pdb structures/7DNY/7dny_ligand.cif structures/7DNY/7dny_complex.pdb structures/7DNY/7dny_complex.cif 7DOC extended Zika virus NS2B-NS3 protease (bZiPro) Zika virus Unlinked NS2B-NS3 protease construct (bZiPro) Na compound 5 "[""CHAIN:I""]" 1 Ki Ki = = 50.2 ± 1.2 μM 50200.0 [] unit_conversion 4.29929628285498 success True biochemical_inhibition Inhibition of unlinked bZiPro using fluorescent substrate Bz-Nle-KRR-AMC; Ki calculated from IC50 values using Cheng–Prusoff relationships. 3 Table 1 reports compound 5, [H-Dap(CINA)-NH2] Cys-Gly-Lys-Arg-Lys-OH, with Ki = 50.2 ± 1.2 μM; the text states compounds were assessed using unlinked bZiPro and fluorescent substrate Bz-Nle-KRR-AMC. auto_single_measurement only accepted activity measurement [1] 1 structures\7DOC\7DOC_metadata.json point structures/7DOC/7doc_protein.pdb structures/7DOC/7doc_pocket.pdb structures/7DOC/7doc_ligand.pdb structures/7DOC/7doc_ligand.cif structures/7DOC/7doc_complex.pdb structures/7DOC/7doc_complex.cif 7DPP classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na myricetin "[""MYC""]" 1 IC50 IC50 = = 0.63 ± 0.01 μM 630.0 [] unit_conversion 6.200659450546418 success True biochemical_inhibition FRET-based protease assay using recombinant SARS-CoV-2 3CLpro. 3 Fig. 1b reports “Myricetin: IC50 = 0.63 ± 0.01 μM”; the caption identifies inhibition of SARS-CoV-2 3CLpro. auto_single_measurement only accepted activity measurement [1] 1 structures\7DPP\7DPP_metadata.json point structures/7DPP/7dpp_protein.pdb structures/7DPP/7dpp_pocket.pdb structures/7DPP/7dpp_ligand.sdf structures/7DPP/7dpp_ligand.pdb structures/7DPP/7dpp_ligand.cif structures/7DPP/7dpp_complex.pdb structures/7DPP/7dpp_complex.cif 7DRO extended PsnB (ATP-grasp ligase) Pleisocystis pacifica PsnB with PsnA2_14-38 precursor peptide; PsnB construct details not specified Na PsnA2_14-38 (minimal precursor, MP) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 1.2 ± 0.072 μM 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding Fluorescence anisotropy; one-site binding fit. 9 Supplementary Figure 4 prints “MP (one-site binding) (Kd = 1.2 ± 0.072 μM)”; Supplementary Table 2 maps 7DRO to the PsnB–PsnA2_14-38 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7DRO\7DRO_metadata.json point structures/7DRO/7dro_protein.pdb structures/7DRO/7dro_pocket.pdb structures/7DRO/7dro_ligand.pdb structures/7DRO/7dro_ligand.cif structures/7DRO/7dro_complex.pdb structures/7DRO/7dro_complex.cif 7DTM classic metallo-beta-lactamase IMP-1 Serratia marcescens Na WT/native IMP-1 citrate "[""FLC""]" 1 IC50 IC50 > > 5 mM 5000000.0 [] unit_conversion 2.3010299956639813 success True biochemical_inhibition Inhibition of IMP-1 enzymatic activity; the paper reports citrate as the parent comparator, with IC50 > 5 mM. 1 “The introduction of a benzyl group into citrate enhanced the inhibitory activity in comparison to citrate (IC50 > 5 mM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7DTM\7DTM_metadata.json point structures/7DTM/7dtm_protein.pdb structures/7DTM/7dtm_pocket.pdb structures/7DTM/7dtm_ligand.sdf structures/7DTM/7dtm_ligand.pdb structures/7DTM/7dtm_ligand.cif structures/7DTM/7dtm_complex.pdb structures/7DTM/7dtm_complex.cif 7DU4 extended MazF-mt9 toxin Mycobacterium tuberculosis (M. tb) MazF-mt9 toxin in complex with the 15-residue MazE-mt9 alpha4 peptide, Asp63-Gly77 Na MazE-mt9 alpha4 peptide, Asp63-Gly77, DEDREWEGTVGDGLG "[""CHAIN:Q""]" 1 Kd Kd = = 87 nM 87.0 [] unit_conversion 7.060480747381382 success True direct_binding ITC measurement of the synthesized 15-residue alpha4 peptide binding to MazF-mt9. 3 “We synthesized the α4-peptide (Asp63–Gly77) and measured its affinity to the toxin by ITC… the kd value was 87 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7DU4\7DU4_metadata.json point structures/7DU4/7du4_protein.pdb structures/7DU4/7du4_pocket.pdb structures/7DU4/7du4_ligand.pdb structures/7DU4/7du4_ligand.cif structures/7DU4/7du4_complex.pdb structures/7DU4/7du4_complex.cif 7DV6 classic transforming growth factor beta type II receptor (TGF-betaRII) Na Na Na compound 20 "[""HJF""]" 1 IC50 IC50 < < 0.0030 (90%) µM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Enzyme IC50, mean of three replicates (Table 3). 3 Table 3 reports compound 20 enzyme IC50 against TGF-βRII as <0.0030 (90%) µM; Figure 1 identifies the TGF-βRII cocrystal of compound 20 as PDB 7DV6. auto_single_measurement only accepted activity measurement [1] 1 structures\7DV6\7DV6_metadata.json point structures/7DV6/7dv6_protein.pdb structures/7DV6/7dv6_pocket.pdb structures/7DV6/7dv6_ligand.sdf structures/7DV6/7dv6_ligand.pdb structures/7DV6/7dv6_ligand.cif structures/7DV6/7dv6_complex.pdb structures/7DV6/7dv6_complex.cif 7DVD extended p53 DNA-binding domain human (Homo sapiens) His-tagged p53 residues 92-293; bound PUMA peptide GJ201 residues 136-150 Na PUMA peptide GJ201 "[""CHAIN:E""]" 1 Kd Kd = = 13 μM 13000.0 [] unit_conversion 4.886056647693163 success True direct_binding Isothermal titration calorimetry (ITC) of isolated recombinant p53 DBD with PUMA peptide GJ201 in vitro. 7 “Isothermal titration calorimetry (ITC) analysis revealed p53 DBD has high binding affinity for PUMA peptide (KD = 13 μM; Fig. 4A).” auto_single_measurement only accepted activity measurement [1] 1 structures\7DVD\7DVD_metadata.json point structures/7DVD/7dvd_protein.pdb structures/7DVD/7dvd_pocket.pdb structures/7DVD/7dvd_ligand.pdb structures/7DVD/7dvd_ligand.cif structures/7DVD/7dvd_complex.pdb structures/7DVD/7dvd_complex.cif 7DVP extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na H41A nsp4|5 peptidyl substrate "[""CHAIN:C""]" 1 Kd Kd = = 28.06 ± 2.70 µM 28060.0 [] unit_conversion 4.5519123333076585 success True direct_binding Microscale thermophoresis binding-affinity assay; data from three independent experiments presented as mean values with SD. 5 Fig. 4H reports H41A–nsp4|5 Kd = 28.06 ± 2.70 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DVP\7DVP_metadata.json point structures/7DVP/7dvp_protein.pdb structures/7DVP/7dvp_pocket.pdb structures/7DVP/7dvp_ligand.pdb structures/7DVP/7dvp_ligand.cif structures/7DVP/7dvp_complex.pdb structures/7DVP/7dvp_complex.cif 7DVR extended PefR Streptococcus agalactiae Na Na heme "[""HEM""]" 1 Kd Kd = = 610 nM 610.0 [] unit_conversion 6.214670164989233 success True direct_binding Isothermal titration calorimetry of hemin into apo-PefR; reported heme:PefR binding ratio 0.9. 5 “The dissociation constant (Kd) of heme from PefR was determined to be 610 nM using isothermal titration calorimetry (ITC).” auto_single_measurement only accepted activity measurement [1] 1 structures\7DVR\7DVR_metadata.json point structures/7DVR/7dvr_protein.pdb structures/7DVR/7dvr_pocket.pdb structures/7DVR/7dvr_ligand.pdb structures/7DVR/7dvr_ligand.cif structures/7DVR/7dvr_complex.pdb structures/7DVR/7dvr_complex.cif 7DVW extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na H41A nsp5|6 peptidyl substrate "[""CHAIN:C""]" 1 Kd Kd = = (2.73 ± 0.90) × 10^3 µM 2730000.0 [] unit_conversion 2.5638373529592435 success True direct_binding Microscale thermophoresis binding-affinity assay; data from three independent experiments presented as mean values with SD. 5 Fig. 4H reports H41A–nsp5|6 Kd = (2.73 ± 0.90) × 10^3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DVW\7DVW_metadata.json point structures/7DVW/7dvw_protein.pdb structures/7DVW/7dvw_pocket.pdb structures/7DVW/7dvw_ligand.pdb structures/7DVW/7dvw_ligand.cif structures/7DVW/7dvw_complex.pdb structures/7DVW/7dvw_complex.cif 7DVX extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na H41A nsp6|7 peptidyl substrate "[""CHAIN:C""]" 1 Kd Kd = = 41.15 ± 3.63 µM 41150.0 [] unit_conversion 4.385630160451711 success True direct_binding Microscale thermophoresis binding-affinity assay; data from three independent experiments presented as mean values with SD. 5 Fig. 4H reports H41A–nsp6|7 Kd = 41.15 ± 3.63 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DVX\7DVX_metadata.json point structures/7DVX/7dvx_protein.pdb structures/7DVX/7dvx_pocket.pdb structures/7DVX/7dvx_ligand.pdb structures/7DVX/7dvx_ligand.cif structures/7DVX/7dvx_complex.pdb structures/7DVX/7dvx_complex.cif 7DVY extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na H41A nsp9|10 peptidyl substrate "[""CHAIN:C""]" 1 Kd Kd = = 115.8 ± 9.12 µM 115800.0 [] unit_conversion 3.9362914406085823 success True direct_binding Microscale thermophoresis binding-affinity assay; data from three independent experiments presented as mean values with SD. 5 Fig. 4H reports H41A–nsp9|10 Kd = 115.8 ± 9.12 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DVY\7DVY_metadata.json point structures/7DVY/7dvy_protein.pdb structures/7DVY/7dvy_pocket.pdb structures/7DVY/7dvy_ligand.pdb structures/7DVY/7dvy_ligand.cif structures/7DVY/7dvy_complex.pdb structures/7DVY/7dvy_complex.cif 7DW0 extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na H41A nsp15|16 peptidyl substrate "[""CHAIN:C""]" 1 Kd Kd = = (1.53 ± 0.35) × 10^3 µM 1530000.0 [] unit_conversion 2.8153085691824016 success True direct_binding Microscale thermophoresis binding-affinity assay; data from three independent experiments presented as mean values with SD. 5 Fig. 4H reports H41A–nsp14|15 Kd = (1.53 ± 0.35) × 10^3 µM. The paper's data-availability mapping on page 8 assigns 7DW0 to H41A–nsp14|15, resolving the supplied sibling-title transposition. auto_single_measurement only accepted activity measurement [1] 1 structures\7DW0\7DW0_metadata.json point structures/7DW0/7dw0_protein.pdb structures/7DW0/7dw0_pocket.pdb structures/7DW0/7dw0_ligand.pdb structures/7DW0/7dw0_ligand.cif structures/7DW0/7dw0_complex.pdb structures/7DW0/7dw0_complex.cif 7DW6 extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na H41A nsp14|15 peptidyl substrate "[""CHAIN:C""]" 1 Kd Kd = = 262.4 ± 30.5 µM 262400.0 [] unit_conversion 3.581036169296377 success True direct_binding Microscale thermophoresis binding-affinity assay; data from three independent experiments presented as mean values with SD. 5 Fig. 4H reports H41A–nsp15|16 Kd = 262.4 ± 30.5 µM. The paper's data-availability mapping on page 8 assigns 7DW6 to H41A–nsp15|16, resolving the supplied sibling-title transposition. auto_single_measurement only accepted activity measurement [1] 1 structures\7DW6\7DW6_metadata.json point structures/7DW6/7dw6_protein.pdb structures/7DW6/7dw6_pocket.pdb structures/7DW6/7dw6_ligand.pdb structures/7DW6/7dw6_ligand.cif structures/7DW6/7dw6_complex.pdb structures/7DW6/7dw6_complex.cif 7DYD classic MERS-CoV nucleocapsid protein N MERS-CoV MERS-CoV N39-165 protein with a histidine tag Na P4-2; 5-Isopropoxy-1H-indole "[""EY3""]" 1 Kd Kd = = 13 ± 4.24 μM 13000.0 [] unit_conversion 4.886056647693163 success True direct_binding Fluorescent quenching assay of purified MERS-CoV N-NTD with P4-2. 7 “The values of binding constant (Kd) for MERS-CoV-N-NTD to ... P4-2 is found to be ... 13 ± 4.24 μM respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7DYD\7DYD_metadata.json point structures/7DYD/7dyd_protein.pdb structures/7DYD/7dyd_pocket.pdb structures/7DYD/7dyd_ligand.sdf structures/7DYD/7dyd_ligand.pdb structures/7DYD/7dyd_ligand.cif structures/7DYD/7dyd_complex.pdb structures/7DYD/7dyd_complex.cif 7DYT classic human JMJD5 human N-terminally His6-tagged JMJD5 residues 183-416 Na 20h; 5-((4-methoxybenzyl)amino)pyridine-2,4-dicarboxylic acid "[""HR3""]" 1 IC50 IC50 = = 0.5 ± 0.1 µM 500.0 [] unit_conversion 6.301029995663981 success True biochemical_inhibition SPE-MS inhibition assay of isolated recombinant human JMJD5; Table 2 reports mean ± SD from three independent runs. 7 Table 2, entry ix (20h), reports JMJD5 IC50 = 0.5 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DYT\7DYT_metadata.json point structures/7DYT/7dyt_protein.pdb structures/7DYT/7dyt_pocket.pdb structures/7DYT/7dyt_ligand.sdf structures/7DYT/7dyt_ligand.pdb structures/7DYT/7dyt_ligand.cif structures/7DYT/7dyt_complex.pdb structures/7DYT/7dyt_complex.cif 7DYU classic human JMJD5 human N-terminally His6-tagged JMJD5 residues 183-416 Na 20d; 5-((4-phenylbutyl)amino)pyridine-2,4-dicarboxylic acid "[""HR9""]" 1 IC50 IC50 = = 0.4 ± 0.2 µM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition SPE-MS inhibition assay of isolated recombinant human JMJD5; Table 2 reports mean ± SD from three independent runs. 7 Table 2, entry vi (20d), reports JMJD5 IC50 = 0.4 ± 0.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DYU\7DYU_metadata.json point structures/7DYU/7dyu_protein.pdb structures/7DYU/7dyu_pocket.pdb structures/7DYU/7dyu_ligand.sdf structures/7DYU/7dyu_ligand.pdb structures/7DYU/7dyu_ligand.cif structures/7DYU/7dyu_complex.pdb structures/7DYU/7dyu_complex.cif 7DYV classic human JMJD5 human N-terminally His6-tagged JMJD5 residues 183-416 Na 20a; 5-(benzylamino)pyridine-2,4-dicarboxylic acid "[""HRF""]" 1 IC50 IC50 = = 0.4 ± 0.1 µM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition SPE-MS inhibition assay of isolated recombinant human JMJD5; Table 2 reports mean ± SD from three independent runs. 7 Table 2, entry ii (20a), reports JMJD5 IC50 = 0.4 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DYV\7DYV_metadata.json point structures/7DYV/7dyv_protein.pdb structures/7DYV/7dyv_pocket.pdb structures/7DYV/7dyv_ligand.sdf structures/7DYV/7dyv_ligand.pdb structures/7DYV/7dyv_ligand.cif structures/7DYV/7dyv_complex.pdb structures/7DYV/7dyv_complex.cif 7DYW classic human JMJD5 human N-terminally His6-tagged JMJD5 residues 183-416 Na 20i; 5-((2-methoxybenzyl)amino)pyridine-2,4-dicarboxylic acid "[""HRL""]" 1 IC50 IC50 = = 0.7 ± 0.2 µM 700.0 [] unit_conversion 6.154901959985743 success True biochemical_inhibition SPE-MS inhibition assay of isolated recombinant human JMJD5; Table 2 reports mean ± SD from three independent runs. 7 Table 2, entry x (20i), reports JMJD5 IC50 = 0.7 ± 0.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DYW\7DYW_metadata.json point structures/7DYW/7dyw_protein.pdb structures/7DYW/7dyw_pocket.pdb structures/7DYW/7dyw_ligand.sdf structures/7DYW/7dyw_ligand.pdb structures/7DYW/7dyw_ligand.cif structures/7DYW/7dyw_complex.pdb structures/7DYW/7dyw_complex.cif 7DYX classic human JMJD5 human N-terminally His6-tagged JMJD5 residues 183-416 Na 20j; 5-((2-cyclopropylbenzyl)amino)pyridine-2,4-dicarboxylic acid "[""HRR""]" 1 IC50 IC50 = = 0.7 ± 0.1 µM 700.0 [] unit_conversion 6.154901959985743 success True biochemical_inhibition SPE-MS inhibition assay of isolated recombinant human JMJD5; Table 2 reports mean ± SD from three independent runs. 7 Table 2, entry xi (20j), reports JMJD5 IC50 = 0.7 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7DYX\7DYX_metadata.json point structures/7DYX/7dyx_protein.pdb structures/7DYX/7dyx_pocket.pdb structures/7DYX/7dyx_ligand.sdf structures/7DYX/7dyx_ligand.pdb structures/7DYX/7dyx_ligand.cif structures/7DYX/7dyx_complex.pdb structures/7DYX/7dyx_complex.cif 7DZM extended T18A TCR and HLA-B*81:01 Na Na Na HIV-1 Gag TL9 peptide (TPQDLNTML) "[""CHAIN:C""]" 1 Kd Kd = = 4.72±0.62 μM 4720.0 [] unit_conversion 5.326058001365912 success True direct_binding In vitro surface plasmon resonance; T18A TCR immobilized on a streptavidin-coated sensor chip and HLA-B*81:01–TL9 pMHC used as analyte. 25 Table 1 reports T18A Kd = 4.72±0.62 μM for B81-TL9; the table caption identifies this as measurement of TCR–pMHC affinity. auto_single_measurement only accepted activity measurement [1] 1 structures\7DZM\7DZM_metadata.json point structures/7DZM/7dzm_protein.pdb structures/7DZM/7dzm_pocket.pdb structures/7DZM/7dzm_ligand.pdb structures/7DZM/7dzm_ligand.cif structures/7DZM/7dzm_complex.pdb structures/7DZM/7dzm_complex.cif 7DZN extended T18A TCR and HLA-B*42:01 Na Na Na HIV-1 Gag TL9 peptide (TPQDLNTML) "[""CHAIN:C""]" 1 Kd Kd = = 46.1±5 μM 46100.0 [] unit_conversion 4.336299074610352 success True direct_binding In vitro surface plasmon resonance; T18A TCR immobilized on a streptavidin-coated sensor chip and HLA-B*42:01–TL9 pMHC used as analyte. 25 Table 1 reports T18A Kd = 46.1±5 μM for B42-TL9; the table caption identifies this as measurement of TCR–pMHC affinity. auto_single_measurement only accepted activity measurement [1] 1 structures\7DZN\7DZN_metadata.json point structures/7DZN/7dzn_protein.pdb structures/7DZN/7dzn_pocket.pdb structures/7DZN/7dzn_ligand.pdb structures/7DZN/7dzn_ligand.cif structures/7DZN/7dzn_complex.pdb structures/7DZN/7dzn_complex.cif 7E0B extended Sorting nexin 27 (SNX27) human SNX27 PDZ domain residues 40-135 with a C-terminal His6 tag Na human ACE2-PBM peptide, residues 799-805 (-DDVQTSF-COO-) "[""CHAIN:B""]" 1 Kd Kd ~ ~ 20 μM 20000.0 [] unit_conversion 4.698970004336019 success True direct_binding Isothermal titration calorimetry of synthesized human ACE2-PBM peptide with the SNX27 PDZ domain at 25 °C. 2 “ITC result shows ACE2-PBM directly engages the PDZ domain of SNX27 with a binding affinity of 20 μM (Kd).” auto_single_measurement only accepted activity measurement [1] 1 structures\7E0B\7E0B_metadata.json point structures/7E0B/7e0b_protein.pdb structures/7E0B/7e0b_pocket.pdb structures/7E0B/7e0b_ligand.pdb structures/7E0B/7e0b_ligand.cif structures/7E0B/7e0b_complex.pdb structures/7E0B/7e0b_complex.cif 7E0O classic human indoleamine 2,3-dioxygenase 1 (hIDO1) human truncated hIDO1 residues 12-403 with an N-terminal hexahistidine tag removed by TEV protease Na 6-Bromo-1H-indazol-4-amine (compound 1) "[""HS0""]" 3 Ki Ki = = 4.48 μM 4480.0 [] unit_conversion 5.3487219860018556 success True biochemical_inhibition Substrate-competitive kinetic analysis. 5 The text states that compound 1 displayed substrate-competitive inhibition and gives a calculated Ki of 4.48 μM for hIDO1. auto_metric_priority unique highest-priority metric family: Ki [3] 3 structures\7E0O\7E0O_metadata.json point structures/7E0O/7e0o_protein.pdb structures/7E0O/7e0o_pocket.pdb structures/7E0O/7e0o_ligand.sdf structures/7E0O/7e0o_ligand.pdb structures/7E0O/7e0o_ligand.cif structures/7E0O/7e0o_complex.pdb structures/7E0O/7e0o_complex.cif 7E0P classic human indoleamine 2,3-dioxygenase 1 (hIDO1) human truncated hIDO1 residues 12-403 with an N-terminal hexahistidine tag removed by TEV protease Na 4-(((6-Bromo-1H-indazol-4-yl)amino)methyl)phenol (compound 2) "[""HU0""]" 2 Ki Ki = = 2.98 μM 2980.0 [] unit_conversion 5.525783735923745 success True biochemical_inhibition Substrate-competitive kinetic analysis. 5 The text reports that compound 2 showed substrate-competitive inhibition, with Ki = 2.98 μM for hIDO1. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7E0P\7E0P_metadata.json point structures/7E0P/7e0p_protein.pdb structures/7E0P/7e0p_pocket.pdb structures/7E0P/7e0p_ligand.sdf structures/7E0P/7e0p_ligand.pdb structures/7E0P/7e0p_ligand.cif structures/7E0P/7e0p_complex.pdb structures/7E0P/7e0p_complex.cif 7E0Q classic human indoleamine 2,3-dioxygenase 1 (hIDO1) human truncated hIDO1 residues 12-403 with an N-terminal hexahistidine tag removed by TEV protease Na (1S,2R)-2-(((6-Bromo-1H-indazol-4-yl)amino)methyl)cyclohexan-1-ol (compound 22) "[""HU3""]" 1 IC50 IC50 = = 2.85 μM 2850.0 [] unit_conversion 5.54515513999149 success True biochemical_inhibition Table 2 enzyme inhibition determination. 8 Table 2 reports compound 22 hIDO1 IC50/LE as “2.85 / 0.41”; the IC50 unit is μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7E0Q\7E0Q_metadata.json point structures/7E0Q/7e0q_protein.pdb structures/7E0Q/7e0q_pocket.pdb structures/7E0Q/7e0q_ligand.sdf structures/7E0Q/7e0q_ligand.pdb structures/7E0Q/7e0q_ligand.cif structures/7E0Q/7e0q_complex.pdb structures/7E0Q/7e0q_complex.cif 7E0S classic human indoleamine 2,3-dioxygenase 1 (hIDO1) human truncated hIDO1 residues 12-403 with an N-terminal hexahistidine tag removed by TEV protease Na (1R,2S)-2-(((6-Bromo-1H-indazol-4-yl)amino)methyl)cyclohexan-1-ol (compound 23) "[""HU6""]" 1 IC50 IC50 = = 0.64 μM 640.0 [] unit_conversion 6.1938200260161125 success True biochemical_inhibition Table 2 enzyme inhibition determination. 8 Table 2 reports compound 23 hIDO1 IC50/LE as “0.64 / 0.46”; the IC50 unit is μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7E0S\7E0S_metadata.json point structures/7E0S/7e0s_protein.pdb structures/7E0S/7e0s_pocket.pdb structures/7E0S/7e0s_ligand.sdf structures/7E0S/7e0s_ligand.pdb structures/7E0S/7e0s_ligand.cif structures/7E0S/7e0s_complex.pdb structures/7E0S/7e0s_complex.cif 7E0T classic human indoleamine 2,3-dioxygenase 1 (hIDO1) human truncated hIDO1 residues 12-403 with an N-terminal hexahistidine tag removed by TEV protease Na (1R,2S)-2-(((5-Bromo-1H-indazol-4-yl)amino)methyl)cyclohexan-1-ol (compound 36) "[""HU9""]" 1 IC50 IC50 = = 1.23 μM 1230.0 [] unit_conversion 5.910094888560602 success True biochemical_inhibition Table 2 enzyme inhibition determination. 9 Table 2 reports compound 36 hIDO1 IC50/LE as “1.23 / 0.44”; the IC50 unit is μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7E0T\7E0T_metadata.json point structures/7E0T/7e0t_protein.pdb structures/7E0T/7e0t_pocket.pdb structures/7E0T/7e0t_ligand.sdf structures/7E0T/7e0t_ligand.pdb structures/7E0T/7e0t_ligand.cif structures/7E0T/7e0t_complex.pdb structures/7E0T/7e0t_complex.cif 7E0Z extended protein kinase A catalytic domain (PKAc) mouse PKAc expressed from pET-28a-HMT with an N-terminal His6-MBP-TEV tag; fusion tag removed before crystallization PLN wild-type (WT) PLN8-22 peptide "[""CHAIN:B""]" 1 Kd Kd = = 184 μM 184000.0 [] unit_conversion 3.735182176990463 success True direct_binding SPR binding of WT PLN peptide to immobilized PKAc in the presence of AMP-PNP; Figure 2A. 7 Figure 2A prints “WT PLN, K_D = 184 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7E0Z\7E0Z_metadata.json point structures/7E0Z/7e0z_protein.pdb structures/7E0Z/7e0z_pocket.pdb structures/7E0Z/7e0z_ligand.pdb structures/7E0Z/7e0z_ligand.cif structures/7E0Z/7e0z_complex.pdb structures/7E0Z/7e0z_complex.cif 7E11 extended protein kinase A catalytic domain (PKAc) mouse PKAc expressed from pET-28a-HMT with an N-terminal His6-MBP-TEV tag; fusion tag removed before crystallization PLN R9C PLN8-22 R9C peptide "[""CHAIN:B""]" 1 Kd Kd = = 750 μM 750000.0 [] unit_conversion 3.1249387366083 success True direct_binding SPR binding of R9C PLN peptide to immobilized PKAc in the presence of AMP-PNP; Figure 2B. 7 Figure 2B prints “R9C PLN, K_D = 750 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7E11\7E11_metadata.json point structures/7E11/7e11_protein.pdb structures/7E11/7e11_pocket.pdb structures/7E11/7e11_ligand.pdb structures/7E11/7e11_ligand.cif structures/7E11/7e11_complex.pdb structures/7E11/7e11_complex.cif 7E12 extended protein kinase A catalytic domain (PKAc) mouse PKAc expressed from pET-28a-HMT with an N-terminal His6-MBP-TEV tag; fusion tag removed before crystallization PLN A11E PLN8-22 A11E peptide "[""CHAIN:B""]" 1 Kd Kd = = 354 μM 354000.0 [] unit_conversion 3.4509967379742124 success True direct_binding SPR binding of A11E PLN peptide to immobilized PKAc in the presence of AMP-PNP; Figure 2E. 7 Figure 2E prints “A11E PLN, K_D = 354 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7E12\7E12_metadata.json point structures/7E12/7e12_protein.pdb structures/7E12/7e12_pocket.pdb structures/7E12/7e12_ligand.pdb structures/7E12/7e12_ligand.cif structures/7E12/7e12_complex.pdb structures/7E12/7e12_complex.cif 7E27 classic Plasmodium falciparum formate-nitrite transporter (PfFNT) Plasmodium falciparum Full-length PfFNT with an N-terminal Strep-tag (WSHPQFEK) Na MMV007839 "[""HV6""]" 1 Kd Kd = = 7.18 ± 1.91 nM 7.18 [] unit_conversion 8.143875555757699 success True direct_binding Isothermal titration calorimetry (ITC) binding assay using purified wild-type PfFNT and MMV007839; representative titration, repeated 3 times; reported as mean ± SD. 5 Fig. 2A prints “Kd = 7.18 ± 1.91 nM”; its caption identifies this as binding affinity between PfFNT and MMV007839. The Methods specify ITC with wild-type PfFNT and MMV007839. auto_single_measurement only accepted activity measurement [1] 1 structures\7E27\7E27_metadata.json point structures/7E27/7e27_protein.pdb structures/7E27/7e27_pocket.pdb structures/7E27/7e27_ligand.sdf structures/7E27/7e27_ligand.pdb structures/7E27/7e27_ligand.cif structures/7E27/7e27_complex.pdb structures/7E27/7e27_complex.cif 7E2S classic GUN4 Synechocystis sp. PCC 6803 Na Na biliverdin IXalpha "[""BLA""]" 1 Kd Kd = = 0.63 μM 630.0 [] unit_conversion 6.200659450546418 success True direct_binding ITC titration of BV to SyGUN4 in the absence of glycerol. 4 “The K_D value of SyGUN4 to BV is 0.63 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7E2S\7E2S_metadata.json point structures/7E2S/7e2s_protein.pdb structures/7E2S/7e2s_pocket.pdb structures/7E2S/7e2s_ligand.sdf structures/7E2S/7e2s_ligand.pdb structures/7E2S/7e2s_ligand.cif structures/7E2S/7e2s_complex.pdb structures/7E2S/7e2s_complex.cif 7E3U classic Pseudomonas aeruginosa dihydropyrimidinase Pseudomonas aeruginosa Na Na 5-AU (5-aminouracil) "[""WBU""]" 1 Kd Kd = = 97.7 ± 2.0 μM 97700.0 [] unit_conversion 4.0101054362812265 success True direct_binding Fluorescence-quenching titration of purified wild-type PaDHPase with 5-AU; Kd obtained from ΔF = ΔFmax − Kd(ΔF/[5-AU]). 7 Table 3 reports PaDHPase binding to 5-AU with a Kd value of 97.7 ± 2.0 μM; Figure 4 caption describes fluorescence titration and Kd determination. auto_single_measurement only accepted activity measurement [1] 1 structures\7E3U\7E3U_metadata.json point structures/7E3U/7e3u_protein.pdb structures/7E3U/7e3u_pocket.pdb structures/7E3U/7e3u_ligand.sdf structures/7E3U/7e3u_ligand.pdb structures/7E3U/7e3u_ligand.cif structures/7E3U/7e3u_complex.pdb structures/7E3U/7e3u_complex.cif 7E48 classic InhA (2-trans-enoyl-acyl carrier protein reductase) Mycobacterium tuberculosis InhA residues Gly3-Leu269; 267 residues modeled as a continuous polypeptide Na 3-nitropropanoic acid (3NP) "[""3NP""]" 1 IC50 IC50 = = 71.2 ± 2.79 μM 71200.0 [] unit_conversion 4.147520006363144 success True biochemical_inhibition InhA inhibition by 3NP; relative inhibition versus log inhibitor concentration, compared with triclosan. 2 “IC50 values for InhA inhibition by 3NP were determined… The IC50 value (71.2 ± 2.79 μM)…” auto_single_measurement only accepted activity measurement [1] 1 structures\7E48\7E48_metadata.json point structures/7E48/7e48_protein.pdb structures/7E48/7e48_pocket.pdb structures/7E48/7e48_ligand.sdf structures/7E48/7e48_ligand.pdb structures/7E48/7e48_ligand.cif structures/7E48/7e48_complex.pdb structures/7E48/7e48_complex.cif 7E4Q classic tubulin (alpha/beta-tubulin heterodimer) porcine T2R-TTL complex containing two tubulins, one RB3-SLD, and one TTL Na L-DM1-SMe "[""BKX""]" 1 Kd Kd = = 5.688 × 10−6 M 5688.0 [] unit_conversion 5.24504041227829 success True direct_binding Biacore SPR binding-affinity assay with immobilized tubulin; equilibrium dissociation constant. 4 “The binding affinity (KD = 5.688 × 10−6 M and 1.315 × 10−5 M, respectively)” for L-DM1-SMe and D-DM1-SMe. auto_single_measurement only accepted activity measurement [1] 1 structures\7E4Q\7E4Q_metadata.json point structures/7E4Q/7e4q_protein.pdb structures/7E4Q/7e4q_pocket.pdb structures/7E4Q/7e4q_ligand.sdf structures/7E4Q/7e4q_ligand.pdb structures/7E4Q/7e4q_ligand.cif structures/7E4Q/7e4q_complex.pdb structures/7E4Q/7e4q_complex.cif 7E4R classic tubulin (alpha/beta-tubulin heterodimer) porcine T2R-TTL complex containing two tubulins, one RB3-SLD, and one TTL Na D-DM1-SMe "[""HZ0""]" 1 Kd Kd = = 1.315 × 10−5 M 13150.000000000002 [] unit_conversion 4.881074247174223 success True direct_binding Biacore SPR binding-affinity assay with immobilized tubulin; equilibrium dissociation constant. 4 “The binding affinity (KD = 5.688 × 10−6 M and 1.315 × 10−5 M, respectively)” for L-DM1-SMe and D-DM1-SMe. auto_single_measurement only accepted activity measurement [1] 1 structures\7E4R\7E4R_metadata.json point structures/7E4R/7e4r_protein.pdb structures/7E4R/7e4r_pocket.pdb structures/7E4R/7e4r_ligand.sdf structures/7E4R/7e4r_ligand.pdb structures/7E4R/7e4r_ligand.cif structures/7E4R/7e4r_complex.pdb structures/7E4R/7e4r_complex.cif 7E6Q classic influenza A virus neuraminidase N5 Na Na Na 1e; 4'-phenyl-1,2,3-triazolylated oseltamivir carboxylate "[""HZF""]" 1 IC50 IC50 = = 12.93 ± 1.57 μM 12930.0 [] unit_conversion 4.888401475119606 success True biochemical_inhibition Purified N5 neuraminidase inhibition assay using MUNANA fluorescent substrate; values are mean ± SD of three experiments. 3 Table 1 reports compound 1e IC50 = 12.93 ± 1.57 μM against N5 (H12N5). Page 6 identifies PDB 7E6Q as the N5–1e complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7E6Q\7E6Q_metadata.json point structures/7E6Q/7e6q_protein.pdb structures/7E6Q/7e6q_pocket.pdb structures/7E6Q/7e6q_ligand.sdf structures/7E6Q/7e6q_ligand.pdb structures/7E6Q/7e6q_ligand.cif structures/7E6Q/7e6q_complex.pdb structures/7E6Q/7e6q_complex.cif 7E9Y classic eLACCO1 Thermus thermophilus TTHA0766 L-lactate-binding protein with cpGFP inserted between residues 191 and 192; N-TTHA0766 residues 1-191 and C-TTHA0766 residues 192-361 Asn439Asp; Lys142Arg L-lactate "[""2OP""]" 1 Kd Kd = = 4.1 µM 4100.0 [] unit_conversion 5.3872161432802645 success True direct_binding Purified eLACCO1 L-lactate titration; apparent dissociation constant. The paper states Ca2+ is required for biosensor function, and the protein-characterization buffers include CaCl2. 2 “The apparent dissociation constant (Kd) of eLACCO1 is 4.1 µM” for L-lactate. auto_single_measurement only accepted activity measurement [1] 1 structures\7E9Y\7E9Y_metadata.json point structures/7E9Y/7e9y_protein.pdb structures/7E9Y/7e9y_pocket.pdb structures/7E9Y/7e9y_ligand.sdf structures/7E9Y/7e9y_ligand.pdb structures/7E9Y/7e9y_ligand.cif structures/7E9Y/7e9y_complex.pdb structures/7E9Y/7e9y_complex.cif 7EA7 extended NAP1; GABARAP Na NAP1(6-16); GABARAP Na Na "[""CHAIN:C""]" 1 Kd Kd = = 5.1 ± 0.4 μM 5100.0 [] unit_conversion 5.292429823902063 success True direct_binding Fluorescence-polarization assay measuring NAP1(6-16) binding to GABARAP. 11 Fig. 7B reports Kd = 5.1 ± 0.4 μM for NAP1 FIR with GABARAP; Fig. 7C identifies the NAP1 construct as NAP1(6-16). auto_single_measurement only accepted activity measurement [1] 1 structures\7EA7\7EA7_metadata.json point structures/7EA7/7ea7_protein.pdb structures/7EA7/7ea7_pocket.pdb structures/7EA7/7ea7_ligand.pdb structures/7EA7/7ea7_ligand.cif structures/7EA7/7ea7_complex.pdb structures/7EA7/7ea7_complex.cif 7EAX classic human p53-V272M human DNA-binding domain residues 94-293 V272M antimony ion (Sb) "[""SB""]" 1 Kd Kd = = 9.09 µM 9090.0 [] unit_conversion 5.041436116778033 success True direct_binding Surface plasmon resonance (SPR) binding of Sb ions to V272M DBD. 3 “According to surface plasmon resonance (SPR), Sb ions bound to V272M with a K_D of 9.09 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7EAX\7EAX_metadata.json point structures/7EAX/7eax_protein.pdb structures/7EAX/7eax_pocket.pdb structures/7EAX/7eax_ligand.sdf structures/7EAX/7eax_ligand.pdb structures/7EAX/7eax_ligand.cif structures/7EAX/7eax_complex.pdb structures/7EAX/7eax_complex.cif 7EBU classic Aedes aegypti Noppera-bo, glutathione S-transferase epsilon 8 Aedes aegypti Na Na daidzein "[""ZF1""]" 1 IC50 IC50 = = 3.87 ± 0.52 µM 3870.0 [] unit_conversion 5.412289034981089 success True biochemical_inhibition In-vitro GST GSH-conjugation inhibition assay using 3,4-DNADCF; assay contains GSH. 5 Table 1 reports daidzein IC50 to AeNobo-WT of 3.87 ± 0.52 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7EBU\7EBU_metadata.json point structures/7EBU/7ebu_protein.pdb structures/7EBU/7ebu_pocket.pdb structures/7EBU/7ebu_ligand.sdf structures/7EBU/7ebu_ligand.pdb structures/7EBU/7ebu_ligand.cif structures/7EBU/7ebu_complex.pdb structures/7EBU/7ebu_complex.cif 7EBV classic Aedes aegypti Noppera-bo, glutathione S-transferase epsilon 8 Aedes aegypti Na Na luteolin "[""LU2""]" 1 IC50 IC50 = = 3.99 ± 0.46 µM 3990.0 [] unit_conversion 5.399027104313252 success True biochemical_inhibition In-vitro GST GSH-conjugation inhibition assay using 3,4-DNADCF; assay contains GSH. 5 Table 1 reports luteolin IC50 to AeNobo-WT of 3.99 ± 0.46 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7EBV\7EBV_metadata.json point structures/7EBV/7ebv_protein.pdb structures/7EBV/7ebv_pocket.pdb structures/7EBV/7ebv_ligand.sdf structures/7EBV/7ebv_ligand.pdb structures/7EBV/7ebv_ligand.cif structures/7EBV/7ebv_complex.pdb structures/7EBV/7ebv_complex.cif 7EDQ classic Macrophage migration inhibitory factor (MIF) Na Na Na D7 (esculetin) "[""HFC""]" 2 Ki Ki = = 184 ± 8.51 µM 184000.0 [] unit_conversion 3.735182176990463 success True biochemical_inhibition Kinetic analysis of MIF inhibition; noncompetitive inhibitor. 3 Table 2 lists D7 with Ki 184 ± 8.51 µM and type Noncompetitive. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7EDQ\7EDQ_metadata.json point structures/7EDQ/7edq_protein.pdb structures/7EDQ/7edq_pocket.pdb structures/7EDQ/7edq_ligand.sdf structures/7EDQ/7edq_ligand.pdb structures/7EDQ/7edq_ligand.cif structures/7EDQ/7edq_complex.pdb structures/7EDQ/7edq_complex.cif 7EF1 extended ZmSHH2a SAWADEE domain Zea mays (maize) SAWADEE domain, residues 125-281 R235G H3(1-10)K9me1 peptide "[""CHAIN:P"", ""CHAIN:Q""]" 1 Kd Kd = = 4.31 μM 4310.0 [] unit_conversion 5.3655227298392685 success True direct_binding ITC binding assay 13 Table 1 reports R235G with H3(1-10)K9me1: Kd 4.31 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7EF1\7EF1_metadata.json point structures/7EF1/7ef1_protein.pdb structures/7EF1/7ef1_pocket.pdb structures/7EF1/7ef1_ligand.pdb structures/7EF1/7ef1_ligand.cif structures/7EF1/7ef1_complex.pdb structures/7EF1/7ef1_complex.cif 7EFQ classic human PPARgamma ligand binding domain Homo sapiens PPARgamma-LBD residues 204-477; expressed with an N-terminal 6xHis tag cleavable by TEV protease Na compound 2; rosiglitazone-based fluorescence probe "[""J3F""]" 1 Kd Kd = = 1558 ± 93.61 nM 1558.0 [] unit_conversion 5.807432546663454 success True direct_binding Fluorescence intensity at 410 nm of compound 2 (1 μM) measured after adding hPPARγ-LBD in Tris–HCl buffer; Kd derived from the binding curve. 6 “We calculated Kd using the fluorescence intensity at 410 nm (2: Kd = 1558 ± 93.61 nM, Figure 7b).” auto_single_measurement only accepted activity measurement [1] 1 structures\7EFQ\7EFQ_metadata.json point structures/7EFQ/7efq_protein.pdb structures/7EFQ/7efq_pocket.pdb structures/7EFQ/7efq_ligand.sdf structures/7EFQ/7efq_ligand.pdb structures/7EFQ/7efq_ligand.cif structures/7EFQ/7efq_complex.pdb structures/7EFQ/7efq_complex.cif 7EGU extended Nicotinamide N-methyltransferase (NNMT) human Na Na macrocyclic peptide X "[""CHAIN:B""]" 1 IC50 IC50 = = 12 nM 12.0 [] unit_conversion 7.920818753952375 success True biochemical_inhibition NNMT-mediated methylation of nicotinamide in the presence of SAM; h/m denotes human/mouse. 5 Figure 3 lists “Peptide X (R = Gly-NH2), IC50 (h/m) = 12 / 243 nM”; its caption identifies peptide X–NNMT as PDB 7EGU. auto_single_measurement only accepted activity measurement [1] 1 structures\7EGU\7EGU_metadata.json point structures/7EGU/7egu_protein.pdb structures/7EGU/7egu_pocket.pdb structures/7EGU/7egu_ligand.pdb structures/7EGU/7egu_ligand.cif structures/7EGU/7egu_complex.pdb structures/7EGU/7egu_complex.cif 7EGV classic Acetolactate synthase Trichoderma harzianum Na Na harzianic acid (HA, 1) "[""J3L""]" 1 Ki Ki = = 6.65 µM 6650.0 [] unit_conversion 5.1771783546968955 success True biochemical_inhibition Purified ThAHAS; HA was reported as a competitive inhibitor. 6 “HA was able to inhibit ThAHAS as a competitive inhibitor with a Ki of 6.65 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7EGV\7EGV_metadata.json point structures/7EGV/7egv_protein.pdb structures/7EGV/7egv_pocket.pdb structures/7EGV/7egv_ligand.sdf structures/7EGV/7egv_ligand.pdb structures/7EGV/7egv_ligand.cif structures/7EGV/7egv_complex.pdb structures/7EGV/7egv_complex.cif 7EHJ classic MTHFD2 human MTHFD2 residues 36-350 with an N-terminal 6xHis tag followed by a thrombin cleavage site Na compound 21 "[""J49""]" 1 IC50 IC50 = = 8.33 µM 8330.0 [] unit_conversion 5.079354998593212 success True biochemical_inhibition Human MTHFD2 enzymatic inhibition; compound 21 is described as a folate analogue with weak inhibition and substrate-site binding. 5 “21 is a folate analogue with weak inhibition (IC50 = 8.33 μM) and binds to the substrate-binding site.” auto_single_measurement only accepted activity measurement [1] 1 structures\7EHJ\7EHJ_metadata.json point structures/7EHJ/7ehj_protein.pdb structures/7EHJ/7ehj_pocket.pdb structures/7EHJ/7ehj_ligand.sdf structures/7EHJ/7ehj_ligand.pdb structures/7EHJ/7ehj_ligand.cif structures/7EHJ/7ehj_complex.pdb structures/7EHJ/7ehj_complex.cif 7EHM classic MTHFD2 human MTHFD2 residues 36-350 with an N-terminal 6xHis tag followed by a thrombin cleavage site Na compound 15 "[""J4C""]" 1 IC50 IC50 = = 0.78 µM 780.0 [] unit_conversion 6.107905397309519 success True biochemical_inhibition Human MTHFD2 enzyme inhibition assay; Table 1 values are means of three independent experiments. 4 Table 1, “Inhibition of MTHFD2 by Xanthine Derivatives,” reports compound 15: MTHFD2 IC50 0.78 μM; footnote: mean of three independent experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\7EHM\7EHM_metadata.json point structures/7EHM/7ehm_protein.pdb structures/7EHM/7ehm_pocket.pdb structures/7EHM/7ehm_ligand.sdf structures/7EHM/7ehm_ligand.pdb structures/7EHM/7ehm_ligand.cif structures/7EHM/7ehm_complex.pdb structures/7EHM/7ehm_complex.cif 7EHN classic MTHFD2 human MTHFD2 residues 36-350 with an N-terminal 6xHis tag followed by a thrombin cleavage site Na compound 9 "[""J4F""]" 1 IC50 IC50 = = 0.69 µM 690.0 [] unit_conversion 6.161150909262744 success True biochemical_inhibition Human MTHFD2 enzyme inhibition assay; Table 1 values are means of three independent experiments. 4 Table 1, “Inhibition of MTHFD2 by Xanthine Derivatives,” reports compound 9: MTHFD2 IC50 0.69 μM; footnote: mean of three independent experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\7EHN\7EHN_metadata.json point structures/7EHN/7ehn_protein.pdb structures/7EHN/7ehn_pocket.pdb structures/7EHN/7ehn_ligand.sdf structures/7EHN/7ehn_ligand.pdb structures/7EHN/7ehn_ligand.cif structures/7EHN/7ehn_complex.pdb structures/7EHN/7ehn_complex.cif 7EHP extended NagB1 Paenibacillus sp. str. FPU-7 Recombinant NagB1 lacking the N-terminal signal peptide Met1-Ser21 and residues Cys22-Phe48, with a C-terminal six-histidine tag Na (GlcNAc)2; N-acetyl-D-glucosamine disaccharide "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 0.173 µM 173.0 [] unit_conversion 6.761953896871205 success True direct_binding Surface plasmon resonance (Biacore X100), one-site binding-model fit. 6 Table 2 reports NagB1 binding to (GlcNAc)2 with KD = 0.173 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7EHP\7EHP_metadata.json point structures/7EHP/7ehp_protein.pdb structures/7EHP/7ehp_pocket.pdb structures/7EHP/7ehp_ligand.pdb structures/7EHP/7ehp_ligand.cif structures/7EHP/7ehp_complex.pdb structures/7EHP/7ehp_complex.cif 7EHQ extended NagB2 Paenibacillus sp. str. FPU-7 Recombinant NagB2 lacking the predicted N-terminal signal peptide Met1-Ala20, with a C-terminal six-histidine tag Na (GlcNAc)2; N-acetyl-D-glucosamine disaccharide "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 0.190 µM 190.0 [] unit_conversion 6.721246399047171 success True direct_binding Surface plasmon resonance (Biacore X100), one-site binding-model fit. 6 Table 2 reports NagB2 binding to (GlcNAc)2 with KD = 0.190 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7EHQ\7EHQ_metadata.json point structures/7EHQ/7ehq_protein.pdb structures/7EHQ/7ehq_pocket.pdb structures/7EHQ/7ehq_ligand.pdb structures/7EHQ/7ehq_ligand.cif structures/7EHQ/7ehq_complex.pdb structures/7EHQ/7ehq_complex.cif 7EHU extended NagB2 Paenibacillus sp. str. FPU-7 Recombinant NagB2 lacking the predicted N-terminal signal peptide Met1-Ala20, with a C-terminal six-histidine tag Na (GlcNAc)3; N-acetyl-D-glucosamine trisaccharide "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 1.12 µM 1120.0 [] unit_conversion 5.950781977329818 success True direct_binding Surface plasmon resonance (Biacore X100), one-site binding-model fit. 6 Table 2 reports NagB2 binding to (GlcNAc)3 with KD = 1.12 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7EHU\7EHU_metadata.json point structures/7EHU/7ehu_protein.pdb structures/7EHU/7ehu_pocket.pdb structures/7EHU/7ehu_ligand.pdb structures/7EHU/7ehu_ligand.cif structures/7EHU/7ehu_complex.pdb structures/7EHU/7ehu_complex.cif 7EHV classic MTHFD2 human MTHFD2 residues 36-350 with an N-terminal 6xHis tag followed by a thrombin cleavage site Na compound 3 "[""J4L""]" 1 IC50 IC50 = = 4.0 µM 4000.0 [] unit_conversion 5.3979400086720375 success True biochemical_inhibition Human MTHFD2 enzyme inhibition assay; Table 1 values are means of three independent experiments. 4 Table 1, “Inhibition of MTHFD2 by Xanthine Derivatives,” reports compound 3: MTHFD2 IC50 4.0 μM; footnote: mean of three independent experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\7EHV\7EHV_metadata.json point structures/7EHV/7ehv_protein.pdb structures/7EHV/7ehv_pocket.pdb structures/7EHV/7ehv_ligand.sdf structures/7EHV/7ehv_ligand.pdb structures/7EHV/7ehv_ligand.cif structures/7EHV/7ehv_complex.pdb structures/7EHV/7ehv_complex.cif 7EHZ extended Nicotinamide N-methyltransferase (NNMT) human Na Na macrocyclic peptide 2 "[""CHAIN:B""]" 1 IC50 IC50 = = 125 nM 125.0 [] unit_conversion 6.903089986991944 success True biochemical_inhibition NNMT-mediated methylation of nicotinamide in the presence of SAM; h/m denotes human/mouse. 2 Table 1 reports peptide 2 IC50 (h/m) = 125/217 nM; Figure 1 caption identifies NNMT complexed with peptide 2 as PDB 7EHZ. auto_single_measurement only accepted activity measurement [1] 1 structures\7EHZ\7EHZ_metadata.json point structures/7EHZ/7ehz_protein.pdb structures/7EHZ/7ehz_pocket.pdb structures/7EHZ/7ehz_ligand.pdb structures/7EHZ/7ehz_ligand.cif structures/7EHZ/7ehz_complex.pdb structures/7EHZ/7ehz_complex.cif 7EI2 extended Nicotinamide N-methyltransferase (NNMT) human Na Na macrocyclic peptide 8 "[""CHAIN:B""]" 1 IC50 IC50 = = 108 nM 108.0 [] unit_conversion 6.96657624451305 success True biochemical_inhibition NNMT-mediated methylation of nicotinamide in the presence of SAM; h/m denotes human/mouse. 4 Table 3 reports peptide 8 IC50 (h/m) = 108/188 nM. The text states that the X-ray structure of peptide 8 was obtained, consistent with the supplied 7EI2 peptide-8 structure frame. auto_single_measurement only accepted activity measurement [1] 1 structures\7EI2\7EI2_metadata.json point structures/7EI2/7ei2_protein.pdb structures/7EI2/7ei2_pocket.pdb structures/7EI2/7ei2_ligand.pdb structures/7EI2/7ei2_ligand.cif structures/7EI2/7ei2_complex.pdb structures/7EI2/7ei2_complex.cif 7EI4 classic MasL Massilia sp. YMA4 Na Na collimonin C (compound 1) "[""J3U""]" 1 Ki Ki = = 297.10 µM 297100.0 [] unit_conversion 3.527097348196336 success True biochemical_inhibition Inhibition kinetic assay of MasL by polyynes; Table 1. 5 Table 1, “Inhibition kinetic of Massilia sp. YMA4 MasL by polyynes,” reports collimonin C 1 with Ki 297.10 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7EI4\7EI4_metadata.json point structures/7EI4/7ei4_protein.pdb structures/7EI4/7ei4_pocket.pdb structures/7EI4/7ei4_ligand.sdf structures/7EI4/7ei4_ligand.pdb structures/7EI4/7ei4_ligand.cif structures/7EI4/7ei4_complex.pdb structures/7EI4/7ei4_complex.cif 7EIN extended SARS-CoV-2 main proteinase (Mpro) SARS-CoV-2 Native SARS-CoV-2 Mpro protein expressed with His and SUMO tags Na leupeptin "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 127.2 µM 127200.0 [] unit_conversion 3.8955128886876054 success True biochemical_inhibition Purified SARS-CoV-2 Mpro fluorescence-resonance-energy-transfer enzymatic inhibition assay. 2 “Fluorescence resonance energy transfer (FRET) enzymatic assays showed that leupeptin has some inhibitory activity against Mpro, with a 50% inhibitory concentration (IC50) value of 127.2 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7EIN\7EIN_metadata.json point structures/7EIN/7ein_protein.pdb structures/7EIN/7ein_pocket.pdb structures/7EIN/7ein_ligand.pdb structures/7EIN/7ein_ligand.cif structures/7EIN/7ein_complex.pdb structures/7EIN/7ein_complex.cif 7EJV classic DYRK2 Na DYRK2 residues 72-479 with an N-terminal 6xHis affinity tag and TEV protease cleavage site Na YK-2-69 "[""YK2""]" 2 Kd Kd = = 92 nM 92.0 [] unit_conversion 7.036212172654444 success True direct_binding Microscale thermophoresis binding assay with DYRK2 protein. 5 Fig. 3b prints for YK-2-69: Kd = 92 nM; the paper identifies microscale thermophoresis as the binding-affinity assay. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7EJV\7EJV_metadata.json point structures/7EJV/7ejv_protein.pdb structures/7EJV/7ejv_pocket.pdb structures/7EJV/7ejv_ligand.sdf structures/7EJV/7ejv_ligand.pdb structures/7EJV/7ejv_ligand.cif structures/7EJV/7ejv_complex.pdb structures/7EJV/7ejv_complex.cif 7EN8 classic SARS-CoV-2 3CLpro SARS-CoV-2 Na Na WU-04 "[""J7R""]" 2 Kd Kd = = 36.6 ± 8.3 nM 36.6 [] unit_conversion 7.436518914605589 success True direct_binding Isothermal titration calorimetry of WU-04 binding to SARS-CoV-2 3CLpro. 2 Figure 1c reports Kd = 36.6 ± 8.3 nM for WU-04 and SARS-CoV-2 3CLpro. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7EN8\7EN8_metadata.json point structures/7EN8/7en8_protein.pdb structures/7EN8/7en8_pocket.pdb structures/7EN8/7en8_ligand.sdf structures/7EN8/7en8_ligand.pdb structures/7EN8/7en8_ligand.cif structures/7EN8/7en8_complex.pdb structures/7EN8/7en8_complex.cif 7EN9 classic SARS-CoV-2 3CLpro SARS-CoV-2 Na Na WU-02 "[""J7O""]" 1 IC50 IC50 = = 71 ± 4 nM 71.0 [] unit_conversion 7.1487416512809245 success True biochemical_inhibition Fluorescent substrate Dabcyl-KTSAVLQSGFRKME-Edans assay with purified SARS-CoV-2 3CLpro. 2 Figure 1b reports WU-02 IC50 = 71 ± 4 nM against SARS-CoV-2 3CLpro. auto_single_measurement only accepted activity measurement [1] 1 structures\7EN9\7EN9_metadata.json point structures/7EN9/7en9_protein.pdb structures/7EN9/7en9_pocket.pdb structures/7EN9/7en9_ligand.sdf structures/7EN9/7en9_ligand.pdb structures/7EN9/7en9_ligand.cif structures/7EN9/7en9_complex.pdb structures/7EN9/7en9_complex.cif 7END classic SARS-CoV 3CLpro SARS-CoV Na Na WU-04 "[""J7R""]" 1 IC50 IC50 = = 55 ± 3 nM 55.0 [] unit_conversion 7.259637310505756 success True biochemical_inhibition Fluorescence-based enzymatic activity assay of SARS-CoV 3CLpro. 5 Figure 4a reports WU-04 IC50 = 55 ± 3 nM against SARS-CoV 3CLpro. auto_single_measurement only accepted activity measurement [1] 1 structures\7END\7END_metadata.json point structures/7END/7end_protein.pdb structures/7END/7end_pocket.pdb structures/7END/7end_ligand.sdf structures/7END/7end_ligand.pdb structures/7END/7end_ligand.cif structures/7END/7end_complex.pdb structures/7END/7end_complex.cif 7ENE classic MERS-CoV 3CLpro MERS-CoV Na Na WU-04 "[""J7R""]" 2 Kd Kd ~ ~ 32 nM 32.0 [] unit_conversion 7.494850021680094 success True direct_binding Binding-affinity determination for MERS-CoV 3CLpro/WU-04, summarized in the main text. 6 The text states that the binding affinity (Kd) of WU-04 to MERS-CoV 3CLpro was about 32 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7ENE\7ENE_metadata.json point structures/7ENE/7ene_protein.pdb structures/7ENE/7ene_pocket.pdb structures/7ENE/7ene_ligand.sdf structures/7ENE/7ene_ligand.pdb structures/7ENE/7ene_ligand.cif structures/7ENE/7ene_complex.pdb structures/7ENE/7ene_complex.cif 7EO7 classic HCoV-NL63 3C-like protease Human coronavirus NL63 (HCoV-NL63) Na Na Shikonin "[""FNO""]" 1 IC50 IC50 = = 16.91 ± 5.13 μM 16910.0 [] unit_conversion 4.771856392402258 success True biochemical_inhibition Recombinant HCoV-NL63 main protease inhibition measured by FRET enzymatic assay; Fig. 2E. 5 Fig. 2E prints “IC50=16.91 ± 5.13 μm” for shikonin inhibition of HCoV-NL63 main protease. auto_single_measurement only accepted activity measurement [1] 1 structures\7EO7\7EO7_metadata.json point structures/7EO7/7eo7_protein.pdb structures/7EO7/7eo7_pocket.pdb structures/7EO7/7eo7_ligand.sdf structures/7EO7/7eo7_ligand.pdb structures/7EO7/7eo7_ligand.cif structures/7EO7/7eo7_complex.pdb structures/7EO7/7eo7_complex.cif 7EO8 classic SARS coronavirus main protease SARS coronavirus (SARS-CoV) Na Na Shikonin "[""FNO""]" 1 IC50 IC50 = = 7.89 ± 1.24 μM 7890.0 [] unit_conversion 5.10292299679058 success True biochemical_inhibition Recombinant SARS-CoV main protease inhibition measured by FRET enzymatic assay; Fig. 2B. 5 Fig. 2B prints “IC50=7.89 ± 1.24 μm” for shikonin inhibition of SARS-CoV main protease. auto_single_measurement only accepted activity measurement [1] 1 structures\7EO8\7EO8_metadata.json point structures/7EO8/7eo8_protein.pdb structures/7EO8/7eo8_pocket.pdb structures/7EO8/7eo8_ligand.sdf structures/7EO8/7eo8_ligand.pdb structures/7EO8/7eo8_ligand.cif structures/7EO8/7eo8_complex.pdb structures/7EO8/7eo8_complex.cif 7EQZ extended Aedes aegypti carboxypeptidase-B1 (CPBAe1) Aedes aegypti Mature active enzyme, peptidase domain Glu7-Phe305 Na Potato carboxypeptidase inhibitor (PCI) "[""CHAIN:I""]" 1 Ki Ki = = 14.70 nM 14.7 [] unit_conversion 7.8326826652518236 success True biochemical_inhibition Competitive inhibition of mature CPBAe1 by PCI using Hippuryl-L-Arg substrate; substrate concentration 0.8 nM. 3 “The activity of CPBAe1 was inhibited by PCI with Ki value 14.70 nM (competitive inhibition; Km = 1.14 nM, IC50 = 25 nM, and substrate concentration = 0.8 nM; Figure 1).” auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\7EQZ\7EQZ_metadata.json point structures/7EQZ/7eqz_protein.pdb structures/7EQZ/7eqz_pocket.pdb structures/7EQZ/7eqz_ligand.pdb structures/7EQZ/7eqz_ligand.cif structures/7EQZ/7eqz_complex.pdb structures/7EQZ/7eqz_complex.cif 7ERK classic V30M-TTR Na N-terminal hexahistidine-tagged TTR V30M dasatinib (compound 32) "[""1N1""]" 1 Kd Kd = = 3.1 ± 0.7 µM 3100.0 [] unit_conversion 5.508638306165727 success True direct_binding Tryptophan intrinsic-fluorescence quenching assay; reported as apparent Kd,app. 5 Table 2 reports Kd,app = 3.1 ± 0.7 µM for compound 32. The assay text states that intrinsic-fluorescence experiments used V30M-TTR, and Figure 6 identifies PDB 7ERK as the V30M-TTR–32 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7ERK\7ERK_metadata.json point structures/7ERK/7erk_protein.pdb structures/7ERK/7erk_pocket.pdb structures/7ERK/7erk_ligand.sdf structures/7ERK/7erk_ligand.pdb structures/7ERK/7erk_ligand.cif structures/7ERK/7erk_complex.pdb structures/7ERK/7erk_complex.cif 7ET9 classic 4-hydroxy-2-keto-heptane-1,7-dioate aldolase (AbHpaI) Acinetobacter baumannii Na Na pyruvate "[""PYR""]" 1 Kd Kd = = 980 ± 60 μM 980000.0 [] unit_conversion 3.008773924307505 success True direct_binding ITC measurement of pyruvate binding to Zn2+-reconstituted AbHpaI. 3 Table 1 prints Kd, pyruvate = 980 ± 60 μM for AbHpaI•Zn2+. auto_single_measurement only accepted activity measurement [1] 1 structures\7ET9\7ET9_metadata.json point structures/7ET9/7et9_protein.pdb structures/7ET9/7et9_pocket.pdb structures/7ET9/7et9_ligand.sdf structures/7ET9/7et9_ligand.pdb structures/7ET9/7et9_ligand.cif structures/7ET9/7et9_complex.pdb structures/7ET9/7et9_complex.cif 7ETA classic 4-hydroxy-2-keto-heptane-1,7-dioate aldolase (AbHpaI) Acinetobacter baumannii Na Na pyruvate "[""PYR""]" 1 Kd Kd = = 320 ± 40 μM 320000.0 [] unit_conversion 3.4948500216800937 success True direct_binding ITC measurement of pyruvate binding to Co2+-reconstituted AbHpaI. 3 Table 1 prints Kd, pyruvate = 320 ± 40 μM for AbHpaI•Co2+. auto_single_measurement only accepted activity measurement [1] 1 structures\7ETA\7ETA_metadata.json point structures/7ETA/7eta_protein.pdb structures/7ETA/7eta_pocket.pdb structures/7ETA/7eta_ligand.sdf structures/7ETA/7eta_ligand.pdb structures/7ETA/7eta_ligand.cif structures/7ETA/7eta_complex.pdb structures/7ETA/7eta_complex.cif 7ETB classic 4-hydroxy-2-keto-heptane-1,7-dioate aldolase (AbHpaI) Acinetobacter baumannii Na Na pyruvate "[""PYR""]" 1 Kd Kd = = 620 ± 500 μM 620000.0 [] unit_conversion 3.2076083105017466 success True direct_binding ITC measurement of pyruvate binding to Mn2+-reconstituted AbHpaI. 3 Table 1 prints Kd, pyruvate = 620 ± 500 μM for AbHpaI•Mn2+. auto_single_measurement only accepted activity measurement [1] 1 structures\7ETB\7ETB_metadata.json point structures/7ETB/7etb_protein.pdb structures/7ETB/7etb_pocket.pdb structures/7ETB/7etb_ligand.sdf structures/7ETB/7etb_ligand.pdb structures/7ETB/7etb_ligand.cif structures/7ETB/7etb_complex.pdb structures/7ETB/7etb_complex.cif 7EU5 classic Human nicotinamide N-methyltransferase (NNMT) Human Full-length human NNMT residues 1-264 with an N-terminal His6 tag and thrombin cleavage site Na JBSNF-000107 "[""JDL""]" 1 IC50 IC50 = = 0.039 ± 0.004 µM 39.0 [] unit_conversion 7.4089353929735005 success True biochemical_inhibition Recombinant human NNMT enzymatic inhibition; SAR table. 3 Table 1 reports Compound (8), hNNMT IC50 = 0.039 ± 0.004 µM. Page 5 explicitly identifies Compound 8 as JBSNF-000107. auto_single_measurement only accepted activity measurement [1] 1 structures\7EU5\7EU5_metadata.json point structures/7EU5/7eu5_protein.pdb structures/7EU5/7eu5_pocket.pdb structures/7EU5/7eu5_ligand.sdf structures/7EU5/7eu5_ligand.pdb structures/7EU5/7eu5_ligand.cif structures/7EU5/7eu5_complex.pdb structures/7EU5/7eu5_complex.cif 7EVJ classic CBP Na Na Na 9c "[""JE9""]" 1 IC50 IC50 = = 21.32±6.83 nM 21.32 [] unit_conversion 7.671212799645465 success True biochemical_inhibition HTRF assay; Table 3 reports CBP bromodomain inhibition for 9c. 6 Table 3 lists compound 9c: HTRF IC50 = 21.32±6.83 nM. Figure 4 identifies the 9c–CBP bromodomain crystal structure as PDB 7EVJ. auto_single_measurement only accepted activity measurement [1] 1 structures\7EVJ\7EVJ_metadata.json point structures/7EVJ/7evj_protein.pdb structures/7EVJ/7evj_pocket.pdb structures/7EVJ/7evj_ligand.sdf structures/7EVJ/7evj_ligand.pdb structures/7EVJ/7evj_ligand.cif structures/7EVJ/7evj_complex.pdb structures/7EVJ/7evj_complex.cif 7EW9 classic KRAS Na KRAS(G12D) residues 1-169 G12D TH-Z816 "[""05C""]" 1 Kd Kd = = 25.8 ± 5.78 μM 25800.0 [] unit_conversion 4.58838029403677 success True direct_binding Isothermal titration calorimetry of TH-Z816 with GDP-bound KRAS(G12D). 3 Fig. 1c reports [TH-Z816] 800 μM, GDP-bound KRAS(G12D) 26 μM, and Kd 25.8 ± 5.78 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7EW9\7EW9_metadata.json point structures/7EW9/7ew9_protein.pdb structures/7EW9/7ew9_pocket.pdb structures/7EW9/7ew9_ligand.sdf structures/7EW9/7ew9_ligand.pdb structures/7EW9/7ew9_ligand.cif structures/7EW9/7ew9_complex.pdb structures/7EW9/7ew9_complex.cif 7EWB classic KRAS Na KRAS(G12D) residues 1-169 G12D TH-Z835 "[""05I""]" 1 IC50 IC50 = = 1.6 μM 1600.0 [] unit_conversion 5.795880017344075 success True biochemical_inhibition SOS-catalyzed nucleotide-exchange assay with GDP as incoming nucleotide. 4 Fig. 2a reports TH-Z835 IC50 = 1.6 μM; the caption identifies a SOS-catalyzed nucleotide-exchange assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7EWB\7EWB_metadata.json point structures/7EWB/7ewb_protein.pdb structures/7EWB/7ewb_pocket.pdb structures/7EWB/7ewb_ligand.sdf structures/7EWB/7ewb_ligand.pdb structures/7EWB/7ewb_ligand.cif structures/7EWB/7ewb_complex.pdb structures/7EWB/7ewb_complex.cif 7EWH classic PHGDH Homo sapiens Na Na Homoharringtonine (HHT) "[""HMT""]" 1 Kd Kd = = 6.5 µM 6500.0 [] unit_conversion 5.187086643357144 success True direct_binding ITC titration of HHT into purified human PHGDH. 6 Fig. 2C reports “HHT titrating PHGDH” with Kd = 6.5 µM; the text identifies the assay as ITC using purified human PHGDH. auto_single_measurement only accepted activity measurement [1] 1 structures\7EWH\7EWH_metadata.json point structures/7EWH/7ewh_protein.pdb structures/7EWH/7ewh_pocket.pdb structures/7EWH/7ewh_ligand.sdf structures/7EWH/7ewh_ligand.pdb structures/7EWH/7ewh_ligand.cif structures/7EWH/7ewh_complex.pdb structures/7EWH/7ewh_complex.cif 7EX2 classic Ebinur Lake virus cap-snatching endonuclease Ebinur Lake virus EN residues 1-183 with an N-terminal 6xHis tag in pET-28a(+) Na L-742,001 (methyl ester form) "[""I0N""]" 1 IC50 IC50 = = 1.2 ± 0.1 µM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition In vitro EBIV endonuclease inhibition assay using purified EBIV EN and 27-mer ssRNA substrate. 6 Table 1 reports L-742,001 IC50 = 1.2 ± 0.1 µM; footnote states IC50 inhibitors were tested by in vitro endonuclease assay. The data-availability statement maps L-742,001 to PDB 7EX2. auto_single_measurement only accepted activity measurement [1] 1 structures\7EX2\7EX2_metadata.json point structures/7EX2/7ex2_protein.pdb structures/7EX2/7ex2_pocket.pdb structures/7EX2/7ex2_ligand.sdf structures/7EX2/7ex2_ligand.pdb structures/7EX2/7ex2_ligand.cif structures/7EX2/7ex2_complex.pdb structures/7EX2/7ex2_complex.cif 7EX3 classic Ebinur Lake virus cap-snatching endonuclease Ebinur Lake virus EN residues 1-183 with an N-terminal 6xHis tag in pET-28a(+) Na IN3 (inhibitor 3) "[""IA3""]" 1 IC50 IC50 = = 2.7 ± 0.2 µM 2700.0 [] unit_conversion 5.568636235841012 success True biochemical_inhibition In vitro EBIV endonuclease inhibition assay using purified EBIV EN and 27-mer ssRNA substrate. 6 Table 1 reports IN3 IC50 = 2.7 ± 0.2 µM; footnote states IC50 inhibitors were tested by in vitro endonuclease assay. The data-availability statement maps IN3 to PDB 7EX3. auto_single_measurement only accepted activity measurement [1] 1 structures\7EX3\7EX3_metadata.json point structures/7EX3/7ex3_protein.pdb structures/7EX3/7ex3_pocket.pdb structures/7EX3/7ex3_ligand.sdf structures/7EX3/7ex3_ligand.pdb structures/7EX3/7ex3_ligand.cif structures/7EX3/7ex3_complex.pdb structures/7EX3/7ex3_complex.cif 7EX4 classic Ebinur Lake virus cap-snatching endonuclease Ebinur Lake virus EN residues 1-183 with an N-terminal 6xHis tag in pET-28a(+) Na IN5 (inhibitor 5) "[""IA5""]" 1 IC50 IC50 = = 1.3 ± 0.1 µM 1300.0 [] unit_conversion 5.886056647693163 success True biochemical_inhibition In vitro EBIV endonuclease inhibition assay using purified EBIV EN and 27-mer ssRNA substrate. 6 Table 1 reports IN5 IC50 = 1.3 ± 0.1 µM; footnote states IC50 inhibitors were tested by in vitro endonuclease assay. The data-availability statement maps IN5 to PDB 7EX4. auto_single_measurement only accepted activity measurement [1] 1 structures\7EX4\7EX4_metadata.json point structures/7EX4/7ex4_protein.pdb structures/7EX4/7ex4_pocket.pdb structures/7EX4/7ex4_ligand.sdf structures/7EX4/7ex4_ligand.pdb structures/7EX4/7ex4_ligand.cif structures/7EX4/7ex4_complex.pdb structures/7EX4/7ex4_complex.cif 7EX6 classic Ebinur Lake virus cap-snatching endonuclease Ebinur Lake virus EN residues 1-183 with an N-terminal 6xHis tag in pET-28a(+) Na IN11 (inhibitor 11) "[""11I""]" 1 IC50 IC50 = = 4.5 ± 0.1 µM 4500.0 [] unit_conversion 5.346787486224656 success True biochemical_inhibition In vitro EBIV endonuclease inhibition assay using purified EBIV EN and 27-mer ssRNA substrate. 6 Table 1 reports IN11 IC50 = 4.5 ± 0.1 µM; footnote states IC50 inhibitors were tested by in vitro endonuclease assay. The data-availability statement maps IN11 to PDB 7EX6. auto_single_measurement only accepted activity measurement [1] 1 structures\7EX6\7EX6_metadata.json point structures/7EX6/7ex6_protein.pdb structures/7EX6/7ex6_pocket.pdb structures/7EX6/7ex6_ligand.sdf structures/7EX6/7ex6_ligand.pdb structures/7EX6/7ex6_ligand.cif structures/7EX6/7ex6_complex.pdb structures/7EX6/7ex6_complex.cif 7EX7 classic Ebinur Lake virus cap-snatching endonuclease Ebinur Lake virus EN residues 1-183 with an N-terminal 6xHis tag in pET-28a(+) Na IN16 (inhibitor 16) "[""1I6""]" 1 IC50 IC50 = = 1.1 ± 0.1 µM 1100.0 [] unit_conversion 5.958607314841775 success True biochemical_inhibition In vitro EBIV endonuclease inhibition assay using purified EBIV EN and 27-mer ssRNA substrate. 6 Table 1 reports IN16 IC50 = 1.1 ± 0.1 µM; footnote states IC50 inhibitors were tested by in vitro endonuclease assay. The data-availability statement maps IN16 to PDB 7EX7. auto_single_measurement only accepted activity measurement [1] 1 structures\7EX7\7EX7_metadata.json point structures/7EX7/7ex7_protein.pdb structures/7EX7/7ex7_pocket.pdb structures/7EX7/7ex7_ligand.sdf structures/7EX7/7ex7_ligand.pdb structures/7EX7/7ex7_ligand.cif structures/7EX7/7ex7_complex.pdb structures/7EX7/7ex7_complex.cif 7EX8 extended Ebinur Lake virus cap-snatching endonuclease Ebinur Lake virus EN residues 1-183 with an N-terminal 6xHis tag in pET-28a(+) Na IN27 (inhibitor 27) "[""I27""]" 1 IC50 IC50 = = 5.9 ± 0.9 µM 5900.0 [] unit_conversion 5.229147988357855 success True biochemical_inhibition In vitro EBIV endonuclease inhibition assay using purified EBIV EN and 27-mer ssRNA substrate. 6 Table 1 reports IN27 IC50 = 5.9 ± 0.9 µM; footnote states IC50 inhibitors were tested by in vitro endonuclease assay. The data-availability statement maps IN27 to PDB 7EX8. auto_single_measurement only accepted activity measurement [1] 1 structures\7EX8\7EX8_metadata.json point structures/7EX8/7ex8_protein.pdb structures/7EX8/7ex8_pocket.pdb structures/7EX8/7ex8_ligand.pdb structures/7EX8/7ex8_ligand.cif structures/7EX8/7ex8_complex.pdb structures/7EX8/7ex8_complex.cif 7EX9 extended Ebinur Lake virus cap-snatching endonuclease Ebinur Lake virus EN residues 1-183 with an N-terminal 6xHis tag in pET-28a(+) Na IN28 (inhibitor 28) "[""U28""]" 1 IC50 IC50 = = 9.5 ± 0.5 µM 9500.0 [] unit_conversion 5.022276394711152 success True biochemical_inhibition In vitro EBIV endonuclease inhibition assay using purified EBIV EN and 27-mer ssRNA substrate. 6 Table 1 reports IN28 IC50 = 9.5 ± 0.5 µM; footnote states IC50 inhibitors were tested by in vitro endonuclease assay. The data-availability statement maps IN28 to PDB 7EX9. auto_single_measurement only accepted activity measurement [1] 1 structures\7EX9\7EX9_metadata.json point structures/7EX9/7ex9_protein.pdb structures/7EX9/7ex9_pocket.pdb structures/7EX9/7ex9_ligand.pdb structures/7EX9/7ex9_ligand.cif structures/7EX9/7ex9_complex.pdb structures/7EX9/7ex9_complex.cif 7EXO classic ArchLec Methanocaldococcus jannaschii 219 amino acid L-type lectin domain corresponding to residues 1463-1682, expressed with an N-terminal hexa-Histidine tag Na mannose "[""BMA""]" 1 Kd Kd = = 317 µM 317000.0 [] unit_conversion 3.498940737782249 success True direct_binding Isothermal titration calorimetry (ITC) of purified ArchLec with monosaccharides; methods specify 100 µM ArchLec and 10 mM sugars. Mannose binding was fitted from three measurements. 3 “ITC studies … revealed ArchLec to be a mannose/glucose-specific lectin. Mannose binds with a Kd of 317 µM … (average of three measurements).” Table 1 maps ArchLec_man to PDB ID 7EXO. auto_single_measurement only accepted activity measurement [1] 1 structures\7EXO\7EXO_metadata.json point structures/7EXO/7exo_protein.pdb structures/7EXO/7exo_pocket.pdb structures/7EXO/7exo_ligand.sdf structures/7EXO/7exo_ligand.pdb structures/7EXO/7exo_ligand.cif structures/7EXO/7exo_complex.pdb structures/7EXO/7exo_complex.cif 7F0C extended capreomycin phosphotransferase (Cph) Streptomyces mutabilis subsp. capreolus (ATCC 23892) Recombinant cph gene cloned into pET-22b and expressed in E. coli BL21 Rosetta (DE3) Na CMN IIA "[""CHAIN:C""]" 1 Kd Kd = = 16.11 μM 16110.0 [] unit_conversion 4.792904459580782 success True direct_binding Isothermal titration calorimetry (ITC) analysis of purified Cph with CMN IIA; fitted using a standard single-site binding model. 6 “Isothermal titration calorimetry (ITC) analysis echoed the observation that both CMN IIA and IIB bind to Cph with different binding affinities (KD), 16.11 and 5.48 μM for CMN IIA and IIB, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7F0C\7F0C_metadata.json point structures/7F0C/7f0c_protein.pdb structures/7F0C/7f0c_pocket.pdb structures/7F0C/7f0c_ligand.pdb structures/7F0C/7f0c_ligand.cif structures/7F0C/7f0c_complex.pdb structures/7F0C/7f0c_complex.cif 7F0F extended capreomycin phosphotransferase (Cph) Streptomyces mutabilis subsp. capreolus (ATCC 23892) Recombinant cph gene cloned into pET-22b and expressed in E. coli BL21 Rosetta (DE3) Na CMN IIB "[""CHAIN:C""]" 1 Kd Kd = = 5.48 μM 5480.0 [] unit_conversion 5.261219441515631 success True direct_binding Isothermal titration calorimetry (ITC) analysis of purified Cph with CMN IIB; fitted using a standard single-site binding model. 6 “Isothermal titration calorimetry (ITC) analysis echoed the observation that both CMN IIA and IIB bind to Cph with different binding affinities (KD), 16.11 and 5.48 μM for CMN IIA and IIB, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7F0F\7F0F_metadata.json point structures/7F0F/7f0f_protein.pdb structures/7F0F/7f0f_pocket.pdb structures/7F0F/7f0f_ligand.pdb structures/7F0F/7f0f_ligand.cif structures/7F0F/7f0f_complex.pdb structures/7F0F/7f0f_complex.cif 7F1D classic BACE1 Na Na Na Compound 6; N-{3-[(4R,5R,6R)-2-amino-5-fluoro-4,6-dimethyl-5,6-dihydro-4H-1,3-thiazin-4-yl]-4-fluorophenyl}-2H,3H-[1,4]dioxino[2,3-c]pyridine-7-carboxamide "[""0QQ""]" 2 Ki Ki = = 0.13 nM 0.13 [] unit_conversion 9.886056647693163 success True direct_binding Competitive radioligand binding assay at pH 6.2 using tritiated nonselective BACE1/BACE2 inhibitor [3H] JNJ-962. 5 Table 2 reports compound 6 BACE1 Ki = 0.13 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7F1D\7F1D_metadata.json point structures/7F1D/7f1d_protein.pdb structures/7F1D/7f1d_pocket.pdb structures/7F1D/7f1d_ligand.sdf structures/7F1D/7f1d_ligand.pdb structures/7F1D/7f1d_ligand.cif structures/7F1D/7f1d_complex.pdb structures/7F1D/7f1d_complex.cif 7F2K classic PDE4D Na PDE4D catalytic domain, residues 86-413 Na 17a "[""0X8""]" 1 IC50 IC50 = = 30 ± 1 nM 30.0 [] unit_conversion 7.522878745280337 success True biochemical_inhibition In vitro enzymatic activity assay; PDE4D2 (residues 86–413) was assayed with radiolabeled cyclic nucleotide substrate. 3 Table 1, “Chemical Structures and Inhibitory Affinities of Mangostanin Derivatives against PDE4D2”, reports 17a IC50 30 ± 1 nM. Figure 3 identifies the PDE4D–17a cocrystal as PDB ID 7F2K. auto_single_measurement only accepted activity measurement [1] 1 structures\7F2K\7F2K_metadata.json point structures/7F2K/7f2k_protein.pdb structures/7F2K/7f2k_pocket.pdb structures/7F2K/7f2k_ligand.sdf structures/7F2K/7f2k_ligand.pdb structures/7F2K/7f2k_ligand.cif structures/7F2K/7f2k_complex.pdb structures/7F2K/7f2k_complex.cif 7F2L classic PDE4D Na PDE4D catalytic domain, residues 86-413 Na 18a "[""1AS""]" 1 IC50 IC50 = = 4.2 ± 0.5 nM 4.2 [] unit_conversion 8.3767507096021 success True biochemical_inhibition In vitro enzymatic activity assay; PDE4D2 (residues 86–413) was assayed with radiolabeled cyclic nucleotide substrate. 3 Table 1 reports compound 18a IC50 4.2 ± 0.5 nM against PDE4D2. Figure 4 maps the PDE4D–18a cocrystal to PDB ID 7F2L. auto_single_measurement only accepted activity measurement [1] 1 structures\7F2L\7F2L_metadata.json point structures/7F2L/7f2l_protein.pdb structures/7F2L/7f2l_pocket.pdb structures/7F2L/7f2l_ligand.sdf structures/7F2L/7f2l_ligand.pdb structures/7F2L/7f2l_ligand.cif structures/7F2L/7f2l_complex.pdb structures/7F2L/7f2l_complex.cif 7F3B classic Escherichia coli dihydrofolate reductase (DHFR) Escherichia coli Na Na OYYF-175 "[""D4C""]" 2 Kd Kd = = 75.20 ± 26.40 nM 75.2 [] unit_conversion 7.123782159408358 success True direct_binding Isothermal titration calorimetry of OYYF-175 with purified ecDHFR. 5 “The fitted ITC curves revealed that ecDHFR titrated by OYYF-175 yielded a KD value of 75.20 ± 26.40 nM.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7F3B\7F3B_metadata.json point structures/7F3B/7f3b_protein.pdb structures/7F3B/7f3b_pocket.pdb structures/7F3B/7f3b_ligand.sdf structures/7F3B/7f3b_ligand.pdb structures/7F3B/7f3b_ligand.cif structures/7F3B/7f3b_complex.pdb structures/7F3B/7f3b_complex.cif 7F3G classic Doublecortin-like kinase 1 (DCLK1) Na DCLK1 kinase domain encompassing residues Gly372-Asp649; N-terminal His6-TEV expression construct, cleaved before purification Na ruxolitinib (INCB018424; compound 9) "[""RXT""]" 1 Kd Kd = = 19.2 (±0.4) μM 19200.0 [] unit_conversion 4.716698771296451 success True direct_binding Surface plasmon resonance (SPR) binding affinity of ruxolitinib to DCLK1 kinase-domain protein. 2 SPR assessment gave a dissociation constant (Kd) of 19.2 (±0.4) μM for ruxolitinib with DCLK1 proteins. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7F3G\7F3G_metadata.json point structures/7F3G/7f3g_protein.pdb structures/7F3G/7f3g_pocket.pdb structures/7F3G/7f3g_ligand.sdf structures/7F3G/7f3g_ligand.pdb structures/7F3G/7f3g_ligand.cif structures/7F3G/7f3g_complex.pdb structures/7F3G/7f3g_complex.cif 7F3M classic FGFR4 human FGFR4 kinase domain residues 445-753 with an N-terminal 6xHis tag followed by a PreScission or TEV cleavage site Na PRN1371 "[""GX3""]" 1 IC50 IC50 = = 31.3 nM 31.3 [] unit_conversion 7.504455662453552 success True biochemical_inhibition In vitro kinase assay against FGFR4; mean of n = 3 independent experiments. 4 Fig. 2d reports PRN1371 against FGFR4 with IC50 = 31.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F3M\7F3M_metadata.json point structures/7F3M/7f3m_protein.pdb structures/7F3M/7f3m_pocket.pdb structures/7F3M/7f3m_ligand.sdf structures/7F3M/7f3m_ligand.pdb structures/7F3M/7f3m_ligand.cif structures/7F3M/7f3m_complex.pdb structures/7F3M/7f3m_complex.cif 7F3O classic GluA2o human Na Na TAK-653 "[""0YK""]" 1 IC50 IC50 = = 0.26 µM 260.0 [] unit_conversion 6.585026652029182 success True direct_binding SPA competitive binding assay: TAK-653 inhibited [3H]-HBT1 binding to His-LBD; TAK-653/LBD binding was glutamate-dependent. 2 “TAK-653 inhibited binding between [3H]-HBT1 and His-LBD with an IC50 value of 0.26 µM (Fig. 1C).” auto_single_measurement only accepted activity measurement [1] 1 structures\7F3O\7F3O_metadata.json point structures/7F3O/7f3o_protein.pdb structures/7F3O/7f3o_pocket.pdb structures/7F3O/7f3o_ligand.sdf structures/7F3O/7f3o_ligand.pdb structures/7F3O/7f3o_ligand.cif structures/7F3O/7f3o_complex.pdb structures/7F3O/7f3o_complex.cif 7F3T classic human TMEM120A Homo sapiens HsTMEM120A with N-terminal FLAG and twin-Strep tags; modeled residues 7-336 Na CoASH (coenzyme A) "[""COA""]" 1 Kd Kd = = 0.685 ± 0.045 µM 685.0 [] unit_conversion 6.164309428507575 success True direct_binding Isothermal titration calorimetry of CoASH binding to purified HsTMEM120A; single-site-binding isotherm. 8 Figure 4 caption reports ITC binding between CoASH and HsTMEM120A and gives Kd = 0.685 ± 0.045 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F3T\7F3T_metadata.json point structures/7F3T/7f3t_protein.pdb structures/7F3T/7f3t_pocket.pdb structures/7F3T/7f3t_ligand.sdf structures/7F3T/7f3t_ligand.pdb structures/7F3T/7f3t_ligand.cif structures/7F3T/7f3t_complex.pdb structures/7F3T/7f3t_complex.cif 7F3Y classic Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) Plasmodium falciparum wild type PfDHFR-TS (TM4) wild type methotrexate (MTX) "[""MTX""]" 1 Ki Ki = = 0.20 ± 0.03 nM 0.2 [] unit_conversion 9.698970004336019 success True biochemical_inhibition Kinetic enzyme-inhibition experiment; the text contrasts the experimental Ki,MTX with the distance-model prediction for the solved PfDHFR-TS–MTX structure (PDB 7F3Y). 6 “the Ki,MTX of PfDHFR-TS from kinetic experiments was 0.20 ± 0.03 nM (Table S4)” following identification of the PfDHFR-TS–MTX X-ray structure as PDB 7F3Y. auto_single_measurement only accepted activity measurement [1] 1 structures\7F3Y\7F3Y_metadata.json point structures/7F3Y/7f3y_protein.pdb structures/7F3Y/7f3y_pocket.pdb structures/7F3Y/7f3y_ligand.sdf structures/7F3Y/7f3y_ligand.pdb structures/7F3Y/7f3y_ligand.cif structures/7F3Y/7f3y_complex.pdb structures/7F3Y/7f3y_complex.cif 7F3Z classic Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) Plasmodium falciparum double mutant PfDHFR-TS (K1) C59R+S108N trimethoprim (TOP) "[""TOP""]" 1 Ki Ki = = 3.62 nM 3.62 [] unit_conversion 8.441291429466835 success True biochemical_inhibition Experimental kinetic inhibition determination for K1 PfDHFR-TS–TOP; the reported value is compared with a 1.45 nM prediction from the PDB 7F3Z structure. 4 “A blind test with the X-ray crystal structure of Plasmodium falciparum DHFR-thymidylate synthase (PfDHFR-TS) in complex with TOP (PDB: 7F3Z) results in a Ki,TOP prediction of 1.45 nM, while the experimental Ki,TOP was 3.62 nM (Table S2).” Figure 2 identifies this as K1 PfDHFR-TS. auto_single_measurement only accepted activity measurement [1] 1 structures\7F3Z\7F3Z_metadata.json point structures/7F3Z/7f3z_protein.pdb structures/7F3Z/7f3z_pocket.pdb structures/7F3Z/7f3z_ligand.sdf structures/7F3Z/7f3z_ligand.pdb structures/7F3Z/7f3z_ligand.cif structures/7F3Z/7f3z_complex.pdb structures/7F3Z/7f3z_complex.cif 7F4M classic TthMTA1; Tthp1; Tthp2 Tetrahymena thermophila N-terminal truncated TthMTA1 residues 126-372 with Tthp1 and Tthp2 Na SAM (S-adenosyl methionine) "[""SAM""]" 1 Kd Kd = = 14.83 ± 2.71 µM 14830.0 [] unit_conversion 4.828858848971618 success True direct_binding ITC assay of SAM binding; four-component TthMTA1c complex. 9 Fig. 5a prints Kd = 14.83 ± 2.71 µM for MTA1-p1-p2. auto_single_measurement only accepted activity measurement [1] 1 structures\7F4M\7F4M_metadata.json point structures/7F4M/7f4m_protein.pdb structures/7F4M/7f4m_pocket.pdb structures/7F4M/7f4m_ligand.sdf structures/7F4M/7f4m_ligand.pdb structures/7F4M/7f4m_ligand.cif structures/7F4M/7f4m_complex.pdb structures/7F4M/7f4m_complex.cif 7F4T classic TthMTA1; Ptep2 Tetrahymena thermophila; Paramecium tetraurelia TthMTA1-Ptep2 binary complex Na SAM (S-adenosyl methionine) "[""SAM""]" 1 Kd Kd = = 77.65 ± 4.10 µM 77650.0 [] unit_conversion 4.109858539935423 success True direct_binding ITC assay of SAM binding in the presence of Ptep2. 9 Fig. 5d prints Kd = 77.65 ± 4.10 µM for TthMTA1+Ptep2. auto_single_measurement only accepted activity measurement [1] 1 structures\7F4T\7F4T_metadata.json point structures/7F4T/7f4t_protein.pdb structures/7F4T/7f4t_pocket.pdb structures/7F4T/7f4t_ligand.sdf structures/7F4T/7f4t_ligand.pdb structures/7F4T/7f4t_ligand.cif structures/7F4T/7f4t_complex.pdb structures/7F4T/7f4t_complex.cif 7F60 extended Rae1-Nup98 complex Homo sapiens; SARS-CoV-2 Rae1 residues 31-368 and Nup98 residues 157-213, in complex with the SARS-CoV-2 ORF6 C-terminal-tail C3 peptide Na SARS-CoV-2 ORF6 C3 C-terminal-tail peptide "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 240 nM 240.0 [] unit_conversion 6.619788758288394 success True direct_binding Isothermal titration calorimetry (ITC) of the SARS-CoV-2 ORF6 C3 peptide with Rae1-Nup98. 2 The text reports that SARS-CoV-2 ORF6 C3 bound Rae1-Nup98 with Kd = 240 nM; Fig. 1g labels Kd = 0.24 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F60\7F60_metadata.json point structures/7F60/7f60_protein.pdb structures/7F60/7f60_pocket.pdb structures/7F60/7f60_ligand.pdb structures/7F60/7f60_ligand.cif structures/7F60/7f60_complex.pdb structures/7F60/7f60_complex.cif 7F7G extended DLG4 (PSD-95) rat Na Na linear peptide (RIRRDEYLKAIQ) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 34.5 ± 8.84 μM 34500.0 [] unit_conversion 4.462180904926726 success True direct_binding ITC-based measurement of PSD95 GK-domain binding to the linear peptide. 3 Fig. 3 prints Kd = 34.5 ± 8.84 μM for the linear peptide; its caption identifies ITC-based measurements between the PSD95 GK domain and linear peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7F7G\7F7G_metadata.json point structures/7F7G/7f7g_protein.pdb structures/7F7G/7f7g_pocket.pdb structures/7F7G/7f7g_ligand.pdb structures/7F7G/7f7g_ligand.cif structures/7F7G/7f7g_complex.pdb structures/7F7G/7f7g_complex.cif 7F7I extended DLG4 (PSD-95) rat Na Na staple 1 peptide "[""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L""]" 1 Kd Kd = = 1.36 ± 0.05 μM 1360.0 [] unit_conversion 5.866461091629782 success True direct_binding ITC-based measurement of PSD95 GK-domain binding to staple 1 peptide. 3 Fig. 3 prints Kd = 1.36 ± 0.05 μM for Staple1; its caption identifies ITC-based measurements between the PSD95 GK domain and staple 1 peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7F7I\7F7I_metadata.json point structures/7F7I/7f7i_protein.pdb structures/7F7I/7f7i_pocket.pdb structures/7F7I/7f7i_ligand.pdb structures/7F7I/7f7i_ligand.cif structures/7F7I/7f7i_complex.pdb structures/7F7I/7f7i_complex.cif 7F8G classic EYA2 ED human EYA2 ED residues 253-538; GST fusion tag removed Na ETC-616 "[""1RI""]" 1 IC50 IC50 = = 0.26 µM 260.0 [] unit_conversion 6.585026652029182 success True biochemical_inhibition EYA2 ED Tyr phosphatase assay; 5 µM MgCl2. Figure 2 reports ETC-616 IC50; methods specify a purified EYA2 ED enzyme assay. 4 Figure 2 visibly labels ETC-616: “IC50 = 0.26 µM.” The PDB mapping table identifies EYA2 ED–ETC-616 as PDB 7F8G; the assay conditions are described on page 8. auto_single_measurement only accepted activity measurement [1] 1 structures\7F8G\7F8G_metadata.json point structures/7F8G/7f8g_protein.pdb structures/7F8G/7f8g_pocket.pdb structures/7F8G/7f8g_ligand.sdf structures/7F8G/7f8g_ligand.pdb structures/7F8G/7f8g_ligand.cif structures/7F8G/7f8g_complex.pdb structures/7F8G/7f8g_complex.cif 7F8H classic EYA2 ED human EYA2 ED residues 253-538; GST fusion tag removed Na ETC-170 "[""1SI""]" 1 IC50 IC50 = = 0.55 µM 550.0 [] unit_conversion 6.259637310505756 success True biochemical_inhibition EYA2 ED Tyr phosphatase assay; 5 µM MgCl2. Figure 2 reports ETC-170 IC50; methods specify a purified EYA2 ED enzyme assay. 4 Figure 2 visibly labels ETC-170: “IC50 = 0.55 µM.” The PDB mapping table identifies EYA2 ED–ETC-170 as PDB 7F8H; the assay conditions are described on page 8. auto_single_measurement only accepted activity measurement [1] 1 structures\7F8H\7F8H_metadata.json point structures/7F8H/7f8h_protein.pdb structures/7F8H/7f8h_pocket.pdb structures/7F8H/7f8h_ligand.sdf structures/7F8H/7f8h_ligand.pdb structures/7F8H/7f8h_ligand.cif structures/7F8H/7f8h_complex.pdb structures/7F8H/7f8h_complex.cif 7F90 extended Rae1-Nup98 complex Homo sapiens; SARS-CoV Rae1 residues 31-368 and Nup98 residues 157-213, in complex with the SARS-CoV ORF6 C-terminal-tail C3 peptide Na SARS-CoV ORF6 C3 C-terminal-tail peptide "[""POLYMER_ENTITY:1""]" 1 Kd Kd = = 370 nM 370.0 [] unit_conversion 6.431798275933005 success True direct_binding Isothermal titration calorimetry (ITC) of the SARS-CoV ORF6 C3 peptide with Rae1-Nup98. 3 The text states that the binding affinity of the SARS-CoV ORF6 C3 peptide to Rae1-Nup98 was Kd = 370 nM; Fig. 1i labels Kd = 0.37 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F90\7F90_metadata.json point structures/7F90/7f90_protein.pdb structures/7F90/7f90_pocket.pdb structures/7F90/7f90_ligand.pdb structures/7F90/7f90_ligand.cif structures/7F90/7f90_complex.pdb structures/7F90/7f90_complex.cif 7F98 classic Prolyl-tRNA synthetase (HsPRS) Homo sapiens Na Na L95 "[""JE6""]" 1 IC50 IC50 = = 45 nM 45.0 [] unit_conversion 7.346787486224656 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the HsPRS IC50 for L95 as 45 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F98\7F98_metadata.json point structures/7F98/7f98_protein.pdb structures/7F98/7f98_pocket.pdb structures/7F98/7f98_ligand.sdf structures/7F98/7f98_ligand.pdb structures/7F98/7f98_ligand.cif structures/7F98/7f98_complex.pdb structures/7F98/7f98_complex.cif 7F99 classic Prolyl-tRNA synthetase (HsPRS) Homo sapiens Na Na L96 "[""1UI""]" 1 IC50 IC50 = = 1078 nM 1078.0 [] unit_conversion 5.9673812391492795 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the HsPRS IC50 for L96 as 1078 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F99\7F99_metadata.json point structures/7F99/7f99_protein.pdb structures/7F99/7f99_pocket.pdb structures/7F99/7f99_ligand.sdf structures/7F99/7f99_ligand.pdb structures/7F99/7f99_ligand.cif structures/7F99/7f99_complex.pdb structures/7F99/7f99_complex.cif 7F9A classic Prolyl-tRNA synthetase (HsPRS) Homo sapiens Na Na L97 "[""1XK""]" 1 IC50 IC50 = = 1400 nM 1400.0 [] unit_conversion 5.853871964321762 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the HsPRS IC50 for L97 as 1400 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F9A\7F9A_metadata.json point structures/7F9A/7f9a_protein.pdb structures/7F9A/7f9a_pocket.pdb structures/7F9A/7f9a_ligand.sdf structures/7F9A/7f9a_ligand.pdb structures/7F9A/7f9a_ligand.cif structures/7F9A/7f9a_complex.pdb structures/7F9A/7f9a_complex.cif 7F9B classic Prolyl-tRNA synthetase (HsPRS) Homo sapiens Na Na L95 "[""JE6""]" 1 IC50 IC50 = = 45 nM 45.0 [] unit_conversion 7.346787486224656 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the HsPRS IC50 for L95 as 45 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F9B\7F9B_metadata.json point structures/7F9B/7f9b_protein.pdb structures/7F9B/7f9b_pocket.pdb structures/7F9B/7f9b_ligand.sdf structures/7F9B/7f9b_ligand.pdb structures/7F9B/7f9b_ligand.cif structures/7F9B/7f9b_complex.pdb structures/7F9B/7f9b_complex.cif 7F9C classic Prolyl-tRNA synthetase (HsPRS) Homo sapiens Na Na L96 "[""1UI""]" 1 IC50 IC50 = = 1078 nM 1078.0 [] unit_conversion 5.9673812391492795 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the HsPRS IC50 for L96 as 1078 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F9C\7F9C_metadata.json point structures/7F9C/7f9c_protein.pdb structures/7F9C/7f9c_pocket.pdb structures/7F9C/7f9c_ligand.sdf structures/7F9C/7f9c_ligand.pdb structures/7F9C/7f9c_ligand.cif structures/7F9C/7f9c_complex.pdb structures/7F9C/7f9c_complex.cif 7F9D classic Prolyl-tRNA synthetase (HsPRS) Homo sapiens Na Na L96 "[""1UI""]" 1 IC50 IC50 = = 1078 nM 1078.0 [] unit_conversion 5.9673812391492795 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the HsPRS IC50 for L96 as 1078 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7F9D\7F9D_metadata.json point structures/7F9D/7f9d_protein.pdb structures/7F9D/7f9d_pocket.pdb structures/7F9D/7f9d_ligand.sdf structures/7F9D/7f9d_ligand.pdb structures/7F9D/7f9d_ligand.cif structures/7F9D/7f9d_complex.pdb structures/7F9D/7f9d_complex.cif 7F9G classic Thrombocorticin (ThC) Na Recombinant ThC (rThC) Na L-fucose "[""FUC""]" 1 Kd Kd = = 4.72 µM 4720.0 [] unit_conversion 5.326058001365912 success True direct_binding Isothermal titration calorimetry; rThC bound to fucose in the presence of 5 mM Ca²⁺. 2 ITC experiments reported that the KDs of rThC bound to fucose or mannose in the presence of 5 mM Ca²⁺ were 4.72 and 66.2 × 10¹ µM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7F9G\7F9G_metadata.json point structures/7F9G/7f9g_protein.pdb structures/7F9G/7f9g_pocket.pdb structures/7F9G/7f9g_ligand.sdf structures/7F9G/7f9g_ligand.pdb structures/7F9G/7f9g_ligand.cif structures/7F9G/7f9g_complex.pdb structures/7F9G/7f9g_complex.cif 7FAI classic CARM1 human CARM1 residues 140-480 Na compound 9 "[""XJ3""]" 1 IC50 IC50 = = 1.63 ± 0.28 nM 1.63 [] unit_conversion 8.787812395596042 success True biochemical_inhibition CARM1 enzymatic activity; assays performed in replicate (n ≥ 2). 3 Table 1 reports compound 9 CARM1 IC50 = 1.63 ± 0.28 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7FAI\7FAI_metadata.json point structures/7FAI/7fai_protein.pdb structures/7FAI/7fai_pocket.pdb structures/7FAI/7fai_ligand.sdf structures/7FAI/7fai_ligand.pdb structures/7FAI/7fai_ligand.cif structures/7FAI/7fai_complex.pdb structures/7FAI/7fai_complex.cif 7FAJ classic CARM1 human CARM1 residues 140-480 Na compound 43 "[""XJ4""]" 1 IC50 IC50 = = 3.7 nM 3.7 [] unit_conversion 8.431798275933005 success True biochemical_inhibition CARM1 enzyme IC50 displayed in the article graphical abstract. 1 The graphical abstract prints “CARM1 enzyme IC50 = 3.7 nM” for compound 43. auto_single_measurement only accepted activity measurement [1] 1 structures\7FAJ\7FAJ_metadata.json point structures/7FAJ/7faj_protein.pdb structures/7FAJ/7faj_pocket.pdb structures/7FAJ/7faj_ligand.sdf structures/7FAJ/7faj_ligand.pdb structures/7FAJ/7faj_ligand.cif structures/7FAJ/7faj_complex.pdb structures/7FAJ/7faj_complex.cif 7FAK classic Prolyl tRNA synthetase (TgPRS) Toxoplasma gondii Na Na L96 "[""1UI""]" 1 IC50 IC50 = = 79 nM 79.0 [] unit_conversion 7.102372908709558 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the TgPRS IC50 for L96 as 79 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7FAK\7FAK_metadata.json point structures/7FAK/7fak_protein.pdb structures/7FAK/7fak_pocket.pdb structures/7FAK/7fak_ligand.sdf structures/7FAK/7fak_ligand.pdb structures/7FAK/7fak_ligand.cif structures/7FAK/7fak_complex.pdb structures/7FAK/7fak_complex.cif 7FAM classic Prolyl tRNA synthetase (TgPRS) Toxoplasma gondii Na Na L97 "[""1XK""]" 1 IC50 IC50 = = 50 nM 50.0 [] unit_conversion 7.301029995663981 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the TgPRS IC50 for L97 as 50 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7FAM\7FAM_metadata.json point structures/7FAM/7fam_protein.pdb structures/7FAM/7fam_pocket.pdb structures/7FAM/7fam_ligand.sdf structures/7FAM/7fam_ligand.pdb structures/7FAM/7fam_ligand.cif structures/7FAM/7fam_complex.pdb structures/7FAM/7fam_complex.cif 7FAQ classic PDE5A Na Na Na L1 "[""2OI""]" 1 IC50 IC50 = = 55 ± 3 nmol/L 55.0 [] unit_conversion 7.259637310505756 success True biochemical_inhibition PDE5 enzymatic inhibition; Table 1 reports L1 IC50, with the paper identifying the L1 crystal complex as PDE5–L1 (PDB 7FAQ). 4 Table 1 lists L1 with IC50 55 ± 3 nmol/L; Figure 5 assigns the PDE5–L1 complex to PDB ID 7FAQ. auto_single_measurement only accepted activity measurement [1] 1 structures\7FAQ\7FAQ_metadata.json point structures/7FAQ/7faq_protein.pdb structures/7FAQ/7faq_pocket.pdb structures/7FAQ/7faq_ligand.sdf structures/7FAQ/7faq_ligand.pdb structures/7FAQ/7faq_ligand.cif structures/7FAQ/7faq_complex.pdb structures/7FAQ/7faq_complex.cif 7FAR extended PDE5A Na Na Na L12 "[""2VI""]" 1 IC50 IC50 = = 8.3 ± 0.2 nmol/L 8.3 [] unit_conversion 8.080921907623926 success True biochemical_inhibition PDE5A enzymatic inhibition; Table 2 lists PDE5A1 (535–860) inhibition by L12. The paper assigns the PDE5–L12 crystal complex to PDB 7FAR. 8 Table 2 reports PDE5A1 (535–860) IC50 of 8.3 ± 0.2 nmol/L for L12; Figure 5 assigns PDE5–L12 to PDB ID 7FAR. auto_single_measurement only accepted activity measurement [1] 1 structures\7FAR\7FAR_metadata.json point structures/7FAR/7far_protein.pdb structures/7FAR/7far_pocket.pdb structures/7FAR/7far_ligand.pdb structures/7FAR/7far_ligand.cif structures/7FAR/7far_complex.pdb structures/7FAR/7far_complex.cif 7FBL classic Thrombocorticin (ThC) Na Recombinant ThC (rThC) Na D-mannose "[""MAN""]" 1 Kd Kd = = 66.2 × 10¹ µM 662000.0 [] unit_conversion 3.1791420105603 success True direct_binding Isothermal titration calorimetry; rThC bound to mannose in the presence of 5 mM Ca²⁺. 2 ITC experiments reported that the KDs of rThC bound to fucose or mannose in the presence of 5 mM Ca²⁺ were 4.72 and 66.2 × 10¹ µM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7FBL\7FBL_metadata.json point structures/7FBL/7fbl_protein.pdb structures/7FBL/7fbl_pocket.pdb structures/7FBL/7fbl_ligand.sdf structures/7FBL/7fbl_ligand.pdb structures/7FBL/7fbl_ligand.cif structures/7FBL/7fbl_complex.pdb structures/7FBL/7fbl_complex.cif 7FBP extended FXIIa (coagulation factor XIIa) Na Na Na cMCoFx1 "[""CHAIN:B""]" 1 Kd Kd = = 0.90 ± 0.04 nM 0.9 [] unit_conversion 9.045757490560675 success True direct_binding Surface plasmon resonance measurement of cyclic cMCoFx1 binding to FXIIa. 4 Figure 3 reports cyclic cMCoFx1 K_D = 0.90 ± 0.04 nM for FXIIa. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7FBP\7FBP_metadata.json point structures/7FBP/7fbp_protein.pdb structures/7FBP/7fbp_pocket.pdb structures/7FBP/7fbp_ligand.pdb structures/7FBP/7fbp_ligand.cif structures/7FBP/7fbp_complex.pdb structures/7FBP/7fbp_complex.cif 7FCM classic Moraxella catarrhalis enoyl-ACP-reductase (FabI) (McFabI) Moraxella catarrhalis Na Na Triclosan (TCL) "[""TCL""]" 1 Ki Ki = = 62.93 ± 3.95 nM 62.93 [] unit_conversion 7.201142268252514 success True biochemical_inhibition McFabI substrate-velocity enzyme-inhibition assay with TCL; reactions contained NADH and crotonyl-CoA. 10 “The TCL inhibited the McFabI catalytic activity with an inhibition constant (K_i) of 62.93 ± 3.95 nM in an uncompetitive fashion (Fig. 6A).” auto_single_measurement only accepted activity measurement [1] 1 structures\7FCM\7FCM_metadata.json point structures/7FCM/7fcm_protein.pdb structures/7FCM/7fcm_pocket.pdb structures/7FCM/7fcm_ligand.sdf structures/7FCM/7fcm_ligand.pdb structures/7FCM/7fcm_ligand.cif structures/7FCM/7fcm_complex.pdb structures/7FCM/7fcm_complex.cif 7FD0 classic RIPK1 human kinase domain Na compound 20 "[""3IU""]" 1 IC50 IC50 = = 6.6 nM 6.6 [] unit_conversion 8.18045606445813 success True biochemical_inhibition Enzymatic ADP-Glo assay; Table 1 in vitro evaluation of RIPK1 inhibitors. 2 Table 1 reports compound 20 with ADP-Glo IC50 = 6.6 nM; surrounding text identifies this as an enzymatic ADP-Glo assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7FD0\7FD0_metadata.json point structures/7FD0/7fd0_protein.pdb structures/7FD0/7fd0_pocket.pdb structures/7FD0/7fd0_ligand.sdf structures/7FD0/7fd0_ligand.pdb structures/7FD0/7fd0_ligand.cif structures/7FD0/7fd0_complex.pdb structures/7FD0/7fd0_complex.cif 7FGC classic neuraminidase (NA) Asiatic toad influenza B-like virus neuraminidase ectodomain, residues 80 to 466, N2 numbering Na zanamivir "[""ZMR""]" 1 IC50 IC50 = = 140.90 ± 17.50 nM 140.9 [] unit_conversion 6.851089006890644 success True biochemical_inhibition MUNANA fluorescence NA-inhibition assay; Table 1 reports mean ± SEM from three independent experiments. 6 Table 1 reports Wuhan Asiatic toad NA IC50 for zanamivir as 140.90 ± 17.50 nM; page 10 maps 7FGC to tNA-zanamivir. auto_single_measurement only accepted activity measurement [1] 1 structures\7FGC\7FGC_metadata.json point structures/7FGC/7fgc_protein.pdb structures/7FGC/7fgc_pocket.pdb structures/7FGC/7fgc_ligand.sdf structures/7FGC/7fgc_ligand.pdb structures/7FGC/7fgc_ligand.cif structures/7FGC/7fgc_complex.pdb structures/7FGC/7fgc_complex.cif 7FGD classic neuraminidase (NA) Asiatic toad influenza B-like virus neuraminidase ectodomain, residues 80 to 466, N2 numbering Na oseltamivir carboxylate "[""G39""]" 1 IC50 IC50 = = 10,378 ± 594 nM 10378.0 [] unit_conversion 4.983886333641092 success True biochemical_inhibition MUNANA fluorescence NA-inhibition assay; Table 1 reports mean ± SEM from three independent experiments. 6 Table 1 reports Wuhan Asiatic toad NA IC50 for oseltamivir carboxylate as 10,378 ± 594 nM; page 10 maps 7FGD to tNA-oseltamivir carboxylate. auto_single_measurement only accepted activity measurement [1] 1 structures\7FGD\7FGD_metadata.json point structures/7FGD/7fgd_protein.pdb structures/7FGD/7fgd_pocket.pdb structures/7FGD/7fgd_ligand.sdf structures/7FGD/7fgd_ligand.pdb structures/7FGD/7fgd_ligand.cif structures/7FGD/7fgd_complex.pdb structures/7FGD/7fgd_complex.cif 7FGE classic neuraminidase (NA) Asiatic toad influenza B-like virus neuraminidase ectodomain, residues 80 to 466, N2 numbering Na peramivir "[""BCZ""]" 1 IC50 IC50 = = 1,771 ± 231 nM 1771.0 [] unit_conversion 5.751781438809925 success True biochemical_inhibition MUNANA fluorescence NA-inhibition assay; Table 1 reports mean ± SEM from three independent experiments. 6 Table 1 reports Wuhan Asiatic toad NA IC50 for peramivir as 1,771 ± 231 nM; page 10 maps 7FGE to tNA-peramivir. auto_single_measurement only accepted activity measurement [1] 1 structures\7FGE\7FGE_metadata.json point structures/7FGE/7fge_protein.pdb structures/7FGE/7fge_pocket.pdb structures/7FGE/7fge_ligand.sdf structures/7FGE/7fge_ligand.pdb structures/7FGE/7fge_ligand.cif structures/7FGE/7fge_complex.pdb structures/7FGE/7fge_complex.cif 7FH2 classic BRD4-BD1 Na N-terminally hexa-His-tagged BRD4-BD1, residues 42-168 Na 16D10 "[""4JI""]" 1 Kd Kd = = 1.5 ± 0.077 μM 1500.0 [] unit_conversion 5.823908740944319 success True direct_binding Reverse isothermal titration calorimetry of BRD4-BD1 with 16D10; table reports two measurements. 4 Fig. 3B reports the thermodynamic parameters for binding to BRD4-BD1: 16D10 Kd = 1.5 ± 0.077 μM (number of measurements, 2). auto_single_measurement only accepted activity measurement [1] 1 structures\7FH2\7FH2_metadata.json point structures/7FH2/7fh2_protein.pdb structures/7FH2/7fh2_pocket.pdb structures/7FH2/7fh2_ligand.sdf structures/7FH2/7fh2_ligand.pdb structures/7FH2/7fh2_ligand.cif structures/7FH2/7fh2_complex.pdb structures/7FH2/7fh2_complex.cif 7FJH classic LecA Pseudomonas aeruginosa Na Na 4-Phenylbutyryl hydroxamic acid; compound 35 "[""4R9""]" 1 Kd Kd = = 4.6 ± 0.9 mM 4600000.0 [] unit_conversion 2.3372421683184257 success True direct_binding Protein-observed 19F NMR (5FW LecA), following CSPs of W42; one-site binding model. 4 Figure 2e and its caption explicitly report “Kd = 4.6 ± 0.9 mM” for compound 35 binding LecA; the caption identifies compound 35 and the ProF NMR assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7FJH\7FJH_metadata.json point structures/7FJH/7fjh_protein.pdb structures/7FJH/7fjh_pocket.pdb structures/7FJH/7fjh_ligand.sdf structures/7FJH/7fjh_ligand.pdb structures/7FJH/7fjh_ligand.cif structures/7FJH/7fjh_complex.pdb structures/7FJH/7fjh_complex.cif 7FV6 classic PHIP Na Na Na Z1334218055 "[""ZKZ""]" 1 Kd Kd = = 18.0 [14.95; 21.05] μM 18000.0 [] unit_conversion 4.7447274948966935 success True direct_binding Grating-coupled interferometry (GCI) kinetic binding assay; Fig. 8 maps LAT33 to PDB 7FV6 and reports its Kd. 12 Fig. 8a labels LAT33 as PDB 7FV6; Fig. 8c prints “3: LAT33 Kd=18.0 [14.95; 21.05] μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\7FV6\7FV6_metadata.json point structures/7FV6/7fv6_protein.pdb structures/7FV6/7fv6_pocket.pdb structures/7FV6/7fv6_ligand.sdf structures/7FV6/7fv6_ligand.pdb structures/7FV6/7fv6_ligand.cif structures/7FV6/7fv6_complex.pdb structures/7FV6/7fv6_complex.cif 7GAW classic SARS-CoV-2 main protease SARS-CoV-2 Na Na MAT-POS-e194df51-1; SARS2_MproA-x0862 "[""KG9""]" 1 IC50 IC50 = = 0.0368 [0.0343, 0.0395] μM 36.8 [] unit_conversion 7.434152181326482 success True biochemical_inhibition Mpro biochemical inhibition; Fig. 5A milestone table. 11 Fig. 5A identifies MAT-POS-e194df51-1 as Mpro-x0862 / 7GAW and prints Mpro IC50 0.0368 [0.0343, 0.0395] μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7GAW\7GAW_metadata.json point structures/7GAW/7gaw_protein.pdb structures/7GAW/7gaw_pocket.pdb structures/7GAW/7gaw_ligand.sdf structures/7GAW/7gaw_ligand.pdb structures/7GAW/7gaw_ligand.cif structures/7GAW/7gaw_complex.pdb structures/7GAW/7gaw_complex.cif 7GDD classic SARS-CoV-2 main protease SARS-CoV-2 Na Na ADA-UCB-6c2cb422-1 (Mpro-x10959) "[""860""]" 1 IC50 IC50 = = 720 nM 720.0 [] unit_conversion 6.142667503568731 success True biochemical_inhibition Direct biochemical screening in the Chan-Lam series; Figure 2D labels ADA-UCB-6c2cb422-1 as Mpro-x10959 / 7GDD and prints IC50 = 720 nM. 7 Figure 2D explicitly labels “ADA-UCB-6c2cb422-1, Mpro-x10959 / 7GDD, IC50 = 720 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7GDD\7GDD_metadata.json point structures/7GDD/7gdd_protein.pdb structures/7GDD/7gdd_pocket.pdb structures/7GDD/7gdd_ligand.sdf structures/7GDD/7gdd_ligand.pdb structures/7GDD/7gdd_ligand.cif structures/7GDD/7gdd_complex.pdb structures/7GDD/7gdd_complex.cif 7GFB classic SARS-CoV-2 main protease SARS-CoV-2 Na Na MAT-POS-b3e365b9-1 (Mpro-x11612) "[""NSR""]" 1 IC50 IC50 = = 0.255 [0.240, 0.270] µM 255.0 [] unit_conversion 6.5934598195660445 success True biochemical_inhibition Experimental Mpro IC50 in the iterative medicinal-chemistry series; biochemical activity assay. 11 Figure 5A lists MAT-POS-b3e365b9-1 with Mpro IC50 0.255 [0.240, 0.270] µM; its caption identifies these as experimental biochemical activities. auto_single_measurement only accepted activity measurement [1] 1 structures\7GFB\7GFB_metadata.json point structures/7GFB/7gfb_protein.pdb structures/7GFB/7gfb_pocket.pdb structures/7GFB/7gfb_ligand.sdf structures/7GFB/7gfb_ligand.pdb structures/7GFB/7gfb_ligand.cif structures/7GFB/7gfb_complex.pdb structures/7GFB/7gfb_complex.cif 7GJM classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na EDJ-MED-e4b030d8-11 (Mpro-P0601) "[""QP0""]" 1 pIC50 IC50 = = 8.6 unitless 2.5118864315095824 [] p_metric_transform 8.6 success True biochemical_inhibition Experimental pIC50 shown for EDJ-MED-e4b030d8-11 in the prospective alchemical free-energy calculation panel; the paper describes Mpro biochemical inhibition assays separately. 7 Fig. 2C explicitly lists for EDJ-MED-e4b030d8-11: “Exp pIC₅₀ = 8.6.” The Fig. 2 caption identifies these as experimental pIC₅₀ values; 7GJM is supplied as the structure of this same ligand. auto_single_measurement only accepted activity measurement [1] 1 structures\7GJM\7GJM_metadata.json point structures/7GJM/7gjm_protein.pdb structures/7GJM/7gjm_pocket.pdb structures/7GJM/7gjm_ligand.sdf structures/7GJM/7gjm_ligand.pdb structures/7GJM/7gjm_ligand.cif structures/7GJM/7gjm_complex.pdb structures/7GJM/7gjm_complex.cif 7GLP classic SARS-CoV-2 main protease SARS-CoV-2 Na Na ADA-UCB-6c2cb422-1 (Mpro-P2005) "[""860""]" 1 IC50 IC50 = = 720 nM 720.0 [] unit_conversion 6.142667503568731 success True biochemical_inhibition Nanomole-scale high-throughput chemistry; direct biochemical screening of crude reactions against Mpro. 7 Fig. 2D explicitly labels ADA-UCB-6c2cb422-1 with “IC50 = 720 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7GLP\7GLP_metadata.json point structures/7GLP/7glp_protein.pdb structures/7GLP/7glp_pocket.pdb structures/7GLP/7glp_ligand.sdf structures/7GLP/7glp_ligand.pdb structures/7GLP/7glp_ligand.cif structures/7GLP/7glp_complex.pdb structures/7GLP/7glp_complex.cif 7GNL classic SARS-CoV-2 main protease SARS-CoV-2 Na Na NIR-WEI-dcc3321b-1 (Mpro-P2757) "[""S1U""]" 1 IC50 IC50 = = 28 nM 28.0 [] unit_conversion 7.552841968657781 success True biochemical_inhibition Direct biochemical screening in the nanomole-scale high-throughput chemistry campaign. 7 Fig. 2D labels NIR-WEI-dcc3321b-1 as Mpro-P2757 / 7GNL and prints IC50 = 28 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7GNL\7GNL_metadata.json point structures/7GNL/7gnl_protein.pdb structures/7GNL/7gnl_pocket.pdb structures/7GNL/7gnl_ligand.sdf structures/7GNL/7gnl_ligand.pdb structures/7GNL/7gnl_ligand.cif structures/7GNL/7gnl_complex.pdb structures/7GNL/7gnl_complex.cif 7HCG classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-0000316 (AVI-316) "[""A1A5B""]" 1 IC50 IC50 > > 1 mM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition Purified Mac1 HTRF competitive binding assay; confirmatory dose-response IC50. 5 Figure 2B labels AVI-316, PDB 7HCG, as “>1 mM”; the caption identifies the printed dose-response values as IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\7HCG\7HCG_metadata.json point structures/7HCG/7hcg_protein.pdb structures/7HCG/7hcg_pocket.pdb structures/7HCG/7hcg_ligand.sdf structures/7HCG/7hcg_ligand.pdb structures/7HCG/7hcg_ligand.cif structures/7HCG/7hcg_complex.pdb structures/7HCG/7hcg_complex.cif 7HCH classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-0000317 (AVI-317) "[""A1A5C""]" 1 IC50 IC50 > > 1 mM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition Purified Mac1 HTRF competitive binding assay; confirmatory dose-response IC50. 5 Figure 2B labels AVI-317, PDB 7HCH, as “>1 mM”; the caption identifies the printed dose-response values as IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\7HCH\7HCH_metadata.json point structures/7HCH/7hch_protein.pdb structures/7HCH/7hch_pocket.pdb structures/7HCH/7hch_ligand.sdf structures/7HCH/7hch_ligand.pdb structures/7HCH/7hch_ligand.cif structures/7HCH/7hch_complex.pdb structures/7HCH/7hch_complex.cif 7HCO classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-0000291 (AVI-291) "[""A1A5X""]" 1 IC50 IC50 > > 1 mM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition Purified Mac1 HTRF competitive binding assay; confirmatory dose-response IC50. 5 Figure 2B labels AVI-291 as “>1 mM”; the caption identifies the printed dose-response values as IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\7HCO\7HCO_metadata.json point structures/7HCO/7hco_protein.pdb structures/7HCO/7hco_pocket.pdb structures/7HCO/7hco_ligand.sdf structures/7HCO/7hco_ligand.pdb structures/7HCO/7hco_ligand.cif structures/7HCO/7hco_complex.pdb structures/7HCO/7hco_complex.cif 7HDL classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-0003731 (AVI-3731) "[""A1A8J""]" 1 IC50 IC50 = = 3.7 µM 3700.0 [] unit_conversion 5.431798275933005 success True biochemical_inhibition Confirmatory HTRF competitive assay; the Figure 9 entry maps the (R) AVI-3731 material to PDB 7HDL. 14 Fig. 9 lists AVI-3731 (R), PDB 7HDL, and IC50 3.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7HDL\7HDL_metadata.json point structures/7HDL/7hdl_protein.pdb structures/7HDL/7hdl_pocket.pdb structures/7HDL/7hdl_ligand.sdf structures/7HDL/7hdl_ligand.pdb structures/7HDL/7hdl_ligand.cif structures/7HDL/7hdl_complex.pdb structures/7HDL/7hdl_complex.cif 7HF4 classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-0004066 (paper: AVI-4066) "[""A1BAO""]" 1 IC50 IC50 = = 720 µM 720000.0 [] unit_conversion 3.142667503568732 success True biochemical_inhibition HTRF peptide-displacement competition assay; Figure 6 reports the confirmatory dose-response IC50. 9 Fig. 6 lists AVI-4066, PDB 7HF4, IC50 720 µM; caption defines listed IC50 values as confirmatory dose-response values. auto_single_measurement only accepted activity measurement [1] 1 structures\7HF4\7HF4_metadata.json point structures/7HF4/7hf4_protein.pdb structures/7HF4/7hf4_pocket.pdb structures/7HF4/7hf4_ligand.sdf structures/7HF4/7hf4_ligand.pdb structures/7HF4/7hf4_ligand.cif structures/7HF4/7hf4_complex.pdb structures/7HF4/7hf4_complex.cif 7HFY classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-0006217 (paper: AVI-6217) "[""A1BCD""]" 1 IC50 IC50 = = 42 µM 42000.0 [] unit_conversion 4.376750709602099 success True direct_binding Confirmatory dose-response HTRF peptide-displacement binding assay. 12 Figure 8 lists AVI-6217, PDB 7HFY, with IC50 42 µM; the caption identifies the confirmatory HTRF dose-response screen. auto_single_measurement only accepted activity measurement [1] 1 structures\7HFY\7HFY_metadata.json point structures/7HFY/7hfy_protein.pdb structures/7HFY/7hfy_pocket.pdb structures/7HFY/7hfy_ligand.sdf structures/7HFY/7hfy_ligand.pdb structures/7HFY/7hfy_ligand.cif structures/7HFY/7hfy_complex.pdb structures/7HFY/7hfy_complex.cif 7I7Y classic CK2a Na Na Na 30 "[""A1BZS""]" 1 IC50 IC50 = = 0.461 ± 0.112 nM 0.461 [] unit_conversion 9.336299074610352 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 0.461 ± 0.112 nM for compound 30. auto_single_measurement only accepted activity measurement [1] 1 structures\7I7Y\7I7Y_metadata.json point structures/7I7Y/7i7y_protein.pdb structures/7I7Y/7i7y_pocket.pdb structures/7I7Y/7i7y_ligand.sdf structures/7I7Y/7i7y_ligand.pdb structures/7I7Y/7i7y_ligand.cif structures/7I7Y/7i7y_complex.pdb structures/7I7Y/7i7y_complex.cif 7I7Z classic CK2a Na Na Na 31 "[""A1BZR""]" 1 IC50 IC50 = = 35.3 ± 5.1 nM 35.3 [] unit_conversion 7.452225294612178 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 35.3 ± 5.1 nM for compound 31. auto_single_measurement only accepted activity measurement [1] 1 structures\7I7Z\7I7Z_metadata.json point structures/7I7Z/7i7z_protein.pdb structures/7I7Z/7i7z_pocket.pdb structures/7I7Z/7i7z_ligand.sdf structures/7I7Z/7i7z_ligand.pdb structures/7I7Z/7i7z_ligand.cif structures/7I7Z/7i7z_complex.pdb structures/7I7Z/7i7z_complex.cif 7I80 classic CK2a Na Na Na 19 "[""A1BZ2""]" 1 IC50 IC50 = = 6.92 ± 2.17 nM 6.92 [] unit_conversion 8.159893905543242 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 6.92 ± 2.17 nM for compound 19. auto_single_measurement only accepted activity measurement [1] 1 structures\7I80\7I80_metadata.json point structures/7I80/7i80_protein.pdb structures/7I80/7i80_pocket.pdb structures/7I80/7i80_ligand.sdf structures/7I80/7i80_ligand.pdb structures/7I80/7i80_ligand.cif structures/7I80/7i80_complex.pdb structures/7I80/7i80_complex.cif 7I81 classic CK2a Na Na Na 22 "[""A1BZ1""]" 1 IC50 IC50 = = 0.244 ± 0.094 nM 0.244 [] unit_conversion 9.61261017366127 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 0.244 ± 0.094 nM for compound 22. auto_single_measurement only accepted activity measurement [1] 1 structures\7I81\7I81_metadata.json point structures/7I81/7i81_protein.pdb structures/7I81/7i81_pocket.pdb structures/7I81/7i81_ligand.sdf structures/7I81/7i81_ligand.pdb structures/7I81/7i81_ligand.cif structures/7I81/7i81_complex.pdb structures/7I81/7i81_complex.cif 7I82 classic CK2a Na Na Na 20 "[""A1BZ0""]" 1 IC50 IC50 = = 2.00 ± 0.31 nM 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 2.00 ± 0.31 nM for compound 20. auto_single_measurement only accepted activity measurement [1] 1 structures\7I82\7I82_metadata.json point structures/7I82/7i82_protein.pdb structures/7I82/7i82_pocket.pdb structures/7I82/7i82_ligand.sdf structures/7I82/7i82_ligand.pdb structures/7I82/7i82_ligand.cif structures/7I82/7i82_complex.pdb structures/7I82/7i82_complex.cif 7I83 extended CK2a Na Na Na 33 "[""A1BZZ""]" 1 IC50 IC50 = = 0.297 ± 0.127 nM 0.297 [] unit_conversion 9.527243550682787 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 0.297 ± 0.127 nM for compound 33. auto_single_measurement only accepted activity measurement [1] 1 structures\7I83\7I83_metadata.json point structures/7I83/7i83_protein.pdb structures/7I83/7i83_pocket.pdb structures/7I83/7i83_ligand.pdb structures/7I83/7i83_ligand.cif structures/7I83/7i83_complex.pdb structures/7I83/7i83_complex.cif 7I85 classic CK2a Na Na Na 49 "[""A1B0C""]" 1 IC50 IC50 = = 65.6 nM 65.6 [] unit_conversion 7.1830961606243395 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 65.6 nM for compound 49. auto_single_measurement only accepted activity measurement [1] 1 structures\7I85\7I85_metadata.json point structures/7I85/7i85_protein.pdb structures/7I85/7i85_pocket.pdb structures/7I85/7i85_ligand.sdf structures/7I85/7i85_ligand.pdb structures/7I85/7i85_ligand.cif structures/7I85/7i85_complex.pdb structures/7I85/7i85_complex.cif 7I86 classic CK2a Na Na Na 23 "[""A1B0D""]" 1 IC50 IC50 = = 0.201 ± 0.052 nM 0.201 [] unit_conversion 9.69680394257951 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 0.201 ± 0.052 nM for compound 23. auto_single_measurement only accepted activity measurement [1] 1 structures\7I86\7I86_metadata.json point structures/7I86/7i86_protein.pdb structures/7I86/7i86_pocket.pdb structures/7I86/7i86_ligand.sdf structures/7I86/7i86_ligand.pdb structures/7I86/7i86_ligand.cif structures/7I86/7i86_complex.pdb structures/7I86/7i86_complex.cif 7I87 classic CK2a Na Na Na 44 "[""A1B0K""]" 1 IC50 IC50 = = 0.306 ± 0.093 nM 0.306 [] unit_conversion 9.51427857351842 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 of 0.306 ± 0.093 nM for compound 44. auto_single_measurement only accepted activity measurement [1] 1 structures\7I87\7I87_metadata.json point structures/7I87/7i87_protein.pdb structures/7I87/7i87_pocket.pdb structures/7I87/7i87_ligand.sdf structures/7I87/7i87_ligand.pdb structures/7I87/7i87_ligand.cif structures/7I87/7i87_complex.pdb structures/7I87/7i87_complex.cif 7I88 classic CK2a Na Na Na 50 "[""A1B0J""]" 1 IC50 IC50 > > 1,000 nM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 9 Table 2 reports CK2α IC50 >1,000 nM for compound 50. auto_single_measurement only accepted activity measurement [1] 1 structures\7I88\7I88_metadata.json point structures/7I88/7i88_protein.pdb structures/7I88/7i88_pocket.pdb structures/7I88/7i88_ligand.sdf structures/7I88/7i88_ligand.pdb structures/7I88/7i88_ligand.cif structures/7I88/7i88_complex.pdb structures/7I88/7i88_complex.cif 7I8A classic CK2a Na Na Na 54f "[""A1B0F""]" 1 IC50 IC50 = = 0.586 ± 0.159 nM 0.586 [] unit_conversion 9.232102383981909 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 12 Table 3 reports CK2α IC50 of 0.586 ± 0.159 nM for compound 54f. auto_single_measurement only accepted activity measurement [1] 1 structures\7I8A\7I8A_metadata.json point structures/7I8A/7i8a_protein.pdb structures/7I8A/7i8a_pocket.pdb structures/7I8A/7i8a_ligand.sdf structures/7I8A/7i8a_ligand.pdb structures/7I8A/7i8a_ligand.cif structures/7I8A/7i8a_complex.pdb structures/7I8A/7i8a_complex.cif 7I8B classic CK2a Na Na Na 54b "[""A1B0G""]" 1 IC50 IC50 = = 0.568 ± 0.106 nM 0.568 [] unit_conversion 9.245651664288982 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 12 Table 3 reports CK2α IC50 of 0.568 ± 0.106 nM for compound 54b. auto_single_measurement only accepted activity measurement [1] 1 structures\7I8B\7I8B_metadata.json point structures/7I8B/7i8b_protein.pdb structures/7I8B/7i8b_pocket.pdb structures/7I8B/7i8b_ligand.sdf structures/7I8B/7i8b_ligand.pdb structures/7I8B/7i8b_ligand.cif structures/7I8B/7i8b_complex.pdb structures/7I8B/7i8b_complex.cif 7I8D classic CK2a Na Na Na 61a "[""A1B0A""]" 1 IC50 IC50 = = 0.404 ± 0.151 nM 0.404 [] unit_conversion 9.393618634889394 success True biochemical_inhibition ADP-Glo kinase inhibition assay; ATP concentration at or below apparent KM. 15 Table 5 reports CK2α IC50 of 0.404 ± 0.151 nM for compound 61a. auto_single_measurement only accepted activity measurement [1] 1 structures\7I8D\7I8D_metadata.json point structures/7I8D/7i8d_protein.pdb structures/7I8D/7i8d_pocket.pdb structures/7I8D/7i8d_ligand.sdf structures/7I8D/7i8d_ligand.pdb structures/7I8D/7i8d_ligand.cif structures/7I8D/7i8d_complex.pdb structures/7I8D/7i8d_complex.cif 7I8K classic CK2a Na CK2alpha_KA mutant Na 61f "[""A1BZ3""]" 1 Kd Kd = = 1.4 ± 0.65 nM 1.4 [] unit_conversion 8.853871964321762 success True direct_binding Surface plasmon resonance binding assay using double-His-tagged CK2α kinase domain. 17 Table 6 prints CK2α Kd = 1.4 ± 0.65 nM for 61f; the SPR method specifies a CK2α kinase domain but does not state its exact construct or mutation. auto_single_measurement only accepted activity measurement [1] 1 structures\7I8K\7I8K_metadata.json point structures/7I8K/7i8k_protein.pdb structures/7I8K/7i8k_pocket.pdb structures/7I8K/7i8k_ligand.sdf structures/7I8K/7i8k_ligand.pdb structures/7I8K/7i8k_ligand.cif structures/7I8K/7i8k_complex.pdb structures/7I8K/7i8k_complex.cif 7JG0 classic Human GAR transformylase (GARFTase) human GAR formyltransferase domain of trifunctional purine biosynthetic protein adenosine-3, residues 808-1010, with a non-cleavable C-terminal hexahistidine tag Na compound 3 "[""V97""]" 1 Ki Ki = = 1.36 (0.63) µM 1360.0 [] unit_conversion 5.866461091629782 success True biochemical_inhibition Biochemical enzyme-inhibition assay. 0 The supplement maps 7JG0 to compound 3 and reports Ki 1.36 (0.63) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7JG0\7JG0_metadata.json point structures/7JG0/7jg0_protein.pdb structures/7JG0/7jg0_pocket.pdb structures/7JG0/7jg0_ligand.sdf structures/7JG0/7jg0_ligand.pdb structures/7JG0/7jg0_ligand.cif structures/7JG0/7jg0_complex.pdb structures/7JG0/7jg0_complex.cif 7JG3 classic Human GAR transformylase (GARFTase) human GAR formyltransferase domain of trifunctional purine biosynthetic protein adenosine-3, residues 808-1010, with a non-cleavable C-terminal hexahistidine tag Na compound 4 "[""V9A""]" 1 Ki Ki = = 10.72 (2.74) µM 10720.0 [] unit_conversion 4.969805214643249 success True biochemical_inhibition Biochemical enzyme-inhibition assay. 0 The supplement maps 7JG3 to compound 4 and reports Ki 10.72 (2.74) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7JG3\7JG3_metadata.json point structures/7JG3/7jg3_protein.pdb structures/7JG3/7jg3_pocket.pdb structures/7JG3/7jg3_ligand.sdf structures/7JG3/7jg3_ligand.pdb structures/7JG3/7jg3_ligand.cif structures/7JG3/7jg3_complex.pdb structures/7JG3/7jg3_complex.cif 7JG4 classic Human GAR transformylase (GARFTase) human GAR formyltransferase domain of trifunctional purine biosynthetic protein adenosine-3, residues 808-1010, with a non-cleavable C-terminal hexahistidine tag Na compound 5 "[""V9V""]" 1 Ki Ki = = 8.19 (3.22) µM 8189.999999999999 [] unit_conversion 5.086716098239581 success True biochemical_inhibition Biochemical enzyme-inhibition assay. 0 The supplement maps 7JG4 to compound 5 and reports Ki 8.19 (3.22) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7JG4\7JG4_metadata.json point structures/7JG4/7jg4_protein.pdb structures/7JG4/7jg4_pocket.pdb structures/7JG4/7jg4_ligand.sdf structures/7JG4/7jg4_ligand.pdb structures/7JG4/7jg4_ligand.cif structures/7JG4/7jg4_complex.pdb structures/7JG4/7jg4_complex.cif 7JGV classic human BCL-XL human BCL-XLDelta27-82 DeltaC24 Na compound 43 (PDB/internal code 1620116) "[""V9S""]" 1 IC50 IC50 = = 0.015 μM 15.0 [] unit_conversion 7.823908740944319 success True biochemical_inhibition AlphaScreen assay using GST-tagged BCL-XL in competition with biotinylated BIM peptide. 7 Table 3 reports compound 43 BCL-XL IC50 0.015 (0.002) μM; the text identifies 7JGV as human BCL-XL bound to compound 43. auto_single_measurement only accepted activity measurement [1] 1 structures\7JGV\7JGV_metadata.json point structures/7JGV/7jgv_protein.pdb structures/7JGV/7jgv_pocket.pdb structures/7JGV/7jgv_ligand.sdf structures/7JGV/7jgv_ligand.pdb structures/7JGV/7jgv_ligand.cif structures/7JGV/7jgv_complex.pdb structures/7JGV/7jgv_complex.cif 7JGW classic human BCL-XL human BCL-XLDelta27-82 DeltaC24 Na compound 43 (PDB/internal code 1620116) "[""V9S""]" 1 IC50 IC50 = = 0.015 μM 15.0 [] unit_conversion 7.823908740944319 success True biochemical_inhibition AlphaScreen assay using GST-tagged BCL-XL in competition with biotinylated BIM peptide. 7 Table 3 reports compound 43 BCL-XL IC50 0.015 (0.002) μM; the text identifies 7JGW as human BCL-XL bound to compound 43. auto_single_measurement only accepted activity measurement [1] 1 structures\7JGW\7JGW_metadata.json point structures/7JGW/7jgw_protein.pdb structures/7JGW/7jgw_pocket.pdb structures/7JGW/7jgw_ligand.sdf structures/7JGW/7jgw_ligand.pdb structures/7JGW/7jgw_ligand.cif structures/7JGW/7jgw_complex.pdb structures/7JGW/7jgw_complex.cif 7JHX extended GABARAPL1 Homo sapiens GABARAPL1 in complex with hEPG5-LIR2 peptide Na hEPG5-LIR2 peptide (residues 560-571) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.09 µM 90.0 [] unit_conversion 7.045757490560675 success True direct_binding Isothermal titration calorimetry of LIR2 peptide titrated into GABARAPL1. 6 Fig. 3b reports Kd 0.09 µM for GABARAPL1 + LIR2; the caption identifies LIR2 as hEPG5 residues 560–571. auto_single_measurement only accepted activity measurement [1] 1 structures\7JHX\7JHX_metadata.json point structures/7JHX/7jhx_protein.pdb structures/7JHX/7jhx_pocket.pdb structures/7JHX/7jhx_ligand.pdb structures/7JHX/7jhx_ligand.cif structures/7JHX/7jhx_complex.pdb structures/7JHX/7jhx_complex.cif 7JI4 classic Universal stress protein (USP) domain of KdpD histidine kinase Staphylococcus aureus (MRSA252) USP_Sa domain, residues T213-N364 Na c-di-AMP "[""2BA""]" 1 Kd Kd = = 0.5 ± 0.06 µM 500.0 [] unit_conversion 6.301029995663981 success True direct_binding MicroScale Thermophoresis (ligand-induced fluorescence change) using purified His6-USP_Sa; c-di-AMP binding. 5 “His6-USPSa bound to c-di-AMP with a dissociation constant (KD) of 0.5 ± 0.06 µM (Table S3)” by MicroScale Thermophoresis. auto_single_measurement only accepted activity measurement [1] 1 structures\7JI4\7JI4_metadata.json point structures/7JI4/7ji4_protein.pdb structures/7JI4/7ji4_pocket.pdb structures/7JI4/7ji4_ligand.sdf structures/7JI4/7ji4_ligand.pdb structures/7JI4/7ji4_ligand.cif structures/7JI4/7ji4_complex.pdb structures/7JI4/7ji4_complex.cif 7JJG classic TAF1 human TAF1 BD2, residues 1501-1635 Na AZ20 "[""VCD""]" 1 Kd Kd > > 25,000 nM 25000.0 [] unit_conversion 4.6020599913279625 success True direct_binding ITC; Figure 1E table. 2 The AZ20 row reports ITC Kd >25,000 nM for TAF1-2. auto_single_measurement only accepted activity measurement [1] 1 structures\7JJG\7JJG_metadata.json point structures/7JJG/7jjg_protein.pdb structures/7JJG/7jjg_pocket.pdb structures/7JJG/7jjg_ligand.sdf structures/7JJG/7jjg_ligand.pdb structures/7JJG/7jjg_ligand.cif structures/7JJG/7jjg_complex.pdb structures/7JJG/7jjg_complex.cif 7JLS extended MtDppA (Rv3666c) Mycobacterium tuberculosis Rv3666c with residues 1-30 truncated, an N-terminal biotin acceptor peptide, and a C-terminal 8xHis tag Na SVA tripeptide "[""CHAIN:B""]" 1 Kd Kd = = 528 ± 2 nM 528.0 [] unit_conversion 6.277366077466188 success True direct_binding Surface plasmon resonance sensorgram; Fig. 2C. 4 Fig. 2 table reports for SVA: K_D (nM) = 528 ± 2; the text states SPR orthogonally validated binding of SVA to MtDppA. auto_single_measurement only accepted activity measurement [1] 1 structures\7JLS\7JLS_metadata.json point structures/7JLS/7jls_protein.pdb structures/7JLS/7jls_pocket.pdb structures/7JLS/7jls_ligand.pdb structures/7JLS/7jls_ligand.cif structures/7JLS/7jls_complex.pdb structures/7JLS/7jls_complex.cif 7JMT extended schistosome BCL-2 (sBCL-2) Schistosoma japonicum sBCL-2DeltaC40 Na ABT-737 "[""N3C""]" 1 IC50 IC50 = = 170 nM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition sBCL-2 AlphaScreen assay with biotinylated BIM BH3 peptide; Table 1 footnote states ABT-737 sBCL-2 IC50. 3 Table 1 footnote explicitly states: ABT-737 (1) sBCL-2 IC50 170 (20) nM. The paper identifies the ABT-737–S. japonicum sBCL-2 structure as PDB 7JMT. auto_single_measurement only accepted activity measurement [1] 1 structures\7JMT\7JMT_metadata.json point structures/7JMT/7jmt_protein.pdb structures/7JMT/7jmt_pocket.pdb structures/7JMT/7jmt_ligand.pdb structures/7JMT/7jmt_ligand.cif structures/7JMT/7jmt_complex.pdb structures/7JMT/7jmt_complex.cif 7JNB classic ZmpB Clostridium perfringens Selenomethionine-labeled CBM32-1/2 construct, residues 28-453 Na GalNAc (N-acetylgalactosamine) "[""A2G""]" 1 Kd Kd = = 2.9 mM 2900000.0 [] unit_conversion 2.5376020021010435 success True direct_binding Isothermal titration calorimetry of isolated recombinant CBM constructs; CBM32-1 bound GalNAc. 5 Only CBM32-1 and CBM51-2 bound GalNAc and GlcNAc, respectively, with measurable dissociation constants (Kd) of 2.9 mM and 2.6 mM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7JNB\7JNB_metadata.json point structures/7JNB/7jnb_protein.pdb structures/7JNB/7jnb_pocket.pdb structures/7JNB/7jnb_ligand.sdf structures/7JNB/7jnb_ligand.pdb structures/7JNB/7jnb_ligand.cif structures/7JNB/7jnb_complex.pdb structures/7JNB/7jnb_complex.cif 7JNF classic ZmpB Clostridium perfringens CBM32-1/2 construct, residues 28-453 Na GalNAc (N-acetylgalactosamine) "[""A2G""]" 1 Kd Kd = = 2.9 mM 2900000.0 [] unit_conversion 2.5376020021010435 success True direct_binding Isothermal titration calorimetry of isolated recombinant CBM constructs; CBM32-1 bound GalNAc. 5 Only CBM32-1 and CBM51-2 bound GalNAc and GlcNAc, respectively, with measurable dissociation constants (Kd) of 2.9 mM and 2.6 mM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7JNF\7JNF_metadata.json point structures/7JNF/7jnf_protein.pdb structures/7JNF/7jnf_pocket.pdb structures/7JNF/7jnf_ligand.sdf structures/7JNF/7jnf_ligand.pdb structures/7JNF/7jnf_ligand.cif structures/7JNF/7jnf_complex.pdb structures/7JNF/7jnf_complex.cif 7JOM classic histone deacetylase 6 (HDAC6) Danio rerio Na Na TO-317 "[""TO3""]" 1 Ki Ki = = 0.7 nM 0.7 [] unit_conversion 9.154901959985743 success True direct_binding Two-step reversible inhibition/jump-dilution kinetic experiment; the paper states TO-317 binds HDAC6 CD2. 6 “TO-317 exhibited a Ki of 0.7 nM and a residence time of 142 min in a two-step reversible inhibition model.” auto_metric_priority unique highest-priority metric family: Ki [1] 3 structures\7JOM\7JOM_metadata.json point structures/7JOM/7jom_protein.pdb structures/7JOM/7jom_pocket.pdb structures/7JOM/7jom_ligand.sdf structures/7JOM/7jom_ligand.pdb structures/7JOM/7jom_ligand.cif structures/7JOM/7jom_complex.pdb structures/7JOM/7jom_complex.cif 7JRL classic ZmpB Clostridium perfringens betaD2/INT construct, residues 1226-1687, containing CBM51-2, alphaD3, and INT Na GlcNAc (N-acetylglucosamine) "[""NAG""]" 1 Kd Kd = = 2.6 mM 2600000.0 [] unit_conversion 2.585026652029182 success True direct_binding Isothermal titration calorimetry of isolated recombinant CBM constructs; CBM51-2 bound GlcNAc. 5 Only CBM32-1 and CBM51-2 bound GalNAc and GlcNAc, respectively, with measurable dissociation constants (Kd) of 2.9 mM and 2.6 mM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7JRL\7JRL_metadata.json point structures/7JRL/7jrl_protein.pdb structures/7JRL/7jrl_pocket.pdb structures/7JRL/7jrl_ligand.sdf structures/7JRL/7jrl_ligand.pdb structures/7JRL/7jrl_ligand.cif structures/7JRL/7jrl_complex.pdb structures/7JRL/7jrl_complex.cif 7JRQ classic MPP1 (manganese porphyrin-binding protein 1) Na MPP1 with an N-terminal 6xHis tag and TEV protease cleavage sequence Na MnDPP (Mn-diphenylporphyrin) "[""SMU""]" 1 Kd Kd = = 122 ± 19 nM 122.0 [] unit_conversion 6.913640169325252 success True direct_binding Electronic-absorption titration of apo-MPP1 into Mn(III)DPP; fitted to a single-site protein–ligand binding model. 17 Figure 4B inset visibly prints “Kd = 122 ± 19 nM” for titration of apo-MPP1 into Mn(III)DPP. auto_single_measurement only accepted activity measurement [1] 1 structures\7JRQ\7JRQ_metadata.json point structures/7JRQ/7jrq_protein.pdb structures/7JRQ/7jrq_pocket.pdb structures/7JRQ/7jrq_ligand.sdf structures/7JRQ/7jrq_ligand.pdb structures/7JRQ/7jrq_ligand.cif structures/7JRQ/7jrq_complex.pdb structures/7JRQ/7jrq_complex.cif 7JS8 classic Human HDAC2 Human Na Na Compound 22 "[""VJV""]" 1 IC50 IC50 < < 1.5 nM 1.5 [] unit_conversion 8.823908740944319 success True biochemical_inhibition Human HDAC enzymatic inhibition (Fluor-de-Lys assay); Table 3 reports HDAC2 IC50 values. 4 Table 3, “HDAC and hERG Activities of Compounds 22–30,” reports compound 22 with HDAC2 IC50 <1.5 nM. The paper identifies 7JS8 as the HDAC2 crystal structure with compound 22. auto_single_measurement only accepted activity measurement [1] 1 structures\7JS8\7JS8_metadata.json point structures/7JS8/7js8_protein.pdb structures/7JS8/7js8_pocket.pdb structures/7JS8/7js8_ligand.sdf structures/7JS8/7js8_ligand.pdb structures/7JS8/7js8_ligand.cif structures/7JS8/7js8_complex.pdb structures/7JS8/7js8_complex.cif 7JTW classic RORgt Na Na Na compound 11a; (4R)-6-[(2,5-dichloro-3-{[(2R,4R)-1-(cyclopentanecarbonyl)-2-methylpiperidin-4-yl]oxy}phenyl)amino]-6-oxo-4-phenylhexanoic acid "[""VK4""]" 1 IC50 IC50 = = 54 nM 54.0 [] unit_conversion 7.267606240177031 success True direct_binding Binding assay reported in Table 2 for the 6a derivatives. 3 Table 2 lists compound 11a with Binding IC50 = 54 nM; the table footnote identifies this column as a binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7JTW\7JTW_metadata.json point structures/7JTW/7jtw_protein.pdb structures/7JTW/7jtw_pocket.pdb structures/7JTW/7jtw_ligand.sdf structures/7JTW/7jtw_ligand.pdb structures/7JTW/7jtw_ligand.cif structures/7JTW/7jtw_complex.pdb structures/7JTW/7jtw_complex.cif 7JW5 classic CYP199A4 Rhodopseudomonas palustris strain HaA2 WT WT/wild-type 4-phenylbenzoic acid "[""Z7Z""]" 1 Kd Kd = = 1.7 ± 0.1 μM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding Substrate binding/high-spin-state assay; Table 1 reports Kd for 4-phenylBA. 3 Table 1, “Substrate Binding and In Vitro Turnover Data for CYP199A4,” lists 4-phenylBA with Kd = 1.7 ± 0.1 μM. The text identifies the 4-phenylbenzoic acid-bound structure as PDB 7JW5. auto_single_measurement only accepted activity measurement [1] 1 structures\7JW5\7JW5_metadata.json point structures/7JW5/7jw5_protein.pdb structures/7JW5/7jw5_pocket.pdb structures/7JW5/7jw5_ligand.sdf structures/7JW5/7jw5_ligand.pdb structures/7JW5/7jw5_ligand.cif structures/7JW5/7jw5_complex.pdb structures/7JW5/7jw5_complex.cif 7JX1 classic E. coli thymidylate synthase (TSase) Escherichia coli Na Na (6S)-4A8DZ-Int-B "[""VLD""]" 1 IC50 IC50 = = 4.7 µM 4700.0 [] unit_conversion 5.327902142064282 success True biochemical_inhibition Each diastereomer was separated by C18 HPLC and tested for inhibition of EcTSase. 2 “each was found to inhibit EcTSase with an IC50 of 4.7 and 17.3 µM for (6S)- and (6R)-diastereomers, respectively”; page 4 maps (6S)-4A8DZ-Int-B to PDB 7JX1. auto_single_measurement only accepted activity measurement [1] 1 structures\7JX1\7JX1_metadata.json point structures/7JX1/7jx1_protein.pdb structures/7JX1/7jx1_pocket.pdb structures/7JX1/7jx1_ligand.sdf structures/7JX1/7jx1_ligand.pdb structures/7JX1/7jx1_ligand.cif structures/7JX1/7jx1_complex.pdb structures/7JX1/7jx1_complex.cif 7JXF classic E. coli thymidylate synthase (TSase) Escherichia coli Na Na (6R)-4A8DZ-Int-B "[""VNM""]" 1 IC50 IC50 = = 17.3 µM 17300.0 [] unit_conversion 4.761953896871205 success True biochemical_inhibition Each diastereomer was separated by C18 HPLC and tested for inhibition of EcTSase. 2 “each was found to inhibit EcTSase with an IC50 of 4.7 and 17.3 µM for (6S)- and (6R)-diastereomers, respectively”; page 4 maps (6R)-4A8DZ-Int-B to PDB 7JXF. auto_single_measurement only accepted activity measurement [1] 1 structures\7JXF\7JXF_metadata.json point structures/7JXF/7jxf_protein.pdb structures/7JXF/7jxf_pocket.pdb structures/7JXF/7jxf_ligand.sdf structures/7JXF/7jxf_ligand.pdb structures/7JXF/7jxf_ligand.cif structures/7JXF/7jxf_complex.pdb structures/7JXF/7jxf_complex.cif 7K03 classic TAF1 human TAF1 tandem bromodomain, residues 1373-1635 Na AZD6738 "[""VJM""]" 1 Kd Kd = = 1,670 ± 60 nM 1670.0 [] unit_conversion 5.777283528852417 success True direct_binding ITC; Figure 1E table. 2 The AZD6738 row reports ITC Kd 1,670 ± 60 nM for TAF1-T. auto_single_measurement only accepted activity measurement [1] 1 structures\7K03\7K03_metadata.json point structures/7K03/7k03_protein.pdb structures/7K03/7k03_pocket.pdb structures/7K03/7k03_ligand.sdf structures/7K03/7k03_ligand.pdb structures/7K03/7k03_ligand.cif structures/7K03/7k03_complex.pdb structures/7K03/7k03_complex.cif 7K27 classic TAF1 human TAF1 tandem bromodomain, residues 1373-1635 Na AZ20 "[""VCD""]" 1 Kd Kd > > 25,000 nM 25000.0 [] unit_conversion 4.6020599913279625 success True direct_binding ITC; Figure 1E table. 2 The AZ20 row reports ITC Kd >25,000 nM for TAF1-T. auto_single_measurement only accepted activity measurement [1] 1 structures\7K27\7K27_metadata.json point structures/7K27/7k27_protein.pdb structures/7K27/7k27_pocket.pdb structures/7K27/7k27_ligand.sdf structures/7K27/7k27_ligand.pdb structures/7K27/7k27_ligand.cif structures/7K27/7k27_complex.pdb structures/7K27/7k27_complex.cif 7K28 extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification L76A in the peptide ligand Ac-ADEETGEFL-NH2 "[""CHAIN:P""]" 2 Ki Ki = = 160 ± 30 nM 160.0 [] unit_conversion 6.795880017344075 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K28, L76A 9-mer, Ki 160 ± 30 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K28\7K28_metadata.json point structures/7K28/7k28_protein.pdb structures/7K28/7k28_pocket.pdb structures/7K28/7k28_ligand.pdb structures/7K28/7k28_ligand.cif structures/7K28/7k28_complex.pdb structures/7K28/7k28_complex.cif 7K29 extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification L84A in the peptide ligand Ac-LDEETGEAL-NH2 "[""CHAIN:P""]" 2 Ki Ki = = 110 ± 7 nM 110.0 [] unit_conversion 6.958607314841775 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K29, L84A 9-mer, Ki 110 ± 7 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K29\7K29_metadata.json point structures/7K29/7k29_protein.pdb structures/7K29/7k29_pocket.pdb structures/7K29/7k29_ligand.pdb structures/7K29/7k29_ligand.cif structures/7K29/7k29_complex.pdb structures/7K29/7k29_complex.cif 7K2A extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification F83A in the peptide ligand Ac-LDEETGEFA-NH2 "[""CHAIN:P""]" 2 Ki Ki = = 30 ± 3 nM 30.0 [] unit_conversion 7.522878745280337 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2A, F83A 9-mer, Ki 30 ± 3 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2A\7K2A_metadata.json point structures/7K2A/7k2a_protein.pdb structures/7K2A/7k2a_pocket.pdb structures/7K2A/7k2a_ligand.pdb structures/7K2A/7k2a_ligand.cif structures/7K2A/7k2a_complex.pdb structures/7K2A/7k2a_complex.cif 7K2B extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification L76A/L84A in the peptide ligand Ac-ADEETGEFA-NH2 "[""CHAIN:P""]" 2 Ki Ki = = 320 ± 20 nM 320.0 [] unit_conversion 6.494850021680094 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2B, L76A/L84A 9-mer, Ki 320 ± 20 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2B\7K2B_metadata.json point structures/7K2B/7k2b_protein.pdb structures/7K2B/7k2b_pocket.pdb structures/7K2B/7k2b_ligand.pdb structures/7K2B/7k2b_ligand.cif structures/7K2B/7k2b_complex.pdb structures/7K2B/7k2b_complex.cif 7K2C extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification L76A/F83A/L84A in the peptide ligand Ac-ADEETGEAA-NH2 "[""CHAIN:P""]" 2 Ki Ki = = 330 ± 10 nM 330.0 [] unit_conversion 6.481486060122112 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2C, AAA 9-mer, Ki 330 ± 10 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2C\7K2C_metadata.json point structures/7K2C/7k2c_protein.pdb structures/7K2C/7k2c_pocket.pdb structures/7K2C/7k2c_ligand.pdb structures/7K2C/7k2c_ligand.cif structures/7K2C/7k2c_complex.pdb structures/7K2C/7k2c_complex.cif 7K2D extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification WT peptide Ac-GDEETGE-NH2 "[""CHAIN:P""]" 2 Ki Ki = = (4.3 ± 0.8) x10^3 nM 4300.0 [] unit_conversion 5.366531544420413 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2D, WT 7-mer, Ki (4.3 ± 0.8) x10^3 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2D\7K2D_metadata.json point structures/7K2D/7k2d_protein.pdb structures/7K2D/7k2d_pocket.pdb structures/7K2D/7k2d_ligand.pdb structures/7K2D/7k2d_ligand.cif structures/7K2D/7k2d_complex.pdb structures/7K2D/7k2d_complex.cif 7K2E extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification WT cyclic peptide c[GDEETGE] "[""CHAIN:P""]" 2 Ki Ki = = 470 ± 20 nM 470.0 [] unit_conversion 6.327902142064282 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2E, WT cyclic, Ki 470 ± 20 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2E\7K2E_metadata.json point structures/7K2E/7k2e_protein.pdb structures/7K2E/7k2e_pocket.pdb structures/7K2E/7k2e_ligand.pdb structures/7K2E/7k2e_ligand.cif structures/7K2E/7k2e_complex.pdb structures/7K2E/7k2e_complex.cif 7K2F extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification D77A in the peptide ligand c[GAEETGE] "[""CHAIN:C""]" 2 Ki Ki = = (100 ± 20) x10^3 nM 100000.0 [] unit_conversion 4.0 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2F, D77A, Ki (100 ± 20) x10^3 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2F\7K2F_metadata.json point structures/7K2F/7k2f_protein.pdb structures/7K2F/7k2f_pocket.pdb structures/7K2F/7k2f_ligand.pdb structures/7K2F/7k2f_ligand.cif structures/7K2F/7k2f_complex.pdb structures/7K2F/7k2f_complex.cif 7K2G extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification T80A in the peptide ligand c[GDEEAGE] "[""CHAIN:P""]" 2 Ki Ki = = (280 ± 60) x10^3 nM 280000.0 [] unit_conversion 3.5528419686577806 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2G, T80A, Ki (280 ± 60) x10^3 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2G\7K2G_metadata.json point structures/7K2G/7k2g_protein.pdb structures/7K2G/7k2g_pocket.pdb structures/7K2G/7k2g_ligand.pdb structures/7K2G/7k2g_ligand.cif structures/7K2G/7k2g_complex.pdb structures/7K2G/7k2g_complex.cif 7K2H extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification E78P in the peptide ligand c[GDPETGE] "[""CHAIN:P""]" 2 Ki Ki = = 140 ± 30 nM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2H, E78P, Ki 140 ± 30 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2H\7K2H_metadata.json point structures/7K2H/7k2h_protein.pdb structures/7K2H/7k2h_pocket.pdb structures/7K2H/7k2h_ligand.pdb structures/7K2H/7k2h_ligand.cif structures/7K2H/7k2h_complex.pdb structures/7K2H/7k2h_complex.cif 7K2I extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification D77A/E78P in the peptide ligand c[GAPETGE] "[""CHAIN:P""]" 2 Ki Ki = = (13 ± 0.7) x10^3 nM 13000.0 [] unit_conversion 4.886056647693163 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2I, D77A/E78P, Ki (13 ± 0.7) x10^3 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2I\7K2I_metadata.json point structures/7K2I/7k2i_protein.pdb structures/7K2I/7k2i_pocket.pdb structures/7K2I/7k2i_ligand.pdb structures/7K2I/7k2i_ligand.cif structures/7K2I/7k2i_complex.pdb structures/7K2I/7k2i_complex.cif 7K2J extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification T80A/E78P in the peptide ligand c[GDPEAGE] "[""CHAIN:P""]" 2 Ki Ki = = (30 ± 0.6) x10^3 nM 30000.0 [] unit_conversion 4.522878745280337 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2J, T80A/E78P, Ki (30 ± 0.6) x10^3 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2J\7K2J_metadata.json point structures/7K2J/7k2j_protein.pdb structures/7K2J/7k2j_pocket.pdb structures/7K2J/7k2j_ligand.pdb structures/7K2J/7k2j_ligand.cif structures/7K2J/7k2j_complex.pdb structures/7K2J/7k2j_complex.cif 7K2K extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification betaAla linker replacing the glycine linker in the peptide ligand c[BAL-DEETGE] "[""CHAIN:P""]" 2 Ki Ki = = 420 ± 30 nM 420.0 [] unit_conversion 6.376750709602099 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2K, βAla cyclic peptide, Ki 420 ± 30 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2K\7K2K_metadata.json point structures/7K2K/7k2k_protein.pdb structures/7K2K/7k2k_pocket.pdb structures/7K2K/7k2k_ligand.pdb structures/7K2K/7k2k_ligand.cif structures/7K2K/7k2k_complex.pdb structures/7K2K/7k2k_complex.cif 7K2L extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification betaAla linker/D77N/E78P in the peptide ligand c[BAL-NPETGE] "[""CHAIN:P""]" 2 Ki Ki = = 250 ± 5 nM 250.0 [] unit_conversion 6.6020599913279625 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2L, βAla/D77N/E78P, Ki 250 ± 5 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2L\7K2L_metadata.json point structures/7K2L/7k2l_protein.pdb structures/7K2L/7k2l_pocket.pdb structures/7K2L/7k2l_ligand.pdb structures/7K2L/7k2l_ligand.cif structures/7K2L/7k2l_complex.pdb structures/7K2L/7k2l_complex.cif 7K2M extended human KEAP1 (Kelch-like ECH-associated protein 1) human (Homo sapiens) KEAP1 Kelch domain residues 312-624; N-terminal His6-TEV construct, with tag cleaved before purification D77E/E78P in the peptide ligand c[GEPETGE] "[""CHAIN:P""]" 2 Ki Ki = = 150 ± 8 nM 150.0 [] unit_conversion 6.823908740944319 success True biochemical_inhibition Competitive fluorescence-anisotropy binding assay; DYNAFIT fit 5 Table 1: 7K2M, D77E/E78P, Ki 150 ± 8 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2M\7K2M_metadata.json point structures/7K2M/7k2m_protein.pdb structures/7K2M/7k2m_pocket.pdb structures/7K2M/7k2m_ligand.pdb structures/7K2M/7k2m_ligand.cif structures/7K2M/7k2m_complex.pdb structures/7K2M/7k2m_complex.cif 7K2O extended human KEAP1 human Kelch domain residues 312-624; N-terminal His6-TEV tag construct E78P in the Nrf2-derived cyclic peptide c[GABA-DPETGE]; compound 17 (gammaBut/E78P) "[""CHAIN:P""]" 2 Ki Ki = = 230 ± 10 nM 230.0 [] unit_conversion 6.638272163982407 success True direct_binding Competitive fluorescence anisotropy binding assay with purified recombinant human KEAP1 Kelch domain. 5 Table 1 maps 7K2O to compound 17, γBut/E78P, c[γDPETGE], with Ki 230 ± 10 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2O\7K2O_metadata.json point structures/7K2O/7k2o_protein.pdb structures/7K2O/7k2o_pocket.pdb structures/7K2O/7k2o_ligand.pdb structures/7K2O/7k2o_ligand.cif structures/7K2O/7k2o_complex.pdb structures/7K2O/7k2o_complex.cif 7K2P extended human KEAP1 human Kelch domain residues 312-624; N-terminal His6-TEV tag construct E78P in the Nrf2-derived cyclic peptide c[AVA-DPETGE]; compound 18 (Ava/E78P) "[""CHAIN:P""]" 2 Ki Ki = = 120 ± 20 nM 120.0 [] unit_conversion 6.920818753952375 success True direct_binding Competitive fluorescence anisotropy binding assay with purified recombinant human KEAP1 Kelch domain. 5 Table 1 maps 7K2P to compound 18, Ava/E78P, c[Ava-DPETGE], with Ki 120 ± 20 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2P\7K2P_metadata.json point structures/7K2P/7k2p_protein.pdb structures/7K2P/7k2p_pocket.pdb structures/7K2P/7k2p_ligand.pdb structures/7K2P/7k2p_ligand.cif structures/7K2P/7k2p_complex.pdb structures/7K2P/7k2p_complex.cif 7K2Q extended human KEAP1 human Kelch domain residues 312-624; N-terminal His6-TEV tag construct E78P in the Nrf2-derived cyclic peptide c[Ahx-DPETGE]; compound 19 (Ahx/E78P) "[""CHAIN:P""]" 2 Ki Ki = = 330 ± 20 nM 330.0 [] unit_conversion 6.481486060122112 success True direct_binding Competitive fluorescence anisotropy binding assay with purified recombinant human KEAP1 Kelch domain. 5 Table 1 maps 7K2Q to compound 19, Ahx/E78P, c[Ahx-DPETGE], with Ki 330 ± 20 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7K2Q\7K2Q_metadata.json point structures/7K2Q/7k2q_protein.pdb structures/7K2Q/7k2q_pocket.pdb structures/7K2Q/7k2q_ligand.pdb structures/7K2Q/7k2q_ligand.cif structures/7K2Q/7k2q_complex.pdb structures/7K2Q/7k2q_complex.cif 7K3D classic NTMT1 human Na Na DC1-13 (DC113) "[""VWP""]" 1 IC50 IC50 = = 0.10 ± 0.01 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition SAHH-coupled fluorescence inhibition assay; saturated SAM (100 µM) and peptide substrate GPKRIA at its Km. 3 Table 1 lists compound 1 (DC113) with IC50 = 0.10 ± 0.01 µM; the paper states that synthesized peptidomimetics were evaluated using the SAHH-coupled fluorescence assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7K3D\7K3D_metadata.json point structures/7K3D/7k3d_protein.pdb structures/7K3D/7k3d_pocket.pdb structures/7K3D/7k3d_ligand.sdf structures/7K3D/7k3d_ligand.pdb structures/7K3D/7k3d_ligand.cif structures/7K3D/7k3d_complex.pdb structures/7K3D/7k3d_complex.cif 7K3K extended dLC8/Ctp Drosophila melanogaster Ctp residues 1-89 in complex with Panx residues 455-466 (Panx1) Na Panoramix TQT peptide "[""CHAIN:B""]" 1 Kd Kd ~ ~ 75 nM 75.0 [] unit_conversion 7.1249387366083 success True direct_binding Isothermal titration calorimetry of purified Ctp and individual Panx TQT/V-site peptides. 6 “ITC measurements revealed comparable affinities for the two individual TQT/V sites in Panx (TQT peptide: Kd ~75 nM; TQV peptide: Kd ~40 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7K3K\7K3K_metadata.json point structures/7K3K/7k3k_protein.pdb structures/7K3K/7k3k_pocket.pdb structures/7K3K/7k3k_ligand.pdb structures/7K3K/7k3k_ligand.cif structures/7K3K/7k3k_complex.pdb structures/7K3K/7k3k_complex.cif 7K3L extended dLC8/Ctp Drosophila melanogaster Ctp residues 1-89 in complex with Panx residues 467-480 (Panx2) Na Panoramix TQ peptide "[""CHAIN:B""]" 1 Kd Kd ~ ~ 40 nM 40.0 [] unit_conversion 7.3979400086720375 success True direct_binding Isothermal titration calorimetry of purified Ctp and individual Panx TQT/V-site peptides. 6 “ITC measurements revealed comparable affinities for the two individual TQT/V sites in Panx (TQT peptide: Kd ~75 nM; TQV peptide: Kd ~40 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7K3L\7K3L_metadata.json point structures/7K3L/7k3l_protein.pdb structures/7K3L/7k3l_pocket.pdb structures/7K3L/7k3l_ligand.pdb structures/7K3L/7k3l_ligand.cif structures/7K3L/7k3l_complex.pdb structures/7K3L/7k3l_complex.cif 7K4G classic Human Arginase 1 human Na Na compound 01 (compound 1) "[""VUV""]" 1 IC50 IC50 = = 16 nM 16.0 [] unit_conversion 7.795880017344075 success True biochemical_inhibition In vitro fluorimetric assay measuring thioornithine production; Arg1 potency. 7 Figure 11 reports compound 1 Arg1 IC50 = 16 nM; the text states Arg1 potency was assessed using an in vitro fluorimetric assay measuring thioornithine production. Figure 2 maps compound 1 bound to hArg1 to PDB 7K4G. auto_single_measurement only accepted activity measurement [1] 1 structures\7K4G\7K4G_metadata.json point structures/7K4G/7k4g_protein.pdb structures/7K4G/7k4g_pocket.pdb structures/7K4G/7k4g_ligand.sdf structures/7K4G/7k4g_ligand.pdb structures/7K4G/7k4g_ligand.cif structures/7K4G/7k4g_complex.pdb structures/7K4G/7k4g_complex.cif 7K4H classic Human Arginase 1 human Na Na compound 04 (compound 4) "[""VV4""]" 1 IC50 IC50 = = 2.2 nM 2.2 [] unit_conversion 8.657577319177793 success True biochemical_inhibition In vitro fluorimetric assay measuring thioornithine production; Arg1 potency. 7 Figure 11 reports compound 4 Arg1 IC50 = 2.2 nM; the text states Arg1 potency was assessed using an in vitro fluorimetric assay measuring thioornithine production. Figure 12 maps compound 4 bound to hArg1 to PDB 7K4H. auto_single_measurement only accepted activity measurement [1] 1 structures\7K4H\7K4H_metadata.json point structures/7K4H/7k4h_protein.pdb structures/7K4H/7k4h_pocket.pdb structures/7K4H/7k4h_ligand.sdf structures/7K4H/7k4h_ligand.pdb structures/7K4H/7k4h_ligand.cif structures/7K4H/7k4h_complex.pdb structures/7K4H/7k4h_complex.cif 7K4I classic Human Arginase 1 human Na Na compound 06 (compound 6) "[""VUY""]" 1 IC50 IC50 = = 25 nM 25.0 [] unit_conversion 7.6020599913279625 success True biochemical_inhibition In vitro fluorimetric assay measuring thioornithine production; Arg1 potency. 7 Figure 11 reports compound 6 Arg1 IC50 = 25 nM; the text states Arg1 potency was assessed using an in vitro fluorimetric assay measuring thioornithine production. Figure 14 maps compound 6 bound to hArg1 to PDB 7K4I. auto_single_measurement only accepted activity measurement [1] 1 structures\7K4I\7K4I_metadata.json point structures/7K4I/7k4i_protein.pdb structures/7K4I/7k4i_pocket.pdb structures/7K4I/7k4i_ligand.sdf structures/7K4I/7k4i_ligand.pdb structures/7K4I/7k4i_ligand.cif structures/7K4I/7k4i_complex.pdb structures/7K4I/7k4i_complex.cif 7K4J classic Human Arginase 1 human Na Na compound 51 "[""VV1""]" 1 IC50 IC50 = = 104 nM 104.0 [] unit_conversion 6.982966660701219 success True biochemical_inhibition In vitro fluorimetric assay measuring thioornithine production; Arg1 potency. 7 Figure 11 reports compound 51 Arg1 IC50 = 104 nM; the text states Arg1 potency was assessed using an in vitro fluorimetric assay measuring thioornithine production. Figure 13 maps compound 51 bound to hArg1 to PDB 7K4J. auto_single_measurement only accepted activity measurement [1] 1 structures\7K4J\7K4J_metadata.json point structures/7K4J/7k4j_protein.pdb structures/7K4J/7k4j_pocket.pdb structures/7K4J/7k4j_ligand.sdf structures/7K4J/7k4j_ligand.pdb structures/7K4J/7k4j_ligand.cif structures/7K4J/7k4j_complex.pdb structures/7K4J/7k4j_complex.cif 7K4K classic Human Arginase 1 human Na Na compound 52 "[""VUS""]" 1 IC50 IC50 = = 1.6 nM 1.6 [] unit_conversion 8.795880017344075 success True biochemical_inhibition In vitro fluorimetric assay measuring thioornithine production; Arg1 potency. 7 Figure 11 reports compound 52 Arg1 IC50 = 1.6 nM; the text states Arg1 potency was assessed using an in vitro fluorimetric assay measuring thioornithine production. Figure 15 maps compound 52 bound to hArg1 to PDB 7K4K. auto_single_measurement only accepted activity measurement [1] 1 structures\7K4K\7K4K_metadata.json point structures/7K4K/7k4k_protein.pdb structures/7K4K/7k4k_pocket.pdb structures/7K4K/7k4k_ligand.sdf structures/7K4K/7k4k_ligand.pdb structures/7K4K/7k4k_ligand.cif structures/7K4K/7k4k_complex.pdb structures/7K4K/7k4k_complex.cif 7K6C classic dihydrofolate reductase (MabDHFR) Mycobacterium abscessus ATCC 19977 / DSM 44196 Na Na P218 "[""MMV""]" 1 IC50 IC50 = = 8.4 nM 8.4 [] unit_conversion 8.075720713938118 success True biochemical_inhibition Purified recombinant DHFR enzymatic NADPH-fluorescence inhibition assay. 48 Table 1 reports P218 IC50 8.4 nM for MabDHFR. auto_single_measurement only accepted activity measurement [1] 1 structures\7K6C\7K6C_metadata.json point structures/7K6C/7k6c_protein.pdb structures/7K6C/7k6c_pocket.pdb structures/7K6C/7k6c_ligand.sdf structures/7K6C/7k6c_ligand.pdb structures/7K6C/7k6c_ligand.cif structures/7K6C/7k6c_complex.pdb structures/7K6C/7k6c_complex.cif 7K6M classic PI3Kalpha Na Na Na compound 1 (PF-06843195) "[""VXY""]" 1 Ki Ki < < 0.018 nM 0.018 [] unit_conversion 10.744727494896694 success True biochemical_inhibition Biochemical PI3Kα kinase assay; Table 5 reports PI3Kα Ki for compound 1. 8 Table 5 lists compound 1 with PI3Kα Ki <0.018 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7K6M\7K6M_metadata.json point structures/7K6M/7k6m_protein.pdb structures/7K6M/7k6m_pocket.pdb structures/7K6M/7k6m_ligand.sdf structures/7K6M/7k6m_ligand.pdb structures/7K6M/7k6m_ligand.cif structures/7K6M/7k6m_complex.pdb structures/7K6M/7k6m_complex.cif 7K6N classic PI3Kalpha Na Na Na compound 11 (11-1575) "[""VY4""]" 1 Ki Ki < < 0.018 nM 0.018 [] unit_conversion 10.744727494896694 success True biochemical_inhibition Biochemical PI3Kα kinase assay; Table 3 reports PI3Kα Ki for compound 11. 5 Table 3 lists compound 11 with PI3Kα Ki <0.018 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7K6N\7K6N_metadata.json point structures/7K6N/7k6n_protein.pdb structures/7K6N/7k6n_pocket.pdb structures/7K6N/7k6n_ligand.sdf structures/7K6N/7k6n_ligand.pdb structures/7K6N/7k6n_ligand.cif structures/7K6N/7k6n_complex.pdb structures/7K6N/7k6n_complex.cif 7K6O classic PI3Kalpha Na Na Na compound 10 (10-5429) "[""VY1""]" 1 Ki Ki = = 0.12 nM 0.12 [] unit_conversion 9.920818753952375 success True biochemical_inhibition Biochemical PI3Kα kinase assay; Table 1 reports PI3Kα Ki for compound 10. 2 Table 1 lists compound 10 with PI3Kα Ki 0.12 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7K6O\7K6O_metadata.json point structures/7K6O/7k6o_protein.pdb structures/7K6O/7k6o_pocket.pdb structures/7K6O/7k6o_ligand.sdf structures/7K6O/7k6o_ligand.pdb structures/7K6O/7k6o_ligand.cif structures/7K6O/7k6o_complex.pdb structures/7K6O/7k6o_complex.cif 7K71 classic PI3Kalpha Na Na Na compound 4 (4-0686) "[""VYP""]" 1 Ki Ki = = 0.64 nM 0.64 [] unit_conversion 9.193820026016112 success True biochemical_inhibition Biochemical PI3Kα kinase assay; Table 1 reports PI3Kα Ki for compound 4. 2 Table 1 lists compound 4 with PI3Kα Ki 0.64 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7K71\7K71_metadata.json point structures/7K71/7k71_protein.pdb structures/7K71/7k71_pocket.pdb structures/7K71/7k71_ligand.sdf structures/7K71/7k71_ligand.pdb structures/7K71/7k71_ligand.cif structures/7K71/7k71_complex.pdb structures/7K71/7k71_complex.cif 7K7O classic Tyrosine kinase 2 (TYK2) Na TYK2 JH2 domain, residues 575-869 Na compound 12 (6-[(cyclopropanecarbonyl)amino]-4-{[2-methoxy-3-(pyrimidin-2-yl)phenyl]amino}-N-methylpyridazine-3-carboxamide) "[""VZJ""]" 1 IC50 IC50 = = 0.48 nM 0.48 [] unit_conversion 9.318758762624412 success True biochemical_inhibition TYK2 JH2 enzymatic assay; Table 1. 3 Table 1 reports compound 12 TYK2 JH2 IC50 = 0.48 nM. Figure 3 identifies compound 12 bound to TYK2 JH2 as PDB 7K7O. auto_single_measurement only accepted activity measurement [1] 1 structures\7K7O\7K7O_metadata.json point structures/7K7O/7k7o_protein.pdb structures/7K7O/7k7o_pocket.pdb structures/7K7O/7k7o_ligand.sdf structures/7K7O/7k7o_ligand.pdb structures/7K7O/7k7o_ligand.cif structures/7K7O/7k7o_complex.pdb structures/7K7O/7k7o_complex.cif 7K7Q classic Tyrosine kinase 2 (TYK2) Na TYK2 JH2 domain, residues 575-869 Na Na "[""VZG""]" 1 IC50 IC50 < < 0.25 nM 0.25 [] unit_conversion 9.602059991327963 success True biochemical_inhibition TYK2 JH2 enzymatic assay; Table 3. 4 Table 3 reports compound 29 TYK2 JH2 IC50 < 0.25 nM. Figure 4 identifies compound 29 bound to TYK2 JH2 as PDB 7K7Q. auto_single_measurement only accepted activity measurement [1] 1 structures\7K7Q\7K7Q_metadata.json point structures/7K7Q/7k7q_protein.pdb structures/7K7Q/7k7q_pocket.pdb structures/7K7Q/7k7q_ligand.sdf structures/7K7Q/7k7q_ligand.pdb structures/7K7Q/7k7q_ligand.cif structures/7K7Q/7k7q_complex.pdb structures/7K7Q/7k7q_complex.cif 7K7R extended MS39p2w174 Fab Na Fab MS39p2w174 in complex with EBNA1 peptide AA386-405 Na EBNA1 peptide AA386-405 "[""CHAIN:C"", ""CHAIN:F""]" 1 Kd Kd = = 2.67E-09 M 2.67 [] unit_conversion 8.573488738635424 success True direct_binding Supplementary Table 6; antibody–peptide binding measurement, n=4 serial-dilution replicates. 11 Table 6 reports MS39p2w174 with “EBNA1 AA386-405”: KD (M) = 2.67E-09. auto_single_measurement only accepted activity measurement [1] 1 structures\7K7R\7K7R_metadata.json point structures/7K7R/7k7r_protein.pdb structures/7K7R/7k7r_pocket.pdb structures/7K7R/7k7r_ligand.pdb structures/7K7R/7k7r_ligand.cif structures/7K7R/7k7r_complex.pdb structures/7K7R/7k7r_complex.cif 7K89 classic RPE65 bovine Na Na 4-fluoro-emixustat (compound 49) "[""W4J""]" 1 IC50 IC50 = = 95 ± 5 nM 95.0 [] unit_conversion 7.022276394711152 success True biochemical_inhibition In vitro inhibition of 11-cis-retinol production by bovine RPE microsomes (RPE65 retinoid-isomerase activity assay). 34 Table 2 lists compound 49 with IC50 95 ± 5 nM; the table reports RPE65 inhibitor activities. The assay is described as bovine RPE microsomal 11-cis-retinol-production inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7K89\7K89_metadata.json point structures/7K89/7k89_protein.pdb structures/7K89/7k89_pocket.pdb structures/7K89/7k89_ligand.sdf structures/7K89/7k89_ligand.pdb structures/7K89/7k89_ligand.cif structures/7K89/7k89_complex.pdb structures/7K89/7k89_complex.cif 7KAA classic Fast skeletal troponin C-troponin I chimera (sChimera) rabbit sNTnC(1-88)-sTnI(99-148) chimera with a GGAGG linker and C-terminal His6 tag Na tirasemtiv "[""W97""]" 1 Kd Kd <= <= 1 µM 1000.0 [] unit_conversion 6.0 success True direct_binding NMR titration of tirasemtiv to 15N-labeled sChimera; slow-exchange binding fitted to a one-to-one equilibrium. 4 The NMR titration of tirasemtiv to sChimera “yielded a dissociation constant (KD) of ≤1 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7KAA\7KAA_metadata.json point structures/7KAA/7kaa_protein.pdb structures/7KAA/7kaa_pocket.pdb structures/7KAA/7kaa_ligand.sdf structures/7KAA/7kaa_ligand.pdb structures/7KAA/7kaa_ligand.cif structures/7KAA/7kaa_complex.pdb structures/7KAA/7kaa_complex.cif 7KC2 classic Yeast alcohol dehydrogenase 1 (ScbADH) Saccharomyces carlsbergensis Na V58T; Q127E; Q147E; I151V NADH "[""NAD""]" 1 Ki Ki = = 0.05 mM 50000.0 [] unit_conversion 4.301029995663981 success True biochemical_inhibition Enzyme-kinetics determination of ligand dissociation constants for commercial ScbADH; NADH Ki reported as 0.05 mM. 2 “dissociation constants (Ki values) determined by enzyme kinetics (NAD+, 1.3 mM; NADH, 0.05 mM)” auto_single_measurement only accepted activity measurement [1] 1 structures\7KC2\7KC2_metadata.json point structures/7KC2/7kc2_protein.pdb structures/7KC2/7kc2_pocket.pdb structures/7KC2/7kc2_ligand.sdf structures/7KC2/7kc2_ligand.pdb structures/7KC2/7kc2_ligand.cif structures/7KC2/7kc2_complex.pdb structures/7KC2/7kc2_complex.cif 7KCB classic Yeast alcohol dehydrogenase 1 (ScbADH) Saccharomyces carlsbergensis Na V58T; Q127E; Q147E; I151V NAD+; 2,2,2-trifluoroethanol "[""ETF""]" 1 Ki Ki = = 2.8 mM 2800000.0 [] unit_conversion 2.5528419686577806 success True biochemical_inhibition Enzyme-kinetics determination of ligand binding to the enzyme–NAD+ complex. 2 “for binding to the enzyme–NAD+ complex, (2,2,2-trifluoroethanol, 2.8 mM; pyrazole, 0.011 mM)” auto_single_measurement only accepted activity measurement [1] 1 structures\7KCB\7KCB_metadata.json point structures/7KCB/7kcb_protein.pdb structures/7KCB/7kcb_pocket.pdb structures/7KCB/7kcb_ligand.sdf structures/7KCB/7kcb_ligand.pdb structures/7KCB/7kcb_ligand.cif structures/7KCB/7kcb_complex.pdb structures/7KCB/7kcb_complex.cif 7KCC classic human methionine adenosyltransferase 2A (MAT2A) human full-length MAT2A expressed from a pET21a-based vector with an N-terminal His6 tag and TEV protease cleavage site Na AG-270 "[""WBG""]" 1 IC50 IC50 = = 0.014 μM 14.0 [] unit_conversion 7.853871964321762 success True biochemical_inhibition Enzymatic MAT2A inhibition assay; Table 8. 14 Table 8 reports AG-270 enzymatic MAT2A IC50 = 0.014 μM; Figure 7 on page 15 maps AG-270 to PDB 7KCC. auto_single_measurement only accepted activity measurement [1] 1 structures\7KCC\7KCC_metadata.json point structures/7KCC/7kcc_protein.pdb structures/7KCC/7kcc_pocket.pdb structures/7KCC/7kcc_ligand.sdf structures/7KCC/7kcc_ligand.pdb structures/7KCC/7kcc_ligand.cif structures/7KCC/7kcc_complex.pdb structures/7KCC/7kcc_complex.cif 7KCE classic human methionine adenosyltransferase 2A (MAT2A) human full-length MAT2A expressed from a pET21a-based vector with an N-terminal His6 tag and TEV protease cleavage site Na compound 2 "[""J41""]" 2 Kd Kd = = 70 μM 70000.0 [] unit_conversion 4.154901959985743 success True direct_binding Surface plasmon resonance binding assay. 2 The text reports that compound 2 showed SPR binding with a dissociation constant (Kd) of 70 μM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7KCE\7KCE_metadata.json point structures/7KCE/7kce_protein.pdb structures/7KCE/7kce_pocket.pdb structures/7KCE/7kce_ligand.sdf structures/7KCE/7kce_ligand.pdb structures/7KCE/7kce_ligand.cif structures/7KCE/7kce_complex.pdb structures/7KCE/7kce_complex.cif 7KCF classic human methionine adenosyltransferase 2A (MAT2A) human full-length MAT2A expressed from a pET21a-based vector with an N-terminal His6 tag and TEV protease cleavage site Na AGI-24512 "[""J4A""]" 1 IC50 IC50 = = 0.008 μM 8.0 [] unit_conversion 8.096910013008056 success True biochemical_inhibition Enzymatic MAT2A inhibition assay; Table 3. 7 Table 3 reports AGI-24512 enzymatic MAT2A IC50 = 0.008 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KCF\7KCF_metadata.json point structures/7KCF/7kcf_protein.pdb structures/7KCF/7kcf_pocket.pdb structures/7KCF/7kcf_ligand.sdf structures/7KCF/7kcf_ligand.pdb structures/7KCF/7kcf_ligand.cif structures/7KCF/7kcf_complex.pdb structures/7KCF/7kcf_complex.cif 7KDA classic human methionine adenosyltransferase 2A (MAT2A) human full-length MAT2A expressed from a pET21a-based vector with an N-terminal His6 tag and TEV protease cleavage site Na compound 34 "[""WBM""]" 1 IC50 IC50 = = 0.27 μM 270.0 [] unit_conversion 6.568636235841012 success True biochemical_inhibition Enzymatic MAT2A inhibition assay; Table 6. 11 Table 6 reports compound 34 enzymatic MAT2A IC50 = 0.27 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KDA\7KDA_metadata.json point structures/7KDA/7kda_protein.pdb structures/7KDA/7kda_pocket.pdb structures/7KDA/7kda_ligand.sdf structures/7KDA/7kda_ligand.pdb structures/7KDA/7kda_ligand.cif structures/7KDA/7kda_complex.pdb structures/7KDA/7kda_complex.cif 7KDB classic human methionine adenosyltransferase 2A (MAT2A) human full-length MAT2A expressed from a pET21a-based vector with an N-terminal His6 tag and TEV protease cleavage site Na compound 35 "[""WBS""]" 1 IC50 IC50 = = 0.007 μM 7.0 [] unit_conversion 8.154901959985743 success True biochemical_inhibition Enzymatic MAT2A inhibition assay; Figure 6 and Table 7. 12 Figure 6 reports compound 35 enzyme IC50 = 0.007 μM; the caption maps the MAT2A:SAM:35 structure to PDB 7KDB. auto_single_measurement only accepted activity measurement [1] 1 structures\7KDB\7KDB_metadata.json point structures/7KDB/7kdb_protein.pdb structures/7KDB/7kdb_pocket.pdb structures/7KDB/7kdb_ligand.sdf structures/7KDB/7kdb_ligand.pdb structures/7KDB/7kdb_ligand.cif structures/7KDB/7kdb_complex.pdb structures/7KDB/7kdb_complex.cif 7KEV extended PCSK9 human Full-length PCSK9 expressed from a pRS5A mammalian expression vector Na peptide 1 "[""CHAIN:C""]" 1 Kd Kd = = 0.3 nM 0.3 [] unit_conversion 9.522878745280337 success True direct_binding Surface plasmon resonance (SPR) binding of peptide 1 to human PCSK9. 4 “Peptide 1 showed high affinity for human (KD = 0.3 nM) ... PCSK9 by surface plasmon resonance (SPR).” auto_single_measurement only accepted activity measurement [1] 1 structures\7KEV\7KEV_metadata.json point structures/7KEV/7kev_protein.pdb structures/7KEV/7kev_pocket.pdb structures/7KEV/7kev_ligand.pdb structures/7KEV/7kev_ligand.cif structures/7KEV/7kev_complex.pdb structures/7KEV/7kev_complex.cif 7KFA extended PCSK9 human Full-length PCSK9 expressed from a pRS5A mammalian expression vector Na 13PCSK9i "[""CHAIN:D""]" 1 Kd Kd = = 6.1 nM 6.1 [] unit_conversion 8.214670164989233 success True direct_binding Surface plasmon resonance (SPR) binding of 13PCSK9i to human PCSK9. 7 Figure 3B reports SPR binding of 13PCSK9i to human PCSK9 with KD [nM] = 6.1. auto_single_measurement only accepted activity measurement [1] 1 structures\7KFA\7KFA_metadata.json point structures/7KFA/7kfa_protein.pdb structures/7KFA/7kfa_pocket.pdb structures/7KFA/7kfa_ligand.pdb structures/7KFA/7kfa_ligand.cif structures/7KFA/7kfa_complex.pdb structures/7KFA/7kfa_complex.cif 7KGB classic Mycobacterium tuberculosis 70S ribosome Mycobacterium tuberculosis 70S ribosome Na SEQ-9 "[""WDP""]" 1 IC50 IC50 = = 0.064 µM 64.0 [] unit_conversion 7.1938200260161125 success True biochemical_inhibition Cell-free translation inhibition of the Mtb methylated ribosome. 5 Table 1 reports “Translation inhibition of Mtb methylated ribosome (IC50 µM)” for SEQ-9 as 0.064. auto_single_measurement only accepted activity measurement [1] 1 structures\7KGB\7KGB_metadata.json point structures/7KGB/7kgb_protein.pdb structures/7KGB/7kgb_pocket.pdb structures/7KGB/7kgb_ligand.sdf structures/7KGB/7kgb_ligand.pdb structures/7KGB/7kgb_ligand.cif structures/7KGB/7kgb_complex.pdb structures/7KGB/7kgb_complex.cif 7KGG classic AdeB multidrug efflux pump Acinetobacter baumannii full-length AdeB multidrug efflux pump Na ethidium bromide (Et) "[""ET""]" 1 Kd Kd = = 2.5 ± 0.1 µM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding Fluorescence-polarization titration of purified full-length AdeB with ethidium bromide. 3 “The measured dissociation constant (K_D) values for Et and R6G are 2.5 ± 0.1 µM and 3.1 ± 0.1 µM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7KGG\7KGG_metadata.json point structures/7KGG/7kgg_protein.pdb structures/7KGG/7kgg_pocket.pdb structures/7KGG/7kgg_ligand.sdf structures/7KGG/7kgg_ligand.pdb structures/7KGG/7kgg_ligand.cif structures/7KGG/7kgg_complex.pdb structures/7KGG/7kgg_complex.cif 7KGH classic AdeB multidrug efflux pump Acinetobacter baumannii full-length AdeB multidrug efflux pump Na ethidium bromide (Et) "[""ET""]" 1 Kd Kd = = 2.5 ± 0.1 µM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding Fluorescence-polarization titration of purified full-length AdeB with ethidium bromide. 3 “The measured dissociation constant (K_D) values for Et and R6G are 2.5 ± 0.1 µM and 3.1 ± 0.1 µM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7KGH\7KGH_metadata.json point structures/7KGH/7kgh_protein.pdb structures/7KGH/7kgh_pocket.pdb structures/7KGH/7kgh_ligand.sdf structures/7KGH/7kgh_ligand.pdb structures/7KGH/7kgh_ligand.cif structures/7KGH/7kgh_complex.pdb structures/7KGH/7kgh_complex.cif 7KGI classic AdeB multidrug efflux pump Acinetobacter baumannii full-length AdeB multidrug efflux pump Na ethidium bromide (Et) "[""ET""]" 1 Kd Kd = = 2.5 ± 0.1 µM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding Fluorescence-polarization titration of purified full-length AdeB with ethidium bromide. 3 “The measured dissociation constant (K_D) values for Et and R6G are 2.5 ± 0.1 µM and 3.1 ± 0.1 µM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7KGI\7KGI_metadata.json point structures/7KGI/7kgi_protein.pdb structures/7KGI/7kgi_pocket.pdb structures/7KGI/7kgi_ligand.sdf structures/7KGI/7kgi_ligand.pdb structures/7KGI/7kgi_ligand.cif structures/7KGI/7kgi_complex.pdb structures/7KGI/7kgi_complex.cif 7KGY classic Faecalibacterium prausnitzii 2-L1 beta-glucuronidase (Fp2-L1 GUS) Faecalibacterium prausnitzii Fp2-L1 GUS Na UNC10201652-glucuronide (GUSi) "[""I9G""]" 1 IC50 IC50 = = 2.8 ± 0.1 μM 2800.0 [] unit_conversion 5.552841968657781 success True biochemical_inhibition Purified Fp2-L1 GUS conversion of TCS-G to TCS in vitro; GUSi inhibition curve. 7 Fig. 4b explicitly labels “F. prausnitzii 2-L1 (Fp2-L1) GUS, IC50 = 2.8 ± 0.1 μM” for GUSi inhibition of TCS-G-to-TCS conversion. auto_single_measurement only accepted activity measurement [1] 1 structures\7KGY\7KGY_metadata.json point structures/7KGY/7kgy_protein.pdb structures/7KGY/7kgy_pocket.pdb structures/7KGY/7kgy_ligand.sdf structures/7KGY/7kgy_ligand.pdb structures/7KGY/7kgy_ligand.cif structures/7KGY/7kgy_complex.pdb structures/7KGY/7kgy_complex.cif 7KH8 classic human LMPTP human residues 4-157 Na 5d "[""WE7""]" 2 Ki Ki = = 26.15 ± 1.21 nM 26.15 [] unit_conversion 7.582528306796707 success True biochemical_inhibition Kinetic inhibition experiment using 20 nM human LMPTP-A and increasing OMFP substrate concentrations in the presence of 5d; the figure labels the fitted apparent Ki as K′i. 4 Figure 3a visibly prints “K′i = 26.15 ± 1.21 nM” for LMPTP and 5d; its caption identifies the enzyme as 20 nM human LMPTP-A. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7KH8\7KH8_metadata.json point structures/7KH8/7kh8_protein.pdb structures/7KH8/7kh8_pocket.pdb structures/7KH8/7kh8_ligand.sdf structures/7KH8/7kh8_ligand.pdb structures/7KH8/7kh8_ligand.cif structures/7KH8/7kh8_complex.pdb structures/7KH8/7kh8_complex.cif 7KHM classic hDHHS20 human human DHHC20 containing the C156S mutation (hDHHS20) C156S palmitoyl-CoA "[""PKZ""]" 1 Kd Kd = = 6.1 µM 6100.0 [] unit_conversion 5.214670164989233 success True direct_binding Isothermal titration calorimetry of purified catalytically inactive hDHHS20 with PCoA. 2 Fig. 1D prints “Kd = 6.1 µM” for hDHHS20 binding to PCoA; the text identifies hDHHS20 as the catalytic-cysteine serine mutant used for the structural complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7KHM\7KHM_metadata.json point structures/7KHM/7khm_protein.pdb structures/7KHM/7khm_pocket.pdb structures/7KHM/7khm_ligand.sdf structures/7KHM/7khm_ligand.pdb structures/7KHM/7khm_ligand.cif structures/7KHM/7khm_complex.pdb structures/7KHM/7khm_complex.cif 7KHN classic NicA2 Na Na N462Y/W427Y (S)-nicotine "[""NCT""]" 1 Kd Kd = = 39 ± 10 ×10^-6 M 39000.0 [] unit_conversion 4.4089353929735005 success True direct_binding Anaerobic stopped-flow spectrophotometry at pH 7.5 and 5.6 °C; Kd obtained from the first-phase reduction kinetics with (S)-nicotine. 8 Table 3 reports Kd = 39 ± 10 × 10^-6 M for NicA2 N462Y/W427Y; the text identifies these as stopped-flow kinetic parameters for (S)-nicotine. auto_single_measurement only accepted activity measurement [1] 1 structures\7KHN\7KHN_metadata.json point structures/7KHN/7khn_protein.pdb structures/7KHN/7khn_pocket.pdb structures/7KHN/7khn_ligand.sdf structures/7KHN/7khn_ligand.pdb structures/7KHN/7khn_ligand.cif structures/7KHN/7khn_complex.pdb structures/7KHN/7khn_complex.cif 7KHO classic NicA2 Na Na N462V (S)-nicotine "[""NCT""]" 1 Kd Kd = = 35 ± 6 ×10^-6 M 35000.0 [] unit_conversion 4.455931955649724 success True direct_binding Anaerobic stopped-flow spectrophotometry at pH 7.5 and 5.6 °C; Kd obtained from the first-phase reduction kinetics with (S)-nicotine. 8 Table 3 reports Kd = 35 ± 6 × 10^-6 M for NicA2 N462V; the text identifies these as stopped-flow kinetic parameters for (S)-nicotine. auto_single_measurement only accepted activity measurement [1] 1 structures\7KHO\7KHO_metadata.json point structures/7KHO/7kho_protein.pdb structures/7KHO/7kho_pocket.pdb structures/7KHO/7kho_ligand.sdf structures/7KHO/7kho_ligand.pdb structures/7KHO/7kho_ligand.cif structures/7KHO/7kho_complex.pdb structures/7KHO/7kho_complex.cif 7KHU extended Carbohydrate-binding domain VP8* of human P[4] rotavirus strain BM5265 human VP8* core fragment, amino acids 64-223, expressed with an N-terminal GST tag; GST tag removed before crystallization Na LNDFH I (Lacto-N-difucohexaose I) "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 2.5 mM 2500000.0 [] unit_conversion 2.6020599913279625 success True direct_binding NMR HSQC titration experiment for P[4] VP8* and LNDFH I. 10 Table 2 reports Kd = 2.5 mM for P[4] with LNDFH I; Figure 4 identifies the LNDFH I–P[4] complex as PDB 7KHU. auto_single_measurement only accepted activity measurement [1] 1 structures\7KHU\7KHU_metadata.json point structures/7KHU/7khu_protein.pdb structures/7KHU/7khu_pocket.pdb structures/7KHU/7khu_ligand.pdb structures/7KHU/7khu_ligand.cif structures/7KHU/7khu_complex.pdb structures/7KHU/7khu_complex.cif 7KJJ classic TTR ancestor Na Na Na thyroxine (T4) "[""T44""]" 1 Kd Kd = = 2.33 μM 2330.0 [] unit_conversion 5.632644078973981 success True direct_binding Isothermal titration calorimetry (ITC) measurement of T4 binding to the reconstructed TTR ancestor. 5 The paper states that the TTR ancestor showed T4 binding by ITC and that its adjusted K_D was 2.33 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KJJ\7KJJ_metadata.json point structures/7KJJ/7kjj_protein.pdb structures/7KJJ/7kjj_pocket.pdb structures/7KJJ/7kjj_ligand.sdf structures/7KJJ/7kjj_ligand.pdb structures/7KJJ/7kjj_ligand.cif structures/7KJJ/7kjj_complex.pdb structures/7KJJ/7kjj_complex.cif 7KJM extended MDM2 human MDM2 residues 25-109 Na DPMI-omega "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.16 ± 0.02 nM 0.16 [] unit_conversion 9.795880017344075 success True direct_binding SPR-based competitive binding assay with synthetic MDM2; Table 1 reports the MDM2 Kd for DPMI-omega. 3 Table 1 lists DPMI-omega: MDM2 Kd = 0.16 ± 0.02 nM. The table title specifies synthetic 25-109 MDM2, determined by competition SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\7KJM\7KJM_metadata.json point structures/7KJM/7kjm_protein.pdb structures/7KJM/7kjm_pocket.pdb structures/7KJM/7kjm_ligand.pdb structures/7KJM/7kjm_ligand.cif structures/7KJM/7kjm_complex.pdb structures/7KJM/7kjm_complex.cif 7KJN extended MDMX human MDMX residues 24-108 Na DPMI-omega "[""CHAIN:B"", ""CHAIN:C""]" 1 Kd Kd = = 28.7 ± 2.5 nM 28.7 [] unit_conversion 7.542118103266008 success True direct_binding SPR-based competitive binding assay with synthetic MDMX; Table 1 reports the MDMX Kd for DPMI-omega. 3 Table 1 lists DPMI-omega: MDMX Kd = 28.7 ± 2.5 nM. The table title specifies synthetic 24-108 MDMX, determined by competition SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\7KJN\7KJN_metadata.json point structures/7KJN/7kjn_protein.pdb structures/7KJN/7kjn_pocket.pdb structures/7KJN/7kjn_ligand.pdb structures/7KJN/7kjn_ligand.cif structures/7KJN/7kjn_complex.pdb structures/7KJN/7kjn_complex.cif 7KJS classic CDK2/cyclin E1 Homo sapiens Full-length human CDK2 and human cyclin E1 residues 96-378; an N-terminal His tag is described for the cyclin E1 construct Na PF-06873600; compound 22 "[""WG1""]" 1 Ki Ki = = 0.13 ± 0.01 nM 0.13 [] unit_conversion 9.886056647693163 success True biochemical_inhibition Mobility-shift biochemical kinase inhibition assay; Table 2 reports arithmetic mean of at least three independent replicates ± SEM. 7 Table 2, compound 22: CDK2/cyclinE1 Ki = 0.13 ± 0.01 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KJS\7KJS_metadata.json point structures/7KJS/7kjs_protein.pdb structures/7KJS/7kjs_pocket.pdb structures/7KJS/7kjs_ligand.sdf structures/7KJS/7kjs_ligand.pdb structures/7KJS/7kjs_ligand.cif structures/7KJS/7kjs_complex.pdb structures/7KJS/7kjs_complex.cif 7KJZ classic PLEKHA7 human PLEKHA7 PH domain, PHA7-D175K D175K inositol-tetraphosphate; IP(3,4,5)P3 "[""4IP""]" 1 Kd Kd = = 3.5 ± 0.5 μM 3500.0 [] unit_conversion 5.455931955649724 success True direct_binding ITC with soluble IP(3,4,5)P3. 6 Table 1 reports Kd = 3.5 ± 0.5 μM for PHA7-D175K with soluble IP(3,4,5)P3. auto_single_measurement only accepted activity measurement [1] 1 structures\7KJZ\7KJZ_metadata.json point structures/7KJZ/7kjz_protein.pdb structures/7KJZ/7kjz_pocket.pdb structures/7KJZ/7kjz_ligand.sdf structures/7KJZ/7kjz_ligand.pdb structures/7KJZ/7kjz_ligand.cif structures/7KJZ/7kjz_complex.pdb structures/7KJZ/7kjz_complex.cif 7KK3 classic poly(ADP-ribose) polymerase 1 (PARP1) Na N-terminally hexahistidine-tagged PARP1 catalytic domain, residues 662-1011 Na talazoparib "[""2YQ""]" 1 Kd Kd = = 0.6 ± 0.1 nM 0.6 [] unit_conversion 9.221848749616356 success True direct_binding SPR single-cycle kinetics; Table 1 reports PARP1 inhibitor binding kinetics. 3 Table 1: Talazoparib, PARP1, Kin. K_D (nM) = 0.6 ± 0.1. auto_single_measurement only accepted activity measurement [1] 1 structures\7KK3\7KK3_metadata.json point structures/7KK3/7kk3_protein.pdb structures/7KK3/7kk3_pocket.pdb structures/7KK3/7kk3_ligand.sdf structures/7KK3/7kk3_ligand.pdb structures/7KK3/7kk3_ligand.cif structures/7KK3/7kk3_complex.pdb structures/7KK3/7kk3_complex.cif 7KK4 classic poly(ADP-ribose) polymerase 1 (PARP1) Na N-terminally hexahistidine-tagged PARP1 catalytic domain, residues 662-1011 Na olaparib "[""09L""]" 1 Kd Kd = = 0.8 ± 0.1 nM 0.8 [] unit_conversion 9.096910013008056 success True direct_binding SPR single-cycle kinetics; Table 1 reports PARP1 inhibitor binding kinetics. 3 Table 1: Olaparib, PARP1, Kin. K_D (nM) = 0.8 ± 0.1. auto_single_measurement only accepted activity measurement [1] 1 structures\7KK4\7KK4_metadata.json point structures/7KK4/7kk4_protein.pdb structures/7KK4/7kk4_pocket.pdb structures/7KK4/7kk4_ligand.sdf structures/7KK4/7kk4_ligand.pdb structures/7KK4/7kk4_ligand.cif structures/7KK4/7kk4_complex.pdb structures/7KK4/7kk4_complex.cif 7KK5 classic poly(ADP-ribose) polymerase 1 (PARP1) Na N-terminally hexahistidine-tagged PARP1 catalytic domain, residues 662-1011 Na niraparib "[""3JD""]" 1 Kd Kd = = 5.4 ± 1.4 nM 5.4 [] unit_conversion 8.267606240177031 success True direct_binding SPR single-cycle kinetics; Table 1 reports PARP1 inhibitor binding kinetics. 3 Table 1: Niraparib, PARP1, Kin. K_D (nM) = 5.4 ± 1.4. auto_single_measurement only accepted activity measurement [1] 1 structures\7KK5\7KK5_metadata.json point structures/7KK5/7kk5_protein.pdb structures/7KK5/7kk5_pocket.pdb structures/7KK5/7kk5_ligand.sdf structures/7KK5/7kk5_ligand.pdb structures/7KK5/7kk5_ligand.cif structures/7KK5/7kk5_complex.pdb structures/7KK5/7kk5_complex.cif 7KK6 classic poly(ADP-ribose) polymerase 1 (PARP1) Na N-terminally hexahistidine-tagged PARP1 catalytic domain, residues 662-1011 Na veliparib "[""78P""]" 1 Kd Kd = = 6.2 ± 3.5 nM 6.2 [] unit_conversion 8.207608310501746 success True direct_binding SPR single-cycle kinetics; Table 1 reports PARP1 inhibitor binding kinetics. 3 Table 1: Veliparib, PARP1, Kin. K_D (nM) = 6.2 ± 3.5. auto_single_measurement only accepted activity measurement [1] 1 structures\7KK6\7KK6_metadata.json point structures/7KK6/7kk6_protein.pdb structures/7KK6/7kk6_pocket.pdb structures/7KK6/7kk6_ligand.sdf structures/7KK6/7kk6_ligand.pdb structures/7KK6/7kk6_ligand.cif structures/7KK6/7kk6_complex.pdb structures/7KK6/7kk6_complex.cif 7KKE classic phosphoinositide 3-kinase gamma (PI3Kγ) human Na Na compound 11 "[""WJV""]" 1 Ki Ki = = 9 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition Table 1 enzymatic PI3Kγ inhibition/selectivity profiling; the same page states that a human PI3Kγ–compound 11 X-ray crystal structure is PDB 7KKE. 3 “Compound 11” has “PI3Kγ Ki (nM)” of 9 in Table 1; text states “an X-ray crystal structure of human PI3Kγ in complex with compound 11 (PDB ID 7KKE) was obtained.” auto_single_measurement only accepted activity measurement [1] 1 structures\7KKE\7KKE_metadata.json point structures/7KKE/7kke_protein.pdb structures/7KKE/7kke_pocket.pdb structures/7KKE/7kke_ligand.sdf structures/7KKE/7kke_ligand.pdb structures/7KKE/7kke_ligand.cif structures/7KKE/7kke_complex.pdb structures/7KKE/7kke_complex.cif 7KKN classic tankyrase 1 (TNKS1) Na N-terminally hexahistidine-tagged TNKS1 ART domain, residues 1104-1314 Na talazoparib "[""2YQ""]" 1 Kd Kd = = 14 ± 1 nM 14.0 [] unit_conversion 7.853871964321762 success True direct_binding SPR single-cycle kinetics; Table 1 reports TNKS1 inhibitor binding kinetics. 3 Table 1: Talazoparib, TNKS1, Kin. K_D (nM) = 14 ± 1. auto_single_measurement only accepted activity measurement [1] 1 structures\7KKN\7KKN_metadata.json point structures/7KKN/7kkn_protein.pdb structures/7KKN/7kkn_pocket.pdb structures/7KKN/7kkn_ligand.sdf structures/7KKN/7kkn_ligand.pdb structures/7KKN/7kkn_ligand.cif structures/7KKN/7kkn_complex.pdb structures/7KKN/7kkn_complex.cif 7KKO classic tankyrase 1 (TNKS1) Na N-terminally hexahistidine-tagged TNKS1 ART domain, residues 1104-1314 Na olaparib "[""09L""]" 1 Kd Kd = = 1700 ± 6 nM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding SPR single-cycle kinetics; Table 1 reports TNKS1 inhibitor binding kinetics. 3 Table 1: Olaparib, TNKS1, Kin. K_D (nM) = 1700 ± 6. auto_single_measurement only accepted activity measurement [1] 1 structures\7KKO\7KKO_metadata.json point structures/7KKO/7kko_protein.pdb structures/7KKO/7kko_pocket.pdb structures/7KKO/7kko_ligand.sdf structures/7KKO/7kko_ligand.pdb structures/7KKO/7kko_ligand.cif structures/7KKO/7kko_complex.pdb structures/7KKO/7kko_complex.cif 7KKP classic tankyrase 1 (TNKS1) Na N-terminally hexahistidine-tagged TNKS1 ART domain, residues 1104-1314 Na niraparib "[""3JD""]" 1 Kd Kd = = 34,800 ± 540 nM 34800.0 [] unit_conversion 4.458420756053419 success True direct_binding SPR single-cycle kinetics; Table 1 reports TNKS1 inhibitor binding kinetics. 3 Table 1: Niraparib, TNKS1, Kin. K_D (nM) = 34,800 ± 540. auto_single_measurement only accepted activity measurement [1] 1 structures\7KKP\7KKP_metadata.json point structures/7KKP/7kkp_protein.pdb structures/7KKP/7kkp_pocket.pdb structures/7KKP/7kkp_ligand.sdf structures/7KKP/7kkp_ligand.pdb structures/7KKP/7kkp_ligand.cif structures/7KKP/7kkp_complex.pdb structures/7KKP/7kkp_complex.cif 7KKQ classic tankyrase 1 (TNKS1) Na N-terminally hexahistidine-tagged TNKS1 ART domain, residues 1104-1314 Na veliparib "[""78P""]" 1 Kd Kd = = 17,500 ± 300 nM 17500.0 [] unit_conversion 4.756961951313706 success True direct_binding SPR single-cycle kinetics; Table 1 reports TNKS1 inhibitor binding kinetics. 3 Table 1: Veliparib, TNKS1, Kin. K_D (nM) = 17,500 ± 300. auto_single_measurement only accepted activity measurement [1] 1 structures\7KKQ\7KKQ_metadata.json point structures/7KKQ/7kkq_protein.pdb structures/7KKQ/7kkq_pocket.pdb structures/7KKQ/7kkq_ligand.sdf structures/7KKQ/7kkq_ligand.pdb structures/7KKQ/7kkq_ligand.cif structures/7KKQ/7kkq_complex.pdb structures/7KKQ/7kkq_complex.cif 7KL5 extended Calmodulin bound to cardiac ryanodine receptor 2 (RyR2) peptide Na Calmodulin bound to a RyR2 peptide spanning Phe4246-Val4271 Na RyR2 CaMBD3 peptide (Phe4246-Val4271) "[""CHAIN:B""]" 1 Kd Kd = = 100 ± 50 nM 100.0 [] unit_conversion 7.0 success True direct_binding Fluorescence polarization binding of fluorescently labeled CaMBD3 peptide to full-length CaMWT in 2.0 mM CaCl2. 4 Figure 3C reports Kd values of 100 ± 50 nM for CaM WT binding CaMBD3 peptide. auto_metric_priority unique highest-priority metric family: Kd [1] 6 structures\7KL5\7KL5_metadata.json point structures/7KL5/7kl5_protein.pdb structures/7KL5/7kl5_pocket.pdb structures/7KL5/7kl5_ligand.pdb structures/7KL5/7kl5_ligand.cif structures/7KL5/7kl5_complex.pdb structures/7KL5/7kl5_complex.cif 7KL6 classic Helicobacter pylori xanthine-guanine-hypoxanthine phosphoribosyltransferase (HpXGHPRT) Helicobacter pylori Na Na 9-[(N-3-phosphonopropyl)-aminomethyl]-9-deazahypoxanthine (compound XII) "[""WG7""]" 1 Ki Ki = = 2400 ± 400 nM 2400.0 [] unit_conversion 5.619788758288394 success True biochemical_inhibition Competitive inhibition assay of HpXGHPRT with compound XII; the paper compares this value with human and PfHGHPRT. 10 “The Ki value of XII for HpXGHPRT is 2400 ± 400 nM”. auto_single_measurement only accepted activity measurement [1] 1 structures\7KL6\7KL6_metadata.json point structures/7KL6/7kl6_protein.pdb structures/7KL6/7kl6_pocket.pdb structures/7KL6/7kl6_ligand.sdf structures/7KL6/7kl6_ligand.pdb structures/7KL6/7kl6_ligand.cif structures/7KL6/7kl6_complex.pdb structures/7KL6/7kl6_complex.cif 7KLK classic Human Arginase1 Human Na Na Compound 3a "[""XFP""]" 1 IC50 IC50 = = 377 nM 377.0 [] unit_conversion 6.423658649794207 success True biochemical_inhibition ARG1 enzymatic IC50 3 Table 1 reports compound 3a with ARG1 enzymatic IC50 = 377 nM; Figure 2 maps compound 3a bound to hARG1 to PDB 7KLK. auto_single_measurement only accepted activity measurement [1] 1 structures\7KLK\7KLK_metadata.json point structures/7KLK/7klk_protein.pdb structures/7KLK/7klk_pocket.pdb structures/7KLK/7klk_ligand.sdf structures/7KLK/7klk_ligand.pdb structures/7KLK/7klk_ligand.cif structures/7KLK/7klk_complex.pdb structures/7KLK/7klk_complex.cif 7KLL classic Human Arginase1 Human Na Na Compound 18 "[""XFG""]" 1 IC50 IC50 = = 3 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition ARG1 enzymatic IC50 4 Table 2 reports compound 18 with ARG1 enzymatic IC50 = 3 nM; Figure 4 maps compound 18 bound to hARG1 to PDB 7KLL. auto_single_measurement only accepted activity measurement [1] 1 structures\7KLL\7KLL_metadata.json point structures/7KLL/7kll_protein.pdb structures/7KLL/7kll_pocket.pdb structures/7KLL/7kll_ligand.sdf structures/7KLL/7kll_ligand.pdb structures/7KLL/7kll_ligand.cif structures/7KLL/7kll_complex.pdb structures/7KLL/7kll_complex.cif 7KLM classic Human Arginase1 Human Na Na Compound 24a "[""0IZ""]" 1 IC50 IC50 = = 2 nM 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition ARG1 enzymatic IC50 5 Table 3 reports compound 24a with ARG1 enzymatic IC50 = 2 nM; Figure 4 maps compound 24a bound to hARG1 to PDB 7KLM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KLM\7KLM_metadata.json point structures/7KLM/7klm_protein.pdb structures/7KLM/7klm_pocket.pdb structures/7KLM/7klm_ligand.sdf structures/7KLM/7klm_ligand.pdb structures/7KLM/7klm_ligand.cif structures/7KLM/7klm_complex.pdb structures/7KLM/7klm_complex.cif 7KMA classic eIF2B alpha Na Recombinant eIF2B alpha expressed with a C-terminal TEV-avi-FLAG tag; tag removed before crystallization Na mannose-6-phosphate (M6P) "[""M6P""]" 1 Kd Kd = = 282 ± 35 µM 282000.0 [] unit_conversion 3.549750891680639 success True direct_binding ITC measurement of recombinant eIF2Bα binding to M6P. 3 “the affinity of eIF2Bα for the F6P isomer mannose-6-phosphate (M6P) was considerably weaker, with Kd = 282 ± 35 μM”. The paper maps PDB 7KMA to the eIF2Bα–M6P X-ray crystal structure. auto_single_measurement only accepted activity measurement [1] 1 structures\7KMA\7KMA_metadata.json point structures/7KMA/7kma_protein.pdb structures/7KMA/7kma_pocket.pdb structures/7KMA/7kma_ligand.sdf structures/7KMA/7kma_ligand.pdb structures/7KMA/7kma_ligand.cif structures/7KMA/7kma_complex.pdb structures/7KMA/7kma_complex.cif 7KPK extended SPOP human SPOP residues 28-43, 49-119, and 121-165 with an exogenous PG N-terminal cloning artifact, complexed with human Pdx1 residues 267-273 Na Pdx1-SBM2 peptide, human Pdx1 residues 265-283 "[""CHAIN:B""]" 1 Kd Kd > > 600 µM 600000.0 [] unit_conversion 3.221848749616356 success True direct_binding Fluorescence-anisotropy binding assessment of synthetic Pdx1 SBM peptides to SPOP-MATH. 8 “Pdx1-SBM2 binds weakly with a K_D > 600 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7KPK\7KPK_metadata.json point structures/7KPK/7kpk_protein.pdb structures/7KPK/7kpk_pocket.pdb structures/7KPK/7kpk_ligand.pdb structures/7KPK/7kpk_ligand.cif structures/7KPK/7kpk_complex.pdb structures/7KPK/7kpk_complex.cif 7KPY classic CBP (CREB-binding protein) Na Cleaved CBP bromodomain Na UMB298 (compound 23) "[""WU1""]" 1 Kd Kd = = 315 ± 7 nM 315.0 [] unit_conversion 6.501689446210399 success True direct_binding BromoELECT direct-binding measurement; Figure 7 reports Kd toward CBP. 31 Figure 7C lists compound 23 Kd toward CREBBP/CBP as 315 ± 7 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7KPY\7KPY_metadata.json point structures/7KPY/7kpy_protein.pdb structures/7KPY/7kpy_pocket.pdb structures/7KPY/7kpy_ligand.sdf structures/7KPY/7kpy_ligand.pdb structures/7KPY/7kpy_ligand.cif structures/7KPY/7kpy_complex.pdb structures/7KPY/7kpy_complex.cif 7KQ0 extended human proliferating cell nuclear antigen (hPCNA) human Na F150Y in the p21_mu peptide p21_mu-F150Y peptide, p21 sequence residues 141-155 "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F""]" 1 Kd Kd = = 20.20 nM 20.2 [] unit_conversion 7.694648630553377 success True direct_binding Surface plasmon resonance (SPR) binding affinity of p21_mu-F150Y to hPCNA. 4 Figure 2B reports p21_mu-F150Y with K_D 20.20 nM; the Figure 3 caption identifies the p21_mu-F150Y:hPCNA cocrystal as PDB 7KQ0. auto_single_measurement only accepted activity measurement [1] 1 structures\7KQ0\7KQ0_metadata.json point structures/7KQ0/7kq0_protein.pdb structures/7KQ0/7kq0_pocket.pdb structures/7KQ0/7kq0_ligand.pdb structures/7KQ0/7kq0_ligand.cif structures/7KQ0/7kq0_complex.pdb structures/7KQ0/7kq0_complex.cif 7KQ1 extended human proliferating cell nuclear antigen (hPCNA) human Na Na p21_mu peptide, p21 sequence residues 141-155 "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F""]" 1 Kd Kd = = 12.3 nM 12.3 [] unit_conversion 7.910094888560602 success True direct_binding Surface plasmon resonance (SPR) binding affinity of truncated p21_mu (residues 141–155) to hPCNA. 3 The Results state that p21_mu (residues 141–155) bound hPCNA with 12.3 nM affinity; the same paragraph identifies the p21_mu:hPCNA cocrystal as PDB 7KQ1. auto_single_measurement only accepted activity measurement [1] 1 structures\7KQ1\7KQ1_metadata.json point structures/7KQ1/7kq1_protein.pdb structures/7KQ1/7kq1_pocket.pdb structures/7KQ1/7kq1_ligand.pdb structures/7KQ1/7kq1_ligand.cif structures/7KQ1/7kq1_complex.pdb structures/7KQ1/7kq1_complex.cif 7KQ8 classic MEMO1 Na Na wild type iron (Fe2+) "[""FE2""]" 1 Kd Kd = = 5.0 ± 2.6 × 10^-6 M 5000.0 [] unit_conversion 5.301029995663981 success True direct_binding Isothermal titration calorimetry of purified MEMO1 with iron in 9.5 mM reduced glutathione and 0.5 mM oxidized glutathione. 10 “The measured Kd value for iron in the presence of glutathione was 5.0±2.6 × 10−6 M (Figure 5A).” auto_single_measurement only accepted activity measurement [1] 1 structures\7KQ8\7KQ8_metadata.json point structures/7KQ8/7kq8_protein.pdb structures/7KQ8/7kq8_pocket.pdb structures/7KQ8/7kq8_ligand.sdf structures/7KQ8/7kq8_ligand.pdb structures/7KQ8/7kq8_ligand.cif structures/7KQ8/7kq8_complex.pdb structures/7KQ8/7kq8_complex.cif 7KRC classic HIV-1 reverse transcriptase HIV-1 recombinant RT52A enzyme wild-type (WT) compound 12 (JLJ709) "[""X2J""]" 1 IC50 IC50 = = 119 nM 119.0 [] unit_conversion 6.924453038607469 success True biochemical_inhibition PicroGreen-based reverse transcriptase assay; standard enzyme-inhibition conditions. 3 Table 1 reports compound 12 IC50 = 119 nM; the text identifies the assay as inhibition of recombinant WT HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\7KRC\7KRC_metadata.json point structures/7KRC/7krc_protein.pdb structures/7KRC/7krc_pocket.pdb structures/7KRC/7krc_ligand.sdf structures/7KRC/7krc_ligand.pdb structures/7KRC/7krc_ligand.cif structures/7KRC/7krc_complex.pdb structures/7KRC/7krc_complex.cif 7KRE classic HIV-1 reverse transcriptase HIV-1 recombinant RT52A enzyme wild-type (WT) compound 6 (JLJ704) "[""X2V""]" 1 IC50 IC50 = = 82.3 nM 82.3 [] unit_conversion 7.08460016478773 success True biochemical_inhibition PicroGreen-based reverse transcriptase assay; standard enzyme-inhibition conditions. 3 Table 1 reports compound 6 IC50 = 82.3 nM; the text identifies the assay as inhibition of recombinant WT HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\7KRE\7KRE_metadata.json point structures/7KRE/7kre_protein.pdb structures/7KRE/7kre_pocket.pdb structures/7KRE/7kre_ligand.sdf structures/7KRE/7kre_ligand.pdb structures/7KRE/7kre_ligand.cif structures/7KRE/7kre_complex.pdb structures/7KRE/7kre_complex.cif 7KRF classic HIV-1 reverse transcriptase HIV-1 recombinant RT52A enzyme wild-type (WT) compound 11 (JLJ710) "[""X2G""]" 1 IC50 IC50 = = 150 nM 150.0 [] unit_conversion 6.823908740944319 success True biochemical_inhibition PicroGreen-based reverse transcriptase assay; standard enzyme-inhibition conditions. 3 Table 1 reports compound 11 IC50 = 150 nM; the text identifies the assay as inhibition of recombinant WT HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\7KRF\7KRF_metadata.json point structures/7KRF/7krf_protein.pdb structures/7KRF/7krf_pocket.pdb structures/7KRF/7krf_ligand.sdf structures/7KRF/7krf_ligand.pdb structures/7KRF/7krf_ligand.cif structures/7KRF/7krf_complex.pdb structures/7KRF/7krf_complex.cif 7KS8 extended human CYP3A4 human truncated Delta3-22 CYP3A4 Na compound 7, [Ru(tpy)(Me2bpy)(4)]Cl2 "[""X8S""]" 1 Kd Kd = = 0.34 µM 340.0 [] unit_conversion 6.468521082957745 success True direct_binding Equilibrium spectral titration of Δ3–22 CYP3A4 with compound 7 under visible-light irradiation; hyperbolic fit. 5 “Hyperbolic fitting to the titration resulted in Kd = 340 nM for 7 under irradiation (Figure 3B).” auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7KS8\7KS8_metadata.json point structures/7KS8/7ks8_protein.pdb structures/7KS8/7ks8_pocket.pdb structures/7KS8/7ks8_ligand.pdb structures/7KS8/7ks8_ligand.cif structures/7KS8/7ks8_complex.pdb structures/7KS8/7ks8_complex.cif 7KSI classic JNK3 human Na Na compound 27 "[""X3S""]" 1 IC50 IC50 = = 0.067 μM 67.0 [] unit_conversion 7.173925197299173 success True biochemical_inhibition Kinase inhibition IC50 reported for JNK3. 4 Figure 3 prints: compound 27, “Kinase inh. IC50”; JNK3: 0.067 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KSI\7KSI_metadata.json point structures/7KSI/7ksi_protein.pdb structures/7KSI/7ksi_pocket.pdb structures/7KSI/7ksi_ligand.sdf structures/7KSI/7ksi_ligand.pdb structures/7KSI/7ksi_ligand.cif structures/7KSI/7ksi_complex.pdb structures/7KSI/7ksi_complex.cif 7KSJ classic JNK3 human Na Na compound 25 "[""X3Y""]" 1 IC50 IC50 = = 0.053 μM 53.0 [] unit_conversion 7.275724130399211 success True biochemical_inhibition Kinase inhibition IC50 reported for JNK3. 4 Figure 3 prints: compound 25, “Kinase inh. IC50”; JNK3: 0.053 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KSJ\7KSJ_metadata.json point structures/7KSJ/7ksj_protein.pdb structures/7KSJ/7ksj_pocket.pdb structures/7KSJ/7ksj_ligand.sdf structures/7KSJ/7ksj_ligand.pdb structures/7KSJ/7ksj_ligand.cif structures/7KSJ/7ksj_complex.pdb structures/7KSJ/7ksj_complex.cif 7KSK classic JNK3 human Na Na compound 17 "[""X3V""]" 1 IC50 IC50 = = 35 nM 35.0 [] unit_conversion 7.455931955649724 success True biochemical_inhibition JNK3 kinase inhibition. 1 The abstract states: “Inhibitor 17 was a potent and isoform selective JNK3 inhibitor (IC50 = 35 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7KSK\7KSK_metadata.json point structures/7KSK/7ksk_protein.pdb structures/7KSK/7ksk_pocket.pdb structures/7KSK/7ksk_ligand.sdf structures/7KSK/7ksk_ligand.pdb structures/7KSK/7ksk_ligand.cif structures/7KSK/7ksk_complex.pdb structures/7KSK/7ksk_complex.cif 7KUA classic MarR_iacR Pseudomonas putida Na Na Indole-3-acetic acid (IAA) "[""IAC""]" 1 Kd Kd = = 4.449 ± 0.196 µM 4449.0 [] unit_conversion 5.351737594251956 success True direct_binding ITC; Extended Data Table 1. 25 Pseudomonas putida 1290 MarR_iacR (7KUA): KD1 = 4.449 ± 0.196 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KUA\7KUA_metadata.json point structures/7KUA/7kua_protein.pdb structures/7KUA/7kua_pocket.pdb structures/7KUA/7kua_ligand.sdf structures/7KUA/7kua_ligand.pdb structures/7KUA/7kua_ligand.cif structures/7KUA/7kua_complex.pdb structures/7KUA/7kua_complex.cif 7KW9 classic tRNA 2'-phosphotransferase Tpt1 (RslTpt1) Runella slithyformis RslTpt1 residues Val5-Val178 with retained N-terminal Gly-Ser-His-Met tag Na NAD+ "[""NAD""]" 1 Kd Kd = = 31 ± 1 µM 31000.0 [] unit_conversion 4.508638306165727 success True direct_binding ITC; duplicate measurements at various times. 9 Table 2 reports an ITC-determined K_D of 31 ± 1 µM for NAD+ and RslTpt1. auto_single_measurement only accepted activity measurement [1] 1 structures\7KW9\7KW9_metadata.json point structures/7KW9/7kw9_protein.pdb structures/7KW9/7kw9_pocket.pdb structures/7KW9/7kw9_ligand.sdf structures/7KW9/7kw9_ligand.pdb structures/7KW9/7kw9_ligand.cif structures/7KW9/7kw9_complex.pdb structures/7KW9/7kw9_complex.cif 7KWU classic HIV-1 reverse transcriptase (RT) Human immunodeficiency virus type 1 (HIV-1) Engineered HIV-1 RT construct RT52A Wild-type (WT) RT 16c; K07-15 "[""K7F""]" 1 IC50 IC50 = = 0.113 ± 0.032 μM 113.0 [] unit_conversion 6.94692155651658 success True biochemical_inhibition Inhibition of biotin deoxyuridine triphosphate incorporation into WT HIV-1 RT; Table 5. 7 Table 5 reports compound 16c IC50 = 0.113 ± 0.032 μM against WT HIV-1 RT; the footnote defines IC50 as the concentration required to inhibit biotin deoxyuridine triphosphate incorporation into WT HIV-1 RT by 50%. auto_single_measurement only accepted activity measurement [1] 1 structures\7KWU\7KWU_metadata.json point structures/7KWU/7kwu_protein.pdb structures/7KWU/7kwu_pocket.pdb structures/7KWU/7kwu_ligand.sdf structures/7KWU/7kwu_ligand.pdb structures/7KWU/7kwu_ligand.cif structures/7KWU/7kwu_complex.pdb structures/7KWU/7kwu_complex.cif 7KXL classic BTK1 Na Na Na compound 5 "[""X9J""]" 1 IC50 IC50 = = 0.4 nM 0.4 [] unit_conversion 9.397940008672037 success True biochemical_inhibition BTK enzyme IC50 reported in Table 1. 3 Table 1 reports compound 5 BTK enzyme/hPBMC IC50 values of 0.4/26(41) nM; the BTK enzyme value is 0.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KXL\7KXL_metadata.json point structures/7KXL/7kxl_protein.pdb structures/7KXL/7kxl_pocket.pdb structures/7KXL/7kxl_ligand.sdf structures/7KXL/7kxl_ligand.pdb structures/7KXL/7kxl_ligand.cif structures/7KXL/7kxl_complex.pdb structures/7KXL/7kxl_complex.cif 7KXN classic BTK1 Na Na Na compound 26 "[""X9P""]" 1 IC50 IC50 = = 1 nM 1.0 [] unit_conversion 9.0 success True biochemical_inhibition BTK enzyme IC50 reported in Table 3. 6 Table 3 reports compound 26 BTK enzyme/hPBMC IC50 values of 1/137 nM; the BTK enzyme value is 1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KXN\7KXN_metadata.json point structures/7KXN/7kxn_protein.pdb structures/7KXN/7kxn_pocket.pdb structures/7KXN/7kxn_ligand.sdf structures/7KXN/7kxn_ligand.pdb structures/7KXN/7kxn_ligand.cif structures/7KXN/7kxn_complex.pdb structures/7KXN/7kxn_complex.cif 7KXO classic BTK1 Na Na Na compound 24 "[""X9S""]" 1 IC50 IC50 = = 0.5 nM 0.5 [] unit_conversion 9.301029995663981 success True biochemical_inhibition BTK enzyme IC50 reported in Table 3. 6 Table 3 reports compound 24 BTK enzyme/hPBMC IC50 values of 0.5/30 nM; the BTK enzyme value is 0.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KXO\7KXO_metadata.json point structures/7KXO/7kxo_protein.pdb structures/7KXO/7kxo_pocket.pdb structures/7KXO/7kxo_ligand.sdf structures/7KXO/7kxo_ligand.pdb structures/7KXO/7kxo_ligand.cif structures/7KXO/7kxo_complex.pdb structures/7KXO/7kxo_complex.cif 7KXP classic BTK1 Na Na Na compound 25 "[""X9V""]" 1 IC50 IC50 = = 0.9 nM 0.9 [] unit_conversion 9.045757490560675 success True biochemical_inhibition BTK enzyme IC50 reported in Table 3. 6 Table 3 reports compound 25 BTK enzyme/hPBMC IC50 values of 0.9/87 nM; the BTK enzyme value is 0.9 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KXP\7KXP_metadata.json point structures/7KXP/7kxp_protein.pdb structures/7KXP/7kxp_pocket.pdb structures/7KXP/7kxp_ligand.sdf structures/7KXP/7kxp_ligand.pdb structures/7KXP/7kxp_ligand.cif structures/7KXP/7kxp_complex.pdb structures/7KXP/7kxp_complex.cif 7KXT classic EED Homo sapiens EED residues 40-441 Na astemizole "[""XB7""]" 1 IC50 IC50 = = 74.2 µM 74200.0 [] unit_conversion 4.129596094720973 success True biochemical_inhibition Fluorescence-polarization competition assay for inhibition of the EED–EZH2 interaction; Table 2/3 reports astemizole. 5 Tables 2 and 3 list astemizole with “FP assay (IC50, µM)” = 74.2. The methods describe this as an EED/EZH2 fluorescence-polarization competition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7KXT\7KXT_metadata.json point structures/7KXT/7kxt_protein.pdb structures/7KXT/7kxt_pocket.pdb structures/7KXT/7kxt_ligand.sdf structures/7KXT/7kxt_ligand.pdb structures/7KXT/7kxt_ligand.cif structures/7KXT/7kxt_complex.pdb structures/7KXT/7kxt_complex.cif 7KXZ classic EGFR Na kinase domain, residues 696-1022 WT BI-4020 "[""XA4""]" 1 IC50 IC50 > > 100 nM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition HTRF KinEASE assay using purified EGFR kinase; n=3, mean ± SD. 13 Table 1 reports BI-4020 IC50 >100 nM against EGFR WT. auto_single_measurement only accepted activity measurement [1] 1 structures\7KXZ\7KXZ_metadata.json point structures/7KXZ/7kxz_protein.pdb structures/7KXZ/7kxz_pocket.pdb structures/7KXZ/7kxz_ligand.sdf structures/7KXZ/7kxz_ligand.pdb structures/7KXZ/7kxz_ligand.cif structures/7KXZ/7kxz_complex.pdb structures/7KXZ/7kxz_complex.cif 7KYF classic Botulinum neurotoxin serotype A light chain (BoNT/A LC) Na Na Na compound 30 "[""XC1""]" 1 IC50 IC50 = = 0.089 μM 89.0 [] unit_conversion 7.050609993355087 success True biochemical_inhibition BoNT/A LC enzymatic assay using 20 nM BoNT/A LC and 8 μM SNAPtide substrate; dipeptide concentration range used to determine IC50. 4 Table 3 reports compound 30, IC50 0.089 μM. The text identifies the BoNT/A LC cocrystal with 30 as PDB 7KYF. auto_single_measurement only accepted activity measurement [1] 1 structures\7KYF\7KYF_metadata.json point structures/7KYF/7kyf_protein.pdb structures/7KYF/7kyf_pocket.pdb structures/7KYF/7kyf_ligand.sdf structures/7KYF/7kyf_ligand.pdb structures/7KYF/7kyf_ligand.cif structures/7KYF/7kyf_complex.pdb structures/7KYF/7kyf_complex.cif 7KYH classic Botulinum neurotoxin serotype A light chain (BoNT/A LC) Na Na Na compound 33 "[""XBM""]" 1 IC50 IC50 = = 0.021 μM 21.0 [] unit_conversion 7.6777807052660805 success True biochemical_inhibition BoNT/A LC enzymatic assay using 20 nM BoNT/A LC and 8 μM SNAPtide substrate; dipeptide concentration range used to determine IC50. 4 Table 3 reports compound 33, IC50 0.021 μM. The text identifies the BoNT/A LC cocrystal with 33 as PDB 7KYH. auto_single_measurement only accepted activity measurement [1] 1 structures\7KYH\7KYH_metadata.json point structures/7KYH/7kyh_protein.pdb structures/7KYH/7kyh_pocket.pdb structures/7KYH/7kyh_ligand.sdf structures/7KYH/7kyh_ligand.pdb structures/7KYH/7kyh_ligand.cif structures/7KYH/7kyh_complex.pdb structures/7KYH/7kyh_complex.cif 7KYK classic Plasmodium falciparum dihydroorotate dehydrogenase Plasmodium falciparum Loop-truncated PfDHODH Delta384-413 in pET28b-TEV-PfDHODH Delta384-413 construct Na DSM589 (compound 18) "[""XAJ""]" 1 IC50 IC50 = = 0.047 µM 47.0 [] unit_conversion 7.327902142064282 success True biochemical_inhibition Recombinant PfDHODH inhibition assay. 5 Table 1 lists compound 18 (DSM589), PfDHODH IC50 0.047 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KYK\7KYK_metadata.json point structures/7KYK/7kyk_protein.pdb structures/7KYK/7kyk_pocket.pdb structures/7KYK/7kyk_ligand.sdf structures/7KYK/7kyk_ligand.pdb structures/7KYK/7kyk_ligand.cif structures/7KYK/7kyk_complex.pdb structures/7KYK/7kyk_complex.cif 7KYV classic Plasmodium falciparum dihydroorotate dehydrogenase Plasmodium falciparum Loop-truncated PfDHODH Delta384-413 in pET28b-TEV-PfDHODH Delta384-413 construct Na DSM634 (compound 56) "[""XBY""]" 1 IC50 IC50 = = 0.046 µM 46.0 [] unit_conversion 7.337242168318426 success True biochemical_inhibition Recombinant PfDHODH inhibition assay. 7 Table 3 lists compound 56 (DSM634), PfDHODH IC50 0.046 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KYV\7KYV_metadata.json point structures/7KYV/7kyv_protein.pdb structures/7KYV/7kyv_pocket.pdb structures/7KYV/7kyv_ligand.sdf structures/7KYV/7kyv_ligand.pdb structures/7KYV/7kyv_ligand.cif structures/7KYV/7kyv_complex.pdb structures/7KYV/7kyv_complex.cif 7KYY classic Plasmodium falciparum dihydroorotate dehydrogenase Plasmodium falciparum Loop-truncated PfDHODH Delta384-413 in pET28b-TEV-PfDHODH Delta384-413 construct Na DSM697 (compound 127) "[""XCD""]" 1 IC50 IC50 = = 0.66 ± 0.25 (5) µM 660.0 [] unit_conversion 6.180456064458131 success True biochemical_inhibition Recombinant PfDHODH inhibition assay. 16 Table 7 lists compound 127 (DSM697), PfDHODH IC50 0.66 ± 0.25 (5) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KYY\7KYY_metadata.json point structures/7KYY/7kyy_protein.pdb structures/7KYY/7kyy_pocket.pdb structures/7KYY/7kyy_ligand.sdf structures/7KYY/7kyy_ligand.pdb structures/7KYY/7kyy_ligand.cif structures/7KYY/7kyy_complex.pdb structures/7KYY/7kyy_complex.cif 7KZ4 classic Plasmodium falciparum dihydroorotate dehydrogenase Plasmodium falciparum Loop-truncated PfDHODH Delta384-413 in pET28b-TEV-PfDHODH Delta384-413 construct Na DSM705 (compound 79) "[""XC7""]" 1 IC50 IC50 = = 0.095 ± 0.040 (11) µM 95.0 [] unit_conversion 7.022276394711152 success True biochemical_inhibition Recombinant PfDHODH inhibition assay. 10 Table 5 lists compound 79 (DSM705), PfDHODH IC50 0.095 ± 0.040 (11) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KZ4\7KZ4_metadata.json point structures/7KZ4/7kz4_protein.pdb structures/7KZ4/7kz4_pocket.pdb structures/7KZ4/7kz4_ligand.sdf structures/7KZ4/7kz4_ligand.pdb structures/7KZ4/7kz4_ligand.cif structures/7KZ4/7kz4_complex.pdb structures/7KZ4/7kz4_complex.cif 7KZY classic Plasmodium falciparum dihydroorotate dehydrogenase Plasmodium falciparum Loop-truncated PfDHODH Delta384-413 in pET28b-TEV-PfDHODH Delta384-413 construct Na DSM778 (compound 81) "[""XCM""]" 1 IC50 IC50 = = 0.057 ± 0.00071 (2) µM 57.0 [] unit_conversion 7.2441251443275085 success True biochemical_inhibition Recombinant PfDHODH inhibition assay. 10 Table 5 lists compound 81 (DSM778), PfDHODH IC50 0.057 ± 0.00071 (2) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7KZY\7KZY_metadata.json point structures/7KZY/7kzy_protein.pdb structures/7KZY/7kzy_pocket.pdb structures/7KZY/7kzy_ligand.sdf structures/7KZY/7kzy_ligand.pdb structures/7KZY/7kzy_ligand.cif structures/7KZY/7kzy_complex.pdb structures/7KZY/7kzy_complex.cif 7L01 classic Plasmodium falciparum dihydroorotate dehydrogenase Plasmodium falciparum Loop-truncated PfDHODH Delta384-413 in pET28b-TEV-PfDHODH Delta384-413 construct Na DSM782 (compound 86) "[""XCV""]" 1 IC50 IC50 = = 0.073 ± 0.018 (2) µM 73.0 [] unit_conversion 7.136677139879544 success True biochemical_inhibition Recombinant PfDHODH inhibition assay. 10 Table 5 lists compound 86 (DSM782), PfDHODH IC50 0.073 ± 0.018 (2) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7L01\7L01_metadata.json point structures/7L01/7l01_protein.pdb structures/7L01/7l01_pocket.pdb structures/7L01/7l01_ligand.sdf structures/7L01/7l01_ligand.pdb structures/7L01/7l01_ligand.cif structures/7L01/7l01_complex.pdb structures/7L01/7l01_complex.cif 7L0D classic SARS-CoV-2 Main Protease (Mpro) SARS-CoV-2 SARS2-Mpro expressed with a C-terminal His tag that was removed by PreScission protease Na ML188 "[""0EN""]" 1 IC50 IC50 = = 2.5 ± 0.3 µM 2500.0 [] unit_conversion 5.6020599913279625 success True biochemical_inhibition FRET-based enzymatic peptide-cleavage inhibition assay using purified SARS2-Mpro; 50 nM enzyme, 25 µM peptide substrate, 30 min at 25 °C. 4 “Using a FRET-based enzymatic assay, ML188 inhibits SARS1-Mpro with an IC50 of 4.5 ± 0.5 µM and inhibits SARS2-Mpro with an IC50 of 2.5 ± 0.3 µM.” Figure 2 identifies the SARS2-Mpro–ML188 complex as PDB 7L0D. auto_single_measurement only accepted activity measurement [1] 1 structures\7L0D\7L0D_metadata.json point structures/7L0D/7l0d_protein.pdb structures/7L0D/7l0d_pocket.pdb structures/7L0D/7l0d_ligand.sdf structures/7L0D/7l0d_ligand.pdb structures/7L0D/7l0d_ligand.cif structures/7L0D/7l0d_complex.pdb structures/7L0D/7l0d_complex.cif 7L0E classic RPE65 bovine Na Na gem-difluoro emixustat (compound 57) "[""XQ7""]" 1 IC50 IC50 = = 103 ± 29 nM 103.0 [] unit_conversion 6.987162775294828 success True biochemical_inhibition In vitro inhibition of 11-cis-retinol production by bovine RPE microsomes (RPE65 retinoid-isomerase activity assay). 34 Table 2 lists compound 57 with IC50 103 ± 29 nM; the assay context is bovine RPE microsomal RPE65 inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7L0E\7L0E_metadata.json point structures/7L0E/7l0e_protein.pdb structures/7L0E/7l0e_pocket.pdb structures/7L0E/7l0e_ligand.sdf structures/7L0E/7l0e_ligand.pdb structures/7L0E/7l0e_ligand.cif structures/7L0E/7l0e_complex.pdb structures/7L0E/7l0e_complex.cif 7L0K classic Plasmodium falciparum dihydroorotate dehydrogenase Plasmodium falciparum Loop-truncated PfDHODH Delta384-413 in pET28b-TEV-PfDHODH Delta384-413 construct Na DSM784 (compound 47) "[""XE7""]" 1 IC50 IC50 = = 0.35 ± 0.028 (2) µM 350.0 [] unit_conversion 6.455931955649724 success True biochemical_inhibition Recombinant PfDHODH inhibition assay. 6 Table 2 lists compound 47 (DSM784), PfDHODH IC50 0.35 ± 0.028 (2) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7L0K\7L0K_metadata.json point structures/7L0K/7l0k_protein.pdb structures/7L0K/7l0k_pocket.pdb structures/7L0K/7l0k_ligand.sdf structures/7L0K/7l0k_ligand.pdb structures/7L0K/7l0k_ligand.cif structures/7L0K/7l0k_complex.pdb structures/7L0K/7l0k_complex.cif 7L10 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 (2019-nCoV) Na Na compound 4 "[""XEY""]" 1 IC50 IC50 = = 4.02 ± 1.36 µM 4019.9999999999995 [] unit_conversion 5.39577394691553 success True biochemical_inhibition Kinetic proteolytic inhibition assay using 100 nM recombinant SARS-CoV-2 Mpro and a fluorogenic peptide substrate; measurements performed in triplicate and averaged. 3 Table 1 lists compound 4 IC50 as 4.02 ± 1.36 µM; Figure 3 identifies the compound 4 complex as PDB 7L10. auto_single_measurement only accepted activity measurement [1] 1 structures\7L10\7L10_metadata.json point structures/7L10/7l10_protein.pdb structures/7L10/7l10_pocket.pdb structures/7L10/7l10_ligand.sdf structures/7L10/7l10_ligand.pdb structures/7L10/7l10_ligand.cif structures/7L10/7l10_complex.pdb structures/7L10/7l10_complex.cif 7L11 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 (2019-nCoV) Na Na compound 5 "[""XF1""]" 1 IC50 IC50 = = 0.14 ± 0.02 µM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition Kinetic proteolytic inhibition assay using 100 nM recombinant SARS-CoV-2 Mpro and a fluorogenic peptide substrate; measurements performed in triplicate and averaged. 3 Table 1 lists compound 5 IC50 as 0.14 ± 0.02 µM; Figure 5 identifies the compound 5 complex as PDB 7L11. auto_single_measurement only accepted activity measurement [1] 1 structures\7L11\7L11_metadata.json point structures/7L11/7l11_protein.pdb structures/7L11/7l11_pocket.pdb structures/7L11/7l11_ligand.sdf structures/7L11/7l11_ligand.pdb structures/7L11/7l11_ligand.cif structures/7L11/7l11_complex.pdb structures/7L11/7l11_complex.cif 7L12 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 (2019-nCoV) Na Na compound 14 "[""XF4""]" 1 IC50 IC50 = = 0.128 ± 0.015 µM 128.0 [] unit_conversion 6.892790030352131 success True biochemical_inhibition Kinetic proteolytic inhibition assay using 100 nM recombinant SARS-CoV-2 Mpro and a fluorogenic peptide substrate; measurements performed in triplicate and averaged. 3 Table 1 lists compound 14 IC50 as 0.128 ± 0.015 µM; Figure 7 identifies the compound 14 complex as PDB 7L12. auto_single_measurement only accepted activity measurement [1] 1 structures\7L12\7L12_metadata.json point structures/7L12/7l12_protein.pdb structures/7L12/7l12_pocket.pdb structures/7L12/7l12_ligand.sdf structures/7L12/7l12_ligand.pdb structures/7L12/7l12_ligand.cif structures/7L12/7l12_complex.pdb structures/7L12/7l12_complex.cif 7L13 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 (2019-nCoV) Na Na compound 21 "[""XF7""]" 1 IC50 IC50 = = 0.018 ± 0.002 µM 18.0 [] unit_conversion 7.7447274948966935 success True biochemical_inhibition Kinetic proteolytic inhibition assay using 100 nM recombinant SARS-CoV-2 Mpro and a fluorogenic peptide substrate; measurements performed in triplicate and averaged. 3 Table 1 lists compound 21 IC50 as 0.018 ± 0.002 µM. Page 6 explicitly identifies the compound 21 Mpro complex as PDB 7L13. auto_single_measurement only accepted activity measurement [1] 1 structures\7L13\7L13_metadata.json point structures/7L13/7l13_protein.pdb structures/7L13/7l13_pocket.pdb structures/7L13/7l13_ligand.sdf structures/7L13/7l13_ligand.pdb structures/7L13/7l13_ligand.cif structures/7L13/7l13_complex.pdb structures/7L13/7l13_complex.cif 7L14 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 (2019-nCoV) Na Na compound 26 "[""XFD""]" 1 IC50 IC50 = = 0.170 ± 0.022 µM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition Kinetic proteolytic inhibition assay using 100 nM recombinant SARS-CoV-2 Mpro and a fluorogenic peptide substrate; measurements performed in triplicate and averaged. 3 Table 1 lists compound 26 IC50 as 0.170 ± 0.022 µM. Page 6 explicitly identifies the compound 26 Mpro complex as PDB 7L14. auto_single_measurement only accepted activity measurement [1] 1 structures\7L14\7L14_metadata.json point structures/7L14/7l14_protein.pdb structures/7L14/7l14_pocket.pdb structures/7L14/7l14_ligand.sdf structures/7L14/7l14_ligand.pdb structures/7L14/7l14_ligand.cif structures/7L14/7l14_complex.pdb structures/7L14/7l14_complex.cif 7L18 extended NADPH-cytochrome P450 reductase rat tandem deletion mutant deletion of Asp675 and Val676 (DeltaD675/DeltaV676) NADP+ "[""NAP""]" 1 Ki Ki = = 71.7 ± 7.1 μM 71700.0 [] unit_conversion 4.1444808443322 success True biochemical_inhibition NADP+ competitive-inhibition constant measured in kinetic characterization with NADPH as cofactor. 3 Table 3 lists Ki NADP+ = 71.7 ± 7.1 μM for ΔD675/ΔV676; the text states these inhibition constants were examined for NADP+ and that WT values measure Kd. auto_single_measurement only accepted activity measurement [1] 1 structures\7L18\7L18_metadata.json point structures/7L18/7l18_ligand.sdf structures/7L18/7l18_ligand.cif structures/7L18/7l18_complex.cif 7L19 classic MarR_Es Enterobacter soli Na Na Indole-3-acetic acid (IAA) "[""IAC""]" 1 Kd Kd = = 2.908 ± 0.096 µM 2908.0 [] unit_conversion 5.536405597812999 success True direct_binding ITC; Extended Data Table 1. 25 Enterobacter soli LF7 MarR_Es (7L19): KD1 = 2.908 ± 0.096 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7L19\7L19_metadata.json point structures/7L19/7l19_protein.pdb structures/7L19/7l19_pocket.pdb structures/7L19/7l19_ligand.sdf structures/7L19/7l19_ligand.pdb structures/7L19/7l19_ligand.cif structures/7L19/7l19_complex.pdb structures/7L19/7l19_complex.cif 7L1A classic Human Methionine Adenosyltransferase 2A Human Na Na 5'-Methylthioadenosine (MTA); PNPNP "[""XE1""]" 1 Ki Ki = = 0.12 ± 0.03 µM 120.0 [] unit_conversion 6.920818753952375 success True biochemical_inhibition MAT2A inhibition assay; Table 2 footnote states assays contained 1 mM methionine and 200 µM ATP. 7 Table 2 lists PNPNP with Ki = 0.12 ± 0.03 µM. The text identifies PNPNP as a diimidotriphosphate inhibitor of MAT2A. auto_single_measurement only accepted activity measurement [1] 1 structures\7L1A\7L1A_metadata.json point structures/7L1A/7l1a_protein.pdb structures/7L1A/7l1a_pocket.pdb structures/7L1A/7l1a_ligand.sdf structures/7L1A/7l1a_ligand.pdb structures/7L1A/7l1a_ligand.cif structures/7L1A/7l1a_complex.pdb structures/7L1A/7l1a_complex.cif 7L1I classic MarR_Ab Acinetobacter baumannii Na Na Indole-3-acetic acid (IAA) "[""IAC""]" 1 Kd Kd = = 1.293 ± 0.101 µM 1293.0 [] unit_conversion 5.888401475119606 success True direct_binding ITC; Extended Data Table 1. 25 Acinetobacter baumannii MarR_Ab (7L1I): KD1 = 1.293 ± 0.101 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7L1I\7L1I_metadata.json point structures/7L1I/7l1i_protein.pdb structures/7L1I/7l1i_pocket.pdb structures/7L1I/7l1i_ligand.sdf structures/7L1I/7l1i_ligand.pdb structures/7L1I/7l1i_ligand.cif structures/7L1I/7l1i_complex.pdb structures/7L1I/7l1i_complex.cif 7L1X classic human CK2alpha1 kinase catalytic subunit human CK2alpha1 catalytic domain, residues 3-339; expressed as a His6-SUMO fusion with the tag removed by Ulp1 protease Na 108600 "[""ON6""]" 1 IC50 IC50 = = 0.05 µM 50.0 [] unit_conversion 7.301029995663981 success True biochemical_inhibition In vitro kinase assay using recombinant CK2α1; IC50 values determined from substrate phosphorylation. 3 Fig. 1B lists the IC50 for 108600 inhibition of CK2α1 as 0.05 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7L1X\7L1X_metadata.json point structures/7L1X/7l1x_protein.pdb structures/7L1X/7l1x_pocket.pdb structures/7L1X/7l1x_ligand.sdf structures/7L1X/7l1x_ligand.pdb structures/7L1X/7l1x_ligand.cif structures/7L1X/7l1x_complex.pdb structures/7L1X/7l1x_complex.cif 7L24 classic HPK1 Na Na Na compound 11 "[""XHV""]" 1 IC50 IC50 = = 89 nM 89.0 [] unit_conversion 7.050609993355087 success True biochemical_inhibition HPK1 IC50 measured at [ATP] approximately Km[ATP]; Table 2 footnote states selectivity ratios are relative to HPK1 IC50. 2 Table 2 lists compound 11 with HPK1 IC50 of 89 nM. Figure 1 identifies the HPK1 co-crystal with compound 11 as PDB 7L24. auto_single_measurement only accepted activity measurement [1] 1 structures\7L24\7L24_metadata.json point structures/7L24/7l24_protein.pdb structures/7L24/7l24_pocket.pdb structures/7L24/7l24_ligand.sdf structures/7L24/7l24_ligand.pdb structures/7L24/7l24_ligand.cif structures/7L24/7l24_complex.pdb structures/7L24/7l24_complex.cif 7L25 classic HPK1 Na Na Na compound 18 "[""XHS""]" 1 IC50 IC50 = = 2.6 nM 2.6 [] unit_conversion 8.585026652029182 success True biochemical_inhibition HPK1 IC50 measured at [ATP] approximately Km[ATP]; Table 3 footnote states selectivity ratios are relative to HPK1 IC50. 3 Table 3 lists compound 18 with HPK1 IC50 of 2.6 nM. Figure 1 identifies the HPK1 co-crystal with compound 18 as PDB 7L25. auto_single_measurement only accepted activity measurement [1] 1 structures\7L25\7L25_metadata.json point structures/7L25/7l25_protein.pdb structures/7L25/7l25_pocket.pdb structures/7L25/7l25_ligand.sdf structures/7L25/7l25_ligand.pdb structures/7L25/7l25_ligand.cif structures/7L25/7l25_complex.pdb structures/7L25/7l25_complex.cif 7L26 classic HPK1 Na Na Na compound 38 "[""XHM""]" 1 IC50 IC50 = = 28 nM 28.0 [] unit_conversion 7.552841968657781 success True biochemical_inhibition HPK1 IC50 measured at [ATP] approximately Km[ATP]; Table 5 footnote states selectivity ratios are relative to HPK1 IC50. 6 Table 5 lists compound 38 with HPK1 IC50 of 28 nM. Figure 1 identifies the HPK1 co-crystal with compound 38 as PDB 7L26. auto_single_measurement only accepted activity measurement [1] 1 structures\7L26\7L26_metadata.json point structures/7L26/7l26_protein.pdb structures/7L26/7l26_pocket.pdb structures/7L26/7l26_ligand.sdf structures/7L26/7l26_ligand.pdb structures/7L26/7l26_ligand.cif structures/7L26/7l26_complex.pdb structures/7L26/7l26_complex.cif 7L4T classic human monoacylglycerol lipase human Na Na compound 1 "[""XPD""]" 1 IC50 IC50 = = 15 (9.9-22) nM 15.0 [] unit_conversion 7.823908740944319 success True biochemical_inhibition Inhibitory activity against human MAGL enzyme; IC50 with 95% confidence interval from duplicate measurements. 3 Table 1 lists compound 1: MAGL IC50 15 (9.9-22) nM; footnote identifies inhibitory activity against human MAGL enzyme. auto_single_measurement only accepted activity measurement [1] 1 structures\7L4T\7L4T_metadata.json point structures/7L4T/7l4t_protein.pdb structures/7L4T/7l4t_pocket.pdb structures/7L4T/7l4t_ligand.sdf structures/7L4T/7l4t_ligand.pdb structures/7L4T/7l4t_ligand.cif structures/7L4T/7l4t_complex.pdb structures/7L4T/7l4t_complex.cif 7L4U classic human monoacylglycerol lipase human Na Na compound 1h "[""XP7""]" 1 IC50 IC50 = = 38 (32-45) nM 38.0 [] unit_conversion 7.42021640338319 success True biochemical_inhibition Inhibitory activity against human MAGL enzyme; IC50 with 95% confidence interval from duplicate measurements. 5 Table 2 lists compound 1h: MAGL IC50 38 (32-45) nM; footnote identifies inhibitory activity against human MAGL enzyme. auto_single_measurement only accepted activity measurement [1] 1 structures\7L4U\7L4U_metadata.json point structures/7L4U/7l4u_protein.pdb structures/7L4U/7l4u_pocket.pdb structures/7L4U/7l4u_ligand.sdf structures/7L4U/7l4u_ligand.pdb structures/7L4U/7l4u_ligand.cif structures/7L4U/7l4u_complex.pdb structures/7L4U/7l4u_complex.cif 7L4W classic human monoacylglycerol lipase human Na Na compound 2d "[""XOV""]" 1 IC50 IC50 = = 3.4 (2.7-4.4) nM 3.4 [] unit_conversion 8.468521082957745 success True biochemical_inhibition Inhibitory activity against human MAGL enzyme; IC50 with 95% confidence interval from duplicate measurements. 5 Table 2 lists compound 2d: MAGL IC50 3.4 (2.7-4.4) nM; footnote identifies inhibitory activity against human MAGL enzyme. auto_single_measurement only accepted activity measurement [1] 1 structures\7L4W\7L4W_metadata.json point structures/7L4W/7l4w_protein.pdb structures/7L4W/7l4w_pocket.pdb structures/7L4W/7l4w_ligand.sdf structures/7L4W/7l4w_ligand.pdb structures/7L4W/7l4w_ligand.cif structures/7L4W/7l4w_complex.pdb structures/7L4W/7l4w_complex.cif 7L4Z extended SARS-CoV-2 spike receptor-binding domain (RBD) Na Na Na cyclic peptide 4 "[""CHAIN:R"", ""CHAIN:S"", ""CHAIN:T"", ""CHAIN:U"", ""CHAIN:V""]" 1 Kd Kd = = 15 nM 15.0 [] unit_conversion 7.823908740944319 success True direct_binding Surface plasmon resonance (SPR) binding of synthetic cyclic peptide 4 to SARS-CoV-2 spike RBD. 3 The paper states that the RBD–4 complex structure is PDB 7L4Z and Table 1 reports peptide 4 with K_D = 15 nM by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\7L4Z\7L4Z_metadata.json point structures/7L4Z/7l4z_protein.pdb structures/7L4Z/7l4z_pocket.pdb structures/7L4Z/7l4z_ligand.pdb structures/7L4Z/7l4z_ligand.cif structures/7L4Z/7l4z_complex.pdb structures/7L4Z/7l4z_complex.cif 7L50 classic human monoacylglycerol lipase human Na Na compound 4f "[""XOM""]" 2 Kd Kd = = 1.5 (±0.33) nM 1.5 [] unit_conversion 8.823908740944319 success True direct_binding Surface plasmon resonance (SPR) binding profile to human MAGL; values expressed as mean ± S.D. (n=6). 9 Table 5 reports the binding profile of 4f to MAGL, including KD 1.5 (±0.33) nM; the footnote states KD was derived from SPR experiments. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7L50\7L50_metadata.json point structures/7L50/7l50_protein.pdb structures/7L50/7l50_pocket.pdb structures/7L50/7l50_ligand.sdf structures/7L50/7l50_ligand.pdb structures/7L50/7l50_ligand.cif structures/7L50/7l50_complex.pdb structures/7L50/7l50_complex.cif 7L5C classic MEMO1 Na Na Na copper (Cu+) "[""CU1""]" 1 Kd Kd ~ ~ 3 × 10^-6 M 3000.0 [] unit_conversion 5.522878745280337 success True direct_binding Isothermal titration calorimetry of purified MEMO1 measuring copper(I) binding. 10 “Copper (I) binding was also detected by ITC, with an estimated Kd of about 3×10−6 M (Figure 5—figure supplement 3).” auto_single_measurement only accepted activity measurement [1] 1 structures\7L5C\7L5C_metadata.json point structures/7L5C/7l5c_protein.pdb structures/7L5C/7l5c_pocket.pdb structures/7L5C/7l5c_ligand.sdf structures/7L5C/7l5c_ligand.pdb structures/7L5C/7l5c_ligand.cif structures/7L5C/7l5c_complex.pdb structures/7L5C/7l5c_complex.cif 7L6X classic TAF1 human TAF1 tandem bromodomain, residues 1373-1635 Na GNE-371 "[""G9V""]" 1 Kd Kd = = 39 nM 39.0 [] unit_conversion 7.4089353929735005 success True direct_binding ITC study; monophasic binding profile. 7 The text states that the BD2-specific inhibitor GNE-371 showed a monophasic profile with TAF1-T, Kd = 39 nM and N = 1.1. auto_single_measurement only accepted activity measurement [1] 1 structures\7L6X\7L6X_metadata.json point structures/7L6X/7l6x_protein.pdb structures/7L6X/7l6x_pocket.pdb structures/7L6X/7l6x_ligand.sdf structures/7L6X/7l6x_ligand.pdb structures/7L6X/7l6x_ligand.cif structures/7L6X/7l6x_complex.pdb structures/7L6X/7l6x_complex.cif 7L7B classic Clostridioides difficile RNA polymerase (RNAP) Clostridioides difficile Na Na fidaxomicin "[""FI8""]" 1 IC50 IC50 = = 0.2 µM 200.0 [] unit_conversion 6.698970004336019 success True biochemical_inhibition in vitro IC50 4 SI Table 1 reports an in vitro IC50 of 0.2 µM for Fdx against C. difficile ('this study'). SI Table 2 identifies PDB 7L7B as Cdiff EσA + Fdx. auto_single_measurement only accepted activity measurement [1] 1 structures\7L7B\7L7B_metadata.json point structures/7L7B/7l7b_protein.pdb structures/7L7B/7l7b_pocket.pdb structures/7L7B/7l7b_ligand.sdf structures/7L7B/7l7b_ligand.pdb structures/7L7B/7l7b_ligand.cif structures/7L7B/7l7b_complex.pdb structures/7L7B/7l7b_complex.cif 7L7G classic eukaryotic translation initiation factor 2B (eIF2B) Homo sapiens Na Na ISRIB "[""C7B""]" 1 IC50 IC50 = = 37 nM 37.0 [] unit_conversion 7.431798275933005 success True direct_binding Fluorescence-polarization competition assay: FAM-ISRIB (2.5 nM) with 100 nM eIF2B(αβγδε)2 and varying ISRIB concentrations. 7 Figure 4 caption explicitly reports ISRIB IC50 = 37 nM (s.e.m. = 1 nM) in the FAM-ISRIB/eIF2B fluorescence-polarization assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7L7G\7L7G_metadata.json point structures/7L7G/7l7g_protein.pdb structures/7L7G/7l7g_pocket.pdb structures/7L7G/7l7g_ligand.sdf structures/7L7G/7l7g_ligand.pdb structures/7L7G/7l7g_ligand.cif structures/7L7G/7l7g_complex.pdb structures/7L7G/7l7g_complex.cif 7L99 classic BRDT bromodomain 2 Homo sapiens Recombinant BRDT bromodomain protein with an N-terminal 6-His tag Na CDD-1302 "[""XWJ""]" 2 Kd Kd = = 1.3 nM 1.3 [] unit_conversion 8.886056647693163 success True direct_binding BROMOscan bromodomain competition binding assay; binding constant shown for BRDT-BD2. 8 Figure 3 reports the BRDT-BD2 binding constant (Kd) for CDD-1302 as 1.3 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7L99\7L99_metadata.json point structures/7L99/7l99_protein.pdb structures/7L99/7l99_pocket.pdb structures/7L99/7l99_ligand.sdf structures/7L99/7l99_ligand.pdb structures/7L99/7l99_ligand.cif structures/7L99/7l99_complex.pdb structures/7L99/7l99_complex.cif 7L9A classic BRDT bromodomain 2 Homo sapiens Recombinant BRDT bromodomain protein with an N-terminal 6-His tag Na CDD-1102 "[""XWP""]" 2 Kd Kd = = 0.75 nM 0.75 [] unit_conversion 9.1249387366083 success True direct_binding BROMOscan bromodomain competition binding assay; binding constant shown for BRDT-BD2. 8 Figure 3 reports the BRDT-BD2 binding constant (Kd) for CDD-1102 as 0.75 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7L9A\7L9A_metadata.json point structures/7L9A/7l9a_protein.pdb structures/7L9A/7l9a_pocket.pdb structures/7L9A/7l9a_ligand.sdf structures/7L9A/7l9a_ligand.pdb structures/7L9A/7l9a_ligand.cif structures/7L9A/7l9a_complex.pdb structures/7L9A/7l9a_complex.cif 7L9F classic human ADP-ribosyl-acceptor hydrolase 3 (ARH3) human full-length ARH3 WT (wild type) ADP-ribose (ADPR) "[""AR6""]" 1 Kd Kd = = 7.81 ± 0.51 μM 7810.0 [] unit_conversion 5.1073489661227 success True direct_binding ITC measurement of ARH3WT binding to ADPR in the presence of Ca2+; Ca2+ condition corresponding to the ARH3–ADPR–Ca2+ structure. 3 Table 1 reports ARH3WT with Ca2+: KD 7.81 ± 0.51 μM; the surrounding text identifies this as ADPR binding measured by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7L9F\7L9F_metadata.json point structures/7L9F/7l9f_protein.pdb structures/7L9F/7l9f_pocket.pdb structures/7L9F/7l9f_ligand.sdf structures/7L9F/7l9f_ligand.pdb structures/7L9F/7l9f_ligand.cif structures/7L9F/7l9f_complex.pdb structures/7L9F/7l9f_complex.cif 7L9H classic human ADP-ribosyl-acceptor hydrolase 3 (ARH3) human Na D77A ADP-ribose (ADPR) "[""AR6""]" 1 Kd Kd = = 0.06 ± 0.01 μM 60.0 [] unit_conversion 7.221848749616356 success True direct_binding ITC measurement of ARH3D77A binding to ADPR in the presence of Mg2+; Mg2+ condition corresponding to the ARH3D77A–ADPR–Mg2+ structure. 3 Table 1 reports ARH3D77A with Mg2+: KD 0.06 ± 0.01 μM. Figure 5 also states that ADPR binds ARH3D77A with KD 0.06 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7L9H\7L9H_metadata.json point structures/7L9H/7l9h_protein.pdb structures/7L9H/7l9h_pocket.pdb structures/7L9H/7l9h_ligand.sdf structures/7L9H/7l9h_ligand.pdb structures/7L9H/7l9h_ligand.cif structures/7L9H/7l9h_complex.pdb structures/7L9H/7l9h_complex.cif 7L9I classic human ADP-ribosyl-acceptor hydrolase 3 (ARH3) human Na D314A ADP-ribose (ADPR) "[""AR6""]" 1 Kd Kd = = 62.89 ± 2.90 μM 62890.0 [] unit_conversion 4.201418405271452 success True direct_binding ITC measurement of ARH3D314A binding to ADPR in the presence of Mg2+; Mg2+ condition corresponding to the ARH3D314A–ADPR–Mg2+ structure. 3 Table 1 reports ARH3D314A with Mg2+: KD 62.89 ± 2.90 μM. Figure 5 states the same ADPR-binding KD for ARH3D314A. auto_single_measurement only accepted activity measurement [1] 1 structures\7L9I\7L9I_metadata.json point structures/7L9I/7l9i_protein.pdb structures/7L9I/7l9i_pocket.pdb structures/7L9I/7l9i_ligand.sdf structures/7L9I/7l9i_ligand.pdb structures/7L9I/7l9i_ligand.cif structures/7L9I/7l9i_complex.pdb structures/7L9I/7l9i_complex.cif 7L9M classic BRD4 human Na Na GXH-II-083 "[""XR4""]" 1 Kd Kd = = 4.0 ± 0.14 nM 4.0 [] unit_conversion 8.397940008672037 success True direct_binding Single qPCR BromoScan binding assay, duplicate (±SD). 3 Table 1 reports GXH-II-083 Kd for BRD4-1 as 4.0 ± 0.14 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7L9M\7L9M_metadata.json point structures/7L9M/7l9m_protein.pdb structures/7L9M/7l9m_pocket.pdb structures/7L9M/7l9m_ligand.sdf structures/7L9M/7l9m_ligand.pdb structures/7L9M/7l9m_ligand.cif structures/7L9M/7l9m_complex.pdb structures/7L9M/7l9m_complex.cif 7L9Y classic PARP14 (ARTD8) human catalytic fragment Na RBN012042 "[""XRM""]" 1 IC50 IC50 = = 18 nM 18.0 [] unit_conversion 7.7447274948966935 success True biochemical_inhibition Biochemical characterization of PARP14 inhibition. 2 “RBN012042 is a potent and selective inhibitor of PARP14 (IC50 = 18 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7L9Y\7L9Y_metadata.json point structures/7L9Y/7l9y_protein.pdb structures/7L9Y/7l9y_pocket.pdb structures/7L9Y/7l9y_ligand.sdf structures/7L9Y/7l9y_ligand.pdb structures/7L9Y/7l9y_ligand.cif structures/7L9Y/7l9y_complex.pdb structures/7L9Y/7l9y_complex.cif 7LA9 classic BRD4 human Na Na NC-III-49-1 "[""XR7""]" 1 Kd Kd = = 0.095 ± 0.036 nM 0.095 [] unit_conversion 10.022276394711152 success True direct_binding Single qPCR BromoScan binding assay, duplicate (±SD). 3 Table 1 reports NC-III-49-1 Kd for BRD4-1 as 0.095 ± 0.036 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7LA9\7LA9_metadata.json point structures/7LA9/7la9_protein.pdb structures/7LA9/7la9_pocket.pdb structures/7LA9/7la9_ligand.sdf structures/7LA9/7la9_ligand.pdb structures/7LA9/7la9_ligand.cif structures/7LA9/7la9_complex.pdb structures/7LA9/7la9_complex.cif 7LAD classic CYP3A5 human Truncated CYP3A5 with N-terminal deletion residues 3-22, C-terminal deletion residues 498-502, and a C-terminal 4x His-tag WT clobetasol propionate (CBZ) "[""XRD""]" 1 IC50 IC50 = = 0.32±0.06 μM 320.0 [] unit_conversion 6.494850021680094 success True biochemical_inhibition Purified-protein P450-Glo biochemical inhibition assay; Figure 5a. Values are means ± standard deviations from three experiments, each run in triplicate. 7 Figure 5a reports CBZ inhibition of CYP3A5 with IC50 0.32±0.06 μM; its caption identifies the P450-Glo biochemical assay. The methods specify purified human CYP3A5 and the truncated CYP3A5 construct used in this work. auto_single_measurement only accepted activity measurement [1] 1 structures\7LAD\7LAD_metadata.json point structures/7LAD/7lad_protein.pdb structures/7LAD/7lad_pocket.pdb structures/7LAD/7lad_ligand.sdf structures/7LAD/7lad_ligand.pdb structures/7LAD/7lad_ligand.cif structures/7LAD/7lad_complex.pdb structures/7LAD/7lad_complex.cif 7LAE classic myeloperoxidase subform C (MPO) Na Na Na Compound-4 "[""XRV""]" 1 IC50 IC50 = = 53 nM 53.0 [] unit_conversion 7.275724130399211 success True biochemical_inhibition MPO chlorination inhibition measured by AminoPhenyl Fluorescein (APF) assay. 3 Table 1 reports Compound 4 MPO APF IC50 = 53 nM; Fig. 3 maps Compound 4 to PDB 7LAE. auto_single_measurement only accepted activity measurement [1] 1 structures\7LAE\7LAE_metadata.json point structures/7LAE/7lae_protein.pdb structures/7LAE/7lae_pocket.pdb structures/7LAE/7lae_ligand.sdf structures/7LAE/7lae_ligand.pdb structures/7LAE/7lae_ligand.cif structures/7LAE/7lae_complex.pdb structures/7LAE/7lae_complex.cif 7LAG classic myeloperoxidase subform C (MPO) Na Na Na Compound-14 (7-({1-[(3-phenoxyphenyl)methyl]-1H-pyrazol-4-yl}methyl)-3H-[1,2,3]triazolo[4,5-b]pyridin-5-amine) "[""XSD""]" 1 IC50 IC50 = = 44 nM 44.0 [] unit_conversion 7.356547323513812 success True biochemical_inhibition MPO chlorination inhibition measured by AminoPhenyl Fluorescein (APF) assay. 3 Table 1 reports Compound 14 MPO APF IC50 = 44 nM; Fig. 4 maps Compound 14 to PDB 7LAG. auto_single_measurement only accepted activity measurement [1] 1 structures\7LAG\7LAG_metadata.json point structures/7LAG/7lag_protein.pdb structures/7LAG/7lag_pocket.pdb structures/7LAG/7lag_ligand.sdf structures/7LAG/7lag_ligand.pdb structures/7LAG/7lag_ligand.cif structures/7LAG/7lag_complex.pdb structures/7LAG/7lag_complex.cif 7LAL classic myeloperoxidase subform C (MPO) Na Na Na Compound-18 (7-(3-(2,3-dihydro-1H-inden-1-ylamino)-1-phenylpropyl)-1H-[1,2,3]triazolo[4,5-b]pyridin-5-amine) "[""XSG""]" 1 IC50 IC50 = = 58 nM 58.0 [] unit_conversion 7.236572006437063 success True biochemical_inhibition MPO chlorination inhibition measured by AminoPhenyl Fluorescein (APF) assay. 4 Fig. 4 labels Compound 18, PDB 7LAL, and APF IC50 = 58 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7LAL\7LAL_metadata.json point structures/7LAL/7lal_protein.pdb structures/7LAL/7lal_pocket.pdb structures/7LAL/7lal_ligand.sdf structures/7LAL/7lal_ligand.pdb structures/7LAL/7lal_ligand.cif structures/7LAL/7lal_complex.pdb structures/7LAL/7lal_complex.cif 7LAN classic myeloperoxidase subform C (MPO) Na Na Na Compound-30 "[""XS1""]" 1 IC50 IC50 = = 5 nM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition MPO chlorination inhibition measured by AminoPhenyl Fluorescein (APF) assay. 5 Table 2 reports Compound 30 MPO APF IC50 = 5 nM; Fig. 6 maps Compound 30 to PDB 7LAN. auto_single_measurement only accepted activity measurement [1] 1 structures\7LAN\7LAN_metadata.json point structures/7LAN/7lan_protein.pdb structures/7LAN/7lan_pocket.pdb structures/7LAN/7lan_ligand.sdf structures/7LAN/7lan_ligand.pdb structures/7LAN/7lan_ligand.cif structures/7LAN/7lan_complex.pdb structures/7LAN/7lan_complex.cif 7LBK extended human Survivin human hSurvivin expressed from p8HIS vector; 8His tag removed by overnight thrombin digestion wild-type histone H3 T3phK4me3 peptide "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 11.5 ± 1.0 μM 11500.0 [] unit_conversion 4.939302159646388 success True direct_binding Isothermal titration calorimetry at 25°C in pH 7.2 triple-component buffer. 2 Table 1 reports Kd = 11.5 ± 1.0 μM for H3T3phK4me3(1-12); the paper states these are thermodynamic parameters of interaction between hSurvivin and histone H3 peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7LBK\7LBK_metadata.json point structures/7LBK/7lbk_protein.pdb structures/7LBK/7lbk_pocket.pdb structures/7LBK/7lbk_ligand.pdb structures/7LBK/7lbk_ligand.cif structures/7LBK/7lbk_complex.pdb structures/7LBK/7lbk_complex.cif 7LBN extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Full-length SARS-CoV-2 Mpro, residues 1-306 Na MG-101 (Calpain inhibitor I) "[""CHAIN:D""]" 1 IC50 IC50 = = 2.89 ± 0.86 μM 2890.0 [] unit_conversion 5.539102157243452 success True biochemical_inhibition Purified Mpro fluorogenic FRET-based inhibition assay; n=3, mean ± SE. 11 Figure 8c explicitly reports Calpain inhibitor I (MG-101) IC50 = 2.89 ± 0.86 μM against Mpro; the caption identifies this as an in-vitro Mpro inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7LBN\7LBN_metadata.json point structures/7LBN/7lbn_protein.pdb structures/7LBN/7lbn_pocket.pdb structures/7LBN/7lbn_ligand.pdb structures/7LBN/7lbn_ligand.cif structures/7LBN/7lbn_complex.pdb structures/7LBN/7lbn_complex.cif 7LBO extended human Survivin human hSurvivin expressed from p8HIS vector; 8His tag removed by overnight thrombin digestion wild-type histone H3 T3phK4me1 peptide "[""CHAIN:C"", ""CHAIN:F""]" 1 Kd Kd = = 3.10 ± 0.14 μM 3100.0 [] unit_conversion 5.508638306165727 success True direct_binding Isothermal titration calorimetry at 25°C in pH 7.2 triple-component buffer. 2 Table 1 reports Kd = 3.10 ± 0.14 μM for H3T3phK4me1(1-12); the paper states these are thermodynamic parameters of interaction between hSurvivin and histone H3 peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7LBO\7LBO_metadata.json point structures/7LBO/7lbo_protein.pdb structures/7LBO/7lbo_pocket.pdb structures/7LBO/7lbo_ligand.pdb structures/7LBO/7lbo_ligand.cif structures/7LBO/7lbo_complex.pdb structures/7LBO/7lbo_complex.cif 7LBP extended human Survivin human hSurvivin expressed from p8HIS vector; 8His tag removed by overnight thrombin digestion wild-type histone H3 T3phK4ac peptide "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 15.4 ± 0.8 μM 15400.0 [] unit_conversion 4.812479279163537 success True direct_binding Isothermal titration calorimetry at 25°C in pH 7.2 triple-component buffer. 2 Table 1 reports Kd = 15.4 ± 0.8 μM for H3T3phK4ac(1-12); the paper states these are thermodynamic parameters of interaction between hSurvivin and histone H3 peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7LBP\7LBP_metadata.json point structures/7LBP/7lbp_protein.pdb structures/7LBP/7lbp_pocket.pdb structures/7LBP/7lbp_ligand.pdb structures/7LBP/7lbp_ligand.cif structures/7LBP/7lbp_complex.pdb structures/7LBP/7lbp_complex.cif 7LBQ extended human Survivin human hSurvivin expressed from p8HIS vector; 8His tag removed by overnight thrombin digestion wild-type histone H3 T3phK4me2 peptide "[""CHAIN:E""]" 1 Kd Kd = = 2.82 ± 0.16 μM 2820.0 [] unit_conversion 5.549750891680639 success True direct_binding Isothermal titration calorimetry at 25°C in pH 7.2 triple-component buffer. 2 Table 1 reports Kd = 2.82 ± 0.16 μM for H3T3phK4me2(1-12); the paper states these are thermodynamic parameters of interaction between hSurvivin and histone H3 peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7LBQ\7LBQ_metadata.json point structures/7LBQ/7lbq_protein.pdb structures/7LBQ/7lbq_pocket.pdb structures/7LBQ/7lbq_ligand.pdb structures/7LBQ/7lbq_ligand.cif structures/7LBQ/7lbq_complex.pdb structures/7LBQ/7lbq_complex.cif 7LBR classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 pp1ab residues 1564-1878, expressed with an N-terminal TEV-cleavable His-tag Na XR8-89 "[""XT7""]" 1 IC50 IC50 = = 0.113 ± 0.004 µM 113.0 [] unit_conversion 6.94692155651658 success True biochemical_inhibition PLpro primary enzyme-inhibition assay; Figure 4 dose-response. 5 Figure 4A prints “XR8-89 IC50 = 0.113 ± 0.004 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7LBR\7LBR_metadata.json point structures/7LBR/7lbr_protein.pdb structures/7LBR/7lbr_pocket.pdb structures/7LBR/7lbr_ligand.sdf structures/7LBR/7lbr_ligand.pdb structures/7LBR/7lbr_ligand.cif structures/7LBR/7lbr_complex.pdb structures/7LBR/7lbr_complex.cif 7LBS classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 pp1ab residues 1564-1878, expressed with an N-terminal TEV-cleavable His-tag Na XR8-24 "[""XR8""]" 1 IC50 IC50 = = 0.39 ± 0.05 µM 390.0 [] unit_conversion 6.4089353929735005 success True biochemical_inhibition PLpro primary enzyme-inhibition assay; Figure 4 dose-response. 5 Figure 4A prints “XR8-24 IC50 = 0.39 ± 0.05 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7LBS\7LBS_metadata.json point structures/7LBS/7lbs_protein.pdb structures/7LBS/7lbs_pocket.pdb structures/7LBS/7lbs_ligand.sdf structures/7LBS/7lbs_ligand.pdb structures/7LBS/7lbs_ligand.cif structures/7LBS/7lbs_complex.pdb structures/7LBS/7lbs_complex.cif 7LBV classic Propionibacterium acnes surface sialidase (PaNA) Propionibacterium acnes KPA171202 Residues 31-481; N-terminal His6-tagged PaNA construct Na Neu5Ac2en "[""DAN""]" 1 Ki Ki = = 120 ± 26 µM 120000.0 [] unit_conversion 3.920818753952375 success True biochemical_inhibition Competitive-inhibition kinetic analysis of PaNA using CF3MU-Neu5Ac substrate; the paper reports an estimated Ki for Neu5Ac2en. 3 “In comparison, Neu5Ac2en is a much weaker inhibitor of PaNA with an estimated Ki of (120 ± 26) µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7LBV\7LBV_metadata.json point structures/7LBV/7lbv_protein.pdb structures/7LBV/7lbv_pocket.pdb structures/7LBV/7lbv_ligand.sdf structures/7LBV/7lbv_ligand.pdb structures/7LBV/7lbv_ligand.cif structures/7LBV/7lbv_complex.pdb structures/7LBV/7lbv_complex.cif 7LCT classic SARS-CoV-2 Mpro SARS-CoV-2 Na Na 1g "[""XU4""]" 1 IC50 IC50 = = 0.27 ± 0.09 µM 270.0 [] unit_conversion 6.568636235841012 success True biochemical_inhibition FRET substrate–enzyme kinetic inhibition assay. 4 Table 1 lists 1g (PDB 7LCT) with IC50 0.27 ± 0.09 µM; the table identifies these as SARS-CoV-2 Mpro IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\7LCT\7LCT_metadata.json point structures/7LCT/7lct_protein.pdb structures/7LCT/7lct_pocket.pdb structures/7LCT/7lct_ligand.sdf structures/7LCT/7lct_ligand.pdb structures/7LCT/7lct_ligand.cif structures/7LCT/7lct_complex.pdb structures/7LCT/7lct_complex.cif 7LCZ classic Drosophila SARM1 Drosophila ARM domain, dSARM1ARM residues 307-678; crystal contained residues 370-678 after partial proteolysis Na NMN "[""NMN""]" 1 Kd Kd = = 6.39 ± 0.04 μM 6390.0 [] unit_conversion 5.1944991418416 success True direct_binding Isothermal titration calorimetry (ITC); direct binding at a 1:1 molar ratio. 7 “ITC ... measurements showed that NMN binds directly to dSARM1ARM at a 1:1 molar ratio, with a KD value of 6.39 ± 0.04 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7LCZ\7LCZ_metadata.json point structures/7LCZ/7lcz_protein.pdb structures/7LCZ/7lcz_pocket.pdb structures/7LCZ/7lcz_ligand.sdf structures/7LCZ/7lcz_ligand.pdb structures/7LCZ/7lcz_ligand.cif structures/7LCZ/7lcz_complex.pdb structures/7LCZ/7lcz_complex.cif 7LH7 classic BCL-XL Na Na Na A-1293102 "[""XZM""]" 2 Kd Kd = = 0.4 nM 0.4 [] unit_conversion 9.397940008672037 success True direct_binding Surface plasmon resonance (SPR) binding kinetics; Table 3. 3 Table 3 reports KD = 0.4 nM for A-1293102 binding to BCL-XL by SPR. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7LH7\7LH7_metadata.json point structures/7LH7/7lh7_protein.pdb structures/7LH7/7lh7_pocket.pdb structures/7LH7/7lh7_ligand.sdf structures/7LH7/7lh7_ligand.pdb structures/7LH7/7lh7_ligand.cif structures/7LH7/7lh7_complex.pdb structures/7LH7/7lh7_complex.cif 7LI9 classic serotonin transporter (SERT) human N- and C-terminally truncated SERT (DeltaN72, DeltaC13), in complex with 15B8 Fab Na 5-HT (serotonin, 5-hydroxytryptamine) "[""SRO""]" 1 Ki Ki = = 198 ± 36 μM 198000.0 [] unit_conversion 3.703334809738469 success True direct_binding Competition binding of 5-HT against [3H]ibogaine in 100 mM KCl, the substrate-release condition used for the inward-facing 5-HT–SERT structure. 5 The text reports a 5-HT Ki of 198 ± 36 μM in KCl and then describes the resulting 5-HT–SERT structure in these substrate-release conditions; Table 1 maps the 5-HT–SERT inward-KCl structure to PDB 7LI9. auto_single_measurement only accepted activity measurement [1] 1 structures\7LI9\7LI9_metadata.json point structures/7LI9/7li9_protein.pdb structures/7LI9/7li9_pocket.pdb structures/7LI9/7li9_ligand.sdf structures/7LI9/7li9_ligand.pdb structures/7LI9/7li9_ligand.cif structures/7LI9/7li9_complex.pdb structures/7LI9/7li9_complex.cif 7LIO extended SPOP Na SPOP MATH domain, residues 28-164, from an N-terminal His6-tagged pET construct with cleavable His6 tag S119D 53BP1 SBM synthetic peptide, residues 1636-1650 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 42.5 ± 4.4 µM 42500.0 [] unit_conversion 4.371611069949688 success True direct_binding Isothermal titration calorimetry (ITC) of SPOP MATH proteins and the 53BP1 peptide. 7 “SPOP MATH S119D had slightly higher affinity for the 53BP1 peptide than WT SPOP MATH with respective dissociation constants (Kds) of 42.5 ± 4.4 and 60.7 ± 8.1 μM determined using isothermal titration calorimetry (ITC).” auto_single_measurement only accepted activity measurement [1] 1 structures\7LIO\7LIO_metadata.json point structures/7LIO/7lio_protein.pdb structures/7LIO/7lio_pocket.pdb structures/7LIO/7lio_ligand.pdb structures/7LIO/7lio_ligand.cif structures/7LIO/7lio_complex.pdb structures/7LIO/7lio_complex.cif 7LJE classic p300 histone acetyltransferase Na Na Na compound 27 "[""Y2P""]" 1 IC50 IC50 = = 19 nM 19.0 [] unit_conversion 7.721246399047171 success True biochemical_inhibition p300 enzymatic inhibition; compound 27 (3R-F epimer). 4 Fig. 4 explicitly reports: “27: 3R-F epimer p300 IC50 = 19 nM.” The text identifies the X-ray crystal structure of compound 27 bound to p300 HAT, and page 6 links its coordinates to PDB 7LJE. auto_single_measurement only accepted activity measurement [1] 1 structures\7LJE\7LJE_metadata.json point structures/7LJE/7lje_protein.pdb structures/7LJE/7lje_pocket.pdb structures/7LJE/7lje_ligand.sdf structures/7LJE/7lje_ligand.pdb structures/7LJE/7lje_ligand.cif structures/7LJE/7lje_complex.pdb structures/7LJE/7lje_complex.cif 7LJS classic Porcine dihydropyrimidine dehydrogenase (DPD) Porcine Na Na 5-Ethynyluracil (5EU) "[""Y3G""]" 1 Kd Kd = = 9.5 ± 1.2 μM 9500.0 [] unit_conversion 5.022276394711152 success True direct_binding 5EU ligand-binding isotherm with DPD; measured in the absence of NADPH. 6 The text reports that the 5EU concentration-dependence of the 497 nm perturbation gave a DPD·5EU dissociation constant of 9.5 ± 1.2 μM; Figure 1 identifies this as a ligand-binding isotherm. auto_single_measurement only accepted activity measurement [1] 1 structures\7LJS\7LJS_metadata.json point structures/7LJS/7ljs_protein.pdb structures/7LJS/7ljs_pocket.pdb structures/7LJS/7ljs_ligand.sdf structures/7LJS/7ljs_ligand.pdb structures/7LJS/7ljs_ligand.cif structures/7LJS/7ljs_complex.pdb structures/7LJS/7ljs_complex.cif 7LKY extended PHF1 Tudor domain Na PHF1 Tudor domain, residues 28-87 Na UNC6641 "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L"", ""CHAIN:M"", ""CHAIN:N"", ""CHAIN:O"", ""CHAIN:P""]" 1 IC50 IC50 = = 1.6 ± 0.5 μM 1600.0 [] unit_conversion 5.795880017344075 success True biochemical_inhibition TR-FRET competitive/displacement assay; three technical replicates (mean ± SD), using 6×His-tagged PHF1 Tudor residues 28–87 and biotin-UNC6641 tracer. 3 Table 2 reports UNC6641 TR-FRET IC50 = 1.6 ± 0.5 μM; the methods specify PHF1 Tudor residues 28–87 for this assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7LKY\7LKY_metadata.json point structures/7LKY/7lky_protein.pdb structures/7LKY/7lky_pocket.pdb structures/7LKY/7lky_ligand.pdb structures/7LKY/7lky_ligand.cif structures/7LKY/7lky_complex.pdb structures/7LKY/7lky_complex.cif 7LM2 classic human PI3Kdelta human Na Na compound 3c (MSD-496486311) "[""Y5Y""]" 1 IC50 IC50 = = 1.2 nM 1.2 [] unit_conversion 8.920818753952375 success True biochemical_inhibition Figure 3 potency and selectivity table; PI3Kδ enzymatic inhibition. 7 Figure 3 lists PI3Kδ IC50 = 1.2 nM for compound 3c; the caption identifies 3c as MSD-496486311 and states its crystal structure with PI3Kδ is PDB ID 7LM2. auto_single_measurement only accepted activity measurement [1] 1 structures\7LM2\7LM2_metadata.json point structures/7LM2/7lm2_protein.pdb structures/7LM2/7lm2_pocket.pdb structures/7LM2/7lm2_ligand.sdf structures/7LM2/7lm2_ligand.pdb structures/7LM2/7lm2_ligand.cif structures/7LM2/7lm2_complex.pdb structures/7LM2/7lm2_complex.cif 7LMD classic SARS-CoV-2 3CLpro SARS-CoV-2 Na Na compound 19; 2-(benzotriazol-1-yl)-N-[4-(1H-pyrazol-4-yl)phenyl]-N-(3-thienylmethyl)acetamide "[""Y6A""]" 1 IC50 IC50 = = 0.270 ± 0.067 µM 270.0 [] unit_conversion 6.568636235841012 success True biochemical_inhibition SARS-CoV-2 3CLpro FRET biochemical inhibition assay (SC2). 7 Table 3 reports compound 19: SC2 3CLpro IC50 = 0.270 ± 0.067 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7LMD\7LMD_metadata.json point structures/7LMD/7lmd_protein.pdb structures/7LMD/7lmd_pocket.pdb structures/7LMD/7lmd_ligand.sdf structures/7LMD/7lmd_ligand.pdb structures/7LMD/7lmd_ligand.cif structures/7LMD/7lmd_complex.pdb structures/7LMD/7lmd_complex.cif 7LME classic SARS-CoV-2 3CLpro SARS-CoV-2 Na Na compound 1 (ML300); N-[4-[[2-(benzotriazol-1-yl)acetyl]-(3-thienylmethyl)amino]phenyl]cyclopropanecarboxamide "[""Y6J""]" 1 IC50 IC50 = = 4.99 ± 0.62 µM 4990.0 [] unit_conversion 5.30189945437661 success True biochemical_inhibition SARS-CoV-2 3CLpro FRET biochemical inhibition assay (SC2). 3 Table 1 reports compound 1 (ML300): SC2 3CLpro IC50 = 4.99 ± 0.62 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7LME\7LME_metadata.json point structures/7LME/7lme_protein.pdb structures/7LME/7lme_pocket.pdb structures/7LME/7lme_ligand.sdf structures/7LME/7lme_ligand.pdb structures/7LME/7lme_ligand.cif structures/7LME/7lme_complex.pdb structures/7LME/7lme_complex.cif 7LMG extended SARS-CoV-1 3CLpro SARS-CoV-1 Na Na compound 21; N-(4-(1H-imidazol-4-yl)phenyl)-2-(1H-benzo[d][1,2,3]triazol-1-yl)-N-(thiophen-3-ylmethyl)acetamide "[""Y6G""]" 1 IC50 IC50 = = 0.019 ± 0.005 µM 19.0 [] unit_conversion 7.721246399047171 success True biochemical_inhibition SARS-CoV-1 3CLpro FRET biochemical inhibition assay (SC1). 7 Table 3 reports compound 21: SC1 3CLpro IC50 = 0.019 ± 0.005 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7LMG\7LMG_metadata.json point structures/7LMG/7lmg_ligand.cif structures/7LMG/7lmg_complex.cif 7LMH extended SARS-CoV-1 3CLpro SARS-CoV-1 Na Na compound 8; 2-(1H-benzo[d][1,2,3]triazol-1-yl)-N-(4-(pyridin-3-yl)phenyl)-N-(thiophen-3-ylmethyl)acetamide "[""Y6D""]" 1 IC50 IC50 = = 0.93 ± 0.05 µM 930.0 [] unit_conversion 6.031517051446064 success True biochemical_inhibition SARS-CoV-1 3CLpro FRET biochemical inhibition assay (SC1). 3 Table 1 reports compound 8: SC1 3CLpro IC50 = 0.93 ± 0.05 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7LMH\7LMH_metadata.json point structures/7LMH/7lmh_ligand.sdf structures/7LMH/7lmh_ligand.cif structures/7LMH/7lmh_complex.cif 7LMI extended SARS-CoV-1 3CLpro SARS-CoV-1 Na Na compound 19; N-(4-(1H-pyrazol-4-yl)phenyl)-2-(1H-benzo[d][1,2,3]triazol-1-yl)-N-(thiophen-3-ylmethyl)acetamide "[""Y6A""]" 1 IC50 IC50 = = 0.109 ± 0.020 µM 109.0 [] unit_conversion 6.962573502059376 success True biochemical_inhibition SARS-CoV-1 3CLpro FRET biochemical inhibition assay (SC1). 7 Table 3 reports compound 19: SC1 3CLpro IC50 = 0.109 ± 0.020 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7LMI\7LMI_metadata.json point structures/7LMI/7lmi_ligand.cif structures/7LMI/7lmi_complex.cif 7LMJ extended SARS-CoV-1 3CLpro SARS-CoV-1 Na Na compound 35; 2-(benzotriazol-1-yl)-N-(3-chlorobenzyl)-N-[4-(2-oxo-1,2-dihydropyridin-3-yl)phenyl]acetamide "[""Y67""]" 1 IC50 IC50 = = 0.657 ± 0.405 µM 657.0 [] unit_conversion 6.18243463044022 success True biochemical_inhibition SARS-CoV-1 3CLpro FRET biochemical inhibition assay (SC1). 7 Table 3 reports compound 35: SC1 3CLpro IC50 = 0.657 ± 0.405 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7LMJ\7LMJ_metadata.json point structures/7LMJ/7lmj_ligand.sdf structures/7LMJ/7lmj_ligand.cif structures/7LMJ/7lmj_complex.cif 7LPW classic HIV-1 reverse transcriptase (RT) Human immunodeficiency virus type 1 Engineered HIV-1 RT clade B construct RT52A Na NBD-14189; compound 189 "[""YBA""]" 1 IC50 IC50 = = 1.5 ± 0.8 μM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition Anti-HIV RT enzyme inhibition; colorimetric Reverse Transcriptase Assay using recombinant HIV-1 RT. 2 Table 1 reports NBD-14189 IC50 = 1.5 ± 0.8 μM. The experimental section describes the RT inhibition assay with recombinant HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\7LPW\7LPW_metadata.json point structures/7LPW/7lpw_protein.pdb structures/7LPW/7lpw_pocket.pdb structures/7LPW/7lpw_ligand.sdf structures/7LPW/7lpw_ligand.pdb structures/7LPW/7lpw_ligand.cif structures/7LPW/7lpw_complex.pdb structures/7LPW/7lpw_complex.cif 7LPX classic HIV-1 reverse transcriptase (RT) Human immunodeficiency virus type 1 Engineered HIV-1 RT clade B construct RT52A Na NBD-14270; compound 270 "[""YB7""]" 1 IC50 IC50 = = 2.3 ± 0.6 μM 2300.0 [] unit_conversion 5.638272163982407 success True biochemical_inhibition Anti-HIV RT enzyme inhibition; colorimetric Reverse Transcriptase Assay using recombinant HIV-1 RT. 2 Table 1 reports NBD-14270 IC50 = 2.3 ± 0.6 μM. The experimental section describes the RT inhibition assay with recombinant HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\7LPX\7LPX_metadata.json point structures/7LPX/7lpx_protein.pdb structures/7LPX/7lpx_pocket.pdb structures/7LPX/7lpx_ligand.sdf structures/7LPX/7lpx_ligand.pdb structures/7LPX/7lpx_ligand.cif structures/7LPX/7lpx_complex.pdb structures/7LPX/7lpx_complex.cif 7LQ1 classic PI3K-delta human Na Na compound 28 "[""YA7""]" 1 IC50 IC50 = = 1.4 nM 1.4 [] unit_conversion 8.853871964321762 success True biochemical_inhibition PI3K isoform HTRF biochemical assay. 3 Table 5 lists compound 28 with PI3K-δ IC50 of 1.4 nM; the text states that potency was measured in an HTRF biochemical assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7LQ1\7LQ1_metadata.json point structures/7LQ1/7lq1_protein.pdb structures/7LQ1/7lq1_pocket.pdb structures/7LQ1/7lq1_ligand.sdf structures/7LQ1/7lq1_ligand.pdb structures/7LQ1/7lq1_ligand.cif structures/7LQ1/7lq1_complex.pdb structures/7LQ1/7lq1_complex.cif 7LQU classic HIV-1 reverse transcriptase (RT) Human immunodeficiency virus type 1 Engineered HIV-1 RT clade B construct RT52A Na NBD-14075; compound 075 "[""YBD""]" 1 IC50 IC50 = = 13.7 ± 1.4 μM 13700.0 [] unit_conversion 4.863279432843593 success True biochemical_inhibition Anti-HIV RT enzyme inhibition; colorimetric Reverse Transcriptase Assay using recombinant HIV-1 RT. 2 Table 1 reports NBD-14075 IC50 = 13.7 ± 1.4 μM. The experimental section describes the RT inhibition assay with recombinant HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\7LQU\7LQU_metadata.json point structures/7LQU/7lqu_protein.pdb structures/7LQU/7lqu_pocket.pdb structures/7LQU/7lqu_ligand.sdf structures/7LQU/7lqu_ligand.pdb structures/7LQU/7lqu_ligand.cif structures/7LQU/7lqu_complex.pdb structures/7LQU/7lqu_complex.cif 7LTG classic HDAC2 human Na Na apicidin (compound 1) "[""YED""]" 1 IC50 IC50 = = 0.009 µM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition HDAC2 enzymatic inhibition; Table 1 reports mean values from at least two assay measurements. 3 Table 1 lists apicidin (1), HDAC2 IC50 = 0.009 µM. The paper describes apicidin bound to human HDAC2 and maps compound 1 to PDB 7LTG. auto_single_measurement only accepted activity measurement [1] 1 structures\7LTG\7LTG_metadata.json point structures/7LTG/7ltg_protein.pdb structures/7LTG/7ltg_pocket.pdb structures/7LTG/7ltg_ligand.sdf structures/7LTG/7ltg_ligand.pdb structures/7LTG/7ltg_ligand.cif structures/7LTG/7ltg_complex.pdb structures/7LTG/7ltg_complex.cif 7LTJ classic SARS-CoV-2 main protease (3CL Mpro) SARS-CoV-2 Mpro (NSP5) cloned in pD451-SR, with an authentic N-terminus generated by NSP4-NSP5 autocleavage and a C-terminal HRV-3C cleavage site followed by His6-tag Na MCULE-5948770040 "[""YD1""]" 3 Ki Ki = = 2.9 µM 2900.0 [] unit_conversion 5.537602002101044 success True biochemical_inhibition FRET activity assay with 20–500 µM substrate and 0–25 µM inhibitor; competitive-inhibition regression. 6 “Initial rates measured at 20–500 μM substrate and 0–25 μM inhibitor were consistent with a competitive mechanism of inhibition with a Ki of 2.9 μM.” auto_metric_priority unique highest-priority metric family: Ki [3] 3 structures\7LTJ\7LTJ_metadata.json point structures/7LTJ/7ltj_protein.pdb structures/7LTJ/7ltj_pocket.pdb structures/7LTJ/7ltj_ligand.sdf structures/7LTJ/7ltj_ligand.pdb structures/7LTJ/7ltj_ligand.cif structures/7LTJ/7ltj_complex.pdb structures/7LTJ/7ltj_complex.cif 7LTR extended SonM alpha-N-methyltransferase Shewanella oneidensis MR-1 SonM with truncated SonA-BBD construct, residues 1-55 Na SonA-BBD "[""POLYMER_ENTITY:2""]" 1 Ki Ki = = 3.9 ± 0.5 µM 3900.0 [] unit_conversion 5.4089353929735005 success True biochemical_inhibition Inhibition data with saturating SAM and varying concentrations of SonA and SonA-BBD (Table 1). 5 Table 1 reports Ki = 3.9 ± 0.5 µM for wt under “Inhibition data: saturating SAM with varying concentrations of SonA and SonA-BBD”. auto_single_measurement only accepted activity measurement [1] 1 structures\7LTR\7LTR_metadata.json point structures/7LTR/7ltr_protein.pdb structures/7LTR/7ltr_pocket.pdb structures/7LTR/7ltr_ligand.pdb structures/7LTR/7ltr_ligand.cif structures/7LTR/7ltr_complex.pdb structures/7LTR/7ltr_complex.cif 7LTY classic Bruton's tyrosine kinase (BTK) human BTK residues 372-659 Na compound 23 "[""YD7""]" 1 IC50 IC50 = = 0.4 nM 0.4 [] unit_conversion 9.397940008672037 success True biochemical_inhibition BTK biochemical FRET inhibition assay; Table 3 reports the mean for n = 9. 5 Table 3 lists compound 23: “BTK IC50 (nM) 0.4 (n = 9)”. auto_single_measurement only accepted activity measurement [1] 1 structures\7LTY\7LTY_metadata.json point structures/7LTY/7lty_protein.pdb structures/7LTY/7lty_pocket.pdb structures/7LTY/7lty_ligand.sdf structures/7LTY/7lty_ligand.pdb structures/7LTY/7lty_ligand.cif structures/7LTY/7lty_complex.pdb structures/7LTY/7lty_complex.cif 7LTZ classic Bruton's tyrosine kinase (BTK) human BTK residues 372-659 Na compound 51 (BIB091) "[""YDA""]" 2 Kd Kd = = 0.07 nM 0.07 [] unit_conversion 10.154901959985743 success True direct_binding DiscoverX KINOMEscan kinase binding assay; Table 7. 11 Table 7 lists BTK for compound 51 with Kd = 0.07 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7LTZ\7LTZ_metadata.json point structures/7LTZ/7ltz_protein.pdb structures/7LTZ/7ltz_pocket.pdb structures/7LTZ/7ltz_ligand.sdf structures/7LTZ/7ltz_ligand.pdb structures/7LTZ/7ltz_ligand.cif structures/7LTZ/7ltz_complex.pdb structures/7LTZ/7ltz_complex.cif 7LU7 extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na NLG919' (NLG919 analog) "[""5PK""]" 1 IC50 IC50 = = 0.37±0.02 μM 370.0 [] unit_conversion 6.431798275933005 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports NLG919' IC50 = 0.37±0.02 μM and PDB 7LU7. auto_single_measurement only accepted activity measurement [1] 1 structures\7LU7\7LU7_metadata.json point structures/7LU7/7lu7_ligand.sdf structures/7LU7/7lu7_ligand.cif structures/7LU7/7lu7_complex.cif 7LUH classic Burkholderia pseudomallei disulfide bond-forming protein A (DsbA) Burkholderia pseudomallei Na Na bromophenoxy propanamide (fragment 1) "[""YCS""]" 1 Kd Kd > > 2 mM 2000000.0 [] unit_conversion 2.6989700043360187 success True direct_binding 2D [15N,1H]-HSQC NMR titration; chemical-shift perturbations did not reach saturation up to 2 mM fragment 1. 13 “The binding of fragments 1 and 2 to BpsDsbA is weak, with an NMR-estimated Kd of >2 mM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7LUH\7LUH_metadata.json point structures/7LUH/7luh_protein.pdb structures/7LUH/7luh_pocket.pdb structures/7LUH/7luh_ligand.sdf structures/7LUH/7luh_ligand.pdb structures/7LUH/7luh_ligand.cif structures/7LUH/7luh_complex.pdb structures/7LUH/7luh_complex.cif 7LUJ classic Burkholderia pseudomallei disulfide bond-forming protein A (DsbA) Burkholderia pseudomallei Na Na 4-methoxy-N-phenylbenzenesulfonamide (fragment 2) "[""YCY""]" 1 Kd Kd > > 2 mM 2000000.0 [] unit_conversion 2.6989700043360187 success True direct_binding 2D [15N,1H]-HSQC NMR titration; chemical-shift perturbations increased linearly and did not reach saturation in the tested concentration range. 13 “The binding of fragments 1 and 2 to BpsDsbA is weak, with an NMR-estimated Kd of >2 mM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7LUJ\7LUJ_metadata.json point structures/7LUJ/7luj_protein.pdb structures/7LUJ/7luj_pocket.pdb structures/7LUJ/7luj_ligand.sdf structures/7LUJ/7luj_ligand.pdb structures/7LUJ/7luj_ligand.cif structures/7LUJ/7luj_complex.pdb structures/7LUJ/7luj_complex.cif 7LUN classic PARP14 (ARTD8) human catalytic fragment Na RBN011980 "[""YFG""]" 1 IC50 IC50 < < 0.003 µM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Biochemical PARP14 catalytic-inhibitor assay. 3 “the PARP14 catalytic inhibitor RBN011980 (PDB ID: 7LUN), which has a biochemical IC50 < 0.003 µM against PARP14” auto_single_measurement only accepted activity measurement [1] 1 structures\7LUN\7LUN_metadata.json point structures/7LUN/7lun_protein.pdb structures/7LUN/7lun_pocket.pdb structures/7LUN/7lun_ligand.sdf structures/7LUN/7lun_ligand.pdb structures/7LUN/7lun_ligand.cif structures/7LUN/7lun_complex.pdb structures/7LUN/7lun_complex.cif 7LWB extended Rab8a GTPase; RILPL2 human Rab8a residues 1-181, Q67L, phosphorylated at T72, complexed with RILPL2 residues 117-165 Q67L GTP "[""CHAIN:D""]" 1 Kd Kd = = 0.54 ± 0.1 µM 540.0 [] unit_conversion 6.267606240177031 success True direct_binding Isothermal titration calorimetry of pRab8a into the extended RILPL2 RBD/RH2 peptide RL2^117 (residues 117–165); typical concentrations were 400–600 µM Rab8a and 40–60 µM RILPL2 variants. 7 Table 2 reports for pRab8a(Q67L), RL2^117: Kd = 0.54 ± 0.1 µM. Figure 3 caption identifies ITC titrations and the pRab8a:RILPL2^117 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7LWB\7LWB_metadata.json point structures/7LWB/7lwb_protein.pdb structures/7LWB/7lwb_pocket.pdb structures/7LWB/7lwb_ligand.pdb structures/7LWB/7lwb_ligand.cif structures/7LWB/7lwb_complex.pdb structures/7LWB/7lwb_complex.cif 7LWD classic human serotonin transporter (SERT) human N- and C-terminally truncated construct (DeltaN72/C13) wild-type vilazodone; imipramine "[""YG7""]" 1 Ki Ki = = 14.1 [11.8; 16.8] nM 14.1 [] unit_conversion 7.85078088734462 success True biochemical_inhibition Allosteric-potency determination from VLZ inhibition of [3H]imipramine dissociation from SERT WT membrane preparations; it measures the SERT:IMI:VLZ relationship represented by the structure. 4 Fig. 2 caption reports an allosteric potency Ki of 14.1 [11.8; 16.8] nM for [3H]IMI dissociation. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\7LWD\7LWD_metadata.json point structures/7LWD/7lwd_protein.pdb structures/7LWD/7lwd_pocket.pdb structures/7LWD/7lwd_ligand.sdf structures/7LWD/7lwd_ligand.pdb structures/7LWD/7lwd_ligand.cif structures/7LWD/7lwd_complex.pdb structures/7LWD/7lwd_complex.cif 7LWG classic BCL6 Na Na Na OICR-12694 "[""YN7""]" 1 Kd Kd = = 0.005 μM 5.0 [] unit_conversion 8.301029995663981 success True direct_binding Biacore SPR direct-binding assay; Table 6. 9 Table 6 reports compound 58 with Biacore SPR K_D = 0.005 μM. The text identifies 58 as OICR12694, and Figure 5 identifies a human BCL6-BTB dimer bound to 58 (OICR12694). auto_single_measurement only accepted activity measurement [1] 1 structures\7LWG\7LWG_metadata.json point structures/7LWG/7lwg_protein.pdb structures/7LWG/7lwg_pocket.pdb structures/7LWG/7lwg_ligand.sdf structures/7LWG/7lwg_ligand.pdb structures/7LWG/7lwg_ligand.cif structures/7LWG/7lwg_complex.pdb structures/7LWG/7lwg_complex.cif 7LZB classic SETD2 Na Na Na Compound 2 "[""YJ1""]" 1 IC50 IC50 = = 22.1 µM 22100.0 [] unit_conversion 4.655607726314889 success True biochemical_inhibition SETD2 biochemical assay; compound 2 was a confirmed screening hit. 1 “Hits 1 and 2 were confirmed in the SETD2 biochemical assay with IC50 values of 166 and 22.1 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7LZB\7LZB_metadata.json point structures/7LZB/7lzb_protein.pdb structures/7LZB/7lzb_pocket.pdb structures/7LZB/7lzb_ligand.sdf structures/7LZB/7lzb_ligand.pdb structures/7LZB/7lzb_ligand.cif structures/7LZB/7lzb_complex.pdb structures/7LZB/7lzb_complex.cif 7M0M classic HPK1 Na Na Na compound 27 (PDB component YK1) "[""YK1""]" 1 IC50 IC50 = = 0.25 nM 0.25 [] unit_conversion 9.602059991327963 success True biochemical_inhibition HPK1 TR-FRET biochemical inhibition assay. 6 Table 4 and Figure 7 report compound 27 HPK1 TR-FRET IC50 0.25 nM; Figure 6 maps compound 27 to PDB 7M0M. auto_single_measurement only accepted activity measurement [1] 1 structures\7M0M\7M0M_metadata.json point structures/7M0M/7m0m_protein.pdb structures/7M0M/7m0m_pocket.pdb structures/7M0M/7m0m_ligand.sdf structures/7M0M/7m0m_ligand.pdb structures/7M0M/7m0m_ligand.cif structures/7M0M/7m0m_complex.pdb structures/7M0M/7m0m_complex.cif 7M1Q classic ABCA4 Human Na Na N-ret-PE "[""HZL""]" 1 Kd Kd = = 1.7 ± 0.3 µM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding Substrate-binding assay measuring N-ret-PE by its absorption peak after ABCA4 was treated with varying all-trans-retinal concentrations in PE. 6 “WT ABCA4 displayed a substrate binding curve with an apparent Kd of 1.7 ± 0.3 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7M1Q\7M1Q_metadata.json point structures/7M1Q/7m1q_protein.pdb structures/7M1Q/7m1q_pocket.pdb structures/7M1Q/7m1q_ligand.sdf structures/7M1Q/7m1q_ligand.pdb structures/7M1Q/7m1q_ligand.cif structures/7M1Q/7m1q_complex.pdb structures/7M1Q/7m1q_complex.cif 7M2E classic BPTF Na Na Na CB02-092; compound 19 "[""YOV""]" 1 IC50 IC50 = = 0.17 μM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition BPTF AlphaScreen competitive binding assay; Table 4. 6 Table 4 reports compound 19 with BPTF AlphaScreen IC50 = 0.17 μM; Figure 3 maps compound 19 to PDB 7M2E. auto_single_measurement only accepted activity measurement [1] 1 structures\7M2E\7M2E_metadata.json point structures/7M2E/7m2e_protein.pdb structures/7M2E/7m2e_pocket.pdb structures/7M2E/7m2e_ligand.sdf structures/7M2E/7m2e_ligand.pdb structures/7M2E/7m2e_ligand.cif structures/7M2E/7m2e_complex.pdb structures/7M2E/7m2e_complex.cif 7M2K classic CDC34A Na Core catalytic domain CDC34A CAT, residues 7-184 Na 2ab "[""GZM""]" 1 IC50 IC50 = = 0.092 ± 0.0033 μM 92.0 [] unit_conversion 7.036212172654444 success True biochemical_inhibition Purified-protein, substrate-independent CDC34A-mediated poly-ubiquitin chain-formation assay; value reported in the comparison of TR-FRET EC50 and ubiquitination IC50 values. 8 Figure 5C reports for 2ab: “Ub IC50 0.092 ± 0.0033 μM”; the caption identifies this as inhibition of CDC34A-mediated in vitro ubiquitination and states IC50 values are mean ± variance (n = 2). auto_single_measurement only accepted activity measurement [1] 1 structures\7M2K\7M2K_metadata.json point structures/7M2K/7m2k_protein.pdb structures/7M2K/7m2k_pocket.pdb structures/7M2K/7m2k_ligand.sdf structures/7M2K/7m2k_ligand.pdb structures/7M2K/7m2k_ligand.cif structures/7M2K/7m2k_complex.pdb structures/7M2K/7m2k_complex.cif 7M2O classic Human glycolate oxidase (GO) human Na Na Compound 15 "[""YOJ""]" 1 IC50 IC50 = = 1.2 nM 1.2 [] unit_conversion 8.920818753952375 success True biochemical_inhibition Enzyme IC50 in the second-generation dual GO/LDHA inhibitor profile. 4 Table 2 reports Compound 15: GO IC50 = 1.2 nM. Page 5 identifies compound 15 in complex with GO as PDB 7M2O. auto_single_measurement only accepted activity measurement [1] 1 structures\7M2O\7M2O_metadata.json point structures/7M2O/7m2o_protein.pdb structures/7M2O/7m2o_pocket.pdb structures/7M2O/7m2o_ligand.sdf structures/7M2O/7m2o_ligand.pdb structures/7M2O/7m2o_ligand.cif structures/7M2O/7m2o_complex.pdb structures/7M2O/7m2o_complex.cif 7M2P extended SARS-CoV-2 3CL protease SARS-CoV-2 Na Na inhibitor 18; compound 18 "[""CHAIN:B""]" 1 Ki Ki = = 9 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition Purified 3CLpro inhibition; stated as an apparent titration result. 12 “Compound 18 was such a potent inhibitor of 3CLpro that its Ki* (9 nM) was a result of apparent titration of the enzyme.” auto_single_measurement only accepted activity measurement [1] 1 structures\7M2P\7M2P_metadata.json point structures/7M2P/7m2p_protein.pdb structures/7M2P/7m2p_pocket.pdb structures/7M2P/7m2p_ligand.pdb structures/7M2P/7m2p_ligand.cif structures/7M2P/7m2p_complex.pdb structures/7M2P/7m2p_complex.cif 7M3Y classic T-cell immunoglobulin and mucin domain-containing molecule 3 (TIM-3) human IgV domain, residues 22-130; tagless expression construct Na compound 22 "[""YQ7""]" 1 Ki Ki = = 4.9 ± 0.9 µM 4900.0 [] unit_conversion 5.309803919971486 success True direct_binding Fluorescence-polarization-anisotropy competition assay; displacement of fluorescent probe 23 from TIM-3. 5 Table 2 reports compound 22 FPA Ki = 4.9 ± 0.9 µM. Figure 3 maps compound 22 bound to TIM-3 to PDB 7M3Y. auto_single_measurement only accepted activity measurement [1] 1 structures\7M3Y\7M3Y_metadata.json point structures/7M3Y/7m3y_protein.pdb structures/7M3Y/7m3y_pocket.pdb structures/7M3Y/7m3y_ligand.sdf structures/7M3Y/7m3y_ligand.pdb structures/7M3Y/7m3y_ligand.cif structures/7M3Y/7m3y_complex.pdb structures/7M3Y/7m3y_complex.cif 7M41 classic T-cell immunoglobulin and mucin domain-containing molecule 3 (TIM-3) human IgV domain, residues 22-130; tagless expression construct Na compound 38 "[""YQG""]" 1 Ki Ki = = 70 ± 20 nM 70.0 [] unit_conversion 7.154901959985743 success True direct_binding Fluorescence-polarization-anisotropy competition assay using probe SP2. 6 Table 3 reports compound 38 FPA Ki = 70 ± 20 nM. Figure 7 maps compound 38 bound to TIM-3 to PDB 7M41. auto_single_measurement only accepted activity measurement [1] 1 structures\7M41\7M41_metadata.json point structures/7M41/7m41_protein.pdb structures/7M41/7m41_pocket.pdb structures/7M41/7m41_ligand.sdf structures/7M41/7m41_ligand.pdb structures/7M41/7m41_ligand.cif structures/7M41/7m41_complex.pdb structures/7M41/7m41_complex.cif 7M4R extended PALS1 (human cell junction protein) human PALS1-PSG domains, residues 236-675, with deletion between residues 411-460 Na Ec18, SARS-CoV-2 envelope protein C-terminal 18-amino-acid peptide "[""CHAIN:C""]" 1 Kd Kd = = 11.2 μM 11200.0 [] unit_conversion 4.950781977329818 success True direct_binding Microscale thermophoresis measurement of fluorescently labelled PSG titrated with Ec18. 2 “Using a microscale thermophoresis (MST) method… we determined the Kd at 11.2 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7M4R\7M4R_metadata.json point structures/7M4R/7m4r_protein.pdb structures/7M4R/7m4r_pocket.pdb structures/7M4R/7m4r_ligand.pdb structures/7M4R/7m4r_ligand.cif structures/7M4R/7m4r_complex.pdb structures/7M4R/7m4r_complex.cif 7M5L extended PCNA Na Na Na peptide 3 "[""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 0.769 ± 0.078 µM 769.0 [] unit_conversion 6.114073660198569 success True direct_binding Surface plasmon resonance (SPR) binding affinity. 4 Table 1 reports peptide 3 (Propyl (7)) affinity K_D ± SE = 0.769 ± 0.078 µM; the text maps peptide 3 co-crystal structure to PDB 7M5L. auto_single_measurement only accepted activity measurement [1] 1 structures\7M5L\7M5L_metadata.json point structures/7M5L/7m5l_protein.pdb structures/7M5L/7m5l_pocket.pdb structures/7M5L/7m5l_ligand.pdb structures/7M5L/7m5l_ligand.cif structures/7M5L/7m5l_complex.pdb structures/7M5L/7m5l_complex.cif 7M5M extended PCNA Na Na Na peptide 5 "[""CHAIN:D"", ""CHAIN:E""]" 1 Kd Kd = = 2.82 ± 0.080 µM 2820.0 [] unit_conversion 5.549750891680639 success True direct_binding Surface plasmon resonance (SPR) binding affinity. 4 Table 1 reports peptide 5 (trans-Butenyl (8)) affinity K_D ± SE = 2.82 ± 0.080 µM; the text maps peptide 5 co-crystal structure to PDB 7M5M. auto_single_measurement only accepted activity measurement [1] 1 structures\7M5M\7M5M_metadata.json point structures/7M5M/7m5m_protein.pdb structures/7M5M/7m5m_pocket.pdb structures/7M5M/7m5m_ligand.pdb structures/7M5M/7m5m_ligand.cif structures/7M5M/7m5m_complex.pdb structures/7M5M/7m5m_complex.cif 7M5U extended Human M-phase phosphoprotein 8 (MPP8) chromodomain human MPP8 chromodomain, residues 55-116, with an N-terminal His-tag Na UNC5246 "[""CHAIN:B""]" 1 Kd Kd = = 0.72 ± 0.05 μM 720.0 [] unit_conversion 6.142667503568731 success True direct_binding Isothermal titration calorimetry (ITC) of UNC5246 binding to MPP8 chromodomain. 3 “ITC, yielding a Kd of 0.72 ± 0.05 μM (Figure 1D).” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7M5U\7M5U_metadata.json point structures/7M5U/7m5u_protein.pdb structures/7M5U/7m5u_pocket.pdb structures/7M5U/7m5u_ligand.pdb structures/7M5U/7m5u_ligand.cif structures/7M5U/7m5u_complex.pdb structures/7M5U/7m5u_complex.cif 7M8M classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 11 "[""YSG""]" 1 IC50 IC50 = = 0.120 ± 0.016 µM 120.0 [] unit_conversion 6.920818753952375 success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; triplicate measurements. 6 Table 1 lists compound 11 IC50 as 0.120 ± 0.016 µM; the table note states activities were calculated from triplicate measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\7M8M\7M8M_metadata.json point structures/7M8M/7m8m_protein.pdb structures/7M8M/7m8m_pocket.pdb structures/7M8M/7m8m_ligand.sdf structures/7M8M/7m8m_ligand.pdb structures/7M8M/7m8m_ligand.cif structures/7M8M/7m8m_complex.pdb structures/7M8M/7m8m_complex.cif 7M8N classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 16 "[""YSP""]" 1 IC50 IC50 = = 0.100 ± 0.035 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; triplicate measurements. 6 Table 1 lists compound 16 IC50 as 0.100 ± 0.035 µM; the table note states activities were calculated from triplicate measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\7M8N\7M8N_metadata.json point structures/7M8N/7m8n_protein.pdb structures/7M8N/7m8n_pocket.pdb structures/7M8N/7m8n_ligand.sdf structures/7M8N/7m8n_ligand.pdb structures/7M8N/7m8n_ligand.cif structures/7M8N/7m8n_complex.pdb structures/7M8N/7m8n_complex.cif 7M8O classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 19 "[""YSM""]" 1 IC50 IC50 = = 0.037 ± 0.007 µM 37.0 [] unit_conversion 7.431798275933005 success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; triplicate measurements. 6 Table 1 lists compound 19 IC50 as 0.037 ± 0.007 µM; the table note states activities were calculated from triplicate measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\7M8O\7M8O_metadata.json point structures/7M8O/7m8o_protein.pdb structures/7M8O/7m8o_pocket.pdb structures/7M8O/7m8o_ligand.sdf structures/7M8O/7m8o_ligand.pdb structures/7M8O/7m8o_ligand.cif structures/7M8O/7m8o_complex.pdb structures/7M8O/7m8o_complex.cif 7M8P classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 23 "[""YSJ""]" 1 IC50 IC50 = = 0.020 ± 0.005 µM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; triplicate measurements. 6 Table 1 lists compound 23 IC50 as 0.020 ± 0.005 µM; the table note states activities were calculated from triplicate measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\7M8P\7M8P_metadata.json point structures/7M8P/7m8p_protein.pdb structures/7M8P/7m8p_pocket.pdb structures/7M8P/7m8p_ligand.sdf structures/7M8P/7m8p_ligand.pdb structures/7M8P/7m8p_ligand.cif structures/7M8P/7m8p_complex.pdb structures/7M8P/7m8p_complex.cif 7M8X classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 6 "[""YTJ""]" 1 IC50 IC50 = = 0.47 ± 0.02 µM 470.0 [] unit_conversion 6.327902142064282 success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; triplicate measurements. 6 Table 1 lists compound 6 IC50 as 0.47 ± 0.02 µM; the table note states activities were calculated from triplicate measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\7M8X\7M8X_metadata.json point structures/7M8X/7m8x_protein.pdb structures/7M8X/7m8x_pocket.pdb structures/7M8X/7m8x_ligand.sdf structures/7M8X/7m8x_ligand.pdb structures/7M8X/7m8x_ligand.cif structures/7M8X/7m8x_complex.pdb structures/7M8X/7m8x_complex.cif 7M8Y classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 15 "[""YTM""]" 1 IC50 IC50 = = 0.110 ± 0.013 µM 110.0 [] unit_conversion 6.958607314841775 success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; triplicate measurements. 6 Table 1 lists compound 15 IC50 as 0.110 ± 0.013 µM; the table note states activities were calculated from triplicate measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\7M8Y\7M8Y_metadata.json point structures/7M8Y/7m8y_protein.pdb structures/7M8Y/7m8y_pocket.pdb structures/7M8Y/7m8y_ligand.sdf structures/7M8Y/7m8y_ligand.pdb structures/7M8Y/7m8y_ligand.cif structures/7M8Y/7m8y_complex.pdb structures/7M8Y/7m8y_complex.cif 7M8Z classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 29 "[""YTV""]" 1 IC50 IC50 range range 0.25–0.50 µM 250.0 500.0 [] range_unit_conversion success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; inhibition did not reach a complete curve, reported as the concentration range reducing Mpro activity to 50%. 6 Table 1 lists compound 29 IC50 as 0.25–0.50 µM; the note explains that incomplete inhibition curves prevented calculation of IC50 and that this range reduced Mpro activity to 50%. auto_single_measurement only accepted activity measurement [1] 1 structures\7M8Z\7M8Z_metadata.json interval structures/7M8Z/7m8z_protein.pdb structures/7M8Z/7m8z_pocket.pdb structures/7M8Z/7m8z_ligand.sdf structures/7M8Z/7m8z_ligand.pdb structures/7M8Z/7m8z_ligand.cif structures/7M8Z/7m8z_complex.pdb structures/7M8Z/7m8z_complex.cif 7M90 classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 50 "[""YTS""]" 1 IC50 IC50 range range 0.25–0.50 µM 250.0 500.0 [] range_unit_conversion success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; inhibition did not reach a complete curve, reported as the concentration range reducing Mpro activity to 50%. 6 Table 1 lists compound 50 IC50 as 0.25–0.50 µM; the note explains that incomplete inhibition curves prevented calculation of IC50 and that this range reduced Mpro activity to 50%. auto_single_measurement only accepted activity measurement [1] 1 structures\7M90\7M90_metadata.json interval structures/7M90/7m90_protein.pdb structures/7M90/7m90_pocket.pdb structures/7M90/7m90_ligand.sdf structures/7M90/7m90_ligand.pdb structures/7M90/7m90_ligand.cif structures/7M90/7m90_complex.pdb structures/7M90/7m90_complex.cif 7M91 classic SARS-CoV-2 3CL main protease (Mpro) SARS-CoV-2 (2019-nCoV) Recombinant SARS-CoV-2 Mpro expressed from pGEX-6p-1 with a His6 tag and PreScission cleavage site Na Compound 25 "[""YU4""]" 1 IC50 IC50 = = 0.025 ± 0.003 µM 25.0 [] unit_conversion 7.6020599913279625 success True biochemical_inhibition Purified Mpro FRET-substrate inhibition assay; triplicate measurements. 6 Table 1 lists compound 25 IC50 as 0.025 ± 0.003 µM; the table note states activities were calculated from triplicate measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\7M91\7M91_metadata.json point structures/7M91/7m91_protein.pdb structures/7M91/7m91_pocket.pdb structures/7M91/7m91_ligand.sdf structures/7M91/7m91_ligand.pdb structures/7M91/7m91_ligand.cif structures/7M91/7m91_complex.pdb structures/7M91/7m91_complex.cif 7M98 extended ATAD2 bromodomain Na residues 966-1112 C1101A Na "[""CHAIN:B""]" 1 Kd Kd = = 15.9 ± 2.5 µM 15900.0 [] unit_conversion 4.798602875679548 success True direct_binding Isothermal titration calorimetry (ITC) of the longer ATAD2 BRD construct. 10 Table 3 reports KD from ITC of 15.9 ± 2.5 µM for H4K5acK8ac (res 1–10) binding to ATAD2 bromodomain residues 966–1112, C1101A. The adjacent text explicitly links this construct–ligand complex to PDB ID 7M98. auto_single_measurement only accepted activity measurement [1] 1 structures\7M98\7M98_metadata.json point structures/7M98/7m98_protein.pdb structures/7M98/7m98_pocket.pdb structures/7M98/7m98_ligand.pdb structures/7M98/7m98_ligand.cif structures/7M98/7m98_complex.pdb structures/7M98/7m98_complex.cif 7MCE classic BRD4 human Na Na compound 5; 2-{(7P)-7-(1,4-dimethyl-1H-1,2,3-triazol-5-yl)-8-fluoro-5-[(S)-(oxan-4-yl)(phenyl)methyl]-5H-pyrido[3,2-b]indol-3-yl}propan-2-ol "[""YWY""]" 1 IC50 IC50 = = 1.3 ± 0.7 nM 1.3 [] unit_conversion 8.886056647693163 success True direct_binding BRD4 binding IC50 ± SEM reported in Table 1; compound 5. 3 Table 1 reports for compound 5: BRD4 IC50 ± SEM (nM) = 1.3 ± 0.7 (2). The Figure 4 caption identifies compound 5 bound to BRD4 (BD1), deposited as PDB 7MCE. auto_single_measurement only accepted activity measurement [1] 1 structures\7MCE\7MCE_metadata.json point structures/7MCE/7mce_protein.pdb structures/7MCE/7mce_pocket.pdb structures/7MCE/7mce_ligand.sdf structures/7MCE/7mce_ligand.pdb structures/7MCE/7mce_ligand.cif structures/7MCE/7mce_complex.pdb structures/7MCE/7mce_complex.cif 7MCF classic human BRD4 human first bromodomain of BRD4 Na compound 12; 2-{3-(1,4-dimethyl-1H-1,2,3-triazol-5-yl)-6-fluoro-5-[(S)-(3-fluoropyridin-2-yl)(oxan-4-yl)methyl]-5H-pyrido[3,2-b]indol-7-yl}propan-2-ol "[""YX4""]" 1 IC50 IC50 = = 0.6 ± 0.3 (4) nM 0.6 [] unit_conversion 9.221848749616356 success True direct_binding BRD4 binding assay; Table 1 reports BRD4 IC50 ± SEM. 3 Table 1 lists compound 12 with BRD4 IC50 = 0.6 ± 0.3 nM (4). The text identifies the BRD4 assay as a binding assay, and Fig. 3 identifies BRD4 domain 1 bound to compound 12. auto_single_measurement only accepted activity measurement [1] 1 structures\7MCF\7MCF_metadata.json point structures/7MCF/7mcf_protein.pdb structures/7MCF/7mcf_pocket.pdb structures/7MCF/7mcf_ligand.sdf structures/7MCF/7mcf_ligand.pdb structures/7MCF/7mcf_ligand.cif structures/7MCF/7mcf_complex.pdb structures/7MCF/7mcf_complex.cif 7MCK classic CHK1-LRRK2 chimera Na CHK1-LRRK2 chimera 10-point mutant compound 18 "[""YXD""]" 1 IC50 IC50 = = 17 (0.31) nM 17.0 [] unit_conversion 7.769551078621726 success True biochemical_inhibition LRRK2 IC50 (LBE), reported in Table 6 for compound 18. 6 Table 6 reports for compound 18: “LRRK2 IC50 (LBE) 17 (0.31)” nM. The main text identifies PDB 7MCK as an X-ray structure of compound 18 with a CHK1-LRRK2 chimera described as a 10-point mutant. auto_single_measurement only accepted activity measurement [1] 1 structures\7MCK\7MCK_metadata.json point structures/7MCK/7mck_protein.pdb structures/7MCK/7mck_pocket.pdb structures/7MCK/7mck_ligand.sdf structures/7MCK/7mck_ligand.pdb structures/7MCK/7mck_ligand.cif structures/7MCK/7mck_complex.pdb structures/7MCK/7mck_complex.cif 7MDS classic AtDHDPS1 Arabidopsis thaliana Na Na MBDTA-2 "[""YXP""]" 1 IC50 IC50 = = 63.3 ± 1.80 μM 63300.0 [] unit_conversion 4.198596289982645 success True biochemical_inhibition DHDPS–DHDPR coupled assay using recombinant A. thaliana DHDPS1; dose-response titration with substrates fixed at previously determined Michaelis–Menten constant values. 4 “The IC50 values of MBDTA-1 and MBDTA-2 against AtDHDPS1 were 126 ± 6.50 μM and 63.3 ± 1.80 μM, respectively.” The paper identifies 7MDS as the structure of MBDTA-2 bound to AtDHDPS1. auto_single_measurement only accepted activity measurement [1] 1 structures\7MDS\7MDS_metadata.json point structures/7MDS/7mds_protein.pdb structures/7MDS/7mds_pocket.pdb structures/7MDS/7mds_ligand.sdf structures/7MDS/7mds_ligand.pdb structures/7MDS/7mds_ligand.cif structures/7MDS/7mds_complex.pdb structures/7MDS/7mds_complex.cif 7MER classic mouse ALDH4A1 (MmALDH4A1) mouse Na Na trans-4-hydroxy-L-proline (THLP) "[""HYP""]" 1 Ki Ki = = 0.7 ± 0.1 mM 700000.0 [] unit_conversion 3.154901959985743 success True biochemical_inhibition Competitive steady-state inhibition; L-P5C variable substrate and NAD+ fixed at 1 mM. 4 Table 1 reports THLP as competitive with Ki = 0.7 ± 0.1 mM. The text identifies the THLP complex as MmALDH4A1 and maps THLP to PDB 7MER. auto_single_measurement only accepted activity measurement [1] 1 structures\7MER\7MER_metadata.json point structures/7MER/7mer_protein.pdb structures/7MER/7mer_pocket.pdb structures/7MER/7mer_ligand.sdf structures/7MER/7mer_ligand.pdb structures/7MER/7mer_ligand.cif structures/7MER/7mer_complex.pdb structures/7MER/7mer_complex.cif 7MES classic mouse ALDH4A1 (MmALDH4A1) mouse Na Na trans-4-hydroxy-D-proline (THDP) "[""UY7""]" 1 Ki Ki = = 9 ± 1 mM 9000000.0 [] unit_conversion 2.045757490560675 success True biochemical_inhibition Uncompetitive steady-state inhibition; L-P5C variable substrate and NAD+ fixed at 1 mM. 4 Table 1 reports THDP as uncompetitive with Ki = 9 ± 1 mM. Table 2 maps the THDP + NAD+ structure to PDB 7MES. auto_single_measurement only accepted activity measurement [1] 1 structures\7MES\7MES_metadata.json point structures/7MES/7mes_protein.pdb structures/7MES/7mes_pocket.pdb structures/7MES/7mes_ligand.sdf structures/7MES/7mes_ligand.pdb structures/7MES/7mes_ligand.cif structures/7MES/7mes_complex.pdb structures/7MES/7mes_complex.cif 7MF0 extended PERK Na Na Na (R)-2-amino-N-cyclopropyl-5-(4-(2-(3,5-difluorophenyl)-2-hydroxyacetamido)-2-methylphenyl)nicotinamide; compound 20 "[""Z6P""]" 1 IC50 IC50 = = 0.003 µM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition PERK biochemical assay measuring direct inhibition of recombinant PERK protein phosphorylation of eIF2α; Table 1 in vitro data. 3 Table 1 reports compound 20 PERK IC50 = 0.003 µM. The text describes the PERK biochemical assay as measuring direct effects on recombinant PERK phosphorylation of eIF2α. auto_single_measurement only accepted activity measurement [1] 1 structures\7MF0\7MF0_metadata.json point structures/7MF0/7mf0_ligand.sdf structures/7MF0/7mf0_ligand.cif structures/7MF0/7mf0_complex.cif 7MFH classic Autotaxin mouse Na Na BIO-32546; compound 6 "[""ZF7""]" 1 IC50 IC50 = = 1 nM 1.0 [] unit_conversion 9.0 success True biochemical_inhibition ATX FRET assay 1 Figure 2 labels compound 6 (BIO-32546) “ATX FRET IC50 = 1 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7MFH\7MFH_metadata.json point structures/7MFH/7mfh_protein.pdb structures/7MFH/7mfh_pocket.pdb structures/7MFH/7mfh_ligand.sdf structures/7MFH/7mfh_ligand.pdb structures/7MFH/7mfh_ligand.cif structures/7MFH/7mfh_complex.pdb structures/7MFH/7mfh_complex.cif 7MGJ classic TNNI3K Na TNNI3K residues 402-730 Na compound 2; N-methyl-4-(4-(3-(3-(trifluoromethyl)phenyl)ureido)phenoxy)picolinamide "[""ZFS""]" 1 IC50 IC50 = = 79 nM 79.0 [] unit_conversion 7.102372908709558 success True direct_binding TNNI3K fluorescence-polarization binding assay; at least two experiments. 3 Table 1 reports compound 2 with TNNI3K IC50 of 79 nM; the table footnote identifies a TNNI3K FP binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7MGJ\7MGJ_metadata.json point structures/7MGJ/7mgj_protein.pdb structures/7MGJ/7mgj_pocket.pdb structures/7MGJ/7mgj_ligand.sdf structures/7MGJ/7mgj_ligand.pdb structures/7MGJ/7mgj_ligand.cif structures/7MGJ/7mgj_complex.pdb structures/7MGJ/7mgj_complex.cif 7MGK classic TNNI3K Na TNNI3K residues 421-730 Na compound 47; 1-(3,5-dichloro-4-((6-(methylamino)pyrimidin-4-yl)oxy)phenyl)-3-(3-(trifluoromethyl)phenyl)urea "[""ZGD""]" 2 Ki Ki = = 0.54 nM 0.54 [] unit_conversion 9.267606240177031 success True direct_binding Stopped-flow competitive binding kinetics; Ki calculated from fitted association and dissociation rates. 8 The text states that stopped-flow kinetic experiments established a Ki of 0.54 nM for compound 47 against human TNNI3K. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7MGK\7MGK_metadata.json point structures/7MGK/7mgk_protein.pdb structures/7MGK/7mgk_pocket.pdb structures/7MGK/7mgk_ligand.sdf structures/7MGK/7mgk_ligand.pdb structures/7MGK/7mgk_ligand.cif structures/7MGK/7mgk_complex.pdb structures/7MGK/7mgk_complex.cif 7MJ5 extended human thrombin human Na Na XC-43 "[""CHAIN:A"", ""CHAIN:N"", ""CHAIN:O"", ""CHAIN:P"", ""CHAIN:Q"", ""CHAIN:R""]" 3 Kd Kd = = 3.0 × 10^-12 M 0.003 [] unit_conversion 11.522878745280337 success True direct_binding Surface plasmon resonance measurement of thrombin binding to biotinylated XC-43 immobilized on a plasmon resonance surface. 2 “measurement of thrombin binding to a biotinylated XC-43-bound plasmon resonance surface (SPR) produced a dissociation constant (KD) of 3.0 × 10^-12 M.” auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\7MJ5\7MJ5_metadata.json point structures/7MJ5/7mj5_protein.pdb structures/7MJ5/7mj5_pocket.pdb structures/7MJ5/7mj5_ligand.pdb structures/7MJ5/7mj5_ligand.cif structures/7MJ5/7mj5_complex.pdb structures/7MJ5/7mj5_complex.cif 7MLD classic PYL10 Na Na Na antabactin "[""ZLG""]" 1 Kd Kd = = 1700 pM 1.7 [] unit_conversion 8.769551078621726 success True direct_binding Fluorescence-polarization equilibrium binding measurement using TAMRA–ANT; PYL10 Kd reported in Fig. 4B. 4 “PYR1 Kd = 1,700 pM; PYL5 Kd = 400 pM; PYL8 Kd = 470 pM” (Fig. 4B), where the first plotted receptor is PYL10 despite the apparent text-label inconsistency in the adjacent paragraph. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7MLD\7MLD_metadata.json point structures/7MLD/7mld_protein.pdb structures/7MLD/7mld_pocket.pdb structures/7MLD/7mld_ligand.sdf structures/7MLD/7mld_ligand.pdb structures/7MLD/7mld_ligand.cif structures/7MLD/7mld_complex.pdb structures/7MLD/7mld_complex.cif 7MLN classic ricin A chain Na Na Na RU-NT-70; 5-(o-tolyl)thiophene-2-carboxylic acid "[""ZJA""]" 1 Kd Kd = = 372 ± 34 µM 372000.0 [] unit_conversion 3.4294570601181027 success True direct_binding Biacore 8K surface plasmon resonance measurement of RU-NT-70 binding to immobilized RTA. 4 Table 1 reports RU-NT-70 K_D = 372 ± 34 µM; affinities were determined by steady-state fitting with the free R_max model. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7MLN\7MLN_metadata.json point structures/7MLN/7mln_protein.pdb structures/7MLN/7mln_pocket.pdb structures/7MLN/7mln_ligand.sdf structures/7MLN/7mln_ligand.pdb structures/7MLN/7mln_ligand.cif structures/7MLN/7mln_complex.pdb structures/7MLN/7mln_complex.cif 7MLO classic ricin A chain Na Na Na RU-NT-75; 5-mesitylthiophene-2-carboxylic acid "[""ZJ7""]" 1 Kd Kd = = 319 ± 9 µM 319000.0 [] unit_conversion 3.496209316942819 success True direct_binding Biacore 8K surface plasmon resonance measurement of RU-NT-75 binding to immobilized RTA. 4 Table 1 reports RU-NT-75 K_D = 319 ± 9 µM. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7MLO\7MLO_metadata.json point structures/7MLO/7mlo_protein.pdb structures/7MLO/7mlo_pocket.pdb structures/7MLO/7mlo_ligand.sdf structures/7MLO/7mlo_ligand.pdb structures/7MLO/7mlo_ligand.cif structures/7MLO/7mlo_complex.pdb structures/7MLO/7mlo_complex.cif 7MLP classic ricin A chain Na Na Na RU-NT-93; 5-(2,6-dimethylphenyl)thiophene-2-carboxylic acid "[""ZJ4""]" 1 Kd Kd = = 130 ± 6 µM 130000.0 [] unit_conversion 3.886056647693163 success True direct_binding Biacore 8K surface plasmon resonance measurement of RU-NT-93 binding to immobilized RTA. 4 Table 1 reports RU-NT-93 K_D = 130 ± 6 µM. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7MLP\7MLP_metadata.json point structures/7MLP/7mlp_protein.pdb structures/7MLP/7mlp_pocket.pdb structures/7MLP/7mlp_ligand.sdf structures/7MLP/7mlp_ligand.pdb structures/7MLP/7mlp_ligand.cif structures/7MLP/7mlp_complex.pdb structures/7MLP/7mlp_complex.cif 7MLQ classic human BRD4 human BRD4(D1) Na compound 26; 2-(4-{5-[6-(2,5-dibromophenoxy)pyridin-2-yl]-4-methyl-1H-1,2,3-triazol-1-yl}piperidin-1-yl)-N,N-dimethylethan-1-amine "[""ZHV""]" 2 Kd Kd = = 6.4 nM 6.4 [] unit_conversion 8.193820026016112 success True direct_binding DiscoverX binding assay 5 Figure 4A table reports BRD4 D1 Kd for compound 26 as 6.4 nM; the footnote states Kd values were determined by DiscoverX. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7MLQ\7MLQ_metadata.json point structures/7MLQ/7mlq_protein.pdb structures/7MLQ/7mlq_pocket.pdb structures/7MLQ/7mlq_ligand.sdf structures/7MLQ/7mlq_ligand.pdb structures/7MLQ/7mlq_ligand.cif structures/7MLQ/7mlq_complex.pdb structures/7MLQ/7mlq_complex.cif 7MLR classic human BRD4 human BRD4(D1) Na DW34; 2-(4-{5-[6-(3,5-dimethylphenoxy)pyridin-2-yl]-4-methyl-1H-1,2,3-triazol-1-yl}piperidin-1-yl)-N,N-dimethylethan-1-amine "[""ZHS""]" 2 Kd Kd = = 12 nM 12.0 [] unit_conversion 7.920818753952375 success True direct_binding DiscoverX binding assay 5 Figure 4A table reports BRD4 D1 Kd for DW34 as 12 nM; the footnote states Kd values were determined by DiscoverX. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7MLR\7MLR_metadata.json point structures/7MLR/7mlr_protein.pdb structures/7MLR/7mlr_pocket.pdb structures/7MLR/7mlr_ligand.sdf structures/7MLR/7mlr_ligand.pdb structures/7MLR/7mlr_ligand.cif structures/7MLR/7mlr_complex.pdb structures/7MLR/7mlr_complex.cif 7MLS classic human BRD4 human BRD4(D1) Na compound 23; 2-(2,5-dibromophenoxy)-6-[4-methyl-1-(piperidin-4-yl)-1H-1,2,3-triazol-5-yl]pyridine "[""ZHM""]" 1 IC50 IC50 = = 0.790 ± 0.03 μM 790.0 [] unit_conversion 6.102372908709558 success True direct_binding Fluorescence anisotropy (FA) 4 Table 3 reports BRD4 D1 IC50 for compound 23 as 0.790 ± 0.03 μM; its footnote states IC50 values were determined by FA. auto_single_measurement only accepted activity measurement [1] 1 structures\7MLS\7MLS_metadata.json point structures/7MLS/7mls_protein.pdb structures/7MLS/7mls_pocket.pdb structures/7MLS/7mls_ligand.sdf structures/7MLS/7mls_ligand.pdb structures/7MLS/7mls_ligand.cif structures/7MLS/7mls_complex.pdb structures/7MLS/7mls_complex.cif 7MLT classic ricin A chain Na Na Na RU-NT-102; 5-(2-ethylphenyl)thiophene-2-carboxylic acid "[""ZJD""]" 1 Kd Kd = = 306 ± 22 µM 306000.0 [] unit_conversion 3.5142785735184203 success True direct_binding Biacore 8K surface plasmon resonance measurement of RU-NT-102 binding to immobilized RTA. 4 Table 1 reports RU-NT-102 K_D = 306 ± 22 µM. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7MLT\7MLT_metadata.json point structures/7MLT/7mlt_protein.pdb structures/7MLT/7mlt_pocket.pdb structures/7MLT/7mlt_ligand.sdf structures/7MLT/7mlt_ligand.pdb structures/7MLT/7mlt_ligand.cif structures/7MLT/7mlt_complex.pdb structures/7MLT/7mlt_complex.cif 7MOS classic HDAC2 Na Na Na compound 4 "[""ZLV""]" 1 IC50 IC50 = = 911 nM 911.0 [] unit_conversion 6.040481623027002 success True biochemical_inhibition HDAC enzymatic potency assay; Table 1. 5 Table 1 reports compound 4 HDAC2 IC50 = 911 nM; Figure 2 maps compound 4 bound to HDAC2 to PDB 7MOS. auto_single_measurement only accepted activity measurement [1] 1 structures\7MOS\7MOS_metadata.json point structures/7MOS/7mos_protein.pdb structures/7MOS/7mos_pocket.pdb structures/7MOS/7mos_ligand.sdf structures/7MOS/7mos_ligand.pdb structures/7MOS/7mos_ligand.cif structures/7MOS/7mos_complex.pdb structures/7MOS/7mos_complex.cif 7MOT classic HDAC2 Na Na Na compound 9 "[""V1P""]" 1 IC50 IC50 = = 18 nM 18.0 [] unit_conversion 7.7447274948966935 success True biochemical_inhibition HDAC enzymatic potency assay; Table 2. 6 Table 2 reports compound 9 HDAC2 IC50 = 18 nM; Figure 3 maps compound 9 bound to HDAC2 to PDB 7MOT. auto_single_measurement only accepted activity measurement [1] 1 structures\7MOT\7MOT_metadata.json point structures/7MOT/7mot_protein.pdb structures/7MOT/7mot_pocket.pdb structures/7MOT/7mot_ligand.sdf structures/7MOT/7mot_ligand.pdb structures/7MOT/7mot_ligand.cif structures/7MOT/7mot_complex.pdb structures/7MOT/7mot_complex.cif 7MOX classic HDAC2 Na Na Na compound 14 "[""ZLS""]" 1 IC50 IC50 = = 36 nM 36.0 [] unit_conversion 7.443697499232712 success True biochemical_inhibition HDAC enzymatic potency assay; Table 3. 7 Table 3 reports compound 14 HDAC2 IC50 = 36 nM; Figure 4 maps compound 14 bound to HDAC2 to PDB 7MOX. auto_single_measurement only accepted activity measurement [1] 1 structures\7MOX\7MOX_metadata.json point structures/7MOX/7mox_protein.pdb structures/7MOX/7mox_pocket.pdb structures/7MOX/7mox_ligand.sdf structures/7MOX/7mox_ligand.pdb structures/7MOX/7mox_ligand.cif structures/7MOX/7mox_complex.pdb structures/7MOX/7mox_complex.cif 7MOY classic HDAC2 Na Na Na compound 19 "[""ZLM""]" 1 IC50 IC50 < < 1.5 nM 1.5 [] unit_conversion 8.823908740944319 success True biochemical_inhibition HDAC enzymatic potency assay; Table 4. 9 Table 4 reports compound 19 HDAC2 IC50 <1.5 nM; Figure 5 maps compound 19 bound to HDAC2 to PDB 7MOY. auto_single_measurement only accepted activity measurement [1] 1 structures\7MOY\7MOY_metadata.json point structures/7MOY/7moy_protein.pdb structures/7MOY/7moy_pocket.pdb structures/7MOY/7moy_ligand.sdf structures/7MOY/7moy_ligand.pdb structures/7MOY/7moy_ligand.cif structures/7MOY/7moy_complex.pdb structures/7MOY/7moy_complex.cif 7MOZ classic HDAC2 Na Na Na compound 25 "[""ZL4""]" 1 IC50 IC50 = = 0.43 nM 0.43 [] unit_conversion 9.366531544420413 success True biochemical_inhibition HDAC enzymatic potency assay; Table 4. 10 Table 4 reports compound 25 HDAC2 IC50 = 0.43 nM; Figure 6 maps compound 25 bound to HDAC2 to PDB 7MOZ. auto_single_measurement only accepted activity measurement [1] 1 structures\7MOZ\7MOZ_metadata.json point structures/7MOZ/7moz_protein.pdb structures/7MOZ/7moz_pocket.pdb structures/7MOZ/7moz_ligand.sdf structures/7MOZ/7moz_ligand.pdb structures/7MOZ/7moz_ligand.cif structures/7MOZ/7moz_complex.pdb structures/7MOZ/7moz_complex.cif 7MP3 extended Grb7-SH2 domain Na Na Na G7-B8 (bicyclic peptide B8) "[""CHAIN:L"", ""CHAIN:N""]" 1 Kd Kd = = 0.86 ± 0.08 µM 860.0 [] unit_conversion 6.065501548756432 success True direct_binding Surface plasmon resonance binding of G7-B8 to tethered Grb7-SH2 domain; binding curves at equilibrium, single-site binding model. 6 “KD values of ... 0.86 ± 0.08 µM ... were calculated for ... G7-B8”; Figure 2 table reports G7-B8 KD 0.86 ± 0.08 µM. The paper identifies the Grb7-SH2/G7-B8 structure as PDB ID 7MP3. auto_single_measurement only accepted activity measurement [1] 1 structures\7MP3\7MP3_metadata.json point structures/7MP3/7mp3_protein.pdb structures/7MP3/7mp3_pocket.pdb structures/7MP3/7mp3_ligand.pdb structures/7MP3/7mp3_ligand.cif structures/7MP3/7mp3_complex.pdb structures/7MP3/7mp3_complex.cif 7MPL extended NrnC Bartonella henselae NrnC_Bh after cleavage of the N-terminal His6-SUMO tag wild-type pGG "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 0.018 ± 0.001 μM 18.0 [] unit_conversion 7.7447274948966935 success True direct_binding DraCALA binding assay with radiolabeled pGG; 5 mM CaCl2 was used to prevent residual catalysis. 11 Figure 5C prints Kd = 0.018 ± 0.001 μM for 32P-pGG. auto_single_measurement only accepted activity measurement [1] 1 structures\7MPL\7MPL_metadata.json point structures/7MPL/7mpl_protein.pdb structures/7MPL/7mpl_pocket.pdb structures/7MPL/7mpl_ligand.pdb structures/7MPL/7mpl_ligand.cif structures/7MPL/7mpl_complex.pdb structures/7MPL/7mpl_complex.cif 7MQB extended NrnC Bartonella henselae NrnC_Bh after cleavage of the N-terminal His6-SUMO tag wild-type pGG "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 0.018 ± 0.001 μM 18.0 [] unit_conversion 7.7447274948966935 success True direct_binding DraCALA binding assay with radiolabeled pGG; 5 mM CaCl2 was used to prevent residual catalysis. 11 Figure 5C prints Kd = 0.018 ± 0.001 μM for 32P-pGG. auto_single_measurement only accepted activity measurement [1] 1 structures\7MQB\7MQB_metadata.json point structures/7MQB/7mqb_protein.pdb structures/7MQB/7mqb_pocket.pdb structures/7MQB/7mqb_ligand.pdb structures/7MQB/7mqb_ligand.cif structures/7MQB/7mqb_complex.pdb structures/7MQB/7mqb_complex.cif 7MQC extended NrnC Bartonella henselae NrnC_Bh after cleavage of the N-terminal His6-SUMO tag wild-type pGG "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H"", ""CHAIN:J"", ""CHAIN:L"", ""CHAIN:N"", ""CHAIN:P""]" 1 Kd Kd = = 0.018 ± 0.001 μM 18.0 [] unit_conversion 7.7447274948966935 success True direct_binding DraCALA binding assay with radiolabeled pGG; 5 mM CaCl2 was used to prevent residual catalysis. 11 Figure 5C prints Kd = 0.018 ± 0.001 μM for 32P-pGG. auto_single_measurement only accepted activity measurement [1] 1 structures\7MQC\7MQC_metadata.json point structures/7MQC/7mqc_protein.pdb structures/7MQC/7mqc_pocket.pdb structures/7MQC/7mqc_ligand.pdb structures/7MQC/7mqc_ligand.cif structures/7MQC/7mqc_complex.pdb structures/7MQC/7mqc_complex.cif 7MQD extended NrnC Bartonella henselae NrnC_Bh after cleavage of the N-terminal His6-SUMO tag wild-type pAGG "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 3.5 ± 0.1 μM 3500.0 [] unit_conversion 5.455931955649724 success True direct_binding DraCALA binding assay with radiolabeled pAGG; 5 mM CaCl2 was used to prevent residual catalysis. 11 Figure 5C prints Kd = 3.5 ± 0.1 μM for 32P-pAGG. auto_single_measurement only accepted activity measurement [1] 1 structures\7MQD\7MQD_metadata.json point structures/7MQD/7mqd_protein.pdb structures/7MQD/7mqd_pocket.pdb structures/7MQD/7mqd_ligand.pdb structures/7MQD/7mqd_ligand.cif structures/7MQD/7mqd_complex.pdb structures/7MQD/7mqd_complex.cif 7MQE extended NrnC Bartonella henselae NrnC_Bh after cleavage of the N-terminal His6-SUMO tag wild-type pAGG "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H"", ""CHAIN:J"", ""CHAIN:L"", ""CHAIN:N"", ""CHAIN:P""]" 1 Kd Kd = = 3.5 ± 0.1 μM 3500.0 [] unit_conversion 5.455931955649724 success True direct_binding DraCALA binding assay with radiolabeled pAGG; 5 mM CaCl2 was used to prevent residual catalysis. 11 Figure 5C prints Kd = 3.5 ± 0.1 μM for 32P-pAGG. auto_single_measurement only accepted activity measurement [1] 1 structures\7MQE\7MQE_metadata.json point structures/7MQE/7mqe_protein.pdb structures/7MQE/7mqe_pocket.pdb structures/7MQE/7mqe_ligand.pdb structures/7MQE/7mqe_ligand.cif structures/7MQE/7mqe_complex.pdb structures/7MQE/7mqe_complex.cif 7MQF extended NrnC Bartonella henselae NrnC_Bh after cleavage of the N-terminal His6-SUMO tag wild-type pAAAGG "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H"", ""CHAIN:J"", ""CHAIN:L"", ""CHAIN:N"", ""CHAIN:P""]" 1 Kd Kd = = 3.2 ± 0.1 μM 3200.0 [] unit_conversion 5.494850021680094 success True direct_binding DraCALA binding assay with radiolabeled pAAAGG; 5 mM CaCl2 was used to prevent residual catalysis. 11 Figure 5C prints Kd = 3.2 ± 0.1 μM for 32P-pAAAGG. auto_single_measurement only accepted activity measurement [1] 1 structures\7MQF\7MQF_metadata.json point structures/7MQF/7mqf_protein.pdb structures/7MQF/7mqf_pocket.pdb structures/7MQF/7mqf_ligand.pdb structures/7MQF/7mqf_ligand.cif structures/7MQF/7mqf_complex.pdb structures/7MQF/7mqf_complex.cif 7MQG extended NrnC Bartonella henselae NrnC_Bh after cleavage of the N-terminal His6-SUMO tag wild-type pAAAGG "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 3.2 ± 0.1 μM 3200.0 [] unit_conversion 5.494850021680094 success True direct_binding DraCALA binding assay with radiolabeled pAAAGG; 5 mM CaCl2 was used to prevent residual catalysis. 11 Figure 5C prints Kd = 3.2 ± 0.1 μM for 32P-pAAAGG. auto_single_measurement only accepted activity measurement [1] 1 structures\7MQG\7MQG_metadata.json point structures/7MQG/7mqg_protein.pdb structures/7MQG/7mqg_pocket.pdb structures/7MQG/7mqg_ligand.pdb structures/7MQG/7mqg_ligand.cif structures/7MQG/7mqg_complex.pdb structures/7MQG/7mqg_complex.cif 7MR5 classic BRD4 human Na Na GXH-II-052 "[""ZMS""]" 1 Kd Kd = = 28 ± 0.71 nM 28.0 [] unit_conversion 7.552841968657781 success True direct_binding Single qPCR BromoScan binding assay, duplicate (±SD). 3 Table 1 reports GXH-II-052 Kd for BRD4-1 as 28 ± 0.71 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7MR5\7MR5_metadata.json point structures/7MR5/7mr5_protein.pdb structures/7MR5/7mr5_pocket.pdb structures/7MR5/7mr5_ligand.sdf structures/7MR5/7mr5_ligand.pdb structures/7MR5/7mr5_ligand.cif structures/7MR5/7mr5_complex.pdb structures/7MR5/7mr5_complex.cif 7MR6 classic BRD4 human Na Na GXH-II-082 "[""ZMV""]" 1 Kd Kd = = 6.4 ± 0.64 nM 6.4 [] unit_conversion 8.193820026016112 success True direct_binding Single qPCR BromoScan binding assay, duplicate (±SD). 3 Table 1 reports GXH-II-082 Kd for BRD4-1 as 6.4 ± 0.64 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7MR6\7MR6_metadata.json point structures/7MR6/7mr6_protein.pdb structures/7MR6/7mr6_pocket.pdb structures/7MR6/7mr6_ligand.sdf structures/7MR6/7mr6_ligand.pdb structures/7MR6/7mr6_ligand.cif structures/7MR6/7mr6_complex.pdb structures/7MR6/7mr6_complex.cif 7MR7 classic BRD4 human Na Na GXH-IV-075 "[""ZN1""]" 1 Kd Kd = = 6.0 ± 0.07 nM 6.0 [] unit_conversion 8.221848749616356 success True direct_binding Single qPCR BromoScan binding assay, duplicate (±SD). 3 Table 1 reports GXH-IV-075 Kd for BRD4-1 as 6.0 ± 0.07 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7MR7\7MR7_metadata.json point structures/7MR7/7mr7_protein.pdb structures/7MR7/7mr7_pocket.pdb structures/7MR7/7mr7_ligand.sdf structures/7MR7/7mr7_ligand.pdb structures/7MR7/7mr7_ligand.cif structures/7MR7/7mr7_complex.pdb structures/7MR7/7mr7_complex.cif 7MRC classic BRDT human Na Na GXH-II-052 "[""ZMS""]" 1 Kd Kd = = 0.60 ± 0.07 nM 0.6 [] unit_conversion 9.221848749616356 success True direct_binding Single qPCR BromoScan binding assay, duplicate (±SD). 3 Table 1 reports GXH-II-052 Kd for BRDT-1 as 0.60 ± 0.07 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7MRC\7MRC_metadata.json point structures/7MRC/7mrc_protein.pdb structures/7MRC/7mrc_pocket.pdb structures/7MRC/7mrc_ligand.sdf structures/7MRC/7mrc_ligand.pdb structures/7MRC/7mrc_ligand.cif structures/7MRC/7mrc_complex.pdb structures/7MRC/7mrc_complex.cif 7MRD classic BRDT human Na Na GXH-II-082 "[""ZMV""]" 1 Kd Kd = = 0.92 ± 0.028 nM 0.92 [] unit_conversion 9.036212172654444 success True direct_binding Single qPCR BromoScan binding assay, duplicate (±SD). 3 Table 1 reports GXH-II-082 Kd for BRDT-1 as 0.92 ± 0.028 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7MRD\7MRD_metadata.json point structures/7MRD/7mrd_protein.pdb structures/7MRD/7mrd_pocket.pdb structures/7MRD/7mrd_ligand.sdf structures/7MRD/7mrd_ligand.pdb structures/7MRD/7mrd_ligand.cif structures/7MRD/7mrd_complex.pdb structures/7MRD/7mrd_complex.cif 7MS5 classic USP5 zinc-finger ubiquitin binding domain Na USP5 residues 171-290 Na compound 1; 4-(4-(4-(3,4-difluoro-phenyl)-piperidin-1-ylsulfonyl)-phenyl)-4-oxo-butanoic acid "[""ZOG""]" 1 Kd Kd = = 12 ± 3 µM 12000.0 [] unit_conversion 4.920818753952375 success True direct_binding SPR binding of compound 1 to USP5 ZnF-UBD. 3 Figure 3 identifies compound 1 in the USP5 ZnF-UBD co-crystal (PDB 7MS5) and reports representative SPR binding with K_D = 12 ± 3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7MS5\7MS5_metadata.json point structures/7MS5/7ms5_protein.pdb structures/7MS5/7ms5_pocket.pdb structures/7MS5/7ms5_ligand.sdf structures/7MS5/7ms5_ligand.pdb structures/7MS5/7ms5_ligand.cif structures/7MS5/7ms5_complex.pdb structures/7MS5/7ms5_complex.cif 7MS6 classic USP5 zinc-finger ubiquitin binding domain Na USP5 residues 171-290 Na compound 48; (2-fluoro-4-((4-phenylpiperidin-1-yl)sulfonyl)benzoyl)glycine "[""ZPV""]" 1 Kd Kd = = 9 ± 2 µM 9000.0 [] unit_conversion 5.045757490560675 success True direct_binding Direct binding determination of compound 48 to USP5 ZnF-UBD. 6 The text states that compound 48 binds USP5 ZnF-UBD with K_D = 9 ± 2 µM and that its co-crystal structure is PDB 7MS6. auto_single_measurement only accepted activity measurement [1] 1 structures\7MS6\7MS6_metadata.json point structures/7MS6/7ms6_protein.pdb structures/7MS6/7ms6_pocket.pdb structures/7MS6/7ms6_ligand.sdf structures/7MS6/7ms6_ligand.pdb structures/7MS6/7ms6_ligand.cif structures/7MS6/7ms6_complex.pdb structures/7MS6/7ms6_complex.cif 7MS7 classic USP5 zinc-finger ubiquitin binding domain Na USP5 residues 171-290 Na compound 64; (5-((4-(4-chlorophenyl)piperidin-1-yl)sulfonyl)picolinoyl)glycine "[""ZQ1""]" 1 Kd Kd = = 2.8 ± 0.5 µM 2800.0 [] unit_conversion 5.552841968657781 success True direct_binding SPR binding of compound 64 to isolated USP5 ZnF-UBD. 10 Figure 5 maps compound 64 to PDB 7MS7; Figure 6 reports an SPR-derived USP5 ZnF-UBD K_D of 2.8 ± 0.5 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7MS7\7MS7_metadata.json point structures/7MS7/7ms7_protein.pdb structures/7MS7/7ms7_pocket.pdb structures/7MS7/7ms7_ligand.sdf structures/7MS7/7ms7_ligand.pdb structures/7MS7/7ms7_ligand.cif structures/7MS7/7ms7_complex.pdb structures/7MS7/7ms7_complex.cif 7MU6 classic Apoptosis signal-regulating kinase 1 (ASK1) human Na Na compound 28 "[""A1AWT""]" 1 IC50 IC50 = = 7 nM 7.0 [] unit_conversion 8.154901959985743 success True biochemical_inhibition ASK1 biochemical assay; inhibition of ASK1 autophosphorylation. 5 Table 3 lists compound 28 with ASK1 biochemical IC50 = 7 nM; its footnote identifies the assay as inhibition of ASK1 autophosphorylation. auto_single_measurement only accepted activity measurement [1] 1 structures\7MU6\7MU6_metadata.json point structures/7MU6/7mu6_protein.pdb structures/7MU6/7mu6_pocket.pdb structures/7MU6/7mu6_ligand.sdf structures/7MU6/7mu6_ligand.pdb structures/7MU6/7mu6_ligand.cif structures/7MU6/7mu6_complex.pdb structures/7MU6/7mu6_complex.cif 7MYL classic DfrA1 dihydrofolate reductase Na Na Na trimethoprim (TMP) "[""TOP""]" 2 Kd Kd = = 27,792 ± 4877 nM 27792.0 [] unit_conversion 4.556080198896977 success True direct_binding Microscale thermophoresis, DfrA1 apo titrated with TMP; Table 5. 12 Table 5 reports TMP KD for DfrA1 apo as 27,792 ± 4877 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7MYL\7MYL_metadata.json point structures/7MYL/7myl_protein.pdb structures/7MYL/7myl_pocket.pdb structures/7MYL/7myl_ligand.sdf structures/7MYL/7myl_ligand.pdb structures/7MYL/7myl_ligand.cif structures/7MYL/7myl_complex.pdb structures/7MYL/7myl_complex.cif 7MYP classic HIV-1 protease (PR), PRS17 Human immunodeficiency virus type 1 (HIV-1) PRS17 protease dimer, residues 1-99 and 1'-99' G48V; V82S GRL-44-10A (paper compound 2, GRL-4410) "[""G04""]" 1 Ki Ki = = 15.8 ± 4.8 nM 15.8 [] unit_conversion 7.801342913045577 success True biochemical_inhibition Inhibition of PRS17 measured by spectroscopic FRET-substrate (BACHEM H-2992) assay at 37 °C and pH 5.6. 2 “The Ki values of compounds 2 and 3 were 15.8 ± 4.8 and 17 ± 1.3 nM, respectively, for PRS17.” Methods specify that inhibition values (Ki) for PRS17 were measured by a spectroscopic FRET-substrate assay; the same page maps 7MYP to PRS17/2. auto_single_measurement only accepted activity measurement [1] 1 structures\7MYP\7MYP_metadata.json point structures/7MYP/7myp_protein.pdb structures/7MYP/7myp_pocket.pdb structures/7MYP/7myp_ligand.sdf structures/7MYP/7myp_ligand.pdb structures/7MYP/7myp_ligand.cif structures/7MYP/7myp_complex.pdb structures/7MYP/7myp_complex.cif 7MYY classic HIV-1 protease (PR), PRS17 Human immunodeficiency virus type 1 (HIV-1) PRS17 protease dimer, residues 1-99 and 1'-99' G48V; V82S GRL-142 (paper compound 3) "[""7OA""]" 1 Ki Ki = = 17 ± 1.3 nM 17.0 [] unit_conversion 7.769551078621726 success True biochemical_inhibition Inhibition of PRS17 measured by spectroscopic FRET-substrate (BACHEM H-2992) assay at 37 °C and pH 5.6. 2 “The Ki values of compounds 2 and 3 were 15.8 ± 4.8 and 17 ± 1.3 nM, respectively, for PRS17.” Methods specify that inhibition values (Ki) for PRS17 were measured by a spectroscopic FRET-substrate assay; the same page maps 7MYY to PRS17/3. auto_single_measurement only accepted activity measurement [1] 1 structures\7MYY\7MYY_metadata.json point structures/7MYY/7myy_protein.pdb structures/7MYY/7myy_pocket.pdb structures/7MYY/7myy_ligand.sdf structures/7MYY/7myy_ligand.pdb structures/7MYY/7myy_ligand.cif structures/7MYY/7myy_complex.pdb structures/7MYY/7myy_complex.cif 7MZS classic UcaD lectin-binding domain Proteus mirabilis (strain PM54) UcaD lectin domain cloned into pET22b with a C-terminal His-tag Na galactose "[""GLA""]" 1 Kd Kd = = 162.3 ± 12.8 μM 162300.0 [] unit_conversion 3.789681480173768 success True direct_binding Competitive SPR using immobilised UcaD; the text identifies pre-bound galactose K_D before competition with lacto-N-fucopentose VI. 12 “pre-bound galactose (K_D = 162.3 μM ± 12.8) could inhibit lacto-N-fucopentose VI ... binding” in an SPR experiment using immobilised UcaD. auto_single_measurement only accepted activity measurement [1] 1 structures\7MZS\7MZS_metadata.json point structures/7MZS/7mzs_protein.pdb structures/7MZS/7mzs_pocket.pdb structures/7MZS/7mzs_ligand.sdf structures/7MZS/7mzs_ligand.pdb structures/7MZS/7mzs_ligand.cif structures/7MZS/7mzs_complex.pdb structures/7MZS/7mzs_complex.cif 7N0X extended Rhesusized RV144 DH827 Fab bound to HIV-1 Env gp120 V2 peptide Macaca mulatta (rhesus macaque) antibody; HIV-1 Env antigen RhDH827 Fab with synthetic clade A/E 92TH023 gp120 V2 peptide, residues 167-184 Na Synthetic HIV-1 gp120 V2 peptide, residues 167-184 "[""CHAIN:G""]" 1 Kd Kd = = 2.73 × 10^3 nM 2730.0 [] unit_conversion 5.5638373529592435 success True direct_binding SPR on Biacore 3000; IgG immobilized and synthetic V2 peptide used as analyte. Table/figure identifies the RhDH827–gp12092TH023 V2-peptide determination. 8 Figure 2C reports RhDH827 with gp12092TH023 V2-peptide (167-184), KD 2.73 × 10^3 nM. The methods state that this synthetic peptide was used for the RhDH827 complex deposited as 7N0X. auto_single_measurement only accepted activity measurement [1] 1 structures\7N0X\7N0X_metadata.json point structures/7N0X/7n0x_protein.pdb structures/7N0X/7n0x_pocket.pdb structures/7N0X/7n0x_ligand.pdb structures/7N0X/7n0x_ligand.cif structures/7N0X/7n0x_complex.pdb structures/7N0X/7n0x_complex.cif 7N14 classic CYP199A4 Rhodopseudomonas palustris HaA2 Na Na 4-(1H-1,2,4-triazol-1-yl)benzoic acid "[""ZRS""]" 1 Kd Kd = = 18.3 ± 0.4 μM 18300.0 [] unit_conversion 4.73754891026957 success True direct_binding Ligand-binding assay; Table 1 reports the dissociation constant for CYP199A4 with 4-(1H-1,2,4-triazol-1-yl)benzoic acid. 5 Table 1 lists Kd = 18.3 ± 0.4 μM for 4-(1H-1,2,4-triazol-1-yl)benzoic acid. The table footnote defines Kd as the dissociation constant. auto_single_measurement only accepted activity measurement [1] 1 structures\7N14\7N14_metadata.json point structures/7N14/7n14_protein.pdb structures/7N14/7n14_pocket.pdb structures/7N14/7n14_ligand.sdf structures/7N14/7n14_ligand.pdb structures/7N14/7n14_ligand.cif structures/7N14/7n14_complex.pdb structures/7N14/7n14_complex.cif 7N1E extended TCR pRLQ3 with HLA-A*02:01 (HLA-A2) Na Soluble RLQ3 TCR, alpha residues 1-204 and beta residues 1-244, bound to soluble RLQ-HLA-A2 Na RLQSLQTYV (RLQ) "[""CHAIN:C""]" 1 Kd Kd = = 32.9 μM 32900.0 [] unit_conversion 4.482804102050026 success True direct_binding Surface plasmon resonance; recombinant RLQ3 TCR flowed over immobilized RLQ–HLA-A2 and equilibrium binding was fitted. 2 The Results state that RLQ3 bound RLQ–HLA-A2 with a dissociation constant (Kd) of 32.9 μM; the same page identifies SPR as the assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7N1E\7N1E_metadata.json point structures/7N1E/7n1e_protein.pdb structures/7N1E/7n1e_pocket.pdb structures/7N1E/7n1e_ligand.pdb structures/7N1E/7n1e_ligand.cif structures/7N1E/7n1e_complex.pdb structures/7N1E/7n1e_complex.cif 7N1F extended TCR pYLQ7 with HLA-A*02:01 (HLA-A2) Na Soluble YLQ7 TCR, alpha residues 1-203 and beta residues 1-241, bound to soluble YLQ-HLA-A2 Na YLQPRTFLL (YLQ) "[""CHAIN:C""]" 1 Kd Kd = = 1.8 μM 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding Surface plasmon resonance; recombinant YLQ7 TCR flowed over immobilized YLQ–HLA-A2 and equilibrium binding was fitted. 2 The Results state that YLQ7 bound YLQ–HLA-A2 with a dissociation constant (Kd) of 1.8 μM; the same page identifies SPR as the assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7N1F\7N1F_metadata.json point structures/7N1F/7n1f_protein.pdb structures/7N1F/7n1f_pocket.pdb structures/7N1F/7n1f_ligand.pdb structures/7N1F/7n1f_ligand.cif structures/7N1F/7n1f_complex.pdb structures/7N1F/7n1f_complex.cif 7N2V extended 70S ribosome; elongation factor G (EF-G) Escherichia coli Na Na spectinomycin (SPC) "[""SCM""]" 1 IC50 IC50 = = 3 mM 3000000.0 [] unit_conversion 2.5228787452803374 success True biochemical_inhibition SPC was used at its half-maximal inhibitory concentration for translocation inhibition to prepare the INT1 cryo-EM intermediate. 6 “SPC (INT1) ... was used at its half-maximum inhibitory concentration (IC50) for translocation inhibition (3 mM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7N2V\7N2V_metadata.json point structures/7N2V/7n2v_ligand.sdf structures/7N2V/7n2v_ligand.cif structures/7N2V/7n2v_complex.cif 7N44 classic SARS-CoV-2 (2019-NCoV) main protease (Mpro) SARS-CoV-2 (2019-NCoV) Na Na Compound 13; 5-(3-{3-chloro-5-[(5-methyl-1,3-thiazol-4-yl)methoxy]phenyl}-2-oxo-2H-[1,3'-bipyridin]-5-yl)pyrimidine-2,4(1H,3H)-dione "[""06I""]" 1 IC50 IC50 = = 0.042 ± 0.015 μM 42.0 [] unit_conversion 7.376750709602099 success True biochemical_inhibition Proteolytic activity inhibition assay with recombinant SARS-CoV-2 Mpro; Table 1 reports the measured enzyme-inhibition activity. 2 Table 1, “Measured Activities for Inhibition of SARS-CoV-2 Mpro,” lists compound 13 with IC50 = 0.042 ± 0.015 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7N44\7N44_metadata.json point structures/7N44/7n44_protein.pdb structures/7N44/7n44_pocket.pdb structures/7N44/7n44_ligand.sdf structures/7N44/7n44_ligand.pdb structures/7N44/7n44_ligand.cif structures/7N44/7n44_complex.pdb structures/7N44/7n44_complex.cif 7N5O classic Bruton's tyrosine kinase (Btk) Na Na Na compound 5 "[""0BQ""]" 1 pIC50 IC50 = = 5.0 10000.0 [] p_metric_transform 5.0 success True biochemical_inhibition Btk enzyme IC50 determined in duplicate; value reported as pIC50 in Table 1. 2 Table 1 lists compound 5 with Btk pIC50 = 5.0; its footnote states enzyme IC50 was determined in duplicate. Figure 2 maps compound 5 to PDB 7N5O. auto_single_measurement only accepted activity measurement [1] 1 structures\7N5O\7N5O_metadata.json point structures/7N5O/7n5o_protein.pdb structures/7N5O/7n5o_pocket.pdb structures/7N5O/7n5o_ligand.sdf structures/7N5O/7n5o_ligand.pdb structures/7N5O/7n5o_ligand.cif structures/7N5O/7n5o_complex.pdb structures/7N5O/7n5o_complex.cif 7N5R classic Bruton's tyrosine kinase (Btk) Na Na Na compound 6 "[""0UW""]" 1 pIC50 IC50 = = 3.3 501187.2336272725 [] p_metric_transform 3.3 success True biochemical_inhibition Btk enzyme IC50 determined in duplicate; value reported as pIC50 in Table 1. 2 Table 1 lists compound 6 with Btk pIC50 = 3.3; its footnote states enzyme IC50 was determined in duplicate. Figure 2 maps compound 6 to PDB 7N5R. auto_single_measurement only accepted activity measurement [1] 1 structures\7N5R\7N5R_metadata.json point structures/7N5R/7n5r_protein.pdb structures/7N5R/7n5r_pocket.pdb structures/7N5R/7n5r_ligand.sdf structures/7N5R/7n5r_ligand.pdb structures/7N5R/7n5r_ligand.cif structures/7N5R/7n5r_complex.pdb structures/7N5R/7n5r_complex.cif 7N5X classic Bruton's tyrosine kinase (Btk) Na Na Na compound 18 "[""0GW""]" 1 pIC50 IC50 = = 7.3 50.11872336272725 [] p_metric_transform 7.3 success True biochemical_inhibition Btk enzyme IC50 determined in duplicate; value reported as pIC50 in Table 2. 3 Table 2 lists compound 18 with Btk pIC50 = 7.3; its footnote states enzyme IC50 was determined in duplicate. The text identifies the compound 18 cocrystal as PDB 7N5X. auto_single_measurement only accepted activity measurement [1] 1 structures\7N5X\7N5X_metadata.json point structures/7N5X/7n5x_protein.pdb structures/7N5X/7n5x_pocket.pdb structures/7N5X/7n5x_ligand.sdf structures/7N5X/7n5x_ligand.pdb structures/7N5X/7n5x_ligand.cif structures/7N5X/7n5x_complex.pdb structures/7N5X/7n5x_complex.cif 7N6J extended E. coli DnaK E. coli substrate-binding domain of E. coli DnaK Na RKQSTIALALLPLLFTPRR "[""CHAIN:B""]" 1 Kd Kd = = 5 ± 1 nM 5.0 [] unit_conversion 8.301029995663981 success True direct_binding Fluorescence-anisotropy competitive binding assay; apparent Kd. 3 Fig. 3 lists peptide A, RKQSTIALALLPLLFTPRR, with Kd = 5 ± 1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7N6J\7N6J_metadata.json point structures/7N6J/7n6j_protein.pdb structures/7N6J/7n6j_pocket.pdb structures/7N6J/7n6j_ligand.pdb structures/7N6J/7n6j_ligand.cif structures/7N6J/7n6j_complex.pdb structures/7N6J/7n6j_complex.cif 7N6L extended E. coli DnaK E. coli substrate-binding domain of E. coli DnaK Na EANQQKPLLGLFADG "[""CHAIN:B""]" 1 Kd Kd = = 115 ± 22 nM 115.0 [] unit_conversion 6.939302159646388 success True direct_binding Fluorescence-anisotropy competitive binding assay; apparent Kd. 3 Fig. 3 lists peptide C, EANQQKPLLGLFADG, with Kd = 115 ± 22 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7N6L\7N6L_metadata.json point structures/7N6L/7n6l_protein.pdb structures/7N6L/7n6l_pocket.pdb structures/7N6L/7n6l_ligand.pdb structures/7N6L/7n6l_ligand.cif structures/7N6L/7n6l_complex.pdb structures/7N6L/7n6l_complex.cif 7N6V classic HIV-1 protease PRS17 HIV-1 PRS17V48G revertant multiple mutant V48G revertant; PRS17 background mutations L10I, K20R, E35D, M36I, S37D, M46L, I54V, D60E, I62V, L63P, A71V, I72V, V77I, V82S, L90M, I93L Amprenavir (APV) "[""478""]" 1 Ki Ki = = 5.2 ± 2 nM 5.2 [] unit_conversion 8.2839966563652 success True biochemical_inhibition Purified-enzyme FRET kinetics/inhibition assay; APV inhibition measurement. 9 Table 1 reports Ki,APV = 5.2 +/- 2 nM for PRS17V48G. auto_single_measurement only accepted activity measurement [1] 1 structures\7N6V\7N6V_metadata.json point structures/7N6V/7n6v_protein.pdb structures/7N6V/7n6v_pocket.pdb structures/7N6V/7n6v_ligand.sdf structures/7N6V/7n6v_ligand.pdb structures/7N6V/7n6v_ligand.cif structures/7N6V/7n6v_complex.pdb structures/7N6V/7n6v_complex.cif 7N7L classic PI5P4KIIAlpha Na Na Na BI-D1870 "[""584""]" 2 Kd Kd = = 1.3 ± 0.2 µM 1300.0 [] unit_conversion 5.886056647693163 success True direct_binding Competitive displacement of a fluorescent ATP analogue from purified PI5P4Kα. 2 Fig. 1B reports “Kd = 1.3 ± 0.2 µM”; the caption states BI-D1870 displaces a bound fluorescent ATP analogue from PI5P4Kα. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7N7L\7N7L_metadata.json point structures/7N7L/7n7l_protein.pdb structures/7N7L/7n7l_pocket.pdb structures/7N7L/7n7l_ligand.sdf structures/7N7L/7n7l_ligand.pdb structures/7N7L/7n7l_ligand.cif structures/7N7L/7n7l_complex.pdb structures/7N7L/7n7l_complex.cif 7N7M classic PI5P4KIIAlpha Na Na Na BI-2536 "[""R78""]" 1 Ki Ki ~ ~ 5 µM 5000.0 [] unit_conversion 5.301029995663981 success True biochemical_inhibition In vitro PI5P4Kα kinase inhibition; Fig. 1A reports the hit-compound Ki. 2 Fig. 1A labels BI-2536 “(~5 µM),” and its caption states that parenthetical values are Ki values for PI5P4Kα. auto_single_measurement only accepted activity measurement [1] 1 structures\7N7M\7N7M_metadata.json point structures/7N7M/7n7m_protein.pdb structures/7N7M/7n7m_pocket.pdb structures/7N7M/7n7m_ligand.sdf structures/7N7M/7n7m_ligand.pdb structures/7N7M/7n7m_ligand.cif structures/7N7M/7n7m_complex.pdb structures/7N7M/7n7m_complex.cif 7N7N classic PI5P4KIIAlpha Na Na Na Volasertib "[""IBI""]" 1 Ki Ki ~ ~ 5 µM 5000.0 [] unit_conversion 5.301029995663981 success True biochemical_inhibition In vitro PI5P4Kα kinase inhibition; Fig. 1A reports the hit-compound Ki. 2 Fig. 1A labels Volasertib “(~5 µM),” and its caption states that parenthetical values are Ki values for PI5P4Kα. auto_single_measurement only accepted activity measurement [1] 1 structures\7N7N\7N7N_metadata.json point structures/7N7N/7n7n_protein.pdb structures/7N7N/7n7n_pocket.pdb structures/7N7N/7n7n_ligand.sdf structures/7N7N/7n7n_ligand.pdb structures/7N7N/7n7n_ligand.cif structures/7N7N/7n7n_complex.pdb structures/7N7N/7n7n_complex.cif 7N7O classic PI5P4KIIAlpha Na Na Na Palbociclib "[""LQQ""]" 1 Ki Ki ~ ~ 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition In vitro PI5P4Kα kinase inhibition; Fig. 1A reports the hit-compound Ki. 2 Fig. 1A labels Palbociclib “(~2 µM),” and its caption states that parenthetical values are Ki values for PI5P4Kα. auto_single_measurement only accepted activity measurement [1] 1 structures\7N7O\7N7O_metadata.json point structures/7N7O/7n7o_protein.pdb structures/7N7O/7n7o_pocket.pdb structures/7N7O/7n7o_ligand.sdf structures/7N7O/7n7o_ligand.pdb structures/7N7O/7n7o_ligand.cif structures/7N7O/7n7o_complex.pdb structures/7N7O/7n7o_complex.cif 7N7X extended human plasma kallikrein human human plasma kallikrein serine protease domain Na BCX7353 (compound 32a; ORLADEYO) "[""0RI""]" 4 Ki Ki = = 0.00044 μM 0.44 [] unit_conversion 9.356547323513812 success True biochemical_inhibition Calculated inhibition constant from the mean purified-plasma-kallikrein IC50. 9 The text reports a calculated inhibition constant (Ki) of 0.00044 μM for BCX7353. auto_metric_priority unique highest-priority metric family: Ki [4] 5 structures\7N7X\7N7X_metadata.json point structures/7N7X/7n7x_ligand.sdf structures/7N7X/7n7x_ligand.cif structures/7N7X/7n7x_complex.cif 7N81 classic PI5P4KIIBeta Na Na Na CC260 "[""HKP""]" 1 Ki Ki ~ ~ 30 nM 30.0 [] unit_conversion 7.522878745280337 success True biochemical_inhibition Concentration-inhibition assay using purified PI5P4Kβ with ATP fixed at 20 µM. 3 The text states that CC260 “improved potency toward PI5P4Kβ (Ki ~30 nM)”; Fig. 2B labels CC260 “(40 nM, 30 nM)” for PI5P4Kα and PI5P4Kβ, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7N81\7N81_metadata.json point structures/7N81/7n81_protein.pdb structures/7N81/7n81_pocket.pdb structures/7N81/7n81_ligand.sdf structures/7N81/7n81_ligand.pdb structures/7N81/7n81_ligand.cif structures/7N81/7n81_complex.pdb structures/7N81/7n81_complex.cif 7N8C extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na Mcule-5948770040 (compound 1) "[""YD1""]" 3 Kd Kd = = 1.30±0.18 µM 1300.0 [] unit_conversion 5.886056647693163 success True direct_binding Isothermal titration calorimetry (ITC). 15 Table 2 reports compound 1 ITC Kd 1.30±0.18 µM. auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\7N8C\7N8C_metadata.json point structures/7N8C/7n8c_protein.pdb structures/7N8C/7n8c_pocket.pdb structures/7N8C/7n8c_ligand.pdb structures/7N8C/7n8c_ligand.cif structures/7N8C/7n8c_complex.pdb structures/7N8C/7n8c_complex.cif 7NA1 classic HDM2 Na Na Na compound 2 "[""1GI""]" 1 IC50 IC50 = = 260 nM 260.0 [] unit_conversion 6.585026652029182 success True biochemical_inhibition TR-FRET HDM2-p53 protein-protein interaction assay. 2 Figure 2A explicitly reports for compound 2: “FRET IC50 = 260 nM”; the figure caption identifies the assay as TR-FRET and states compound 2 is bound to HDM2. auto_single_measurement only accepted activity measurement [1] 1 structures\7NA1\7NA1_metadata.json point structures/7NA1/7na1_protein.pdb structures/7NA1/7na1_pocket.pdb structures/7NA1/7na1_ligand.sdf structures/7NA1/7na1_ligand.pdb structures/7NA1/7na1_ligand.cif structures/7NA1/7na1_complex.pdb structures/7NA1/7na1_complex.cif 7NA2 classic HDM2 Na Na Na compound 56 "[""1I0""]" 1 IC50 IC50 = = 0.65 nM 0.65 [] unit_conversion 9.187086643357144 success True biochemical_inhibition TR-FRET HDM2-p53 protein-protein interaction assay. 10 Table 4 explicitly reports compound 56 TR-FRET IC50 = 0.65 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NA2\7NA2_metadata.json point structures/7NA2/7na2_protein.pdb structures/7NA2/7na2_pocket.pdb structures/7NA2/7na2_ligand.sdf structures/7NA2/7na2_ligand.pdb structures/7NA2/7na2_ligand.cif structures/7NA2/7na2_complex.pdb structures/7NA2/7na2_complex.cif 7NA3 classic HDM2 Na Na Na compound 62 "[""1I3""]" 1 IC50 IC50 = = 1.6 nM 1.6 [] unit_conversion 8.795880017344075 success True biochemical_inhibition TR-FRET HDM2-p53 protein-protein interaction assay. 10 Table 4 explicitly reports compound 62 TR-FRET IC50 = 1.6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NA3\7NA3_metadata.json point structures/7NA3/7na3_protein.pdb structures/7NA3/7na3_pocket.pdb structures/7NA3/7na3_ligand.sdf structures/7NA3/7na3_ligand.pdb structures/7NA3/7na3_ligand.cif structures/7NA3/7na3_complex.pdb structures/7NA3/7na3_complex.cif 7NA4 classic HDM2 Na Na Na compound 63 "[""1I9""]" 1 IC50 IC50 = = 0.35 nM 0.35 [] unit_conversion 9.455931955649724 success True biochemical_inhibition TR-FRET HDM2-p53 protein-protein interaction assay. 10 Table 4 explicitly reports compound 63 TR-FRET IC50 = 0.35 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NA4\7NA4_metadata.json point structures/7NA4/7na4_protein.pdb structures/7NA4/7na4_pocket.pdb structures/7NA4/7na4_ligand.sdf structures/7NA4/7na4_ligand.pdb structures/7NA4/7na4_ligand.cif structures/7NA4/7na4_complex.pdb structures/7NA4/7na4_complex.cif 7NAE classic E. coli dihydrofolate reductase (EcDHFR) Escherichia coli Na Na trimethoprim (TMP) "[""TOP""]" 2 Kd Kd = = 23.6 ± 5.1 nM 23.6 [] unit_conversion 7.627087997029894 success True direct_binding Microscale thermophoresis, EcDHFR apo titrated with TMP; Table 5. 12 Table 5 reports TMP KD for EcDHFR apo as 23.6 ± 5.1 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7NAE\7NAE_metadata.json point structures/7NAE/7nae_protein.pdb structures/7NAE/7nae_pocket.pdb structures/7NAE/7nae_ligand.sdf structures/7NAE/7nae_ligand.pdb structures/7NAE/7nae_ligand.cif structures/7NAE/7nae_complex.pdb structures/7NAE/7nae_complex.cif 7NAM extended LRP6 Na LRP6 E1 domain Na Lr-EET-3.5 "[""CHAIN:B""]" 1 Kd Kd = = 1.01 nM 1.01 [] unit_conversion 8.995678626217357 success True direct_binding SPR measurement of affinity-matured CKP binding to LRP6 E1. 3 Fig. 1F prints “E1 / Lr-EET-3.5, KD = 1.01 nM”; the surrounding text identifies Lr-EET-3.5 as an affinity-matured LRP6 E1-binding CKP. auto_single_measurement only accepted activity measurement [1] 1 structures\7NAM\7NAM_metadata.json point structures/7NAM/7nam_protein.pdb structures/7NAM/7nam_pocket.pdb structures/7NAM/7nam_ligand.pdb structures/7NAM/7nam_ligand.cif structures/7NAM/7nam_complex.pdb structures/7NAM/7nam_complex.cif 7NB4 classic Mcl-1 Na Na Na compound 1 "[""U6Q""]" 2 Kd Kd = = 1.1 μM 1100.0 [] unit_conversion 5.958607314841775 success True direct_binding Isothermal-titration calorimetry binding measurement (Table 1 footnote). 2 Table 1 reports compound 1 as 0.51/1.1 μM, with footnote a stating Kd was measured by ITC. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7NB4\7NB4_metadata.json point structures/7NB4/7nb4_protein.pdb structures/7NB4/7nb4_pocket.pdb structures/7NB4/7nb4_ligand.sdf structures/7NB4/7nb4_ligand.pdb structures/7NB4/7nb4_ligand.cif structures/7NB4/7nb4_complex.pdb structures/7NB4/7nb4_complex.cif 7NBT extended SARS-CoV-2 main protease (Nsp5) SARS-CoV-2 Residues S1-Q306; N-terminal GST tag followed by an Mpro recognition sequence; C-terminal 6x His tag preceded by an HRV Mpro recognition sequence Na compound 21 "[""U7W""]" 2 Kd Kd = = 2.3 μM 2300.0 [] unit_conversion 5.638272163982407 success True direct_binding SPR biosensor assay of purified Mpro. 7 The text reports SPR Kd values of 4.7 and 2.3 μM for compounds 20 and 21, respectively. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7NBT\7NBT_metadata.json point structures/7NBT/7nbt_ligand.sdf structures/7NBT/7nbt_ligand.cif structures/7NBT/7nbt_complex.cif 7NCF classic HIPK2 Na Na Na MU135 (compound 21e) "[""U82""]" 1 IC50 IC50 = = 119 nM 119.0 [] unit_conversion 6.924453038607469 success True biochemical_inhibition Radiometric kinase assay (Eurofins); Table 2 reports IC50 values for compounds 21a–k. 5 Table 2 lists compound 21e (MU135) with HIPK2 IC50 = 119 nM. The table caption states the data were determined using a radiometric assay (Eurofins). auto_single_measurement only accepted activity measurement [1] 1 structures\7NCF\7NCF_metadata.json point structures/7NCF/7ncf_protein.pdb structures/7NCF/7ncf_pocket.pdb structures/7NCF/7ncf_ligand.sdf structures/7NCF/7ncf_ligand.pdb structures/7NCF/7ncf_ligand.cif structures/7NCF/7ncf_complex.pdb structures/7NCF/7ncf_complex.cif 7NDS classic TphC (tripartite tricarboxylate transporter solute-binding protein) Comamonas sp. strain E6 Mature TphC, residues N29-L322, expressed as an N-terminal 6xHis-tag fusion Na terephthalate (TPA; disodium terephthalate) "[""UB7""]" 1 Kd Kd = = 0.364 µM 364.0 [] unit_conversion 6.438898616350944 success True direct_binding Isothermal titration calorimetry of terephthalate (1) against 100 µM TphC at 22 °C; Table 1 reports the thermodynamic parameters. 5 Table 1 lists terephthalate (1) with K_D 0.364 µM; Fig. 3 caption identifies the experiment as terephthalate 1 against 100 µM TphC. auto_single_measurement only accepted activity measurement [1] 1 structures\7NDS\7NDS_metadata.json point structures/7NDS/7nds_protein.pdb structures/7NDS/7nds_pocket.pdb structures/7NDS/7nds_ligand.sdf structures/7NDS/7nds_ligand.pdb structures/7NDS/7nds_ligand.cif structures/7NDS/7nds_complex.pdb structures/7NDS/7nds_complex.cif 7NEO extended SARS-CoV-2 main protease (Nsp5) SARS-CoV-2 Residues S1-Q306; N-terminal GST tag followed by an Mpro recognition sequence; C-terminal 6x His tag preceded by an HRV Mpro recognition sequence Na compound 15 "[""U9H""]" 2 Kd Kd = = 6.6 μM 6600.0 [] unit_conversion 5.180456064458131 success True direct_binding SPR biosensor assay of purified Mpro. 7 The text states that SPR measurements confirmed compound 15 interacted with Mpro with Kd = 6.6 μM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7NEO\7NEO_metadata.json point structures/7NEO/7neo_ligand.sdf structures/7NEO/7neo_ligand.cif structures/7NEO/7neo_complex.cif 7NEU classic Thrombin Activatable Fibrinolysis Inhibitor (TAFIa) Na Na Na 28k "[""U9K""]" 2 Ki Ki = = 0.00075 μM 0.75 [] unit_conversion 9.1249387366083 success True biochemical_inhibition In vitro ADME/selectivity table for 28k; Ki against human TAFIa. 8 Table 5 reports Ki (huTAFIa) = 0.00075 μM for 28k. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7NEU\7NEU_metadata.json point structures/7NEU/7neu_protein.pdb structures/7NEU/7neu_pocket.pdb structures/7NEU/7neu_ligand.sdf structures/7NEU/7neu_ligand.pdb structures/7NEU/7neu_ligand.cif structures/7NEU/7neu_complex.pdb structures/7NEU/7neu_complex.cif 7NEX classic alpha carbonic anhydrase from Schistosoma mansoni (SmCA) Schistosoma mansoni recombinant SmCA Na compound 22b; 1-(4-fluorophenyl)-3-(4-sulfamoylphenyl)thiourea "[""8JS""]" 1 Ki Ki = = 23.3 nM 23.3 [] unit_conversion 7.632644078973981 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay using recombinant SmCA; Table 1. 3 Table 1 reports Ki = 23.3 nM for compound 22b against SmCA; the text identifies recombinant SmCA and the stopped-flow assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7NEX\7NEX_metadata.json point structures/7NEX/7nex_protein.pdb structures/7NEX/7nex_pocket.pdb structures/7NEX/7nex_ligand.sdf structures/7NEX/7nex_ligand.pdb structures/7NEX/7nex_ligand.cif structures/7NEX/7nex_complex.pdb structures/7NEX/7nex_complex.cif 7NG1 classic alpha carbonic anhydrase from Schistosoma mansoni (SmCA) Schistosoma mansoni recombinant SmCA Na compound 18; 4-(2-(3-(4-iodophenyl)selenoureido)ethyl)benzenesulfonamide "[""TN8""]" 1 Ki Ki = = 4.7 nM 4.7 [] unit_conversion 8.327902142064282 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay using recombinant SmCA; Table 1. 3 Table 1 reports Ki = 4.7 nM for compound 18 against SmCA; the text identifies recombinant SmCA and the stopped-flow assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7NG1\7NG1_metadata.json point structures/7NG1/7ng1_protein.pdb structures/7NG1/7ng1_pocket.pdb structures/7NG1/7ng1_ligand.sdf structures/7NG1/7ng1_ligand.pdb structures/7NG1/7ng1_ligand.cif structures/7NG1/7ng1_complex.pdb structures/7NG1/7ng1_complex.cif 7NG7 classic SRC kinase human Na Na eCF506 "[""UCW""]" 1 IC50 IC50 < < 0.0005 μmol/L 0.5 [] unit_conversion 9.301029995663981 success True biochemical_inhibition Enzymatic inhibition screen against 340 wild-type protein kinases; eCF506 activity against SRC. 5 “the potency of eCF506 against SRC (IC50 < 0.0005 μmol/L)” auto_single_measurement only accepted activity measurement [1] 1 structures\7NG7\7NG7_metadata.json point structures/7NG7/7ng7_protein.pdb structures/7NG7/7ng7_pocket.pdb structures/7NG7/7ng7_ligand.sdf structures/7NG7/7ng7_ligand.pdb structures/7NG7/7ng7_ligand.cif structures/7NG7/7ng7_complex.pdb structures/7NG7/7ng7_complex.cif 7NH4 classic Akt1 Na full-length Akt1 Na Covalent-Allosteric Akt Inhibitor 3 "[""UCE""]" 1 IC50 IC50 = = 186 ± 79 nM 186.0 [] unit_conversion 6.730487055782083 success True biochemical_inhibition HTRF kinase assay; biochemical evaluation of covalent-allosteric Akt inhibitors. 4 Table 1 reports compound 3 IC50 for Akt1 as 186 ± 79 nM. Figure 3 identifies PDB 7NH4 as full-length Akt1 in complex with compound 3. auto_single_measurement only accepted activity measurement [1] 1 structures\7NH4\7NH4_metadata.json point structures/7NH4/7nh4_protein.pdb structures/7NH4/7nh4_pocket.pdb structures/7NH4/7nh4_ligand.sdf structures/7NH4/7nh4_ligand.pdb structures/7NH4/7nh4_ligand.cif structures/7NH4/7nh4_complex.pdb structures/7NH4/7nh4_complex.cif 7NH5 classic Akt1 Na full-length Akt1 Na Covalent-Allosteric Akt Inhibitor 6 "[""UC8""]" 1 IC50 IC50 = = 112 ± 21 nM 112.0 [] unit_conversion 6.950781977329818 success True biochemical_inhibition HTRF kinase assay; biochemical evaluation of covalent-allosteric Akt inhibitors. 4 Table 1 reports compound 6 IC50 for Akt1 as 112 ± 21 nM. Figure 3 identifies PDB 7NH5 as full-length Akt1 in complex with compound 6. auto_single_measurement only accepted activity measurement [1] 1 structures\7NH5\7NH5_metadata.json point structures/7NH5/7nh5_protein.pdb structures/7NH5/7nh5_pocket.pdb structures/7NH5/7nh5_ligand.sdf structures/7NH5/7nh5_ligand.pdb structures/7NH5/7nh5_ligand.cif structures/7NH5/7nh5_complex.pdb structures/7NH5/7nh5_complex.cif 7NH6 extended human carbonic anhydrase II human Na Na compound 9: 3-(3-((1-(2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl)-1H-1,2,3-triazol-4-yl)methyl)ureido)benzenesulfonamide "[""UDE""]" 1 Ki Ki = = 6.3 nM 6.3 [] unit_conversion 8.200659450546418 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay. 2 Table 1 reports compound 9 Ki = 6.3 nM for hCA II. auto_single_measurement only accepted activity measurement [1] 1 structures\7NH6\7NH6_metadata.json point structures/7NH6/7nh6_ligand.sdf structures/7NH6/7nh6_ligand.cif structures/7NH6/7nh6_complex.cif 7NH8 extended human carbonic anhydrase II human Na Na compound 8b (N-((1-(6-((3aR,7R,7aS)-7-hydroxy-2,2-dimethyltetrahydro-[1,3]dioxolo[4,5-c]pyridin-5(4H)-yl)hexyl)-1H-1,2,3-triazol-4-yl)methyl)-4-sulfamoylbenzamide) "[""UD8""]" 1 Ki Ki = = 64.7 nM 64.7 [] unit_conversion 7.189095719331299 success True biochemical_inhibition Stopped Flow CO2 Hydrase Assay using recombinant CA isoforms. 5 Table 2 reports compound 8b Ki = 64.7 nM for hCA II; the table caption identifies the assay as a Stopped Flow CO2 Hydrase Assay. Figure 3 maps the hCA II–compound 8b complex to PDB 7NH8. auto_single_measurement only accepted activity measurement [1] 1 structures\7NH8\7NH8_metadata.json point structures/7NH8/7nh8_ligand.sdf structures/7NH8/7nh8_ligand.cif structures/7NH8/7nh8_complex.cif 7NIN classic LsAA9A Lentinus similis Na Na Cinnamtannin B1 (1) "[""UFK""]" 1 IC50 IC50 = = 0.46 ± 0.04 mM 460000.0 [] unit_conversion 3.3372421683184257 success True biochemical_inhibition AZCL-HEC LPMO activity assay with pure cinnamtannin B1; concentration-response inhibition. 9 “Cinnamtannin B1 inhibited the LPMO with an IC50 of 0.46 ± 0.04 mM.” Page 6 identifies the pure-cinnamtannin-B1 complex as PDB 7NIN. auto_single_measurement only accepted activity measurement [1] 1 structures\7NIN\7NIN_metadata.json point structures/7NIN/7nin_protein.pdb structures/7NIN/7nin_pocket.pdb structures/7NIN/7nin_ligand.sdf structures/7NIN/7nin_ligand.pdb structures/7NIN/7nin_ligand.cif structures/7NIN/7nin_complex.pdb structures/7NIN/7nin_complex.cif 7NIY classic E. coli NfsA Escherichia coli Na Na FMN (second FMN ligand) "[""FMN""]" 2 Ki Ki = = 7 μM 7000.0 [] unit_conversion 5.154901959985743 success True biochemical_inhibition Steady-state NfsA inhibition assay with nitrofurazone; FMN inhibition parameter for nitrofurazone. 13 Figure 8 caption prints: “Ki nitrofurazone 7 μM”. Page 12 states FMN binds to oxidised and reduced enzyme forms and gives inhibition versus nitrofurazone and NADPH. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\7NIY\7NIY_metadata.json point structures/7NIY/7niy_protein.pdb structures/7NIY/7niy_pocket.pdb structures/7NIY/7niy_ligand.sdf structures/7NIY/7niy_ligand.pdb structures/7NIY/7niy_ligand.cif structures/7NIY/7niy_complex.pdb structures/7NIY/7niy_complex.cif 7NL6 classic DC-SIGN Na 6-His-tagged DC-SIGN CRD construct Na 1s "[""UH8""]" 1 Kd Kd = = 160 (151–170) µM 160000.0 [] unit_conversion 3.795880017344075 success True direct_binding Isothermal titration calorimetry (ITC) of monovalent glycomimetic 1s with recombinant DC-SIGN CRD. 6 Figure 3 identifies initial screening hit 1s with K_D = 160 (151–170) µM; the paper describes ITC measurement of monovalent ligands with DC-SIGN CRD. auto_single_measurement only accepted activity measurement [1] 1 structures\7NL6\7NL6_metadata.json point structures/7NL6/7nl6_protein.pdb structures/7NL6/7nl6_pocket.pdb structures/7NL6/7nl6_ligand.sdf structures/7NL6/7nl6_ligand.pdb structures/7NL6/7nl6_ligand.cif structures/7NL6/7nl6_complex.pdb structures/7NL6/7nl6_complex.cif 7NLD classic Programmed cell death 1 ligand 1 (PD-L1) human PD-L1 residues 18-134 Na 8g "[""UGZ""]" 1 IC50 IC50 = = 2.07 ± 0.04 nM 2.07 [] unit_conversion 8.684029654543082 success True biochemical_inhibition HTRF PD-1/PD-L1 complex dissociation assay at 5 nM inhibitor screening concentration, followed by IC50 determination. 7 Table 4 reports compound 8g with IC50 2.07 ± 0.04 nM; the text identifies 8g as one of the two compounds for which half-maximal inhibitory concentration was successfully determined. auto_single_measurement only accepted activity measurement [1] 1 structures\7NLD\7NLD_metadata.json point structures/7NLD/7nld_protein.pdb structures/7NLD/7nld_pocket.pdb structures/7NLD/7nld_ligand.sdf structures/7NLD/7nld_ligand.pdb structures/7NLD/7nld_ligand.cif structures/7NLD/7nld_complex.pdb structures/7NLD/7nld_complex.cif 7NLN classic ArgB Mycobacterium tuberculosis Na Na N-acetyl-glutamate (NAG) "[""NLG""]" 1 Kd Kd = = 56 ± 5 µM 56000.0 [] unit_conversion 4.251811972993799 success True direct_binding ITC, ArgB–NAG. 32 Table 1 reports NAG ITC Kd 56 ± 5 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NLN\7NLN_metadata.json point structures/7NLN/7nln_protein.pdb structures/7NLN/7nln_pocket.pdb structures/7NLN/7nln_ligand.sdf structures/7NLN/7nln_ligand.pdb structures/7NLN/7nln_ligand.cif structures/7NLN/7nln_complex.pdb structures/7NLN/7nln_complex.cif 7NLP classic ArgB Mycobacterium tuberculosis Na Na L-canavanine "[""GGB""]" 1 Kd Kd = = 4.5 ± 1.2; 4.8 ± 1.0; 6.4 ± 1.2; 34 ± 6.7; 35 ± 5.1; 137 ± 26 µM 4500.0 [] unit_conversion 5.346787486224656 success True direct_binding ITC; six-site sequential-binding model. 32 Table 1 footnote prints the six L-canavanine Kd values from a sequential-binding model. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7NLP\7NLP_metadata.json point structures/7NLP/7nlp_protein.pdb structures/7NLP/7nlp_pocket.pdb structures/7NLP/7nlp_ligand.sdf structures/7NLP/7nlp_ligand.pdb structures/7NLP/7nlp_ligand.cif structures/7NLP/7nlp_complex.pdb structures/7NLP/7nlp_complex.cif 7NM2 classic MLKL Na MLKL N-terminal executioner domain, residues 2-154 Na Cpd 5 "[""UJ5""]" 1 Kd Kd = = 50 ± 4 μM 50000.0 [] unit_conversion 4.301029995663981 success True direct_binding Protein-detected 2D 1H,15N NMR titration; Table 1. 5 Table 1 reports Cpd 5 K_D = 50 ± 4 μM; Figure 4 caption maps the Cpd 5 complex to PDB 7NM2. auto_single_measurement only accepted activity measurement [1] 1 structures\7NM2\7NM2_metadata.json point structures/7NM2/7nm2_protein.pdb structures/7NM2/7nm2_pocket.pdb structures/7NM2/7nm2_ligand.sdf structures/7NM2/7nm2_ligand.pdb structures/7NM2/7nm2_ligand.cif structures/7NM2/7nm2_complex.pdb structures/7NM2/7nm2_complex.cif 7NM4 classic MLKL Na MLKL N-terminal executioner domain, residues 2-154 Na Cpd 3 "[""UJ8""]" 1 Kd Kd = = 1807 ± 348 μM 1807000.0 [] unit_conversion 2.743041847439068 success True direct_binding Protein-detected 2D 1H,15N NMR titration; Table 1. 5 Table 1 reports Cpd 3 K_D = 1807 ± 348 μM; Figure 3 caption identifies the Cpd 3 complex as PDB 7NM4. auto_single_measurement only accepted activity measurement [1] 1 structures\7NM4\7NM4_metadata.json point structures/7NM4/7nm4_protein.pdb structures/7NM4/7nm4_pocket.pdb structures/7NM4/7nm4_ligand.sdf structures/7NM4/7nm4_ligand.pdb structures/7NM4/7nm4_ligand.cif structures/7NM4/7nm4_complex.pdb structures/7NM4/7nm4_complex.cif 7NM5 classic MLKL Na MLKL N-terminal executioner domain, residues 2-154 Na Cpd 7 "[""UJ2""]" 1 Kd Kd = = 50 ± 17 μM 50000.0 [] unit_conversion 4.301029995663981 success True direct_binding Protein-detected 2D 1H,15N NMR titration; Table 1. 5 Table 1 reports Cpd 7 K_D = 50 ± 17 μM; Figure 4 caption identifies the Cpd 7 complex as PDB 7NM5. auto_single_measurement only accepted activity measurement [1] 1 structures\7NM5\7NM5_metadata.json point structures/7NM5/7nm5_protein.pdb structures/7NM5/7nm5_pocket.pdb structures/7NM5/7nm5_ligand.sdf structures/7NM5/7nm5_ligand.pdb structures/7NM5/7nm5_ligand.cif structures/7NM5/7nm5_complex.pdb structures/7NM5/7nm5_complex.cif 7NMA extended 14-3-3 sigma Na 14-3-3sigmaDeltaC, C-terminally truncated after T231 Na 13-mer Amot-p130 peptide "[""CHAIN:P""]" 1 Kd Kd ~ ~ 100 μM 100000.0 [] unit_conversion 4.0 success True direct_binding Fluorescence-polarization titration of 14-3-3σ against FITC-labelled 13-mer Amot-p130 peptide. 2 Fig. 1C prints the 14-3-3σ affinity as “~ 100” μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NMA\7NMA_metadata.json point structures/7NMA/7nma_protein.pdb structures/7NMA/7nma_pocket.pdb structures/7NMA/7nma_ligand.pdb structures/7NMA/7nma_ligand.cif structures/7NMA/7nma_complex.pdb structures/7NMA/7nma_complex.cif 7NNB classic ArgB Mycobacterium tuberculosis Na Na 2,8-bis(trifluoromethyl)quinolin-4-ol "[""97Q""]" 1 Kd Kd = = 7.7 ± 0.8 µM 7700.0 [] unit_conversion 5.113509274827518 success True direct_binding ITC measurement reported in Table 1. 32 Table 1 lists NMR711 with ITC Kd 7.7 ± 0.8 µM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7NNB\7NNB_metadata.json point structures/7NNB/7nnb_protein.pdb structures/7NNB/7nnb_pocket.pdb structures/7NNB/7nnb_ligand.sdf structures/7NNB/7nnb_ligand.pdb structures/7NNB/7nnb_ligand.cif structures/7NNB/7nnb_complex.pdb structures/7NNB/7nnb_complex.cif 7NNZ classic ArgF Mycobacterium tuberculosis Na Na 5-methyl-4-phenylthiazol-2-amine "[""PTZ""]" 1 Kd Kd = = 161 ± 20 µM 161000.0 [] unit_conversion 3.79317412396815 success True direct_binding ITC measurement reported in Table 4. 33 Table 4 lists NMR007 with ITC Kd 161 ± 20 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NNZ\7NNZ_metadata.json point structures/7NNZ/7nnz_protein.pdb structures/7NNZ/7nnz_pocket.pdb structures/7NNZ/7nnz_ligand.sdf structures/7NNZ/7nnz_ligand.pdb structures/7NNZ/7nnz_ligand.cif structures/7NNZ/7nnz_complex.pdb structures/7NNZ/7nnz_complex.cif 7NOU extended ArgF Mycobacterium tuberculosis Na Na (3,5-dichlorophenyl)boronic acid "[""NMR""]" 1 Kd Kd = = 120 ± 30 µM 120000.0 [] unit_conversion 3.920818753952375 success True direct_binding ITC measurement reported in Table 4. 34 Table 4 lists NMR812 with ITC Kd 120 ± 30 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NOU\7NOU_metadata.json point structures/7NOU/7nou_protein.pdb structures/7NOU/7nou_pocket.pdb structures/7NOU/7nou_ligand.pdb structures/7NOU/7nou_ligand.cif structures/7NOU/7nou_complex.pdb structures/7NOU/7nou_complex.cif 7NQ1 extended BRD2 human Na Na compound 36 (6-((S)-hydroxy(phenyl)methyl)-N2-methyl-N4-((1S,2S)-2-methylcyclopropyl)pyridine-2,4-dicarboxamide) "[""ULK""]" 2 pKd Kd = = 8.0 unitless 10.0 [] p_metric_transform 8.0 success True direct_binding BD2 BROMOscan binding assay. 9 Table 6 reports for compound 36 and BRD2: BD2 BROMOscan pKd 8.0. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7NQ1\7NQ1_metadata.json point structures/7NQ1/7nq1_ligand.sdf structures/7NQ1/7nq1_ligand.cif structures/7NQ1/7nq1_complex.cif 7NQM classic Mycobacterium tuberculosis Cytochrome P450 CYP121 Mycobacterium tuberculosis untagged CYP121A1 Na compound 10 "[""UMZ""]" 1 Kd Kd = = 483 ± 76 μM 483000.0 [] unit_conversion 3.3160528692484874 success True direct_binding UV–Visible spectrophotometry; compounds screened at 300 μM. 6 Table 2 reports compound 10 with Kd 483 ± 76 μM; Table 2 is UV–Visible spectrophotometric data against CYP121A1. auto_single_measurement only accepted activity measurement [1] 1 structures\7NQM\7NQM_metadata.json point structures/7NQM/7nqm_protein.pdb structures/7NQM/7nqm_pocket.pdb structures/7NQM/7nqm_ligand.sdf structures/7NQM/7nqm_ligand.pdb structures/7NQM/7nqm_ligand.cif structures/7NQM/7nqm_complex.pdb structures/7NQM/7nqm_complex.cif 7NQN classic Mycobacterium tuberculosis Cytochrome P450 CYP121 Mycobacterium tuberculosis untagged CYP121A1 Na compound 14 "[""UMT""]" 1 Kd Kd ~ ~ 100 μM 100000.0 [] unit_conversion 4.0 success True direct_binding Isothermal titration calorimetry (ITC) measurement of compound 14 against CYP121A1. 5 “Isothermal titration calorimetry (ITC) was attempted with 14 … In these experiments, 14 showed lower affinity (Kd: ~100 μM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7NQN\7NQN_metadata.json point structures/7NQN/7nqn_protein.pdb structures/7NQN/7nqn_pocket.pdb structures/7NQN/7nqn_ligand.sdf structures/7NQN/7nqn_ligand.pdb structures/7NQN/7nqn_ligand.cif structures/7NQN/7nqn_complex.pdb structures/7NQN/7nqn_complex.cif 7NR4 classic PRMT6 Na Na Na 3a "[""UO2""]" 1 IC50 IC50 = = 0.5 ± 0.1 µM 500.0 [] unit_conversion 6.301029995663981 success True biochemical_inhibition PRMT6 inhibitory activity; average ± SD of three IC50 values from three experiments. 2 Table 1 reports compound 3a: PRMT6 IC50 = 0.5 ± 0.1 µM. The adjoining text identifies the co-crystal structure of 3a with PRMT6 as PDB entry 7NR4. auto_single_measurement only accepted activity measurement [1] 1 structures\7NR4\7NR4_metadata.json point structures/7NR4/7nr4_protein.pdb structures/7NR4/7nr4_pocket.pdb structures/7NR4/7nr4_ligand.sdf structures/7NR4/7nr4_ligand.pdb structures/7NR4/7nr4_ligand.cif structures/7NR4/7nr4_complex.pdb structures/7NR4/7nr4_complex.cif 7NTB classic human carbonic anhydrase II (hCA II) human Na Na photoprobe 3 (benzophenone-based sulfonamide inhibitor) "[""URH""]" 1 Ki Ki = = 1050 nM 1050.0 [] unit_conversion 5.978810700930062 success True biochemical_inhibition Stopped-flow CO2 hydrase assay; Table 1 reports inhibition data of photoprobes 1–3 against hCA I–XIV. 3 Table 1 lists hCA II Ki for photoprobe 3 as 1050 nM; the text identifies these as in vitro inhibitory assays by a stopped-flow CO2 hydrase assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7NTB\7NTB_metadata.json point structures/7NTB/7ntb_protein.pdb structures/7NTB/7ntb_pocket.pdb structures/7NTB/7ntb_ligand.sdf structures/7NTB/7ntb_ligand.pdb structures/7NTB/7ntb_ligand.cif structures/7NTB/7ntb_complex.pdb structures/7NTB/7ntb_complex.cif 7NUG classic Influenza A polymerase acidic (PA) subunit N-terminal endonuclease domain Influenza A/California/07/2009(H1N1) PA-Nter, first 196 amino acids, with residues 51-72 replaced by a GS linker wild-type orientin "[""USE""]" 1 IC50 IC50 = = 42 nM 42.0 [] unit_conversion 7.376750709602099 success True biochemical_inhibition AlphaScreen titration curve for orientin. 6 Figure 2A caption states that the orientin AlphaScreen titration curve reveals an IC50 value of 42 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NUG\7NUG_metadata.json point structures/7NUG/7nug_protein.pdb structures/7NUG/7nug_pocket.pdb structures/7NUG/7nug_ligand.sdf structures/7NUG/7nug_ligand.pdb structures/7NUG/7nug_ligand.cif structures/7NUG/7nug_complex.pdb structures/7NUG/7nug_complex.cif 7NUS extended MDM2 (HDM2) Na Na Na CMR19 "[""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F""]" 1 IC50 IC50 = = 0.18 nM 0.18 [] unit_conversion 9.744727494896694 success True biochemical_inhibition TR-FRET p53-derived-peptide displacement assay measuring inhibition of the MDM2–p53 interaction. 8 “CMR19 exhibited picomolar potency ... with an IC50 value of 0.18 nM”; the assay assessed inhibition of the interaction between MDM2 and a p53-derived peptide. The MDM2/CMR19 coordinates are assigned PDB code 7NUS on page 11. auto_single_measurement only accepted activity measurement [1] 1 structures\7NUS\7NUS_metadata.json point structures/7NUS/7nus_protein.pdb structures/7NUS/7nus_pocket.pdb structures/7NUS/7nus_ligand.pdb structures/7NUS/7nus_ligand.cif structures/7NUS/7nus_complex.pdb structures/7NUS/7nus_complex.cif 7NWQ extended CkCBM9.3 Caldicellulosiruptor kristjanssonii CkCBM9.3, residues Lys1072-Leu1252, with C-terminal linker Lys1253-Pro1265 Na cellotriose "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 2.1 ± 0.14 ×10⁻⁴ M 210000.0 [] unit_conversion 3.6777807052660805 success True direct_binding Isothermal titration calorimetry (ITC); Table 2, parameters for binding of CBM9.3 to oligosaccharides. 8 Table 2 reports K_D = 2.1 ± 0.14 (×10⁻⁴ M) for cellotriose. auto_single_measurement only accepted activity measurement [1] 1 structures\7NWQ\7NWQ_metadata.json point structures/7NWQ/7nwq_ligand.cif structures/7NWQ/7nwq_complex.cif 7NWY extended alpha carbonic anhydrase from Schistosoma mansoni (SmCA) Schistosoma mansoni recombinant SmCA Na compound 22a; 4-(3-(4-fluorophenyl)ureido)benzenesulfonamide "[""WWZ""]" 1 Ki Ki = = 54.3 nM 54.3 [] unit_conversion 7.265200170411153 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay using recombinant SmCA; Table 1. 3 Table 1 reports Ki = 54.3 nM for compound 22a against SmCA; the text identifies recombinant SmCA and the stopped-flow assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7NWY\7NWY_metadata.json point structures/7NWY/7nwy_ligand.sdf structures/7NWY/7nwy_ligand.cif structures/7NWY/7nwy_complex.cif 7NXJ classic human CDK13/Cyclin K human Na Na THZ531 "[""5I1""]" 1 IC50 IC50 = = 657.1 nM 657.1 [] unit_conversion 6.182368532809485 success True biochemical_inhibition Recombinant CDK13/Cyclin K radioactive kinase inhibition assay. 33 Table 1 explicitly identifies 10a as THZ531 and reports a CDK13 IC50 of 657.1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NXJ\7NXJ_metadata.json point structures/7NXJ/7nxj_protein.pdb structures/7NXJ/7nxj_pocket.pdb structures/7NXJ/7nxj_ligand.sdf structures/7NXJ/7nxj_ligand.pdb structures/7NXJ/7nxj_ligand.cif structures/7NXJ/7nxj_complex.pdb structures/7NXJ/7nxj_complex.cif 7NXK classic human CDK12/Cyclin K human Na Na BSJ-01-175 "[""UUB""]" 1 IC50 IC50 = = 156 nM 156.0 [] unit_conversion 6.806875401645538 success True biochemical_inhibition Recombinant CDK12/Cyclin K radioactive kinase inhibition assay. 35 Table 3 explicitly identifies 22a as BSJ-01-175 and reports a CDK12 IC50 of 156 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7NXK\7NXK_metadata.json point structures/7NXK/7nxk_protein.pdb structures/7NXK/7nxk_pocket.pdb structures/7NXK/7nxk_ligand.sdf structures/7NXK/7nxk_ligand.pdb structures/7NXK/7nxk_ligand.cif structures/7NXK/7nxk_complex.pdb structures/7NXK/7nxk_complex.cif 7O08 classic human METTL3-METTL14 complex human METTL3 residues 354-580; METTL14 residues 106-396 Na Compound 5 (ADO_AB_075) "[""UXE""]" 1 IC50 IC50 = = 0.79 µM 790.0 [] unit_conversion 6.102372908709558 success True biochemical_inhibition TR-FRET assay; means of at least three measurements. 2 Table 1 reports compound 5 with IC50 0.79 µM; the table footnote defines a TR-FRET assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7O08\7O08_metadata.json point structures/7O08/7o08_protein.pdb structures/7O08/7o08_pocket.pdb structures/7O08/7o08_ligand.sdf structures/7O08/7o08_ligand.pdb structures/7O08/7o08_ligand.cif structures/7O08/7o08_complex.pdb structures/7O08/7o08_complex.cif 7O09 classic human METTL3-METTL14 complex human METTL3 residues 354-580; METTL14 residues 106-396 Na Compound 7 (ADO_AC_074) "[""UXK""]" 1 IC50 IC50 = = 0.28 µM 280.0 [] unit_conversion 6.552841968657781 success True biochemical_inhibition TR-FRET assay; means of at least three measurements. 3 Table 2 reports compound 7 with IC50 0.28 µM; the table footnote defines a TR-FRET assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7O09\7O09_metadata.json point structures/7O09/7o09_protein.pdb structures/7O09/7o09_pocket.pdb structures/7O09/7o09_ligand.sdf structures/7O09/7o09_ligand.pdb structures/7O09/7o09_ligand.cif structures/7O09/7o09_complex.pdb structures/7O09/7o09_complex.cif 7O0L classic human METTL3-METTL14 complex human METTL3 residues 354-580; METTL14 residues 106-396 Na Compound 8 (ADO_AC_093) "[""UXW""]" 1 IC50 IC50 = = 0.037 µM 37.0 [] unit_conversion 7.431798275933005 success True biochemical_inhibition TR-FRET assay; means of at least three measurements. 3 Table 2 reports compound 8 with IC50 0.037 µM; the table footnote defines a TR-FRET assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7O0L\7O0L_metadata.json point structures/7O0L/7o0l_protein.pdb structures/7O0L/7o0l_pocket.pdb structures/7O0L/7o0l_ligand.sdf structures/7O0L/7o0l_ligand.pdb structures/7O0L/7o0l_ligand.cif structures/7O0L/7o0l_complex.pdb structures/7O0L/7o0l_complex.cif 7O1B classic human phosphomannomutase 2 (PMM2) human recombinant hPMM2, 246 aa, expressed with an N-terminal PreScission-cleavable His6-tag that was removed before crystallization wild-type glucose-1,6-bisphosphate (Glc-1,6-P2) "[""G16""]" 1 Kd Kd = = 0.98 μM 980.0 [] unit_conversion 6.008773924307505 success True direct_binding ITC, Figure 1D. 5 Figure 1D prints KD = 0.98 μM for Glc-1,6-P2 binding to hPMM2; Table 1 assigns 7O1B to WT hPMM2 co-crystallized with Glc-1,6-P2. auto_single_measurement only accepted activity measurement [1] 1 structures\7O1B\7O1B_metadata.json point structures/7O1B/7o1b_protein.pdb structures/7O1B/7o1b_pocket.pdb structures/7O1B/7o1b_ligand.sdf structures/7O1B/7o1b_ligand.pdb structures/7O1B/7o1b_ligand.cif structures/7O1B/7o1b_complex.pdb structures/7O1B/7o1b_complex.cif 7O1F extended PCNA (proliferating cell nuclear antigen) Chaetomium thermophilum Ct PCNA in complex with Ct PolD4 PIP peptide residues 21-35 Na Ct PolD4 PIP peptide (21KHQSTL NFKHRVTKP35) "[""CHAIN:J"", ""CHAIN:K"", ""CHAIN:M"", ""CHAIN:O""]" 1 Kd Kd = = 22 ± 0.6 μM 22000.0 [] unit_conversion 4.657577319177793 success True direct_binding Isothermal titration calorimetry at 25 °C; Ct PCNA titrated with synthetic Ct PolD4 PIP peptide; fitted to a single-site model (1 peptide:1 PCNA protomer). 5 The paper reports that ITC determined a dissociation constant (Kd) of 22 ± 0.6 μM at 25 °C for the Ct PolD4 PIP peptide–Ct PCNA interaction; the peptide–PCNA complex is deposited as PDB 7O1F. auto_single_measurement only accepted activity measurement [1] 1 structures\7O1F\7O1F_metadata.json point structures/7O1F/7o1f_protein.pdb structures/7O1F/7o1f_pocket.pdb structures/7O1F/7o1f_ligand.pdb structures/7O1F/7o1f_ligand.cif structures/7O1F/7o1f_complex.pdb structures/7O1F/7o1f_complex.cif 7O1U classic furin human Arg33-Gly634 Na inhibitor 1 (BEV241) "[""UYN""]" 1 Ki Ki = = 3.3 ± 0.1 μM 3300.0 [] unit_conversion 5.481486060122112 success True biochemical_inhibition Enzyme-kinetic inhibition assay; Table 2 reports Ki for inhibitor 1 against furin. 5 Table 2, “Ki of Inhibitors 1 and 2 for Selected PCs”, reports inhibitor 1: furin 3.3 ± 0.1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7O1U\7O1U_metadata.json point structures/7O1U/7o1u_protein.pdb structures/7O1U/7o1u_pocket.pdb structures/7O1U/7o1u_ligand.sdf structures/7O1U/7o1u_ligand.pdb structures/7O1U/7o1u_ligand.cif structures/7O1U/7o1u_complex.pdb structures/7O1U/7o1u_complex.cif 7O1W classic furin human Arg33-Gly634 Na inhibitor 2 (mi307) "[""UYQ""]" 1 Ki Ki = = 3.1 ± 0.2 μM 3100.0 [] unit_conversion 5.508638306165727 success True biochemical_inhibition Enzyme-kinetic inhibition assay; Table 2 reports Ki for inhibitor 2 against furin. 5 Table 2 reports inhibitor 2: furin 3.1 ± 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7O1W\7O1W_metadata.json point structures/7O1W/7o1w_protein.pdb structures/7O1W/7o1w_pocket.pdb structures/7O1W/7o1w_ligand.sdf structures/7O1W/7o1w_ligand.pdb structures/7O1W/7o1w_ligand.cif structures/7O1W/7o1w_complex.pdb structures/7O1W/7o1w_complex.cif 7O1Y classic furin human Arg33-Gly634 Na inhibitor 2 (mi307) "[""UYQ""]" 1 Ki Ki = = 3.1 ± 0.2 μM 3100.0 [] unit_conversion 5.508638306165727 success True biochemical_inhibition Enzyme-kinetic inhibition assay; Table 2 reports Ki for inhibitor 2 against furin. 5 Table 2 reports inhibitor 2: furin 3.1 ± 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7O1Y\7O1Y_metadata.json point structures/7O1Y/7o1y_protein.pdb structures/7O1Y/7o1y_pocket.pdb structures/7O1Y/7o1y_ligand.sdf structures/7O1Y/7o1y_ligand.pdb structures/7O1Y/7o1y_ligand.cif structures/7O1Y/7o1y_complex.pdb structures/7O1Y/7o1y_complex.cif 7O29 classic human METTL3-METTL14 complex human METTL3 residues 354-580; METTL14 residues 106-396 Na Compound 20 (ADO_AD_044) "[""UZE""]" 1 IC50 IC50 = = 0.038 µM 38.0 [] unit_conversion 7.42021640338319 success True biochemical_inhibition TR-FRET assay; means of at least three measurements. 5 Table 4 reports compound 20 with IC50 0.038 µM; the table footnote defines a TR-FRET assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7O29\7O29_metadata.json point structures/7O29/7o29_protein.pdb structures/7O29/7o29_pocket.pdb structures/7O29/7o29_ligand.sdf structures/7O29/7o29_ligand.pdb structures/7O29/7o29_ligand.cif structures/7O29/7o29_complex.pdb structures/7O29/7o29_complex.cif 7O2A classic SMYD3 human SMYD3 amino acids 1-428; N-terminal TEV-cleavable 6xHis purification tag, cleaved before final purification Na compound 15 "[""UZT""]" 1 IC50 IC50 = = 2.45E-8 M 24.5 [] unit_conversion 7.610833915635467 success True biochemical_inhibition SMYD3 scintillation proximity assay (SPA); table reports SMYD3 SPA IC50. 8 Table I lists compound 15, stereoisomer (S), with SMYD3 SPA IC50 = 2.45 E-8 M. auto_single_measurement only accepted activity measurement [1] 1 structures\7O2A\7O2A_metadata.json point structures/7O2A/7o2a_protein.pdb structures/7O2A/7o2a_pocket.pdb structures/7O2A/7o2a_ligand.sdf structures/7O2A/7o2a_ligand.pdb structures/7O2A/7o2a_ligand.cif structures/7O2A/7o2a_complex.pdb structures/7O2A/7o2a_complex.cif 7O2B classic SMYD3 human SMYD3 amino acids 1-428; N-terminal TEV-cleavable 6xHis purification tag, cleaved before final purification Na compound 6 "[""UZQ""]" 1 IC50 IC50 = = 12 µM 12000.0 [] unit_conversion 4.920818753952375 success True biochemical_inhibition SMYD3 scintillation proximity assay (SPA) used to confirm catalytic inhibition of the selected benzodiazepine hit. 6 Figure 2 caption states that compound 6 showed the lowest SMYD3 SPA IC50 of 12 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7O2B\7O2B_metadata.json point structures/7O2B/7o2b_protein.pdb structures/7O2B/7o2b_pocket.pdb structures/7O2B/7o2b_ligand.sdf structures/7O2B/7o2b_ligand.pdb structures/7O2B/7o2b_ligand.cif structures/7O2B/7o2b_complex.pdb structures/7O2B/7o2b_complex.cif 7O2E classic human METTL3-METTL14 complex human METTL3 residues 354-580; METTL14 residues 106-396 Na Compound 21 (ADO_AD_089) "[""UZH""]" 1 IC50 IC50 = = 0.032 µM 32.0 [] unit_conversion 7.494850021680094 success True biochemical_inhibition TR-FRET assay; means of at least three measurements. 5 Table 4 reports compound 21 with IC50 0.032 µM; the table footnote defines a TR-FRET assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7O2E\7O2E_metadata.json point structures/7O2E/7o2e_protein.pdb structures/7O2E/7o2e_pocket.pdb structures/7O2E/7o2e_ligand.sdf structures/7O2E/7o2e_ligand.pdb structures/7O2E/7o2e_ligand.cif structures/7O2E/7o2e_complex.pdb structures/7O2E/7o2e_complex.cif 7O2F classic human METTL3-METTL14 complex human METTL3 residues 354-580; METTL14 residues 106-396 Na Compound 22 (UZH2) "[""UZ5""]" 1 IC50 IC50 = = 0.005 µM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition TR-FRET assay; means of at least three measurements. 5 Table 4 reports compound 22 (UZH2) with IC50 0.005 µM; the table footnote defines a TR-FRET assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7O2F\7O2F_metadata.json point structures/7O2F/7o2f_protein.pdb structures/7O2F/7o2f_pocket.pdb structures/7O2F/7o2f_ligand.sdf structures/7O2F/7o2f_ligand.pdb structures/7O2F/7o2f_ligand.cif structures/7O2F/7o2f_complex.pdb structures/7O2F/7o2f_complex.cif 7O2Y extended Sandercyanin fluorescent protein (SFP) Canadian walleye (Stizostedion vitreum) Monomeric SFP variant V71E Biliverdin IX-alpha (BV) "[""BLA""]" 1 Kd Kd = = 1.97 ± 0.12 μM 1970.0 [] unit_conversion 5.7055337738384075 success True direct_binding Binding curve of BV to V71E monomeric SFP protein. 4 Fig. 2B caption prints: “The Kd of BV to wild-type protein is 7.06 μM (±0.71 μM), V71E, L135E, and Y142A have Kd values of 1.97 (±0.12) μM, 1.2 (±0.10) μM, and 4.1 (±0.09) μM, respectively.” Page 7 maps PDB 7O2Y to V71E. auto_single_measurement only accepted activity measurement [1] 1 structures\7O2Y\7O2Y_metadata.json point structures/7O2Y/7o2y_ligand.cif structures/7O2Y/7o2y_complex.cif 7O35 classic SARS-CoV-2 nucleocapsid protein N-CTD SARS-CoV-2 N-CTD, residues 256-364 Na GTP "[""GTP""]" 1 Kd Kd = = 196 μM 196000.0 [] unit_conversion 3.7077439286435236 success True direct_binding Microscale thermophoresis (MST) measurement of N-CTD binding to GTP. 3 “NCTD presents a Kd value of 196 μM for GTP”. auto_single_measurement only accepted activity measurement [1] 1 structures\7O35\7O35_metadata.json point structures/7O35/7o35_protein.pdb structures/7O35/7o35_pocket.pdb structures/7O35/7o35_ligand.sdf structures/7O35/7o35_ligand.pdb structures/7O35/7o35_ligand.cif structures/7O35/7o35_complex.pdb structures/7O35/7o35_complex.cif 7O36 classic SARS-CoV-2 nucleocapsid protein N-CTD SARS-CoV-2 N-CTD, residues 256-364 Na GTP "[""GTP""]" 1 Kd Kd = = 196 μM 196000.0 [] unit_conversion 3.7077439286435236 success True direct_binding Microscale thermophoresis (MST) measurement of N-CTD binding to GTP. 3 “NCTD presents a Kd value of 196 μM for GTP”. auto_single_measurement only accepted activity measurement [1] 1 structures\7O36\7O36_metadata.json point structures/7O36/7o36_protein.pdb structures/7O36/7o36_pocket.pdb structures/7O36/7o36_ligand.sdf structures/7O36/7o36_ligand.pdb structures/7O36/7o36_ligand.cif structures/7O36/7o36_complex.pdb structures/7O36/7o36_complex.cif 7O3K classic Sandercyanin fluorescent protein (SFP) Canadian walleye (Stizostedion vitreum) Monomeric SFP variant L135E Biliverdin IX-alpha (BV) "[""BLA""]" 1 Kd Kd = = 1.2 ± 0.10 μM 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding Binding curve of BV to L135E monomeric SFP protein. 4 Fig. 2B caption prints: “The Kd of BV to wild-type protein is 7.06 μM (±0.71 μM), V71E, L135E, and Y142A have Kd values of 1.97 (±0.12) μM, 1.2 (±0.10) μM, and 4.1 (±0.09) μM, respectively.” Page 7 maps PDB 7O3K to L135E. auto_single_measurement only accepted activity measurement [1] 1 structures\7O3K\7O3K_metadata.json point structures/7O3K/7o3k_protein.pdb structures/7O3K/7o3k_pocket.pdb structures/7O3K/7o3k_ligand.sdf structures/7O3K/7o3k_ligand.pdb structures/7O3K/7o3k_ligand.cif structures/7O3K/7o3k_complex.pdb structures/7O3K/7o3k_complex.cif 7O48 classic alpha carbonic anhydrase from Schistosoma mansoni (SmCA) Schistosoma mansoni recombinant SmCA Na compound 23; 4-(2-(3-(4-iodophenyl)thioureido)ethyl)benzenesulfonamide "[""TKE""]" 1 Ki Ki = = 37.6 nM 37.6 [] unit_conversion 7.424812155072339 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay using recombinant SmCA; Table 1. 3 Table 1 reports Ki = 37.6 nM for compound 23 against SmCA; the text identifies recombinant SmCA and the stopped-flow assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7O48\7O48_metadata.json point structures/7O48/7o48_protein.pdb structures/7O48/7o48_pocket.pdb structures/7O48/7o48_ligand.sdf structures/7O48/7o48_ligand.pdb structures/7O48/7o48_ligand.cif structures/7O48/7o48_complex.pdb structures/7O48/7o48_complex.cif 7O4D classic human quinone reductase 2 (hQR2) human Na Na YB-537 "[""V1Z""]" 1 IC50 IC50 = = 0.003 µM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Comparative SAR evaluation in QR2 activity assay; Table/Figure 2D. 4 Figure 2D lists YB-537 with QR2 IC50 0.003 µM; the caption identifies these as QR2 inhibitors evaluated by activity assays. auto_single_measurement only accepted activity measurement [1] 1 structures\7O4D\7O4D_metadata.json point structures/7O4D/7o4d_protein.pdb structures/7O4D/7o4d_pocket.pdb structures/7O4D/7o4d_ligand.sdf structures/7O4D/7o4d_ligand.pdb structures/7O4D/7o4d_ligand.cif structures/7O4D/7o4d_complex.pdb structures/7O4D/7o4d_complex.cif 7O4G classic human phosphomannomutase 2 (PMM2) human recombinant hPMM2, 246 aa, expressed with an N-terminal PreScission-cleavable His6-tag that was removed before crystallization wild-type glucose-1,6-bisphosphate (Glc-1,6-P2) "[""G16""]" 1 Kd Kd = = 0.98 μM 980.0 [] unit_conversion 6.008773924307505 success True direct_binding ITC, Figure 1D. 5 Figure 1D prints KD = 0.98 μM for Glc-1,6-P2 binding to hPMM2; Table 1 assigns 7O4G to WT hPMM2 soaked with Glc-1,6-P2. auto_single_measurement only accepted activity measurement [1] 1 structures\7O4G\7O4G_metadata.json point structures/7O4G/7o4g_protein.pdb structures/7O4G/7o4g_pocket.pdb structures/7O4G/7o4g_ligand.sdf structures/7O4G/7o4g_ligand.pdb structures/7O4G/7o4g_ligand.cif structures/7O4G/7o4g_complex.pdb structures/7O4G/7o4g_complex.cif 7O4N classic Staphylococcus aureus m1A22-tRNA methyltransferase (SaTrmK) Staphylococcus aureus Na Na S-adenosylmethionine (SAM) "[""SAM""]" 1 Kd Kd = = 39 ± 4 µM 39000.0 [] unit_conversion 4.4089353929735005 success True direct_binding Isothermal titration calorimetry (ITC), single-site 1:1 protein:ligand binding model, 20 °C. 4 “Binding of SAM to SaTrmK yielded a KD of 39 ± 4 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7O4N\7O4N_metadata.json point structures/7O4N/7o4n_protein.pdb structures/7O4N/7o4n_pocket.pdb structures/7O4N/7o4n_ligand.sdf structures/7O4N/7o4n_ligand.pdb structures/7O4N/7o4n_ligand.cif structures/7O4N/7o4n_complex.pdb structures/7O4N/7o4n_complex.cif 7O4O classic Staphylococcus aureus m1A22-tRNA methyltransferase (SaTrmK) Staphylococcus aureus Na Na S-adenosylhomocysteine (SAH) "[""SAH""]" 1 Kd Kd = = 0.94 ± 0.05 µM 940.0 [] unit_conversion 6.026872146400301 success True direct_binding Isothermal titration calorimetry (ITC), single-site 1:1 protein:ligand binding model, 20 °C. 4 “binding of SAH resulted in a KD of 0.94 ± 0.05 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7O4O\7O4O_metadata.json point structures/7O4O/7o4o_protein.pdb structures/7O4O/7o4o_pocket.pdb structures/7O4O/7o4o_ligand.sdf structures/7O4O/7o4o_ligand.pdb structures/7O4O/7o4o_ligand.cif structures/7O4O/7o4o_complex.pdb structures/7O4O/7o4o_complex.cif 7O6N extended ERH-2 Caenorhabditis elegans ERH-2deltaC, residues 1-99, bound to PID-3pep; PID-3pep construct residues 171-203 with ordered residues 177-193 and 179-193 Na PID-3pep "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.65 ± 0.08 µM 650.0 [] unit_conversion 6.187086643357144 success True direct_binding Isothermal titration calorimetry of ERH-2 with PID-3pep; reported stoichiometry N~1 (0.97). 7 “We determined a dissociation constant (Kd) of 0.65 µM and a stoichiometry N~1 (0.97)” for ERH-2/PID-3pep; Table 1 prints Kd 0.65 ± 0.08 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7O6N\7O6N_metadata.json point structures/7O6N/7o6n_protein.pdb structures/7O6N/7o6n_pocket.pdb structures/7O6N/7o6n_ligand.pdb structures/7O6N/7o6n_ligand.cif structures/7O6N/7o6n_complex.pdb structures/7O6N/7o6n_complex.cif 7O6R classic Hsc70 bovine Hsc70(aa1-554), truncated after residue 554 E213A; D214A 1-IND (1H-indazole) "[""LZ1""]" 1 Kd Kd = = 1.1 mM 1100000.0 [] unit_conversion 2.9586073148417746 success True direct_binding Protein-based XL-ALSOFAST-HMQC titration of 1H-indazole with 480 μM bHsc70ΔC; Figure 9 reports the mean K_D from four fitted receptor-signal shifts. 10 Figure 9 explicitly reports “K_D,mean 1.1 ± 0.2 mM” for 1H-indazole titration to bHsc70ΔC. auto_single_measurement only accepted activity measurement [1] 1 structures\7O6R\7O6R_metadata.json point structures/7O6R/7o6r_protein.pdb structures/7O6R/7o6r_pocket.pdb structures/7O6R/7o6r_ligand.sdf structures/7O6R/7o6r_ligand.pdb structures/7O6R/7o6r_ligand.cif structures/7O6R/7o6r_complex.pdb structures/7O6R/7o6r_complex.cif 7O7J classic HIPK3 human HIPK3 kinase domain residues 159-562 wild-type abemaciclib "[""6ZV""]" 2 Kd Kd = = 0.8 nM 0.8 [] unit_conversion 9.096910013008056 success True direct_binding Surface plasmon resonance single-cycle kinetic measurement of abemaciclib binding to immobilized HIPK3 (Fig. 7a). 10 Fig. 7a explicitly reports HIPK3 KD = 0.8 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7O7J\7O7J_metadata.json point structures/7O7J/7o7j_protein.pdb structures/7O7J/7o7j_pocket.pdb structures/7O7J/7o7j_ligand.sdf structures/7O7J/7o7j_ligand.pdb structures/7O7J/7o7j_ligand.cif structures/7O7J/7o7j_complex.pdb structures/7O7J/7o7j_complex.cif 7O7K classic DYRK1A human DYRK1A kinase domain residues 127-485 with an N-terminal His6 affinity tag followed by a TEV protease cleavage site Na abemaciclib "[""6ZV""]" 2 Kd Kd = = 8.6 nM 8.6 [] unit_conversion 8.065501548756432 success True direct_binding Surface plasmon resonance single-cycle kinetic measurement of abemaciclib binding to immobilized DYRK1A (Fig. 7a). 10 Fig. 7a explicitly reports DYRK1A KD = 8.6 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7O7K\7O7K_metadata.json point structures/7O7K/7o7k_protein.pdb structures/7O7K/7o7k_pocket.pdb structures/7O7K/7o7k_ligand.sdf structures/7O7K/7o7k_ligand.pdb structures/7O7K/7o7k_ligand.cif structures/7O7K/7o7k_complex.pdb structures/7O7K/7o7k_complex.cif 7O9H classic FtsY Escherichia coli FtsY-NG domain with C-terminal hexahistidine tag Na pppGpp "[""0O2""]" 1 Kd Kd = = 66.6 ± 18.6 µM 66600.0 [] unit_conversion 4.176525770829699 success True direct_binding Microscale thermophoresis (MST). 5 Figure 3e lists the MST K_D for (Ec)FtsY binding pppGpp as 66.6 ± 18.6 µM; the ITC entry is n.d. and is not a reported value. auto_single_measurement only accepted activity measurement [1] 1 structures\7O9H\7O9H_metadata.json point structures/7O9H/7o9h_protein.pdb structures/7O9H/7o9h_pocket.pdb structures/7O9H/7o9h_ligand.sdf structures/7O9H/7o9h_ligand.pdb structures/7O9H/7o9h_ligand.cif structures/7O9H/7o9h_complex.pdb structures/7O9H/7o9h_complex.cif 7OA1 extended alpha carbonic anhydrase from Schistosoma mansoni (SmCA) Schistosoma mansoni recombinant SmCA Na compound 27; 4-(2-(3-(4-iodophenyl)ureido)ethyl)benzenesulfonamide "[""TKQ""]" 1 Ki Ki = = 71.3 nM 71.3 [] unit_conversion 7.146910470148135 success True biochemical_inhibition Stopped-flow CO2-hydration inhibition assay using recombinant SmCA; Table 1. 3 Table 1 reports Ki = 71.3 nM for compound 27 against SmCA; the text identifies recombinant SmCA and the stopped-flow assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7OA1\7OA1_metadata.json point structures/7OA1/7oa1_ligand.sdf structures/7OA1/7oa1_ligand.cif structures/7OA1/7oa1_complex.cif 7OA4 extended La Crosse virus L-protein La Crosse virus N-terminal 183 residues Na L-742,001 "[""0N8""]" 1 Kd Kd = = 0.614 ± 0.098 µM 614.0 [] unit_conversion 6.211831628858832 success True direct_binding Microscale thermophoresis (MST) direct binding measurement in the presence of MnCl2. 5 Table 2 reports an MST Kd of 0.614 ± 0.098 µM for L-742,001; the text states binding was lost without metal ions. auto_single_measurement only accepted activity measurement [1] 1 structures\7OA4\7OA4_metadata.json point structures/7OA4/7oa4_ligand.sdf structures/7OA4/7oa4_ligand.cif structures/7OA4/7oa4_complex.cif 7OAJ classic CASK Na CASK pseudokinase domain, residues 1-337, with an N-terminal histidine tag Na compound 7 "[""V6E""]" 1 Kd Kd = = 0.22 ± 0.06 µM 220.0 [] unit_conversion 6.657577319177793 success True direct_binding Isothermal titration calorimetry of compound 7 binding to CASK. 4 Table 2A reports compound 7, CASK ITC KD = 0.22 ± 0.06 µM. Figure 2 identifies the CASK–7 structure as PDB 7OAJ. auto_single_measurement only accepted activity measurement [1] 1 structures\7OAJ\7OAJ_metadata.json point structures/7OAJ/7oaj_protein.pdb structures/7OAJ/7oaj_pocket.pdb structures/7OAJ/7oaj_ligand.sdf structures/7OAJ/7oaj_ligand.pdb structures/7OAJ/7oaj_ligand.cif structures/7OAJ/7oaj_complex.pdb structures/7OAJ/7oaj_complex.cif 7OAK classic CASK Na CASK pseudokinase domain, residues 1-337, with an N-terminal histidine tag Na compound 26 "[""V6B""]" 1 Kd Kd = = 22 ± 1 nM 22.0 [] unit_conversion 7.657577319177793 success True direct_binding Isothermal titration calorimetry of compound 26 binding to CASK. 7 The text states that ITC confirmed CASK KD values of 38 ± 6 nM and 22 ± 1 nM for compounds 25 and 26, respectively. Figure 3 maps compound 26 bound to CASK to PDB 7OAK. auto_single_measurement only accepted activity measurement [1] 1 structures\7OAK\7OAK_metadata.json point structures/7OAK/7oak_protein.pdb structures/7OAK/7oak_pocket.pdb structures/7OAK/7oak_ligand.sdf structures/7OAK/7oak_ligand.pdb structures/7OAK/7oak_ligand.cif structures/7OAK/7oak_complex.pdb structures/7OAK/7oak_complex.cif 7OAL classic CASK Na CASK pseudokinase domain, residues 1-337, with an N-terminal histidine tag Na compound 25 "[""V62""]" 1 Kd Kd = = 38 ± 6 nM 38.0 [] unit_conversion 7.42021640338319 success True direct_binding Isothermal titration calorimetry of compound 25 binding to CASK. 7 The text states that ITC confirmed CASK KD values of 38 ± 6 nM and 22 ± 1 nM for compounds 25 and 26, respectively. The supplied structure title identifies PDB 7OAL as the CASK–25 complex; the paper lists 7OAL among deposited CASK inhibitor complexes. auto_single_measurement only accepted activity measurement [1] 1 structures\7OAL\7OAL_metadata.json point structures/7OAL/7oal_protein.pdb structures/7OAL/7oal_pocket.pdb structures/7OAL/7oal_ligand.sdf structures/7OAL/7oal_ligand.pdb structures/7OAL/7oal_ligand.cif structures/7OAL/7oal_complex.pdb structures/7OAL/7oal_complex.cif 7OC7 classic LasB Na Na Na 7d "[""V85""]" 1 IC50 IC50 = = 1.2 ± 0.1 µM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition In vitro LasB inhibitory activity; Table 1. 2 Table 1 lists compound 7d with IC50 1.2 ± 0.1 µM against LasB; Figure 2 identifies 7OC7 as LasB in complex with 7d. auto_single_measurement only accepted activity measurement [1] 1 structures\7OC7\7OC7_metadata.json point structures/7OC7/7oc7_protein.pdb structures/7OC7/7oc7_pocket.pdb structures/7OC7/7oc7_ligand.sdf structures/7OC7/7oc7_ligand.pdb structures/7OC7/7oc7_ligand.cif structures/7OC7/7oc7_complex.pdb structures/7OC7/7oc7_complex.cif 7OCV classic TNKS1 human Na Na M2912 (30g); 3-[4-(1-Hydroxy-1-methyl-ethyl)-phenyl]-6-methyl-2H-pyrrolo[1,2-a]pyrazin-1-one "[""V8B""]" 2 Kd Kd < < 2 nM 2.0 [] unit_conversion 8.698970004336019 success True direct_binding Isothermal titration calorimetry (ITC) binding measurement; affinity was too tight for exact resolution. 10 The text states that binding affinity of M2912 (30g) could only be estimated to be KD < 2 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 3 structures\7OCV\7OCV_metadata.json point structures/7OCV/7ocv_protein.pdb structures/7OCV/7ocv_pocket.pdb structures/7OCV/7ocv_ligand.sdf structures/7OCV/7ocv_ligand.pdb structures/7OCV/7ocv_ligand.cif structures/7OCV/7ocv_complex.pdb structures/7OCV/7ocv_complex.cif 7OD6 extended Hepatitis B core protein (HBc) Human hepatitis B virus (HBV), genotype D, strain ayw HBc capsid-like particle (HBc-CLP), genotype D, strain ayw WT GSLLGRMKGA (P2) "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 68 ± 4 µM 68000.0 [] unit_conversion 4.167491087293763 success True direct_binding Isothermal titration calorimetry; six repeats; P2 binding to WT-HBc. 9 Table 1 reports WT-HBc with P2: KD 68 ± 4 µM (6 repeats). auto_single_measurement only accepted activity measurement [1] 1 structures\7OD6\7OD6_metadata.json point structures/7OD6/7od6_protein.pdb structures/7OD6/7od6_pocket.pdb structures/7OD6/7od6_ligand.pdb structures/7OD6/7od6_ligand.cif structures/7OD6/7od6_complex.pdb structures/7OD6/7od6_complex.cif 7OD8 extended Hepatitis B core protein (HBc) Human hepatitis B virus (HBV), genotype D, strain ayw HBc capsid-like particle (HBc-CLP), genotype D, strain ayw L60V GSLLGRMKGA (P2) "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 127 ± 19 µM 127000.0 [] unit_conversion 3.8961962790440428 success True direct_binding Isothermal titration calorimetry; three repeats; P2 binding to L60V-HBc; stoichiometry fixed at 0.5. 9 Table 1 reports L60V-HBc with P2: KD 127 ± 19 µM (3 repeats). auto_single_measurement only accepted activity measurement [1] 1 structures\7OD8\7OD8_metadata.json point structures/7OD8/7od8_protein.pdb structures/7OD8/7od8_pocket.pdb structures/7OD8/7od8_ligand.pdb structures/7OD8/7od8_ligand.cif structures/7OD8/7od8_complex.pdb structures/7OD8/7od8_complex.cif 7OE5 extended BRD2 human C-terminal bromodomain of human BRD2 Na compound 23 (GSK809; N5-hydroxycyclohexyl-N3-methyl-1-phenylethyl-1H-pyrazole-3,5-dicarboxamide) "[""V9H""]" 1 pIC50 IC50 = = 6.6 pIC50 251.18864315095823 [] p_metric_transform 6.6 success True biochemical_inhibition TR-FRET pIC50; n=8. 9 Table 7 prints BRD2 BD2/BD1 pIC50 for compound 23 as 6.6 (8)/4.6 (1). auto_single_measurement only accepted activity measurement [1] 1 structures\7OE5\7OE5_metadata.json point structures/7OE5/7oe5_ligand.sdf structures/7OE5/7oe5_ligand.cif structures/7OE5/7oe5_complex.cif 7OE6 extended BRD2 human C-terminal bromodomain of human BRD2 Na compound 24 (GSK743; N4-hydroxycyclohexyl-N2-methyl-5-phenylethyl-furan-2,4-dicarboxamide) "[""V9K""]" 1 pIC50 IC50 = = 7.3 pIC50 50.11872336272725 [] p_metric_transform 7.3 success True biochemical_inhibition TR-FRET pIC50; n=2. 9 Table 7 prints BRD2 BD2/BD1 pIC50 for compound 24 as 7.3 (2)/4.7 (3). auto_single_measurement only accepted activity measurement [1] 1 structures\7OE6\7OE6_metadata.json point structures/7OE6/7oe6_ligand.sdf structures/7OE6/7oe6_ligand.cif structures/7OE6/7oe6_complex.cif 7OEN extended Hepatitis B core protein (HBc) Human hepatitis B virus (HBV), genotype D, strain ayw HBc capsid-like particle (HBc-CLP), genotype D, strain ayw P5T GSLLGRMKGA (P2) "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 74 ± 5 µM 74000.0 [] unit_conversion 4.130768280269024 success True direct_binding Isothermal titration calorimetry; six repeats; P2 binding to P5T-HBc. 9 Table 1 reports P5T-HBc with P2: KD 74 ± 5 µM (6 repeats). auto_single_measurement only accepted activity measurement [1] 1 structures\7OEN\7OEN_metadata.json point structures/7OEN/7oen_protein.pdb structures/7OEN/7oen_pocket.pdb structures/7OEN/7oen_ligand.pdb structures/7OEN/7oen_ligand.cif structures/7OEN/7oen_complex.pdb structures/7OEN/7oen_complex.cif 7OEV extended Hepatitis B core protein (HBc) Human hepatitis B virus (HBV), genotype D, strain ayw HBc capsid-like particle (HBc-CLP), genotype D, strain ayw F97L GSLLGRMKGA (P2) "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 155 ± 14 µM 155000.0 [] unit_conversion 3.809668301829708 success True direct_binding Isothermal titration calorimetry; five repeats; P2 binding to F97L-HBc. 9 Table 1 reports F97L-HBc with P2: KD 155 ± 14 µM (5 repeats). auto_single_measurement only accepted activity measurement [1] 1 structures\7OEV\7OEV_metadata.json point structures/7OEV/7oev_protein.pdb structures/7OEV/7oev_pocket.pdb structures/7OEV/7oev_ligand.pdb structures/7OEV/7oev_ligand.cif structures/7OEV/7oev_complex.pdb structures/7OEV/7oev_complex.cif 7OFS classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 PLpro domain of SARS-CoV-2 NSP3, residues 746-1060, expressed with an N-terminal His6-TEV construct; cleavage leaves GA wild type YRL; 4-(2-hydroxyethyl)phenol "[""YRL""]" 1 IC50 IC50 = = 6.68 ± 1.20 μM 6680.0 [] unit_conversion 5.175223537524454 success True biochemical_inhibition PLpro deISGylation activity assay using ISG15-Rhodamine substrate. 6 Fig. 3 reports YRL IC50: 6.68 ± 1.20 μM in the deISGylation activity assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7OFS\7OFS_metadata.json point structures/7OFS/7ofs_protein.pdb structures/7OFS/7ofs_pocket.pdb structures/7OFS/7ofs_ligand.sdf structures/7OFS/7ofs_ligand.pdb structures/7OFS/7ofs_ligand.cif structures/7OFS/7ofs_complex.pdb structures/7OFS/7ofs_complex.cif 7OFT classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 PLpro domain of SARS-CoV-2 NSP3, residues 746-1060, expressed with an N-terminal His6-TEV construct; cleavage leaves GA wild type HBA; p-hydroxybenzaldehyde "[""HBA""]" 2 Kd Kd ~ ~ 400 μM 400000.0 [] unit_conversion 3.3979400086720375 success True direct_binding nanoDSF fluorescence-quenching binding measurement with PLpro. 4 The paper states that nanoDSF resulted in a Kd value of ~400 μM for HBA. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7OFT\7OFT_metadata.json point structures/7OFT/7oft_protein.pdb structures/7OFT/7oft_pocket.pdb structures/7OFT/7oft_ligand.sdf structures/7OFT/7oft_ligand.pdb structures/7OFT/7oft_ligand.cif structures/7OFT/7oft_complex.pdb structures/7OFT/7oft_complex.cif 7OFU extended SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 PLpro domain of SARS-CoV-2 NSP3, residues 746-1060, expressed with an N-terminal His6-TEV construct; cleavage leaves GA wild type HE9; methyl 3,4-dihydroxybenzoate; 3,4-dihydroxybenzoic acid, methyl ester "[""HE9""]" 2 Kd Kd = = 1 mM 1000000.0 [] unit_conversion 3.0 success True direct_binding nanoDSF fluorescence-quenching binding measurement with PLpro. 4 The paper states that nanoDSF resulted in a Kd value of 1 mM for HE9. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7OFU\7OFU_metadata.json point structures/7OFU/7ofu_ligand.sdf structures/7OFU/7ofu_ligand.cif structures/7OFU/7ofu_complex.cif 7OFV extended EphA4 ligand binding domain (EphA4-LBD) Na EphA4-LBD residues 29-209 with an N-terminal His tag C204A 150D4 "[""CHAIN:B""]" 1 Kd Kd = = 113 nM 113.0 [] unit_conversion 6.94692155651658 success True direct_binding Isothermal titration calorimetry of 150D4 binding to recombinant EphA4-LBD. 9 The paper states that ITC indicated a Kd of 113 nM for 150D4 versus EphA4-LBD and, in the same results section, identifies the X-ray EphA4-LBD–150D4 complex (PDB ID 7OFV). auto_single_measurement only accepted activity measurement [1] 1 structures\7OFV\7OFV_metadata.json point structures/7OFV/7ofv_protein.pdb structures/7OFV/7ofv_pocket.pdb structures/7OFV/7ofv_ligand.pdb structures/7OFV/7ofv_ligand.cif structures/7OFV/7ofv_complex.pdb structures/7OFV/7ofv_complex.cif 7OFW extended Nontypeable Haemophilus influenzae SapA Nontypeable Haemophilus influenzae SapA residues 33-560 with the signal peptide excluded; S3C cleavage site Na heme "[""HEM""]" 1 Kd Kd = = 282 ± 18.3 µM 282000.0 [] unit_conversion 3.549750891680639 success True direct_binding Isothermal titration calorimetry of purified SapA with hemin; binding stoichiometry fixed to 1. 8 “Therefore, the binding stoichiometry of the reaction was fixed to 1, allowing a Kd of 282 ± 18.3 μM to be proposed.” auto_single_measurement only accepted activity measurement [1] 1 structures\7OFW\7OFW_metadata.json point structures/7OFW/7ofw_protein.pdb structures/7OFW/7ofw_pocket.pdb structures/7OFW/7ofw_ligand.pdb structures/7OFW/7ofw_ligand.cif structures/7OFW/7ofw_complex.pdb structures/7OFW/7ofw_complex.cif 7OFY classic SmoF SQ binding protein Agrobacterium tumefaciens Na Na SQGro sulfoquinovosyl glycerol "[""VCW""]" 1 Kd Kd = = 0.29 ± 0.17 µM 290.0 [] unit_conversion 6.537602002101044 success True direct_binding ITC measurement of recombinant SmoF binding SQGro. 2 “we produced recombinant SmoF ... and demonstrated that it binds SQGro with Kd = 0.29 ± 0.17 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7OFY\7OFY_metadata.json point structures/7OFY/7ofy_protein.pdb structures/7OFY/7ofy_pocket.pdb structures/7OFY/7ofy_ligand.sdf structures/7OFY/7ofy_ligand.pdb structures/7OFY/7ofy_ligand.cif structures/7OFY/7ofy_complex.pdb structures/7OFY/7ofy_complex.cif 7OHI extended AP2 alpha ear Na AP2 alpha ear complexed with FCHO1 C-block peptide Na FCHO1 C-block peptide, residues 426-448, SEEQVSKNLFGPPLESAFDHED "[""CHAIN:B""]" 1 Kd Kd ~ ~ 50 μM 50000.0 [] unit_conversion 4.301029995663981 success True direct_binding Isothermal titration calorimetry of FCHO1 C peptide binding to the α-appendage. 11 Fig. 9 caption: “ITC showing ~50 μM KD binding of LFGPPL to α-appendage.” The text identifies the FCHO1 C peptide as residues 426-448. auto_single_measurement only accepted activity measurement [1] 1 structures\7OHI\7OHI_metadata.json point structures/7OHI/7ohi_protein.pdb structures/7OHI/7ohi_pocket.pdb structures/7OHI/7ohi_ligand.pdb structures/7OHI/7ohi_ligand.cif structures/7OHI/7ohi_complex.pdb structures/7OHI/7ohi_complex.cif 7OIQ extended AP2 Mu2 subunit Na Recombinant His6-tagged Cmu2 Na FCHO2-derived C-block WxxPhi peptide, SDLLAWDPLFG "[""POLYMER_ENTITY:2""]" 1 Kd Kd ~ ~ 25 μM 25000.0 [] unit_conversion 4.6020599913279625 success True direct_binding Isothermal titration calorimetry of the FCHO2 WxxL peptide with Cμ2. 10 The text states that an FCHO2 peptide incorporating the WxxL motif bound Cμ2 by ITC with a KD of ~25 μM. The methods identify the FCHO2-derived C-block peptide as SDLLAWDPLFG. auto_single_measurement only accepted activity measurement [1] 1 structures\7OIQ\7OIQ_metadata.json point structures/7OIQ/7oiq_ligand.cif structures/7OIQ/7oiq_complex.cif 7OIT extended AP2 Mu2 subunit Na Recombinant His6-tagged Cmu2 Na FCHO2-derived C-block WxxPhi peptide, SDLLAWDPLFG "[""CHAIN:BBB""]" 1 Kd Kd ~ ~ 25 μM 25000.0 [] unit_conversion 4.6020599913279625 success True direct_binding Isothermal titration calorimetry of the FCHO2 WxxL peptide with Cμ2. 10 The text states that an FCHO2 peptide incorporating the WxxL motif bound Cμ2 by ITC with a KD of ~25 μM. The methods identify the FCHO2-derived C-block peptide as SDLLAWDPLFG. auto_single_measurement only accepted activity measurement [1] 1 structures\7OIT\7OIT_metadata.json point structures/7OIT/7oit_ligand.cif structures/7OIT/7oit_complex.cif 7OJ6 classic Pseudomonas aeruginosa LpxA Pseudomonas aeruginosa Na Na compound 1 "[""VFE""]" 1 IC50 IC50 = = 400 nM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition Purified P. aeruginosa LpxA enzymatic inhibition. 3 Compound 1 inhibited P. aeruginosa LpxA with IC50 = 400 nM; the accession list maps 7OJ6 to P. aeruginosa LpxA–compound 1. auto_single_measurement only accepted activity measurement [1] 1 structures\7OJ6\7OJ6_metadata.json point structures/7OJ6/7oj6_protein.pdb structures/7OJ6/7oj6_pocket.pdb structures/7OJ6/7oj6_ligand.sdf structures/7OJ6/7oj6_ligand.pdb structures/7OJ6/7oj6_ligand.cif structures/7OJ6/7oj6_complex.pdb structures/7OJ6/7oj6_complex.cif 7OJ9 extended SNX9 SH3 domain Homo sapiens Human SNX9 SH3 residues 1-64; N-terminal His-tagged expression construct with the tag removed before NMR Na EEEV nsP3 peptide "[""CHAIN:B""]" 1 Kd Kd = = 0.3 ± 0.03 µM 300.0 [] unit_conversion 6.522878745280337 success True direct_binding ITC measurement of SNX9 SH3 binding to EEEV nsP3 peptide; 25°C. 7 Table 2 lists EEEV nsP3 binding to SNX9 SH3 with Kd 0.3 ± 0.03 µM; the methods state ITC experiments were performed at 25°C. auto_single_measurement only accepted activity measurement [1] 1 structures\7OJ9\7OJ9_metadata.json point structures/7OJ9/7oj9_protein.pdb structures/7OJ9/7oj9_pocket.pdb structures/7OJ9/7oj9_ligand.pdb structures/7OJ9/7oj9_ligand.cif structures/7OJ9/7oj9_complex.pdb structures/7OJ9/7oj9_complex.cif 7OJP classic Pseudomonas aeruginosa LpxA Pseudomonas aeruginosa Na Na compound 1 "[""VFE""]" 1 IC50 IC50 = = 400 nM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition Purified P. aeruginosa LpxA enzymatic inhibition. 3 Compound 1 inhibited P. aeruginosa LpxA with IC50 = 400 nM; the accession list maps 7OJP to P. aeruginosa LpxA–compound 1. auto_single_measurement only accepted activity measurement [1] 1 structures\7OJP\7OJP_metadata.json point structures/7OJP/7ojp_protein.pdb structures/7OJP/7ojp_pocket.pdb structures/7OJP/7ojp_ligand.sdf structures/7OJP/7ojp_ligand.pdb structures/7OJP/7ojp_ligand.cif structures/7OJP/7ojp_complex.pdb structures/7OJP/7ojp_complex.cif 7OJQ classic Pseudomonas aeruginosa LpxA Pseudomonas aeruginosa Na Na compound 7 "[""VJE""]" 1 IC50 IC50 = = 230 nM 230.0 [] unit_conversion 6.638272163982407 success True biochemical_inhibition Table 1, purified P. aeruginosa LpxA enzyme inhibition. 4 Table 1 reports compound 7, IC50 230 nM, against P. aeruginosa LpxA. auto_single_measurement only accepted activity measurement [1] 1 structures\7OJQ\7OJQ_metadata.json point structures/7OJQ/7ojq_protein.pdb structures/7OJQ/7ojq_pocket.pdb structures/7OJQ/7ojq_ligand.sdf structures/7OJQ/7ojq_ligand.pdb structures/7OJQ/7ojq_ligand.cif structures/7OJQ/7ojq_complex.pdb structures/7OJQ/7ojq_complex.cif 7OJY classic Pseudomonas aeruginosa LpxA Pseudomonas aeruginosa Na Na compound 6 "[""VGQ""]" 1 IC50 IC50 = = 180 nM 180.0 [] unit_conversion 6.7447274948966935 success True biochemical_inhibition Table 1, purified P. aeruginosa LpxA enzyme inhibition. 4 Table 1 reports compound 6, IC50 180 nM, against P. aeruginosa LpxA. auto_single_measurement only accepted activity measurement [1] 1 structures\7OJY\7OJY_metadata.json point structures/7OJY/7ojy_protein.pdb structures/7OJY/7ojy_pocket.pdb structures/7OJY/7ojy_ligand.sdf structures/7OJY/7ojy_ligand.pdb structures/7OJY/7ojy_ligand.cif structures/7OJY/7ojy_complex.pdb structures/7OJY/7ojy_complex.cif 7OKC classic Escherichia coli LpxA Escherichia coli Na Na compound 1 "[""VFE""]" 1 IC50 IC50 > > 50 µM 50000.0 [] unit_conversion 4.301029995663981 success True biochemical_inhibition Purified E. coli LpxA enzymatic inhibition. 3 Figure 3 explicitly states E. coli IC50 > 50 µM for compound 1; the accession list assigns 7OKC to the E. coli LpxA–compound 1 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKC\7OKC_metadata.json point structures/7OKC/7okc_protein.pdb structures/7OKC/7okc_pocket.pdb structures/7OKC/7okc_ligand.sdf structures/7OKC/7okc_ligand.pdb structures/7OKC/7okc_ligand.cif structures/7OKC/7okc_complex.pdb structures/7OKC/7okc_complex.cif 7OKE classic BCL6 human Na Na compound 2 "[""VHQ""]" 1 IC50 IC50 = = 2.72 µM 2720.0 [] unit_conversion 5.565431095965801 success True biochemical_inhibition TR-FRET biochemical assay of BCL6 BTB domain with a short corepressor peptide. 2 Figure 1 reports compound 2 TR-FRET IC50 2.72 µM; text identifies this as a biochemical TR-FRET assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKE\7OKE_metadata.json point structures/7OKE/7oke_protein.pdb structures/7OKE/7oke_pocket.pdb structures/7OKE/7oke_ligand.sdf structures/7OKE/7oke_ligand.pdb structures/7OKE/7oke_ligand.cif structures/7OKE/7oke_complex.pdb structures/7OKE/7oke_complex.cif 7OKF classic BCL6 human Na Na compound 8c "[""VH5""]" 1 IC50 IC50 = = 2.64 µM 2640.0 [] unit_conversion 5.578396073130168 success True biochemical_inhibition TR-FRET biochemical assay of BCL6 BTB domain with a short corepressor peptide. 5 Table 1 reports compound 8c TR-FRET IC50 2.64 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKF\7OKF_metadata.json point structures/7OKF/7okf_protein.pdb structures/7OKF/7okf_pocket.pdb structures/7OKF/7okf_ligand.sdf structures/7OKF/7okf_ligand.pdb structures/7OKF/7okf_ligand.cif structures/7OKF/7okf_complex.pdb structures/7OKF/7okf_complex.cif 7OKG classic BCL6 human Na Na compound 8e "[""VHB""]" 1 IC50 IC50 = = 1.82 µM 1820.0 [] unit_conversion 5.739928612014925 success True biochemical_inhibition TR-FRET biochemical assay of BCL6 BTB domain with a short corepressor peptide. 5 Table 1 reports compound 8e TR-FRET IC50 1.82 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKG\7OKG_metadata.json point structures/7OKG/7okg_protein.pdb structures/7OKG/7okg_pocket.pdb structures/7OKG/7okg_ligand.sdf structures/7OKG/7okg_ligand.pdb structures/7OKG/7okg_ligand.cif structures/7OKG/7okg_complex.pdb structures/7OKG/7okg_complex.cif 7OKH classic BCL6 human Na Na compound 8f "[""VHK""]" 1 IC50 IC50 = = 1.31 µM 1310.0 [] unit_conversion 5.882728704344236 success True biochemical_inhibition TR-FRET biochemical assay of BCL6 BTB domain with a short corepressor peptide. 5 Table 1 reports compound 8f TR-FRET IC50 1.31 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKH\7OKH_metadata.json point structures/7OKH/7okh_protein.pdb structures/7OKH/7okh_pocket.pdb structures/7OKH/7okh_ligand.sdf structures/7OKH/7okh_ligand.pdb structures/7OKH/7okh_ligand.cif structures/7OKH/7okh_complex.pdb structures/7OKH/7okh_complex.cif 7OKI classic BCL6 human Na Na compound 12b "[""VHZ""]" 1 IC50 IC50 = = 0.25 µM 250.0 [] unit_conversion 6.6020599913279625 success True biochemical_inhibition TR-FRET biochemical assay of BCL6 BTB domain with a short corepressor peptide. 7 Table 3 reports (R)-12b TR-FRET IC50 0.25 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKI\7OKI_metadata.json point structures/7OKI/7oki_protein.pdb structures/7OKI/7oki_pocket.pdb structures/7OKI/7oki_ligand.sdf structures/7OKI/7oki_ligand.pdb structures/7OKI/7oki_ligand.cif structures/7OKI/7oki_complex.pdb structures/7OKI/7oki_complex.cif 7OKK classic BCL6 human Na Na compound 12e "[""VH8""]" 1 IC50 IC50 = = 23.8 µM 23800.0 [] unit_conversion 4.623423042943488 success True biochemical_inhibition TR-FRET biochemical assay of BCL6 BTB domain with a short corepressor peptide. 7 Table 3 reports compound 12e TR-FRET IC50 23.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKK\7OKK_metadata.json point structures/7OKK/7okk_protein.pdb structures/7OKK/7okk_pocket.pdb structures/7OKK/7okk_ligand.sdf structures/7OKK/7okk_ligand.pdb structures/7OKK/7okk_ligand.cif structures/7OKK/7okk_complex.pdb structures/7OKK/7okk_complex.cif 7OKL classic BCL6 human Na Na compound 13e "[""VJ5""]" 1 IC50 IC50 = = 0.14 µM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition TR-FRET biochemical assay of BCL6 BTB domain with a short corepressor peptide. 8 Table 4 reports compound 13e TR-FRET IC50 0.14 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKL\7OKL_metadata.json point structures/7OKL/7okl_protein.pdb structures/7OKL/7okl_pocket.pdb structures/7OKL/7okl_ligand.sdf structures/7OKL/7okl_ligand.pdb structures/7OKL/7okl_ligand.cif structures/7OKL/7okl_complex.pdb structures/7OKL/7okl_complex.cif 7OKM classic BCL6 human Na Na compound 13g "[""VJ2""]" 1 IC50 IC50 = = 0.046 µM 46.0 [] unit_conversion 7.337242168318426 success True biochemical_inhibition TR-FRET biochemical assay of BCL6 BTB domain with a short corepressor peptide. 9 Table 5 reports compound 13g TR-FRET IC50 0.046 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OKM\7OKM_metadata.json point structures/7OKM/7okm_protein.pdb structures/7OKM/7okm_pocket.pdb structures/7OKM/7okm_ligand.sdf structures/7OKM/7okm_ligand.pdb structures/7OKM/7okm_ligand.cif structures/7OKM/7okm_complex.pdb structures/7OKM/7okm_complex.cif 7OLJ extended Tankyrase 2 (TNKS2) human Na Na OUL219 (compound 7) "[""VJN""]" 1 IC50 IC50 = = 22 µM 22000.0 [] unit_conversion 4.657577319177793 success True biochemical_inhibition Dose-response activity assay against a panel of human ARTs; Table 1. 3 Table 1 reports TNKS2 IC50 = 22 µM for compound 7 and maps its TNKS2 crystal structure to 7OLJ. auto_single_measurement only accepted activity measurement [1] 1 structures\7OLJ\7OLJ_metadata.json point structures/7OLJ/7olj_ligand.sdf structures/7OLJ/7olj_ligand.cif structures/7OLJ/7olj_complex.cif 7OLS classic MerTK kinase Na Na Na compound 21 "[""VJZ""]" 1 pIC50 IC50 = = 8.7 1.9952623149688828 [] p_metric_transform 8.7 success True biochemical_inhibition Mer enzyme biochemical assay; Table 3 SAR for pyrazole B-ring. 4 Table 3 reports compound 21: Mer enzyme pIC50 = 8.7. The paper maps compound 21 to PDB 7OLS. auto_single_measurement only accepted activity measurement [1] 1 structures\7OLS\7OLS_metadata.json point structures/7OLS/7ols_protein.pdb structures/7OLS/7ols_pocket.pdb structures/7OLS/7ols_ligand.sdf structures/7OLS/7ols_ligand.pdb structures/7OLS/7ols_ligand.cif structures/7OLS/7ols_complex.pdb structures/7OLS/7ols_complex.cif 7OLV classic MerTK kinase Na Na Na compound 22 "[""VK2""]" 1 pIC50 IC50 = = 8.8 1.584893192461111 [] p_metric_transform 8.8 success True biochemical_inhibition Mer enzyme biochemical assay; Table 3 SAR for pyrazole B-ring. 4 Table 3 reports compound 22: Mer enzyme pIC50 = 8.8. The paper maps compound 22 to PDB 7OLV. auto_single_measurement only accepted activity measurement [1] 1 structures\7OLV\7OLV_metadata.json point structures/7OLV/7olv_protein.pdb structures/7OLV/7olv_pocket.pdb structures/7OLV/7olv_ligand.sdf structures/7OLV/7olv_ligand.pdb structures/7OLV/7olv_ligand.cif structures/7OLV/7olv_complex.pdb structures/7OLV/7olv_complex.cif 7OLW extended BC2L-C lectin Burkholderia cenocepacia N-terminal domain, residues 1-131 Na 8c "[""VJW""]" 1 Kd Kd = = 2.36 ± 0.97 mM 2360000.0 [] unit_conversion 2.6270879970298937 success True direct_binding Surface plasmon resonance (SPR) affinity evaluation against rBC2L-CN. 4 Table 1 reports for 8c: SPR KD = 2.36 ± 0.97 mM; Figure 5 maps 8c to PDB 7OLW. auto_single_measurement only accepted activity measurement [1] 1 structures\7OLW\7OLW_metadata.json point structures/7OLW/7olw_ligand.sdf structures/7OLW/7olw_ligand.cif structures/7OLW/7olw_complex.cif 7ONF classic Rabbit muscle glycogen phosphorylase b (rmGPb) rabbit Na Na p-coumaroyl glucose (compound 5; 1-O-(4-coumaroyl)-beta-D-glucose) "[""VKK""]" 1 Ki Ki = = 31.4 ± 1.9 μM 31400.0 [] unit_conversion 4.503070351926785 success True biochemical_inhibition Enzymatic activity was measured in the direction of glycogen synthesis; Ki values were calculated from Km(app) versus inhibitor plots. The paper reports p-coumaroyl glucose as a competitive inhibitor of rmGPb. 4 “p-Coumaroyl glucose is a potent, competitive to Glc-1-P, inhibitor of rmGPb (Ki = 31.4 ± 1.9 μM)”. auto_single_measurement only accepted activity measurement [1] 1 structures\7ONF\7ONF_metadata.json point structures/7ONF/7onf_protein.pdb structures/7ONF/7onf_pocket.pdb structures/7ONF/7onf_ligand.sdf structures/7ONF/7onf_ligand.pdb structures/7ONF/7onf_ligand.cif structures/7ONF/7onf_complex.pdb structures/7ONF/7onf_complex.cif 7OOX extended PIM-1 Na Na Na ARC-3126 "[""CHAIN:B""]" 1 Kd Kd = = 1.8 ± 0.7 nM 1.8 [] unit_conversion 8.744727494896694 success True direct_binding Binding/displacement assay with TGLI or fluorescence-anisotropy readout; mean ± SEM, N = 2. 8 Table 2 reports ARC-3126 K_D = 1.8 ± 0.7 nM toward PIM-1; its footnote states K_D values were determined in binding/displacement assays with TGLI or FA readout. auto_single_measurement only accepted activity measurement [1] 1 structures\7OOX\7OOX_metadata.json point structures/7OOX/7oox_protein.pdb structures/7OOX/7oox_pocket.pdb structures/7OOX/7oox_ligand.pdb structures/7OOX/7oox_ligand.cif structures/7OOX/7oox_complex.pdb structures/7OOX/7oox_complex.cif 7OP0 extended complement C5 Na Na Na K92chemFE "[""CHAIN:C""]" 1 Kd Kd = = 0.41 nM 0.41 [] unit_conversion 9.387216143280265 success True direct_binding SPR multicycle kinetics experiment; mean equilibrium dissociation constant from n = 3 experiments. 3 Figure 2C labels K92chemFE with “mean K_D = 0.41 nM”; the caption identifies these as SPR multicycle kinetics measurements. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7OP0\7OP0_metadata.json point structures/7OP0/7op0_protein.pdb structures/7OP0/7op0_pocket.pdb structures/7OP0/7op0_ligand.pdb structures/7OP0/7op0_ligand.cif structures/7OP0/7op0_complex.pdb structures/7OP0/7op0_complex.cif 7OPJ classic Trypanosoma brucei PTR1 (TbPTR1) Trypanosoma brucei Na Na pyrimethamine (PYR) "[""CP6""]" 1 IC50 IC50 = = 0.090 µM 90.0 [] unit_conversion 7.045757490560675 success True biochemical_inhibition Direct spectrophotometric kinetic inhibition assay using purified recombinant TbPTR1; Table 1 reports TbPTR1 inhibition by PYR. 4 Table 1 lists PYR with TbPTR1 IC50 = 0.090 µM. The text immediately below states “IC50 TbPTR1 = 90 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7OPJ\7OPJ_metadata.json point structures/7OPJ/7opj_protein.pdb structures/7OPJ/7opj_pocket.pdb structures/7OPJ/7opj_ligand.sdf structures/7OPJ/7opj_ligand.pdb structures/7OPJ/7opj_ligand.cif structures/7OPJ/7opj_complex.pdb structures/7OPJ/7opj_complex.cif 7OPO extended RSK2 Homo sapiens (human) RSK2 N-terminal kinase domain, residues 39-351 Na ORF45(16-76) peptide "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H"", ""CHAIN:J"", ""CHAIN:L""]" 2 Kd Kd = = 4.3 nM 4.3 [] unit_conversion 8.366531544420413 success True direct_binding SPR binding-affinity summary for WT NTK with the ORF45 peptide; mutant NTK values are separately shown and are not transferred. 4 Fig. 2d lists the SPR-derived K_D table for ORF45 binding to NTK: “WT 4.3” nM. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\7OPO\7OPO_metadata.json point structures/7OPO/7opo_protein.pdb structures/7OPO/7opo_pocket.pdb structures/7OPO/7opo_ligand.pdb structures/7OPO/7opo_ligand.cif structures/7OPO/7opo_complex.pdb structures/7OPO/7opo_complex.cif 7OQQ classic PARP15 human catalytic domain Na TIQ-A (compound 1) "[""G18""]" 1 IC50 IC50 = = 230 nM 230.0 [] unit_conversion 6.638272163982407 success True biochemical_inhibition Dose-response activity assay against a panel of human ARTs; Table 1. 3 Table 1 reports PARP15 IC50 = 230 nM for compound 1 and maps its PARP15 crystal structure to 7OQQ. auto_single_measurement only accepted activity measurement [1] 1 structures\7OQQ\7OQQ_metadata.json point structures/7OQQ/7oqq_protein.pdb structures/7OQQ/7oqq_pocket.pdb structures/7OQQ/7oqq_ligand.sdf structures/7OQQ/7oqq_ligand.pdb structures/7OQQ/7oqq_ligand.cif structures/7OQQ/7oqq_complex.pdb structures/7OQQ/7oqq_complex.cif 7OR2 classic UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) Pseudomonas aeruginosa Na Na fragment 4 "[""9FH""]" 1 Kd Kd = = 2.88 ± 0.2 mM 2880000.0 [] unit_conversion 2.5406075122407694 success True direct_binding ITC affinity measurement. 2 Abstract: fragment 4 was shown by ITC to bind with an affinity of Kd = 2.88 ± 0.2 mM. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\7OR2\7OR2_metadata.json point structures/7OR2/7or2_protein.pdb structures/7OR2/7or2_pocket.pdb structures/7OR2/7or2_ligand.sdf structures/7OR2/7or2_ligand.pdb structures/7OR2/7or2_ligand.cif structures/7OR2/7or2_complex.pdb structures/7OR2/7or2_complex.cif 7ORZ classic UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) Pseudomonas aeruginosa Na Na fragment 18 "[""0IM""]" 1 Kd Kd = = 0.25 ± 0.04 mM 250000.0 [] unit_conversion 3.6020599913279625 success True direct_binding ITC; Table 2, 50 μM Pa MurB and 3.0 mM fragment. 57 Table 2 reports fragment 18 (CF3 analogue) Kd (mM) ITC = 0.25 ± 0.04. auto_single_measurement only accepted activity measurement [1] 1 structures\7ORZ\7ORZ_metadata.json point structures/7ORZ/7orz_protein.pdb structures/7ORZ/7orz_pocket.pdb structures/7ORZ/7orz_ligand.sdf structures/7ORZ/7orz_ligand.pdb structures/7ORZ/7orz_ligand.cif structures/7ORZ/7orz_complex.pdb structures/7ORZ/7orz_complex.cif 7OSE classic cytochrome bd-II type oxidase Escherichia coli AppC, AppB and AppX; AppC C-terminal His-tag affinity peptide; appCBX expressed from pET28b(+) Na aurachin D "[""0NI""]" 1 IC50 IC50 = = 1.1 μM 1100.0 [] unit_conversion 5.958607314841775 success True biochemical_inhibition Duroquinol:dioxygen oxidoreductase activity of isolated E. coli bd-II monitored by oxygen consumption; inhibition by aurachin D. 3 “we titrated the duroquinol:dioxygen oxidoreductase activity of our bd-II preparation with increasing amounts of aurachin C and D and determined the apparent IC50 to 7.1 and 1.1 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7OSE\7OSE_metadata.json point structures/7OSE/7ose_protein.pdb structures/7OSE/7ose_pocket.pdb structures/7OSE/7ose_ligand.sdf structures/7OSE/7ose_ligand.pdb structures/7OSE/7ose_ligand.cif structures/7OSE/7ose_complex.pdb structures/7OSE/7ose_complex.cif 7OSP classic PARP15 human catalytic domain Na OUL113 (compound 2) "[""0Q6""]" 1 IC50 IC50 = = 1.2 µM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition Dose-response activity assay against a panel of human ARTs; Table 1. 3 Table 1 reports PARP15 IC50 = 1.2 µM for compound 2 and maps its PARP15 crystal structure to 7OSP. auto_single_measurement only accepted activity measurement [1] 1 structures\7OSP\7OSP_metadata.json point structures/7OSP/7osp_protein.pdb structures/7OSP/7osp_pocket.pdb structures/7OSP/7osp_ligand.sdf structures/7OSP/7osp_ligand.pdb structures/7OSP/7osp_ligand.cif structures/7OSP/7osp_complex.pdb structures/7OSP/7osp_complex.cif 7OSS classic PARP15 human catalytic domain Na OUL194 (compound 4) "[""0SI""]" 1 IC50 IC50 > > 10 µM 10000.0 [] unit_conversion 5.0 success True biochemical_inhibition Dose-response activity assay against a panel of human ARTs; Table 1. 3 Table 1 reports PARP15 IC50 >10 µM for compound 4 and maps its PARP15 crystal structure to 7OSS. auto_single_measurement only accepted activity measurement [1] 1 structures\7OSS\7OSS_metadata.json point structures/7OSS/7oss_protein.pdb structures/7OSS/7oss_pocket.pdb structures/7OSS/7oss_ligand.sdf structures/7OSS/7oss_ligand.pdb structures/7OSS/7oss_ligand.cif structures/7OSS/7oss_complex.pdb structures/7OSS/7oss_complex.cif 7OSX classic PARP15 human catalytic domain Na OUL205 (compound 5) "[""0UI""]" 1 IC50 IC50 = = 1.4 µM 1400.0 [] unit_conversion 5.853871964321762 success True biochemical_inhibition Dose-response activity assay against a panel of human ARTs; Table 1. 3 Table 1 reports PARP15 IC50 = 1.4 µM for compound 5 and maps its PARP15 crystal structure to 7OSX. auto_single_measurement only accepted activity measurement [1] 1 structures\7OSX\7OSX_metadata.json point structures/7OSX/7osx_protein.pdb structures/7OSX/7osx_pocket.pdb structures/7OSX/7osx_ligand.sdf structures/7OSX/7osx_ligand.pdb structures/7OSX/7osx_ligand.cif structures/7OSX/7osx_complex.pdb structures/7OSX/7osx_complex.cif 7OTF classic PARP15 human catalytic domain Na OUL213 (compound 6) "[""1H9""]" 1 IC50 IC50 > > 10 µM 10000.0 [] unit_conversion 5.0 success True biochemical_inhibition Dose-response activity assay against a panel of human ARTs; Table 1. 3 Table 1 prints PARP15 IC50 ≫10 µM for compound 6 and maps its PARP15 crystal structure to 7OTF. auto_single_measurement only accepted activity measurement [1] 1 structures\7OTF\7OTF_metadata.json point structures/7OTF/7otf_protein.pdb structures/7OTF/7otf_pocket.pdb structures/7OTF/7otf_ligand.sdf structures/7OTF/7otf_ligand.pdb structures/7OTF/7otf_ligand.cif structures/7OTF/7otf_complex.pdb structures/7OTF/7otf_complex.cif 7OTG classic ABCB1/P-glycoprotein (P-gp) mouse (murine) opti-mdr3 gene product (abcb1a) expressed in Pichia pastoris Na ivacaftor "[""VX7""]" 1 Kd Kd = = 0.2 µM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Static light-scattering measurement of ivacaftor binding to murine P-gp. 4 “Static light scattering ... yielded K_D values of 0.2 µM”. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\7OTG\7OTG_metadata.json point structures/7OTG/7otg_protein.pdb structures/7OTG/7otg_pocket.pdb structures/7OTG/7otg_ligand.sdf structures/7OTG/7otg_ligand.pdb structures/7OTG/7otg_ligand.cif structures/7OTG/7otg_complex.pdb structures/7OTG/7otg_complex.cif 7OU6 extended O-GlcNAc hydrolase human dimeric catalytic domain Na compound 16 "[""1XI""]" 1 Ki Ki = = 3 ± 1 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Competitive hOGA inhibition assay; Table 1 states Ki values are from at least two assays. 4 Table 1 reports hOGA Ki for compound 16 as 3 ± 1 nM. The text identifies compound 16 as the ligand in the hOGA catalytic-domain crystal structure, and page 9 identifies that hOGA structure as PDB 7OU6. auto_single_measurement only accepted activity measurement [1] 1 structures\7OU6\7OU6_metadata.json point structures/7OU6/7ou6_ligand.sdf structures/7OU6/7ou6_ligand.cif structures/7OU6/7ou6_complex.cif 7OUX classic PARP15 human catalytic domain Na OUL228 (compound 10) "[""1O7""]" 1 IC50 IC50 = = 2.1 µM 2100.0 [] unit_conversion 5.6777807052660805 success True biochemical_inhibition Dose-response activity assay against a panel of human ARTs; Table 1. 3 Table 1 reports PARP15 IC50 = 2.1 µM for compound 10 and maps its PARP15 crystal structure to 7OUX. auto_single_measurement only accepted activity measurement [1] 1 structures\7OUX\7OUX_metadata.json point structures/7OUX/7oux_protein.pdb structures/7OUX/7oux_pocket.pdb structures/7OUX/7oux_ligand.sdf structures/7OUX/7oux_ligand.pdb structures/7OUX/7oux_ligand.cif structures/7OUX/7oux_complex.pdb structures/7OUX/7oux_complex.cif 7OVD classic Human soluble adenylyl cyclase human Na Na TDI10229 (TDI-10229; compound 12) "[""1S2""]" 1 IC50 IC50 = = 195 nM 195.0 [] unit_conversion 6.709965388637482 success True biochemical_inhibition Biochemical IC50 reported for 5-substituted pyrazole analogue compound 12 (TDI-10229); tested at minimum in triplicate unless otherwise noted. 3 Table 2 lists compound 12 (TDI-10229) with biochemical IC50 of 195 nM. Figure 2 identifies the crystal structure of sAC in complex with compound 12, and page 4 maps the sAC/TDI-10229 crystal structure to PDB 7OVD. auto_single_measurement only accepted activity measurement [1] 1 structures\7OVD\7OVD_metadata.json point structures/7OVD/7ovd_protein.pdb structures/7OVD/7ovd_pocket.pdb structures/7OVD/7ovd_ligand.sdf structures/7OVD/7ovd_ligand.pdb structures/7OVD/7ovd_ligand.cif structures/7OVD/7ovd_complex.pdb structures/7OVD/7ovd_complex.cif 7OVO classic Heterodimeric murine tRNA-guanine transglycosylase (QTRT1/QTRT2) mouse Recombinant QTRT1/QTRT2 heterodimer; Strep-tag II from QTRT2 and His6 tag from QTRT1 removed QTRT1 N-terminal 10 residues replaced by Gly-Pro; QTRT2 N-terminal methionine replaced by Gly-Pro queuine "[""QEI""]" 1 Ki Ki = = 0.33 ± 0.02 μmol L−1 330.0 [] unit_conversion 6.481486060122112 success True biochemical_inhibition Competitive-inhibition determination versus [8-3H]-guanine during tRNATyr guanine-insertion assays using recombinant murine TGT. 9 Table 2 prints Ki (queuine) = 0.33 ± 0.02 μmol L−1; the text states substrate bases were used as competitive inhibitors with respect to [8-3H]-guanine. The enzyme used for crystallization was generated by dual recombinant expression of QTRT1 and QTRT2. auto_single_measurement only accepted activity measurement [1] 1 structures\7OVO\7OVO_metadata.json point structures/7OVO/7ovo_protein.pdb structures/7OVO/7ovo_pocket.pdb structures/7OVO/7ovo_ligand.sdf structures/7OVO/7ovo_ligand.pdb structures/7OVO/7ovo_ligand.cif structures/7OVO/7ovo_complex.pdb structures/7OVO/7ovo_complex.cif 7OWJ classic Odinarchaeota adenylate kinase (OdinAK) Na Na Na GTP "[""GTP""]" 1 Kd Kd = = 7.2 ± 0.6 µM 7200.0 [] unit_conversion 5.142667503568731 success True direct_binding Isothermal titration calorimetry (ITC), 25°C; OdinAK titrated with GTP. 5 Table 1 reports GTP Kd = 7.2 ± 0.6 µM for binding to OdinAK using ITC at 25°C. auto_single_measurement only accepted activity measurement [1] 1 structures\7OWJ\7OWJ_metadata.json point structures/7OWJ/7owj_protein.pdb structures/7OWJ/7owj_pocket.pdb structures/7OWJ/7owj_ligand.sdf structures/7OWJ/7owj_ligand.pdb structures/7OWJ/7owj_ligand.cif structures/7OWJ/7owj_complex.pdb structures/7OWJ/7owj_complex.cif 7OWK classic Odinarchaeota adenylate kinase (OdinAK) Na Na Na dTTP "[""TTP""]" 1 Kd Kd = = 24.2 ± 8 µM 24200.0 [] unit_conversion 4.616184634019569 success True direct_binding Isothermal titration calorimetry (ITC), 25°C; OdinAK titrated with dTTP. 5 Table 1 reports dTTP Kd = 24.2 ± 8 µM for binding to OdinAK using ITC at 25°C. auto_single_measurement only accepted activity measurement [1] 1 structures\7OWK\7OWK_metadata.json point structures/7OWK/7owk_protein.pdb structures/7OWK/7owk_pocket.pdb structures/7OWK/7owk_ligand.sdf structures/7OWK/7owk_ligand.pdb structures/7OWK/7owk_ligand.cif structures/7OWK/7owk_complex.pdb structures/7OWK/7owk_complex.cif 7OWL classic Odinarchaeota adenylate kinase (OdinAK) Na Na Na CTP "[""CTP""]" 1 Kd Kd = = 28.7 ± 7 µM 28700.0 [] unit_conversion 4.542118103266008 success True direct_binding Isothermal titration calorimetry (ITC), 25°C; OdinAK titrated with CTP. 5 Table 1 reports CTP Kd = 28.7 ± 7 µM for binding to OdinAK using ITC at 25°C. auto_single_measurement only accepted activity measurement [1] 1 structures\7OWL\7OWL_metadata.json point structures/7OWL/7owl_protein.pdb structures/7OWL/7owl_pocket.pdb structures/7OWL/7owl_ligand.sdf structures/7OWL/7owl_ligand.pdb structures/7OWL/7owl_ligand.cif structures/7OWL/7owl_complex.pdb structures/7OWL/7owl_complex.cif 7OXG extended SlyD Thermus thermophilus SlyD DeltaIF, FKBP domain only psWT peptide substitutions P6A, K9L, I12A, with M8A M8A pseudo-wild-type S2 peptide "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 19.4 ± 1.0 µM 19400.0 [] unit_conversion 4.7121982700697735 success True direct_binding ITC; SlyDΔIF construct, one-binding-site model, FKBP-site peptide binding. 4 Table 1 reports SlyDΔIF M8A K_D = 19.4 ± 1.0 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OXG\7OXG_metadata.json point structures/7OXG/7oxg_protein.pdb structures/7OXG/7oxg_pocket.pdb structures/7OXG/7oxg_ligand.pdb structures/7OXG/7oxg_ligand.cif structures/7OXG/7oxg_complex.pdb structures/7OXG/7oxg_complex.cif 7OXH extended SlyD Thermus thermophilus Full-length SlyD WT WT protein; psWT peptide substitutions P6A, K9L, I12A Pseudo-wild-type S2 peptide (psWT) "[""CHAIN:B""]" 1 Kd Kd = = 3.5 ± 0.1 µM 3500.0 [] unit_conversion 5.455931955649724 success True direct_binding ITC; full-length SlyDWT, two-binding-site model; FKBP-site Kd. 4 Table 1 reports the psWT SlyDWT FKBP K_D = 3.5 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OXH\7OXH_metadata.json point structures/7OXH/7oxh_protein.pdb structures/7OXH/7oxh_pocket.pdb structures/7OXH/7oxh_ligand.pdb structures/7OXH/7oxh_ligand.cif structures/7OXH/7oxh_complex.pdb structures/7OXH/7oxh_complex.cif 7OXJ extended SlyD Thermus thermophilus Full-length SlyD WT WT protein; psWT peptide substitutions P6A, K9L, I12A, with M8A M8A pseudo-wild-type S2 peptide "[""CHAIN:D""]" 1 Kd Kd = = 6.0 ± 0.1 µM 6000.0 [] unit_conversion 5.221848749616356 success True direct_binding ITC; full-length SlyDWT, two-binding-site model; FKBP-site Kd. 4 Table 1 reports the M8A SlyDWT FKBP K_D = 6.0 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OXJ\7OXJ_metadata.json point structures/7OXJ/7oxj_protein.pdb structures/7OXJ/7oxj_pocket.pdb structures/7OXJ/7oxj_ligand.pdb structures/7OXJ/7oxj_ligand.cif structures/7OXJ/7oxj_complex.pdb structures/7OXJ/7oxj_complex.cif 7OYM extended human carbonic anhydrase II Homo sapiens Na Na Hit2 (MH65) "[""CHAIN:B""]" 1 Ki Ki = = 16.0 ± 1.3 nM 16.0 [] unit_conversion 7.795880017344075 success True biochemical_inhibition Stopped-flow carbon dioxide hydration inhibition assay. 4 Table 1 reports Hit2 Ki (hCA II) = 16.0 ± 1.3 nM; the text identifies the Ki values as determined using a stopped-flow carbon dioxide hydration assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYM\7OYM_metadata.json point structures/7OYM/7oym_protein.pdb structures/7OYM/7oym_pocket.pdb structures/7OYM/7oym_ligand.pdb structures/7OYM/7oym_ligand.cif structures/7OYM/7oym_complex.pdb structures/7OYM/7oym_complex.cif 7OYN extended human carbonic anhydrase II Homo sapiens Na Na Hit3 (MH57) "[""CHAIN:B""]" 1 Ki Ki = = 13.0 ± 1.0 nM 13.0 [] unit_conversion 7.886056647693163 success True biochemical_inhibition Stopped-flow carbon dioxide hydration inhibition assay. 4 Table 1 reports Hit3 Ki (hCA II) = 13.0 ± 1.0 nM; the text identifies the Ki values as determined using a stopped-flow carbon dioxide hydration assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYN\7OYN_metadata.json point structures/7OYN/7oyn_protein.pdb structures/7OYN/7oyn_pocket.pdb structures/7OYN/7oyn_ligand.pdb structures/7OYN/7oyn_ligand.cif structures/7OYN/7oyn_complex.pdb structures/7OYN/7oyn_complex.cif 7OYO extended human carbonic anhydrase II Homo sapiens Na Na Hit4 (MH70) "[""TKR""]" 1 Ki Ki = = 66.0 ± 4.2 nM 66.0 [] unit_conversion 7.180456064458131 success True biochemical_inhibition Stopped-flow carbon dioxide hydration inhibition assay. 4 Table 1 reports Hit4 Ki (hCA II) = 66.0 ± 4.2 nM; the text identifies the Ki values as determined using a stopped-flow carbon dioxide hydration assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYO\7OYO_metadata.json point structures/7OYO/7oyo_protein.pdb structures/7OYO/7oyo_pocket.pdb structures/7OYO/7oyo_ligand.pdb structures/7OYO/7oyo_ligand.cif structures/7OYO/7oyo_complex.pdb structures/7OYO/7oyo_complex.cif 7OYP classic human carbonic anhydrase II Homo sapiens Na Na Hit3-t1 (MH172) "[""3I4""]" 1 Ki Ki = = 23 ± 1.6 nM 23.0 [] unit_conversion 7.638272163982407 success True biochemical_inhibition Stopped-flow carbon dioxide hydration inhibition assay of truncated Hit3 variants. 7 Table 2 reports Hit3-t1 Ki (hCA II) = 23 ± 1.6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYP\7OYP_metadata.json point structures/7OYP/7oyp_protein.pdb structures/7OYP/7oyp_pocket.pdb structures/7OYP/7oyp_ligand.sdf structures/7OYP/7oyp_ligand.pdb structures/7OYP/7oyp_ligand.cif structures/7OYP/7oyp_complex.pdb structures/7OYP/7oyp_complex.cif 7OYQ extended human carbonic anhydrase II Homo sapiens Na Na Hit3-t2 (MH174) "[""CHAIN:B"", ""CHAIN:C""]" 1 Ki Ki = = 14.6 ± 0.9 nM 14.6 [] unit_conversion 7.835647144215563 success True biochemical_inhibition Stopped-flow carbon dioxide hydration inhibition assay of truncated Hit3 variants. 7 Table 2 reports Hit3-t2 Ki (hCA II) = 14.6 ± 0.9 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYQ\7OYQ_metadata.json point structures/7OYQ/7oyq_protein.pdb structures/7OYQ/7oyq_pocket.pdb structures/7OYQ/7oyq_ligand.pdb structures/7OYQ/7oyq_ligand.cif structures/7OYQ/7oyq_complex.pdb structures/7OYQ/7oyq_complex.cif 7OYR extended human carbonic anhydrase II Homo sapiens Na Na Hit3-t4 (MH181) "[""CHAIN:B"", ""CHAIN:C""]" 1 Ki Ki = = 8.6 ± 0.9 nM 8.6 [] unit_conversion 8.065501548756432 success True biochemical_inhibition Stopped-flow carbon dioxide hydration inhibition assay of truncated Hit3 variants. 7 Table 2 reports Hit3-t4 Ki (hCA II) = 8.6 ± 0.9 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYR\7OYR_metadata.json point structures/7OYR/7oyr_protein.pdb structures/7OYR/7oyr_pocket.pdb structures/7OYR/7oyr_ligand.pdb structures/7OYR/7oyr_ligand.cif structures/7OYR/7oyr_complex.pdb structures/7OYR/7oyr_complex.cif 7OYS classic putrescine receptor variant PotF/D E. coli PotF/D (4JDF) E39D; Y87S spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 9.44 ± 0.91 µM 9440.0 [] unit_conversion 5.025028005701931 success True direct_binding Isothermal titration calorimetry (ITC); biological triplicates. 7 Table 2 reports K_D(SPD) = 9.44 ± 0.91 µM for PotF/D-E39D-Y87S; Figure 4 maps this construct to PDB 7OYS. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYS\7OYS_metadata.json point structures/7OYS/7oys_protein.pdb structures/7OYS/7oys_pocket.pdb structures/7OYS/7oys_ligand.sdf structures/7OYS/7oys_ligand.pdb structures/7OYS/7oys_ligand.cif structures/7OYS/7oys_complex.pdb structures/7OYS/7oys_complex.cif 7OYT classic putrescine receptor variant PotF/D E. coli PotF/D (4JDF) E39D; F88L spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 9.90 ± 0.54 µM 9900.0 [] unit_conversion 5.004364805402449 success True direct_binding Isothermal titration calorimetry (ITC); biological triplicates. 7 Table 2 reports K_D(SPD) = 9.90 ± 0.54 µM for PotF/D-E39D-F88L; Figure 4 maps this construct to PDB 7OYT. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYT\7OYT_metadata.json point structures/7OYT/7oyt_protein.pdb structures/7OYT/7oyt_pocket.pdb structures/7OYT/7oyt_ligand.sdf structures/7OYT/7oyt_ligand.pdb structures/7OYT/7oyt_ligand.cif structures/7OYT/7oyt_complex.pdb structures/7OYT/7oyt_complex.cif 7OYU classic putrescine receptor variant PotF/D E. coli PotF/D (4JDF) E39D; Y87S; F88Y spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 5.32 ± 1.43 µM 5320.0 [] unit_conversion 5.274088367704952 success True direct_binding Isothermal titration calorimetry (ITC); biological triplicates. 7 Table 2 reports K_D(SPD) = 5.32 ± 1.43 µM for PotF/D-E39D-Y87S-F88Y; Figure 4 maps this construct to PDB 7OYU. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYU\7OYU_metadata.json point structures/7OYU/7oyu_protein.pdb structures/7OYU/7oyu_pocket.pdb structures/7OYU/7oyu_ligand.sdf structures/7OYU/7oyu_ligand.pdb structures/7OYU/7oyu_ligand.cif structures/7OYU/7oyu_complex.pdb structures/7OYU/7oyu_complex.cif 7OYV classic putrescine receptor variant PotF/D E. coli PotF/D (4JDF) E39D; F88A; S247D spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 1.48 ± 0.14 µM 1480.0 [] unit_conversion 5.8297382846050425 success True direct_binding Isothermal titration calorimetry (ITC); biological triplicates. 7 Table 2 reports K_D(SPD) = 1.48 ± 0.14 µM for PotF/D-E39D-F88A-S247D; Figure 5 maps this construct to PDB 7OYV. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYV\7OYV_metadata.json point structures/7OYV/7oyv_protein.pdb structures/7OYV/7oyv_pocket.pdb structures/7OYV/7oyv_ligand.sdf structures/7OYV/7oyv_ligand.pdb structures/7OYV/7oyv_ligand.cif structures/7OYV/7oyv_complex.pdb structures/7OYV/7oyv_complex.cif 7OYW classic putrescine receptor variant PotF/D E. coli PotF/D (4JDF) E39D; F88L; S247D spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 3.33 ± 0.53 µM 3330.0 [] unit_conversion 5.47755576649368 success True direct_binding Isothermal titration calorimetry (ITC); biological triplicates. 7 Table 2 reports K_D(SPD) = 3.33 ± 0.53 µM for PotF/D-E39D-F88L-S247D; Figure 5 maps this construct to PDB 7OYW. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYW\7OYW_metadata.json point structures/7OYW/7oyw_protein.pdb structures/7OYW/7oyw_pocket.pdb structures/7OYW/7oyw_ligand.sdf structures/7OYW/7oyw_ligand.pdb structures/7OYW/7oyw_ligand.cif structures/7OYW/7oyw_complex.pdb structures/7OYW/7oyw_complex.cif 7OYX classic putrescine receptor variant PotF/D E. coli PotF/D (4JDF) E39D; Y87S; F88Y; S247D spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 0.84 ± 0.27 µM 840.0 [] unit_conversion 6.075720713938118 success True direct_binding Isothermal titration calorimetry (ITC); biological triplicates. 7 Table 2 reports K_D(SPD) = 0.84 ± 0.27 µM for PotF/D-E39D-Y87S-F88Y-S247D; Figure 5 maps this construct to PDB 7OYX. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYX\7OYX_metadata.json point structures/7OYX/7oyx_protein.pdb structures/7OYX/7oyx_pocket.pdb structures/7OYX/7oyx_ligand.sdf structures/7OYX/7oyx_ligand.pdb structures/7OYX/7oyx_ligand.cif structures/7OYX/7oyx_complex.pdb structures/7OYX/7oyx_complex.cif 7OYY classic putrescine receptor variant PotF/D E. coli PotF/D (4JDF) S247D spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 9.43 ± 3.07 µM 9430.0 [] unit_conversion 5.0254883072626715 success True direct_binding Isothermal titration calorimetry (ITC); biological triplicates. 7 Table 2 reports K_D(SPD) = 9.43 ± 3.07 µM for PotF/D-S247D; the Data availability section includes PDB 7OYY among the solved structures. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYY\7OYY_metadata.json point structures/7OYY/7oyy_protein.pdb structures/7OYY/7oyy_pocket.pdb structures/7OYY/7oyy_ligand.sdf structures/7OYY/7oyy_ligand.pdb structures/7OYY/7oyy_ligand.cif structures/7OYY/7oyy_complex.pdb structures/7OYY/7oyy_complex.cif 7OYZ classic putrescine receptor variant PotF/D E. coli PotF/D Na spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 37.32 ± 2.4 µM 37320.0 [] unit_conversion 4.428058364925538 success True direct_binding Isothermal titration calorimetry (ITC); biological triplicates. 2 Table 1 reports K_D(SPD) = 37.32 ± 2.4 µM for PotF/D. The paper identifies PDB 7OYZ as the ligated PotF/D crystal structure, and its Data availability section lists 7OYZ. auto_single_measurement only accepted activity measurement [1] 1 structures\7OYZ\7OYZ_metadata.json point structures/7OYZ/7oyz_protein.pdb structures/7OYZ/7oyz_pocket.pdb structures/7OYZ/7oyz_ligand.sdf structures/7OYZ/7oyz_ligand.pdb structures/7OYZ/7oyz_ligand.cif structures/7OYZ/7oyz_complex.pdb structures/7OYZ/7oyz_complex.cif 7OZY extended FGFR2 kinase domain Na residues 461-763 WT compound 38 "[""47I""]" 1 IC50 IC50 = = 29 ± 0.2 nM 29.0 [] unit_conversion 7.537602002101044 success True biochemical_inhibition FRET-based kinase assay; Table 4 biological results against FGFR1–3. 8 Table 4 reports compound 38 IC50 = 29 ± 0.2 nM against FGFR2. The paper describes expression of the WT FGFR2 residues 461–763 construct used in the work. auto_single_measurement only accepted activity measurement [1] 1 structures\7OZY\7OZY_metadata.json point structures/7OZY/7ozy_ligand.sdf structures/7OZY/7ozy_ligand.cif structures/7OZY/7ozy_complex.cif 7P1N extended human acetylcholinesterase human Na Na compound 4; (2R,3R,4S,5S,6R)-2-{4-[1-(4-{5-hydroxy-6-[(E)-(hydroxyimino)methyl]pyridin-2-yl}butyl)-1H-1,2,3-triazol-4-yl]butoxy}-6-(hydroxymethyl)oxane-3,4,5-triol oxime "[""4J1""]" 1 IC50 IC50 = = 580 ± 10 µM 580000.0 [] unit_conversion 3.236572006437063 success True biochemical_inhibition Half-maximal inhibitory concentration for native hAChE. 6 Table 2 lists oxime 4 IC50 as 580 ± 10 µM for hAChE; adjacent text identifies this as native hAChE. auto_single_measurement only accepted activity measurement [1] 1 structures\7P1N\7P1N_metadata.json point structures/7P1N/7p1n_ligand.sdf structures/7P1N/7p1n_ligand.cif structures/7P1N/7p1n_complex.cif 7P1P extended human acetylcholinesterase human Na Na compound 3; (E)-3-hydroxy-6-(3-(4-(4-(((2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)butyl)-1H-1,2,3-triazol-1-yl)propyl)picolinaldehyde oxime "[""4IX""]" 1 IC50 IC50 = = 1600 ± 200 µM 1600000.0 [] unit_conversion 2.795880017344075 success True biochemical_inhibition Half-maximal inhibitory concentration for native hAChE. 6 Table 2 lists oxime 3 IC50 as 1600 ± 200 µM for hAChE; adjacent text identifies this as native hAChE. auto_single_measurement only accepted activity measurement [1] 1 structures\7P1P\7P1P_metadata.json point structures/7P1P/7p1p_ligand.sdf structures/7P1P/7p1p_ligand.cif structures/7P1P/7p1p_complex.cif 7P2G classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Mpro with a C-terminal His-tag Na Z222979552 "[""4N0""]" 1 IC50 IC50 = = 1.0 μM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition In vitro Mpro protease-activity assay; the compound was characterized as the most potent dihydro-quinolinone inhibitor. 4 The paper states that Z222979552 had an IC50 of 1.0 μM; Figure 1 identifies it as the most active dihydro-quinolinone compound and describes its Mpro dose-response curves. auto_single_measurement only accepted activity measurement [1] 1 structures\7P2G\7P2G_metadata.json point structures/7P2G/7p2g_protein.pdb structures/7P2G/7p2g_pocket.pdb structures/7P2G/7p2g_ligand.sdf structures/7P2G/7p2g_ligand.pdb structures/7P2G/7p2g_ligand.cif structures/7P2G/7p2g_complex.pdb structures/7P2G/7p2g_complex.cif 7P2T classic Schistosoma mansoni HDAC8 Schistosoma mansoni Na Na NF2886 "[""4VX""]" 2 Ki Ki = = 9.7 ± 7.2 µM 9700.0 [] unit_conversion 5.013228265733755 success True direct_binding Intrinsic-protein-fluorescence quenching binding assay in the absence of substrate. 7 Table 4 prints a calculated Ki of 9.7 ± 7.2 µM for NF2886 binding to SmHDAC8. auto_metric_priority unique highest-priority metric family: Ki [2] 4 structures\7P2T\7P2T_metadata.json point structures/7P2T/7p2t_protein.pdb structures/7P2T/7p2t_pocket.pdb structures/7P2T/7p2t_ligand.sdf structures/7P2T/7p2t_ligand.pdb structures/7P2T/7p2t_ligand.cif structures/7P2T/7p2t_complex.pdb structures/7P2T/7p2t_complex.cif 7P37 classic NrdR Streptomyces coelicolor Na Na ATP "[""ATP""]" 1 Kd Kd = = 4 µM 4000.0 [] unit_conversion 5.3979400086720375 success True direct_binding Isothermal titration calorimetry (ITC) of nucleotide binding to S. coelicolor NrdR. 6 “ATP is more weakly bound compared to dATP (KDs of 4 and 1 µM, respectively).” auto_single_measurement only accepted activity measurement [1] 1 structures\7P37\7P37_metadata.json point structures/7P37/7p37_protein.pdb structures/7P37/7p37_pocket.pdb structures/7P37/7p37_ligand.sdf structures/7P37/7p37_ligand.pdb structures/7P37/7p37_ligand.cif structures/7P37/7p37_complex.pdb structures/7P37/7p37_complex.cif 7P3V classic B-Raf V600E Na B-Raf kinase domain residues 448-723 with an N-terminal His tag and thrombin cleavage site V600E; solubilizing mutations I543A, I544S, I551K, Q562R, L588H, K630S, F667E, Y673S, A688R, L706S, Q709R, S713E, L716E, S720E, P722S, K723G compound 4c (lead compound) "[""5I4""]" 1 IC50 IC50 = = 6.0 nM 6.0 [] unit_conversion 8.221848749616356 success True biochemical_inhibition In vitro inhibition assay on purified recombinant B-Raf-V600E; Table 1 reports the B-Raf V600E inhibition IC50 for compound 4c. 3 Table 1 lists compound 4c with B-Raf V600E inhibition IC50 = 6.0 nM. The methods state that kinase activity was monitored in vitro on recombinant B-Raf-V600E. auto_single_measurement only accepted activity measurement [1] 1 structures\7P3V\7P3V_metadata.json point structures/7P3V/7p3v_protein.pdb structures/7P3V/7p3v_pocket.pdb structures/7P3V/7p3v_ligand.sdf structures/7P3V/7p3v_ligand.pdb structures/7P3V/7p3v_ligand.cif structures/7P3V/7p3v_complex.pdb structures/7P3V/7p3v_complex.cif 7P4F classic monoamine oxidase B (MAO B) human Na Na inhibitor 1 "[""5IK""]" 1 Ki Ki = = 4.5 ± 0.2 µM 4500.0 [] unit_conversion 5.346787486224656 success True biochemical_inhibition Spectrophotometric experiments through HRP-coupled assay on purified recombinant enzyme; tight-binding Ki determined by Morrison equation. 2 Table 1 reports human MAO B Ki for 1 as 4.5 ± 0.2 µM; footnotes specify purified recombinant enzyme and tight-binding Morrison-equation determination. auto_single_measurement only accepted activity measurement [1] 1 structures\7P4F\7P4F_metadata.json point structures/7P4F/7p4f_protein.pdb structures/7P4F/7p4f_pocket.pdb structures/7P4F/7p4f_ligand.sdf structures/7P4F/7p4f_ligand.pdb structures/7P4F/7p4f_ligand.cif structures/7P4F/7p4f_complex.pdb structures/7P4F/7p4f_complex.cif 7P4H classic monoamine oxidase B (MAO B) human Na Na inhibitor (+)-2 "[""5IH""]" 1 Ki Ki = = 0.093 ± 0.015 µM 93.0 [] unit_conversion 7.031517051446065 success True biochemical_inhibition Spectrophotometric experiments through HRP-coupled assay on purified recombinant enzyme. 2 Table 1 reports human MAO B Ki for (+)-2 as 0.093 ± 0.015 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7P4H\7P4H_metadata.json point structures/7P4H/7p4h_protein.pdb structures/7P4H/7p4h_pocket.pdb structures/7P4H/7p4h_ligand.sdf structures/7P4H/7p4h_ligand.pdb structures/7P4H/7p4h_ligand.cif structures/7P4H/7p4h_complex.pdb structures/7P4H/7p4h_complex.cif 7P4S classic human TAF1(2) human Na Na compound 18 (naphthyridinone) "[""5LV""]" 1 pIC50 IC50 = = 7.5 31.622776601683793 [] p_metric_transform 7.5 success True biochemical_inhibition TR-FRET competitive binding assay against TAF1(2). 3 Table 1 reports compound 18: TAF1(2) pIC50 = 7.5. The text identifies the TAF1(2) assay as a TR-FRET competitive assay, and Figure 2 maps compound 18 bound to human TAF1(2) to PDB 7p4s. auto_single_measurement only accepted activity measurement [1] 1 structures\7P4S\7P4S_metadata.json point structures/7P4S/7p4s_protein.pdb structures/7P4S/7p4s_pocket.pdb structures/7P4S/7p4s_ligand.sdf structures/7P4S/7p4s_ligand.pdb structures/7P4S/7p4s_ligand.cif structures/7P4S/7p4s_complex.pdb structures/7P4S/7p4s_complex.cif 7P51 classic SARS-CoV-2 Main Protease SARS-CoV-2 Na Na F01 "[""5P9""]" 1 Kd Kd = = 73 ± 14 μM 73000.0 [] unit_conversion 4.136677139879544 success True direct_binding NMR titration of F01 with 3CLp. 5 “NMR titration experiments, we determined a dissociation constant KD=73±14 μM for the interaction between F01 and 3CLp.” Figure 6 identifies the F01-bound crystal structure as PDB 7P51. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7P51\7P51_metadata.json point structures/7P51/7p51_protein.pdb structures/7P51/7p51_pocket.pdb structures/7P51/7p51_ligand.sdf structures/7P51/7p51_ligand.pdb structures/7P51/7p51_ligand.cif structures/7P51/7p51_complex.pdb structures/7P51/7p51_complex.cif 7P5P classic KEAP1 murine Kelch domain residues 322-624; N-terminal thrombin-cleavable hexahistidine tag removed before crystallization Na compound 37 "[""5RB""]" 1 Kd Kd = = 2.5 nM 2.5 [] unit_conversion 8.602059991327963 success True direct_binding Surface plasmon resonance using murine KEAP1 Kelch domain; Taylor-dispersion analysis; n = 2 geometric mean. 22 The SPR section states that binding of compound 37 (TFA salt) gave KD = 2.5 nM (n = 2 geometric mean) to the murine KEAP1 Kelch domain (322–624). auto_single_measurement only accepted activity measurement [1] 1 structures\7P5P\7P5P_metadata.json point structures/7P5P/7p5p_protein.pdb structures/7P5P/7p5p_pocket.pdb structures/7P5P/7p5p_ligand.sdf structures/7P5P/7p5p_ligand.pdb structures/7P5P/7p5p_ligand.cif structures/7P5P/7p5p_complex.pdb structures/7P5P/7p5p_complex.cif 7P5T classic CYP142A1 (Rv3518c) Mycobacterium tuberculosis N-terminally truncated CYP142A1 residues 2-398, pET21a construct with TEV-cleavable Twin-Strep/hexa-histidine tag; tag-free protein used for crystallography Na compound 5m (deposited alias MEK216; PDB component 5YG) "[""5YG""]" 1 Kd Kd = = 0.16 ± 0.14 µM 160.0 [] unit_conversion 6.795880017344075 success True direct_binding Optical titration of compound 5m binding CYP142A1. 5 Table 1 reports compound 5m CYP142 Kd 0.16 ± 0.14 µM; Figure 3 maps CYP142-5m to PDB 7P5T. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7P5T\7P5T_metadata.json point structures/7P5T/7p5t_protein.pdb structures/7P5T/7p5t_pocket.pdb structures/7P5T/7p5t_ligand.sdf structures/7P5T/7p5t_ligand.pdb structures/7P5T/7p5t_ligand.cif structures/7P5T/7p5t_complex.pdb structures/7P5T/7p5t_complex.cif 7P5U extended Neuropilin-1 b1 domain (NRP1-b1) Na NRP1-b1 domain Na MGC0122 (VEGF-B186-derived peptide; Hpt-DRAATPHHRQPQR) "[""CHAIN:CCC"", ""CHAIN:EEE""]" 1 Kd Kd = = 9.55 ± 0.17 μM 9550.0 [] unit_conversion 5.019996628416253 success True direct_binding SPR binding of VEGF-B186-derived peptide MGC0122 to NRP1-b1. 4 Table 1 reports MGC0122 (VEGF-B186) SPR binding to NRP1-b1: K_D 9.55 ± 0.17 μM. The text identifies MGC0122 as crystallised with NRP1-b1; the deposited structure is 7P5U. auto_single_measurement only accepted activity measurement [1] 1 structures\7P5U\7P5U_metadata.json point structures/7P5U/7p5u_ligand.cif structures/7P5U/7p5u_complex.cif 7P6N classic ROCK2 Na Na Na compound 12 "[""5YS""]" 1 IC50 IC50 = = 0.074 µM 74.0 [] unit_conversion 7.130768280269024 success True biochemical_inhibition ROCK2 biochemical IC50; purified recombinant ROCK2 kinase-domain ADP-Glo assay described in the Experimental Section. 4 Table 3 reports compound 12 ROCK2 biochemical IC50 = 0.074 µM; page 6 identifies PDB 7P6N as ROCK2 with compound 12. auto_single_measurement only accepted activity measurement [1] 1 structures\7P6N\7P6N_metadata.json point structures/7P6N/7p6n_protein.pdb structures/7P6N/7p6n_pocket.pdb structures/7P6N/7p6n_ligand.sdf structures/7P6N/7p6n_ligand.pdb structures/7P6N/7p6n_ligand.cif structures/7P6N/7p6n_complex.pdb structures/7P6N/7p6n_complex.cif 7P6O classic ROCK2 Na Na Na compound 8 "[""5YK""]" 1 IC50 IC50 = = 0.026 µM 26.0 [] unit_conversion 7.585026652029182 success True biochemical_inhibition ROCK2 biochemical IC50; purified recombinant ROCK2 kinase-domain ADP-Glo assay described in the Experimental Section. 3 Table 2 reports compound 8 ROCK2 biochemical IC50 = 0.026 µM; Figure 3 identifies PDB 7P6O as ROCK2 bound to compound 8. auto_single_measurement only accepted activity measurement [1] 1 structures\7P6O\7P6O_metadata.json point structures/7P6O/7p6o_protein.pdb structures/7P6O/7p6o_pocket.pdb structures/7P6O/7p6o_ligand.sdf structures/7P6O/7p6o_ligand.pdb structures/7P6O/7p6o_ligand.cif structures/7P6O/7p6o_complex.pdb structures/7P6O/7p6o_complex.cif 7P6P classic ROCK2 Na Na Na compound 17 "[""5YV""]" 1 IC50 IC50 = = 0.098 µM 98.0 [] unit_conversion 7.008773924307505 success True biochemical_inhibition ROCK2 biochemical IC50; purified recombinant ROCK2 kinase-domain ADP-Glo assay described in the Experimental Section. 4 Table 3 reports compound 17 ROCK2 biochemical IC50 = 0.098 µM; pages 6–7 identify PDB 7P6P as ROCK2 with compound 17. auto_single_measurement only accepted activity measurement [1] 1 structures\7P6P\7P6P_metadata.json point structures/7P6P/7p6p_protein.pdb structures/7P6P/7p6p_pocket.pdb structures/7P6P/7p6p_ligand.sdf structures/7P6P/7p6p_ligand.pdb structures/7P6P/7p6p_ligand.cif structures/7P6P/7p6p_complex.pdb structures/7P6P/7p6p_complex.cif 7P6Q classic ROCK2 Na Na Na compound 21 "[""5YO""]" 1 IC50 IC50 = = 0.007 µM 7.0 [] unit_conversion 8.154901959985743 success True biochemical_inhibition ROCK2 biochemical IC50; purified recombinant ROCK2 kinase-domain ADP-Glo assay described in the Experimental Section. 8 Table 4 reports compound 21 ROCK2 biochemical IC50 = 0.007 µM; page 7 identifies PDB 7P6Q as ROCK2 with compound 21. auto_single_measurement only accepted activity measurement [1] 1 structures\7P6Q\7P6Q_metadata.json point structures/7P6Q/7p6q_protein.pdb structures/7P6Q/7p6q_pocket.pdb structures/7P6Q/7p6q_ligand.sdf structures/7P6Q/7p6q_ligand.pdb structures/7P6Q/7p6q_ligand.cif structures/7P6Q/7p6q_complex.pdb structures/7P6Q/7p6q_complex.cif 7P6V extended BRD4 human N-terminal bromodomain (BD1) Na compound 3ag "[""5Z4""]" 1 pIC50 IC50 = = 7.8 unitless 15.848931924611142 [] p_metric_transform 7.8 success True biochemical_inhibition TR-FRET assay with recombinant BRD4 BD1; Table 2 reports pIC50 ±0.5. 4 Table 2 lists compound 3ag with pIC50 BD1 = 7.8; Figure 4 maps 3ag to BRD4 BD1 structure PDB 7P6V. auto_single_measurement only accepted activity measurement [1] 1 structures\7P6V\7P6V_metadata.json point structures/7P6V/7p6v_ligand.sdf structures/7P6V/7p6v_ligand.cif structures/7P6V/7p6v_complex.cif 7P6W extended BRD4 human N-terminal bromodomain (BD1) Na compound 3bg "[""5YY""]" 1 pIC50 IC50 = = 7.8 unitless 15.848931924611142 [] p_metric_transform 7.8 success True biochemical_inhibition TR-FRET assay with recombinant BRD4 BD1; Table 2 reports pIC50 ±0.5. 4 Table 2 lists compound 3bg with pIC50 BD1 = 7.8; Figure 4 maps 3bg to BRD4 BD1 structure PDB 7P6W. auto_single_measurement only accepted activity measurement [1] 1 structures\7P6W\7P6W_metadata.json point structures/7P6W/7p6w_ligand.sdf structures/7P6W/7p6w_ligand.cif structures/7P6W/7p6w_complex.cif 7P6Y extended BRD4 human N-terminal bromodomain (BD1) Na compound 5ef "[""5Z1""]" 1 pIC50 IC50 = = 8.3 unitless 5.011872336272715 [] p_metric_transform 8.3 success True biochemical_inhibition TR-FRET assay with recombinant BRD4 BD1; Table 2 reports pIC50 ±0.5. 4 Table 2 lists compound 5ef with pIC50 BD1 = 8.3; Figure 4 maps 5ef to BRD4 BD1 structure PDB 7P6Y. auto_single_measurement only accepted activity measurement [1] 1 structures\7P6Y\7P6Y_metadata.json point structures/7P6Y/7p6y_ligand.sdf structures/7P6Y/7p6y_ligand.cif structures/7P6Y/7p6y_complex.cif 7P70 extended SNTB1 Na PDZ domain with an N-terminal TEV protease-cleavable His6 tag and a C-terminal ANXA2 C-terminal PDZ-binding motif tag Na PDZ-binding motif of HPV35-E6 "[""CHAIN:C""]" 1 pKd Kd = = 4.7 19952.62314968879 [] p_metric_transform 4.7 success True direct_binding Quantitative PDZ–PBM affinity profiling by holdup assay; Fig. 3B reports the SNTB1–HPV35 E6 complex affinity. 4 Fig. 3B labels the SNTB1–HPV35 E6 complex with “pKd = 4.7”. auto_single_measurement only accepted activity measurement [1] 1 structures\7P70\7P70_metadata.json point structures/7P70/7p70_protein.pdb structures/7P70/7p70_pocket.pdb structures/7P70/7p70_ligand.pdb structures/7P70/7p70_ligand.cif structures/7P70/7p70_complex.pdb structures/7P70/7p70_complex.cif 7P71 extended MAGI1_2 Na PDZ domain with an N-terminal TEV protease-cleavable His6 tag and a C-terminal ANXA2 C-terminal PDZ-binding motif tag Na PDZ-binding motif of HPV35-E6 "[""CHAIN:C"", ""CHAIN:D""]" 1 pKd Kd = = 5.1 7943.282347242822 [] p_metric_transform 5.1 success True direct_binding Quantitative PDZ–PBM affinity profiling by holdup assay; Fig. 3C reports the MAGI1_2–HPV35 E6 complex affinity. 4 Fig. 3C labels the MAGI1_2–HPV35 E6 complex with “pKd = 5.1”. auto_single_measurement only accepted activity measurement [1] 1 structures\7P71\7P71_metadata.json point structures/7P71/7p71_protein.pdb structures/7P71/7p71_pocket.pdb structures/7P71/7p71_ligand.pdb structures/7P71/7p71_ligand.cif structures/7P71/7p71_complex.pdb structures/7P71/7p71_complex.cif 7P72 extended SNX27 Na PDZ domain with an N-terminal TEV protease-cleavable His6 tag and a C-terminal ANXA2 C-terminal PDZ-binding motif tag Na PDZ-binding motif of MERS-E "[""CHAIN:B""]" 1 pKd Kd = = 4.6 25118.864315095823 [] p_metric_transform 4.6 success True direct_binding Quantitative PDZ–PBM affinity profiling by holdup assay; Fig. 3H reports the SNX27–MERS E complex affinity. 4 Fig. 3H labels the SNX27–MERS E complex with “pKd = 4.6”. auto_single_measurement only accepted activity measurement [1] 1 structures\7P72\7P72_metadata.json point structures/7P72/7p72_protein.pdb structures/7P72/7p72_pocket.pdb structures/7P72/7p72_ligand.pdb structures/7P72/7p72_ligand.cif structures/7P72/7p72_complex.pdb structures/7P72/7p72_complex.cif 7P7P classic ERAP2 aminopeptidase Na Na Na Compound 1; phosphinic pseudotripeptide ((1R)-1-amino-3-phenylpropyl){(2S)-3-[((2S)-1-amino-1-oxo-3-phenylpropan-2-yl)amino]-2-{[3-(2-hydroxyphenyl)-isoxazol-5-yl]methyl}-3-oxopropyl}phosphinic acid "[""62S""]" 1 IC50 IC50 = = 0.083 μM 83.0 [] unit_conversion 7.080921907623926 success True biochemical_inhibition In vitro inhibition; Scheme 1. 2 Scheme 1 prints: “ERAP2 IC50 = 0.083 μM” for Compound 1. The paper deposits PDB 7P7P for compound 1. auto_single_measurement only accepted activity measurement [1] 1 structures\7P7P\7P7P_metadata.json point structures/7P7P/7p7p_protein.pdb structures/7P7P/7p7p_pocket.pdb structures/7P7P/7p7p_ligand.sdf structures/7P7P/7p7p_ligand.pdb structures/7P7P/7p7p_ligand.cif structures/7P7P/7p7p_complex.pdb structures/7P7P/7p7p_complex.cif 7PAD classic PDE6D Na Na Na DW-0254 (DW0254) "[""O7W""]" 1 Kd Kd = = 436 (±6) nM 436.0 [] unit_conversion 6.360513510731414 success True direct_binding Isothermal titration calorimetry (ITC) of recombinant PDE6D with DW0254; Fig. 5A reports ligand-binding affinity and thermodynamic parameters. 8 Fig. 5A lists DW0254 with Kd 436 (±6) nM; the Fig. 5 caption identifies these as ITC binding affinities for ligand binding to PDE6D. auto_single_measurement only accepted activity measurement [1] 1 structures\7PAD\7PAD_metadata.json point structures/7PAD/7pad_protein.pdb structures/7PAD/7pad_pocket.pdb structures/7PAD/7pad_ligand.sdf structures/7PAD/7pad_ligand.pdb structures/7PAD/7pad_ligand.cif structures/7PAD/7pad_complex.pdb structures/7PAD/7pad_complex.cif 7PAE classic PDE6D Na Na Na Deltarasin "[""O7T""]" 1 Kd Kd = = 194 (±41) nM 194.0 [] unit_conversion 6.7121982700697735 success True direct_binding Isothermal titration calorimetry (ITC) of recombinant PDE6D with Deltarasin; Fig. 5A reports ligand-binding affinity and thermodynamic parameters. 8 Fig. 5A lists Deltarasin with Kd 194 (±41) nM; the Fig. 5 caption identifies these as ITC binding affinities for ligand binding to PDE6D. auto_single_measurement only accepted activity measurement [1] 1 structures\7PAE\7PAE_metadata.json point structures/7PAE/7pae_protein.pdb structures/7PAE/7pae_pocket.pdb structures/7PAE/7pae_ligand.sdf structures/7PAE/7pae_ligand.pdb structures/7PAE/7pae_ligand.cif structures/7PAE/7pae_complex.pdb structures/7PAE/7pae_complex.cif 7PFS classic ERAP2 aminopeptidase Na Na Na Compound 2; phosphinic pseudotripeptide ((1R)-1-amino-3-phenylpropyl){2-([1,1:3,1-terphenyl]-5-ylmethyl)-3-[((2S)-1-amino-1-oxo-3-phenylpropan-2-yl)amino]-3-oxopropyl}phosphinic acid "[""7OO""]" 1 IC50 IC50 = = 2.7 μM 2700.0 [] unit_conversion 5.568636235841012 success True biochemical_inhibition In vitro inhibition; Scheme 1. 2 Scheme 1 prints: “ERAP2 IC50 = 2.7 μM” for Compound 2. The paper deposits PDB 7PFS for compound 2. auto_single_measurement only accepted activity measurement [1] 1 structures\7PFS\7PFS_metadata.json point structures/7PFS/7pfs_protein.pdb structures/7PFS/7pfs_pocket.pdb structures/7PFS/7pfs_ligand.sdf structures/7PFS/7pfs_ligand.pdb structures/7PFS/7pfs_ligand.cif structures/7PFS/7pfs_complex.pdb structures/7PFS/7pfs_complex.cif 7PHZ extended SARS-CoV-2 main protease (Mpro/3CLpro) SARS-CoV-2 ORF1ab polyprotein residues 3264-3569 Na X77 "[""X77""]" 1 IC50 IC50 = = 1.7 µM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition FRET biochemical assay with dual-labeled protease substrate; X77 is identified as the R enantiomer. 5 “The racemate showed an IC50 of 3.7 μM, while that of X77 is 1.7 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7PHZ\7PHZ_metadata.json point structures/7PHZ/7phz_protein.pdb structures/7PHZ/7phz_pocket.pdb structures/7PHZ/7phz_ligand.pdb structures/7PHZ/7phz_ligand.cif structures/7PHZ/7phz_complex.pdb structures/7PHZ/7phz_complex.cif 7PIM classic tyrosine hydroxylase (TH) human THDelta35, lacking the first 35 residues Deletion of the first 35 residues (THDelta35) dopamine (DA) "[""LDP""]" 1 IC50 IC50 = = 0.22 ± 0.02 μM 220.0 [] unit_conversion 6.657577319177793 success True biochemical_inhibition Purified THΔ35 activity inhibition by dopamine; IC50 from four-parameter logistic fitting of triplicate curves. 8 “THNΔ35 shows a slightly lower IC50 (0.22 ± 0.02 μM) than TH”; Fig. 5 identifies IC50 values from TH activity versus DA concentration. auto_single_measurement only accepted activity measurement [1] 1 structures\7PIM\7PIM_metadata.json point structures/7PIM/7pim_protein.pdb structures/7PIM/7pim_pocket.pdb structures/7PIM/7pim_ligand.sdf structures/7PIM/7pim_ligand.pdb structures/7PIM/7pim_ligand.cif structures/7PIM/7pim_complex.pdb structures/7PIM/7pim_complex.cif 7PJN classic IDH1 Na Na R132C/S280F DS-1001B "[""7SU""]" 1 IC50 IC50 = = 2.2±0.2 nM 2.2 [] unit_conversion 8.657577319177793 success True biochemical_inhibition UV-based NADPH absorbance inhibition assay; Fig. 3a conditions state IDH1 variants at 30 nM. 5 Fig. 3a lists DS-1001B IC50 for R132C/S280F as 2.2±0.2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7PJN\7PJN_metadata.json point structures/7PJN/7pjn_protein.pdb structures/7PJN/7pjn_pocket.pdb structures/7PJN/7pjn_ligand.sdf structures/7PJN/7pjn_ligand.pdb structures/7PJN/7pjn_ligand.cif structures/7PJN/7pjn_complex.pdb structures/7PJN/7pjn_complex.cif 7PK3 classic Notum Na Na Na 8l (ARUK3001185) "[""7T0""]" 1 IC50 IC50 = = 0.0067 ± 0.0001 µM 6.7 [] unit_conversion 8.173925197299173 success True biochemical_inhibition Notum biochemical inhibition SAR assay; Table 2. 4 Table 2 reports compound 8l IC50 0.0067 ± 0.0001 µM. The preceding text identifies the biochemical assay as human Notum (81–451 Cys330Ser); Figure 5 maps 8l to PDB 7PK3. auto_single_measurement only accepted activity measurement [1] 1 structures\7PK3\7PK3_metadata.json point structures/7PK3/7pk3_protein.pdb structures/7PK3/7pk3_pocket.pdb structures/7PK3/7pk3_ligand.sdf structures/7PK3/7pk3_ligand.pdb structures/7PK3/7pk3_ligand.cif structures/7PK3/7pk3_complex.pdb structures/7PK3/7pk3_complex.cif 7PLR extended La Crosse virus L-protein La Crosse virus N-terminal 183 residues Na baloxavir "[""E4Z""]" 1 Kd Kd = = 0.019 ± 0.006 µM 19.0 [] unit_conversion 7.721246399047171 success True direct_binding Microscale thermophoresis (MST) direct binding measurement in the presence of MnCl2. 5 Table 2 reports an MST Kd of 0.019 ± 0.006 µM for baloxavir; the text states binding was lost without metal ions. auto_single_measurement only accepted activity measurement [1] 1 structures\7PLR\7PLR_metadata.json point structures/7PLR/7plr_ligand.sdf structures/7PLR/7plr_ligand.cif structures/7PLR/7plr_complex.cif 7PMZ classic guaB (IMP dehydrogenase) Streptomyces coelicolor Na Na ATP; ppGpp "[""G4P""]" 1 IC50 IC50 = = 2.0 ± 0.03 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition In-vitro catalytic-activity assay in the presence of 0.25 mM ATP; ppGpp titration. 6 Figure 5 caption reports estimated IC50 values of 8.9 ± 0.4 µM and 2.0 ± 0.03 µM for BsIMPDH and StcIMPDH, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7PMZ\7PMZ_metadata.json point structures/7PMZ/7pmz_protein.pdb structures/7PMZ/7pmz_pocket.pdb structures/7PMZ/7pmz_ligand.sdf structures/7PMZ/7pmz_ligand.pdb structures/7PMZ/7pmz_ligand.cif structures/7PMZ/7pmz_complex.pdb structures/7PMZ/7pmz_complex.cif 7POL classic profragilysin-3 (proBFT-3) Bacteroides fragilis proBFT-3 precursor, residues A18-D397 Na flumequine (C-4) "[""7X9""]" 1 Kd Kd = = 20 (18–23) μM 20000.0 [] unit_conversion 4.698970004336019 success True direct_binding ITC at 25°C and pH 7.4; zinc-bound (+Zn) proBFT-3. 5 Table 1 reports Kd = 20 (18–23) μM for C-4 with +Zn proBFT-3. Page 10 maps C-4/flumequine to PDB 7POL. auto_single_measurement only accepted activity measurement [1] 1 structures\7POL\7POL_metadata.json point structures/7POL/7pol_protein.pdb structures/7POL/7pol_pocket.pdb structures/7POL/7pol_ligand.sdf structures/7POL/7pol_ligand.pdb structures/7POL/7pol_ligand.cif structures/7POL/7pol_complex.pdb structures/7POL/7pol_complex.cif 7POO classic profragilysin-3 (proBFT-3) Bacteroides fragilis proBFT-3 precursor, residues A18-D397 Na foliosidine (C-9) "[""7WK""]" 1 Kd Kd = = 14 (13–16) μM 14000.0 [] unit_conversion 4.853871964321762 success True direct_binding ITC at 25°C and pH 7.4; zinc-bound (+Zn) proBFT-3. 5 Table 1 reports Kd = 14 (13–16) μM for C-9 with +Zn proBFT-3. Page 10 maps the orthorhombic C-9 complex to PDB 7POO. auto_single_measurement only accepted activity measurement [1] 1 structures\7POO\7POO_metadata.json point structures/7POO/7poo_protein.pdb structures/7POO/7poo_pocket.pdb structures/7POO/7poo_ligand.sdf structures/7POO/7poo_ligand.pdb structures/7POO/7poo_ligand.cif structures/7POO/7poo_complex.pdb structures/7POO/7poo_complex.cif 7POP classic PI3 kinase delta Na Na Na compound 5; 5-[3,6-dihydro-2H-pyran-4-yl]-2-methoxy-N-[2-methylpyridin-4-yl]pyridine-3-sulfonamide "[""7VT""]" 1 pIC50 IC50 = = 7.5 31.622776601683793 [] p_metric_transform 7.5 success True biochemical_inhibition Purified PI3Kδ biochemical inhibition assay; Table 1 reports PI3Kδ pIC50. 2 Table 1, compound 5: PI3Kδ pIC50 = 7.5. auto_single_measurement only accepted activity measurement [1] 1 structures\7POP\7POP_metadata.json point structures/7POP/7pop_protein.pdb structures/7POP/7pop_pocket.pdb structures/7POP/7pop_ligand.sdf structures/7POP/7pop_ligand.pdb structures/7POP/7pop_ligand.cif structures/7POP/7pop_complex.pdb structures/7POP/7pop_complex.cif 7POQ classic profragilysin-3 (proBFT-3) Bacteroides fragilis proBFT-3 precursor, residues A18-D397 Na foliosidine (C-9) "[""7WK""]" 1 Kd Kd = = 14 (13–16) μM 14000.0 [] unit_conversion 4.853871964321762 success True direct_binding ITC at 25°C and pH 7.4; zinc-bound (+Zn) proBFT-3. 5 Table 1 reports Kd = 14 (13–16) μM for C-9 with +Zn proBFT-3. Page 10 maps the tetragonal C-9 complex to PDB 7POQ. auto_single_measurement only accepted activity measurement [1] 1 structures\7POQ\7POQ_metadata.json point structures/7POQ/7poq_protein.pdb structures/7POQ/7poq_pocket.pdb structures/7POQ/7poq_ligand.sdf structures/7POQ/7poq_ligand.pdb structures/7POQ/7poq_ligand.cif structures/7POQ/7poq_complex.pdb structures/7POQ/7poq_complex.cif 7POR classic PI3 kinase delta Na Na Na compound 31 (GSK251); N-[2-(2-fluoro-4-{[4-(propan-2-yl)piperazin-1-yl]methyl}phenyl)pyridin-4-yl]-2-methoxy-5-(morpholin-4-yl)pyridine-3-sulfonamide "[""7XH""]" 2 pKi Ki = = 10.9 0.012589254117941661 [] p_metric_transform 10.9 success True biochemical_inhibition Purified PI3Kδ biochemical inhibition assay; Table 3 reports the compound 31 PI3Kδ pIC50/pKi pair. 5 Table 3, compound 31 (GSK251): PI3Kδ pIC50/pKi = 9.1/10.9; 10.9 is the printed pKi value. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7POR\7POR_metadata.json point structures/7POR/7por_protein.pdb structures/7POR/7por_pocket.pdb structures/7POR/7por_ligand.sdf structures/7POR/7por_ligand.pdb structures/7POR/7por_ligand.cif structures/7POR/7por_complex.pdb structures/7POR/7por_complex.cif 7POS classic PI3 kinase delta Na Na Na compound 9; 5-(3,6-dihydro-2H-pyran-4-yl)-2-methoxy-N-(5-{3-[4-(propan-2-yl)piperazin-1-yl]prop-1-yn-1-yl}pyridin-3-yl)pyridine-3-sulfonamide "[""7XN""]" 1 pIC50 IC50 = = 8.2 6.309573444801943 [] p_metric_transform 8.2 success True biochemical_inhibition Purified PI3Kδ biochemical inhibition assay; Table 2 reports PI3Kδ pIC50. 4 Table 2, compound 9: PI3Kδ pIC50 = 8.2. auto_single_measurement only accepted activity measurement [1] 1 structures\7POS\7POS_metadata.json point structures/7POS/7pos_protein.pdb structures/7POS/7pos_pocket.pdb structures/7POS/7pos_ligand.sdf structures/7POS/7pos_ligand.pdb structures/7POS/7pos_ligand.cif structures/7POS/7pos_complex.pdb structures/7POS/7pos_complex.cif 7POT classic PI3 kinase delta Na Na Na compound 4; N-[5-(3,6-dihydro-2H-pyran-4-yl)-2-methoxypyridin-3-yl]benzenesulfonamide "[""7XW""]" 1 pIC50 IC50 = = 7.4 39.81071705534969 [] p_metric_transform 7.4 success True biochemical_inhibition Purified PI3Kδ biochemical inhibition assay; Table 1 reports PI3Kδ pIC50. 2 Table 1, compound 4: PI3Kδ pIC50 = 7.4. auto_single_measurement only accepted activity measurement [1] 1 structures\7POT\7POT_metadata.json point structures/7POT/7pot_protein.pdb structures/7POT/7pot_pocket.pdb structures/7POT/7pot_ligand.sdf structures/7POT/7pot_ligand.pdb structures/7POT/7pot_ligand.cif structures/7POT/7pot_complex.pdb structures/7POT/7pot_complex.cif 7POU classic profragilysin-3 (proBFT-3) Bacteroides fragilis proBFT-3 precursor, residues A18-D397 Na hesperetin (C-10) "[""6JP""]" 1 Kd Kd = = 22 (18–27) μM 22000.0 [] unit_conversion 4.657577319177793 success True direct_binding ITC at 25°C and pH 7.4; zinc-bound (+Zn) proBFT-3. 5 Table 1 reports Kd = 22 (18–27) μM for C-10 with +Zn proBFT-3. Page 10 maps C-10/hesperetin to PDB 7POU. auto_single_measurement only accepted activity measurement [1] 1 structures\7POU\7POU_metadata.json point structures/7POU/7pou_protein.pdb structures/7POU/7pou_pocket.pdb structures/7POU/7pou_ligand.sdf structures/7POU/7pou_ligand.pdb structures/7POU/7pou_ligand.cif structures/7POU/7pou_complex.pdb structures/7POU/7pou_complex.cif 7PP0 extended VIM-2 acquired metallo-beta-lactamase Na Na Na compound 28 (JMV-7038) "[""7ZN""]" 1 Ki Ki = = 0.34 ± 0.02 μM 340.0 [] unit_conversion 6.468521082957745 success True biochemical_inhibition Purified VIM-2 inhibition assay; Ki determined from competitive-inhibition analysis of substrate hydrolysis. 5 Table 1 reports compound 28: VIM-2 Ki = 0.34 ± 0.02 μM. The table footnote states Ki values were determined when inhibition was >75%. auto_single_measurement only accepted activity measurement [1] 1 structures\7PP0\7PP0_metadata.json point structures/7PP0/7pp0_protein.pdb structures/7PP0/7pp0_pocket.pdb structures/7PP0/7pp0_ligand.pdb structures/7PP0/7pp0_ligand.cif structures/7PP0/7pp0_complex.pdb structures/7PP0/7pp0_complex.cif 7PPL extended SHP2 (PTPN11) human (IRS1 substrate peptide) Crystallization-optimized SHP2 phosphatase-domain construct derived from residues 219-528; residues 219-245 removed, loop 315-323 replaced with GSSG, and SGS inserted between the hexahistidine tag and domain C459S human IRS1 ppIRS1 phosphopeptide, residues 625-639, pTyr632 and pSer636 "[""CHAIN:B""]" 1 Kd Kd = = 5.25 ± 0.30 µM 5250.0 [] unit_conversion 5.279840696594043 success True direct_binding Fluorescence-polarization competitive titration using the doubly phosphorylated IRS1 peptide. 3 Fig. 2 reports for SHP2 the ppIRS1 (pTyr+pSer) competitor Kd = 5.25 ± 0.30 µM; the figure caption specifies inactive Cys→Ser mutant phosphatase domains. auto_single_measurement only accepted activity measurement [1] 1 structures\7PPL\7PPL_metadata.json point structures/7PPL/7ppl_protein.pdb structures/7PPL/7ppl_pocket.pdb structures/7PPL/7ppl_ligand.pdb structures/7PPL/7ppl_ligand.cif structures/7PPL/7ppl_complex.pdb structures/7PPL/7ppl_complex.cif 7PPM extended SHP2 (PTPN11) human (IRS1 substrate peptide) Crystallization-optimized SHP2 phosphatase-domain construct derived from residues 219-528; residues 219-245 removed, loop 315-323 replaced with GSSG, and SGS inserted between the hexahistidine tag and domain C459S human IRS1 ppSRev-IRS1 phosphopeptide, residues 889-901, pSer892 and pTyr896 "[""CHAIN:B""]" 1 Kd Kd = = 0.72 ± 0.06 µM 720.0 [] unit_conversion 6.142667503568731 success True direct_binding Fluorescence-polarization assay comparing tyrosine-phosphorylated and doubly phosphorylated SRev-IRS1 peptides. 4 Fig. 3d reports Kd = 0.72 ± 0.06 µM for the pTyr+pSer SRev-IRS1 competitor; the article identifies the crystallographic ppSRev-IRS1 complex as the C459S SHP2 catalytic domain. auto_single_measurement only accepted activity measurement [1] 1 structures\7PPM\7PPM_metadata.json point structures/7PPM/7ppm_protein.pdb structures/7PPM/7ppm_pocket.pdb structures/7PPM/7ppm_ligand.pdb structures/7PPM/7ppm_ligand.cif structures/7PPM/7ppm_complex.pdb structures/7PPM/7ppm_complex.cif 7PPN extended SHP2 (PTPN11) human (CD28 substrate peptide) Crystallization-optimized SHP2 phosphatase-domain construct derived from residues 219-528; residues 219-245 removed, loop 315-323 replaced by GSSG, and SGS inserted between the hexahistidine tag and domain C459S human CD28 ppCD28 phosphopeptide, residues 183-198, pTyr191 and pThr195 "[""CHAIN:B""]" 1 Kd Kd = = 5.66 ± 0.29 µM 5660.0 [] unit_conversion 5.247183568811728 success True direct_binding Fluorescence-polarization competitive titration using the doubly phosphorylated CD28 peptide. 3 Fig. 2 reports for SHP2 the ppCD28 (pTyr+pThr) competitor Kd = 5.66 ± 0.29 µM; the figure caption specifies inactive Cys→Ser mutant phosphatase domains. auto_single_measurement only accepted activity measurement [1] 1 structures\7PPN\7PPN_metadata.json point structures/7PPN/7ppn_protein.pdb structures/7PPN/7ppn_pocket.pdb structures/7PPN/7ppn_ligand.pdb structures/7PPN/7ppn_ligand.cif structures/7PPN/7ppn_complex.pdb structures/7PPN/7ppn_complex.cif 7PRG extended LecB lectin Pseudomonas aeruginosa Perdeuterated LecB (D-LecB) Na Perdeuterated fucose (fucose-d12) "[""FUC""]" 1 Kd Kd = = 7.96 ± 0.42 μM 7960.0 [] unit_conversion 5.099086932262331 success True direct_binding Isothermal titration calorimetry at 25 °C; fully deuterated LecB/fucose system in D2O. 5 “The dissociation constants were also almost identical with KD values of 7.64 (±0.15) μM and 7.96 (±0.42) μM, respectively” for the hydrogenated and deuterated systems. auto_single_measurement only accepted activity measurement [1] 1 structures\7PRG\7PRG_metadata.json point structures/7PRG/7prg_protein.pdb structures/7PRG/7prg_pocket.pdb structures/7PRG/7prg_ligand.pdb structures/7PRG/7prg_ligand.cif structures/7PRG/7prg_complex.pdb structures/7PRG/7prg_complex.cif 7PRQ classic PctD (PA4633) chemoreceptor Pseudomonas aeruginosa PAO1 Ligand-binding domain (LBD), residues 32-361 Na Choline "[""CHT""]" 1 Kd Kd = = 2.6 ± 0.1 µM 2600.0 [] unit_conversion 5.585026652029182 success True direct_binding Isothermal titration calorimetry of purified PctD(PA4633)-LBD. 5 Table 1 reports PctD(PA4633)-LBD binding choline with K_D = 2.6 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7PRQ\7PRQ_metadata.json point structures/7PRQ/7prq_protein.pdb structures/7PRQ/7prq_pocket.pdb structures/7PRQ/7prq_ligand.sdf structures/7PRQ/7prq_ligand.pdb structures/7PRQ/7prq_ligand.cif structures/7PRQ/7prq_complex.pdb structures/7PRQ/7prq_complex.cif 7PRR classic PctD (PA4633) chemoreceptor Pseudomonas aeruginosa PAO1 Ligand-binding domain (LBD), residues 32-361 Na Acetylcholine "[""ACH""]" 1 Kd Kd = = 23 ± 1 µM 23000.0 [] unit_conversion 4.638272163982407 success True direct_binding Isothermal titration calorimetry of purified PctD(PA4633)-LBD. 5 Table 1 reports PctD(PA4633)-LBD binding acetylcholine with K_D = 23 ± 1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7PRR\7PRR_metadata.json point structures/7PRR/7prr_protein.pdb structures/7PRR/7prr_pocket.pdb structures/7PRR/7prr_ligand.sdf structures/7PRR/7prr_ligand.pdb structures/7PRR/7prr_ligand.cif structures/7PRR/7prr_complex.pdb structures/7PRR/7prr_complex.cif 7PS9 classic Cereblon isoform 4 (MsCI4) Magnetospirillum gryphiswaldense Wild-type MsCI4 cloned into pETHis1a; histidine tag cleaved by TEV Wild-type MsCI4 Iberdomide (CC-220) "[""8W7""]" 1 Kd Kd = = 0.409 ± 0.03 µM 409.0 [] unit_conversion 6.388276691992658 success True direct_binding Labelled MST assay measuring iberdomide binding to MsCI4. 5 Table 4 reports MsCI4 (Kd, µM), labelled MST: Iberdomide 0.409 ± 0.03. Table 2 assigns the MsCI4–iberdomide structure to PDB 7ps9. auto_single_measurement only accepted activity measurement [1] 1 structures\7PS9\7PS9_metadata.json point structures/7PS9/7ps9_protein.pdb structures/7PS9/7ps9_pocket.pdb structures/7PS9/7ps9_ligand.sdf structures/7PS9/7ps9_ligand.pdb structures/7PS9/7ps9_ligand.cif structures/7PS9/7ps9_complex.pdb structures/7PS9/7ps9_complex.cif 7PSG classic PacA chemoreceptor (ECA2226; ECA_RS10935) Pectobacterium atrosepticum SCRI1043 Ligand-binding domain (LBD) Na Betaine "[""BET""]" 1 Kd Kd = = 7.5 ± 0.1 µM 7500.0 [] unit_conversion 5.1249387366083 success True direct_binding Isothermal titration calorimetry of purified PacA(ECA_RS10935)-LBD. 5 Table 1 reports PacA(ECA_RS10935)-LBD binding betaine with K_D = 7.5 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7PSG\7PSG_metadata.json point structures/7PSG/7psg_protein.pdb structures/7PSG/7psg_pocket.pdb structures/7PSG/7psg_ligand.sdf structures/7PSG/7psg_ligand.pdb structures/7PSG/7psg_ligand.cif structures/7PSG/7psg_complex.pdb structures/7PSG/7psg_complex.cif 7PSO classic Cereblon isoform 4 (MsCI4) Magnetospirillum gryphiswaldense Wild-type MsCI4 cloned into pETHis1a; histidine tag cleaved by TEV Wild-type MsCI4 Avadomide (CC-122) "[""835""]" 1 Kd Kd = = 4.84 ± 0.3 µM 4840.0 [] unit_conversion 5.315154638355588 success True direct_binding Labelled MST assay measuring avadomide binding to MsCI4. 5 Table 4 reports MsCI4 (Kd, µM), labelled MST: Avadomide 4.84 ± 0.3. Table 2 assigns the MsCI4–avadomide structure to PDB 7pso. auto_single_measurement only accepted activity measurement [1] 1 structures\7PSO\7PSO_metadata.json point structures/7PSO/7pso_protein.pdb structures/7PSO/7pso_pocket.pdb structures/7PSO/7pso_ligand.sdf structures/7PSO/7pso_ligand.pdb structures/7PSO/7pso_ligand.cif structures/7PSO/7pso_complex.pdb structures/7PSO/7pso_complex.cif 7PSY classic LecB lectin Pseudomonas aeruginosa Perdeuterated LecB (D-LecB) Na Perdeuterated fucose (fucose-d12) "[""FUC""]" 1 Kd Kd = = 7.96 ± 0.42 μM 7960.0 [] unit_conversion 5.099086932262331 success True direct_binding Isothermal titration calorimetry at 25 °C; fully deuterated LecB/fucose system in D2O. 5 “The dissociation constants were also almost identical with KD values of 7.64 (±0.15) μM and 7.96 (±0.42) μM, respectively” for the hydrogenated and deuterated systems. auto_single_measurement only accepted activity measurement [1] 1 structures\7PSY\7PSY_metadata.json point structures/7PSY/7psy_protein.pdb structures/7PSY/7psy_pocket.pdb structures/7PSY/7psy_ligand.sdf structures/7PSY/7psy_ligand.pdb structures/7PSY/7psy_ligand.cif structures/7PSY/7psy_complex.pdb structures/7PSY/7psy_complex.cif 7PSZ classic calmodulin (CaM) human Na Na calmidazolium chloride (CDZ; R_24571) "[""85H""]" 1 Kd Kd = = 3 ± 2 µM 3000.0 [] unit_conversion 5.522878745280337 success True direct_binding Isothermal titration calorimetry of CDZ binding to holo-CaM; reported binding stoichiometry 1.2 ± 0.5, consistent with the one-CDZ 7PSZ complex. 3 “The data indicated an apparent equilibrium dissociation KD constant of 3 ± 2 µM with a stoichiometry of 1.2 ± 0.5.” auto_single_measurement only accepted activity measurement [1] 1 structures\7PSZ\7PSZ_metadata.json point structures/7PSZ/7psz_protein.pdb structures/7PSZ/7psz_pocket.pdb structures/7PSZ/7psz_ligand.sdf structures/7PSZ/7psz_ligand.pdb structures/7PSZ/7psz_ligand.cif structures/7PSZ/7psz_complex.pdb structures/7PSZ/7psz_complex.cif 7PU7 classic DNA polymerase III alpha subunit (DnaE1) Mycobacterium tuberculosis full-length Mtb DnaE1 Na nargenicin (nargenicin A1) "[""82W""]" 1 IC50 IC50 = = 125 nM 125.0 [] unit_conversion 6.903089986991944 success True biochemical_inhibition Real-time purified-polymerase activity assay using Mtb DnaE1 and a fluorescently labelled DNA substrate. 5 Figure 4 caption states that nargenicin inhibition curves for S. aureus DnaE, Mtb DnaE1, and E. coli Pol IIIα show IC50 values of 8, 125, and 13,000 nM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7PU7\7PU7_metadata.json point structures/7PU7/7pu7_protein.pdb structures/7PU7/7pu7_pocket.pdb structures/7PU7/7pu7_ligand.sdf structures/7PU7/7pu7_ligand.pdb structures/7PU7/7pu7_ligand.cif structures/7PU7/7pu7_complex.pdb structures/7PU7/7pu7_complex.cif 7PUS extended ERK5 Na ERK5 kinase domain, residues 46-402 Na compound 34b "[""86E""]" 1 IC50 IC50 = = 79 ± 40 nM 79.0 [] unit_conversion 7.102372908709558 success True biochemical_inhibition ERK5 IMAP FP progressive binding-system inhibition assay. 10 Table 4 reports ERK5 IC50 = 79 ± 40 nM for compound 34b; the table footnote specifies an IMAP FP progressive binding system kit. auto_single_measurement only accepted activity measurement [1] 1 structures\7PUS\7PUS_metadata.json point structures/7PUS/7pus_ligand.cif structures/7PUS/7pus_complex.cif 7PWY classic alpha-amino-beta-carboxymuconate-e-semialdehyde decarboxylase (ACMSD) Homo sapiens (human) Na Na TES-1025 "[""8EK""]" 1 Ki Ki = = 0.85 ± 0.22 nM 0.85 [] unit_conversion 9.070581074285707 success True biochemical_inhibition Coupled spectrophotometric ACMSD activity assay with varying TES-1025 and substrate concentrations; Dixon analysis for tightly bound competitive inhibition. 6 “A Ki value of 0.85 ± 0.22 nM was calculated.” auto_single_measurement only accepted activity measurement [1] 1 structures\7PWY\7PWY_metadata.json point structures/7PWY/7pwy_protein.pdb structures/7PWY/7pwy_pocket.pdb structures/7PWY/7pwy_ligand.sdf structures/7PWY/7pwy_ligand.pdb structures/7PWY/7pwy_ligand.cif structures/7PWY/7pwy_complex.pdb structures/7PWY/7pwy_complex.cif 7PX4 extended adenosine A2A receptor Na A2A-PSB1-bRIL S91K PSB-2113 "[""8E2""]" 1 Ki Ki = = 19.6 nM 19.6 [] unit_conversion 7.707743928643524 success True direct_binding Competitive radioligand binding using [3H]MSX-2 in Sf9 insect-cell membranes expressing A2A-PSB1-bRIL; reported as the mutant affinity versus WT (19.6 nM versus 6.30 nM). 5 “the affinity of PSB-2113 was slightly (≈3-fold) lower at the mutant than at the wt A2AAR, but still in the low nanomolar range (19.6 nM vs. 6.30 nM)” auto_single_measurement only accepted activity measurement [1] 1 structures\7PX4\7PX4_metadata.json point structures/7PX4/7px4_protein.pdb structures/7PX4/7px4_pocket.pdb structures/7PX4/7px4_ligand.pdb structures/7PX4/7px4_ligand.cif structures/7PX4/7px4_complex.pdb structures/7PX4/7px4_complex.cif 7PX5 extended ATPase family AAA domain-containing protein 2 (ATAD2) Na Na Na 1-Methyl-2-quinolone "[""12Q""]" 1 IC50 IC50 = = 2.6 mM 2600000.0 [] unit_conversion 2.585026652029182 success True biochemical_inhibition 384-well low-volume HTRF assay measuring displacement/inhibition of the GST-ATAD2–biotinylated histone H4 interaction; 1-methyl-2-quinolone was a structurally guided analogue. 6 “One of these catalogue compounds was 1-methyl-2-quinolone, the crystal structure with which (PDB entry 7px5) ... resulted in an on-scale IC50 of 2.6 mM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7PX5\7PX5_metadata.json point structures/7PX5/7px5_ligand.sdf structures/7PX5/7px5_ligand.cif structures/7PX5/7px5_complex.cif 7PZ1 extended mouse 8-oxoguanine DNA glycosylase 1 (mOGG1) mouse Na Na TH8535 "[""8HA""]" 1 IC50 IC50 = = 0.20 μM 200.0 [] unit_conversion 6.698970004336019 success True biochemical_inhibition Biochemical OGG1 inhibition assay; Table 5 reports the TH8535 (compound 55) result with a 95% confidence interval of 0.11–0.36 μM. 4 Table 5 lists TH8535 (55) with IC50 0.20 (0.11–0.36) μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7PZ1\7PZ1_metadata.json point structures/7PZ1/7pz1_ligand.sdf structures/7PZ1/7pz1_ligand.cif structures/7PZ1/7pz1_complex.cif 7PZA classic Clr Sinorhizobium meliloti Na Na cAMP "[""CMP""]" 1 Kd Kd = = 6.7 ± 2.7 µM 6700.0 [] unit_conversion 5.173925197299173 success True direct_binding ITC; cell: Clr, DNA; injectant: cAMP. Ternary Clr-cAMP-DNA assembly. 8 Table 1 reports Clr, DNA with cAMP: K_D 6.7 ± 2.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7PZA\7PZA_metadata.json point structures/7PZA/7pza_protein.pdb structures/7PZA/7pza_pocket.pdb structures/7PZA/7pza_ligand.sdf structures/7PZA/7pza_ligand.pdb structures/7PZA/7pza_ligand.cif structures/7PZA/7pza_complex.pdb structures/7PZA/7pza_complex.cif 7PZB classic Clr Sinorhizobium meliloti Na Na Na "[""PCG""]" 1 Kd Kd = = 10.7 ± 3.7 µM 10700.0 [] unit_conversion 4.97061622231479 success True direct_binding ITC; cell: Clr, DNA; injectant: cGMP. Ternary Clr-cGMP-DNA assembly. 8 Table 1 reports Clr, DNA with cGMP: K_D 10.7 ± 3.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7PZB\7PZB_metadata.json point structures/7PZB/7pzb_protein.pdb structures/7PZB/7pzb_pocket.pdb structures/7PZB/7pzb_ligand.sdf structures/7PZB/7pzb_ligand.pdb structures/7PZB/7pzb_ligand.cif structures/7PZB/7pzb_complex.pdb structures/7PZB/7pzb_complex.cif 7PZK classic HBc Na Na wild-type (WT) Triton X-100 (TX100) "[""TRT""]" 1 Kd Kd = = 11.6 ± 0.4 µM 11600.0 [] unit_conversion 4.935542010773082 success True direct_binding ITC of TX100 binding to wt HBc-CLPs at 310 K. 5 “Binding of wt HBc-CLPs to TX100 was quantified by Isothermal Titration Calorimetry (ITC) ... K_D = 11.6 ± 0.4 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7PZK\7PZK_metadata.json point structures/7PZK/7pzk_protein.pdb structures/7PZK/7pzk_pocket.pdb structures/7PZK/7pzk_ligand.sdf structures/7PZK/7pzk_ligand.pdb structures/7PZK/7pzk_ligand.cif structures/7PZK/7pzk_complex.pdb structures/7PZK/7pzk_complex.cif 7Q19 extended beta-lactoglobulin Na FAW mutant with N-terminal L1A/I2S substitutions L1A/I2S; L39A/I56F/M107W desipramine (DSM), FAW-DSM#3 "[""DSM""]" 1 Kd Kd = = 31 ± 6 μM 31000.0 [] unit_conversion 4.508638306165727 success True direct_binding ITC titration at pH 7.5 and 293 K; one-set-of-binding-sites model. 9 Table 2 reports FAW (pH 7.5) Kd = 31 ± 6 μM for DSM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q19\7Q19_metadata.json point structures/7Q19/7q19_ligand.sdf structures/7Q19/7q19_ligand.cif structures/7Q19/7q19_complex.cif 7Q1B classic Trypanosoma cruzi histone deacetylase DAC2 Trypanosoma cruzi tcDAC2_deltaIns2 Na Quisinostat "[""GOK""]" 1 IC50 IC50 = = 45 ± 5 nM 45.0 [] unit_conversion 7.346787486224656 success True biochemical_inhibition Biochemical inhibition of tcDAC2 DeltaIns2. 0 The supplement reports Quisinostat IC50 45 ± 5 nM for tcDAC2 DeltaIns2. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q1B\7Q1B_metadata.json point structures/7Q1B/7q1b_protein.pdb structures/7Q1B/7q1b_pocket.pdb structures/7Q1B/7q1b_ligand.sdf structures/7Q1B/7q1b_ligand.pdb structures/7Q1B/7q1b_ligand.cif structures/7Q1B/7q1b_complex.pdb structures/7Q1B/7q1b_complex.cif 7Q1C classic Trypanosoma cruzi histone deacetylase DAC2 Trypanosoma cruzi tcDAC2_deltaIns2 Na TB56 "[""T56""]" 1 IC50 IC50 = = 1150 ± 220 nM 1150.0 [] unit_conversion 5.939302159646388 success True biochemical_inhibition Biochemical inhibition of tcDAC2. 0 The supplement reports TB56 IC50 1150 ± 220 nM for tcDAC2. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q1C\7Q1C_metadata.json point structures/7Q1C/7q1c_protein.pdb structures/7Q1C/7q1c_pocket.pdb structures/7Q1C/7q1c_ligand.sdf structures/7Q1C/7q1c_ligand.pdb structures/7Q1C/7q1c_ligand.cif structures/7Q1C/7q1c_complex.pdb structures/7Q1C/7q1c_complex.cif 7Q1W extended Ruminococcus gnavus ATCC 29149 endo-beta-1,4-galactosidase (RgGH98) Ruminococcus gnavus Residues 44-946, excluding the signal peptide, C-terminal GBLD, and C-terminal FN3 domain; N-terminal His6 tag E411A BgA II (blood group A tetrasaccharide type II) "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 490.3 ± 48.3 μM 490300.0 [] unit_conversion 3.3095381067538217 success True direct_binding Isothermal titration calorimetry (ITC) of RgGH98 E411A with BgA II; the paper states the mutant bound BgA II with this Kd. 9 “RgGH98 E411A bound to BgA II with a Kd of 490.3 μM (Fig 6A, S2 Table).” Figure 6 prints Kd = 490.3 ± 48.3 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q1W\7Q1W_metadata.json point structures/7Q1W/7q1w_protein.pdb structures/7Q1W/7q1w_pocket.pdb structures/7Q1W/7q1w_ligand.pdb structures/7Q1W/7q1w_ligand.cif structures/7Q1W/7q1w_complex.pdb structures/7Q1W/7q1w_complex.cif 7Q3F classic Bromodomain-containing 4 (BRD4) Na Na Na CRCM5484 "[""8M6""]" 1 IC50 IC50 = = 130 nM 130.0 [] unit_conversion 6.886056647693163 success True direct_binding HTRF assay on purified BRD4-BDI. 5 “CRCM5484 ... exhibited a BDII-selective profile with values of 130, 20, and 71 nM for the BDIs ... of BRD4, BRD3, and BRD2, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7Q3F\7Q3F_metadata.json point structures/7Q3F/7q3f_protein.pdb structures/7Q3F/7q3f_pocket.pdb structures/7Q3F/7q3f_ligand.sdf structures/7Q3F/7q3f_ligand.pdb structures/7Q3F/7q3f_ligand.cif structures/7Q3F/7q3f_complex.pdb structures/7Q3F/7q3f_complex.cif 7Q5O classic Bromodomain-containing 2 (BRD2) Na Na Na CRCM5484 "[""8M6""]" 1 IC50 IC50 = = 4700 nM 4700.0 [] unit_conversion 5.327902142064282 success True direct_binding HTRF assay on purified BRD2-BDII. 5 “CRCM5484 ... exhibited a BDII-selective profile with values of ... 1300, 9500, and 4700 nM for the BDIIs of BRD4, BRD3, and BRD2, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7Q5O\7Q5O_metadata.json point structures/7Q5O/7q5o_protein.pdb structures/7Q5O/7q5o_pocket.pdb structures/7Q5O/7q5o_ligand.sdf structures/7Q5O/7q5o_ligand.pdb structures/7Q5O/7q5o_ligand.cif structures/7Q5O/7q5o_complex.pdb structures/7Q5O/7q5o_complex.cif 7Q6H extended JAK3 human Na Na compound 18; 1-(4-((2-((1-methyl-1H-pyrazol-4-yl)amino)quinazolin-8-yl)amino)piperidin-1-yl)ethan-1-one "[""934""]" 1 pIC50 IC50 = = 7.3 50.11872336272725 [] p_metric_transform 7.3 success True biochemical_inhibition JAK FRET biochemical assay at ATP Km; JAK3 pIC50 (LE) reported for compound 18. 3 Table 1 reports compound 18 JAK3 pIC50 (LE) = 7.3 (0.37). Figure 2 identifies compound 18 bound to JAK3 as PDB 7Q6H. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q6H\7Q6H_metadata.json point structures/7Q6H/7q6h_ligand.sdf structures/7Q6H/7q6h_ligand.cif structures/7Q6H/7q6h_complex.cif 7Q6R classic OleP Streptomyces antibioticus Recombinant His-tagged OleP mutant produced from the pET28b(+)-OleP construct E89Y 6DEB "[""DEB""]" 1 Kd Kd = = 8.5 ± 0.8 µM 8500.0 [] unit_conversion 5.070581074285707 success True direct_binding Equilibrium UV-visible spectroscopic titration of purified recombinant His-tagged OleP E89Y with 6DEB at 298 K; hyperbolic fit. 4 Figure 2 reports E89Y binding to 6DEB with K_D = 8.5 ± 0.8 µM; the methods state that all OleP mutants were tested for equilibrium binding to 6DEB. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q6R\7Q6R_metadata.json point structures/7Q6R/7q6r_protein.pdb structures/7Q6R/7q6r_pocket.pdb structures/7Q6R/7q6r_ligand.sdf structures/7Q6R/7q6r_ligand.pdb structures/7Q6R/7q6r_ligand.cif structures/7Q6R/7q6r_complex.pdb structures/7Q6R/7q6r_complex.cif 7Q6T classic ATAD2 Na 6His-TEV-ATAD2, residues 981-1108 Na AZ13824374; compound 5 "[""96L""]" 1 pKd Kd = = 8.9 unitless 1.2589254117941662 [] p_metric_transform 8.9 success True direct_binding BROMOscan panel; ATAD2 binding potency. 2 Table 1 reports compound 5 (AZ13824374), PDB 7Q6T, with ATAD2 binding potency pKD 8.9 by BROMOscan. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q6T\7Q6T_metadata.json point structures/7Q6T/7q6t_protein.pdb structures/7Q6T/7q6t_pocket.pdb structures/7Q6T/7q6t_ligand.sdf structures/7Q6T/7q6t_ligand.pdb structures/7Q6T/7q6t_ligand.cif structures/7Q6T/7q6t_complex.pdb structures/7Q6T/7q6t_complex.cif 7Q6X classic OleP Streptomyces antibioticus Recombinant His-tagged OleP mutant produced from the pET28b(+)-OleP construct S240Y 6DEB "[""DEB""]" 1 Kd Kd = = 0.7 ± 0.1 µM 700.0 [] unit_conversion 6.154901959985743 success True direct_binding Equilibrium UV-visible spectroscopic titration of purified recombinant His-tagged OleP S240Y with 6DEB at 298 K; hyperbolic fit. 4 Figure 2 reports S240Y binding to 6DEB with K_D = 0.7 ± 0.1 µM; the methods state that all OleP mutants were tested for equilibrium binding to 6DEB. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q6X\7Q6X_metadata.json point structures/7Q6X/7q6x_protein.pdb structures/7Q6X/7q6x_pocket.pdb structures/7Q6X/7q6x_ligand.sdf structures/7Q6X/7q6x_ligand.pdb structures/7Q6X/7q6x_ligand.cif structures/7Q6X/7q6x_complex.pdb structures/7Q6X/7q6x_complex.cif 7Q7I classic JAK2 Na Na Na compound 19; 4-(8-methoxy-2-((1-methyl-1H-pyrazol-4-yl)amino)quinazolin-6-yl)phenol "[""9I8""]" 1 pIC50 IC50 > < 9.8 0.1584893192461111 [] p_metric_transform 9.8 success True biochemical_inhibition JAK FRET biochemical assay at ATP Km; JAK2 pIC50 (LE) reported for compound 19. 5 Table 2 reports compound 19 JAK2 pIC50 (LE) >9.8 (>0.52). Figure 4a identifies the JAK2 crystal structure of compound 19 as PDB 7Q7I. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7I\7Q7I_metadata.json point structures/7Q7I/7q7i_protein.pdb structures/7Q7I/7q7i_pocket.pdb structures/7Q7I/7q7i_ligand.sdf structures/7Q7I/7q7i_ligand.pdb structures/7Q7I/7q7i_ligand.cif structures/7Q7I/7q7i_complex.pdb structures/7Q7I/7q7i_complex.cif 7Q7K classic JAK2 Na Na Na compound 20; 4-(2-amino-8-methoxyquinazolin-6-yl)phenol "[""9I5""]" 1 pIC50 IC50 = = 7.5 31.622776601683793 [] p_metric_transform 7.5 success True biochemical_inhibition JAK FRET biochemical assay at ATP Km; JAK2 pIC50 (LE) reported for compound 20. 5 Table 2 reports compound 20 JAK2 pIC50 (LE) = 7.5 (0.51). Figure 4b identifies the JAK2 crystal structure of compound 20 as PDB 7Q7K. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7K\7Q7K_metadata.json point structures/7Q7K/7q7k_protein.pdb structures/7Q7K/7q7k_pocket.pdb structures/7Q7K/7q7k_ligand.sdf structures/7Q7K/7q7k_ligand.pdb structures/7Q7K/7q7k_ligand.cif structures/7Q7K/7q7k_complex.pdb structures/7Q7K/7q7k_complex.cif 7Q7L classic JAK2 Na Na Na compound 46e; 4-(2-amino-8-(((2S)-1-hydroxypropan-2-yl)amino)quinazolin-6-yl)-5-ethyl-2-fluorophenol "[""9I2""]" 1 pIC50 IC50 = = 9.1 0.7943282347242822 [] p_metric_transform 9.1 success True biochemical_inhibition JAK FRET biochemical assay at ATP Km; JAK2 pIC50 (LE) reported for compound 46e. 8 Table 4 reports compound 46e JAK pIC50 values 9.3, 9.1, 9.1, and 7.4 for JAK1, JAK2, JAK3, and TYK2, respectively. Figure 5 identifies compound 46e in JAK2 as PDB 7Q7L. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7L\7Q7L_metadata.json point structures/7Q7L/7q7l_protein.pdb structures/7Q7L/7q7l_pocket.pdb structures/7Q7L/7q7l_ligand.sdf structures/7Q7L/7q7l_ligand.pdb structures/7Q7L/7q7l_ligand.cif structures/7Q7L/7q7l_complex.pdb structures/7Q7L/7q7l_complex.cif 7Q7R classic BCL6 human Na Na compound 1 (CCT372064) "[""9IH""]" 1 IC50 IC50 = = 0.0039 µM 3.9 [] unit_conversion 8.4089353929735 success True biochemical_inhibition BCL6 TR-FRET biochemical assay. 6 Table 3 reports compound 1 BCL6 TR-FRET IC50 = 0.0039 µM; Figure 5 maps compound 1 to PDB 7Q7R. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7R\7Q7R_metadata.json point structures/7Q7R/7q7r_protein.pdb structures/7Q7R/7q7r_pocket.pdb structures/7Q7R/7q7r_ligand.sdf structures/7Q7R/7q7r_ligand.pdb structures/7Q7R/7q7r_ligand.cif structures/7Q7R/7q7r_complex.pdb structures/7Q7R/7q7r_complex.cif 7Q7S classic BCL6 human Na Na compound 4 "[""97S""]" 1 IC50 IC50 = = 5.6 µM 5600.0 [] unit_conversion 5.251811972993799 success True biochemical_inhibition BCL6 TR-FRET biochemical assay. 3 Table 1 reports compound 4 BCL6 TR-FRET IC50 = 5.6 µM; Figure 2B maps compound 4 to PDB 7Q7S. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7S\7Q7S_metadata.json point structures/7Q7S/7q7s_protein.pdb structures/7Q7S/7q7s_pocket.pdb structures/7Q7S/7q7s_ligand.sdf structures/7Q7S/7q7s_ligand.pdb structures/7Q7S/7q7s_ligand.cif structures/7Q7S/7q7s_complex.pdb structures/7Q7S/7q7s_complex.cif 7Q7T classic BCL6 human Na Na compound 7 "[""9FW""]" 1 IC50 IC50 = = 0.094 µM 94.0 [] unit_conversion 7.026872146400302 success True biochemical_inhibition BCL6 TR-FRET biochemical assay. 3 Table 1 reports compound 7 BCL6 TR-FRET IC50 = 0.094 µM; Figure 3 maps compound 7 to PDB 7Q7T. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7T\7Q7T_metadata.json point structures/7Q7T/7q7t_protein.pdb structures/7Q7T/7q7t_pocket.pdb structures/7Q7T/7q7t_ligand.sdf structures/7Q7T/7q7t_ligand.pdb structures/7Q7T/7q7t_ligand.cif structures/7Q7T/7q7t_complex.pdb structures/7Q7T/7q7t_complex.cif 7Q7U classic BCL6 human Na Na compound 9a "[""9IE""]" 1 IC50 IC50 = = 0.13 µM 130.0 [] unit_conversion 6.886056647693163 success True biochemical_inhibition BCL6 TR-FRET biochemical assay. 3 Table 1 reports compound 9a BCL6 TR-FRET IC50 = 0.13 µM; Figure 3 maps compound 9a to PDB 7Q7U. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7U\7Q7U_metadata.json point structures/7Q7U/7q7u_protein.pdb structures/7Q7U/7q7u_pocket.pdb structures/7Q7U/7q7u_ligand.sdf structures/7Q7U/7q7u_ligand.pdb structures/7Q7U/7q7u_ligand.cif structures/7Q7U/7q7u_complex.pdb structures/7Q7U/7q7u_complex.cif 7Q7V classic BCL6 human Na Na compound 12a "[""9GR""]" 1 IC50 IC50 = = 0.039 µM 39.0 [] unit_conversion 7.4089353929735005 success True biochemical_inhibition BCL6 TR-FRET biochemical assay. 6 Table 3 reports compound 12a BCL6 TR-FRET IC50 = 0.039 µM; Figure 4 maps compound 12a to PDB 7Q7V. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7V\7Q7V_metadata.json point structures/7Q7V/7q7v_protein.pdb structures/7Q7V/7q7v_pocket.pdb structures/7Q7V/7q7v_ligand.sdf structures/7Q7V/7q7v_ligand.pdb structures/7Q7V/7q7v_ligand.cif structures/7Q7V/7q7v_complex.pdb structures/7Q7V/7q7v_complex.cif 7Q7W classic JAK2 Na Na Na compound 54c; 4-(2-((5-(dimethylamino)pentyl)amino)-8-(((2S)-1-hydroxypropan-2-yl)amino)quinazolin-6-yl)-5-ethyl-2-fluorophenol "[""9HR""]" 1 pIC50 IC50 = = 9.3 0.5011872336272715 [] p_metric_transform 9.3 success True biochemical_inhibition JAK FRET biochemical assay at ATP Km; JAK2 pIC50 (LE) reported for compound 54c. 12 Table 5 reports compound 54c JAK pIC50 values 9.2, 9.3, 9.3, and 7.7 for JAK1, JAK2, JAK3, and TYK2, respectively. Figure 14 identifies compound 54c in JAK2 as PDB 7Q7W. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q7W\7Q7W_metadata.json point structures/7Q7W/7q7w_protein.pdb structures/7Q7W/7q7w_pocket.pdb structures/7Q7W/7q7w_ligand.sdf structures/7Q7W/7q7w_ligand.pdb structures/7Q7W/7q7w_ligand.cif structures/7Q7W/7q7w_complex.pdb structures/7Q7W/7q7w_complex.cif 7Q89 classic OleP Streptomyces antibioticus Recombinant His-tagged OleP mutant produced from the pET28b(+)-OleP construct G92W 6DEB "[""DEB""]" 1 Kd Kd = = 1.2 ± 0.1 µM 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding Equilibrium UV-visible spectroscopic titration of purified recombinant His-tagged OleP G92W with 6DEB at 298 K; hyperbolic fit. 4 Figure 2 reports G92W binding to 6DEB with K_D = 1.2 ± 0.1 µM; the methods state that all OleP mutants were tested for equilibrium binding to 6DEB. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q89\7Q89_metadata.json point structures/7Q89/7q89_protein.pdb structures/7Q89/7q89_pocket.pdb structures/7Q89/7q89_ligand.sdf structures/7Q89/7q89_ligand.pdb structures/7Q89/7q89_ligand.cif structures/7Q89/7q89_complex.pdb structures/7Q89/7q89_complex.cif 7Q8V classic TTBK1 human TTBK1 residues 13-320 Na VNG2.73 (compound 42) "[""9IV""]" 1 IC50 IC50 = = 0.53 μM 530.0 [] unit_conversion 6.275724130399211 success True biochemical_inhibition Inhibition of human recombinant TTBK1 measured by the MRC Phosphorylation Unit; Table 2 reports the compound-42 enzymatic result. 5 Table 2 lists compound 42 with TTBK1 IC50 = 0.53 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q8V\7Q8V_metadata.json point structures/7Q8V/7q8v_protein.pdb structures/7Q8V/7q8v_pocket.pdb structures/7Q8V/7q8v_ligand.sdf structures/7Q8V/7q8v_ligand.pdb structures/7Q8V/7q8v_ligand.cif structures/7Q8V/7q8v_complex.pdb structures/7Q8V/7q8v_complex.cif 7Q8W classic TTBK1 human TTBK1 residues 13-320 Na VNG1.35 (compound 23) "[""9IO""]" 1 IC50 IC50 = = 0.52 μM 520.0 [] unit_conversion 6.2839966563652006 success True biochemical_inhibition Inhibition of human recombinant TTBK1 measured by the MRC Phosphorylation Unit; Table 1 reports the compound-23 enzymatic result. 4 Table 1 lists compound 23 with TTBK1 IC50 = 0.52 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q8W\7Q8W_metadata.json point structures/7Q8W/7q8w_protein.pdb structures/7Q8W/7q8w_pocket.pdb structures/7Q8W/7q8w_ligand.sdf structures/7Q8W/7q8w_ligand.pdb structures/7Q8W/7q8w_ligand.cif structures/7Q8W/7q8w_complex.pdb structures/7Q8W/7q8w_complex.cif 7Q8Y classic TTBK2 Na TTBK2 residues 1-299 Na VNG2.73 (compound 42) "[""9IV""]" 1 IC50 IC50 = = 0.49 μM 490.0 [] unit_conversion 6.309803919971486 success True biochemical_inhibition Inhibition of human recombinant TTBK2 measured by the MRC Phosphorylation Unit; Table 2 reports the compound-42 enzymatic result. 5 Table 2 lists compound 42 with TTBK2 IC50 = 0.49 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q8Y\7Q8Y_metadata.json point structures/7Q8Y/7q8y_protein.pdb structures/7Q8Y/7q8y_pocket.pdb structures/7Q8Y/7q8y_ligand.sdf structures/7Q8Y/7q8y_ligand.pdb structures/7Q8Y/7q8y_ligand.cif structures/7Q8Y/7q8y_complex.pdb structures/7Q8Y/7q8y_complex.cif 7Q8Z classic TTBK2 Na TTBK2 residues 1-299 Na VNG1.33 (compound 27) "[""9IK""]" 1 IC50 IC50 = = 0.85 μM 850.0 [] unit_conversion 6.070581074285707 success True biochemical_inhibition Inhibition of human recombinant TTBK2 measured by the MRC Phosphorylation Unit; Table 1 reports the compound-27 enzymatic result. 4 Table 1 lists compound 27 with TTBK2 IC50 = 0.85 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q8Z\7Q8Z_metadata.json point structures/7Q8Z/7q8z_protein.pdb structures/7Q8Z/7q8z_pocket.pdb structures/7Q8Z/7q8z_ligand.sdf structures/7Q8Z/7q8z_ligand.pdb structures/7Q8Z/7q8z_ligand.cif structures/7Q8Z/7q8z_complex.pdb structures/7Q8Z/7q8z_complex.cif 7Q90 classic TTBK2 Na TTBK2 residues 1-299 Na VNG1.63 (compound 32) "[""9IS""]" 1 IC50 IC50 = = 0.97 μM 970.0 [] unit_conversion 6.013228265733755 success True biochemical_inhibition Inhibition of human recombinant TTBK2 measured by the MRC Phosphorylation Unit; Table 2 reports the compound-32 enzymatic result. 5 Table 2 lists compound 32 with TTBK2 IC50 = 0.97 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Q90\7Q90_metadata.json point structures/7Q90/7q90_protein.pdb structures/7Q90/7q90_pocket.pdb structures/7Q90/7q90_ligand.sdf structures/7Q90/7q90_ligand.pdb structures/7Q90/7q90_ligand.cif structures/7Q90/7q90_complex.pdb structures/7Q90/7q90_complex.cif 7QAK classic acetylcholinesterase (AChE) Mus musculus Na Na compound 1; 7-[(4-{[benzyl(methyl)amino]methyl}benzyl)oxy]-4-(hydroxymethyl)-2H-chromen-2-one "[""5IK""]" 1 IC50 IC50 = = 0.40 ± 0.03 µM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition Spectrophotometric Ellman's method on purified recombinant enzyme. 2 Table 1 reports mouse AChE IC50 for 1 as 0.40 ± 0.03 µM; Table 2 maps mouse AChE–1 to 7QAK. auto_single_measurement only accepted activity measurement [1] 1 structures\7QAK\7QAK_metadata.json point structures/7QAK/7qak_protein.pdb structures/7QAK/7qak_pocket.pdb structures/7QAK/7qak_ligand.sdf structures/7QAK/7qak_ligand.pdb structures/7QAK/7qak_ligand.cif structures/7QAK/7qak_complex.pdb structures/7QAK/7qak_complex.cif 7QB1 extended PPARgamma human PPARgamma ligand binding domain (LBD) Na compound 10 "[""9WQ""]" 1 IC50 IC50 = = 24 ± 14 nM 24.0 [] unit_conversion 7.619788758288394 success True direct_binding PPARγ binding IC50; the text identifies compound 10 as a 24 nM binder to human PPARγ. 3 Table 1 prints “PPARγ binding IC50 (nM)” for compound 10 as “24 ± 14”; adjacent text states that compound 10 is “a 24 nM binder to human PPARγ.” auto_single_measurement only accepted activity measurement [1] 1 structures\7QB1\7QB1_metadata.json point structures/7QB1/7qb1_ligand.sdf structures/7QB1/7qb1_ligand.cif structures/7QB1/7qb1_complex.cif 7QBB classic SARS-CoV-2 main protease (Nsp5) SARS-CoV-2 Residues S1-Q306; N-terminal GST tag followed by an Mpro recognition sequence; C-terminal 6x His tag preceded by an HRV Mpro recognition sequence Na compound 18 "[""V1B""]" 2 Kd Kd = = 0.17 μM 170.0 [] unit_conversion 6.769551078621726 success True direct_binding SPR biosensor assay of purified Mpro. 7 The text states that compound 18 displayed Kd = 0.17 μM and identifies its Mpro crystal structure in Figure 3c. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7QBB\7QBB_metadata.json point structures/7QBB/7qbb_protein.pdb structures/7QBB/7qbb_pocket.pdb structures/7QBB/7qbb_ligand.sdf structures/7QBB/7qbb_ligand.pdb structures/7QBB/7qbb_ligand.cif structures/7QBB/7qbb_complex.pdb structures/7QBB/7qbb_complex.cif 7QBR classic human butyrylcholinesterase human Na Na compound 15; (Z)-N-tert-butyl-1-(8-(3-(4-(prop-2-yn-1-yl)piperazin-1-yl)propoxy)quinolin-2-yl)methanimine oxide "[""AI6""]" 1 IC50 IC50 = = 0.0073 ± 0.0011 µmol/L 7.3 [] unit_conversion 8.136677139879545 success True biochemical_inhibition Ellman cholinesterase inhibition assay; Table 2 reports IC50 as average ± SEM (n = 3, triplicates). 5 Table 2 lists compound 15: hBChE IC50 = 0.0073 ± 0.0011 µmol/L. auto_single_measurement only accepted activity measurement [1] 1 structures\7QBR\7QBR_metadata.json point structures/7QBR/7qbr_protein.pdb structures/7QBR/7qbr_pocket.pdb structures/7QBR/7qbr_ligand.sdf structures/7QBR/7qbr_ligand.pdb structures/7QBR/7qbr_ligand.cif structures/7QBR/7qbr_complex.pdb structures/7QBR/7qbr_complex.cif 7QC5 classic human wild type transthyretin human Na wild type M-23; (3,4-dihydroxy-5-nitrophenyl)-(3-fluoro-5-hydroxyphenyl)methanone "[""AQI""]" 1 Kd Kd = = 6.2 nM 6.2 [] unit_conversion 8.207608310501746 success True direct_binding Isothermal titration calorimetry binding of M-23 to WT-TTR; Table 4. 7 Table 4, “Thermodynamic Parameters Determined by ITC for the Binding of M-20, M-21, and M-23 to WT-TTR,” reports M-23 Kd = 6.2 nM. The text identifies M-23 as the ligand whose crystal structure with TTR was determined (PDB 7QC5). auto_single_measurement only accepted activity measurement [1] 1 structures\7QC5\7QC5_metadata.json point structures/7QC5/7qc5_protein.pdb structures/7QC5/7qc5_pocket.pdb structures/7QC5/7qc5_ligand.sdf structures/7QC5/7qc5_ligand.pdb structures/7QC5/7qc5_ligand.cif structures/7QC5/7qc5_complex.pdb structures/7QC5/7qc5_complex.cif 7QCM classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 PLpro residues 746-1060 of SARS-CoV-2 nsp3, cloned into pETM11 with an N-terminal His6-tag and TEV-cleavage site Na T5; N-(3-methoxy-4-hydroxy-acetophenone)thiosemicarbazone "[""A3X""]" 1 Kd Kd ~ ~ 200 µM 200000.0 [] unit_conversion 3.6989700043360187 success True direct_binding Nano differential scanning fluorimetry fluorescence titration; higher-concentration T5 data, with initial fluorescence at 330 nm, yielded an apparent dissociation constant. 8 “A fit of the initial fluorescence at 330 nm yields an apparent K_D of approximately 200 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7QCM\7QCM_metadata.json point structures/7QCM/7qcm_protein.pdb structures/7QCM/7qcm_pocket.pdb structures/7QCM/7qcm_ligand.sdf structures/7QCM/7qcm_ligand.pdb structures/7QCM/7qcm_ligand.cif structures/7QCM/7qcm_complex.pdb structures/7QCM/7qcm_complex.cif 7QCR extended MLLT4/Afadin PDZ domain human MLLT4 PDZ domain, residues 1002-1095 Na Acetylated SARS-CoV-2 protein E PBM peptide, Ac-NLNSSRVPDLLV-COOH "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 569 (±129) µM 569000.0 [] unit_conversion 3.244887733604929 success True direct_binding Microscale thermophoresis (MST) measurement of the SARS-CoV-2 WT E-protein PBM peptide with MLLT4 PDZ. 8 Table 3 reports MLLT4 PDZ Kd = 569 (±129) µM for SARS-CoV-2 WT; the MST method specifies acetylated 12-residue E PBM peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7QCR\7QCR_metadata.json point structures/7QCR/7qcr_protein.pdb structures/7QCR/7qcr_pocket.pdb structures/7QCR/7qcr_ligand.pdb structures/7QCR/7qcr_ligand.cif structures/7QCR/7qcr_complex.pdb structures/7QCR/7qcr_complex.cif 7QCS extended PALS1/MPP5 PDZ domain human MPP5 PDZ domain, residues 238-336 Na Acetylated SARS-CoV-2 protein E PBM peptide, Ac-NLNSSRVPDLLV-COOH "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 30 (±24) µM 30000.0 [] unit_conversion 4.522878745280337 success True direct_binding Microscale thermophoresis (MST) measurement of the SARS-CoV-2 WT E-protein PBM peptide with MPP5 PDZ. 8 Table 3 reports MPP5 PDZ Kd = 30 (±24) µM for SARS-CoV-2 WT; the MST method specifies acetylated 12-residue E PBM peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7QCS\7QCS_metadata.json point structures/7QCS/7qcs_protein.pdb structures/7QCS/7qcs_pocket.pdb structures/7QCS/7qcs_ligand.pdb structures/7QCS/7qcs_ligand.cif structures/7QCS/7qcs_complex.pdb structures/7QCS/7qcs_complex.cif 7QCT extended LNX2 PDZ2 human LNX2 PDZ2, residues 334-426 Na Acetylated SARS-CoV-2 protein E PBM peptide, Ac-NLNSSRVPDLLV-COOH "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 289 (±116) µM 289000.0 [] unit_conversion 3.539102157243452 success True direct_binding Microscale thermophoresis (MST) measurement of the SARS-CoV-2 WT E-protein PBM peptide with LNX2 PDZ2. 8 Table 3 reports LNX2 PDZ2 Kd = 289 (±116) µM for SARS-CoV-2 WT; the MST method specifies acetylated 12-residue E PBM peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7QCT\7QCT_metadata.json point structures/7QCT/7qct_protein.pdb structures/7QCT/7qct_pocket.pdb structures/7QCT/7qct_ligand.pdb structures/7QCT/7qct_ligand.cif structures/7QCT/7qct_complex.pdb structures/7QCT/7qct_complex.cif 7QDL extended BRD4 human Na Na I-BET567; compound 27 "[""AKQ""]" 1 pIC50 IC50 = = 6.9 125.89254117941663 [] p_metric_transform 6.9 success True biochemical_inhibition BRD4 BD1 TR-FRET assay; Table 2 reports BRD4 BD1/BD2 FRET pIC50 values. 9 Table 2, compound 27: BRD4 BD1/BD2 FRET pIC50 = 6.9 / 7.2. The BD1 value (6.9) matches the 7QDL BRD4 BD1 complex; 7QDL is identified as the BRD4 BD1/27 complex on page 12. auto_single_measurement only accepted activity measurement [1] 1 structures\7QDL\7QDL_metadata.json point structures/7QDL/7qdl_ligand.sdf structures/7QDL/7qdl_ligand.cif structures/7QDL/7qdl_complex.cif 7QEI classic human MTHFD2L human MTHFD2L residues 50-347, His-tagged Na TH7299 "[""9L9""]" 1 IC50 IC50 = = 174 nM 174.0 [] unit_conversion 6.7594507517174005 success True biochemical_inhibition Purified MTHFD2L TH7299 dose-response assay; Figure 2 reports n=3. The assay uses NADP+ as cofactor. 3 “We performed a TH7299 dose-response curve for purified MTHFD2L which indicated an IC50 value of 174 nM (Figure 2).” auto_single_measurement only accepted activity measurement [1] 1 structures\7QEI\7QEI_metadata.json point structures/7QEI/7qei_protein.pdb structures/7QEI/7qei_pocket.pdb structures/7QEI/7qei_ligand.sdf structures/7QEI/7qei_ligand.pdb structures/7QEI/7qei_ligand.cif structures/7QEI/7qei_complex.pdb structures/7QEI/7qei_complex.cif 7QF8 classic bacterial pyranose 2-oxidase (PsG3Ox) Pseudoarthrobacter siccitolerans Na Na FAD "[""FAD""]" 1 Kd Kd = = (2.0 ± 0.7) × 10⁻⁷ M 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Apo-PsG3Ox was incubated with FAD; FAD binding was followed by quenching of intrinsic tryptophan fluorescence and fitted to a one-binding-site equation. 4 “Apo-PsG3Ox binds exogenous FAD with an estimated dissociation constant K_D = (2.0 ± 0.7) × 10⁻⁷ M.” auto_single_measurement only accepted activity measurement [1] 1 structures\7QF8\7QF8_metadata.json point structures/7QF8/7qf8_protein.pdb structures/7QF8/7qf8_pocket.pdb structures/7QF8/7qf8_ligand.sdf structures/7QF8/7qf8_ligand.pdb structures/7QF8/7qf8_ligand.cif structures/7QF8/7qf8_complex.pdb structures/7QF8/7qf8_complex.cif 7QFB extended Protein Phosphatase 1 (PP1) Na PP1 residues 7-300 in complex with PTG peptide residues 81-107 Na PTG PP1-binding peptide residues 81-107 "[""CHAIN:B""]" 1 Kd Kd = = 14 nM 14.0 [] unit_conversion 7.853871964321762 success True direct_binding GCI measurement of PP1 binding to the PTG PP1-binding peptide 81–107. 5 “GCI titrations confirmed that the main PTG binding determinant to PP1 resides in its RVXF region and surrounding residues with a K_D = 14 nM for the PTG peptide 81–107.” auto_single_measurement only accepted activity measurement [1] 1 structures\7QFB\7QFB_metadata.json point structures/7QFB/7qfb_protein.pdb structures/7QFB/7qfb_pocket.pdb structures/7QFB/7qfb_ligand.pdb structures/7QFB/7qfb_ligand.cif structures/7QFB/7qfb_complex.pdb structures/7QFB/7qfb_complex.cif 7QG7 classic SARS-CoV-2 macrodomain Nsp3b SARS-CoV-2 SARS-CoV-2 MD residues 207-376 with an N-terminal His6 tag and TEV cleavage site Na GS-441524 (remdesivir nucleoside) "[""U08""]" 1 Kd Kd = = 10.3 µM 10300.0 [] unit_conversion 4.987162775294828 success True direct_binding Isothermal titration calorimetry (Table 2/Figure 7). 12 Table 2 reports K_D = 10.3 µM for GS-441524 binding to SARS-CoV-2 MD. The paper identifies the GS-441524-bound SARS-CoV-2 MD structure as PDB 7QG7. auto_single_measurement only accepted activity measurement [1] 1 structures\7QG7\7QG7_metadata.json point structures/7QG7/7qg7_protein.pdb structures/7QG7/7qg7_pocket.pdb structures/7QG7/7qg7_ligand.sdf structures/7QG7/7qg7_ligand.pdb structures/7QG7/7qg7_ligand.cif structures/7QG7/7qg7_complex.pdb structures/7QG7/7qg7_complex.cif 7QGA classic Human CD73 (ecto-5'-nucleotidase) human Na Na MRS4598; compound 16 "[""BOI""]" 1 Ki Ki = = 0.673 ± 0.091 nM 0.673 [] unit_conversion 9.171984935776024 success True biochemical_inhibition Inhibition of soluble hCD73; mean of three independent determinations, each in duplicate. 3 Table 1 reports compound 16 Ki ± SEM of 0.673 ± 0.091 nM for inhibition of soluble hCD73. Table 2 maps compound 16 open state to PDB 7QGA. auto_single_measurement only accepted activity measurement [1] 1 structures\7QGA\7QGA_metadata.json point structures/7QGA/7qga_protein.pdb structures/7QGA/7qga_pocket.pdb structures/7QGA/7qga_ligand.sdf structures/7QGA/7qga_ligand.pdb structures/7QGA/7qga_ligand.cif structures/7QGA/7qga_complex.pdb structures/7QGA/7qga_complex.cif 7QGL classic Human CD73 (ecto-5'-nucleotidase) human Na Na MRS4602; compound 21 "[""BW0""]" 1 Ki Ki = = 0.848 ± 0.229 nM 0.848 [] unit_conversion 9.071604147743287 success True biochemical_inhibition Inhibition of soluble hCD73; mean of three independent determinations, each in duplicate. 3 Table 1 reports compound 21 Ki ± SEM of 0.848 ± 0.229 nM for inhibition of soluble hCD73. Table 2 maps compound 21 open state to PDB 7QGL. auto_single_measurement only accepted activity measurement [1] 1 structures\7QGL\7QGL_metadata.json point structures/7QGL/7qgl_protein.pdb structures/7QGL/7qgl_pocket.pdb structures/7QGL/7qgl_ligand.sdf structures/7QGL/7qgl_ligand.pdb structures/7QGL/7qgl_ligand.cif structures/7QGL/7qgl_complex.pdb structures/7QGL/7qgl_complex.cif 7QGM classic Human CD73 (ecto-5'-nucleotidase) human Na Na MRS4598; compound 16 "[""BOI""]" 1 Ki Ki = = 0.673 ± 0.091 nM 0.673 [] unit_conversion 9.171984935776024 success True biochemical_inhibition Inhibition of soluble hCD73; mean of three independent determinations, each in duplicate. 3 Table 1 reports compound 16 Ki ± SEM of 0.673 ± 0.091 nM for inhibition of soluble hCD73. Table 2 maps compound 16 closed state to PDB 7QGM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QGM\7QGM_metadata.json point structures/7QGM/7qgm_protein.pdb structures/7QGM/7qgm_pocket.pdb structures/7QGM/7qgm_ligand.sdf structures/7QGM/7qgm_ligand.pdb structures/7QGM/7qgm_ligand.cif structures/7QGM/7qgm_complex.pdb structures/7QGM/7qgm_complex.cif 7QGO classic Human CD73 (ecto-5'-nucleotidase) human Na Na MRS4602; compound 21 "[""BW0""]" 1 Ki Ki = = 0.848 ± 0.229 nM 0.848 [] unit_conversion 9.071604147743287 success True biochemical_inhibition Inhibition of soluble hCD73; mean of three independent determinations, each in duplicate. 3 Table 1 reports compound 21 Ki ± SEM of 0.848 ± 0.229 nM for inhibition of soluble hCD73. Table 2 maps compound 21 closed state to PDB 7QGO. auto_single_measurement only accepted activity measurement [1] 1 structures\7QGO\7QGO_metadata.json point structures/7QGO/7qgo_protein.pdb structures/7QGO/7qgo_pocket.pdb structures/7QGO/7qgo_ligand.sdf structures/7QGO/7qgo_ligand.pdb structures/7QGO/7qgo_ligand.cif structures/7QGO/7qgo_complex.pdb structures/7QGO/7qgo_complex.cif 7QHD classic human butyrylcholinesterase human Na Na compound 39; (S)-1-(4-((2-(1H-indol-3-yl)ethyl)carbamoyl)benzyl)-N-(3-((1,2,3,4-tetrahydroacridin-9-yl)amino)propyl)piperidine-3-carboxamide "[""C0I""]" 1 IC50 IC50 = = 3.49 ± 0.41 nM 3.49 [] unit_conversion 8.45717457304082 success True biochemical_inhibition Ellman cholinesterase inhibition assay against human BuChE. 10 Table 6 reports compound 39 human BuChE IC50 = 3.49 ± 0.41 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QHD\7QHD_metadata.json point structures/7QHD/7qhd_protein.pdb structures/7QHD/7qhd_pocket.pdb structures/7QHD/7qhd_ligand.sdf structures/7QHD/7qhd_ligand.pdb structures/7QHD/7qhd_ligand.cif structures/7QHD/7qhd_complex.pdb structures/7QHD/7qhd_complex.cif 7QHE classic human butyrylcholinesterase human Na Na compound 43; (S)-1-(4-((naphthalen-1-yl)carbamoyl)benzyl)-N-(3-((1,2,3,4-tetrahydroacridin-9-yl)amino)propyl)piperidine-3-carboxamide "[""C4I""]" 1 IC50 IC50 = = 7.44 ± 1.74 nM 7.44 [] unit_conversion 8.12842706445412 success True biochemical_inhibition Ellman cholinesterase inhibition assay against human BuChE. 10 Table 6 reports compound 43 human BuChE IC50 = 7.44 ± 1.74 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QHE\7QHE_metadata.json point structures/7QHE/7qhe_protein.pdb structures/7QHE/7qhe_pocket.pdb structures/7QHE/7qhe_ligand.sdf structures/7QHE/7qhe_ligand.pdb structures/7QHE/7qhe_ligand.cif structures/7QHE/7qhe_complex.pdb structures/7QHE/7qhe_complex.cif 7QHN classic lysyl-tRNA synthetase (LysRS) Mycobacterium tuberculosis Na Na compound 2 "[""C6I""]" 1 IC50 IC50 = = 9 µM 9000.0 [] unit_conversion 5.045757490560675 success True biochemical_inhibition In vitro M. tuberculosis LysRS enzyme inhibition; Fig. 1 reports the geometric mean of at least two independent replicates. 2 Compound 2 is labelled “LysRS IC50 = 9 µM”; Fig. 2 identifies compound 2 in the LysRS catalytic site as PDB 7QHN. auto_single_measurement only accepted activity measurement [1] 1 structures\7QHN\7QHN_metadata.json point structures/7QHN/7qhn_protein.pdb structures/7QHN/7qhn_pocket.pdb structures/7QHN/7qhn_ligand.sdf structures/7QHN/7qhn_ligand.pdb structures/7QHN/7qhn_ligand.cif structures/7QHN/7qhn_complex.pdb structures/7QHN/7qhn_complex.cif 7QHW extended TTBK1 human TEV-TTBK1 residues 14-313 Na inhibitor 29 (compound 29) "[""CGI""]" 1 IC50 IC50 = = 0.24 μM 240.0 [] unit_conversion 6.619788758288394 success True biochemical_inhibition Inhibition of human recombinant TTBK1 measured by the MRC Phosphorylation Unit; Table 2 reports the compound-29 enzymatic result. 5 Table 2 lists compound 29 with TTBK1 IC50 = 0.24 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QHW\7QHW_metadata.json point structures/7QHW/7qhw_ligand.cif structures/7QHW/7qhw_complex.cif 7QHZ classic KLK6 human Na Na DKFZ-917 "[""CI5""]" 1 pIC50 IC50 = = 8.51 unitless 3.090295432513592 [] p_metric_transform 8.51 success True biochemical_inhibition KLK6 enzymatic inhibition assay; 95% confidence interval printed as 8.49–8.52. 3 “DKFZ-917 and DKFZ-918 behaved as expected in a KLK6 enzymatic inhibition assay with pIC50 values of 8.51 … and 8.22 … respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7QHZ\7QHZ_metadata.json point structures/7QHZ/7qhz_protein.pdb structures/7QHZ/7qhz_pocket.pdb structures/7QHZ/7qhz_ligand.sdf structures/7QHZ/7qhz_ligand.pdb structures/7QHZ/7qhz_ligand.cif structures/7QHZ/7qhz_complex.pdb structures/7QHZ/7qhz_complex.cif 7QI0 classic KLK6 human Na Na DKFZ-918 "[""C9I""]" 1 pIC50 IC50 = = 8.22 unitless 6.025595860743569 [] p_metric_transform 8.22 success True biochemical_inhibition KLK6 enzymatic inhibition assay; 95% confidence interval printed as 8.18–8.25. 3 “DKFZ-917 and DKFZ-918 behaved as expected in a KLK6 enzymatic inhibition assay with pIC50 values of 8.51 … and 8.22 … respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7QI0\7QI0_metadata.json point structures/7QI0/7qi0_protein.pdb structures/7QI0/7qi0_pocket.pdb structures/7QI0/7qi0_ligand.sdf structures/7QI0/7qi0_ligand.pdb structures/7QI0/7qi0_ligand.cif structures/7QI0/7qi0_complex.pdb structures/7QI0/7qi0_complex.cif 7QI8 classic lysyl-tRNA synthetase (LysRS) Mycobacterium tuberculosis Na Na compound 8 (DDD02049209) "[""DD0""]" 1 IC50 IC50 = = 0.05 µM 50.0 [] unit_conversion 7.301029995663981 success True biochemical_inhibition In vitro M. tuberculosis LysRS enzyme inhibition; Fig. 1 reports the geometric mean of at least two independent replicates. 2 Compound 8 is labelled “LysRS IC50 = 0.05 µM”; Fig. 2 identifies compound 8 in the LysRS catalytic site as PDB 7QI8. auto_single_measurement only accepted activity measurement [1] 1 structures\7QI8\7QI8_metadata.json point structures/7QI8/7qi8_protein.pdb structures/7QI8/7qi8_pocket.pdb structures/7QI8/7qi8_ligand.sdf structures/7QI8/7qi8_ligand.pdb structures/7QI8/7qi8_ligand.cif structures/7QI8/7qi8_complex.pdb structures/7QI8/7qi8_complex.cif 7QIE classic phosphatidylinositol 5-phosphate 4-kinase gamma (PI5P4K2C) human Truncated protein comprising residues His32 to Ala421, with residues 300-341 deleted Na compound 40 "[""DVF""]" 1 Kd Kd = = 68 nM 68.0 [] unit_conversion 7.167491087293763 success True direct_binding Commercially available binding assay. 5 “Binding constants (KDs) were determined for compound 40 … for PI5P4Kγ-WT (68 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7QIE\7QIE_metadata.json point structures/7QIE/7qie_protein.pdb structures/7QIE/7qie_pocket.pdb structures/7QIE/7qie_ligand.sdf structures/7QIE/7qie_ligand.pdb structures/7QIE/7qie_ligand.cif structures/7QIE/7qie_complex.pdb structures/7QIE/7qie_complex.cif 7QJG classic EED Na Na Na compound 6 "[""EKR""]" 1 IC50 IC50 = = 2600 nM 2600.0 [] unit_conversion 5.585026652029182 success True biochemical_inhibition Biochemical PRC2 inhibition assay; Table 1 reports biochemical IC50 values for compounds evaluated in the EED H3K27me3-pocket program. 3 Table 1 lists compound 6 with biochemical IC50 = 2600 nM. Figure 2 identifies the EED co-structure with compound 6 as PDB 7QJG. auto_single_measurement only accepted activity measurement [1] 1 structures\7QJG\7QJG_metadata.json point structures/7QJG/7qjg_protein.pdb structures/7QJG/7qjg_pocket.pdb structures/7QJG/7qjg_ligand.sdf structures/7QJG/7qjg_ligand.pdb structures/7QJG/7qjg_ligand.cif structures/7QJG/7qjg_complex.pdb structures/7QJG/7qjg_complex.cif 7QJK extended PDE6D Na Na Na Compound-2 "[""9VO""]" 1 Kd Kd > > 0.5 mM 500000.0 [] unit_conversion 3.3010299956639813 success True direct_binding SPR dose-response experiment for Compound-2 binding PDE6D alone. 10 The text states that Compound-2 in complex with PDE6D alone had affinity in the low-millimolar range, Kd > 0.5 mM (Figure 8E,F). auto_single_measurement only accepted activity measurement [1] 1 structures\7QJK\7QJK_metadata.json point structures/7QJK/7qjk_ligand.sdf structures/7QJK/7qjk_ligand.cif structures/7QJK/7qjk_complex.cif 7QJU classic EED Na Na Na compound 7 "[""EKF""]" 1 IC50 IC50 = = 20 nM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition Biochemical PRC2 inhibition assay; Table 1 reports biochemical IC50 values for compounds evaluated in the EED H3K27me3-pocket program. 3 Table 1 lists compound 7 with biochemical IC50 = 20 nM. Figure 2 identifies the EED co-structure with compound 7 as PDB 7QJU. auto_single_measurement only accepted activity measurement [1] 1 structures\7QJU\7QJU_metadata.json point structures/7QJU/7qju_protein.pdb structures/7QJU/7qju_pocket.pdb structures/7QJU/7qju_ligand.sdf structures/7QJU/7qju_ligand.pdb structures/7QJU/7qju_ligand.cif structures/7QJU/7qju_complex.pdb structures/7QJU/7qju_complex.cif 7QK0 classic BCL6 human Na Na CCT373566 (compound 12a) "[""EBL""]" 1 IC50 IC50 = = 2.2 nM 2.2 [] unit_conversion 8.657577319177793 success True biochemical_inhibition BCL6 TR-FRET biochemical inhibition assay. 5 Table 2 lists compound 12a (CCT373566) with BCL6 TR-FRET IC50 = 2.2 nM. Figure 1 identifies the BCL6 BTB-domain crystal structure with CCT373566 as PDB 7QK0. auto_single_measurement only accepted activity measurement [1] 1 structures\7QK0\7QK0_metadata.json point structures/7QK0/7qk0_protein.pdb structures/7QK0/7qk0_pocket.pdb structures/7QK0/7qk0_ligand.sdf structures/7QK0/7qk0_ligand.pdb structures/7QK0/7qk0_ligand.cif structures/7QK0/7qk0_complex.pdb structures/7QK0/7qk0_complex.cif 7QK4 classic EED Na Na Na compound 22 (MAK683) "[""EJR""]" 1 IC50 IC50 = = 9 ± 4 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition Biochemical PRC2 inhibition assay; Table 4 gives the in vitro profile of compound 22 selected for PK/PD and efficacy studies. 6 Table 4 lists compound 22 with biochemical IC50 = 9 ± 4 nM. Figure 8 identifies compound 22 (MAK683) in complex with EED as PDB 7QK4. auto_single_measurement only accepted activity measurement [1] 1 structures\7QK4\7QK4_metadata.json point structures/7QK4/7qk4_protein.pdb structures/7QK4/7qk4_pocket.pdb structures/7QK4/7qk4_ligand.sdf structures/7QK4/7qk4_ligand.pdb structures/7QK4/7qk4_ligand.cif structures/7QK4/7qk4_complex.pdb structures/7QK4/7qk4_complex.cif 7QLB classic SMYD3 Na full length recombinant SMYD3 Na FL06268 "[""E4I""]" 1 Kd Kd = = 24.5 µM 24500.0 [] unit_conversion 4.610833915635467 success True direct_binding Initial multiplexed GCI kinetic screening against apo SMYD3. 4 Table 1 lists FL06268 under “SMYD3 apo” with K_D = 24.5 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QLB\7QLB_metadata.json point structures/7QLB/7qlb_protein.pdb structures/7QLB/7qlb_pocket.pdb structures/7QLB/7qlb_ligand.sdf structures/7QLB/7qlb_ligand.pdb structures/7QLB/7qlb_ligand.cif structures/7QLB/7qlb_complex.pdb structures/7QLB/7qlb_complex.cif 7QNV extended human carbonic anhydrase II Homo sapiens Na Na 3b; 3-methylbenzoselenoate "[""E6H""]" 1 Ki Ki = = 9.67 μM 9670.0 [] unit_conversion 5.014573525916998 success True biochemical_inhibition Stopped-flow CO₂ hydration assay against human CA isoforms. 3 Table 1 reports compound 3b with Ki 9.67 μM against hCA II; the text identifies the hCA II X-ray complex with compound 3b as PDB 7QNV. auto_single_measurement only accepted activity measurement [1] 1 structures\7QNV\7QNV_metadata.json point structures/7QNV/7qnv_ligand.sdf structures/7QNV/7qnv_ligand.cif structures/7QNV/7qnv_complex.cif 7QOB extended human carbonic anhydrase I Homo sapiens Na Na 3a; benzoselenoate "[""E7I""]" 1 Ki Ki = = 4.04 μM 4040.0 [] unit_conversion 5.393618634889394 success True biochemical_inhibition Stopped-flow CO₂ hydration assay against human CA isoforms. 3 Table 1 reports compound 3a with Ki 4.04 μM against hCA I; the text identifies the hCA I X-ray complex with compound 3a as PDB 7QOB. auto_single_measurement only accepted activity measurement [1] 1 structures\7QOB\7QOB_metadata.json point structures/7QOB/7qob_ligand.sdf structures/7QOB/7qob_ligand.cif structures/7QOB/7qob_complex.cif 7QQ6 classic GCN2 (EIF2ALPHA KINASE 4, E2AK4) human 6His-TEV-GCN2(S577-T1020, DeltaA663-P788, D848N) D848N Compound 1 (dovitinib) "[""38O""]" 1 IC50 IC50 = = 0.9 µM 900.0 [] unit_conversion 6.045757490560675 success True biochemical_inhibition Purified-protein biochemical activity assay; IC50 determination for the D848N GCN2 construct with Compound 1. 5 “Pre-incubation of GCN2 S577-T1020, ΔA663-P788, D848N ... with Dovitinib (Compound 1; IC50 0.9 μM) ...” auto_single_measurement only accepted activity measurement [1] 1 structures\7QQ6\7QQ6_metadata.json point structures/7QQ6/7qq6_protein.pdb structures/7QQ6/7qq6_pocket.pdb structures/7QQ6/7qq6_ligand.sdf structures/7QQ6/7qq6_ligand.pdb structures/7QQ6/7qq6_ligand.cif structures/7QQ6/7qq6_complex.pdb structures/7QQ6/7qq6_complex.cif 7QQ7 classic CYP142A1 (Rv3518c) Mycobacterium tuberculosis N-terminally truncated CYP142A1 residues 2-398, pET21a construct with TEV-cleavable Twin-Strep/hexa-histidine tag; tag-free protein used for crystallography Na 5j "[""EIQ""]" 1 Kd Kd = = 0.88 ± 0.055 µM 880.0 [] unit_conversion 6.055517327849831 success True direct_binding Optical titration; Table 1 binding value for compound 5j. 5 Table 1 reports compound 5j K_D = 0.88 ± 0.055 µM for CYP142. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7QQ7\7QQ7_metadata.json point structures/7QQ7/7qq7_protein.pdb structures/7QQ7/7qq7_pocket.pdb structures/7QQ7/7qq7_ligand.sdf structures/7QQ7/7qq7_ligand.pdb structures/7QQ7/7qq7_ligand.cif structures/7QQ7/7qq7_complex.pdb structures/7QQ7/7qq7_complex.cif 7QQG classic MYORG Na MYORG residues 80-714 with an N-terminal TEV-cleavable 6xHis tag and honey-bee melittin signal sequence wild-type 1-deoxygalactonojirimycin (DGJ) "[""DGJ""]" 1 Kd Kd = = 1.33 ± 0.45 µM 1330.0 [] unit_conversion 5.876148359032914 success True direct_binding Isothermal titration calorimetry of DGJ binding to MYORG_GH31; mean of 2 technical repeats ± standard deviation. 5 “we used isothermal titration calorimetry to determine a K_D value of 1.33 ± 0.45 μM ... for binding of DGJ to MYORG_GH31.” auto_single_measurement only accepted activity measurement [1] 1 structures\7QQG\7QQG_metadata.json point structures/7QQG/7qqg_protein.pdb structures/7QQG/7qqg_pocket.pdb structures/7QQG/7qqg_ligand.sdf structures/7QQG/7qqg_ligand.pdb structures/7QQG/7qqg_ligand.cif structures/7QQG/7qqg_complex.pdb structures/7QQG/7qqg_complex.cif 7QRC classic PEX14 Trypanosoma cruzi PEX14 N-terminal domain, residues 19-84 Na compound 1 "[""ET7""]" 1 Kd Kd = = 56 µM 56000.0 [] unit_conversion 4.251811972993799 success True direct_binding Microscale thermophoresis (MST) direct-binding assay; Table 1 reports TcPEX14 Kd for compound 1. 5 Table 1 lists compound 1 with MST TcPEX14 Kd = 56 µM. The experimental section identifies TcPEX14 NTD as residues 19–84 and states that MST determined inhibitor binding constants. auto_single_measurement only accepted activity measurement [1] 1 structures\7QRC\7QRC_metadata.json point structures/7QRC/7qrc_protein.pdb structures/7QRC/7qrc_pocket.pdb structures/7QRC/7qrc_ligand.sdf structures/7QRC/7qrc_ligand.pdb structures/7QRC/7qrc_ligand.cif structures/7QRC/7qrc_complex.pdb structures/7QRC/7qrc_complex.cif 7QS6 extended E. coli LptA E. coli LptAm, monomeric N-terminal truncated LptA Na compound 7 "[""CHAIN:B""]" 1 Ki Ki = = 1.9 ± 0.1 nM 1.9 [] unit_conversion 8.721246399047171 success True direct_binding Fluorescence-polarization direct binding assay; LptAm–compound 7 binary interaction. 4 “K_i = 1.9 ± 0.1 nM in LptAm versus 17.2 ± 3.1 nM in LptAmQ62L.” The paper maps E. coli LptAm-7 to 7QS6. auto_single_measurement only accepted activity measurement [1] 1 structures\7QS6\7QS6_metadata.json point structures/7QS6/7qs6_protein.pdb structures/7QS6/7qs6_pocket.pdb structures/7QS6/7qs6_ligand.pdb structures/7QS6/7qs6_ligand.cif structures/7QS6/7qs6_complex.pdb structures/7QS6/7qs6_complex.cif 7QSA extended Human Scribble PDZ3 domain; TBEV NS5 Homo sapiens; Tick-borne encephalitis virus Scribble PDZ3 residues 1002-1094 with TBEV NS5_CTN peptide residues 3407-3414 Na TBEV NS5_CTN peptide (LRLESSII) "[""CHAIN:C""]" 1 Kd Kd = = 18.4 ± 1.3 µM 18400.0 [] unit_conversion 4.735182176990463 success True direct_binding Isothermal titration calorimetry of recombinant SCRIB PDZ3 with synthetic TBEV NS5 C-terminal peptide; mean of three independent experiments ± SD. 4 Table 1 reports PDZ3:CTN K_D = 18.4 ± 1.3 µM; CTN is defined as C-terminal sequence LRLESSII. The methods state ITC was performed three times. auto_single_measurement only accepted activity measurement [1] 1 structures\7QSA\7QSA_metadata.json point structures/7QSA/7qsa_protein.pdb structures/7QSA/7qsa_pocket.pdb structures/7QSA/7qsa_ligand.pdb structures/7QSA/7qsa_ligand.cif structures/7QSA/7qsa_complex.pdb structures/7QSA/7qsa_complex.cif 7QSI extended human carbonic anhydrase II (hCA II) human Na Na indoline-1-sulfonamide (compound 2v) "[""EWF""]" 1 Ki Ki = = 472.2 nM 472.2 [] unit_conversion 6.325874017257291 success True biochemical_inhibition Stopped-flow carbonic-anhydrase CO2-hydration inhibition assay; Table 1 reports mean Ki values. 5 Table 1 lists compound 2v with Ki = 472.2 nM for hCA II; Figure 3 identifies the hCA II–2v co-crystal as PDB 7QSI. auto_single_measurement only accepted activity measurement [1] 1 structures\7QSI\7QSI_metadata.json point structures/7QSI/7qsi_ligand.sdf structures/7QSI/7qsi_ligand.cif structures/7QSI/7qsi_complex.cif 7QT2 classic FenAb208 antibody mouse Fab fragment Na fentanyl "[""7V7""]" 1 Kd Kd = = 2.2 nM 2.2 [] unit_conversion 8.657577319177793 success True direct_binding ITC measurement of FenAb208 Fab binding to fentanyl. 39 Figure 5C lists FenAb208 ITC-KD (fentanyl) as 2.2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QT2\7QT2_metadata.json point structures/7QT2/7qt2_protein.pdb structures/7QT2/7qt2_pocket.pdb structures/7QT2/7qt2_ligand.sdf structures/7QT2/7qt2_ligand.pdb structures/7QT2/7qt2_ligand.cif structures/7QT2/7qt2_complex.pdb structures/7QT2/7qt2_complex.cif 7QT3 classic FenAb609 antibody mouse Fab fragment Na fentanyl "[""7V7""]" 1 Kd Kd = = 2.3 nM 2.3 [] unit_conversion 8.638272163982407 success True direct_binding ITC measurement of FenAb609 Fab binding to fentanyl. 39 Figure 5C lists FenAb609 ITC-KD (fentanyl) as 2.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QT3\7QT3_metadata.json point structures/7QT3/7qt3_protein.pdb structures/7QT3/7qt3_pocket.pdb structures/7QT3/7qt3_ligand.sdf structures/7QT3/7qt3_ligand.pdb structures/7QT3/7qt3_ligand.cif structures/7QT3/7qt3_complex.pdb structures/7QT3/7qt3_complex.cif 7QTO extended Human Scribble (SCRIB) human SCRIB PDZ1 domain, residues 725-815 Na ESEV PBM peptide (KMARTIESEV) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 21.4 ± 1.7 µM 21400.0 [] unit_conversion 4.669586226650809 success True direct_binding Isothermal titration calorimetry (ITC); purified SCRIB PDZ1 with Vietnam H5N1 NS1 ESEV peptide. 5 Table 2 reports SCRIB PDZ1 with Vietnam (ESEV): KD 21.4 ± 1.7 µM. The table states affinities were measured by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7QTO\7QTO_metadata.json point structures/7QTO/7qto_protein.pdb structures/7QTO/7qto_pocket.pdb structures/7QTO/7qto_ligand.pdb structures/7QTO/7qto_ligand.cif structures/7QTO/7qto_complex.pdb structures/7QTO/7qto_complex.cif 7QTP extended Human Scribble (SCRIB) human SCRIB PDZ1 domain, residues 725-815 Na ESKV PBM peptide (KMARTIESKV) "[""CHAIN:B""]" 1 Kd Kd = = 30.0 ± 0.9 µM 30000.0 [] unit_conversion 4.522878745280337 success True direct_binding Isothermal titration calorimetry (ITC); purified SCRIB PDZ1 with Hubei H5N1 NS1 ESKV peptide. 5 Table 2 reports SCRIB PDZ1 with Hubei (ESKV): KD 30.0 ± 0.9 µM. The table states affinities were measured by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7QTP\7QTP_metadata.json point structures/7QTP/7qtp_protein.pdb structures/7QTP/7qtp_pocket.pdb structures/7QTP/7qtp_ligand.pdb structures/7QTP/7qtp_ligand.cif structures/7QTP/7qtp_complex.pdb structures/7QTP/7qtp_complex.cif 7QTU extended Human Scribble (SCRIB) human SCRIB PDZ3 domain, residues 1002-1093 Na ESKV PBM peptide (KMARTIESKV) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 12.1 ± 0.9 µM 12100.0 [] unit_conversion 4.91721462968355 success True direct_binding Isothermal titration calorimetry (ITC); purified SCRIB PDZ3 with Hubei H5N1 NS1 ESKV peptide. 5 Table 2 reports SCRIB PDZ3 with Hubei (ESKV): KD 12.1 ± 0.9 µM. The table states affinities were measured by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7QTU\7QTU_metadata.json point structures/7QTU/7qtu_protein.pdb structures/7QTU/7qtu_pocket.pdb structures/7QTU/7qtu_ligand.pdb structures/7QTU/7qtu_ligand.cif structures/7QTU/7qtu_complex.pdb structures/7QTU/7qtu_complex.cif 7QTW extended KSHV-encoded apoptosis inhibitor KsBcl-2 Kaposi sarcoma-associated herpesvirus (KSHV, HHV8) KsBcl-2 residues 1-146, lacking the C-terminal 29 residues comprising the transmembrane motif V117A Bid BH3 "[""CHAIN:B""]" 1 IC50 IC50 = = 20 ± 9 nM 20.0 [] unit_conversion 7.698970004336019 success True direct_binding Purified recombinant KsBcl-2; solution-competition surface plasmon resonance assay with BH3-domain peptides and 10 nM KsBcl-2. 5 Table 1 reports Bid IC50 20 ± 9 nM; Table 2 assigns the KsBcl-2:Bid BH3 structure to PDB 7QTW. Methods describe the V117A, residues 1–146 recombinant construct and SPR competition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7QTW\7QTW_metadata.json point structures/7QTW/7qtw_protein.pdb structures/7QTW/7qtw_pocket.pdb structures/7QTW/7qtw_ligand.pdb structures/7QTW/7qtw_ligand.cif structures/7QTW/7qtw_complex.pdb structures/7QTW/7qtw_complex.cif 7QTX extended KSHV-encoded apoptosis inhibitor KsBcl-2 Kaposi sarcoma-associated herpesvirus (KSHV, HHV8) KsBcl-2 residues 1-146, lacking the C-terminal 29 residues comprising the transmembrane motif V117A Puma BH3 "[""CHAIN:B""]" 1 IC50 IC50 = = 26 ± 9 nM 26.0 [] unit_conversion 7.585026652029182 success True direct_binding Purified recombinant KsBcl-2; solution-competition surface plasmon resonance assay with BH3-domain peptides and 10 nM KsBcl-2. 5 Table 1 reports Puma IC50 26 ± 9 nM; Table 2 assigns the KsBcl-2:Puma BH3 structure to PDB 7QTX. Methods describe the V117A, residues 1–146 recombinant construct and SPR competition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7QTX\7QTX_metadata.json point structures/7QTX/7qtx_protein.pdb structures/7QTX/7qtx_pocket.pdb structures/7QTX/7qtx_ligand.pdb structures/7QTX/7qtx_ligand.cif structures/7QTX/7qtx_complex.pdb structures/7QTX/7qtx_complex.cif 7QUE classic STK17A (DRAK1) human DRAK1 residues V50-P350 Na CKJB68; compound 14 "[""F7I""]" 1 IC50 IC50 = = 155 nM 155.0 [] unit_conversion 6.809668301829708 success True biochemical_inhibition 33PanQinase enzyme kinetic assay. 8 Table 1 reports compound 14 with a 33PanQinase DRAK1 IC50 of 155 nM; the text identifies this as an enzymatic activity assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7QUE\7QUE_metadata.json point structures/7QUE/7que_protein.pdb structures/7QUE/7que_pocket.pdb structures/7QUE/7que_ligand.sdf structures/7QUE/7que_ligand.pdb structures/7QUE/7que_ligand.cif structures/7QUE/7que_complex.pdb structures/7QUE/7que_complex.cif 7QUF classic STK17A (DRAK1) human DRAK1 residues V50-P350 Na CK156; compound 34 "[""F8I""]" 1 Kd Kd = = 21 nM 21.0 [] unit_conversion 7.6777807052660805 success True direct_binding Isothermal titration calorimetry (ITC). 7 Figure 5, panel A, reports KD = 21 nM for CK156 (34) binding to DRAK1 by ITC. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7QUF\7QUF_metadata.json point structures/7QUF/7quf_protein.pdb structures/7QUF/7quf_pocket.pdb structures/7QUF/7quf_ligand.sdf structures/7QUF/7quf_ligand.pdb structures/7QUF/7quf_ligand.cif structures/7QUF/7quf_complex.pdb structures/7QUF/7quf_complex.cif 7QUI classic Siglec-8 human Siglec-8_d1, residues 17-155, removable C-terminal His6 tag C42S NSA Neu5Ac "[""F9I""]" 1 Kd Kd = = 2.37 ± 0.67 µM 2370.0 [] unit_conversion 5.625251653989896 success True direct_binding NMR-based ligand binding measurement of NSA Neu5Ac to Siglec-8; the paper identifies Siglec-8_d1 as the C42S construct used for these studies. 2 “the reported high affinity (K_D = 2.37 ± 0.67 μM, estimated by NMR) of NSA Neu5Ac to Siglec-8” auto_single_measurement only accepted activity measurement [1] 1 structures\7QUI\7QUI_metadata.json point structures/7QUI/7qui_protein.pdb structures/7QUI/7qui_pocket.pdb structures/7QUI/7qui_ligand.sdf structures/7QUI/7qui_ligand.pdb structures/7QUI/7qui_ligand.cif structures/7QUI/7qui_complex.pdb structures/7QUI/7qui_complex.cif 7QUX extended CK2alpha Na Na Na P7C8 "[""CHAIN:D""]" 1 IC50 IC50 = = 15.6 ± 5.1 μM 15600.0 [] unit_conversion 4.806875401645539 success True direct_binding Fluorescence-polarisation assay of cyclic peptides against CK2α; Table 2 reports IC50 ± SEM. 3 Table 2 lists P7C8 with IC50 15.6 ± 5.1 μM; the text states the cyclic peptides were tested in an FP assay against CK2α. auto_single_measurement only accepted activity measurement [1] 1 structures\7QUX\7QUX_metadata.json point structures/7QUX/7qux_protein.pdb structures/7QUX/7qux_pocket.pdb structures/7QUX/7qux_ligand.pdb structures/7QUX/7qux_ligand.cif structures/7QUX/7qux_complex.pdb structures/7QUX/7qux_complex.cif 7QVJ classic Estrogen receptor alpha Na Na Na compound 29 "[""H09""]" 1 pIC50 IC50 = = 9.1 0.7943282347242822 [] p_metric_transform 9.1 success True direct_binding ERα binding assay; Table 5 reports compound 29 ER bind pIC50. 10 Table 5 lists compound 29 with ER bind pIC50 9.1; Figure 4 maps compound 29 to PDB 7qvj. auto_single_measurement only accepted activity measurement [1] 1 structures\7QVJ\7QVJ_metadata.json point structures/7QVJ/7qvj_protein.pdb structures/7QVJ/7qvj_pocket.pdb structures/7QVJ/7qvj_ligand.sdf structures/7QVJ/7qvj_ligand.pdb structures/7QVJ/7qvj_ligand.cif structures/7QVJ/7qvj_complex.pdb structures/7QVJ/7qvj_complex.cif 7QVL classic Estrogen receptor alpha Na Na Na compound 38 "[""GZI""]" 1 pIC50 IC50 = = 8.8 1.584893192461111 [] p_metric_transform 8.8 success True direct_binding ERα binding assay; Table 7 reports compound 38 ER bind pIC50. 11 Table 7 lists compound 38 with ER bind pIC50 8.8; the paper maps compound 38 to PDB 7qvl. auto_single_measurement only accepted activity measurement [1] 1 structures\7QVL\7QVL_metadata.json point structures/7QVL/7qvl_protein.pdb structures/7QVL/7qvl_pocket.pdb structures/7QVL/7qvl_ligand.sdf structures/7QVL/7qvl_ligand.pdb structures/7QVL/7qvl_ligand.cif structures/7QVL/7qvl_complex.pdb structures/7QVL/7qvl_complex.cif 7QVU classic BAZ2A Na Na Na fragment 25 "[""FIY""]" 1 IC50 IC50 = = 33.2 ± 0.3 μM 33200.0 [] unit_conversion 4.478861916295964 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 2 Table 1 reports compound 25 IC50 BAZ2A = 33.2 ± 0.3 μM; page 9 maps PDB 7QVU to compound 25. auto_single_measurement only accepted activity measurement [1] 1 structures\7QVU\7QVU_metadata.json point structures/7QVU/7qvu_protein.pdb structures/7QVU/7qvu_pocket.pdb structures/7QVU/7qvu_ligand.sdf structures/7QVU/7qvu_ligand.pdb structures/7QVU/7qvu_ligand.cif structures/7QVU/7qvu_complex.pdb structures/7QVU/7qvu_complex.cif 7QWF classic BAZ2A Na Na Na compound 45 "[""FS6""]" 1 IC50 IC50 = = 109.2 ± 12.3 μM 109200.0 [] unit_conversion 3.961777361631282 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 3 Table 2 reports compound 45 IC50 BAZ2A = 109.2 ± 12.3 μM; page 9 maps PDB 7QWF to compound 45. auto_single_measurement only accepted activity measurement [1] 1 structures\7QWF\7QWF_metadata.json point structures/7QWF/7qwf_protein.pdb structures/7QWF/7qwf_pocket.pdb structures/7QWF/7qwf_ligand.sdf structures/7QWF/7qwf_ligand.pdb structures/7QWF/7qwf_ligand.cif structures/7QWF/7qwf_complex.pdb structures/7QWF/7qwf_complex.cif 7QWK classic GCN2 (EIF2ALPHA KINASE 4, E2AK4) human 6His-TEV-GCN2(S577-T1020, DeltaA663-P788, T899A, T904A) T899A, T904A Compound 2 ((2S)-N-[(1S)-1-(4-{[6-(4-pyridinyl)-2-quinazolinyl]amino}phenyl)ethyl]-2-piperidinecarboxamide) "[""G41""]" 1 IC50 IC50 = = 6.8 µM 6800.0 [] unit_conversion 5.167491087293763 success True biochemical_inhibition Purified-protein biochemical activity assay; IC50 determination for the T899A/T904A GCN2 construct with Compound 2. 5 “Pre-incubation of GCN2 S577-T1020, ΔA663-P788, T899A,T904A with compound (2S)-N-[(1S)-1-(4-{[6-(4-pyridinyl)-2-quinazolinyl]amino}phenyl)ethyl]-2-piperidinecarboxamide (Compound 2, IC50 6.8 μM) ...” auto_single_measurement only accepted activity measurement [1] 1 structures\7QWK\7QWK_metadata.json point structures/7QWK/7qwk_protein.pdb structures/7QWK/7qwk_pocket.pdb structures/7QWK/7qwk_ligand.sdf structures/7QWK/7qwk_ligand.pdb structures/7QWK/7qwk_ligand.cif structures/7QWK/7qwk_complex.pdb structures/7QWK/7qwk_complex.cif 7QWU classic BAZ2A Na Na Na compound 44 "[""FWR""]" 1 IC50 IC50 = = 57.9 ± 6.0 μM 57900.0 [] unit_conversion 4.2373214362725635 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 3 Table 2 reports compound 44 IC50 BAZ2A = 57.9 ± 6.0 μM; page 9 maps PDB 7QWU to compound 44. auto_single_measurement only accepted activity measurement [1] 1 structures\7QWU\7QWU_metadata.json point structures/7QWU/7qwu_protein.pdb structures/7QWU/7qwu_pocket.pdb structures/7QWU/7qwu_ligand.sdf structures/7QWU/7qwu_ligand.pdb structures/7QWU/7qwu_ligand.cif structures/7QWU/7qwu_complex.pdb structures/7QWU/7qwu_complex.cif 7QWV extended REC114-TOPOVIBL complex mouse REC114 residues 15-159; TOPOVIBL peptide residues 559-576 Na Na "[""CHAIN:B""]" 1 Kd Kd = = 3.3 µM 3300.0 [] unit_conversion 5.481486060122112 success True direct_binding Isothermal titration calorimetry of REC114 PH domain with TOPOVIBL peptide spanning residues 559–576. 3 Figure 1h reports REC114(15–159) binding TOPOVIBL(559–576), Kd = 3.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QWV\7QWV_metadata.json point structures/7QWV/7qwv_protein.pdb structures/7QWV/7qwv_pocket.pdb structures/7QWV/7qwv_ligand.pdb structures/7QWV/7qwv_ligand.cif structures/7QWV/7qwv_complex.pdb structures/7QWV/7qwv_complex.cif 7QWY classic BAZ2A Na Na Na compound 61 "[""G0I""]" 1 IC50 IC50 = = 54.0 ± 0.2 μM 54000.0 [] unit_conversion 4.267606240177032 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 3 Table 2 reports compound 61 IC50 BAZ2A = 54.0 ± 0.2 μM; page 9 maps PDB 7QWY to compound 61. auto_single_measurement only accepted activity measurement [1] 1 structures\7QWY\7QWY_metadata.json point structures/7QWY/7qwy_protein.pdb structures/7QWY/7qwy_pocket.pdb structures/7QWY/7qwy_ligand.sdf structures/7QWY/7qwy_ligand.pdb structures/7QWY/7qwy_ligand.cif structures/7QWY/7qwy_complex.pdb structures/7QWY/7qwy_complex.cif 7QX2 classic BAZ2A Na Na Na compound 63 "[""G1U""]" 1 IC50 IC50 = = 60.5 ± 9.4 μM 60500.0 [] unit_conversion 4.218244625347531 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 3 Table 2 reports compound 63 IC50 BAZ2A = 60.5 ± 9.4 μM; page 9 maps PDB 7QX2 to compound 63. auto_single_measurement only accepted activity measurement [1] 1 structures\7QX2\7QX2_metadata.json point structures/7QX2/7qx2_protein.pdb structures/7QX2/7qx2_pocket.pdb structures/7QX2/7qx2_ligand.sdf structures/7QX2/7qx2_ligand.pdb structures/7QX2/7qx2_ligand.cif structures/7QX2/7qx2_complex.pdb structures/7QX2/7qx2_complex.cif 7QX9 classic BAZ2A Na Na Na compound 65 "[""G2U""]" 1 IC50 IC50 = = 54.0 ± 0.3 μM 54000.0 [] unit_conversion 4.267606240177032 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 3 Table 2 reports compound 65 IC50 BAZ2A = 54.0 ± 0.3 μM; page 9 maps PDB 7QX9 to compound 65. auto_single_measurement only accepted activity measurement [1] 1 structures\7QX9\7QX9_metadata.json point structures/7QX9/7qx9_protein.pdb structures/7QX9/7qx9_pocket.pdb structures/7QX9/7qx9_ligand.sdf structures/7QX9/7qx9_ligand.pdb structures/7QX9/7qx9_ligand.cif structures/7QX9/7qx9_complex.pdb structures/7QX9/7qx9_complex.cif 7QXL classic BAZ2A Na Na Na compound 77 "[""GGQ""]" 1 IC50 IC50 = = 38.9 ± 2.0 μM 38900.0 [] unit_conversion 4.410050398674292 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 5 Table 3 reports compound 77 IC50 BAZ2A = 38.9 ± 2.0 μM; page 9 maps PDB 7QXL to compound 77. auto_single_measurement only accepted activity measurement [1] 1 structures\7QXL\7QXL_metadata.json point structures/7QXL/7qxl_protein.pdb structures/7QXL/7qxl_pocket.pdb structures/7QXL/7qxl_ligand.sdf structures/7QXL/7qxl_ligand.pdb structures/7QXL/7qxl_ligand.cif structures/7QXL/7qxl_complex.pdb structures/7QXL/7qxl_complex.cif 7QXQ classic Renilla-type luciferase (AncFT) Na Na Na coelenteramide (CEI) "[""CEI""]" 1 Kd Kd = = 16 ± 2 µM 16000.0 [] unit_conversion 4.795880017344075 success True direct_binding Anaerobic equilibrium binding experiment. 15 Supplementary Fig. 11c reports an AncFT coelenteramide-product Kd of 16 ± 2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7QXQ\7QXQ_metadata.json point structures/7QXQ/7qxq_protein.pdb structures/7QXQ/7qxq_pocket.pdb structures/7QXQ/7qxq_ligand.sdf structures/7QXQ/7qxq_ligand.pdb structures/7QXQ/7qxq_ligand.cif structures/7QXQ/7qxq_complex.pdb structures/7QXQ/7qxq_complex.cif 7QY0 classic furin Na Na Na inhibitor 1 "[""I0T""]" 3 Ki Ki = = 3.8 ± 0.8 nM 3.8 [] unit_conversion 8.42021640338319 success True biochemical_inhibition Enzyme kinetic Dixon plot with fluorogenic PC substrate pyr-ERTKR-7-amino-4-methylcoumarin; competitive inhibition. 3 The Dixon plot for compound 1 indicated competitive inhibition (Ki = 3.8 ± 0.8 nM). auto_metric_priority unique highest-priority metric family: Ki [3] 3 structures\7QY0\7QY0_metadata.json point structures/7QY0/7qy0_protein.pdb structures/7QY0/7qy0_pocket.pdb structures/7QY0/7qy0_ligand.sdf structures/7QY0/7qy0_ligand.pdb structures/7QY0/7qy0_ligand.cif structures/7QY0/7qy0_complex.pdb structures/7QY0/7qy0_complex.cif 7QYE classic BAZ2A Na Na Na compound 78 "[""GQF""]" 1 IC50 IC50 = = 40.1 ± 3.4 μM 40100.0 [] unit_conversion 4.396855627379818 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 5 Table 3 reports compound 78 IC50 BAZ2A = 40.1 ± 3.4 μM; page 9 maps PDB 7QYE to compound 78. auto_single_measurement only accepted activity measurement [1] 1 structures\7QYE\7QYE_metadata.json point structures/7QYE/7qye_protein.pdb structures/7QYE/7qye_pocket.pdb structures/7QYE/7qye_ligand.sdf structures/7QYE/7qye_ligand.pdb structures/7QYE/7qye_ligand.cif structures/7QYE/7qye_complex.pdb structures/7QYE/7qye_complex.cif 7QYO classic BAZ2A Na Na Na compound 79 "[""GKI""]" 1 IC50 IC50 = = 12.5 ± 0.4 μM 12500.0 [] unit_conversion 4.903089986991944 success True biochemical_inhibition AlphaScreen competitive binding assay against BAZ2A bromodomain binding to acetylated peptide. 5 Table 3 reports compound 79 IC50 BAZ2A = 12.5 ± 0.4 μM; page 9 maps PDB 7QYO to compound 79. auto_single_measurement only accepted activity measurement [1] 1 structures\7QYO\7QYO_metadata.json point structures/7QYO/7qyo_protein.pdb structures/7QYO/7qyo_pocket.pdb structures/7QYO/7qyo_ligand.sdf structures/7QYO/7qyo_ligand.pdb structures/7QYO/7qyo_ligand.cif structures/7QYO/7qyo_complex.pdb structures/7QYO/7qyo_complex.cif 7QYT classic BAZ2A Na Na Na compound 80 "[""GJI""]" 1 IC50 IC50 = = 11.4 ± 0.3 µM 11400.0 [] unit_conversion 4.943095148663527 success True biochemical_inhibition AlphaScreen dose-response competitive binding assay against acetylated peptide. 5 Table 3 reports compound 80 IC50 BAZ2A = 11.4 ± 0.3 µM; page 9 maps 7QYT to compound 80. auto_single_measurement only accepted activity measurement [1] 1 structures\7QYT\7QYT_metadata.json point structures/7QYT/7qyt_protein.pdb structures/7QYT/7qyt_pocket.pdb structures/7QYT/7qyt_ligand.sdf structures/7QYT/7qyt_ligand.pdb structures/7QYT/7qyt_ligand.cif structures/7QYT/7qyt_complex.pdb structures/7QYT/7qyt_complex.cif 7QYU classic BAZ2A Na Na Na compound 88 "[""GJC""]" 1 IC50 IC50 = = 42.9 ± 4.6 µM 42900.0 [] unit_conversion 4.367542707815276 success True biochemical_inhibition AlphaScreen dose-response competitive binding assay against acetylated peptide. 6 Table 3 reports compound 88 IC50 BAZ2A = 42.9 ± 4.6 µM; page 9 maps 7QYU to compound 88. auto_single_measurement only accepted activity measurement [1] 1 structures\7QYU\7QYU_metadata.json point structures/7QYU/7qyu_protein.pdb structures/7QYU/7qyu_pocket.pdb structures/7QYU/7qyu_ligand.sdf structures/7QYU/7qyu_ligand.pdb structures/7QYU/7qyu_ligand.cif structures/7QYU/7qyu_complex.pdb structures/7QYU/7qyu_complex.cif 7QZ0 classic BAZ2A Na Na Na compound 83 "[""GQX""]" 1 IC50 IC50 = = 11.0 ± 0.2 µM 11000.0 [] unit_conversion 4.958607314841775 success True biochemical_inhibition AlphaScreen dose-response competitive binding assay against acetylated peptide. 5 Table 3 reports compound 83 IC50 BAZ2A = 11.0 ± 0.2 µM; page 9 maps 7QZ0 to compound 83. auto_single_measurement only accepted activity measurement [1] 1 structures\7QZ0\7QZ0_metadata.json point structures/7QZ0/7qz0_protein.pdb structures/7QZ0/7qz0_pocket.pdb structures/7QZ0/7qz0_ligand.sdf structures/7QZ0/7qz0_ligand.pdb structures/7QZ0/7qz0_ligand.cif structures/7QZ0/7qz0_complex.pdb structures/7QZ0/7qz0_complex.cif 7QZ4 classic BAZ2A Na Na Na compound 87 "[""GIZ""]" 1 IC50 IC50 = = 46.6 ± 2.5 µM 46600.0 [] unit_conversion 4.33161408331 success True biochemical_inhibition AlphaScreen dose-response competitive binding assay against acetylated peptide. 6 Table 3 reports compound 87 IC50 BAZ2A = 46.6 ± 2.5 µM; page 9 maps 7QZ4 to compound 87. auto_single_measurement only accepted activity measurement [1] 1 structures\7QZ4\7QZ4_metadata.json point structures/7QZ4/7qz4_protein.pdb structures/7QZ4/7qz4_pocket.pdb structures/7QZ4/7qz4_ligand.sdf structures/7QZ4/7qz4_ligand.pdb structures/7QZ4/7qz4_ligand.cif structures/7QZ4/7qz4_complex.pdb structures/7QZ4/7qz4_complex.cif 7QZB classic BAZ2A Na Na Na compound 98 "[""GI0""]" 1 IC50 IC50 = = 12.6 ± 1.4 µM 12600.0 [] unit_conversion 4.8996294548824375 success True biochemical_inhibition AlphaScreen dose-response competitive binding assay against acetylated peptide. 5 Table 3 reports compound 98 IC50 BAZ2A = 12.6 ± 1.4 µM; page 9 maps 7QZB to compound 98. auto_single_measurement only accepted activity measurement [1] 1 structures\7QZB\7QZB_metadata.json point structures/7QZB/7qzb_protein.pdb structures/7QZB/7qzb_pocket.pdb structures/7QZB/7qzb_ligand.sdf structures/7QZB/7qzb_ligand.pdb structures/7QZB/7qzb_ligand.cif structures/7QZB/7qzb_complex.pdb structures/7QZB/7qzb_complex.cif 7QZT classic BAZ2A Na Na Na fragment 9 "[""GIU""]" 1 IC50 IC50 > > 200 µM 200000.0 [] unit_conversion 3.6989700043360187 success True biochemical_inhibition AlphaScreen competitive binding assay against acetylated peptide. 2 Table 1 reports compound 9 IC50 BAZ2A > 200 µM; page 9 maps 7QZT to compound 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7QZT\7QZT_metadata.json point structures/7QZT/7qzt_protein.pdb structures/7QZT/7qzt_pocket.pdb structures/7QZT/7qzt_ligand.sdf structures/7QZT/7qzt_ligand.pdb structures/7QZT/7qzt_ligand.cif structures/7QZT/7qzt_complex.pdb structures/7QZT/7qzt_complex.cif 7QZX extended Carbonic anhydrase II human Na Na Na "[""HIL""]" 1 Ki Ki = = 13.7 ± 1.2 nM 13.7 [] unit_conversion 7.863279432843593 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay. 7 Table 1 reports Ki = 13.7 ± 1.2 nM for compound 34c against hCA II. Figure 3 identifies hCA II–34c as PDB 7QZX. auto_single_measurement only accepted activity measurement [1] 1 structures\7QZX\7QZX_metadata.json point structures/7QZX/7qzx_ligand.sdf structures/7QZX/7qzx_ligand.cif structures/7QZX/7qzx_complex.cif 7R01 classic BAZ2A Na Na Na fragment 18 "[""GI7""]" 1 IC50 IC50 > > 200 µM 200000.0 [] unit_conversion 3.6989700043360187 success True biochemical_inhibition AlphaScreen competitive binding assay against acetylated peptide. 2 Table 1 reports compound 18 IC50 BAZ2A > 200 µM; page 9 maps 7R01 to compound 18. auto_single_measurement only accepted activity measurement [1] 1 structures\7R01\7R01_metadata.json point structures/7R01/7r01_protein.pdb structures/7R01/7r01_pocket.pdb structures/7R01/7r01_ligand.sdf structures/7R01/7r01_ligand.pdb structures/7R01/7r01_ligand.cif structures/7R01/7r01_complex.pdb structures/7R01/7r01_complex.cif 7R0B classic BAZ2A Na Na Na compound 47 "[""GIE""]" 1 IC50 IC50 = = 33.3 ± 0.4 µM 33300.0 [] unit_conversion 4.47755576649368 success True biochemical_inhibition AlphaScreen dose-response competitive binding assay against acetylated peptide. 3 Table 2 reports compound 47 IC50 BAZ2A = 33.3 ± 0.4 µM; page 9 maps 7R0B to compound 47. auto_single_measurement only accepted activity measurement [1] 1 structures\7R0B\7R0B_metadata.json point structures/7R0B/7r0b_protein.pdb structures/7R0B/7r0b_pocket.pdb structures/7R0B/7r0b_ligand.sdf structures/7R0B/7r0b_ligand.pdb structures/7R0B/7r0b_ligand.cif structures/7R0B/7r0b_complex.pdb structures/7R0B/7r0b_complex.cif 7R1O extended p62 (SQSTM1) Homo sapiens ZZ domain of human p62, residues 115-190 Na dusquetide "[""CHAIN:EEE"", ""CHAIN:FFF""]" 1 Kd Kd = = 0.8 µM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Fluorescent microscale thermophoresis direct-binding assay using purified p62 ZZ domain and fluorescein-labeled dusquetide. 4 The paper reports a microscale thermophoresis dissociation constant of Kd = 0.8 µM for p62ZZ-dusquetide; the methods specify direct MST binding with purified ZZ domain (aa 115-190) and fluorescein-labeled dusquetide. auto_single_measurement only accepted activity measurement [1] 1 structures\7R1O\7R1O_metadata.json point structures/7R1O/7r1o_ligand.cif structures/7R1O/7r1o_complex.cif 7R1T classic SARS-CoV-2 nsp10/nsp16 SARS-CoV-2 Truncated nsp10 residues 10-131 and full-length nsp16 residues 1-298, expressed with N-terminal His8-SUMO tags that were removed before purification Na SS148 "[""6NR""]" 1 IC50 IC50 = = 1.2 ± 0.4 μM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition Radiometric nsp10–nsp16 MTase activity assay; Table 1 values are mean ± SD from triplicate experiments (N = 3). 3 Table 1, “Inhibition of nsp10–nsp16 MTase activity,” reports SS148 IC50 = 1.2 ± 0.4 μM. The adjacent text explicitly maps the nsp10–nsp16/SS148 structure to PDB ID 7R1T. auto_single_measurement only accepted activity measurement [1] 1 structures\7R1T\7R1T_metadata.json point structures/7R1T/7r1t_protein.pdb structures/7R1T/7r1t_pocket.pdb structures/7R1T/7r1t_ligand.sdf structures/7R1T/7r1t_ligand.pdb structures/7R1T/7r1t_ligand.cif structures/7R1T/7r1t_complex.pdb structures/7R1T/7r1t_complex.cif 7R1U classic SARS-CoV-2 nsp10/nsp16 SARS-CoV-2 Truncated nsp10 residues 10-131 and full-length nsp16 residues 1-298, expressed with N-terminal His8-SUMO tags that were removed before purification Na WZ16 "[""4IK""]" 1 IC50 IC50 = = 3.4 ± 0.7 μM 3400.0 [] unit_conversion 5.468521082957745 success True biochemical_inhibition Radiometric nsp10–nsp16 MTase activity assay; Table 1 values are mean ± SD from triplicate experiments (N = 3). 3 Table 1, “Inhibition of nsp10–nsp16 MTase activity,” reports WZ16 IC50 = 3.4 ± 0.7 μM. The adjacent text explicitly maps the nsp10–nsp16/WZ16 structure to PDB ID 7R1U. auto_single_measurement only accepted activity measurement [1] 1 structures\7R1U\7R1U_metadata.json point structures/7R1U/7r1u_protein.pdb structures/7R1U/7r1u_pocket.pdb structures/7R1U/7r1u_ligand.sdf structures/7R1U/7r1u_ligand.pdb structures/7R1U/7r1u_ligand.cif structures/7R1U/7r1u_complex.pdb structures/7R1U/7r1u_complex.cif 7R1V extended BamA E. coli BamA beta-barrel Na dynobactin A "[""CHAIN:B""]" 1 Kd Kd = = 2.1 ± 0.2 nM 2.1 [] unit_conversion 8.67778070526608 success True direct_binding SPR equilibrium measurement of BamA and dynobactin A. 17 Supplementary Table 8 reports dynobactin A Kd [nM] (equil.) = 2.1 ± 0.2 for BamA and ligands. auto_single_measurement only accepted activity measurement [1] 1 structures\7R1V\7R1V_metadata.json point structures/7R1V/7r1v_protein.pdb structures/7R1V/7r1v_pocket.pdb structures/7R1V/7r1v_ligand.pdb structures/7R1V/7r1v_ligand.cif structures/7R1V/7r1v_complex.pdb structures/7R1V/7r1v_complex.cif 7R1X extended Carbonic anhydrase II human Na Na compound 35c; 4-oxo-N-(4-sulfamoylphenethyl)-1,3,4,6,7,11b-hexahydro-2H-pyrazino[2,1-a]isoquinoline-2-carbothioamide "[""HFF""]" 1 Ki Ki = = 7.6 ± 0.4 nM 7.6 [] unit_conversion 8.119186407719209 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay. 7 Table 1 reports Ki = 7.6 ± 0.4 nM for compound 35c against hCA II. Figure 2 identifies hCA II–35c as PDB 7R1X. auto_single_measurement only accepted activity measurement [1] 1 structures\7R1X\7R1X_metadata.json point structures/7R1X/7r1x_ligand.sdf structures/7R1X/7r1x_ligand.cif structures/7R1X/7r1x_complex.cif 7R44 classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R44\7R44_metadata.json point structures/7R44/7r44_protein.pdb structures/7R44/7r44_pocket.pdb structures/7R44/7r44_ligand.sdf structures/7R44/7r44_ligand.pdb structures/7R44/7r44_ligand.cif structures/7R44/7r44_complex.pdb structures/7R44/7r44_complex.cif 7R45 classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R45\7R45_metadata.json point structures/7R45/7r45_protein.pdb structures/7R45/7r45_pocket.pdb structures/7R45/7r45_ligand.sdf structures/7R45/7r45_ligand.pdb structures/7R45/7r45_ligand.cif structures/7R45/7r45_complex.pdb structures/7R45/7r45_complex.cif 7R46 classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R46\7R46_metadata.json point structures/7R46/7r46_protein.pdb structures/7R46/7r46_pocket.pdb structures/7R46/7r46_ligand.sdf structures/7R46/7r46_ligand.pdb structures/7R46/7r46_ligand.cif structures/7R46/7r46_complex.pdb structures/7R46/7r46_complex.cif 7R47 classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R47\7R47_metadata.json point structures/7R47/7r47_protein.pdb structures/7R47/7r47_pocket.pdb structures/7R47/7r47_ligand.sdf structures/7R47/7r47_ligand.pdb structures/7R47/7r47_ligand.cif structures/7R47/7r47_complex.pdb structures/7R47/7r47_complex.cif 7R48 classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R48\7R48_metadata.json point structures/7R48/7r48_protein.pdb structures/7R48/7r48_pocket.pdb structures/7R48/7r48_ligand.sdf structures/7R48/7r48_ligand.pdb structures/7R48/7r48_ligand.cif structures/7R48/7r48_complex.pdb structures/7R48/7r48_complex.cif 7R4C classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R4C\7R4C_metadata.json point structures/7R4C/7r4c_protein.pdb structures/7R4C/7r4c_pocket.pdb structures/7R4C/7r4c_ligand.sdf structures/7R4C/7r4c_ligand.pdb structures/7R4C/7r4c_ligand.cif structures/7R4C/7r4c_complex.pdb structures/7R4C/7r4c_complex.cif 7R4D classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R4D\7R4D_metadata.json point structures/7R4D/7r4d_protein.pdb structures/7R4D/7r4d_pocket.pdb structures/7R4D/7r4d_ligand.sdf structures/7R4D/7r4d_ligand.pdb structures/7R4D/7r4d_ligand.cif structures/7R4D/7r4d_complex.pdb structures/7R4D/7r4d_complex.cif 7R4F classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R4F\7R4F_metadata.json point structures/7R4F/7r4f_protein.pdb structures/7R4F/7r4f_pocket.pdb structures/7R4F/7r4f_ligand.sdf structures/7R4F/7r4f_ligand.pdb structures/7R4F/7r4f_ligand.cif structures/7R4F/7r4f_complex.pdb structures/7R4F/7r4f_complex.cif 7R4G classic Bovine complex I bovine Na Na IM1761092 (IM1092) "[""I49""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition Detergent-solubilized purified enzyme catalysis 3 IM1092 IC50 for purified bovine complex I catalysis. auto_single_measurement only accepted activity measurement [1] 1 structures\7R4G\7R4G_metadata.json point structures/7R4G/7r4g_protein.pdb structures/7R4G/7r4g_pocket.pdb structures/7R4G/7r4g_ligand.sdf structures/7R4G/7r4g_ligand.pdb structures/7R4G/7r4g_ligand.cif structures/7R4G/7r4g_complex.pdb structures/7R4G/7r4g_complex.cif 7R52 classic human TLR8 human Na Na Compound 2 "[""I6A""]" 1 IC50 IC50 = = 0.53 μM 530.0 [] unit_conversion 6.275724130399211 success True direct_binding TLR8 FRET binding assay 2 Figure 1 prints “TLR8 binding IC50: 0.53 μM” for compound 2. auto_single_measurement only accepted activity measurement [1] 1 structures\7R52\7R52_metadata.json point structures/7R52/7r52_protein.pdb structures/7R52/7r52_pocket.pdb structures/7R52/7r52_ligand.sdf structures/7R52/7r52_ligand.pdb structures/7R52/7r52_ligand.cif structures/7R52/7r52_complex.pdb structures/7R52/7r52_complex.cif 7R54 classic human TLR8 human Na Na Compound 4 "[""I5B""]" 1 IC50 IC50 = = 0.039 μM 39.0 [] unit_conversion 7.4089353929735005 success True direct_binding TLR8 FRET binding assay. 3 Table 1 reports FRET IC50 0.039 μM for compound 4. auto_single_measurement only accepted activity measurement [1] 1 structures\7R54\7R54_metadata.json point structures/7R54/7r54_protein.pdb structures/7R54/7r54_pocket.pdb structures/7R54/7r54_ligand.sdf structures/7R54/7r54_ligand.pdb structures/7R54/7r54_ligand.cif structures/7R54/7r54_complex.pdb structures/7R54/7r54_complex.cif 7R75 classic human SHP2 (PTPN11) Homo sapiens (human) Na Na compound 16 "[""33I""]" 1 IC50 IC50 = = 101 nM 101.0 [] unit_conversion 6.995678626217357 success True biochemical_inhibition Full-length human SHP2 enzyme assay. 4 Table 2 reports compound 16, SHP2 IC50 = 101 nM; the accompanying text identifies it as the SHP2 enzyme assay. Figure 4 identifies PDB 7R75 as compound 16 bound to SHP2. auto_single_measurement only accepted activity measurement [1] 1 structures\7R75\7R75_metadata.json point structures/7R75/7r75_protein.pdb structures/7R75/7r75_pocket.pdb structures/7R75/7r75_ligand.sdf structures/7R75/7r75_ligand.pdb structures/7R75/7r75_ligand.cif structures/7R75/7r75_complex.pdb structures/7R75/7r75_complex.cif 7R7D classic human SHP2 (PTPN11) Homo sapiens (human) Na Na compound 22 "[""37I""]" 1 IC50 IC50 = = 53 nM 53.0 [] unit_conversion 7.275724130399211 success True biochemical_inhibition Full-length human SHP2 enzyme assay. 5 Table 5 reports compound 22, SHP2 IC50 = 53 nM. Figure 6 identifies PDB 7R7D as compound 22 bound to SHP2. auto_single_measurement only accepted activity measurement [1] 1 structures\7R7D\7R7D_metadata.json point structures/7R7D/7r7d_protein.pdb structures/7R7D/7r7d_pocket.pdb structures/7R7D/7r7d_ligand.sdf structures/7R7D/7r7d_ligand.pdb structures/7R7D/7r7d_ligand.cif structures/7R7D/7r7d_complex.pdb structures/7R7D/7r7d_complex.cif 7R7I classic human SHP2 (PTPN11) Homo sapiens (human) Na Na compound 27 "[""3CW""]" 1 IC50 IC50 = = 1 nM 1.0 [] unit_conversion 9.0 success True biochemical_inhibition Full-length human SHP2 enzyme assay. 7 Table 7 reports compound 27, SHP2 IC50 = 1 nM. Figure 7 identifies PDB 7R7I as compound 27 bound to SHP2. auto_single_measurement only accepted activity measurement [1] 1 structures\7R7I\7R7I_metadata.json point structures/7R7I/7r7i_protein.pdb structures/7R7I/7r7i_pocket.pdb structures/7R7I/7r7i_ligand.sdf structures/7R7I/7r7i_ligand.pdb structures/7R7I/7r7i_ligand.cif structures/7R7I/7r7i_complex.pdb structures/7R7I/7r7i_complex.cif 7R7L classic human SHP2 (PTPN11) Homo sapiens (human) Na Na compound 30 (IACS-15414) "[""3ED""]" 1 IC50 IC50 = = 122 nM 122.0 [] unit_conversion 6.913640169325252 success True biochemical_inhibition Full-length human SHP2 enzyme assay. 8 Table 8 reports compound 30, the (Ra) atropisomer, SHP2 IC50 = 122 nM. Figure 8 identifies compound 30 as IACS-15414; Figure 9 identifies PDB 7R7L as compound 30 bound to SHP2. auto_single_measurement only accepted activity measurement [1] 1 structures\7R7L\7R7L_metadata.json point structures/7R7L/7r7l_protein.pdb structures/7R7L/7r7l_pocket.pdb structures/7R7L/7r7l_ligand.sdf structures/7R7L/7r7l_ligand.pdb structures/7R7L/7r7l_ligand.cif structures/7R7L/7r7l_complex.pdb structures/7R7L/7r7l_complex.cif 7R8R classic BRD3-BD1 Na Na Na Physachenolide C (PCC) "[""8L6""]" 2 Kd Kd = = 14.1 ± 1.5 nM 14.1 [] unit_conversion 7.85078088734462 success True direct_binding Microscale thermophoresis (MST) direct binding of PCC to BRD3-BD1. 2 Figure 1 caption states: PCC binds BRD3-BD1 by MST with a Kd of 14.1 ± 1.5 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7R8R\7R8R_metadata.json point structures/7R8R/7r8r_protein.pdb structures/7R8R/7r8r_pocket.pdb structures/7R8R/7r8r_ligand.sdf structures/7R8R/7r8r_ligand.pdb structures/7R8R/7r8r_ligand.cif structures/7R8R/7r8r_complex.pdb structures/7R8R/7r8r_complex.cif 7R8S classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na Na 4-n-propylbenzoic acid "[""8ZU""]" 1 Kd Kd = = 0.54 ± 0.02 μM 540.0 [] unit_conversion 6.267606240177031 success True direct_binding UV-visible spectroscopic substrate-binding titration of CYP199A4; dissociation constants reported in Table 1. 6 Table 1 reports Kd = 0.54 ± 0.02 μM for 4-n-propylBA; the text identifies this table as substrate-binding data for CYP199A4. auto_single_measurement only accepted activity measurement [1] 1 structures\7R8S\7R8S_metadata.json point structures/7R8S/7r8s_protein.pdb structures/7R8S/7r8s_pocket.pdb structures/7R8S/7r8s_ligand.sdf structures/7R8S/7r8s_ligand.pdb structures/7R8S/7r8s_ligand.cif structures/7R8S/7r8s_complex.pdb structures/7R8S/7r8s_complex.cif 7R8X extended LNK (SH2B3) Mus musculus Mouse LNK SH2 domain, residues 324-446, expressed with an N-terminal NusA fusion cleaved by TEV WT (wild type) EPOR pY454 phosphopeptide "[""CHAIN:C""]" 1 IC50 IC50 = = 651 nM 651.0 [] unit_conversion 6.186419011431807 success True biochemical_inhibition Phosphopeptide SPR competition assay. 5 Table 2 lists EPOR pY454 with an IC50 of 651 nM from the phosphopeptide competition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7R8X\7R8X_metadata.json point structures/7R8X/7r8x_protein.pdb structures/7R8X/7r8x_pocket.pdb structures/7R8X/7r8x_ligand.pdb structures/7R8X/7r8x_ligand.cif structures/7R8X/7r8x_complex.pdb structures/7R8X/7r8x_complex.cif 7R9C classic BRD4 Na Na Na compound 32; N,N-dimethyl-2-[(3R)-3-(5-{2-[2-methyl-5-(propan-2-yl)phenoxy]pyrimidin-4-yl}-4-[4-(trifluoromethyl)phenyl]-1H-imidazol-1-yl)pyrrolidin-1-yl]ethan-1-amine "[""2IR""]" 2 Kd Kd = = 37.2 nM 37.2 [] unit_conversion 7.429457060118103 success True direct_binding Isothermal titration calorimetry (ITC) 5 The text states that inhibitor 32 bound weaker with a Kd of 37.2 nM by ITC. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7R9C\7R9C_metadata.json point structures/7R9C/7r9c_protein.pdb structures/7R9C/7r9c_pocket.pdb structures/7R9C/7r9c_ligand.sdf structures/7R9C/7r9c_ligand.pdb structures/7R9C/7r9c_ligand.cif structures/7R9C/7r9c_complex.pdb structures/7R9C/7r9c_complex.cif 7RA5 classic CDK2 Na Na Na compound 4 "[""3I3""]" 1 IC50 IC50 = = 78 nM 78.0 [] unit_conversion 7.107905397309519 success True biochemical_inhibition CDK2 enzymatic activity assay; Table 1. 2 Table 1 reports compound 4 with CDK2 enzymatic activity IC50 of 78 nM. The paper identifies the X-ray crystal structure of compound 4 with CDK2 as PDB 7RA5. auto_single_measurement only accepted activity measurement [1] 1 structures\7RA5\7RA5_metadata.json point structures/7RA5/7ra5_protein.pdb structures/7RA5/7ra5_pocket.pdb structures/7RA5/7ra5_ligand.sdf structures/7RA5/7ra5_ligand.pdb structures/7RA5/7ra5_ligand.cif structures/7RA5/7ra5_complex.pdb structures/7RA5/7ra5_complex.cif 7RBG classic Human DNA polymerase beta Human Na Na DNA^dRP (crosslinked dRP-18-mer); dCTP "[""DCP""]" 1 Kd Kd = = 0.38 ± 0.08 µM 380.0 [] unit_conversion 6.42021640338319 success True direct_binding Presteady-state kinetic analysis of correct dCTP incorporation onto the cross-linked hPolβ–DNA^dRP complex; Table 1 reports apparent dCTP Kd. 5 Table 1 reports Kd = 0.38 ± 0.08 µM for dCTP with the cross-linked hPolβ–DNA^dRP complex; the adjacent text identifies this as the apparent binding affinity for correct dCTP. auto_single_measurement only accepted activity measurement [1] 1 structures\7RBG\7RBG_metadata.json point structures/7RBG/7rbg_protein.pdb structures/7RBG/7rbg_pocket.pdb structures/7RBG/7rbg_ligand.sdf structures/7RBG/7rbg_ligand.pdb structures/7RBG/7rbg_ligand.cif structures/7RBG/7rbg_complex.pdb structures/7RBG/7rbg_complex.cif 7RBH classic Human DNA polymerase beta Human Na Na DNA^dRP (crosslinked dRP-18-mer); dCTP "[""DCP""]" 1 Kd Kd = = 0.38 ± 0.08 µM 380.0 [] unit_conversion 6.42021640338319 success True direct_binding Presteady-state kinetic analysis of correct dCTP incorporation onto the cross-linked hPolβ–DNA^dRP complex; Table 1 reports apparent dCTP Kd. 5 Table 1 reports Kd = 0.38 ± 0.08 µM for dCTP with the cross-linked hPolβ–DNA^dRP complex; the adjacent text identifies this as the apparent binding affinity for correct dCTP. auto_single_measurement only accepted activity measurement [1] 1 structures\7RBH\7RBH_metadata.json point structures/7RBH/7rbh_protein.pdb structures/7RBH/7rbh_pocket.pdb structures/7RBH/7rbh_ligand.sdf structures/7RBH/7rbh_ligand.pdb structures/7RBH/7rbh_ligand.cif structures/7RBH/7rbh_complex.pdb structures/7RBH/7rbh_complex.cif 7RCI classic PMS2 Na N-terminal domain of PMS2, residues 1-365 p.Asn335Ser ATP "[""ATP""]" 1 Kd Kd = = 0.103 mM 103000.0 [] unit_conversion 3.987162775294828 success True direct_binding Isothermal titration calorimetry of ATP binding to the purified PMS2 N-terminal ATPase-domain variant, with MgCl2 present. 11 The K_D was 0.103 mM for the p.Asn335Ser variant (mean of three experiments). auto_single_measurement only accepted activity measurement [1] 1 structures\7RCI\7RCI_metadata.json point structures/7RCI/7rci_protein.pdb structures/7RCI/7rci_pocket.pdb structures/7RCI/7rci_ligand.sdf structures/7RCI/7rci_ligand.pdb structures/7RCI/7rci_ligand.cif structures/7RCI/7rci_complex.pdb structures/7RCI/7rci_complex.cif 7RCK classic PMS2 Na N-terminal domain of PMS2, residues 1-365 WT (wild-type) ATP "[""ATP""]" 1 Kd Kd = = 0.059 mM 59000.0 [] unit_conversion 4.229147988357856 success True direct_binding Isothermal titration calorimetry of ATP binding to purified WT PMS2 N-terminal ATPase domain, with MgCl2 present. 11 The K_D was 0.059 mM for WT PMS2 (mean of three experiments). auto_single_measurement only accepted activity measurement [1] 1 structures\7RCK\7RCK_metadata.json point structures/7RCK/7rck_protein.pdb structures/7RCK/7rck_pocket.pdb structures/7RCK/7rck_ligand.sdf structures/7RCK/7rck_ligand.pdb structures/7RCK/7rck_ligand.cif structures/7RCK/7rck_complex.pdb structures/7RCK/7rck_complex.cif 7REB classic E. coli dihydrofolate reductase (EcDHFR) Escherichia coli Na Na UCP1223 (5-(3-(7-(4-(aminomethyl)phenyl)benzo[d][1,3]dioxol-5-yl)but-1-yn-1-yl)-6-ethylpyrimidine-2,4-diamine) "[""560""]" 1 Ki Ki = = 1.58 ± 0.26 nM 1.58 [] unit_conversion 8.801342913045577 success True biochemical_inhibition Steady-state enzyme inhibition assay; Table 3. 11 Table 3 reports EcDHFR Ki for UCP1223 as 1.58 ± 0.26 nM; Table 2 maps 7REB to EcDHFR:UCP1223. auto_single_measurement only accepted activity measurement [1] 1 structures\7REB\7REB_metadata.json point structures/7REB/7reb_protein.pdb structures/7REB/7reb_pocket.pdb structures/7REB/7reb_ligand.sdf structures/7REB/7reb_ligand.pdb structures/7REB/7reb_ligand.cif structures/7REB/7reb_complex.pdb structures/7REB/7reb_complex.cif 7REC classic CaMKII alpha (CaMKIIalpha) human CaMKII alpha hub Thr354Asn; Glu355Gln; Thr412Asn; Ile414Met; Ile464His; Phe467Met 5-HDC "[""7ZV""]" 1 Kd Kd = = 0.30 μM 300.0 [] unit_conversion 6.522878745280337 success True direct_binding Surface plasmon resonance binding of 5-HDC to immobilized CaMKIIα 6x Hub. 4 “By surface plasmon resonance, we detected binding to the isolated CaMKIIα hub by GHB analogs, the strongest interaction being with 5-HDC (K_D 0.30 μM).” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7REC\7REC_metadata.json point structures/7REC/7rec_protein.pdb structures/7REC/7rec_pocket.pdb structures/7REC/7rec_ligand.sdf structures/7REC/7rec_ligand.pdb structures/7REC/7rec_ligand.cif structures/7REC/7rec_complex.pdb structures/7REC/7rec_complex.cif 7REH classic T252E CYP199A4 Rhodopseudomonas palustris HaA2 Na T252E 4-methoxybenzoic acid (4-methoxybenzoate) "[""ANN""]" 1 Kd Kd = = 1.1 μM 1100.0 [] unit_conversion 5.958607314841775 success True direct_binding Native mass spectrometry used to confirm 4-methoxybenzoic acid binding and determine its affinity. 3 “A slightly lower affinity for 4-methoxybenzoic acid was determined when compared to that of the WT enzyme (1.1 μM vs 0.22 μM...)”; the preceding sentence identifies the affinity as Kd. auto_single_measurement only accepted activity measurement [1] 1 structures\7REH\7REH_metadata.json point structures/7REH/7reh_protein.pdb structures/7REH/7reh_pocket.pdb structures/7REH/7reh_ligand.sdf structures/7REH/7reh_ligand.pdb structures/7REH/7reh_ligand.cif structures/7REH/7reh_complex.pdb structures/7REH/7reh_complex.cif 7RFE classic IMPDH1 human IMPDH1(514), canonical 514-aa isoform Na GTP "[""GTP""]" 1 IC50 IC50 = = 188 µM 188000.0 [] unit_conversion 3.7258421507363204 success True biochemical_inhibition Biochemical GTP inhibition of human IMPDH1(514) with ATP, IMP, and NAD+ present. 4 Supplementary Table 3 reports WT IMPDH1(514) GTP IC50 188 µM; the publisher data-availability statement maps 7RFE to compressed IMPDH1(514). auto_single_measurement only accepted activity measurement [1] 1 structures\7RFE\7RFE_metadata.json point structures/7RFE/7rfe_protein.pdb structures/7RFE/7rfe_pocket.pdb structures/7RFE/7rfe_ligand.sdf structures/7RFE/7rfe_ligand.pdb structures/7RFE/7rfe_ligand.cif structures/7RFE/7rfe_complex.pdb structures/7RFE/7rfe_complex.cif 7RFG classic IMPDH1 human IMPDH1(514), canonical 514-aa isoform Na GTP "[""GTP""]" 1 IC50 IC50 = = 188 µM 188000.0 [] unit_conversion 3.7258421507363204 success True biochemical_inhibition Biochemical GTP inhibition of human IMPDH1(514) with ATP, IMP, and NAD+ present. 4 Supplementary Table 3 reports WT IMPDH1(514) GTP IC50 188 µM; the publisher data-availability statement maps 7RFG to compressed IMPDH1(514). auto_single_measurement only accepted activity measurement [1] 1 structures\7RFG\7RFG_metadata.json point structures/7RFG/7rfg_protein.pdb structures/7RFG/7rfg_pocket.pdb structures/7RFG/7rfg_ligand.sdf structures/7RFG/7rfg_ligand.pdb structures/7RFG/7rfg_ligand.cif structures/7RFG/7rfg_complex.pdb structures/7RFG/7rfg_complex.cif 7RFI classic IMPDH1 human retinal variant IMPDH1(595) Na GTP; ATP; IMP; NAD+ "[""GTP""]" 1 IC50 IC50 = = 1104 μM 1104000.0 [] unit_conversion 2.95703092660682 success True biochemical_inhibition GTP inhibition; 1 μM protein, 1 mM ATP, 1 mM IMP, 300 μM NAD+, varying GTP. 4 Supplemental Table 3 reports IMPDH1(595) WT IC50 for GTP of 1104 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7RFI\7RFI_metadata.json point structures/7RFI/7rfi_protein.pdb structures/7RFI/7rfi_pocket.pdb structures/7RFI/7rfi_ligand.sdf structures/7RFI/7rfi_ligand.pdb structures/7RFI/7rfi_ligand.cif structures/7RFI/7rfi_complex.pdb structures/7RFI/7rfi_complex.cif 7RFK classic CamA adenine methyltransferase Clostridioides difficile Na Na Sinefungin "[""SFG""]" 1 IC50 IC50 = = 24±2 µM 24000.0 [] unit_conversion 4.619788758288394 success True biochemical_inhibition CamA methylation inhibition assay with 50 nM CamA, 40 µM SAM, and 5 µM double-stranded DNA substrate; Figure 2 summary. 4 Figure 2e prints Sinefungin IC50 = 24±2 µM; the figure caption identifies IC50 measurements as inhibition of CamA methylation on DNA substrate. Page 10 maps the CamA-DNA-sinefungin structure to PDB 7RFK. auto_single_measurement only accepted activity measurement [1] 1 structures\7RFK\7RFK_metadata.json point structures/7RFK/7rfk_protein.pdb structures/7RFK/7rfk_pocket.pdb structures/7RFK/7rfk_ligand.sdf structures/7RFK/7rfk_ligand.pdb structures/7RFK/7rfk_ligand.cif structures/7RFK/7rfk_complex.pdb structures/7RFK/7rfk_complex.cif 7RFL classic CamA adenine methyltransferase Clostridioides difficile Na Na SGC0946 "[""AW2""]" 1 IC50 IC50 = = 4.7±0.4 µM 4700.0 [] unit_conversion 5.327902142064282 success True biochemical_inhibition CamA methylation inhibition assay with 50 nM CamA, 40 µM SAM, and 5 µM double-stranded DNA substrate; Figure 2 summary. 4 Figure 2e prints SGC0946 IC50 = 4.7±0.4 µM; the figure caption identifies IC50 measurements as inhibition of CamA methylation on DNA substrate. Page 10 maps the CamA-DNA-SGC0946 structure to PDB 7RFL. auto_single_measurement only accepted activity measurement [1] 1 structures\7RFL\7RFL_metadata.json point structures/7RFL/7rfl_protein.pdb structures/7RFL/7rfl_pocket.pdb structures/7RFL/7rfl_ligand.sdf structures/7RFL/7rfl_ligand.pdb structures/7RFL/7rfl_ligand.cif structures/7RFL/7rfl_complex.pdb structures/7RFL/7rfl_complex.cif 7RFM classic CamA adenine methyltransferase Clostridioides difficile Na Na EPZ004777 "[""0QK""]" 1 IC50 IC50 = = 43±3 µM 43000.0 [] unit_conversion 4.366531544420414 success True biochemical_inhibition CamA methylation inhibition assay with 50 nM CamA, 40 µM SAM, and 5 µM double-stranded DNA substrate; Figure 2 summary. 4 Figure 2e prints EPZ004777 IC50 = 43±3 µM; the figure caption identifies IC50 measurements as inhibition of CamA methylation on DNA substrate. Page 10 maps the CamA-DNA-EPZ004777 structure to PDB 7RFM. auto_single_measurement only accepted activity measurement [1] 1 structures\7RFM\7RFM_metadata.json point structures/7RFM/7rfm_protein.pdb structures/7RFM/7rfm_pocket.pdb structures/7RFM/7rfm_ligand.sdf structures/7RFM/7rfm_ligand.pdb structures/7RFM/7rfm_ligand.cif structures/7RFM/7rfm_complex.pdb structures/7RFM/7rfm_complex.cif 7RFN classic CamA adenine methyltransferase Clostridioides difficile Na Na SGC8158 "[""MJ7""]" 1 IC50 IC50 = = 7.1±0.8 µM 7100.0 [] unit_conversion 5.1487416512809245 success True biochemical_inhibition CamA methylation inhibition assay with 50 nM CamA, 40 µM SAM, and 5 µM double-stranded DNA substrate; Figure 4 summary. 6 Figure 4e prints SGC8158 IC50 = 7.1±0.8 µM; the caption identifies IC50 measurements as inhibition of CamA methylation. Page 10 maps the CamA-DNA-SGC8158 structure to PDB 7RFN. auto_single_measurement only accepted activity measurement [1] 1 structures\7RFN\7RFN_metadata.json point structures/7RFN/7rfn_protein.pdb structures/7RFN/7rfn_pocket.pdb structures/7RFN/7rfn_ligand.sdf structures/7RFN/7rfn_ligand.pdb structures/7RFN/7rfn_ligand.cif structures/7RFN/7rfn_complex.pdb structures/7RFN/7rfn_complex.cif 7RFT extended Starch adherence system protein 20 (Sas20) Ruminococcus bromii Sas20d1 Na maltotriose "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 187.9 ± 58.1 µM 187900.0 [] unit_conversion 3.726073219899474 success True direct_binding ITC; Table 3 affinity determination for Sas20d1 with maltotriose. 7 Table 3 reports Sas20d1–maltotriose Kd = 187.9 ± 58.1 µM. The text identifies 7RFT as the maltotriose-bound Sas20d1 structure. auto_single_measurement only accepted activity measurement [1] 1 structures\7RFT\7RFT_metadata.json point structures/7RFT/7rft_protein.pdb structures/7RFT/7rft_pocket.pdb structures/7RFT/7rft_ligand.pdb structures/7RFT/7rft_ligand.cif structures/7RFT/7rft_complex.pdb structures/7RFT/7rft_complex.cif 7RGD classic IMPDH1 human retinal variant IMPDH1(595) Na GTP; ATP; IMP; NAD+ "[""GTP""]" 1 IC50 IC50 = = 1104 μM 1104000.0 [] unit_conversion 2.95703092660682 success True biochemical_inhibition GTP inhibition; 1 μM protein, 1 mM ATP, 1 mM IMP, 300 μM NAD+, varying GTP. 4 Supplemental Table 3 reports IMPDH1(595) WT IC50 for GTP of 1104 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7RGD\7RGD_metadata.json point structures/7RGD/7rgd_protein.pdb structures/7RGD/7rgd_pocket.pdb structures/7RGD/7rgd_ligand.sdf structures/7RGD/7rgd_ligand.pdb structures/7RGD/7rgd_ligand.cif structures/7RGD/7rgd_complex.pdb structures/7RGD/7rgd_complex.cif 7RGK classic DfrA5 dihydrofolate reductase Na Na Na UCP1223 (5-(3-(7-(4-(aminomethyl)phenyl)benzo[d][1,3]dioxol-5-yl)but-1-yn-1-yl)-6-ethylpyrimidine-2,4-diamine) "[""560""]" 1 Ki Ki = = 16.76 ± 0.29 nM 16.76 [] unit_conversion 7.775725985705742 success True biochemical_inhibition Steady-state enzyme inhibition assay; Table 3. 11 Table 3 reports DfrA5 Ki for UCP1223 as 16.76 ± 0.29 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7RGK\7RGK_metadata.json point structures/7RGK/7rgk_protein.pdb structures/7RGK/7rgk_pocket.pdb structures/7RGK/7rgk_ligand.sdf structures/7RGK/7rgk_ligand.pdb structures/7RGK/7rgk_ligand.cif structures/7RGK/7rgk_complex.pdb structures/7RGK/7rgk_complex.cif 7RGQ classic IMPDH1 human retinal variant IMPDH1(546) Na GTP; ATP; IMP; NAD+ "[""GTP""]" 1 IC50 IC50 = = 903 μM 903000.0 [] unit_conversion 3.0443122496864943 success True biochemical_inhibition GTP inhibition; 1 μM protein, 1 mM ATP, 1 mM IMP, 300 μM NAD+, varying GTP. 4 Supplemental Table 3 reports IMPDH1(546) WT IC50 for GTP of 903 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7RGQ\7RGQ_metadata.json point structures/7RGQ/7rgq_protein.pdb structures/7RGQ/7rgq_pocket.pdb structures/7RGQ/7rgq_ligand.sdf structures/7RGQ/7rgq_ligand.pdb structures/7RGQ/7rgq_ligand.cif structures/7RGQ/7rgq_complex.pdb structures/7RGQ/7rgq_complex.cif 7RH7 classic Mycobacterial CIII2CIV2 supercomplex Mycobacterium smegmatis QcrB C-terminal 3xFLAG-tagged construct Na Telacebec (Q203); QTE "[""HUU""]" 1 IC50 IC50 = = 53 ± 19 nM 53.0 [] unit_conversion 7.275724130399211 success True biochemical_inhibition Titration of purified CIII2CIV2 (65 nM) with telacebec using 100 µM DMWH2; oxygen-reduction/DMWH2:O2 oxidoreductase activity assay with added bovine SOD. 7 Figure 2 caption states that titration of CIII2CIV2 with telacebec shows an IC50 of 53 ± 19 nM (± s.d., n = 3 independent titrations) with 100 µM DMWH2; page 8 specifies 65 nM CIII2CIV2. auto_single_measurement only accepted activity measurement [1] 1 structures\7RH7\7RH7_metadata.json point structures/7RH7/7rh7_protein.pdb structures/7RH7/7rh7_pocket.pdb structures/7RH7/7rh7_ligand.sdf structures/7RH7/7rh7_ligand.pdb structures/7RH7/7rh7_ligand.cif structures/7RH7/7rh7_complex.pdb structures/7RH7/7rh7_complex.cif 7RIE classic Plasmodium falciparum M17 aminopeptidase (Pfa-M17) Plasmodium falciparum Na Na MIPS2571 (compound 3) "[""5IF""]" 1 Ki Ki = = 18 ± 3 nM 18.0 [] unit_conversion 7.7447274948966935 success True biochemical_inhibition Morrison inhibition assay using recombinant purified Pfa-M17; compound 3 inhibition. 9 Figure 4 explicitly prints: “Ki(app) (Pfa-M17) = 18 ± 3 nM” for compound 3; the figure caption identifies 3 as a specific Pfa-M17 inhibitor. auto_single_measurement only accepted activity measurement [1] 1 structures\7RIE\7RIE_metadata.json point structures/7RIE/7rie_protein.pdb structures/7RIE/7rie_pocket.pdb structures/7RIE/7rie_ligand.sdf structures/7RIE/7rie_ligand.pdb structures/7RIE/7rie_ligand.cif structures/7RIE/7rie_complex.pdb structures/7RIE/7rie_complex.cif 7RJE classic Complex III2 Candida albicans Candida albicans strain CaLC5421 with both QCR2 alleles encoding a C-terminal His6-3xFLAG tag Na Inz-5 "[""ZL5""]" 1 IC50 IC50 = = 24 ± 3 nM 24.0 [] unit_conversion 7.619788758288394 success True biochemical_inhibition Purified CIII2; ubiquinol:cytochrome c oxidoreductase assay with decylubiquinol as electron donor; mean ± SD, n = 4 independent measurements. 5 “In UQH2:cyt c oxidoreductase assays, Inz-5 inhibits CIII2 with an IC50 of 24 ± 3 nM (mean ± SD, n = 4 measurements per inhibitor concentration).” auto_single_measurement only accepted activity measurement [1] 1 structures\7RJE\7RJE_metadata.json point structures/7RJE/7rje_protein.pdb structures/7RJE/7rje_pocket.pdb structures/7RJE/7rje_ligand.sdf structures/7RJE/7rje_ligand.pdb structures/7RJE/7rje_ligand.cif structures/7RJE/7rje_complex.pdb structures/7RJE/7rje_complex.cif 7RJK extended Bromodomain containing protein 3 (BRD3) human BRD3-BD1 Na acetylated hnRNPK peptide segment containing KacGGKac (Lys60 and Lys63) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 118 ± 8.3 µM 118000.0 [] unit_conversion 3.928117992693875 success True direct_binding Isothermal titration calorimetry of the acetylated hnRNPK peptide with the first bromodomain of BRD3. 10 Figure 5B reports BRD3-BD1 Kd = 118 ± 8.3 µM for hnRNPK peptide 4; Figure 6 maps BRD3-hnRNPK to PDB 7RJK. auto_single_measurement only accepted activity measurement [1] 1 structures\7RJK\7RJK_metadata.json point structures/7RJK/7rjk_protein.pdb structures/7RJK/7rjk_pocket.pdb structures/7RJK/7rjk_ligand.pdb structures/7RJK/7rjk_ligand.cif structures/7RJK/7rjk_complex.pdb structures/7RJK/7rjk_complex.cif 7RJL extended Bromodomain containing protein 3 (BRD3) human BRD3-BD1 Na acetylated SHMT peptide segment KacGVKac (Lys271 and Lys274) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 70.9 ± 23.0 µM 70900.0 [] unit_conversion 4.149353764816934 success True direct_binding Isothermal titration calorimetry of the acetylated SHMT peptide with the first bromodomain of BRD3. 10 Figure 5B reports BRD3-BD1 Kd = 70.9 ± 23.0 µM for SHMT peptide 8; Figure 6 identifies the BRD3-SHMT complex as PDB 7RJL. auto_single_measurement only accepted activity measurement [1] 1 structures\7RJL\7RJL_metadata.json point structures/7RJL/7rjl_protein.pdb structures/7RJL/7rjl_pocket.pdb structures/7RJL/7rjl_ligand.pdb structures/7RJL/7rjl_ligand.cif structures/7RJL/7rjl_complex.pdb structures/7RJL/7rjl_complex.cif 7RJM extended Bromodomain containing protein 3 (BRD3) human BRD3-BD1 Na acetylated ILF3 peptide KacGLLLKac (Lys100 and Lys105) "[""CHAIN:C""]" 1 Kd Kd = = 227 ± 71.0 µM 227000.0 [] unit_conversion 3.6439741428068775 success True direct_binding Isothermal titration calorimetry of the diacetylated ILF3 peptide with the first bromodomain of BRD3. 10 Figure 5B reports BRD3-BD1 Kd = 227 ± 71.0 µM for ILF3 peptide 10; Figure 7 maps BRD3-ILF3 to PDB 7RJM. auto_single_measurement only accepted activity measurement [1] 1 structures\7RJM\7RJM_metadata.json point structures/7RJM/7rjm_protein.pdb structures/7RJM/7rjm_pocket.pdb structures/7RJM/7rjm_ligand.pdb structures/7RJM/7rjm_ligand.cif structures/7RJM/7rjm_complex.pdb structures/7RJM/7rjm_complex.cif 7RJO extended Bromodomain containing protein 4 (BRD4) human BRD4-BD1 Na acetylated hnRNPK peptide segment containing KacGGKac (Lys60 and Lys63) "[""CHAIN:B""]" 1 Kd Kd = = 25.3 ± 9.4 µM 25300.0 [] unit_conversion 4.5968794788241825 success True direct_binding Isothermal titration calorimetry of the acetylated hnRNPK peptide with the first bromodomain of BRD4. 10 Figure 5B reports BRD4-BD1 Kd = 25.3 ± 9.4 µM for hnRNPK peptide 4; Figure 6 states that the BRD4-hnRNPK complex is PDB 7RJO. auto_single_measurement only accepted activity measurement [1] 1 structures\7RJO\7RJO_metadata.json point structures/7RJO/7rjo_protein.pdb structures/7RJO/7rjo_pocket.pdb structures/7RJO/7rjo_ligand.pdb structures/7RJO/7rjo_ligand.cif structures/7RJO/7rjo_complex.pdb structures/7RJO/7rjo_complex.cif 7RKK classic Nicotinamide N-Methyltransferase (NNMT) human Na Na II399 (PDB component 5R4) "[""5R4""]" 5 Kd Kd = = 336 ± 70 nM 336.0 [] unit_conversion 6.4736607226101555 success True direct_binding ITC direct binding of II399 to NNMT. 5 Figure 5E reports II399 binding to NNMT with Kd 336 ± 70 nM. auto_metric_priority unique highest-priority metric family: Kd [5] 5 structures\7RKK\7RKK_metadata.json point structures/7RKK/7rkk_protein.pdb structures/7RKK/7rkk_pocket.pdb structures/7RKK/7rkk_ligand.sdf structures/7RKK/7rkk_ligand.pdb structures/7RKK/7rkk_ligand.cif structures/7RKK/7rkk_complex.pdb structures/7RKK/7rkk_complex.cif 7RKL classic Nicotinamide N-Methyltransferase (NNMT) human Na Na II399 "[""5R4""]" 5 Kd Kd = = 336 ± 70 nM 336.0 [] unit_conversion 6.4736607226101555 success True direct_binding ITC experiment for NNMT binding affinity. 5 Figure 5E reports II399 binding to NNMT with “KD = 336 ± 70 nM.” auto_metric_priority unique highest-priority metric family: Kd [5] 5 structures\7RKL\7RKL_metadata.json point structures/7RKL/7rkl_protein.pdb structures/7RKL/7rkl_pocket.pdb structures/7RKL/7rkl_ligand.sdf structures/7RKL/7rkl_ligand.pdb structures/7RKL/7rkl_ligand.cif structures/7RKL/7rkl_complex.pdb structures/7RKL/7rkl_complex.cif 7RL2 classic Human cytochrome P450 2C9*8 (CYP2C9*8) genetic variant human CYP2C9 construct with residues 1-23 replaced by MAAKKT, Val490 mutated to Ile, and a His-tag or four-histidine purification tag R150H losartan "[""LSN""]" 1 Kd Kd = = 8.95 ± 0.97 μM 8950.0 [] unit_conversion 5.048176964684088 success True direct_binding Isothermal titration calorimetry (ITC) measurement of losartan binding to CYP2C9*8; average apparent dissociation constant. 8 “the average K_D for losartan binding to CYP2C9*8 was 8.95 ± 0.97 μM” auto_single_measurement only accepted activity measurement [1] 1 structures\7RL2\7RL2_metadata.json point structures/7RL2/7rl2_protein.pdb structures/7RL2/7rl2_pocket.pdb structures/7RL2/7rl2_ligand.sdf structures/7RL2/7rl2_ligand.pdb structures/7RL2/7rl2_ligand.cif structures/7RL2/7rl2_complex.pdb structures/7RL2/7rl2_complex.cif 7RLS classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na HL-3-68 "[""5YN""]" 3 Kd Kd = = 0.69±0.21 µM 690.0 [] unit_conversion 6.161150909262744 success True direct_binding Isothermal titration calorimetry (ITC). 15 Table 2 reports HL-3-68 ITC Kd 0.69±0.21 µM. auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\7RLS\7RLS_metadata.json point structures/7RLS/7rls_protein.pdb structures/7RLS/7rls_pocket.pdb structures/7RLS/7rls_ligand.sdf structures/7RLS/7rls_ligand.pdb structures/7RLS/7rls_ligand.cif structures/7RLS/7rls_complex.pdb structures/7RLS/7rls_complex.cif 7RLV extended Antibody 2F2 Mus musculus Fab fragment Na P. vivax CSP peptide GDRADGQPAGDRADGQPA "[""CHAIN:P"", ""CHAIN:Q"", ""CHAIN:R""]" 1 Kd Kd = = 17.1 nM 17.1 [] unit_conversion 7.767003889607846 success True direct_binding ITC measurement of 2F2 Fab binding to peptide 210-1. 6 Figure 3A reports K_D 17.1 nM for 2F2 Fab with peptide 210-1; Figure 3B gives the 210-1 sequence. auto_single_measurement only accepted activity measurement [1] 1 structures\7RLV\7RLV_metadata.json point structures/7RLV/7rlv_protein.pdb structures/7RLV/7rlv_pocket.pdb structures/7RLV/7rlv_ligand.pdb structures/7RLV/7rlv_ligand.cif structures/7RLV/7rlv_complex.pdb structures/7RLV/7rlv_complex.cif 7RLW extended Antibody 2F2 Mus musculus Fab fragment Na P. vivax CSP peptide GDRAAGQPAGDRAAGQPA "[""POLYMER_ENTITY:1""]" 1 Kd Kd = = 37.5 nM 37.5 [] unit_conversion 7.425968732272281 success True direct_binding ITC measurement of 2F2 Fab binding to peptide 210-2. 6 Figure 3A reports K_D 37.5 nM for 2F2 Fab with peptide 210-2; Figure 3B gives the 210-2 sequence. auto_single_measurement only accepted activity measurement [1] 1 structures\7RLW\7RLW_metadata.json point structures/7RLW/7rlw_protein.pdb structures/7RLW/7rlw_pocket.pdb structures/7RLW/7rlw_ligand.pdb structures/7RLW/7rlw_ligand.cif structures/7RLW/7rlw_complex.pdb structures/7RLW/7rlw_complex.cif 7RLX extended Antibody 2F2 Mus musculus Fab fragment Na P. vivax CSP peptide GDRADGQPAGDRAAGQPA "[""CHAIN:P""]" 1 Kd Kd = = 13.8 nM 13.8 [] unit_conversion 7.860120913598763 success True direct_binding ITC measurement of 2F2 Fab binding to peptide 210-3. 6 Figure 3A reports K_D 13.8 nM for 2F2 Fab with peptide 210-3; Figure 3B gives the 210-3 sequence. auto_single_measurement only accepted activity measurement [1] 1 structures\7RLX\7RLX_metadata.json point structures/7RLX/7rlx_protein.pdb structures/7RLX/7rlx_pocket.pdb structures/7RLX/7rlx_ligand.pdb structures/7RLX/7rlx_ligand.cif structures/7RLX/7rlx_complex.pdb structures/7RLX/7rlx_complex.cif 7RLZ extended Antibody 2F2 Mus musculus Fab fragment Na P. vivax CSP peptide GDRAAGQPAGNGAGGQAA "[""POLYMER_ENTITY:1""]" 1 Kd Kd = = 18.3 nM 18.3 [] unit_conversion 7.73754891026957 success True direct_binding ITC measurement of 2F2 Fab binding to peptide 210-5. 6 Figure 3A reports K_D 18.3 nM for 2F2 Fab with peptide 210-5; Figure 3B gives the 210-5 sequence. auto_single_measurement only accepted activity measurement [1] 1 structures\7RLZ\7RLZ_metadata.json point structures/7RLZ/7rlz_protein.pdb structures/7RLZ/7rlz_pocket.pdb structures/7RLZ/7rlz_ligand.pdb structures/7RLZ/7rlz_ligand.cif structures/7RLZ/7rlz_complex.pdb structures/7RLZ/7rlz_complex.cif 7RM0 extended Antibody 2E10.E9 Mus musculus Fab fragment Na P. vivax CSP peptide ANGAGNQPGANGAGNQPG "[""CHAIN:P"", ""CHAIN:Q"", ""CHAIN:R"", ""CHAIN:S""]" 1 Kd Kd = = 0.507 μM 507.0 [] unit_conversion 6.2949920406666635 success True direct_binding ITC measurement of 2E10.E9 Fab binding to peptide 247-4. 10 Figure 4A reports K_D 0.507 μM for 2E10.E9 Fab with peptide 247-4; Figure 4B gives the 247-4 sequence. auto_single_measurement only accepted activity measurement [1] 1 structures\7RM0\7RM0_metadata.json point structures/7RM0/7rm0_protein.pdb structures/7RM0/7rm0_pocket.pdb structures/7RM0/7rm0_ligand.pdb structures/7RM0/7rm0_ligand.cif structures/7RM0/7rm0_complex.pdb structures/7RM0/7rm0_complex.cif 7RM2 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na Mcule-CSR-494190-S1 "[""5YJ""]" 3 Kd Kd = = 1.32±0.29 µM 1320.0 [] unit_conversion 5.8794260687941495 success True direct_binding Isothermal titration calorimetry (ITC). 15 Table 2 reports Mcule-CSR-494190-S1 ITC Kd 1.32±0.29 µM. auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\7RM2\7RM2_metadata.json point structures/7RM2/7rm2_protein.pdb structures/7RM2/7rm2_pocket.pdb structures/7RM2/7rm2_ligand.sdf structures/7RM2/7rm2_ligand.pdb structures/7RM2/7rm2_ligand.cif structures/7RM2/7rm2_complex.pdb structures/7RM2/7rm2_complex.cif 7RM3 extended Antibody 2E10.E9 Mus musculus Fab fragment Na P. vivax CSP peptide ANGAGNQPGANGAGNQPGANGAGGQAA "[""CHAIN:P"", ""CHAIN:Q""]" 1 Kd Kd = = 1.52 μM 1520.0 [] unit_conversion 5.818156412055227 success True direct_binding ITC measurement of 2E10.E9 Fab binding to peptide 247-3. 10 Figure 4A reports K_D 1.52 μM for 2E10.E9 Fab with peptide 247-3; Figure 4B gives the 247-3 sequence. auto_single_measurement only accepted activity measurement [1] 1 structures\7RM3\7RM3_metadata.json point structures/7RM3/7rm3_protein.pdb structures/7RM3/7rm3_pocket.pdb structures/7RM3/7rm3_ligand.pdb structures/7RM3/7rm3_ligand.cif structures/7RM3/7rm3_complex.pdb structures/7RM3/7rm3_complex.cif 7RMB classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na HL-3-78 "[""5Z7""]" 1 IC50 IC50 = = 0.61 [0.37, 0.96] µM 610.0 [] unit_conversion 6.214670164989233 success True biochemical_inhibition In vitro Mpro FRET peptide-substrate inhibition assay. 10 Table 1 reports HL-3-78 IC50 0.61 [0.37, 0.96] µM and PDB ID 7RMB. auto_single_measurement only accepted activity measurement [1] 1 structures\7RMB\7RMB_metadata.json point structures/7RMB/7rmb_protein.pdb structures/7RMB/7rmb_pocket.pdb structures/7RMB/7rmb_ligand.sdf structures/7RMB/7rmb_ligand.pdb structures/7RMB/7rmb_ligand.cif structures/7RMB/7rmb_complex.pdb structures/7RMB/7rmb_complex.cif 7RMD classic BRD4 Homo sapiens First bromodomain of human BRD4 Na 1q (SJ1461); SJ001011461-1 "[""5Z0""]" 1 IC50 IC50 = = 0.0065 µM 6.5 [] unit_conversion 8.187086643357144 success True direct_binding TR-FRET assay against BRD4(BD1). 4 Table 1 reports compound 1q (SJ1461): IC50 0.0065 µM for BRD4 (BD1); the text maps 1q to PDB 7RMD. auto_single_measurement only accepted activity measurement [1] 1 structures\7RMD\7RMD_metadata.json point structures/7RMD/7rmd_protein.pdb structures/7RMD/7rmd_pocket.pdb structures/7RMD/7rmd_ligand.sdf structures/7RMD/7rmd_ligand.pdb structures/7RMD/7rmd_ligand.cif structures/7RMD/7rmd_complex.pdb structures/7RMD/7rmd_complex.cif 7RME classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na HL-3-52 "[""5Z3""]" 1 IC50 IC50 = = 1.4 [0.80, 2.3] µM 1400.0 [] unit_conversion 5.853871964321762 success True biochemical_inhibition In vitro Mpro FRET peptide-substrate inhibition assay. 10 Table 1 reports HL-3-52 IC50 1.4 [0.80, 2.3] µM and PDB ID 7RME. auto_single_measurement only accepted activity measurement [1] 1 structures\7RME\7RME_metadata.json point structures/7RME/7rme_protein.pdb structures/7RME/7rme_pocket.pdb structures/7RME/7rme_ligand.sdf structures/7RME/7rme_ligand.pdb structures/7RME/7rme_ligand.cif structures/7RME/7rme_complex.pdb structures/7RME/7rme_complex.cif 7RMT classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na HL-3-70 "[""5ZN""]" 1 IC50 IC50 = = 6.2 [4.8, 8.0] µM 6200.0 [] unit_conversion 5.207608310501746 success True biochemical_inhibition In vitro Mpro FRET peptide-substrate inhibition assay. 10 Table 1 reports HL-3-70 IC50 6.2 [4.8, 8.0] µM and PDB ID 7RMT. auto_single_measurement only accepted activity measurement [1] 1 structures\7RMT\7RMT_metadata.json point structures/7RMT/7rmt_protein.pdb structures/7RMT/7rmt_pocket.pdb structures/7RMT/7rmt_ligand.sdf structures/7RMT/7rmt_ligand.pdb structures/7RMT/7rmt_ligand.cif structures/7RMT/7rmt_complex.pdb structures/7RMT/7rmt_complex.cif 7RMW classic Bacillus subtilis PurR Bacillus subtilis Na Na ppGpp "[""G4P""]" 1 Kd Kd = = 4.4 ± 0.3 µM 4400.0 [] unit_conversion 5.356547323513812 success True direct_binding DRaCALA binding curve using purified untagged B. subtilis PurR and 32P-ppGpp; technical triplicates. 8 “Both ppGpp and pppGpp interacted with B. subtilis PurR similarly, with binding curves best fit with a Kd ~ 4.4 μM...” Figure 1H prints ppGpp Kd 4.4 ± 0.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7RMW\7RMW_metadata.json point structures/7RMW/7rmw_protein.pdb structures/7RMW/7rmw_pocket.pdb structures/7RMW/7rmw_ligand.sdf structures/7RMW/7rmw_ligand.pdb structures/7RMW/7rmw_ligand.cif structures/7RMW/7rmw_complex.pdb structures/7RMW/7rmw_complex.cif 7RMZ classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na HL-3-63 "[""5ZJ""]" 1 IC50 IC50 = = 6.4 [4.3, 9.5] µM 6400.0 [] unit_conversion 5.1938200260161125 success True biochemical_inhibition In vitro Mpro FRET peptide-substrate inhibition assay. 10 Table 1 reports HL-3-63 IC50 6.4 [4.3, 9.5] µM and PDB ID 7RMZ. auto_single_measurement only accepted activity measurement [1] 1 structures\7RMZ\7RMZ_metadata.json point structures/7RMZ/7rmz_protein.pdb structures/7RMZ/7rmz_pocket.pdb structures/7RMZ/7rmz_ligand.sdf structures/7RMZ/7rmz_ligand.pdb structures/7RMZ/7rmz_ligand.cif structures/7RMZ/7rmz_complex.pdb structures/7RMZ/7rmz_complex.cif 7RN2 classic BRD4 Homo sapiens First bromodomain of human BRD4 Na 1k; SJ001010551-2 "[""5ZQ""]" 1 IC50 IC50 = = 0.0405 µM 40.5 [] unit_conversion 7.392544976785332 success True direct_binding TR-FRET assay against BRD4(BD1). 4 Table 1 reports compound 1k: IC50 0.0405 µM for BRD4 (BD1); the text maps 1k to PDB 7RN2. auto_single_measurement only accepted activity measurement [1] 1 structures\7RN2\7RN2_metadata.json point structures/7RN2/7rn2_protein.pdb structures/7RN2/7rn2_pocket.pdb structures/7RN2/7rn2_ligand.sdf structures/7RN2/7rn2_ligand.pdb structures/7RN2/7rn2_ligand.cif structures/7RN2/7rn2_complex.pdb structures/7RN2/7rn2_complex.cif 7RN4 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na HL-3-69 "[""H69""]" 1 IC50 IC50 = = 8.8 [6.3, 13] µM 8800.0 [] unit_conversion 5.055517327849831 success True biochemical_inhibition In vitro Mpro FRET peptide-substrate inhibition assay. 10 Table 1 reports HL-3-69 IC50 8.8 [6.3, 13] µM and PDB ID 7RN4. auto_single_measurement only accepted activity measurement [1] 1 structures\7RN4\7RN4_metadata.json point structures/7RN4/7rn4_protein.pdb structures/7RN4/7rn4_pocket.pdb structures/7RN4/7rn4_ligand.sdf structures/7RN4/7rn4_ligand.pdb structures/7RN4/7rn4_ligand.cif structures/7RN4/7rn4_complex.pdb structures/7RN4/7rn4_complex.cif 7RN7 extended caspase-3 human Na Na Ac-VD(Aly)VD-CHO "[""CHAIN:F"", ""CHAIN:G""]" 1 pKi Ki = = 7.21 ± 0.08 unitless 61.65950018614822 [] p_metric_transform 7.21 success True biochemical_inhibition Fluorescence-based caspase inhibition assay; Table 2 reports pKi mean ± SD. 6 Table 2 lists AcVDRVD-CHO (21): Casp3 pKi 7.21 ± 0.08. The accession-code order on page 18 maps compound 21 to 7RN7. auto_single_measurement only accepted activity measurement [1] 1 structures\7RN7\7RN7_metadata.json point structures/7RN7/7rn7_protein.pdb structures/7RN7/7rn7_pocket.pdb structures/7RN7/7rn7_ligand.pdb structures/7RN7/7rn7_ligand.cif structures/7RN7/7rn7_complex.pdb structures/7RN7/7rn7_complex.cif 7RNA extended caspase-3 Na Na Na Ac-ITV(Dab)D-CHO (compound 23) "[""CHAIN:F"", ""CHAIN:G""]" 1 pKi Ki = = 5.04 ± 0.11 unitless 9120.108393559096 [] p_metric_transform 5.04 success True biochemical_inhibition Fluorometric enzyme-inhibition assay; Table 2 pKi value for Casp3. 5 Table 2 lists AcITV(Dab)D-CHO (23) with Casp3 pKi 5.04 ± 0.11. The paper states that compound 23 was among the Casp3 crystallographic complexes. auto_single_measurement only accepted activity measurement [1] 1 structures\7RNA\7RNA_metadata.json point structures/7RNA/7rna_protein.pdb structures/7RNA/7rna_pocket.pdb structures/7RNA/7rna_ligand.pdb structures/7RNA/7rna_ligand.cif structures/7RNA/7rna_complex.pdb structures/7RNA/7rna_complex.cif 7RND extended caspase-3 human Na Na Ac-VDPVD-CHO "[""CHAIN:F"", ""CHAIN:G""]" 1 pKi Ki = = 5.70 ± 0.04 unitless 1995.2623149688789 [] p_metric_transform 5.7 success True biochemical_inhibition Fluorescence-based caspase inhibition assay; Table 2 reports pKi mean ± SD. 6 Table 2 lists AcVDPVD-CHO (3): Casp3 pKi 5.70 ± 0.04. The accession-code order on page 18 maps compound 3 to 7RND. auto_single_measurement only accepted activity measurement [1] 1 structures\7RND\7RND_metadata.json point structures/7RND/7rnd_protein.pdb structures/7RND/7rnd_pocket.pdb structures/7RND/7rnd_ligand.pdb structures/7RND/7rnd_ligand.cif structures/7RND/7rnd_complex.pdb structures/7RND/7rnd_complex.cif 7RNG extended caspase-3 Na Na Na Ac-ITAKD-CHO (compound 36) "[""CHAIN:F"", ""CHAIN:G""]" 1 pKi Ki = = 5.92 ± 0.01 unitless 1202.2644346174131 [] p_metric_transform 5.92 success True biochemical_inhibition Fluorometric enzyme-inhibition assay; Table 2 pKi value for Casp3. 6 Table 2 lists AcITAKD-CHO (36) with Casp3 pKi 5.92 ± 0.01. auto_single_measurement only accepted activity measurement [1] 1 structures\7RNG\7RNG_metadata.json point structures/7RNG/7rng_protein.pdb structures/7RNG/7rng_pocket.pdb structures/7RNG/7rng_ligand.pdb structures/7RNG/7rng_ligand.cif structures/7RNG/7rng_complex.pdb structures/7RNG/7rng_complex.cif 7RNH classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na HL-3-45 "[""5ZW""]" 1 IC50 IC50 > > 20 µM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition In vitro Mpro FRET peptide-substrate inhibition assay. 10 Table 1 reports HL-3-45 IC50 > 20 µM and PDB ID 7RNH. auto_single_measurement only accepted activity measurement [1] 1 structures\7RNH\7RNH_metadata.json point structures/7RNH/7rnh_protein.pdb structures/7RNH/7rnh_pocket.pdb structures/7RNH/7rnh_ligand.sdf structures/7RNH/7rnh_ligand.pdb structures/7RNH/7rnh_ligand.cif structures/7RNH/7rnh_complex.pdb structures/7RNH/7rnh_complex.cif 7RNK classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na HL-3-71 "[""5ZT""]" 1 IC50 IC50 > > 20 µM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition In vitro Mpro FRET peptide-substrate inhibition assay. 11 Table 1 reports HL-3-71 IC50 > 20 µM and PDB ID 7RNK. auto_single_measurement only accepted activity measurement [1] 1 structures\7RNK\7RNK_metadata.json point structures/7RNK/7rnk_protein.pdb structures/7RNK/7rnk_pocket.pdb structures/7RNK/7rnk_ligand.sdf structures/7RNK/7rnk_ligand.pdb structures/7RNK/7rnk_ligand.cif structures/7RNK/7rnk_complex.pdb structures/7RNK/7rnk_complex.cif 7RNW extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na Se-1 "[""CHAIN:W"", ""CHAIN:X"", ""CHAIN:Y"", ""CHAIN:Z""]" 1 Ki Ki = = 17 ± 14 nM 17.0 [] unit_conversion 7.769551078621726 success True biochemical_inhibition Inhibitory activity against SARS-CoV-2 Mpro; Se-1 was assessed as a synthetic selenoether analogue of cyclic peptide 1. 6 “Se-1 displayed identical inhibitory activity against SARS-CoV-2 Mpro as 1 (Ki of Se-1 = 17 nM and 14 nM for 1)” (printed with ±14 nM and ±3 nM, respectively). auto_single_measurement only accepted activity measurement [1] 1 structures\7RNW\7RNW_metadata.json point structures/7RNW/7rnw_protein.pdb structures/7RNW/7rnw_pocket.pdb structures/7RNW/7rnw_ligand.pdb structures/7RNW/7rnw_ligand.cif structures/7RNW/7rnw_complex.pdb structures/7RNW/7rnw_complex.cif 7RNY classic human carbonic anhydrase II human Na Na 11g; 3-(3-benzyl-3-methylureido)benzenesulfonamide "[""65M""]" 1 Ki Ki = = 388.5 nM 388.5 [] unit_conversion 6.410608976863067 success True biochemical_inhibition Stopped-flow CO2 hydrase assay. 4 Table 1 reports compound 11g with a Ki of 388.5 nM against hCA II. Figure 2 explicitly identifies 11g as PDB 7RNY. auto_single_measurement only accepted activity measurement [1] 1 structures\7RNY\7RNY_metadata.json point structures/7RNY/7rny_protein.pdb structures/7RNY/7rny_pocket.pdb structures/7RNY/7rny_ligand.sdf structures/7RNY/7rny_ligand.pdb structures/7RNY/7rny_ligand.cif structures/7RNY/7rny_complex.pdb structures/7RNY/7rny_complex.cif 7RPY extended Sca5 Ruminococcus bromii Sca5X25-2, residues 491-734 Na maltotriose "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 595.8 ± 51.4 µM 595800.0 [] unit_conversion 3.2248995011209756 success True direct_binding ITC; Table 3 affinity determination for Sca5X25-2 with maltotriose. 7 Table 3 reports Sca5X25-2–maltotriose Kd = 595.8 ± 51.4 µM. The paper describes the maltotriose-bound Sca5X25-2 crystal structure. auto_single_measurement only accepted activity measurement [1] 1 structures\7RPY\7RPY_metadata.json point structures/7RPY/7rpy_protein.pdb structures/7RPY/7rpy_pocket.pdb structures/7RPY/7rpy_ligand.pdb structures/7RPY/7rpy_ligand.cif structures/7RPY/7rpy_complex.pdb structures/7RPY/7rpy_complex.cif 7RPZ classic KRAS Na Na G12D MRTX-1133 (compound 1) "[""6IC""]" 1 Kd Kd ~ ~ 0.0002 nM 0.0002 [] unit_conversion 12.698970004336019 success True direct_binding KRAS G12D K_D listed in the in-vitro profile. 6 Table 4 lists “KRAS G12D K_D (nM)” as “~0.0002”. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7RPZ\7RPZ_metadata.json point structures/7RPZ/7rpz_protein.pdb structures/7RPZ/7rpz_pocket.pdb structures/7RPZ/7rpz_ligand.sdf structures/7RPZ/7rpz_ligand.pdb structures/7RPZ/7rpz_ligand.cif structures/7RPZ/7rpz_complex.pdb structures/7RPZ/7rpz_complex.cif 7RT4 classic KRAS Na Na G12D compound 5B "[""7IZ""]" 1 Kd Kd = = 3.5 µM 3500.0 [] unit_conversion 5.455931955649724 success True direct_binding SPR assay with GDP-loaded KRAS G12D. 2 The text states that compound 5B “demonstrated a K_D of 3.5 µM in a KRAS G12D SPR assay with GDP-loaded KRAS G12D”; Figure 3 maps compound 5B/KRAS G12D/GDP to 7RT4. auto_single_measurement only accepted activity measurement [1] 1 structures\7RT4\7RT4_metadata.json point structures/7RT4/7rt4_protein.pdb structures/7RT4/7rt4_pocket.pdb structures/7RT4/7rt4_ligand.sdf structures/7RT4/7rt4_ligand.pdb structures/7RT4/7rt4_ligand.cif structures/7RT4/7rt4_complex.pdb structures/7RT4/7rt4_complex.cif 7RT5 classic KRAS Na Na G12D compound 36 "[""7OE""]" 1 IC50 IC50 < < 0.002 µM 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition HTRF KRAS G12D competitive biochemical assay. 5 Table 3 lists compound 36 with HTRF KRAS G12D IC50 <0.002 µM; Figure 9 maps compound 36/KRAS G12D/GDP to 7RT5. auto_single_measurement only accepted activity measurement [1] 1 structures\7RT5\7RT5_metadata.json point structures/7RT5/7rt5_protein.pdb structures/7RT5/7rt5_pocket.pdb structures/7RT5/7rt5_ligand.sdf structures/7RT5/7rt5_ligand.pdb structures/7RT5/7rt5_ligand.cif structures/7RT5/7rt5_complex.pdb structures/7RT5/7rt5_complex.cif 7RUN classic RET tyrosine kinase Na Na Na compound 10 "[""7QU""]" 1 IC50 IC50 = = 0.00085 µM 0.85 [] unit_conversion 9.070581074285707 success True biochemical_inhibition Biochemical HTRF-based assay using RET amino acids 658–1072. 3 Table 2 reports compound 10 enzymatic RET IC50 = 0.00085 µM; its footnote specifies a biochemical (aa 658–1072) HTRF-based assay. Figure 1 identifies compound 10 in the RET kinase crystal structure, and page 7 gives PDB accession 7RUN. auto_single_measurement only accepted activity measurement [1] 1 structures\7RUN\7RUN_metadata.json point structures/7RUN/7run_protein.pdb structures/7RUN/7run_pocket.pdb structures/7RUN/7run_ligand.sdf structures/7RUN/7run_ligand.pdb structures/7RUN/7run_ligand.cif structures/7RUN/7run_complex.pdb structures/7RUN/7run_complex.cif 7RW5 classic human methionine adenosyltransferase 2A (MAT2A) human full-length MAT2A with an N-terminal His6 tag and TEV protease cleavage site Na Compound 1 "[""7U2""]" 1 IC50 IC50 = = 7.2 µM 7200.0 [] unit_conversion 5.142667503568731 success True biochemical_inhibition Biochemical MAT2A enzyme-inhibition assay; reported as relative IC50 for activity inhibition, with SAM-product inhibition measured. 2 Figure 1 reports compound 1 with “Relative IC50 (7.2 μM)”; the caption identifies this as a biochemical assay readout of MAT2A inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7RW5\7RW5_metadata.json point structures/7RW5/7rw5_protein.pdb structures/7RW5/7rw5_pocket.pdb structures/7RW5/7rw5_ligand.sdf structures/7RW5/7rw5_ligand.pdb structures/7RW5/7rw5_ligand.cif structures/7RW5/7rw5_complex.pdb structures/7RW5/7rw5_complex.cif 7RW7 classic human methionine adenosyltransferase 2A (MAT2A) human full-length MAT2A with an N-terminal His6 tag and TEV protease cleavage site Na Compound 9 "[""7UB""]" 1 IC50 IC50 = = 0.69 µM 690.0 [] unit_conversion 6.161150909262744 success True biochemical_inhibition Biochemical MAT2A enzyme-inhibition assay; relative IC50 from Table 1. 5 Table 1, “Biochemical Activity of Analogues of 3,” reports compound 9 with relative IC50 0.69 μM. Figure 3 identifies the co-crystal of MAT2A with spirocyclic pyrazole 9 as PDB 7RW7. auto_single_measurement only accepted activity measurement [1] 1 structures\7RW7\7RW7_metadata.json point structures/7RW7/7rw7_protein.pdb structures/7RW7/7rw7_pocket.pdb structures/7RW7/7rw7_ligand.sdf structures/7RW7/7rw7_ligand.pdb structures/7RW7/7rw7_ligand.cif structures/7RW7/7rw7_complex.pdb structures/7RW7/7rw7_complex.cif 7RWH classic human methionine adenosyltransferase 2A (MAT2A) human full-length MAT2A with an N-terminal His6 tag and TEV protease cleavage site Na AGI-41998 "[""7UI""]" 1 IC50 IC50 = = 0.022 (±0.0031) µM 22.0 [] unit_conversion 7.657577319177793 success True biochemical_inhibition Biochemical MAT2A enzyme-inhibition assay; relative IC50, reported as an average of eight individual test occasions, each run in duplicate (±SD). 7 Table 2 reports AGI-41998 with relative IC50 0.022 (±0.0031) μM. The accession list maps AGI-41998 to PDB 7RWH. auto_single_measurement only accepted activity measurement [1] 1 structures\7RWH\7RWH_metadata.json point structures/7RWH/7rwh_protein.pdb structures/7RWH/7rwh_pocket.pdb structures/7RWH/7rwh_ligand.sdf structures/7RWH/7rwh_ligand.pdb structures/7RWH/7rwh_ligand.cif structures/7RWH/7rwh_complex.pdb structures/7RWH/7rwh_complex.cif 7RWN classic BPTF Na Na Na compound 11; 4-chloro-5-{4-[(dimethylamino)methyl]anilino}-2-methylpyridazin-3(2H)-one "[""7WE""]" 1 IC50 IC50 = = 0.31 μM 310.0 [] unit_conversion 6.508638306165727 success True biochemical_inhibition BPTF AlphaScreen competitive binding assay; Table 3. 6 Table 3 reports compound 11 with BPTF AlphaScreen IC50 = 0.31 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7RWN\7RWN_metadata.json point structures/7RWN/7rwn_protein.pdb structures/7RWN/7rwn_pocket.pdb structures/7RWN/7rwn_ligand.sdf structures/7RWN/7rwn_ligand.pdb structures/7RWN/7rwn_ligand.cif structures/7RWN/7rwn_complex.pdb structures/7RWN/7rwn_complex.cif 7RWO classic BPTF Na Na Na compound 13; 4-chloro-2-methyl-5-[(1,2,3,4-tetrahydroisoquinolin-7-yl)amino]pyridazin-3(2H)-one "[""7WN""]" 1 IC50 IC50 = = 0.37 μM 370.0 [] unit_conversion 6.431798275933005 success True biochemical_inhibition BPTF AlphaScreen competitive binding assay; Table 3. 6 Table 3 reports compound 13 with BPTF AlphaScreen IC50 = 0.37 μM; Figure 3 maps compound 13 to PDB 7RWO. auto_single_measurement only accepted activity measurement [1] 1 structures\7RWO\7RWO_metadata.json point structures/7RWO/7rwo_protein.pdb structures/7RWO/7rwo_pocket.pdb structures/7RWO/7rwo_ligand.sdf structures/7RWO/7rwo_ligand.pdb structures/7RWO/7rwo_ligand.cif structures/7RWO/7rwo_complex.pdb structures/7RWO/7rwo_complex.cif 7RWP classic BPTF Na Na Na compound 10; 5-[4-(aminomethyl)anilino]-4-chloro-2-methylpyridazin-3(2H)-one "[""7WZ""]" 1 IC50 IC50 = = 0.29 ± 0.08 μM 290.0 [] unit_conversion 6.537602002101044 success True biochemical_inhibition BPTF AlphaScreen competitive binding assay; Table 3. 6 Table 3 reports compound 10 with BPTF AlphaScreen IC50 = 0.29 ± 0.08 μM; Figure 3 maps compound 10 to PDB 7RWP. auto_single_measurement only accepted activity measurement [1] 1 structures\7RWP\7RWP_metadata.json point structures/7RWP/7rwp_protein.pdb structures/7RWP/7rwp_pocket.pdb structures/7RWP/7rwp_ligand.sdf structures/7RWP/7rwp_ligand.pdb structures/7RWP/7rwp_ligand.cif structures/7RWP/7rwp_complex.pdb structures/7RWP/7rwp_complex.cif 7RWQ classic BPTF Na Na Na compound 12; 4-chloro-2-methyl-5-[(1,2,3,4-tetrahydroisoquinolin-6-yl)amino]pyridazin-3(2H)-one "[""7XE""]" 1 IC50 IC50 = = 0.25 μM 250.0 [] unit_conversion 6.6020599913279625 success True biochemical_inhibition BPTF AlphaScreen competitive binding assay; Table 3. 6 Table 3 reports compound 12 with BPTF AlphaScreen IC50 = 0.25 μM; Figure 3 maps compound 12 to PDB 7RWQ. auto_single_measurement only accepted activity measurement [1] 1 structures\7RWQ\7RWQ_metadata.json point structures/7RWQ/7rwq_protein.pdb structures/7RWQ/7rwq_pocket.pdb structures/7RWQ/7rwq_ligand.sdf structures/7RWQ/7rwq_ligand.pdb structures/7RWQ/7rwq_ligand.cif structures/7RWQ/7rwq_complex.pdb structures/7RWQ/7rwq_complex.cif 7RXQ extended junctophilin-2 (JPH2) Homo sapiens (JPH2); Oryctolagus cuniculus (CaV1.1 peptide) JPH2 residues 1-161 and 275-437, with the joining region removed, in complex with a synthetic minimal CaV1.1 peptide Na CaV1.1 peptide, residues 1594-1609 "[""CHAIN:B""]" 1 Kd Kd = = 1.6 µM 1600.0 [] unit_conversion 5.795880017344075 success True direct_binding Representative ITC titration of 300 µM CaV1.1 peptide into 30 µM JPH2 (residues 1-161, 275-437). 4 Fig. 2 caption: “Representative ITC titration of 300 µM CaV1.1 peptide into 30 µM JPH2 (1 to 161, 275 to 437) (Kd = 1.6 µM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7RXQ\7RXQ_metadata.json point structures/7RXQ/7rxq_protein.pdb structures/7RXQ/7rxq_pocket.pdb structures/7RXQ/7rxq_ligand.pdb structures/7RXQ/7rxq_ligand.cif structures/7RXQ/7rxq_complex.pdb structures/7RXQ/7rxq_complex.cif 7RXS classic BRD4 Na Na Na compound 20; 2-[(3S)-3-{5-[2-(3,5-dimethylphenoxy)pyrimidin-4-yl]-4-(4-iodophenyl)-1H-imidazol-1-yl}pyrrolidin-1-yl]ethan-1-amine "[""7ZT""]" 1 IC50 IC50 = = 0.10 ± 0.01 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition Fluorescence anisotropy 4 Table 4 reports BRD4 D1 IC50 by fluorescence anisotropy for compound 20; Figure 3 maps compound 20 to PDB 7RXS. auto_single_measurement only accepted activity measurement [1] 1 structures\7RXS\7RXS_metadata.json point structures/7RXS/7rxs_protein.pdb structures/7RXS/7rxs_pocket.pdb structures/7RXS/7rxs_ligand.sdf structures/7RXS/7rxs_ligand.pdb structures/7RXS/7rxs_ligand.cif structures/7RXS/7rxs_complex.pdb structures/7RXS/7rxs_complex.cif 7RXT classic BRD4 Na Na Na compound 22; 2-[(3R)-3-{5-[2-(3,5-dimethylphenoxy)pyrimidin-4-yl]-4-(4-iodophenyl)-1H-imidazol-1-yl}pyrrolidin-1-yl]ethan-1-amine "[""7ZK""]" 1 IC50 IC50 = = 0.26 ± 0.01 µM 260.0 [] unit_conversion 6.585026652029182 success True biochemical_inhibition Fluorescence anisotropy 4 Table 4 reports BRD4 D1 IC50 by fluorescence anisotropy for compound 22; Figure 3 maps compound 22 to PDB 7RXT. auto_single_measurement only accepted activity measurement [1] 1 structures\7RXT\7RXT_metadata.json point structures/7RXT/7rxt_protein.pdb structures/7RXT/7rxt_pocket.pdb structures/7RXT/7rxt_ligand.sdf structures/7RXT/7rxt_ligand.pdb structures/7RXT/7rxt_ligand.cif structures/7RXT/7rxt_complex.pdb structures/7RXT/7rxt_complex.cif 7RZD extended HLA-B*07:02 Homo sapiens HLA-B*0702 fragment residues 25-299 with beta2-microglobulin fragment residues 21-119 Na MLL_747-755 (EPRPSHSM) "[""CHAIN:C""]" 1 Kd Kd = = 27.0 nM 27.0 [] unit_conversion 7.568636235841012 success True direct_binding Peptide–HLA-B*07:02 binding determined by Alpha assay. 4 Fig. 2b lists MLL (EPRPSHSM) K_D = 27.0 nM; the caption states peptide K_D values were determined using Alpha assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7RZD\7RZD_metadata.json point structures/7RZD/7rzd_protein.pdb structures/7RZD/7rzd_pocket.pdb structures/7RZD/7rzd_ligand.pdb structures/7RZD/7rzd_ligand.cif structures/7RZD/7rzd_complex.pdb structures/7RZD/7rzd_complex.cif 7RZJ extended HLA-B*07:02 Homo sapiens HLA-B*0702 fragment residues 25-299 with beta2-microglobulin fragment residues 21-119 Na pMLL_747-755 (EPR(pS)PSHSM) "[""CHAIN:E""]" 1 Kd Kd = = 56.7 nM 56.7 [] unit_conversion 7.246416941107094 success True direct_binding Peptide–HLA-B*07:02 binding determined by Alpha assay. 4 Fig. 2b lists pMLL (EPR(pS)PSHSM) K_D = 56.7 nM; the caption states peptide K_D values were determined using Alpha assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7RZJ\7RZJ_metadata.json point structures/7RZJ/7rzj_protein.pdb structures/7RZJ/7rzj_pocket.pdb structures/7RZJ/7rzj_ligand.pdb structures/7RZJ/7rzj_ligand.cif structures/7RZJ/7rzj_complex.pdb structures/7RZJ/7rzj_complex.cif 7S04 classic 1-deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) Acinetobacter baumannii Recombinant A. baumannii IspC with an N-terminal His6-tag Na FR900098 "[""F98""]" 1 IC50 IC50 = = 23.9 (21.4–26.7) nM 23.9 [] unit_conversion 7.621602099051862 success True biochemical_inhibition Purified recombinant AbIspC enzyme inhibition assay; FR900098 IC50 determined from dose-response inhibition of DXP-dependent NADPH oxidation, with inhibitor preincubated with enzyme before substrate addition. 4 Table 2 reports AbIspC IC50 for FR900098 as 23.9 (21.4–26.7) nM; Figure 5 independently displays the same AbIspC/FR900098 dose-response result. auto_single_measurement only accepted activity measurement [1] 1 structures\7S04\7S04_metadata.json point structures/7S04/7s04_protein.pdb structures/7S04/7s04_pocket.pdb structures/7S04/7s04_ligand.sdf structures/7S04/7s04_ligand.pdb structures/7S04/7s04_ligand.cif structures/7S04/7s04_complex.pdb structures/7S04/7s04_complex.cif 7S0U extended PRMT5/MEP50 Na Na Na F1 (4-(aminomethyl)phthalazin-1(2H)-one) "[""81X""]" 1 Kd Kd = = 10 μM 10000.0 [] unit_conversion 5.0 success True direct_binding SPR, PRMT5/MEP50 preincubated with 20 μM MTA. 9 Table 3 reports F1 K_D = 10 μM with MTA; the table footnote specifies a PRMT5/MEP50 SPR assay with 20 μM MTA preincubation. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7S0U\7S0U_metadata.json point structures/7S0U/7s0u_protein.pdb structures/7S0U/7s0u_pocket.pdb structures/7S0U/7s0u_ligand.pdb structures/7S0U/7s0u_ligand.cif structures/7S0U/7s0u_complex.pdb structures/7S0U/7s0u_complex.cif 7S1N classic JNK3 human Na Na inhibitor 29 "[""86C""]" 1 IC50 IC50 = = 0.005 µM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition Biochemical inhibition assay; Table 2 reports JNK3 IC50 values for lead compounds. 4 Table 2 lists compound 29 with biochemical JNK3 inhibition IC50 = 0.005 µM. Figure 4 identifies inhibitor 29 in human JNK3 as PDB ID 7S1N. auto_single_measurement only accepted activity measurement [1] 1 structures\7S1N\7S1N_metadata.json point structures/7S1N/7s1n_protein.pdb structures/7S1N/7s1n_pocket.pdb structures/7S1N/7s1n_ligand.sdf structures/7S1N/7s1n_ligand.pdb structures/7S1N/7s1n_ligand.cif structures/7S1N/7s1n_complex.pdb structures/7S1N/7s1n_complex.cif 7S1Q classic PRMT5/MEP50 Na Na Na compound 9 "[""84W""]" 1 Kd Kd = = 5 nM 5.0 [] unit_conversion 8.301029995663981 success True direct_binding SPR, PRMT5/MEP50 preincubated with 20 μM MTA. 9 Table 3 reports compound 9 K_D = 5 nM with MTA; its footnote specifies PRMT5/MEP50 SPR with 20 μM MTA preincubation. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7S1Q\7S1Q_metadata.json point structures/7S1Q/7s1q_protein.pdb structures/7S1Q/7s1q_pocket.pdb structures/7S1Q/7s1q_ligand.sdf structures/7S1Q/7s1q_ligand.pdb structures/7S1Q/7s1q_ligand.cif structures/7S1Q/7s1q_complex.pdb structures/7S1Q/7s1q_complex.cif 7S1S classic PRMT5/MEP50 Na Na Na MRTX1719 "[""85K""]" 1 Kd Kd = = 0.14 pM 0.00014000000000000001 [] unit_conversion 12.853871964321762 success True direct_binding Chaser SPR, PRMT5/MEP50 preincubated with 20 μM MTA. 9 Table 3 reports MRTX-1719 K_D = 0.14 pM with MTA; its footnote specifies a PRMT5/MEP50 chaser SPR assay with 20 μM MTA preincubation. auto_single_measurement only accepted activity measurement [1] 1 structures\7S1S\7S1S_metadata.json point structures/7S1S/7s1s_protein.pdb structures/7S1S/7s1s_pocket.pdb structures/7S1S/7s1s_ligand.sdf structures/7S1S/7s1s_ligand.pdb structures/7S1S/7s1s_ligand.cif structures/7S1S/7s1s_complex.pdb structures/7S1S/7s1s_complex.cif 7S25 classic ROCK1 Homo sapiens (human) Residues 6-405 with an N-terminal TEV-cleavable His tag; expressed in insect cells Na compound 1 "[""86G""]" 1 Ki Ki = = 0.038 ± 0.001 µM 38.0 [] unit_conversion 7.42021640338319 success True biochemical_inhibition ROCK1 biochemical inhibition assay. 0 The supplement maps 7S25 to compound 1 and reports ROCK1 Ki 0.038 ± 0.001 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7S25\7S25_metadata.json point structures/7S25/7s25_protein.pdb structures/7S25/7s25_pocket.pdb structures/7S25/7s25_ligand.sdf structures/7S25/7s25_ligand.pdb structures/7S25/7s25_ligand.cif structures/7S25/7s25_complex.pdb structures/7S25/7s25_complex.cif 7S26 classic ROCK1 Homo sapiens (human) Residues 6-405 with an N-terminal TEV-cleavable His tag; expressed in insect cells Na compound 22 "[""86K""]" 1 Ki Ki = = 0.097 ± 0.004 µM 97.0 [] unit_conversion 7.013228265733755 success True biochemical_inhibition ROCK1 biochemical inhibition assay. 0 The supplement maps 7S26 to compound 22 and reports ROCK1 Ki 0.097 ± 0.004 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7S26\7S26_metadata.json point structures/7S26/7s26_protein.pdb structures/7S26/7s26_pocket.pdb structures/7S26/7s26_ligand.sdf structures/7S26/7s26_ligand.pdb structures/7S26/7s26_ligand.cif structures/7S26/7s26_complex.pdb structures/7S26/7s26_complex.cif 7S3K classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 12; Z1530718726 "[""Z26""]" 1 IC50 IC50 = = 1.8 ± 0.8 µM 1800.0 [] unit_conversion 5.7447274948966935 success True biochemical_inhibition FRET enzymatic inhibition assay; Table 2 reports the inhibitory concentration for compound 12. 3 Table 2 lists compound 12 with IC50 = 1.8 ± 0.8 µM; the text identifies compound 12 as co-crystallized with Mpro and PDB 7S3K. auto_single_measurement only accepted activity measurement [1] 1 structures\7S3K\7S3K_metadata.json point structures/7S3K/7s3k_protein.pdb structures/7S3K/7s3k_pocket.pdb structures/7S3K/7s3k_ligand.sdf structures/7S3K/7s3k_ligand.pdb structures/7S3K/7s3k_ligand.cif structures/7S3K/7s3k_complex.pdb structures/7S3K/7s3k_complex.cif 7S3P classic BRD3 human Na Na Physachenolide C (PCC) "[""8L6""]" 2 Kd Kd = = 149 ± 17 nM 149.0 [] unit_conversion 6.826813731587726 success True direct_binding Microscale thermophoresis (MST) direct binding of PCC to BRD3-BD2. 2 Figure 1 caption states: PCC binds BRD3-BD2 by MST with a Kd of 149 ± 17 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7S3P\7S3P_metadata.json point structures/7S3P/7s3p_protein.pdb structures/7S3P/7s3p_pocket.pdb structures/7S3P/7s3p_ligand.sdf structures/7S3P/7s3p_ligand.pdb structures/7S3P/7s3p_ligand.cif structures/7S3P/7s3p_complex.pdb structures/7S3P/7s3p_complex.cif 7S3S classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 21; Z1530724813 "[""860""]" 1 IC50 IC50 = = 1.6 ± 0.7 µM 1600.0 [] unit_conversion 5.795880017344075 success True biochemical_inhibition FRET enzymatic inhibition assay; Table 2 reports the inhibitory concentration for compound 21. 3 Table 2 lists compound 21 with IC50 = 1.6 ± 0.7 µM; the text identifies compound 21 as co-crystallized with Mpro and PDB 7S3S. auto_single_measurement only accepted activity measurement [1] 1 structures\7S3S\7S3S_metadata.json point structures/7S3S/7s3s_protein.pdb structures/7S3S/7s3s_pocket.pdb structures/7S3S/7s3s_ligand.sdf structures/7S3S/7s3s_ligand.pdb structures/7S3S/7s3s_ligand.cif structures/7S3S/7s3s_complex.pdb structures/7S3S/7s3s_complex.cif 7S48 extended p21-activated kinase 4 (PAK4) Na PAK4 catalytic domain (PAK4cat), residues 300-589, co-crystallized with integrin beta5 760-770 peptide; modeled integrin residues 762-768 wild-type (WT) Integrin beta5 760-770 peptide (ERSRARYEMAS) "[""CHAIN:B""]" 1 IC50 IC50 = = 160 ± 40 µM 160000.0 [] unit_conversion 3.795880017344075 success True biochemical_inhibition In-vitro kinase assay measuring inhibition of PAK4-cat phosphorylation of a LIMK1 10mer substrate by the β5 11mer. 5 The paper reports that the short 11mer integrin β5 peptide inhibits with an IC50 of 160 ± 40 µM; its sequence is identified as ERSRARYEMAS. auto_single_measurement only accepted activity measurement [1] 1 structures\7S48\7S48_metadata.json point structures/7S48/7s48_protein.pdb structures/7S48/7s48_pocket.pdb structures/7S48/7s48_ligand.pdb structures/7S48/7s48_ligand.cif structures/7S48/7s48_complex.pdb structures/7S48/7s48_complex.cif 7S4B classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 19; Z1530724963 "[""87H""]" 1 IC50 IC50 = = 2.1 ± 1.0 µM 2100.0 [] unit_conversion 5.6777807052660805 success True biochemical_inhibition FRET enzymatic inhibition assay; Table 2 reports the inhibitory concentration for compound 19. 3 Table 2 lists compound 19 with IC50 = 2.1 ± 1.0 µM; the text identifies compound 19 as co-crystallized with Mpro and PDB 7S4B. auto_single_measurement only accepted activity measurement [1] 1 structures\7S4B\7S4B_metadata.json point structures/7S4B/7s4b_protein.pdb structures/7S4B/7s4b_pocket.pdb structures/7S4B/7s4b_ligand.sdf structures/7S4B/7s4b_ligand.pdb structures/7S4B/7s4b_ligand.cif structures/7S4B/7s4b_complex.pdb structures/7S4B/7s4b_complex.cif 7S79 extended HLA-B*07:02 Homo sapiens HLA-B*0702 fragment residues 25-299 with beta2-microglobulin fragment residues 21-119 Na E7P-MLL_747-755 (EPR(E7P)PSHSM) "[""CHAIN:E""]" 1 Kd Kd = = 33.9 nM 33.9 [] unit_conversion 7.4698003017969175 success True direct_binding Peptide–HLA-B*07:02 binding determined by Alpha assay. 4 Fig. 2b lists E7P-MLL (EPR(E7P)PSHSM) K_D = 33.9 nM; the caption states peptide K_D values were determined using Alpha assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7S79\7S79_metadata.json point structures/7S79/7s79_protein.pdb structures/7S79/7s79_pocket.pdb structures/7S79/7s79_ligand.pdb structures/7S79/7s79_ligand.cif structures/7S79/7s79_complex.pdb structures/7S79/7s79_complex.cif 7S7D extended HLA-B*07:02 Homo sapiens HLA-B*0702 fragment residues 25-299 with beta2-microglobulin fragment residues 21-119 Na OSE-MLL_747-755 (EPR(OSE)PSHSM) "[""CHAIN:E""]" 1 Kd Kd = = 26.2 nM 26.2 [] unit_conversion 7.581698708680254 success True direct_binding Peptide–HLA-B*07:02 binding determined by Alpha assay. 4 Fig. 2b lists OSE-MLL (EPR(OSE)PSHSM) K_D = 26.2 nM; the caption states peptide K_D values were determined using Alpha assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7S7D\7S7D_metadata.json point structures/7S7D/7s7d_protein.pdb structures/7S7D/7s7d_pocket.pdb structures/7S7D/7s7d_ligand.pdb structures/7S7D/7s7d_ligand.cif structures/7S7D/7s7d_complex.pdb structures/7S7D/7s7d_complex.cif 7S7E extended HLA-B*07:02 Homo sapiens HLA-B*0702 fragment residues 25-299 with beta2-microglobulin fragment residues 21-119 Na DOT1L_998-1006 (LPASPAHQL) "[""CHAIN:C""]" 1 Kd Kd = = 54.3 nM 54.3 [] unit_conversion 7.265200170411153 success True direct_binding Peptide–HLA-B*07:02 binding determined by Alpha assay. 4 Fig. 2b lists DOT1L (LPASPAHQL) K_D = 54.3 nM; the caption states peptide K_D values were determined using Alpha assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7S7E\7S7E_metadata.json point structures/7S7E/7s7e_protein.pdb structures/7S7E/7s7e_pocket.pdb structures/7S7E/7s7e_ligand.pdb structures/7S7E/7s7e_ligand.cif structures/7S7E/7s7e_complex.pdb structures/7S7E/7s7e_complex.cif 7S7F extended HLA-B*07:02 Homo sapiens HLA-B*0702 fragment residues 25-299 with beta2-microglobulin fragment residues 21-119 Na pDOT1L_998-1006 (LPA(pS)PAHQL) "[""CHAIN:C""]" 1 Kd Kd = = 309.2 nM 309.2 [] unit_conversion 6.5097605147537125 success True direct_binding Peptide–HLA-B*07:02 binding determined by Alpha assay. 4 Fig. 2b lists pDOT1L (LPA(pS)PAHQL) K_D = 309.2 nM; the caption states peptide K_D values were determined using Alpha assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7S7F\7S7F_metadata.json point structures/7S7F/7s7f_protein.pdb structures/7S7F/7s7f_pocket.pdb structures/7S7F/7s7f_ligand.pdb structures/7S7F/7s7f_ligand.cif structures/7S7F/7s7f_complex.pdb structures/7S7F/7s7f_complex.cif 7S84 classic Cyclin-dependent kinase 2 (CDK2) Homo sapiens CDK2 residues 1-298, expressed with an N-terminal GST tag that was removed during purification Na TW8972 "[""8IL""]" 1 Kd Kd = = 2300 nM 2300.0 [] unit_conversion 5.638272163982407 success True direct_binding ITC binding of purified CDK2 to compound 2. 3 Table 1, headed “as determined by ITC,” reports compound 2 KD = 2300 nM; page 2 identifies the compound-2 structure as PDB 7S84. auto_single_measurement only accepted activity measurement [1] 1 structures\7S84\7S84_metadata.json point structures/7S84/7s84_protein.pdb structures/7S84/7s84_pocket.pdb structures/7S84/7s84_ligand.sdf structures/7S84/7s84_ligand.pdb structures/7S84/7s84_ligand.cif structures/7S84/7s84_complex.pdb structures/7S84/7s84_complex.cif 7S8A extended HLA-B*07:02 Homo sapiens HLA-B*0702 fragment residues 25-299 with beta2-microglobulin fragment residues 21-119 Na pMLL_747-755 (EPR(pS)PSHSM) "[""CHAIN:C""]" 1 Kd Kd = = 56.7 nM 56.7 [] unit_conversion 7.246416941107094 success True direct_binding Peptide–HLA-B*07:02 binding determined by Alpha assay. 4 Fig. 2b lists pMLL (EPR(pS)PSHSM) K_D = 56.7 nM; the caption states peptide K_D values were determined using Alpha assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7S8A\7S8A_metadata.json point structures/7S8A/7s8a_protein.pdb structures/7S8A/7s8a_pocket.pdb structures/7S8A/7s8a_ligand.pdb structures/7S8A/7s8a_ligand.cif structures/7S8A/7s8a_complex.pdb structures/7S8A/7s8a_complex.cif 7S8E extended HLA-B*07:02 Homo sapiens HLA-B*0702 fragment residues 25-299 with beta2-microglobulin fragment residues 21-119 Na pMLL_747-755 (EPR(pS)PSHSM) "[""CHAIN:E""]" 1 Kd Kd = = 56.7 nM 56.7 [] unit_conversion 7.246416941107094 success True direct_binding Peptide–HLA-B*07:02 binding determined by Alpha assay; glycerol is not the measured ligand. 4 Fig. 2b lists pMLL (EPR(pS)PSHSM) K_D = 56.7 nM; the caption states peptide K_D values were determined using Alpha assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7S8E\7S8E_metadata.json point structures/7S8E/7s8e_protein.pdb structures/7S8E/7s8e_pocket.pdb structures/7S8E/7s8e_ligand.pdb structures/7S8E/7s8e_ligand.cif structures/7S8E/7s8e_complex.pdb structures/7S8E/7s8e_complex.cif 7SAN classic human HGPRT human Na Na (S,S)-48; (4S,7S)-7-hydroxy-4-((guanin-9-yl)methyl)-2,5-dioxaheptan-1,7-diphosphonate "[""8QI""]" 1 Ki Ki = = 0.07 ± 0.03 μM 70.0 [] unit_conversion 7.154901959985743 success True biochemical_inhibition Table 3 enzyme-inhibition assay of stereo-defined acyclic nucleoside phosphonates/bisphosphonates against 6-oxopurine PRTs. 8 Table 3 reports human HGPRT Ki = 0.07 ± 0.03 μM for purified hydroxyl isomer (S,S)-48; Figure 6 maps the human HGPRT·(S,S)-48 complex to PDB 7SAN. auto_single_measurement only accepted activity measurement [1] 1 structures\7SAN\7SAN_metadata.json point structures/7SAN/7san_protein.pdb structures/7SAN/7san_pocket.pdb structures/7SAN/7san_ligand.sdf structures/7SAN/7san_ligand.pdb structures/7SAN/7san_ligand.cif structures/7SAN/7san_complex.pdb structures/7SAN/7san_complex.cif 7SB7 classic TbrHGPRT1 Trypanosoma brucei Na Na (S,S)-48; (4S,7S)-7-hydroxy-4-((guanin-9-yl)methyl)-2,5-dioxaheptan-1,7-diphosphonate "[""8QI""]" 1 Ki Ki = = 0.002 ± 0.001 μM 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition Table 3 enzyme-inhibition assay of stereo-defined acyclic nucleoside phosphonates/bisphosphonates against 6-oxopurine PRTs. 8 Table 3 reports TbrHGPRT1 Ki = 0.002 ± 0.001 μM for purified hydroxyl isomer (S,S)-48; Figure 6 maps the TbrHGPRT1·(S,S)-48 complex to PDB 7SB7. auto_single_measurement only accepted activity measurement [1] 1 structures\7SB7\7SB7_metadata.json point structures/7SB7/7sb7_protein.pdb structures/7SB7/7sb7_pocket.pdb structures/7SB7/7sb7_ligand.sdf structures/7SB7/7sb7_ligand.pdb structures/7SB7/7sb7_ligand.cif structures/7SB7/7sb7_complex.pdb structures/7SB7/7sb7_complex.cif 7SBF classic mu-opioid receptor (muOR) Na muOR-Gi-scFv16 complex Na PZM21 "[""8QY""]" 1 Ki Ki = = 31 nM 31.0 [] unit_conversion 7.508638306165727 success True direct_binding Radioligand-binding assay assessing receptor affinity. 2 “PZM21 (K_i(μOR)=31 nM)” auto_single_measurement only accepted activity measurement [1] 1 structures\7SBF\7SBF_metadata.json point structures/7SBF/7sbf_protein.pdb structures/7SBF/7sbf_pocket.pdb structures/7SBF/7sbf_ligand.sdf structures/7SBF/7sbf_ligand.pdb structures/7SBF/7sbf_ligand.cif structures/7SBF/7sbf_complex.pdb structures/7SBF/7sbf_complex.cif 7SCR classic TbrHGXPRT Trypanosoma brucei Na Na (S,S)-48; (4S,7S)-7-hydroxy-4-((guanin-9-yl)methyl)-2,5-dioxaheptan-1,7-diphosphonate "[""8QI""]" 1 Ki Ki = = 0.02 ± 0.01 μM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition Table 3 enzyme-inhibition assay of stereo-defined acyclic nucleoside phosphonates/bisphosphonates against 6-oxopurine PRTs. 8 Table 3 reports TbrHGXPRT Ki = 0.02 ± 0.01 μM for purified hydroxyl isomer (S,S)-48; Figure 6 maps the TbrHGXPRT·(S,S)-48 complex to PDB 7SCR. auto_single_measurement only accepted activity measurement [1] 1 structures\7SCR\7SCR_metadata.json point structures/7SCR/7scr_protein.pdb structures/7SCR/7scr_pocket.pdb structures/7SCR/7scr_ligand.sdf structures/7SCR/7scr_ligand.pdb structures/7SCR/7scr_ligand.cif structures/7SCR/7scr_complex.pdb structures/7SCR/7scr_complex.cif 7SEO extended caspase-3 human Na Na Ac-VDV(DAB)D-CHO "[""CHAIN:F"", ""CHAIN:G""]" 1 pKi Ki = = 8.02 ± 0.26 unitless 9.549925860214369 [] p_metric_transform 8.02 success True biochemical_inhibition Fluorescence-based caspase inhibition assay; Table 2 reports pKi mean ± SD. 6 Table 2 lists AcVDFVD-CHO (31): Casp3 pKi 8.02 ± 0.26. The accession-code order on page 18 maps compound 31 to 7SEO. auto_single_measurement only accepted activity measurement [1] 1 structures\7SEO\7SEO_metadata.json point structures/7SEO/7seo_protein.pdb structures/7SEO/7seo_pocket.pdb structures/7SEO/7seo_ligand.pdb structures/7SEO/7seo_ligand.cif structures/7SEO/7seo_complex.pdb structures/7SEO/7seo_complex.cif 7SFC classic DNMT1 human DNMT1 residues 729-1600 Na GSK3735967A "[""I67""]" 1 IC50 IC50 = = 40±6 nM 40.0 [] unit_conversion 7.3979400086720375 success True biochemical_inhibition Radioactive scintillation proximity assay using full-length DNMT1 and a 40-mer hemimethylated DNA duplex. 4 Figure 1D reports GSK3735967 IC50 ± SEM of 40±6 nM; its legend identifies a full-length DNMT1 radioactive SPA assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7SFC\7SFC_metadata.json point structures/7SFC/7sfc_protein.pdb structures/7SFC/7sfc_pocket.pdb structures/7SFC/7sfc_ligand.sdf structures/7SFC/7sfc_ligand.pdb structures/7SFC/7sfc_ligand.cif structures/7SFC/7sfc_complex.pdb structures/7SFC/7sfc_complex.cif 7SFD classic DNMT1 human DNMT1 residues 729-1600 Na GSK3543105A "[""IO5""]" 1 IC50 IC50 = = 33±6 nM 33.0 [] unit_conversion 7.481486060122112 success True biochemical_inhibition Radioactive scintillation proximity assay using full-length DNMT1 and a 40-mer hemimethylated DNA duplex. 4 Figure 1D reports GSK3543105 IC50 ± SEM of 33±6 nM; its legend identifies a full-length DNMT1 radioactive SPA assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7SFD\7SFD_metadata.json point structures/7SFD/7sfd_protein.pdb structures/7SFD/7sfd_pocket.pdb structures/7SFD/7sfd_ligand.sdf structures/7SFD/7sfd_ligand.pdb structures/7SFD/7sfd_ligand.cif structures/7SFD/7sfd_complex.pdb structures/7SFD/7sfd_complex.cif 7SFE classic DNMT1 human DNMT1 residues 729-1600 Na GSK3830334A "[""96I""]" 1 IC50 IC50 = = 190±10 nM 190.0 [] unit_conversion 6.721246399047171 success True biochemical_inhibition Radioactive scintillation proximity assay using full-length DNMT1 and a 40-mer hemimethylated DNA duplex. 4 Figure 1D reports GSK3830334 IC50 ± SEM of 190±10 nM; its legend identifies a full-length DNMT1 radioactive SPA assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7SFE\7SFE_metadata.json point structures/7SFE/7sfe_protein.pdb structures/7SFE/7sfe_pocket.pdb structures/7SFE/7sfe_ligand.sdf structures/7SFE/7sfe_ligand.pdb structures/7SFE/7sfe_ligand.cif structures/7SFE/7sfe_complex.pdb structures/7SFE/7sfe_complex.cif 7SFF classic DNMT1 human DNMT1 residues 729-1600 Na GSK3852279B "[""C79""]" 1 IC50 IC50 = = 56±7 nM 56.0 [] unit_conversion 7.251811972993799 success True biochemical_inhibition Radioactive scintillation proximity assay using full-length DNMT1 and a 40-mer hemimethylated DNA duplex. 4 Figure 1D reports GSK3852279 IC50 ± SEM of 56±7 nM; its legend identifies a full-length DNMT1 radioactive SPA assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7SFF\7SFF_metadata.json point structures/7SFF/7sff_protein.pdb structures/7SFF/7sff_pocket.pdb structures/7SFF/7sff_ligand.sdf structures/7SFF/7sff_ligand.pdb structures/7SFF/7sff_ligand.cif structures/7SFF/7sff_complex.pdb structures/7SFF/7sff_complex.cif 7SFR classic Mycobacterium tuberculosis 50S ribosome Mycobacterium tuberculosis 50S ribosome Na SEQ-9 "[""WDP""]" 1 IC50 IC50 = = 0.075 µM 75.0 [] unit_conversion 7.1249387366083 success True biochemical_inhibition Cell-free protein-synthesis/translation inhibition using the unmethylated Mtb ribosome. 5 Table 1 reports “Inhibition of Mtb translation (IC50 µM)” for SEQ-9 as 0.075. auto_single_measurement only accepted activity measurement [1] 1 structures\7SFR\7SFR_metadata.json point structures/7SFR/7sfr_protein.pdb structures/7SFR/7sfr_pocket.pdb structures/7SFR/7sfr_ligand.sdf structures/7SFR/7sfr_ligand.pdb structures/7SFR/7sfr_ligand.cif structures/7SFR/7sfr_complex.pdb structures/7SFR/7sfr_complex.cif 7SG5 extended CIS43_Var2 antibody human Fab VH V2R; VL L27F PfCSP Peptide 21 (Pep21) "[""CHAIN:A""]" 1 Kd Kd = = 3.6 ± 0.2 nM 3.6 [] unit_conversion 8.443697499232712 success True direct_binding BLI affinity of CIS43 variants against Pep21. 26 The BLI affinity table reports CIS43-Var2 Pep21 K_D = 3.6 ± 0.2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7SG5\7SG5_metadata.json point structures/7SG5/7sg5_protein.pdb structures/7SG5/7sg5_pocket.pdb structures/7SG5/7sg5_ligand.pdb structures/7SG5/7sg5_ligand.cif structures/7SG5/7sg5_complex.pdb structures/7SG5/7sg5_complex.cif 7SG6 extended CIS43_Var10 antibody human Fab VH V2R; VL L27F, V85S PfCSP Peptide 21 (Pep21) "[""CHAIN:A""]" 1 Kd Kd = = 4.0 ± 0.3 nM 4.0 [] unit_conversion 8.397940008672037 success True direct_binding BLI affinity of CIS43 variants against Pep21. 26 The BLI affinity table reports CIS43-Var10 Pep21 K_D = 4.0 ± 0.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7SG6\7SG6_metadata.json point structures/7SG6/7sg6_protein.pdb structures/7SG6/7sg6_pocket.pdb structures/7SG6/7sg6_ligand.pdb structures/7SG6/7sg6_ligand.cif structures/7SG6/7sg6_complex.pdb structures/7SG6/7sg6_complex.cif 7SH0 classic Endoplasmic reticulum aminopeptidase 2 (ERAP2) Na Na Na 4e (BDM88952) "[""GIY""]" 1 IC50 IC50 = = 0.0039 µM 3.9 [] unit_conversion 8.4089353929735 success True biochemical_inhibition Inhibition of ERAP2 by selected analogues; mean of two to four independent measurements. 4 Table 2 reports compound 4e with IC50 0.0039 µM; the table footnote states IC50 values are means of two to four independent measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\7SH0\7SH0_metadata.json point structures/7SH0/7sh0_protein.pdb structures/7SH0/7sh0_pocket.pdb structures/7SH0/7sh0_ligand.sdf structures/7SH0/7sh0_ligand.pdb structures/7SH0/7sh0_ligand.cif structures/7SH0/7sh0_complex.pdb structures/7SH0/7sh0_complex.cif 7SH5 classic CYP142A3 Mycobacterium ulcerans Codon-optimized CYP142A3 with a C-terminal 6xHis tag in pET29 Na cholest-4-en-3-one "[""K2B""]" 1 Kd Kd = = 0.03 ± 0.01 μM 30.0 [] unit_conversion 7.522878745280337 success True direct_binding Purified-protein UV–visible substrate-binding titration; Table 1. 4 Table 1 reports MulcCYP142A3 binding to cholest-4-en-3-one: Kd 0.03 ± 0.01 μM. Table 3 identifies 7SH5 as the M. ulcerans cholest-4-en-3-one-bound structure. auto_single_measurement only accepted activity measurement [1] 1 structures\7SH5\7SH5_metadata.json point structures/7SH5/7sh5_protein.pdb structures/7SH5/7sh5_pocket.pdb structures/7SH5/7sh5_ligand.sdf structures/7SH5/7sh5_ligand.pdb structures/7SH5/7sh5_ligand.cif structures/7SH5/7sh5_complex.pdb structures/7SH5/7sh5_complex.cif 7SHO classic hSTING human hSTING CBD (aa 155-341) Na c[2',3'-(ara-2'-G, ribo-3'-A)-MP] (RJ242); ara/ribo-13 "[""9UH""]" 1 Kd Kd = = 0.77 µM 770.0 [] unit_conversion 6.113509274827518 success True direct_binding Isothermal titration calorimetry (ITC) with hSTING CBD. 5 The hSTING ITC table reports Kd = 0.77 µM for ara/ribo-13; the text identifies ara/ribo-13 as the arabinose-modified 2′,3′-cGAMP analogue. auto_single_measurement only accepted activity measurement [1] 1 structures\7SHO\7SHO_metadata.json point structures/7SHO/7sho_protein.pdb structures/7SHO/7sho_pocket.pdb structures/7SHO/7sho_ligand.sdf structures/7SHO/7sho_ligand.pdb structures/7SHO/7sho_ligand.cif structures/7SHO/7sho_complex.pdb structures/7SHO/7sho_complex.cif 7SHP classic hSTING human hSTING CBD (aa 155-341) Na c[2',3'-(ribo-2'-G, xylo-3'-A)-MP] (RJ244); ribo/xylo-19 "[""9UR""]" 1 Kd Kd = = 4.0 µM 4000.0 [] unit_conversion 5.3979400086720375 success True direct_binding Isothermal titration calorimetry (ITC) with hSTING CBD. 5 The hSTING ITC table reports Kd = 4.0 µM for ribo/xylo-19; the text identifies ribo/xylo-19 as the xylose-modified 2′,3′-cGAMP analogue. auto_single_measurement only accepted activity measurement [1] 1 structures\7SHP\7SHP_metadata.json point structures/7SHP/7shp_protein.pdb structures/7SHP/7shp_pocket.pdb structures/7SHP/7shp_ligand.sdf structures/7SHP/7shp_ligand.pdb structures/7SHP/7shp_ligand.cif structures/7SHP/7shp_complex.pdb structures/7SHP/7shp_complex.cif 7SJP extended Fab15H6.v4 Na Fab15H6.v4 Fab fragment Na HTRA1 LoopA peptide "[""CHAIN:E""]" 1 Kd Kd = = 0.77 ± 0.14 nM 0.77 [] unit_conversion 9.113509274827518 success True direct_binding SPR binding kinetics of immobilized Fab15H6.v4 to the wild-type HTRA1 LoopA synthetic peptide. 7 Fig. 4e reports LoopAHTRA1 peptide:Fab15H6.v4 KD = 0.77 ± 0.14 nM; the caption identifies this as SPR binding kinetics to LoopA peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7SJP\7SJP_metadata.json point structures/7SJP/7sjp_protein.pdb structures/7SJP/7sjp_pocket.pdb structures/7SJP/7sjp_ligand.pdb structures/7SJP/7sjp_ligand.cif structures/7SJP/7sjp_complex.pdb structures/7SJP/7sjp_complex.cif 7SKQ classic BtSCoV-Rf1.2004 papain-like protease (PLpro) Rhinolophus ferrumequinum-associated BtSCoV-Rf1.2004 PLpro residues 1536-1850 of pp1ab; construct residues 2-316 Na GRL-0617 "[""TTT""]" 1 IC50 IC50 = = 1.2 ± 0.0 µM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition Peptide-AMC cleavage inhibition assay; Table 3 color key assigns the gray value to BtSCoV-Rf1.2004 PLpro. 8 Table 3 reports GRL-0617 IC50 values of 2.4 ± 0.2 (SARS-CoV-2, blue), 1.4 ± 0.0 (SARS-CoV-1, red), and 1.2 ± 0.0 µM (BtSCoV-Rf1.2004, gray). auto_single_measurement only accepted activity measurement [1] 1 structures\7SKQ\7SKQ_metadata.json point structures/7SKQ/7skq_protein.pdb structures/7SKQ/7skq_pocket.pdb structures/7SKQ/7skq_ligand.sdf structures/7SKQ/7skq_ligand.pdb structures/7SKQ/7skq_ligand.cif structures/7SKQ/7skq_complex.pdb structures/7SKQ/7skq_complex.cif 7SKR classic BtSCoV-Rf1.2004 papain-like protease (PLpro) Rhinolophus ferrumequinum-associated BtSCoV-Rf1.2004 PLpro residues 1536-1850 of pp1ab; construct residues 2-316 Na compound 37 "[""9OZ""]" 1 IC50 IC50 = = 7.5 ± 0.5 µM 7500.0 [] unit_conversion 5.1249387366083 success True biochemical_inhibition Peptide-AMC cleavage inhibition assay; Table 3 color key assigns the gray value to BtSCoV-Rf1.2004 PLpro. 8 Table 3 reports compound 37 IC50 values of 5.4 ± 0.2 (SARS-CoV-2, blue), 10.7 ± 0.7 (SARS-CoV-1, red), and 7.5 ± 0.5 µM (BtSCoV-Rf1.2004, gray). auto_single_measurement only accepted activity measurement [1] 1 structures\7SKR\7SKR_metadata.json point structures/7SKR/7skr_protein.pdb structures/7SKR/7skr_pocket.pdb structures/7SKR/7skr_ligand.sdf structures/7SKR/7skr_ligand.pdb structures/7SKR/7skr_ligand.cif structures/7SKR/7skr_complex.pdb structures/7SKR/7skr_complex.cif 7SME extended p107 human p107DeltaL pocket domain, residues 389-972, with deletions 600-779 and 888-923 Na HDAC1 peptide "[""CHAIN:B""]" 1 Kd Kd = = 80 ± 10 µM 80000.0 [] unit_conversion 4.096910013008056 success True direct_binding AlphaScreen competition-derived equilibrium dissociation constant for HDAC1 peptide binding to p107 pocket domain. 22 Figure 1B reports hsHDAC1: p107 pocket Kd = 80 ± 10 µM. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\7SME\7SME_metadata.json point structures/7SME/7sme_protein.pdb structures/7SME/7sme_pocket.pdb structures/7SME/7sme_ligand.pdb structures/7SME/7sme_ligand.cif structures/7SME/7sme_complex.pdb structures/7SME/7sme_complex.cif 7SMF extended p107 human p107DeltaL pocket domain, residues 389-972, with deletions 600-779 and 888-923 R413D; A415Y; E417Y mutated HDAC1-3X peptide "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.105 ± 0.005 µM 105.0 [] unit_conversion 6.978810700930062 success True direct_binding ITC measurement of the engineered HDAC1 3X peptide binding to the p107 pocket domain. 28 Figure 6A reports HDAC1 3X mutant–p107 pocket Kd = 0.105 ± 0.005 µM; the caption identifies the mutations as D413, Y415, and Y417 introduced into HDAC1. auto_single_measurement only accepted activity measurement [1] 1 structures\7SMF\7SMF_metadata.json point structures/7SMF/7smf_protein.pdb structures/7SMF/7smf_pocket.pdb structures/7SMF/7smf_ligand.pdb structures/7SMF/7smf_ligand.cif structures/7SMF/7smf_complex.pdb structures/7SMF/7smf_complex.cif 7SMZ classic CYP142A3 Mycobacterium marinum M. marinum CYP142A3 gene cloned into pET26 Na cholest-4-en-3-one "[""K2B""]" 1 Kd Kd = = 0.2 ± 0.1 μM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Purified-protein UV–visible substrate-binding titration; Table 1. 4 Table 1 reports MmarCYP142A3 binding to cholest-4-en-3-one: Kd 0.2 ± 0.1 μM. Table 3 identifies 7SMZ as the M. marinum cholest-4-en-3-one-bound structure. auto_single_measurement only accepted activity measurement [1] 1 structures\7SMZ\7SMZ_metadata.json point structures/7SMZ/7smz_protein.pdb structures/7SMZ/7smz_pocket.pdb structures/7SMZ/7smz_ligand.sdf structures/7SMZ/7smz_ligand.pdb structures/7SMZ/7smz_ligand.cif structures/7SMZ/7smz_complex.pdb structures/7SMZ/7smz_complex.cif 7SNM classic CYP51-ferredoxin fusion protein Methylococcus capsulatus CYP51-ferredoxin fusion protein of approximately 561 residues: 451-residue P450 domain, 20-residue linker, 80-residue ferredoxin domain, and 10-residue C-terminal His tag; 443 P450 residues were modeled Na lanosterol "[""LAN""]" 1 Kd Kd = = 3 nM 3.0 [] unit_conversion 8.522878745280337 success True direct_binding Purified M. capsulatus CYP51-ferredoxin fusion protein; apparent sterol substrate-binding affinities were determined from spectral titration curves fitted with a quadratic binding (Morrison) equation. 6 Figure 4 explicitly labels the M. capsulatus CYP51–lanosterol interaction “Kd = 3 nM.” The methods state that apparent sterol substrate-binding affinities in solution were calculated from spectral titration curves. auto_single_measurement only accepted activity measurement [1] 1 structures\7SNM\7SNM_metadata.json point structures/7SNM/7snm_protein.pdb structures/7SNM/7snm_pocket.pdb structures/7SNM/7snm_ligand.sdf structures/7SNM/7snm_ligand.pdb structures/7SNM/7snm_ligand.cif structures/7SNM/7snm_complex.pdb structures/7SNM/7snm_complex.cif 7SNU classic ShHTL7 Striga hermonthica ShHTL7 residues 3-270 Na RG6 "[""HFJ""]" 1 Kd Kd = = 4.54 μM 4540.0 [] unit_conversion 5.342944147142896 success True direct_binding Differential scanning fluorimetry with ShHTL7; dissociation constant calculated by DSF fitting. 5 “RG6 showed the highest Kd of 4.54 μM.” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7SNU\7SNU_metadata.json point structures/7SNU/7snu_protein.pdb structures/7SNU/7snu_pocket.pdb structures/7SNU/7snu_ligand.sdf structures/7SNU/7snu_ligand.pdb structures/7SNU/7snu_ligand.cif structures/7SNU/7snu_complex.pdb structures/7SNU/7snu_complex.cif 7SPS classic human glucose transporter GLUT3 human GLUT3 N43T; WT with respect to S64W/I305W exofacial-locking substitutions SA47 "[""A0E""]" 2 Kd Kd = = 316.5 ± 47.2 nM 316.5 [] unit_conversion 6.499626285646626 success True direct_binding Microscale thermophoresis measurement of SA47 binding to GLUT3. 3 “the affinity of SA47 with GLUT1 and GLUT3 was measured with KD values of 309.5 ± 58.2 nM and 316.5 ± 47.2 nM, respectively, using MST.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7SPS\7SPS_metadata.json point structures/7SPS/7sps_protein.pdb structures/7SPS/7sps_pocket.pdb structures/7SPS/7sps_ligand.sdf structures/7SPS/7sps_ligand.pdb structures/7SPS/7sps_ligand.cif structures/7SPS/7sps_complex.pdb structures/7SPS/7sps_complex.cif 7SQL classic Human uridine-cytidine kinase 2 (UCK2) human Na Na compound 1 "[""AQX""]" 1 Ki Ki = = 55.1 ± 3.8 µM 55100.0 [] unit_conversion 4.258848401148215 success True biochemical_inhibition Steady-state kinetic analysis of recombinant human UCK2; noncompetitive inhibitory parameter. 3 Table 1 reports compound 1 Ki = 55.1 ± 3.8 µM; Figure 2 caption identifies recombinant human UCK2, and the text states that all inhibitors attenuated kcat consistently with noncompetitive inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7SQL\7SQL_metadata.json point structures/7SQL/7sql_protein.pdb structures/7SQL/7sql_pocket.pdb structures/7SQL/7sql_ligand.sdf structures/7SQL/7sql_ligand.pdb structures/7SQL/7sql_ligand.cif structures/7SQL/7sql_complex.pdb structures/7SQL/7sql_complex.cif 7SS6 classic Klebsiella pneumoniae LpxH (KpLpxH) Klebsiella pneumoniae KpLpxH fusion protein with a C-terminal TEV protease site followed by a His10 tag; cloned into modified pET21b Na JH-LPH-45; compound 8 "[""BKB""]" 2 Ki Ki = = 7.3 nM 7.3 [] unit_conversion 8.136677139879545 success True biochemical_inhibition LpxE-coupled KpLpxH enzymatic inhibition assay; competitive binding mode. 5 “compound 8 displayed a significant reduction of the IC50 value (IC50=18 nM, Ki=7.3 nM, Figure 3E)” auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7SS6\7SS6_metadata.json point structures/7SS6/7ss6_protein.pdb structures/7SS6/7ss6_pocket.pdb structures/7SS6/7ss6_ligand.sdf structures/7SS6/7ss6_ligand.pdb structures/7SS6/7ss6_ligand.cif structures/7SS6/7ss6_complex.pdb structures/7SS6/7ss6_complex.cif 7SS7 classic Klebsiella pneumoniae LpxH (KpLpxH) Klebsiella pneumoniae KpLpxH fusion protein with a C-terminal TEV protease site followed by a His10 tag; cloned into modified pET21b Na JH-LPH-50; compound 13 "[""BN8""]" 2 Ki Ki = = 3.1 nM 3.1 [] unit_conversion 8.508638306165727 success True biochemical_inhibition LpxE-coupled KpLpxH enzymatic inhibition assay; competitive binding mode. 5 “the lower IC50 value of 13 (IC50=7.7 nM, Ki=3.1 nM; Figure 4E)” auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7SS7\7SS7_metadata.json point structures/7SS7/7ss7_protein.pdb structures/7SS7/7ss7_pocket.pdb structures/7SS7/7ss7_ligand.sdf structures/7SS7/7ss7_ligand.pdb structures/7SS7/7ss7_ligand.cif structures/7SS7/7ss7_complex.pdb structures/7SS7/7ss7_complex.cif 7SSM classic STING human Residues 155-341; N-terminal hexahistidine tag and tobacco etch virus protease cleavage site R232 (Arg232) variant compound 11 "[""B7L""]" 1 IC50 IC50 = = 40 µM 40000.0 [] unit_conversion 4.3979400086720375 success True direct_binding HTRF competition/displacement assay; human WT STING. 2 Table 1 reports HTRF displacement IC50 values for compound 11 as 40/14/1.1 µM for H-WT/H-AQ/M, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\7SSM\7SSM_metadata.json point structures/7SSM/7ssm_protein.pdb structures/7SSM/7ssm_pocket.pdb structures/7SSM/7ssm_ligand.sdf structures/7SSM/7ssm_ligand.pdb structures/7SSM/7ssm_ligand.cif structures/7SSM/7ssm_complex.pdb structures/7SSM/7ssm_complex.cif 7STN classic Chitin Synthase 2 Candida albicans Na Na Nikkomycin Z "[""BGI""]" 2 Ki Ki = = 1.49 ± 0.51 µM 1490.0 [] unit_conversion 5.826813731587726 success True biochemical_inhibition Enzymatic parameters of CaChs2, WT. 4 Supplementary Table 1 reports Nikkomycin Z Ki of 1.49 ± 0.51 µM for WT CaChs2. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7STN\7STN_metadata.json point structures/7STN/7stn_protein.pdb structures/7STN/7stn_pocket.pdb structures/7STN/7stn_ligand.sdf structures/7STN/7stn_ligand.pdb structures/7STN/7stn_ligand.cif structures/7STN/7stn_complex.pdb structures/7STN/7stn_complex.cif 7STO classic Chitin Synthase 2 Candida albicans Na Na polyoxin D "[""BJ9""]" 2 Ki Ki = = 3.19 ± 1.35 µM 3190.0 [] unit_conversion 5.496209316942819 success True biochemical_inhibition Enzymatic parameters of CaChs2, WT. 4 Supplementary Table 1 reports Polyoxin D Ki of 3.19 ± 1.35 µM for WT CaChs2. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7STO\7STO_metadata.json point structures/7STO/7sto_protein.pdb structures/7STO/7sto_pocket.pdb structures/7STO/7sto_ligand.sdf structures/7STO/7sto_ligand.pdb structures/7STO/7sto_ligand.cif structures/7STO/7sto_complex.pdb structures/7STO/7sto_complex.cif 7STQ classic Arabidopsis thaliana acetohydroxyacid synthase (AtAHAS) Arabidopsis thaliana Na W574L chlorimuron-ethyl (CE) "[""CIE""]" 1 Ki Ki = = 5200 ± 300 nM 5200.0 [] unit_conversion 5.2839966563652006 success True biochemical_inhibition Ki of commercial herbicides measured for W574L AtAHAS mutant. 4 Table 1 reports CE Ki for W574L as 5200 ± 300 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7STQ\7STQ_metadata.json point structures/7STQ/7stq_protein.pdb structures/7STQ/7stq_pocket.pdb structures/7STQ/7stq_ligand.sdf structures/7STQ/7stq_ligand.pdb structures/7STQ/7stq_ligand.cif structures/7STQ/7stq_complex.pdb structures/7STQ/7stq_complex.cif 7SUO extended G3BP1 Homo sapiens (G3BP1); SARS-CoV-2 (nucleocapsid peptide) G3BP1 NTF2-like domain residues 1-139 bound to SARS-CoV-2 nucleocapsid N1-25 peptide Na SARS-CoV-2 nucleocapsid N1-25 peptide (IDR1) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 8.5 µM 8500.0 [] unit_conversion 5.070581074285707 success True direct_binding Isothermal titration calorimetry (ITC), G3BP1 NTF2 domain titrated with SARS-CoV-2 N1-25 peptide. 5 The text reports Kd values of 7.9 µM, 8.5 µM, and 10.9 µM for full-length G3BP1, G3BP1NTF2, and G3BP2NTF2, respectively, with the N1-25 peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7SUO\7SUO_metadata.json point structures/7SUO/7suo_protein.pdb structures/7SUO/7suo_pocket.pdb structures/7SUO/7suo_ligand.pdb structures/7SUO/7suo_ligand.cif structures/7SUO/7suo_complex.pdb structures/7SUO/7suo_complex.cif 7SUP classic cTnC-TnI chimera human N-terminal His6-tagged human cardiac TnC residues D2-G91, followed by an -AGAG- linker and human cardiac TnI switch region residues V147-D180; TEV cleavage site ENLYFQG Na A1 "[""BQ6""]" 1 Kd Kd = = 1.2 ± 0.2 µM 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding ITC, TC + A1 ↔ TCA1 4 Table 1 reports K_D = 1.2 ± 0.2 µM for A1 binding to the calcium-bound chimera. auto_single_measurement only accepted activity measurement [1] 1 structures\7SUP\7SUP_metadata.json point structures/7SUP/7sup_protein.pdb structures/7SUP/7sup_pocket.pdb structures/7SUP/7sup_ligand.sdf structures/7SUP/7sup_ligand.pdb structures/7SUP/7sup_ligand.cif structures/7SUP/7sup_complex.pdb structures/7SUP/7sup_complex.cif 7SUW classic Carbonic Anhydrase IX-mimic human hCA IX-mimic Na compound 41; 2-((3-Aminopropyl)(phenethyl)amino)-N-(furan-2-ylmethyl)-N-(4-sulfamoylphenethyl)acetamide "[""U77""]" 1 Ki Ki = = 11.1 nM 11.1 [] unit_conversion 7.954677021213342 success True biochemical_inhibition Stopped-flow CO2 hydration inhibition assay; Table 1 reports hCA IX inhibition. 4 Table 1 lists compound 41 with hCA IX Ki = 11.1 nM; the table caption specifies a stopped-flow CO2 hydrase assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7SUW\7SUW_metadata.json point structures/7SUW/7suw_protein.pdb structures/7SUW/7suw_pocket.pdb structures/7SUW/7suw_ligand.sdf structures/7SUW/7suw_ligand.pdb structures/7SUW/7suw_ligand.cif structures/7SUW/7suw_complex.pdb structures/7SUW/7suw_complex.cif 7SV2 classic Human cytochrome P450 3A5 (CYP3A5) human N-terminal transmembrane helix and short luminal extension deleted (Delta3-24); five C-terminal amino acids replaced by a 4-histidine tag; construct 3A5C2dH Na azamulin "[""MWY""]" 1 Kd Kd = = 3.41 ± 0.60 μM 3410.0 [] unit_conversion 5.467245621007502 success True direct_binding Two-site sequential binding-model fit; Kd for formation of the ternary 3A5 complex with a second azamulin molecule. 5 “3.41 ± 0.60 μM for the ternary complex”; Table 1 lists Kd2 as 3.41 ± 0.60 μM for azamulin. auto_single_measurement only accepted activity measurement [1] 1 structures\7SV2\7SV2_metadata.json point structures/7SV2/7sv2_protein.pdb structures/7SV2/7sv2_pocket.pdb structures/7SV2/7sv2_ligand.sdf structures/7SV2/7sv2_ligand.pdb structures/7SV2/7sv2_ligand.cif structures/7SV2/7sv2_complex.pdb structures/7SV2/7sv2_complex.cif 7SV3 classic SpaA_SLH Paenibacillus alvei SpaA_SLH amino acids 21-193 with a Ser-Gly-Ser linker and C-terminal His6 tag wild-type 4,6-Pyr-beta-D-ManNAc-(1->4)-beta-D-GlcNAcOMe "[""D2Y""]" 1 Kd Kd = = 64 nM 64.0 [] unit_conversion 7.1938200260161125 success True direct_binding ITC, 20 °C; disaccharide-binding data. 3 Table 1 reports SpaA_SLH disaccharide-binding K_D of 64 nM; Table 2 maps the wild-type disaccharide complex to PDB 7SV3. auto_single_measurement only accepted activity measurement [1] 1 structures\7SV3\7SV3_metadata.json point structures/7SV3/7sv3_protein.pdb structures/7SV3/7sv3_pocket.pdb structures/7SV3/7sv3_ligand.sdf structures/7SV3/7sv3_ligand.pdb structures/7SV3/7sv3_ligand.cif structures/7SV3/7sv3_complex.pdb structures/7SV3/7sv3_complex.cif 7SV4 classic SpaA_SLH Paenibacillus alvei SpaA_SLH amino acids 21-193 with a Ser-Gly-Ser linker and C-terminal His6 tag wild-type 4,6-Pyr-beta-D-ManNAc-(1->4)-beta-D-GlcNAc-(1->3)-4,6-Pyr-beta-D-ManNAcOMe "[""D4I""]" 1 Kd Kd = = 4.7 nM 4.7 [] unit_conversion 8.327902142064282 success True direct_binding ITC, 20 °C; trisaccharide-binding data. 3 Table 1 reports SpaA_SLH trisaccharide-binding K_D of 4.7 nM; Table 2 maps the wild-type trisaccharide complex to PDB 7SV4. auto_single_measurement only accepted activity measurement [1] 1 structures\7SV4\7SV4_metadata.json point structures/7SV4/7sv4_protein.pdb structures/7SV4/7sv4_pocket.pdb structures/7SV4/7sv4_ligand.sdf structures/7SV4/7sv4_ligand.pdb structures/7SV4/7sv4_ligand.cif structures/7SV4/7sv4_complex.pdb structures/7SV4/7sv4_complex.cif 7SV5 classic SpaA_SLH/G109A Paenibacillus alvei SpaA_SLH amino acids 21-193 with a Ser-Gly-Ser linker and C-terminal His6 tag G109A 4,6-Pyr-beta-D-ManNAc-(1->4)-beta-D-GlcNAcOMe "[""D2Y""]" 1 Kd Kd = = 288 nM 288.0 [] unit_conversion 6.5406075122407685 success True direct_binding ITC, 20 °C; disaccharide-binding data. 3 Table 1 reports SpaA_SLH/G109A disaccharide-binding K_D of 288 nM; Table 2 maps this mutant disaccharide complex to PDB 7SV5. auto_single_measurement only accepted activity measurement [1] 1 structures\7SV5\7SV5_metadata.json point structures/7SV5/7sv5_protein.pdb structures/7SV5/7sv5_pocket.pdb structures/7SV5/7sv5_ligand.sdf structures/7SV5/7sv5_ligand.pdb structures/7SV5/7sv5_ligand.cif structures/7SV5/7sv5_complex.pdb structures/7SV5/7sv5_complex.cif 7SVC classic cTnC-TnI chimera human N-terminal His6-tagged human cardiac TnC residues D2-G91, followed by an -AGAG- linker and human cardiac TnI switch region residues V147-D180; TEV cleavage site ENLYFQG Na A2 "[""C9W""]" 1 Kd Kd = = 1.6 ± 0.1 µM 1600.0 [] unit_conversion 5.795880017344075 success True direct_binding ITC, TC + A2 ↔ TCA2 4 Table 1 reports K_D = 1.6 ± 0.1 µM for A2 binding to the calcium-bound chimera. auto_single_measurement only accepted activity measurement [1] 1 structures\7SVC\7SVC_metadata.json point structures/7SVC/7svc_protein.pdb structures/7SVC/7svc_pocket.pdb structures/7SVC/7svc_ligand.sdf structures/7SVC/7svc_ligand.pdb structures/7SVC/7svc_ligand.cif structures/7SVC/7svc_complex.pdb structures/7SVC/7svc_complex.cif 7SVP classic human Phospholipase D2 human Na Na compound 34 "[""CI0""]" 1 IC50 IC50 = = 0.23 µM 230.0 [] unit_conversion 6.638272163982407 success True biochemical_inhibition Biochemical PLD1/2 inhibition determined by immunoprecipitation on a plate (IPoP) from HEK cells. 5 Table 4 reports compound 34 PLD1/PLD2 IC50 values of 0.044 / 0.23 µM; the table footnote defines the biochemical IPoP assay of PLD1/2 from HEK cells. Figure 4 identifies compound 34 bound to hPLD2 (PDB 7SVP). auto_single_measurement only accepted activity measurement [1] 1 structures\7SVP\7SVP_metadata.json point structures/7SVP/7svp_protein.pdb structures/7SVP/7svp_pocket.pdb structures/7SVP/7svp_ligand.sdf structures/7SVP/7svp_ligand.pdb structures/7SVP/7svp_ligand.cif structures/7SVP/7svp_complex.pdb structures/7SVP/7svp_complex.cif 7SVR classic human cystic fibrosis transmembrane conductance regulator (CFTR) human Na WT (wild-type) Lumacaftor (VX-809) "[""VX8""]" 1 Kd Kd = = 8.3 ± 2.2 nM 8.3 [] unit_conversion 8.080921907623926 success True direct_binding Saturation binding/nonlinear regression analysis of [3H]lumacaftor binding to wtCFTR in the absence of phosphorylation and ATP. 3 Figure 1B caption reports: “Kd = 8.3 ± 2.2 nM” for [3H]lumacaftor binding to wtCFTR in the absence of phosphorylation and ATP. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7SVR\7SVR_metadata.json point structures/7SVR/7svr_protein.pdb structures/7SVR/7svr_pocket.pdb structures/7SVR/7svr_ligand.sdf structures/7SVR/7svr_ligand.pdb structures/7SVR/7svr_ligand.cif structures/7SVR/7svr_complex.pdb structures/7SVR/7svr_complex.cif 7SVT classic Mycobacterium tuberculosis 3-hydroxyl-ACP dehydratase HadAB Mycobacterium tuberculosis Na Na compound 9 (1,3-diarylpyrazolyl-acylsulfonamide inhibitor) "[""CI7""]" 1 IC50 IC50 = = 0.03±0.01 µM 30.0 [] unit_conversion 7.522878745280337 success True biochemical_inhibition Purified Mtb HadAB enzymatic-complex spectrophotometric inhibition assay; Table 2. 4 Table 2 reports compound 9 HadAB IC50 = 0.03±0.01 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7SVT\7SVT_metadata.json point structures/7SVT/7svt_protein.pdb structures/7SVT/7svt_pocket.pdb structures/7SVT/7svt_ligand.sdf structures/7SVT/7svt_ligand.pdb structures/7SVT/7svt_ligand.cif structures/7SVT/7svt_complex.pdb structures/7SVT/7svt_complex.cif 7SWG classic cTnC-TnI chimera human N-terminal His6-tagged human cardiac TnC residues D2-G91, followed by an -AGAG- linker and human cardiac TnI switch region residues V147-D180; TEV cleavage site ENLYFQG Na A1 "[""BQ6""]" 1 Kd Kd = = 4.1 ± 0.4 µM 4100.0 [] unit_conversion 5.3872161432802645 success True direct_binding ITC, T + A1 ↔ TA1 4 Table 1 reports K_D = 4.1 ± 0.4 µM for A1 binding to the calcium-free chimera. auto_single_measurement only accepted activity measurement [1] 1 structures\7SWG\7SWG_metadata.json point structures/7SWG/7swg_protein.pdb structures/7SWG/7swg_pocket.pdb structures/7SWG/7swg_ligand.sdf structures/7SWG/7swg_ligand.pdb structures/7SWG/7swg_ligand.cif structures/7SWG/7swg_complex.pdb structures/7SWG/7swg_complex.cif 7SWI classic cTnC-TnI chimera human N-terminal His6-tagged human cardiac TnC residues D2-G91, followed by an -AGAG- linker and human cardiac TnI switch region residues V147-D180; TEV cleavage site ENLYFQG Na A2 "[""C9W""]" 1 Kd Kd = = 22.0 ± 0.50 µM 22000.0 [] unit_conversion 4.657577319177793 success True direct_binding ITC, T + A2 ↔ TA2 4 Table 1 reports K_D = 22.0 ± 0.50 µM for A2 binding to the calcium-free chimera. auto_single_measurement only accepted activity measurement [1] 1 structures\7SWI\7SWI_metadata.json point structures/7SWI/7swi_protein.pdb structures/7SWI/7swi_pocket.pdb structures/7SWI/7swi_ligand.sdf structures/7SWI/7swi_ligand.pdb structures/7SWI/7swi_ligand.cif structures/7SWI/7swi_complex.pdb structures/7SWI/7swi_complex.cif 7SZQ classic Human P300 Human Na Na compound 19 "[""ETL""]" 1 pIC50 IC50 = = 9.8 unitless 0.1584893192461111 [] p_metric_transform 9.8 success True biochemical_inhibition RapidFire-MS/MS biochemical inhibition of p300; Table 3 reports the p300 value for compound 19. 4 Table 3 lists compound 19 with “p300, pIC50 = 9.8” and states that the data were generated using the RapidFire-MS/MS method. Figure 3 identifies compound 19 as the ligand in PDB 7SZQ. auto_single_measurement only accepted activity measurement [1] 1 structures\7SZQ\7SZQ_metadata.json point structures/7SZQ/7szq_protein.pdb structures/7SZQ/7szq_pocket.pdb structures/7SZQ/7szq_ligand.sdf structures/7SZQ/7szq_ligand.pdb structures/7SZQ/7szq_ligand.cif structures/7SZQ/7szq_complex.pdb structures/7SZQ/7szq_complex.cif 7T1H classic CAB1 pantothenate kinase Saccharomyces cerevisiae Na Na YU281445 "[""E5B""]" 1 Ki Ki = = 113.8 nM 113.8 [] unit_conversion 6.943857737940948 success True biochemical_inhibition Cab1 enzyme inhibition kinetic determination using ADP-Glo; Figure 7 compound-specific curve. 9 Figure 7L prints Ki = 113.8 nM for YU281445 against Cab1; the caption states Ki was determined using ADP-Glo assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7T1H\7T1H_metadata.json point structures/7T1H/7t1h_protein.pdb structures/7T1H/7t1h_pocket.pdb structures/7T1H/7t1h_ligand.sdf structures/7T1H/7t1h_ligand.pdb structures/7T1H/7t1h_ligand.cif structures/7T1H/7t1h_complex.pdb structures/7T1H/7t1h_complex.cif 7T1K extended superbinder Fes SH2 domain (sFes1) Na Na S-BC1G; G-BC3S; K-BC4Q; Q-BC5P; E-BC6D pEZ (sequence PPPVpTyrEPVSYH) "[""CHAIN:B""]" 1 IC50 IC50 = = 0.0016 ± 0.00089 μM 1.6 [] unit_conversion 8.795880017344075 success True direct_binding Competitive SH2 phage ELISA binding curve for the Fes-derived superbinder and pEZ phosphopeptide. 3 Figure 2b reports sFes1 IC50 = 0.0016 ± 0.00089 μM; its caption assigns Fes variants to pEZ. Figure 3 identifies sFes1 as pEZ-bound, and page 11 maps sFes1 to PDB 7T1K. auto_single_measurement only accepted activity measurement [1] 1 structures\7T1K\7T1K_metadata.json point structures/7T1K/7t1k_protein.pdb structures/7T1K/7t1k_pocket.pdb structures/7T1K/7t1k_ligand.pdb structures/7T1K/7t1k_ligand.cif structures/7T1K/7t1k_complex.pdb structures/7T1K/7t1k_complex.cif 7T1L extended superbinder Fes SH2 domain (sFesS) Na Na Q-BC2E; G-BC3T; K-BC4V; Q-BC5K; E-BC6G; V-BC7A; I-betaC2A; I-betaD6L pEZ (sequence PPPVpTyrEPVSYH) "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 0.042 ± 0.007 μM 42.0 [] unit_conversion 7.376750709602099 success True direct_binding Competitive SH2 phage ELISA binding curve for the Fes-derived superbinder and pEZ phosphopeptide. 3 Figure 2b reports sFesS IC50 = 0.042 ± 0.007 μM; its caption assigns Fes variants to pEZ. Figure 3 identifies sFesS as pEZ-bound, and page 11 maps sFesS to PDB 7T1L. auto_single_measurement only accepted activity measurement [1] 1 structures\7T1L\7T1L_metadata.json point structures/7T1L/7t1l_protein.pdb structures/7T1L/7t1l_pocket.pdb structures/7T1L/7t1l_ligand.pdb structures/7T1L/7t1l_ligand.cif structures/7T1L/7t1l_complex.pdb structures/7T1L/7t1l_complex.cif 7T1U extended superbinder Src SH2 domain (sSrcF) Na Na S-BC1G; E-BC2Q; T-BC3S; T-BC4Q; K-BC5P; G-BC6D; S-betaC2V; K-betaD6I pMT (sequence EPQpTyrEEI) "[""CHAIN:D"", ""CHAIN:E""]" 1 IC50 IC50 = = 0.0043 ± 0.00065 μM 4.3 [] unit_conversion 8.366531544420413 success True direct_binding Competitive SH2 phage ELISA binding curve for the Src-derived superbinder and pMT phosphopeptide. 3 Figure 2a reports sSrcF IC50 = 0.0043 ± 0.00065 μM; its caption assigns Src variants to pMT. Figure 3 identifies sSrcF as pMT-bound, and page 11 maps sSrcF to PDB 7T1U. auto_single_measurement only accepted activity measurement [1] 1 structures\7T1U\7T1U_metadata.json point structures/7T1U/7t1u_protein.pdb structures/7T1U/7t1u_pocket.pdb structures/7T1U/7t1u_ligand.pdb structures/7T1U/7t1u_ligand.cif structures/7T1U/7t1u_complex.pdb structures/7T1U/7t1u_complex.cif 7T1Y extended Fbw7-Skp1 Na Fbw7 residues 263-707 with truncated Skp1; GST tag removed by TEV protease before crystallization Na Myc T244 degron peptide (C-terminal degron) "[""CHAIN:C""]" 1 IC50 IC50 = = 260 nM 260.0 [] unit_conversion 6.585026652029182 success True direct_binding Quantitative peptide-competition (ALPHA) assay for Fbw7 binding. 2 Fig. 1E prints an IC50 of 260 nM for the diphosphorylated pT244/pT248 Myc peptide; page 3 states this peptide has about 260 nM affinity toward Fbw7. auto_single_measurement only accepted activity measurement [1] 1 structures\7T1Y\7T1Y_metadata.json point structures/7T1Y/7t1y_protein.pdb structures/7T1Y/7t1y_pocket.pdb structures/7T1Y/7t1y_ligand.pdb structures/7T1Y/7t1y_ligand.cif structures/7T1Y/7t1y_complex.pdb structures/7T1Y/7t1y_complex.cif 7T1Z extended Fbw7-Skp1 Na Fbw7 residues 263-707 with truncated Skp1; GST tag removed by TEV protease before crystallization Na Myc T58 degron peptide (N-terminal degron) "[""CHAIN:C""]" 1 IC50 IC50 = = 9.8 nM 9.8 [] unit_conversion 8.008773924307505 success True direct_binding Quantitative peptide-competition assay for T58-degron phosphopeptides with cyclin E pT380/pS384 peptide for Fbw7 binding. 5 Fig. 3A prints an IC50 of 9.8 nM for the pT58/pS62 peptide; Fig. 3 and the text identify the corresponding pT58/pS62 Myc peptide structure bound to Fbw7. auto_single_measurement only accepted activity measurement [1] 1 structures\7T1Z\7T1Z_metadata.json point structures/7T1Z/7t1z_protein.pdb structures/7T1Z/7t1z_pocket.pdb structures/7T1Z/7t1z_ligand.pdb structures/7T1Z/7t1z_ligand.cif structures/7T1Z/7t1z_complex.pdb structures/7T1Z/7t1z_complex.cif 7T2C extended B5 TCR; HLA-DP4 human B5 TCR-HLA-DP4 (DPA1*01:03/DPB1*04:01)-Ply427-441 ternary complex Ply E427G; C428A Ply427-441 "[""CHAIN:C""]" 1 Kd Kd = = 11.48 ± 0.68 μM 11480.0 [] unit_conversion 4.940058111938045 success True direct_binding Surface plasmon resonance measurement of recombinant B5 TCR binding to HLA-DP4-Ply427–441. 8 Table 1 reports B5-HLA-DP4-Ply K_D = 11.48 ± 0.68 μM; the text identifies SPR as the assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7T2C\7T2C_metadata.json point structures/7T2C/7t2c_protein.pdb structures/7T2C/7t2c_pocket.pdb structures/7T2C/7t2c_ligand.pdb structures/7T2C/7t2c_ligand.cif structures/7T2C/7t2c_complex.pdb structures/7T2C/7t2c_complex.cif 7T5R classic LpxA Pseudomonas aeruginosa Na Na H7 "[""F30""]" 1 Kd Kd > > 1 mM 1000000.0 [] unit_conversion 3.0 success True direct_binding Surface plasmon resonance (SPR), dose-dependent titration against LpxA. 3 The text reports that H16, H9, H10, and H7 had K_D values of 35.2 ± 3.9, 114.3 ± 24.3, 139.1 ± 33.2, and >1 mM, respectively; page 9 maps 7T5R to H7. auto_single_measurement only accepted activity measurement [1] 1 structures\7T5R\7T5R_metadata.json point structures/7T5R/7t5r_protein.pdb structures/7T5R/7t5r_pocket.pdb structures/7T5R/7t5r_ligand.sdf structures/7T5R/7t5r_ligand.pdb structures/7T5R/7t5r_ligand.cif structures/7T5R/7t5r_complex.pdb structures/7T5R/7t5r_complex.cif 7T5S classic LpxA Pseudomonas aeruginosa Na Na H16 "[""F3R""]" 1 Kd Kd = = 35.2 ± 3.9 μM 35200.0 [] unit_conversion 4.453457336521869 success True direct_binding Surface plasmon resonance (SPR), dose-dependent titration against LpxA. 3 The text reports that H16 had a K_D of 35.2 ± 3.9 μM; page 9 maps 7T5S to H16. auto_single_measurement only accepted activity measurement [1] 1 structures\7T5S\7T5S_metadata.json point structures/7T5S/7t5s_protein.pdb structures/7T5S/7t5s_pocket.pdb structures/7T5S/7t5s_ligand.sdf structures/7T5S/7t5s_ligand.pdb structures/7T5S/7t5s_ligand.cif structures/7T5S/7t5s_complex.pdb structures/7T5S/7t5s_complex.cif 7T5Z classic LpxA Pseudomonas aeruginosa Na Na L8 "[""F6I""]" 1 Kd Kd = = 41.5 ± 4.8 μM 41500.0 [] unit_conversion 4.3819519032879075 success True direct_binding Surface plasmon resonance (SPR), concentration-dependent response curve. 4 Figure 4 reports L8 K_D = 41.5 ± 4.8 μM; page 9 maps 7T5Z to L8. auto_single_measurement only accepted activity measurement [1] 1 structures\7T5Z\7T5Z_metadata.json point structures/7T5Z/7t5z_protein.pdb structures/7T5Z/7t5z_pocket.pdb structures/7T5Z/7t5z_ligand.sdf structures/7T5Z/7t5z_ligand.pdb structures/7T5Z/7t5z_ligand.cif structures/7T5Z/7t5z_complex.pdb structures/7T5Z/7t5z_complex.cif 7T66 classic Chaetomium thermophilum ER alpha-glucosidase I (Ct alpha-GluI) Chaetomium thermophilum Ct alpha-GluI residues 33-827, with the transmembrane segment replaced by an N-terminal secretion signal, C-terminal His6 tag, and removed RDEL retention signal Na UV-4 "[""6A9""]" 1 IC50 IC50 = = 7.97 µM 7970.0 [] unit_conversion 5.098541678603888 success True biochemical_inhibition Purified recombinant Ct α-GluI 96-well enzymatic inhibition assay using a synthetic trisaccharide substrate and glucose oxidase reporter; Figure 2 reports UV-4 inhibition. 4 Figure 2C visibly prints “UV-4 7.97 µM”; its caption states that IC50 was determined from enzyme inhibition data. The paper identifies the Ct α-GluI–UV-4 complex as PDB 7T66. auto_single_measurement only accepted activity measurement [1] 1 structures\7T66\7T66_metadata.json point structures/7T66/7t66_protein.pdb structures/7T66/7t66_pocket.pdb structures/7T66/7t66_ligand.sdf structures/7T66/7t66_ligand.pdb structures/7T66/7t66_ligand.cif structures/7T66/7t66_complex.pdb structures/7T66/7t66_complex.cif 7T68 classic Chaetomium thermophilum ER alpha-glucosidase I (Ct alpha-GluI) Chaetomium thermophilum Ct alpha-GluI residues 33-827, with the transmembrane segment replaced by an N-terminal secretion signal, C-terminal His6 tag, and removed RDEL retention signal Na UV-5 "[""GII""]" 1 IC50 IC50 = = 1.88 µM 1880.0 [] unit_conversion 5.7258421507363195 success True biochemical_inhibition Purified recombinant Ct α-GluI 96-well enzymatic inhibition assay using a synthetic trisaccharide substrate and glucose oxidase reporter; Figure 2 reports UV-5 inhibition. 4 Figure 2D visibly prints “UV-5 1.88 µM”; its caption states that IC50 was determined from enzyme inhibition data. The paper identifies the Ct α-GluI–UV-5 complex as PDB 7T68. auto_single_measurement only accepted activity measurement [1] 1 structures\7T68\7T68_metadata.json point structures/7T68/7t68_protein.pdb structures/7T68/7t68_pocket.pdb structures/7T68/7t68_ligand.sdf structures/7T68/7t68_ligand.pdb structures/7T68/7t68_ligand.cif structures/7T68/7t68_complex.pdb structures/7T68/7t68_complex.cif 7T78 classic glucokinase (hexokinase 4) human Na Na compound 11 "[""G2T""]" 1 IC50 IC50 = = 122 nM 122.0 [] unit_conversion 6.913640169325252 success True direct_binding Fluorescence-polarization binding assay, 12 mM glucose; compound binding assessed by displacement of a fluorescently labeled compound-11 derivative from recombinant human hepatic GK. 13 Table 6 reports FB binding IC50/nM (12 mM glucose) of 122 for compound 11. The experimental section describes this as a fluorescence-polarization binding assay using recombinant human hepatic GK. auto_single_measurement only accepted activity measurement [1] 1 structures\7T78\7T78_metadata.json point structures/7T78/7t78_protein.pdb structures/7T78/7t78_pocket.pdb structures/7T78/7t78_ligand.sdf structures/7T78/7t78_ligand.pdb structures/7T78/7t78_ligand.cif structures/7T78/7t78_complex.pdb structures/7T78/7t78_complex.cif 7T79 classic glucokinase (hexokinase 4) human Na Na compound 31 (BMS-820132) "[""G1S""]" 1 IC50 IC50 = = 123 nM 123.0 [] unit_conversion 6.910094888560602 success True direct_binding Fluorescence-polarization binding assay, 12 mM glucose; compound binding assessed by displacement of a fluorescently labeled compound-11 derivative from recombinant human hepatic GK. 13 Table 6 reports FB binding IC50/nM (12 mM glucose) of 123 for compound 31. The experimental section describes this as a fluorescence-polarization binding assay using recombinant human hepatic GK. auto_single_measurement only accepted activity measurement [1] 1 structures\7T79\7T79_metadata.json point structures/7T79/7t79_protein.pdb structures/7T79/7t79_pocket.pdb structures/7T79/7t79_ligand.sdf structures/7T79/7t79_ligand.pdb structures/7T79/7t79_ligand.cif structures/7T79/7t79_complex.pdb structures/7T79/7t79_complex.cif 7T7H classic Vaccinia virus decapping enzyme D9 Vaccinia virus Na wild-type D9 CP-100356 "[""G7R""]" 1 IC50 IC50 = = 2.7 ± 0.7 µM 2700.0 [] unit_conversion 5.568636235841012 success True biochemical_inhibition Fluorescence-based D9 hydrolytic-activity assay using probe 1b; CP-100356 was a LOPAC screening hit and its IC50 was determined. 8 Table 2 lists CP-100356 monohydrochloride (P3_B7) with IC50 = 2.7 ± 0.7 µM; Figure 6/Table 3 map D9 + CP-100356 to PDB 7T7H. The text identifies the structure as wild-type D9 bound to CP-100356. auto_single_measurement only accepted activity measurement [1] 1 structures\7T7H\7T7H_metadata.json point structures/7T7H/7t7h_protein.pdb structures/7T7H/7t7h_pocket.pdb structures/7T7H/7t7h_ligand.sdf structures/7T7H/7t7h_ligand.pdb structures/7T7H/7t7h_ligand.cif structures/7T7H/7t7h_complex.pdb structures/7T7H/7t7h_complex.cif 7T8V classic Chaetomium thermophilum ER alpha-glucosidase I (Ct alpha-GluI) Chaetomium thermophilum Ct alpha-GluI residues 33-827, with the transmembrane segment replaced by an N-terminal secretion signal, C-terminal His6 tag, and removed RDEL retention signal Na EB-0159 "[""W9Y""]" 1 IC50 IC50 = = 19.49 µM 19490.0 [] unit_conversion 4.710188160882378 success True biochemical_inhibition Purified recombinant Ct α-GluI 96-well enzymatic inhibition assay using a synthetic trisaccharide substrate and glucose oxidase reporter; Figure 2 reports EB-0159 inhibition. 4 Figure 2E visibly prints “EB-0159 19.49 µM”; its caption states that IC50 was determined from enzyme inhibition data. The paper identifies the Ct α-GluI–EB-0159 complex as PDB 7T8V. auto_single_measurement only accepted activity measurement [1] 1 structures\7T8V\7T8V_metadata.json point structures/7T8V/7t8v_protein.pdb structures/7T8V/7t8v_pocket.pdb structures/7T8V/7t8v_ligand.sdf structures/7T8V/7t8v_ligand.pdb structures/7T8V/7t8v_ligand.cif structures/7T8V/7t8v_complex.pdb structures/7T8V/7t8v_complex.cif 7T8X classic M2 muscarinic receptor (M2R) Na ICL3-truncated M2Rmini with FLAG tag and C-terminal 8xHis tag Na acetylcholine (ACh) "[""ACH""]" 1 IC50 IC50 = = 67 nM 67.0 [] unit_conversion 7.173925197299173 success True direct_binding [3H]-NMS competition binding of M2R reconstituted into HDL particles, with GoA. 2 Fig. 1b prints “ACh+GoA IC50=67 nM”; its legend identifies ACh/Ixo competition curves of M2R reconstituted into HDL particles in the presence or absence of GoA. auto_single_measurement only accepted activity measurement [1] 1 structures\7T8X\7T8X_metadata.json point structures/7T8X/7t8x_protein.pdb structures/7T8X/7t8x_pocket.pdb structures/7T8X/7t8x_ligand.sdf structures/7T8X/7t8x_ligand.pdb structures/7T8X/7t8x_ligand.cif structures/7T8X/7t8x_complex.pdb structures/7T8X/7t8x_complex.cif 7T90 classic M2 muscarinic receptor (M2R) Na ICL3-truncated M2Rmini with FLAG tag and C-terminal 8xHis tag Na acetylcholine (ACh) "[""ACH""]" 1 IC50 IC50 = = 67 nM 67.0 [] unit_conversion 7.173925197299173 success True direct_binding [3H]-NMS competition binding of M2R reconstituted into HDL particles, with GoA. 2 Fig. 1b prints “ACh+GoA IC50=67 nM”; its legend identifies ACh/Ixo competition curves of M2R reconstituted into HDL particles in the presence or absence of GoA. auto_single_measurement only accepted activity measurement [1] 1 structures\7T90\7T90_metadata.json point structures/7T90/7t90_protein.pdb structures/7T90/7t90_pocket.pdb structures/7T90/7t90_ligand.sdf structures/7T90/7t90_ligand.pdb structures/7T90/7t90_ligand.cif structures/7T90/7t90_complex.pdb structures/7T90/7t90_complex.cif 7TA3 extended TNF-alpha monomer Na Na Na alpha-peptide 3 "[""CHAIN:A"", ""CHAIN:C""]" 1 Kd Kd = = 2.1 ± 0.5 µM 2100.0 [] unit_conversion 5.6777807052660805 success True direct_binding ITC of α-peptide 3 with TNFα in PBS containing 0.05% TWEEN-20; 1:1 binding stoichiometry reported. 4 “Analysis of the ITC data revealed a 1:1 binding stoichiometry (N = 0.93 ± 0.09), and an apparent K_D of 2.1 ± 0.5 μM.” Figure 4 maps the TNFα+3 structure to PDB ID 7TA3. auto_single_measurement only accepted activity measurement [1] 1 structures\7TA3\7TA3_metadata.json point structures/7TA3/7ta3_protein.pdb structures/7TA3/7ta3_pocket.pdb structures/7TA3/7ta3_ligand.pdb structures/7TA3/7ta3_ligand.cif structures/7TA3/7ta3_complex.pdb structures/7TA3/7ta3_complex.cif 7TA6 extended TNF-alpha monomer Na Na Na unnatural alpha/beta-peptide 1 "[""POLYMER_ENTITY:2""]" 1 IC50 IC50 = = 11 nM 11.0 [] unit_conversion 7.958607314841775 success True biochemical_inhibition TNFα–TNFR1 ELISA biochemical inhibition assay. 2 Figure 1a labels “TNFα-TNFR1 ELISA IC50 (nM)” and reports 11 for “α/β-Pep 1.” Figure 2 maps α/β-peptide 1 bound to TNFα to PDB ID 7TA6. auto_single_measurement only accepted activity measurement [1] 1 structures\7TA6\7TA6_metadata.json point structures/7TA6/7ta6_protein.pdb structures/7TA6/7ta6_pocket.pdb structures/7TA6/7ta6_ligand.pdb structures/7TA6/7ta6_ligand.cif structures/7TA6/7ta6_complex.pdb structures/7TA6/7ta6_complex.cif 7TAK classic PurT_Cp Colwellia psychrerythraea N-terminal deca-histidine-tagged PurT_Cp from strain 34H Na guanine nucleobase "[""GUN""]" 1 Kd Kd = = 3.02 ± 0.33 μM 3020.0 [] unit_conversion 5.51999305704285 success True direct_binding Scintillation proximity assay of purified His-tagged PurT_Cp; guanine binding, Fig. 1C. 3 Fig. 1 legend: “Data … yielded a dissociation constant (Kd) for … guanine binding of 3.02 ± 0.33 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7TAK\7TAK_metadata.json point structures/7TAK/7tak_protein.pdb structures/7TAK/7tak_pocket.pdb structures/7TAK/7tak_ligand.sdf structures/7TAK/7tak_ligand.pdb structures/7TAK/7tak_ligand.cif structures/7TAK/7tak_complex.pdb structures/7TAK/7tak_complex.cif 7TB1 extended STUB1 Na recombinant STUB1 (GGGGG-aa25-aa153) Na peptide 1 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 160 nM 160.0 [] unit_conversion 6.795880017344075 success True direct_binding Isothermal titration calorimetry (ITC) validation of peptide 1 binding to STUB1. 3 Table 1 reports peptide 1 with K_D (nM, ITC) = 160; Figure 3 identifies peptide 1 bound to STUB1 as PDB ID 7TB1. auto_single_measurement only accepted activity measurement [1] 1 structures\7TB1\7TB1_metadata.json point structures/7TB1/7tb1_protein.pdb structures/7TB1/7tb1_pocket.pdb structures/7TB1/7tb1_ligand.pdb structures/7TB1/7tb1_ligand.cif structures/7TB1/7tb1_complex.pdb structures/7TB1/7tb1_complex.cif 7TCQ extended Neutralizing antibody WS6 Fab mouse Fab WS6 Na SARS-CoV-2 S2 peptide Ac-FKEELDKYFK-biotin-PEG "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 22 nM 22.0 [] unit_conversion 7.657577319177793 success True direct_binding Isothermal titration calorimetry (ITC) of WS6 with SARS-CoV-2 S2 peptides. 8 The paper states that ITC measured KDs of 22 and 0.25 nM for the short and long SARS-CoV-2 peptides, respectively. The crystallized peptide is the 10-residue acetylated, biotin-PEGylated S2 peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7TCQ\7TCQ_metadata.json point structures/7TCQ/7tcq_protein.pdb structures/7TCQ/7tcq_pocket.pdb structures/7TCQ/7tcq_ligand.pdb structures/7TCQ/7tcq_ligand.cif structures/7TCQ/7tcq_complex.pdb structures/7TCQ/7tcq_complex.cif 7TEK classic SARS-CoV-2 3CLpro SARS-CoV-2 Na Na Compound 7; N-(4-(1H-pyrazol-4-yl)phenyl)-N-(3-chlorobenzyl)-2-(pyridin-3-yl)acetamide "[""I2D""]" 1 IC50 IC50 = = 1.27 ± 0.31 µM 1270.0 [] unit_conversion 5.896196279044043 success True biochemical_inhibition SARS-CoV-2 3CLpro biochemical assay inhibition; values are averages of at least three independent assays, each run as technical duplicates. 4 Table 1 reports compound 7, SARS-CoV-2 3CLpro IC50 = 1.27 ± 0.31 µM; table footnote identifies the biochemical inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7TEK\7TEK_metadata.json point structures/7TEK/7tek_protein.pdb structures/7TEK/7tek_pocket.pdb structures/7TEK/7tek_ligand.sdf structures/7TEK/7tek_ligand.pdb structures/7TEK/7tek_ligand.cif structures/7TEK/7tek_complex.pdb structures/7TEK/7tek_complex.cif 7TF6 extended glutamine synthetase (GS) Staphylococcus aureus Na Na Q-GlnR peptide (12) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 7.2 ± 0.3 μM 7200.0 [] unit_conversion 5.142667503568731 success True direct_binding Fluorescence-polarization binding of fluorescently labeled GlnR C-tail peptide to FBI-GS. 3 Figure 1B reports a Kd of 7.2 ± 0.3 μM for Sa FBI-GS binding its corresponding fluorescent GlnR C-tail peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7TF6\7TF6_metadata.json point structures/7TF6/7tf6_protein.pdb structures/7TF6/7tf6_pocket.pdb structures/7TF6/7tf6_ligand.pdb structures/7TF6/7tf6_ligand.cif structures/7TF6/7tf6_complex.pdb structures/7TF6/7tf6_complex.cif 7TF9 extended glutamine synthetase (GS) Listeria monocytogenes Na Na Q-GlnR peptide (14) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 27.2 ± 3.4 μM 27200.0 [] unit_conversion 4.565431095965801 success True direct_binding Fluorescence-polarization binding of fluorescently labeled GlnR C-tail peptide to FBI-GS. 3 Figure 1B reports a Kd of 27.2 ± 3.4 μM for Lm FBI-GS binding its corresponding fluorescent GlnR C-tail peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7TF9\7TF9_metadata.json point structures/7TF9/7tf9_protein.pdb structures/7TF9/7tf9_pocket.pdb structures/7TF9/7tf9_ligand.pdb structures/7TF9/7tf9_ligand.cif structures/7TF9/7tf9_complex.pdb structures/7TF9/7tf9_complex.cif 7TFA extended glutamine synthetase (GS) Paenibacillus polymyxa Na Na P. polymyxa GlnR C-tail peptide "[""CHAIN:A"", ""CHAIN:C"", ""CHAIN:D"", ""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I"", ""CHAIN:M"", ""CHAIN:N"", ""CHAIN:O"", ""CHAIN:P"", ""CHAIN:U"", ""CHAIN:V""]" 1 Kd Kd = = 18.7 ± 3.3 μM 18700.0 [] unit_conversion 4.728158393463501 success True direct_binding Fluorescence-polarization binding of fluorescently labeled Pp GlnR C-tail peptide to FBI-GS. 3 Figure 1B reports a Kd of 18.7 ± 3.3 μM for Pp FBI-GS binding its corresponding fluorescent GlnR C-tail peptide, but does not specify whether the assayed peptide is the 12- or 14-residue structural peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7TFA\7TFA_metadata.json point structures/7TFA/7tfa_protein.pdb structures/7TFA/7tfa_pocket.pdb structures/7TFA/7tfa_ligand.pdb structures/7TFA/7tfa_ligand.cif structures/7TFA/7tfa_complex.pdb structures/7TFA/7tfa_complex.cif 7TFB extended glutamine synthetase (GS) Paenibacillus polymyxa Na Na P. polymyxa GlnR C-tail peptide "[""CHAIN:A"", ""CHAIN:C"", ""CHAIN:E"", ""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I"", ""CHAIN:M"", ""CHAIN:O"", ""CHAIN:P"", ""CHAIN:Q"", ""CHAIN:R"", ""CHAIN:W"", ""CHAIN:X""]" 1 Kd Kd = = 18.7 ± 3.3 μM 18700.0 [] unit_conversion 4.728158393463501 success True direct_binding Fluorescence-polarization binding of fluorescently labeled Pp GlnR C-tail peptide to FBI-GS. 3 Figure 1B reports a Kd of 18.7 ± 3.3 μM for Pp FBI-GS binding its corresponding fluorescent GlnR C-tail peptide, but does not specify whether the assayed peptide is the 12- or 14-residue structural peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7TFB\7TFB_metadata.json point structures/7TFB/7tfb_protein.pdb structures/7TFB/7tfb_pocket.pdb structures/7TFB/7tfb_ligand.pdb structures/7TFB/7tfb_ligand.cif structures/7TFB/7tfb_complex.pdb structures/7TFB/7tfb_complex.cif 7TFC extended glutamine synthetase (GS) Bacillus subtilis Na Na Q-GlnR peptide (14) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 4.2 ± 0.3 μM 4200.0 [] unit_conversion 5.376750709602099 success True direct_binding Fluorescence-polarization binding of fluorescently labeled GlnR C-tail peptide to FBI-GS. 3 Figure 1B reports a Kd of 4.2 ± 0.3 μM for Bs FBI-GS binding its corresponding fluorescent GlnR C-tail peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\7TFC\7TFC_metadata.json point structures/7TFC/7tfc_protein.pdb structures/7TFC/7tfc_pocket.pdb structures/7TFC/7tfc_ligand.pdb structures/7TFC/7tfc_ligand.cif structures/7TFC/7tfc_complex.pdb structures/7TFC/7tfc_complex.cif 7THS classic mu-plasmin (microplasmin) human serine protease domain, residues 540-791 Ser195(741)Ala inhibitor 9 "[""I5Y""]" 1 Ki Ki = = 1.95 ± 0.02 nM 1.95 [] unit_conversion 8.709965388637482 success True biochemical_inhibition Slow-binding enzyme-kinetic inhibition measurement with plasmin; Table 2. 6 Table 2 reports inhibitor 9 plasmin Ki = 1.95 ± 0.02 nM. The crystallography section identifies the PDB construct as Ser195(741)Ala μ-plasmin, but the kinetic assay does not establish this mutation. auto_single_measurement only accepted activity measurement [1] 1 structures\7THS\7THS_metadata.json point structures/7THS/7ths_protein.pdb structures/7THS/7ths_pocket.pdb structures/7THS/7ths_ligand.sdf structures/7THS/7ths_ligand.pdb structures/7THS/7ths_ligand.cif structures/7THS/7ths_complex.pdb structures/7THS/7ths_complex.cif 7TJC classic VHH Chl-B2 Na Na Na chloramphenicol "[""CLM""]" 2 Kd Kd = = 0.94 µM 940.0 [] unit_conversion 6.026872146400301 success True direct_binding Isothermal titration calorimetry of VHH Chl-B2 binding chloramphenicol. 8 Table 2 lists the chloramphenicol Kd for B2 as 0.94 µM; the preceding ITC results identify B2 as Chl-B2. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7TJC\7TJC_metadata.json point structures/7TJC/7tjc_protein.pdb structures/7TJC/7tjc_pocket.pdb structures/7TJC/7tjc_ligand.sdf structures/7TJC/7tjc_ligand.pdb structures/7TJC/7tjc_ligand.cif structures/7TJC/7tjc_complex.pdb structures/7TJC/7tjc_complex.cif 7TL7 extended independent phosphoglycerate mutase (iPGM) C. elegans residues M19-I539 with a C-terminal hexahistidine tag Na Sa-D2 macrocyclic peptide inhibitor "[""CHAIN:A"", ""CHAIN:B"", ""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 1.8 nM 1.8 [] unit_conversion 8.744727494896694 success True direct_binding SPR binding kinetics of Sa-D2 to C. elegans iPGM. 5 “The Sa-D2–C. elegans iPGM binding kinetics were determined by SPR as K_D = 1.8 nM and t_1/2 = 15 min (Figure 3b).” auto_single_measurement only accepted activity measurement [1] 1 structures\7TL7\7TL7_metadata.json point structures/7TL7/7tl7_protein.pdb structures/7TL7/7tl7_pocket.pdb structures/7TL7/7tl7_ligand.pdb structures/7TL7/7tl7_ligand.cif structures/7TL7/7tl7_complex.pdb structures/7TL7/7tl7_complex.cif 7TL8 extended independent phosphoglycerate mutase (iPGM) S. aureus residues M26-H538 with a C-terminal hexahistidine tag Na Sa-D3 macrocyclic peptide inhibitor "[""CHAIN:B""]" 1 Kd Kd = = 790 nM 790.0 [] unit_conversion 6.102372908709558 success True direct_binding SPR binding kinetics of Sa-D3 to S. aureus iPGM. 5 “the non-thiolate-containing inhibitor Sa-D3, which functionally inhibits (Table 1) and displays measurable binding kinetics (K_D = 790 nM, t_1/2 = 27 s; Figure 3e)” auto_single_measurement only accepted activity measurement [1] 1 structures\7TL8\7TL8_metadata.json point structures/7TL8/7tl8_protein.pdb structures/7TL8/7tl8_pocket.pdb structures/7TL8/7tl8_ligand.pdb structures/7TL8/7tl8_ligand.cif structures/7TL8/7tl8_complex.pdb structures/7TL8/7tl8_complex.cif 7TO5 classic HIV-1 protease HIV-1 Na wild type GRL-05816A (inhibitor 4b) "[""G8R""]" 1 Ki Ki = = 0.32 nM 0.32 [] unit_conversion 9.494850021680094 success True biochemical_inhibition HIV-1 protease inhibition assay; Table 1. 4 Table 1 lists inhibitor 4b with Ki 0.32 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7TO5\7TO5_metadata.json point structures/7TO5/7to5_protein.pdb structures/7TO5/7to5_pocket.pdb structures/7TO5/7to5_ligand.sdf structures/7TO5/7to5_ligand.pdb structures/7TO5/7to5_ligand.cif structures/7TO5/7to5_complex.pdb structures/7TO5/7to5_complex.cif 7TO6 classic HIV-1 protease HIV-1 Na wild type GRL-01717A (inhibitor 5d) "[""G77""]" 1 Ki Ki = = 18.6 pM 0.018600000000000002 [] unit_conversion 10.730487055782083 success True biochemical_inhibition HIV-1 protease inhibition assay; Table 2. 5 Table 2 lists inhibitor 5d with Ki 18.6 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\7TO6\7TO6_metadata.json point structures/7TO6/7to6_protein.pdb structures/7TO6/7to6_pocket.pdb structures/7TO6/7to6_ligand.sdf structures/7TO6/7to6_ligand.pdb structures/7TO6/7to6_ligand.cif structures/7TO6/7to6_complex.pdb structures/7TO6/7to6_complex.cif 7TO7 extended BRD3 human BRD3 BD1 residues 25-147 Na RaPID linear peptide 1xAcK.4XE (monoAcK.4xE) "[""CHAIN:C"", ""CHAIN:F""]" 1 Kd Kd > > 200 µM 200000.0 [] unit_conversion 3.6989700043360187 success True direct_binding SPR; C-terminally biotinylated 1AcK.4E immobilized and unlabelled BRD3-BD1 flowed over the chip. 5 Table 1 reports BRD3-BD1 SPR K_D >200 µM for 1AcK.4E. auto_single_measurement only accepted activity measurement [1] 1 structures\7TO7\7TO7_metadata.json point structures/7TO7/7to7_protein.pdb structures/7TO7/7to7_pocket.pdb structures/7TO7/7to7_ligand.pdb structures/7TO7/7to7_ligand.cif structures/7TO7/7to7_complex.pdb structures/7TO7/7to7_complex.cif 7TOQ extended Mammalian 80S ribosome Oryctolagus cuniculus Na Na poly-PR (PR20) "[""CHAIN:PR""]" 1 IC50 IC50 = = 0.98 ± 0.10 µM 980.0 [] unit_conversion 6.008773924307505 success True biochemical_inhibition Nanluciferase translation assay in rabbit reticulocyte lysate; PR20 was added 300–400 s after nanoluciferase mRNA, after translation initiation, measuring elongation-associated inhibition. 3 Fig. 1b prints “IC50 = 0.98±0.10 µM” for +PR20; the Fig. 1 caption identifies this as translation inhibition by PR20 after mRNA addition. auto_single_measurement only accepted activity measurement [1] 1 structures\7TOQ\7TOQ_metadata.json point structures/7TOQ/7toq_ligand.cif structures/7TOQ/7toq_complex.cif 7TOS extended E. coli 70S ribosome Escherichia coli MRE600 Na Na PR20 "[""CHAIN:PR""]" 1 Ki Ki = = 44 ± 9 nM 44.0 [] unit_conversion 7.356547323513812 success True biochemical_inhibition Puromycin peptide-bond-formation assay using E. coli ribosome-catalyzed peptidyl transfer. 4 The text states that PR20 and GR20 strongly inhibit the reaction with apparent inhibition constants (Ki) of “44 ± 9 nM and 164 ± 31 nM, respectively” in the E. coli ribosome-catalyzed peptidyl-transfer assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7TOS\7TOS_metadata.json point structures/7TOS/7tos_ligand.cif structures/7TOS/7tos_complex.cif 7TP5 classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na T252E 4-ethylthiobenzoic acid "[""81M""]" 1 Kd Kd = = 0.02 ± 0.06 µM 20.0 [] unit_conversion 7.698970004336019 success True direct_binding UV-vis substrate-binding/Soret-shift analysis; Table 1. 7 Table 1 reports Kd = 0.02 ± 0.06 µM for 4-ethylthioBA/T252E. auto_single_measurement only accepted activity measurement [1] 1 structures\7TP5\7TP5_metadata.json point structures/7TP5/7tp5_protein.pdb structures/7TP5/7tp5_pocket.pdb structures/7TP5/7tp5_ligand.sdf structures/7TP5/7tp5_ligand.pdb structures/7TP5/7tp5_ligand.cif structures/7TP5/7tp5_complex.pdb structures/7TP5/7tp5_complex.cif 7TP6 classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na T252E 4-methylthiobenzoic acid "[""4MI""]" 1 Kd Kd = = 0.1 ± 0.1 µM 100.0 [] unit_conversion 7.0 success True direct_binding UV-vis substrate-binding/Soret-shift analysis; Table 1. 7 Table 1 reports Kd = 0.1 ± 0.1 µM for 4-methylthioBA/T252E. auto_single_measurement only accepted activity measurement [1] 1 structures\7TP6\7TP6_metadata.json point structures/7TP6/7tp6_protein.pdb structures/7TP6/7tp6_pocket.pdb structures/7TP6/7tp6_ligand.sdf structures/7TP6/7tp6_ligand.pdb structures/7TP6/7tp6_ligand.cif structures/7TP6/7tp6_complex.pdb structures/7TP6/7tp6_complex.cif 7TQM classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na D251N 4-methylthiobenzoic acid "[""4MI""]" 1 Kd Kd = = 0.83 ± 0.08 µM 830.0 [] unit_conversion 6.080921907623926 success True direct_binding UV-vis substrate-binding/Soret-shift analysis; Table 1. 7 Table 1 reports Kd = 0.83 ± 0.08 µM for 4-methylthioBA/D251N. auto_single_measurement only accepted activity measurement [1] 1 structures\7TQM\7TQM_metadata.json point structures/7TQM/7tqm_protein.pdb structures/7TQM/7tqm_pocket.pdb structures/7TQM/7tqm_ligand.sdf structures/7TQM/7tqm_ligand.pdb structures/7TQM/7tqm_ligand.cif structures/7TQM/7tqm_complex.pdb structures/7TQM/7tqm_complex.cif 7TRL extended BIRC2 human Na Na histone H3 "[""CHAIN:B""]" 1 Kd Kd = = 340 ± 44 nM 340.0 [] unit_conversion 6.468521082957745 success True direct_binding Microscale thermophoresis binding curve with fluorescently labeled H3 peptide. 3 The BIRC2_BIR3 + H3_1–12 MST plot prints Kd = 340 ± 44 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7TRL\7TRL_metadata.json point structures/7TRL/7trl_protein.pdb structures/7TRL/7trl_pocket.pdb structures/7TRL/7trl_ligand.pdb structures/7TRL/7trl_ligand.cif structures/7TRL/7trl_complex.pdb structures/7TRL/7trl_complex.cif 7TRT classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na Na 4-(furan-2-yl)benzoic acid "[""KQF""]" 1 Kd Kd = = 2.7 ± 0.3 μM 2700.0 [] unit_conversion 5.568636235841012 success True direct_binding UV-vis titration of substrate binding to CYP199A4. 3 Table 1 reports Kd 2.7 ± 0.3 μM for 4-(furan-2-yl)benzoic acid; the text identifies this as UV-vis-measured dissociation constant. Figure 7 and the crystal-structure text map this ligand complex to PDB 7TRT. auto_single_measurement only accepted activity measurement [1] 1 structures\7TRT\7TRT_metadata.json point structures/7TRT/7trt_protein.pdb structures/7TRT/7trt_pocket.pdb structures/7TRT/7trt_ligand.sdf structures/7TRT/7trt_ligand.pdb structures/7TRT/7trt_ligand.cif structures/7TRT/7trt_complex.pdb structures/7TRT/7trt_complex.cif 7TRU classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na WT 4-(thiophen-2-yl)benzoic acid "[""KQR""]" 1 Kd Kd = = 0.60 ± 0.10 μM 600.0 [] unit_conversion 6.221848749616356 success True direct_binding UV-vis titration of substrate binding to CYP199A4. 3 Table 1 reports Kd 0.60 ± 0.10 μM for 4-(thiophen-2-yl)benzoic acid; the text identifies this as UV-vis-measured dissociation constant. Figure 8 and the crystal-structure text map this ligand complex to PDB 7TRU. auto_single_measurement only accepted activity measurement [1] 1 structures\7TRU\7TRU_metadata.json point structures/7TRU/7tru_protein.pdb structures/7TRU/7tru_pocket.pdb structures/7TRU/7tru_ligand.sdf structures/7TRU/7tru_ligand.pdb structures/7TRU/7tru_ligand.cif structures/7TRU/7tru_complex.pdb structures/7TRU/7tru_complex.cif 7TTI classic potassium-chloride cotransporter 1 (KCC1) human full-length human KCC1 isoform A Na VU0463271 "[""JUX""]" 1 IC50 IC50 = = 69.80 nM 69.8 [] unit_conversion 7.156144577376839 success True biochemical_inhibition Proteoliposome thallium influx assay of wild-type human KCC1; inhibition by VU0463271. 3 Fig. 2D prints: “WT IC50 = 69.80 nM”; the caption states wild-type KCC1 is inhibited by VU0463271 with an IC50 of 69.8 nM in liposomes. auto_single_measurement only accepted activity measurement [1] 1 structures\7TTI\7TTI_metadata.json point structures/7TTI/7tti_protein.pdb structures/7TTI/7tti_pocket.pdb structures/7TTI/7tti_ligand.sdf structures/7TTI/7tti_ligand.pdb structures/7TTI/7tti_ligand.cif structures/7TTI/7tti_complex.pdb structures/7TTI/7tti_complex.cif 7TTQ classic OxyA_kis Na Na Na imidazole "[""IMD""]" 1 Kd Kd = = 121.1 ± 2.3 µM 121100.0 [] unit_conversion 3.916855856856948 success True direct_binding UV–Visible spectroscopic azole-binding assay; one-site binding model. 7 Figure 5D reports imidazole binding to OxyA_kis with Kd = 121.1 ± 2.3 µM; the figure caption states Kd values were derived from the one-site binding model. auto_single_measurement only accepted activity measurement [1] 1 structures\7TTQ\7TTQ_metadata.json point structures/7TTQ/7ttq_protein.pdb structures/7TTQ/7ttq_pocket.pdb structures/7TTQ/7ttq_ligand.sdf structures/7TTQ/7ttq_ligand.pdb structures/7TTQ/7ttq_ligand.cif structures/7TTQ/7ttq_complex.pdb structures/7TTQ/7ttq_complex.cif 7TTV classic E. coli DsbA Escherichia coli Na Na 4-phenyl-2-(3-phenylpropyl)thiazole-5-carboxylic acid (phenylthiazole 1) "[""QVP""]" 1 Kd Kd = = 0.9 mM 900000.0 [] unit_conversion 3.045757490560675 success True direct_binding Chemical-shift perturbations measured in HSQC spectra with increasing ligand concentration; Kd calculated using a ligand-depletion model. 2 “The ligand affinity (Kd) was estimated at 0.9 mM based on chemical shift perturbations measured in HSQC spectra recorded with increasing ligand concentration.” auto_single_measurement only accepted activity measurement [1] 1 structures\7TTV\7TTV_metadata.json point structures/7TTV/7ttv_protein.pdb structures/7TTV/7ttv_pocket.pdb structures/7TTV/7ttv_ligand.sdf structures/7TTV/7ttv_ligand.pdb structures/7TTV/7ttv_ligand.cif structures/7TTV/7ttv_complex.pdb structures/7TTV/7ttv_complex.cif 7TUQ extended BRD4 bromodomain 1 Na BRD4 BD1 residues 43-180 Na Monoacetylated SARS-CoV-2 E K63ac peptide (aa 60-68) "[""CHAIN:C""]" 1 Kd Kd = = 660 μM 660000.0 [] unit_conversion 3.1804560644581317 success True direct_binding Chemical-shift perturbation (NMR) analysis of BRD4 BD1 with monoacetylated SARS-CoV-2 E K63ac peptide. 4 “BD1 selected for acetylated K63 (Kd = 660 μM)” after CSP analysis of BRD4 BDs with acetylated SARS-CoV-2 E peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\7TUQ\7TUQ_metadata.json point structures/7TUQ/7tuq_protein.pdb structures/7TUQ/7tuq_pocket.pdb structures/7TUQ/7tuq_ligand.pdb structures/7TUQ/7tuq_ligand.cif structures/7TUQ/7tuq_complex.pdb structures/7TUQ/7tuq_complex.cif 7TV0 extended BRD4 bromodomain 1 Na BRD4 BD1 residues 43-180 Na Dual-acetylated SARS-CoV-2 E K53ac/K63ac peptide (aa 53-64) "[""CHAIN:E"", ""CHAIN:G""]" 1 Kd Kd = = 36 μM 36000.0 [] unit_conversion 4.443697499232713 success True direct_binding Chemical-shift perturbation (NMR) analysis of BRD4 BD1 with diacetylated SARS-CoV-2 E K53ac/K63ac peptide. 4 “Binding affinity of BD1 for SARS-CoV-2 E K53ac/K63ac, measured via CSP analysis, was found to be 36 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7TV0\7TV0_metadata.json point structures/7TV0/7tv0_protein.pdb structures/7TV0/7tv0_pocket.pdb structures/7TV0/7tv0_ligand.pdb structures/7TV0/7tv0_ligand.cif structures/7TV0/7tv0_complex.pdb structures/7TV0/7tv0_complex.cif 7TW7 classic SARS-CoV-2 nsp14 N7-methyltransferase domain fused with TELSAM SARS-CoV-2 nsp14 MTase residues 300-527 fused to TELSAM residues 47-124; N-terminal 6xHis-SUMO tag Na SAM "[""SAM""]" 1 Kd Kd = = 25 µM 25000.0 [] unit_conversion 4.6020599913279625 success True direct_binding ITC analysis of the TEL-MTase fusion. 12 Extended Data Fig. 6a reports TEL-MTase binding to SAM with K_D 25 µM. Page 5 maps TELSAM-MTase-SAM to PDB 7TW7. auto_single_measurement only accepted activity measurement [1] 1 structures\7TW7\7TW7_metadata.json point structures/7TW7/7tw7_protein.pdb structures/7TW7/7tw7_pocket.pdb structures/7TW7/7tw7_ligand.sdf structures/7TW7/7tw7_ligand.pdb structures/7TW7/7tw7_ligand.cif structures/7TW7/7tw7_complex.pdb structures/7TW7/7tw7_complex.cif 7TW8 classic SARS-CoV-2 nsp14 N7-methyltransferase domain fused with TELSAM SARS-CoV-2 nsp14 MTase residues 300-527 fused to TELSAM residues 47-124; N-terminal 6xHis-SUMO tag Na SAH "[""SAH""]" 1 Kd Kd = = 5 µM 5000.0 [] unit_conversion 5.301029995663981 success True direct_binding ITC analysis of the TEL-MTase fusion. 12 Extended Data Fig. 6a reports TEL-MTase binding to SAH with K_D 5 µM. Page 5 maps TELSAM-MTase-SAH to PDB 7TW8. auto_single_measurement only accepted activity measurement [1] 1 structures\7TW8\7TW8_metadata.json point structures/7TW8/7tw8_protein.pdb structures/7TW8/7tw8_pocket.pdb structures/7TW8/7tw8_ligand.sdf structures/7TW8/7tw8_ligand.pdb structures/7TW8/7tw8_ligand.cif structures/7TW8/7tw8_complex.pdb structures/7TW8/7tw8_complex.cif 7TW9 classic SARS-CoV-2 nsp14 N7-methyltransferase domain fused with TELSAM SARS-CoV-2 nsp14 MTase residues 300-527 fused to TELSAM residues 47-124; N-terminal 6xHis-SUMO tag Na Sinefungin (SFG) "[""SFG""]" 1 Kd Kd = = 22 µM 22000.0 [] unit_conversion 4.657577319177793 success True direct_binding ITC analysis of the TEL-MTase fusion. 12 Extended Data Fig. 6a reports TEL-MTase binding to sinefungin with K_D 22 µM. Page 5 maps TELSAM-MTase-SFG to PDB 7TW9. auto_single_measurement only accepted activity measurement [1] 1 structures\7TW9\7TW9_metadata.json point structures/7TW9/7tw9_protein.pdb structures/7TW9/7tw9_pocket.pdb structures/7TW9/7tw9_ligand.sdf structures/7TW9/7tw9_ligand.pdb structures/7TW9/7tw9_ligand.cif structures/7TW9/7tw9_complex.pdb structures/7TW9/7tw9_complex.cif 7TXT extended human serotonin transporter (SERT) human DeltaN72/DeltaC13 N- and C-terminally truncated human wild-type SERT, nanodisc-reconstituted and complexed with Fab15B8 wild-type '8090 "[""KWC""]" 1 Ki Ki = = 14 nM 14.0 [] unit_conversion 7.853871964321762 success True direct_binding Radioligand-displacement affinity measurement during structure-guided optimization. 5 The paper states that optimized analog ‘8090 had a Ki of 14 nM; Figure 1D labels “Optimized lead Compound ‘8090 Ki = 14 nM.” The nearby SERT binding assay is [125I]β-CIT displacement. auto_single_measurement only accepted activity measurement [1] 1 structures\7TXT\7TXT_metadata.json point structures/7TXT/7txt_protein.pdb structures/7TXT/7txt_pocket.pdb structures/7TXT/7txt_ligand.pdb structures/7TXT/7txt_ligand.cif structures/7TXT/7txt_complex.pdb structures/7TXT/7txt_complex.cif 7TZ6 classic Bovine mitochondrial cytochrome bc1 complex (Btb c1) Bos taurus Na Na CK-2-68 "[""JHB""]" 1 IC50 IC50 = = 1.7 μM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition Dose-dependent inhibition of purified Btb c1 activity by CK-2-68. 4 Figure 3A labels Btb c1 (IC50=1.7 μM); the text identifies this as CK-2-68 inhibition of Btb c1. auto_single_measurement only accepted activity measurement [1] 1 structures\7TZ6\7TZ6_metadata.json point structures/7TZ6/7tz6_protein.pdb structures/7TZ6/7tz6_pocket.pdb structures/7TZ6/7tz6_ligand.sdf structures/7TZ6/7tz6_ligand.pdb structures/7TZ6/7tz6_ligand.cif structures/7TZ6/7tz6_complex.pdb structures/7TZ6/7tz6_complex.cif 7TZ7 classic PI3K alpha Na Na Na compound 40 "[""KVJ""]" 1 IC50 IC50 = = 12 ± 1.5 nM 12.0 [] unit_conversion 7.920818753952375 success True biochemical_inhibition Biochemical PI3K isoform profiling assay (Table 7). 11 Table 7 reports biochemical PI3Kα IC50 = 12 ± 1.5 nM for compound 40; the paper maps 7TZ7 to compound 40 bound in the PI3Kα kinase domain. auto_single_measurement only accepted activity measurement [1] 1 structures\7TZ7\7TZ7_metadata.json point structures/7TZ7/7tz7_protein.pdb structures/7TZ7/7tz7_pocket.pdb structures/7TZ7/7tz7_ligand.sdf structures/7TZ7/7tz7_ligand.pdb structures/7TZ7/7tz7_ligand.cif structures/7TZ7/7tz7_complex.pdb structures/7TZ7/7tz7_complex.cif 7TZZ classic Arabidopsis thaliana acetohydroxyacid synthase (AtAHAS) Arabidopsis thaliana Na P197T bispyribac-sodium (BS) "[""6QL""]" 1 Ki Ki = = 106 ± 4.8 nM 106.0 [] unit_conversion 6.97469413473523 success True biochemical_inhibition Ki of commercial herbicides measured for P197T AtAHAS mutant. 4 Table 1 reports BS Ki for P197T as 106 ± 4.8 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7TZZ\7TZZ_metadata.json point structures/7TZZ/7tzz_protein.pdb structures/7TZZ/7tzz_pocket.pdb structures/7TZZ/7tzz_ligand.sdf structures/7TZZ/7tzz_ligand.pdb structures/7TZZ/7tzz_ligand.cif structures/7TZZ/7tzz_complex.pdb structures/7TZZ/7tzz_complex.cif 7U1D classic Arabidopsis thaliana acetohydroxyacid synthase (AtAHAS) Arabidopsis thaliana Na P197T chlorimuron-ethyl (CE) "[""CIE""]" 1 Ki Ki = = 2200 ± 200 nM 2200.0 [] unit_conversion 5.657577319177793 success True biochemical_inhibition Ki of commercial herbicides measured for P197T AtAHAS mutant. 4 Table 1 reports CE Ki for P197T as 2200 ± 200 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7U1D\7U1D_metadata.json point structures/7U1D/7u1d_protein.pdb structures/7U1D/7u1d_pocket.pdb structures/7U1D/7u1d_ligand.sdf structures/7U1D/7u1d_ligand.pdb structures/7U1D/7u1d_ligand.cif structures/7U1D/7u1d_complex.pdb structures/7U1D/7u1d_complex.cif 7U25 classic Arabidopsis thaliana acetohydroxyacid synthase (AtAHAS) Arabidopsis thaliana Na W574L bispyribac-sodium (BS) "[""6QL""]" 1 Ki Ki = = 6100 ± 1000 nM 6100.0 [] unit_conversion 5.214670164989233 success True biochemical_inhibition Ki of commercial herbicides measured for W574L AtAHAS mutant. 4 Table 1 reports BS Ki for W574L as 6100 ± 1000 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7U25\7U25_metadata.json point structures/7U25/7u25_protein.pdb structures/7U25/7u25_pocket.pdb structures/7U25/7u25_ligand.sdf structures/7U25/7u25_ligand.pdb structures/7U25/7u25_ligand.cif structures/7U25/7u25_complex.pdb structures/7U25/7u25_complex.cif 7U2Z classic human GSK3B human Na Na G12 "[""L7C""]" 1 Kd Kd = = 66.5 ± 31.8 µM 66500.0 [] unit_conversion 4.1771783546968955 success True direct_binding Microscale thermophoresis (MST) binding affinity assay. 4 “A complete binding affinity curve was obtained only for the G12 compound with an affinity parameter (kd) of 66.5 ± 31.8 µM.” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7U2Z\7U2Z_metadata.json point structures/7U2Z/7u2z_protein.pdb structures/7U2Z/7u2z_pocket.pdb structures/7U2Z/7u2z_ligand.sdf structures/7U2Z/7u2z_ligand.pdb structures/7U2Z/7u2z_ligand.cif structures/7U2Z/7u2z_complex.pdb structures/7U2Z/7u2z_complex.cif 7U31 classic human GSK3B human Na Na G5 "[""L7I""]" 1 IC50 IC50 = = 14.81 ± 0.55 µM 14810.0 [] unit_conversion 4.829444941478791 success True biochemical_inhibition TR-FRET kinase inhibition dose-response assay using ULigth-GS substrate. 5 “IC50 values were (14.81 ± 0.55) µM and (15.25 ± 1.34) µM for G5 and G12, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7U31\7U31_metadata.json point structures/7U31/7u31_protein.pdb structures/7U31/7u31_pocket.pdb structures/7U31/7u31_ligand.sdf structures/7U31/7u31_ligand.pdb structures/7U31/7u31_ligand.cif structures/7U31/7u31_complex.pdb structures/7U31/7u31_complex.cif 7U33 classic human GSK3B human Na Na ARN9133 "[""L7R""]" 1 IC50 IC50 = = 27.2 µM 27200.0 [] unit_conversion 4.565431095965801 success True biochemical_inhibition GSK-3β inhibition dose-response assay for homologous compounds. 11 “Out of seven identified homologous, two compounds, ARN1484 and ARN9133 (Figure 13), showed a similar inhibitory activity (IC50) to G5 and G12 (38.1 µM and 27.2 µM, respectively; Figure 14).” auto_single_measurement only accepted activity measurement [1] 1 structures\7U33\7U33_metadata.json point structures/7U33/7u33_protein.pdb structures/7U33/7u33_pocket.pdb structures/7U33/7u33_ligand.sdf structures/7U33/7u33_ligand.pdb structures/7U33/7u33_ligand.cif structures/7U33/7u33_complex.pdb structures/7U33/7u33_complex.cif 7U36 classic human GSK3B human Na Na ARN1484 "[""L7W""]" 1 IC50 IC50 = = 38.1 µM 38100.0 [] unit_conversion 4.419075024324381 success True biochemical_inhibition GSK-3β inhibition dose-response assay for homologous compounds. 11 “Out of seven identified homologous, two compounds, ARN1484 and ARN9133 (Figure 13), showed a similar inhibitory activity (IC50) to G5 and G12 (38.1 µM and 27.2 µM, respectively; Figure 14).” auto_single_measurement only accepted activity measurement [1] 1 structures\7U36\7U36_metadata.json point structures/7U36/7u36_protein.pdb structures/7U36/7u36_pocket.pdb structures/7U36/7u36_ligand.sdf structures/7U36/7u36_ligand.pdb structures/7U36/7u36_ligand.cif structures/7U36/7u36_complex.pdb structures/7U36/7u36_complex.cif 7U3A classic Streptomyces venezuelae GlgX Streptomyces venezuelae Na Na c-di-GMP "[""C2E""]" 1 Kd Kd = = 8.3 μM 8300.0 [] unit_conversion 5.080921907623926 success True direct_binding Microscale thermophoresis of purified fluorescently labelled GlgX titrated with nonlabelled c-di-GMP. 6 “This experiment produced a Kd of 8.3 μM … which is in line with our FP data.” auto_single_measurement only accepted activity measurement [1] 1 structures\7U3A\7U3A_metadata.json point structures/7U3A/7u3a_protein.pdb structures/7U3A/7u3a_pocket.pdb structures/7U3A/7u3a_ligand.sdf structures/7U3A/7u3a_ligand.pdb structures/7U3A/7u3a_ligand.cif structures/7U3A/7u3a_complex.pdb structures/7U3A/7u3a_complex.cif 7U4C classic HtpG Borrelia burgdorferi N-terminal domain, residues 1-228 Na BX-2819 "[""819""]" 1 Kd Kd = = 12 ± 5.8 nM 12.0 [] unit_conversion 7.920818753952375 success True direct_binding FLECS/Hill-plot affinity determination using GFP-BbHtpG captured on immobilized ATP; n = 2, SDM. 3 Figure 1A prints “K_D BX-2819 12 ± 5.8 nM”; its caption identifies the graphs as Hill plots and states affinities were determined with respect to immobilized ATP using the Cheng-Prusoff equation. auto_single_measurement only accepted activity measurement [1] 1 structures\7U4C\7U4C_metadata.json point structures/7U4C/7u4c_protein.pdb structures/7U4C/7u4c_pocket.pdb structures/7U4C/7u4c_ligand.sdf structures/7U4C/7u4c_ligand.pdb structures/7U4C/7u4c_ligand.cif structures/7U4C/7u4c_complex.pdb structures/7U4C/7u4c_complex.cif 7U67 classic E. coli dGTPase (Dgt) E. coli Na Na GTP "[""GTP""]" 1 IC50 IC50 = = 310 ± 50 nM 310.0 [] unit_conversion 6.508638306165727 success True biochemical_inhibition GTP titration against a partially inhibited Dgt complex containing 100 nM Gp1.2, under apparent kcat conditions with 2 mM dGTP. 6 “Under these conditions, GTP inhibits the Dgt–Gp1.2 complex to completion with IC50 = 310 ± 50 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7U67\7U67_metadata.json point structures/7U67/7u67_protein.pdb structures/7U67/7u67_pocket.pdb structures/7U67/7u67_ligand.sdf structures/7U67/7u67_ligand.pdb structures/7U67/7u67_ligand.cif structures/7U67/7u67_complex.pdb structures/7U67/7u67_complex.cif 7U8H classic KRAS Na BIT-blocked KRAS G12V,C118S,S39C G12V; C118S; S39C compound 1 "[""LX6""]" 1 Kd Kd = = 116±19 µM 116000.0 [] unit_conversion 3.935542010773082 success True direct_binding HSQC-NMR direct-binding measurement on BIT-blocked KRAS construct. 2 Table 1 reports compound 1 HSQC Kd = 116±19 µM; Figure 1 identifies the BIT-blocked KRAS G12V,C118S,S39C screening construct. auto_single_measurement only accepted activity measurement [1] 1 structures\7U8H\7U8H_metadata.json point structures/7U8H/7u8h_protein.pdb structures/7U8H/7u8h_pocket.pdb structures/7U8H/7u8h_ligand.sdf structures/7U8H/7u8h_ligand.pdb structures/7U8H/7u8h_ligand.cif structures/7U8H/7u8h_complex.pdb structures/7U8H/7u8h_complex.cif 7U99 classic EGFR Na EGFR kinase domain spanning residues 696-1022 with a TEV-cleavable N-terminal 6xHis-GST fusion WT (wild type) 9d "[""M0R""]" 1 IC50 IC50 > > 100000 nM 100000.0 [] unit_conversion 4.0 success True biochemical_inhibition HTRF biochemical kinase-inhibition assay; Table 1 reports IC50 values from a 12-point dose-response curve (mean ± SD, n = 3 in triplicate). 4 Table 1, row 9d: EGFR WT IC50 >100000 nM. Footnote b states that IC50 values were determined using an HTRF assay in a 12-point dose-response curve. auto_single_measurement only accepted activity measurement [1] 1 structures\7U99\7U99_metadata.json point structures/7U99/7u99_protein.pdb structures/7U99/7u99_pocket.pdb structures/7U99/7u99_ligand.sdf structures/7U99/7u99_ligand.pdb structures/7U99/7u99_ligand.cif structures/7U99/7u99_complex.pdb structures/7U99/7u99_complex.cif 7U9A classic EGFR Na EGFR kinase domain spanning residues 696-1022 with a TEV-cleavable N-terminal 6xHis-GST fusion WT (wild type) 2f "[""M19""]" 1 IC50 IC50 = = 1795.3 ± 859.1 nM 1795.3 [] unit_conversion 5.7458629691145315 success True biochemical_inhibition HTRF biochemical kinase-inhibition assay; Table 1 reports IC50 values from a 12-point dose-response curve (mean ± SD, n = 3 in triplicate). 4 Table 1, row 2f: EGFR WT IC50 1795.3 ± 859.1 nM. Footnote b states that IC50 values were determined using an HTRF assay in a 12-point dose-response curve. auto_single_measurement only accepted activity measurement [1] 1 structures\7U9A\7U9A_metadata.json point structures/7U9A/7u9a_protein.pdb structures/7U9A/7u9a_pocket.pdb structures/7U9A/7u9a_ligand.sdf structures/7U9A/7u9a_ligand.pdb structures/7U9A/7u9a_ligand.cif structures/7U9A/7u9a_complex.pdb structures/7U9A/7u9a_complex.cif 7U9S classic human D-amino acid oxidase human Na Na compound 12 "[""M7I""]" 1 IC50 IC50 = = 0.34 µM 340.0 [] unit_conversion 6.468521082957745 success True biochemical_inhibition hDAO biochemical assay 3 Table 1 reports compound 12 hDAO IC50 = 0.34 µM; the figure caption on the same page maps compound 12 to PDB ID 7U9S. auto_single_measurement only accepted activity measurement [1] 1 structures\7U9S\7U9S_metadata.json point structures/7U9S/7u9s_protein.pdb structures/7U9S/7u9s_pocket.pdb structures/7U9S/7u9s_ligand.sdf structures/7U9S/7u9s_ligand.pdb structures/7U9S/7u9s_ligand.cif structures/7U9S/7u9s_complex.pdb structures/7U9S/7u9s_complex.cif 7U9U classic human D-amino acid oxidase human Na Na compound 59 "[""M89""]" 1 IC50 IC50 = = 0.020 µM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition hDAO biochemical assay 8 Table 7 reports compound 59 hDAO IC50 = 0.020 µM; Figure 4 caption maps compound 59 to hDAO PDB ID 7U9U. auto_single_measurement only accepted activity measurement [1] 1 structures\7U9U\7U9U_metadata.json point structures/7U9U/7u9u_protein.pdb structures/7U9U/7u9u_pocket.pdb structures/7U9U/7u9u_ligand.sdf structures/7U9U/7u9u_ligand.pdb structures/7U9U/7u9u_ligand.cif structures/7U9U/7u9u_complex.pdb structures/7U9U/7u9u_complex.cif 7UAF classic meprin alpha human active inhibitory complex, tetramer Na compound 10d; N3,N3-bis[(2H-1,3-benzodioxol-5-yl)methyl]-N-hydroxy-beta-alaninamide "[""M6X""]" 2 Ki Ki = = 180 nM 180.0 [] unit_conversion 6.7447274948966935 success True biochemical_inhibition Compound 10d is shown at the meprin alpha active site in the inhibitor-bound structural figure. 7 Figure 4 displays compound 10d at the active site with the printed label “Ki = 180 nM”; the caption identifies compound 10d as the prototype inhibitor. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7UAF\7UAF_metadata.json point structures/7UAF/7uaf_protein.pdb structures/7UAF/7uaf_pocket.pdb structures/7UAF/7uaf_ligand.sdf structures/7UAF/7uaf_ligand.pdb structures/7UAF/7uaf_ligand.cif structures/7UAF/7uaf_complex.pdb structures/7UAF/7uaf_complex.cif 7UAH classic mu-plasmin (microplasmin) human serine protease domain, residues 540-791 Ser195(741)Ala inhibitor 3 "[""M63""]" 1 Ki Ki = = 1.61 ± 0.03 nM 1.61 [] unit_conversion 8.79317412396815 success True biochemical_inhibition Slow-binding enzyme-kinetic inhibition measurement with plasmin; Table 1. 3 Table 1 reports inhibitor 3 plasmin Ki = 1.61 ± 0.03 nM. The crystallography section identifies the PDB construct as Ser195(741)Ala μ-plasmin, but the kinetic assay does not establish this mutation. auto_single_measurement only accepted activity measurement [1] 1 structures\7UAH\7UAH_metadata.json point structures/7UAH/7uah_protein.pdb structures/7UAH/7uah_pocket.pdb structures/7UAH/7uah_ligand.sdf structures/7UAH/7uah_ligand.pdb structures/7UAH/7uah_ligand.cif structures/7UAH/7uah_complex.pdb structures/7UAH/7uah_complex.cif 7UAT classic Escherichia coli pyridoxal 5'-phosphate homeostasis protein (YggS) Escherichia coli Na K36A PLP "[""PLP""]" 1 Kd Kd = = 124 ± 19 nM 124.0 [] unit_conversion 6.906578314837764 success True direct_binding Fluorimetric PLP-binding equilibrium analysis of purified K36A YggS. 4 Table 1 reports Kd = 124 ± 19 nM for K36A. auto_single_measurement only accepted activity measurement [1] 1 structures\7UAT\7UAT_metadata.json point structures/7UAT/7uat_protein.pdb structures/7UAT/7uat_pocket.pdb structures/7UAT/7uat_ligand.sdf structures/7UAT/7uat_ligand.pdb structures/7UAT/7uat_ligand.cif structures/7UAT/7uat_complex.pdb structures/7UAT/7uat_complex.cif 7UBO classic BRDT human first bromodomain of human BRDT Na CCD-956 "[""MJN""]" 2 Kd Kd = = 0.33 nM 0.33 [] unit_conversion 9.481486060122112 success True direct_binding BromoKdELECT assay 6 Table 3, compound binding constants determined by BromoKdELECT assay, reports BRDT-BD1 Kd = 0.33 nM for CDD-956. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7UBO\7UBO_metadata.json point structures/7UBO/7ubo_protein.pdb structures/7UBO/7ubo_pocket.pdb structures/7UBO/7ubo_ligand.sdf structures/7UBO/7ubo_ligand.pdb structures/7UBO/7ubo_ligand.cif structures/7UBO/7ubo_complex.pdb structures/7UBO/7ubo_complex.cif 7UBP classic Escherichia coli pyridoxal 5'-phosphate homeostasis protein (YggS) Escherichia coli Na K36A/K137A PLP "[""PLP""]" 1 Kd Kd = = 59 ± 10 nM 59.0 [] unit_conversion 7.229147988357855 success True direct_binding Fluorimetric PLP-binding equilibrium analysis of purified K36A/K137A YggS. 4 Table 1 reports Kd = 59 ± 10 nM for K36A/K137A. auto_single_measurement only accepted activity measurement [1] 1 structures\7UBP\7UBP_metadata.json point structures/7UBP/7ubp_protein.pdb structures/7UBP/7ubp_pocket.pdb structures/7UBP/7ubp_ligand.sdf structures/7UBP/7ubp_ligand.pdb structures/7UBP/7ubp_ligand.cif structures/7UBP/7ubp_complex.pdb structures/7UBP/7ubp_complex.cif 7UBQ classic Escherichia coli pyridoxal 5'-phosphate homeostasis protein (YggS) Escherichia coli Na wild-type PNP "[""PXP""]" 1 Kd Kd = = 31 ± 23 nM 31.0 [] unit_conversion 7.508638306165727 success True direct_binding Fluorimetric analysis of PNP binding to purified apo-YggS. 3 Binding of PNP to YggS was analyzed by the fluorimetric method, obtaining a Kd of 31 ± 23 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7UBQ\7UBQ_metadata.json point structures/7UBQ/7ubq_protein.pdb structures/7UBQ/7ubq_pocket.pdb structures/7UBQ/7ubq_ligand.sdf structures/7UBQ/7ubq_ligand.pdb structures/7UBQ/7ubq_ligand.cif structures/7UBQ/7ubq_complex.pdb structures/7UBQ/7ubq_complex.cif 7UBT classic STAT5A human STAT5A residues 136-705; N-terminal 6xHis-MBP-TEV fusion construct Na Compound 18 "[""MIW""]" 1 Ki Ki = = 1.8 ± 0.4 µM 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding Fluorescence-polarization competitive binding; Table 1 reports Ki values for STAT5A/5B/6 SH2-domain ligands. 2 Table 1 lists Compound 18 Ki values: STAT5A 1.8 ± 0.4 µM, STAT5B 1.3 ± 0.4 µM, and STAT6 0.4 ± 0.1 µM. Figure 2 maps Compound 18–STAT5A to PDB 7UBT. auto_single_measurement only accepted activity measurement [1] 1 structures\7UBT\7UBT_metadata.json point structures/7UBT/7ubt_protein.pdb structures/7UBT/7ubt_pocket.pdb structures/7UBT/7ubt_ligand.sdf structures/7UBT/7ubt_ligand.pdb structures/7UBT/7ubt_ligand.cif structures/7UBT/7ubt_complex.pdb structures/7UBT/7ubt_complex.cif 7UC6 classic STAT5A human STAT5A residues 136-705; N-terminal 6xHis-MBP-TEV fusion construct Na Compound 12 "[""MJ6""]" 1 Ki Ki = = 1.5 ± 0.2 µM 1500.0 [] unit_conversion 5.823908740944319 success True direct_binding Fluorescence-polarization competitive binding; Table 1 reports Ki values for STAT5A/5B/6 SH2-domain ligands. 2 Table 1 lists Compound 12 Ki values: STAT5A 1.5 ± 0.2 µM, STAT5B 2.1 ± 0.1 µM, and STAT6 0.3 ± 0.2 µM. Figure 2 maps Compound 12–STAT5A to PDB 7UC6. auto_single_measurement only accepted activity measurement [1] 1 structures\7UC6\7UC6_metadata.json point structures/7UC6/7uc6_protein.pdb structures/7UC6/7uc6_pocket.pdb structures/7UC6/7uc6_ligand.sdf structures/7UC6/7uc6_ligand.pdb structures/7UC6/7uc6_ligand.cif structures/7UC6/7uc6_complex.pdb structures/7UC6/7uc6_complex.cif 7UC7 classic STAT5A human STAT5A residues 136-705; N-terminal 6xHis-MBP-TEV fusion construct Na Compound 17 "[""MQX""]" 1 Ki Ki = = 3.1 ± 1.4 µM 3100.0 [] unit_conversion 5.508638306165727 success True direct_binding Fluorescence-polarization competitive binding; Table 1 reports Ki values for STAT5A/5B/6 SH2-domain ligands. 2 Table 1 lists Compound 17 Ki values: STAT5A 3.1 ± 1.4 µM, STAT5B 2.0 ± 0.2 µM, and STAT6 0.2 ± 0.1 µM. Figure 2 maps Compound 17–STAT5A to PDB 7UC7. auto_single_measurement only accepted activity measurement [1] 1 structures\7UC7\7UC7_metadata.json point structures/7UC7/7uc7_protein.pdb structures/7UC7/7uc7_pocket.pdb structures/7UC7/7uc7_ligand.sdf structures/7UC7/7uc7_ligand.pdb structures/7UC7/7uc7_ligand.cif structures/7UC7/7uc7_complex.pdb structures/7UC7/7uc7_complex.cif 7UDL extended RPB_PLP1_R6 Na designed helical repeat protein RPB_PLP1_R6 Na PLPx6 "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd < < 0.5 nM 0.5 [] unit_conversion 9.301029995663981 success True direct_binding Bio-layer interferometry (Octet) of the designed protein with biotinylated target peptide. 4 Fig. 2e reports Kd < 0.5 nM for the PLPx6 cognate designed-protein interaction; the figure caption identifies the assay as bio-layer interferometry. auto_single_measurement only accepted activity measurement [1] 1 structures\7UDL\7UDL_metadata.json point structures/7UDL/7udl_protein.pdb structures/7UDL/7udl_pocket.pdb structures/7UDL/7udl_ligand.pdb structures/7UDL/7udl_ligand.cif structures/7UDL/7udl_complex.pdb structures/7UDL/7udl_complex.cif 7UDM extended RPB_PLP1_R6 Na designed helical repeat protein RPB_PLP1_R6, alternative conformation 1 Na PLPx6 "[""CHAIN:C""]" 1 Kd Kd < < 0.5 nM 0.5 [] unit_conversion 9.301029995663981 success True direct_binding Bio-layer interferometry (Octet) of the designed protein with biotinylated target peptide. 4 Fig. 2e reports Kd < 0.5 nM for the PLPx6 cognate designed-protein interaction; the figure caption identifies the assay as bio-layer interferometry. auto_single_measurement only accepted activity measurement [1] 1 structures\7UDM\7UDM_metadata.json point structures/7UDM/7udm_protein.pdb structures/7UDM/7udm_pocket.pdb structures/7UDM/7udm_ligand.pdb structures/7UDM/7udm_ligand.cif structures/7UDM/7udm_complex.pdb structures/7UDM/7udm_complex.cif 7UDP classic COQ8A Na Na Na CA157 "[""MVS""]" 1 IC50 IC50 = = 0.47 μM 470.0 [] unit_conversion 6.327902142064282 success True biochemical_inhibition Supplementary Table 1, “Inhibition data from Extended Data Figure 1a.” 4 Supplementary Table 1 lists UNC-CA157 with IC50 0.47 μM (95% confidence interval ±0.076 μM). auto_single_measurement only accepted activity measurement [1] 1 structures\7UDP\7UDP_metadata.json point structures/7UDP/7udp_protein.pdb structures/7UDP/7udp_pocket.pdb structures/7UDP/7udp_ligand.sdf structures/7UDP/7udp_ligand.pdb structures/7UDP/7udp_ligand.cif structures/7UDP/7udp_complex.pdb structures/7UDP/7udp_complex.cif 7UDQ classic COQ8A Na Na Na CA157 "[""MVS""]" 1 IC50 IC50 = = 0.47 μM 470.0 [] unit_conversion 6.327902142064282 success True biochemical_inhibition Supplementary Table 1, “Inhibition data from Extended Data Figure 1a.” 4 Supplementary Table 1 lists UNC-CA157 with IC50 0.47 μM (95% confidence interval ±0.076 μM). auto_single_measurement only accepted activity measurement [1] 1 structures\7UDQ\7UDQ_metadata.json point structures/7UDQ/7udq_protein.pdb structures/7UDQ/7udq_pocket.pdb structures/7UDQ/7udq_ligand.sdf structures/7UDQ/7udq_ligand.pdb structures/7UDQ/7udq_ligand.cif structures/7UDQ/7udq_complex.pdb structures/7UDQ/7udq_complex.cif 7UE2 extended RPB_PLP3_R6 Na designed helical repeat protein RPB_PLP3_R6 Na PLPx6 "[""CHAIN:B""]" 1 Kd Kd = = 47 nM 47.0 [] unit_conversion 7.327902142064282 success True direct_binding Bio-layer interferometry (Octet) specificity matrix using biotinylated target peptides. 7 Fig. 5b labels the cognate RPB_PLP3_R6–PLPx6 Octet binding trace with 47 nM; its caption identifies the experiment as bio-layer interferometry and marks cognate complexes. auto_single_measurement only accepted activity measurement [1] 1 structures\7UE2\7UE2_metadata.json point structures/7UE2/7ue2_protein.pdb structures/7UE2/7ue2_pocket.pdb structures/7UE2/7ue2_ligand.pdb structures/7UE2/7ue2_ligand.cif structures/7UE2/7ue2_complex.pdb structures/7UE2/7ue2_complex.cif 7UE3 classic PANK3 Na PANK3 with two amino acids (DD) added to the carboxy terminus Na compound 3; PZ-3804 "[""ND6""]" 1 IC50 IC50 = = 7.5 ± 0.6 nM 7.5 [] unit_conversion 8.1249387366083 success True biochemical_inhibition PANK3 activity assay; Table 1 biochemical PANK3 IC50. 2 Table 1 reports compound 3 PANK3 IC50 = 7.5 ± 0.6 nM. The PANK3 activity assay is described on page 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7UE3\7UE3_metadata.json point structures/7UE3/7ue3_protein.pdb structures/7UE3/7ue3_pocket.pdb structures/7UE3/7ue3_ligand.sdf structures/7UE3/7ue3_ligand.pdb structures/7UE3/7ue3_ligand.cif structures/7UE3/7ue3_complex.pdb structures/7UE3/7ue3_complex.cif 7UE4 classic PANK3 Na PANK3 with two amino acids (DD) added to the carboxy terminus Na compound 5; PZ-3855 "[""Y89""]" 1 IC50 IC50 = = 5.8 ± 0.4 nM 5.8 [] unit_conversion 8.236572006437063 success True biochemical_inhibition PANK3 activity assay; Table 1 biochemical PANK3 IC50. 2 Table 1 reports compound 5 PANK3 IC50 = 5.8 ± 0.4 nM. The PANK3 activity assay is described on page 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7UE4\7UE4_metadata.json point structures/7UE4/7ue4_protein.pdb structures/7UE4/7ue4_pocket.pdb structures/7UE4/7ue4_ligand.sdf structures/7UE4/7ue4_ligand.pdb structures/7UE4/7ue4_ligand.cif structures/7UE4/7ue4_complex.pdb structures/7UE4/7ue4_complex.cif 7UE6 classic PANK3 Na PANK3 with two amino acids (DD) added to the carboxy terminus Na compound 18; PZ-3802 "[""NDK""]" 1 IC50 IC50 = = 20.0 ± 2.9 nM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition PANK3 activity assay; Table 2 biochemical PANK3 IC50. 4 Table 2 reports compound 18 PANK3 IC50 = 20.0 ± 2.9 nM. The PANK3 activity assay is described on page 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7UE6\7UE6_metadata.json point structures/7UE6/7ue6_protein.pdb structures/7UE6/7ue6_pocket.pdb structures/7UE6/7ue6_ligand.sdf structures/7UE6/7ue6_ligand.pdb structures/7UE6/7ue6_ligand.cif structures/7UE6/7ue6_complex.pdb structures/7UE6/7ue6_complex.cif 7UE7 classic PANK3 Na PANK3 with two amino acids (DD) added to the carboxy terminus Na compound 21; PZ-3883 "[""NE3""]" 1 IC50 IC50 = = 8.9 ± 0.8 nM 8.9 [] unit_conversion 8.050609993355087 success True biochemical_inhibition PANK3 activity assay; Table 2 biochemical PANK3 IC50. 4 Table 2 reports compound 21 PANK3 IC50 = 8.9 ± 0.8 nM. The PANK3 activity assay is described on page 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7UE7\7UE7_metadata.json point structures/7UE7/7ue7_protein.pdb structures/7UE7/7ue7_pocket.pdb structures/7UE7/7ue7_ligand.sdf structures/7UE7/7ue7_ligand.pdb structures/7UE7/7ue7_ligand.cif structures/7UE7/7ue7_complex.pdb structures/7UE7/7ue7_complex.cif 7UEO classic PANK3 Na PANK3 with two amino acids (DD) added to the carboxy terminus Na compound 23; PZ-3977 "[""Y90""]" 1 IC50 IC50 = = 1.03 ± 0.1 nM 1.03 [] unit_conversion 8.987162775294827 success True biochemical_inhibition PANK3 activity assay; Table 2 biochemical PANK3 IC50. 4 Table 2 reports compound 23 PANK3 IC50 = 1.03 ± 0.1 nM. The PANK3 activity assay is described on page 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7UEO\7UEO_metadata.json point structures/7UEO/7ueo_protein.pdb structures/7UEO/7ueo_pocket.pdb structures/7UEO/7ueo_ligand.sdf structures/7UEO/7ueo_ligand.pdb structures/7UEO/7ueo_ligand.cif structures/7UEO/7ueo_complex.pdb structures/7UEO/7ueo_complex.cif 7UEP classic PANK3 Na PANK3 with two amino acids (DD) added to the carboxy terminus Na compound 29; PZ-3860 "[""Y93""]" 1 IC50 IC50 = = 3.8 ± 0.4 nM 3.8 [] unit_conversion 8.42021640338319 success True biochemical_inhibition PANK3 activity assay; Table 3 biochemical PANK3 IC50. 6 Table 3 reports compound 29 PANK3 IC50 = 3.8 ± 0.4 nM. The PANK3 activity assay is described on page 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7UEP\7UEP_metadata.json point structures/7UEP/7uep_protein.pdb structures/7UEP/7uep_pocket.pdb structures/7UEP/7uep_ligand.sdf structures/7UEP/7uep_ligand.pdb structures/7UEP/7uep_ligand.cif structures/7UEP/7uep_complex.pdb structures/7UEP/7uep_complex.cif 7UEQ classic PANK3 Na PANK3 with two amino acids (DD) added to the carboxy terminus Na compound 14; PZ-4061 "[""N06""]" 1 IC50 IC50 = = 16.8 ± 1.8 nM 16.8 [] unit_conversion 7.774690718274137 success True biochemical_inhibition PANK3 activity assay; Table 1 biochemical PANK3 IC50. 2 Table 1 reports compound 14 PANK3 IC50 = 16.8 ± 1.8 nM. The PANK3 activity assay is described on page 9. auto_single_measurement only accepted activity measurement [1] 1 structures\7UEQ\7UEQ_metadata.json point structures/7UEQ/7ueq_protein.pdb structures/7UEQ/7ueq_pocket.pdb structures/7UEQ/7ueq_ligand.sdf structures/7UEQ/7ueq_ligand.pdb structures/7UEQ/7ueq_ligand.cif structures/7UEQ/7ueq_complex.pdb structures/7UEQ/7ueq_complex.cif 7UFG extended PAPP-A Na Catalytically inactive full-length PAPP-A (E483A) in complex with IGFBP5 E483A IGFBP5 anchor peptide (P119-S143) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 380 nM 380.0 [] unit_conversion 6.42021640338319 success True direct_binding Fluorescence-polarization direct-binding assay with PAPP-A (E483A) and the IGFBP5 anchor peptide. 5 Fig. 3b visibly prints “PAPP-A (E483A) and IGFBP5 anchor peptide” and “Kd=380 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7UFG\7UFG_metadata.json point structures/7UFG/7ufg_protein.pdb structures/7UFG/7ufg_pocket.pdb structures/7UFG/7ufg_ligand.pdb structures/7UFG/7ufg_ligand.cif structures/7UFG/7ufg_complex.pdb structures/7UFG/7ufg_complex.cif 7UH9 extended cNTnC-cTnI chimera Na cNTnC residues 1-90 fused to cTnI residues 136-163 Na W8 (N-(7-aminohexyl)-5-chloro-1-naphthalenesulfonamide) "[""WW9""]" 1 Kd Kd = = 270 ± 40 μM 270000.0 [] unit_conversion 3.568636235841013 success True direct_binding Titration of W8 into calcium-saturated 15N-labeled cNTnC-cTnI chimera monitored by 2D 1H,15N-HSQC NMR; global Kd determined from chemical-shift perturbation. 3 “W8 and W9 bind significantly tighter to cChimera than W7 … (KD of 270 ± 40 μM for W8)” ; Table 1 prints W8, 270 ± 40 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7UH9\7UH9_metadata.json point structures/7UH9/7uh9_protein.pdb structures/7UH9/7uh9_pocket.pdb structures/7UH9/7uh9_ligand.pdb structures/7UH9/7uh9_ligand.cif structures/7UH9/7uh9_complex.pdb structures/7UH9/7uh9_complex.cif 7UIQ extended CaMKII-alpha (CAMK2A) human kinase domain, residues 7-274, lacking the regulatory domain D135N Tiam1 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 1 ± 0.1 μM 1000.0 [] unit_conversion 6.0 success True direct_binding ITC. 4 Tiam1 Kd = 1 ± 0.1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7UIQ\7UIQ_metadata.json point structures/7UIQ/7uiq_protein.pdb structures/7UIQ/7uiq_pocket.pdb structures/7UIQ/7uiq_ligand.pdb structures/7UIQ/7uiq_ligand.cif structures/7UIQ/7uiq_complex.pdb structures/7UIQ/7uiq_complex.cif 7UIS extended CaMKII-alpha (CAMK2A) human kinase domain, residues 7-274, lacking the regulatory domain D135N; GluN2B S1303D GluN2B(S1303D) "[""CHAIN:B""]" 1 Kd Kd = = 493 ± 47 nM 493.0 [] unit_conversion 6.30715308072277 success True direct_binding ITC, phosphomimetic GluN2B peptide. 11 Phosphomimetic GluN2B peptide (S1303D), Kd = 493 ± 47 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7UIS\7UIS_metadata.json point structures/7UIS/7uis_protein.pdb structures/7UIS/7uis_pocket.pdb structures/7UIS/7uis_ligand.pdb structures/7UIS/7uis_ligand.cif structures/7UIS/7uis_complex.pdb structures/7UIS/7uis_complex.cif 7UJD extended PSMD2 human full-length human PSMD2 Na MC1 "[""CHAIN:Z""]" 1 Kd Kd = = 1.3 nM 1.3 [] unit_conversion 8.886056647693163 success True direct_binding Purified PSMD2 direct-binding measurement; Fig. 1a lists the PSMD2 Kd for macrocyclic ligand MC1. 2 Fig. 1a explicitly lists MC1 with “PSMD2 Kd” of 1.3 nM. The paper identifies the PSMD2–MC1 structure as PDB 7UJD (page 15). auto_single_measurement only accepted activity measurement [1] 1 structures\7UJD\7UJD_metadata.json point structures/7UJD/7ujd_protein.pdb structures/7UJD/7ujd_pocket.pdb structures/7UJD/7ujd_ligand.pdb structures/7UJD/7ujd_ligand.cif structures/7UJD/7ujd_complex.pdb structures/7UJD/7ujd_complex.cif 7UJQ extended CaMKII-alpha (CAMK2A) human kinase domain, residues 7-274, lacking the regulatory domain D135N GluN2B "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 107 ± 47 nM 107.0 [] unit_conversion 6.97061622231479 success True direct_binding Binary ITC. 4 GluN2B Kd = 107 ± 47 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7UJQ\7UJQ_metadata.json point structures/7UJQ/7ujq_protein.pdb structures/7UJQ/7ujq_pocket.pdb structures/7UJQ/7ujq_ligand.pdb structures/7UJQ/7ujq_ligand.cif structures/7UJQ/7ujq_complex.pdb structures/7UJQ/7ujq_complex.cif 7UJV extended PHD2 Na PHD2 prolyl-hydroxylase domain residues 181-426 in complex with WT HIF2a-CODD peptide WT HIF2a-CODD peptide HIF2a-CODD peptide "[""CHAIN:A""]" 1 Kd Kd = = 34 ± 2 µM 34000.0 [] unit_conversion 4.468521082957745 success True direct_binding Microscale thermophoresis (MST) measurement of PHD2–647 binding to WT HIF2α-CODD peptide; assay buffer contained NOG and FeSO4. 4 Table 2 reports “HIF2α WT” Kd = 34 ± 2 µM; the text identifies this as the Kd of the HIF2α-CODD WT peptide and PHD2. Pages 4 and 11 establish the PHD2/HIF2α-CODD complex and MST format. auto_single_measurement only accepted activity measurement [1] 1 structures\7UJV\7UJV_metadata.json point structures/7UJV/7ujv_protein.pdb structures/7UJV/7ujv_pocket.pdb structures/7UJV/7ujv_ligand.pdb structures/7UJV/7ujv_ligand.cif structures/7UJV/7ujv_complex.pdb structures/7UJV/7ujv_complex.cif 7UKN extended DDB1 Na DDB1 with a TEV-cleavable N-terminal His tag, in complex with pUL145 H-box peptide residues N25-G37 Na pUL145 H-box peptide (residues N25-G37) "[""CHAIN:B""]" 1 Kd Kd = = 24 ± 4.0 nM 24.0 [] unit_conversion 7.619788758288394 success True direct_binding Fluorescence-polarization assay using fluorescently labeled pUL145-derived H-box peptide and purified DDB1. 3 Figure 1D reports pUL145 Kd = 24 ± 4.0 nM; the Results text states the pUL145-derived peptide bound DDB1 with Kd 24 ± 4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7UKN\7UKN_metadata.json point structures/7UKN/7ukn_protein.pdb structures/7UKN/7ukn_pocket.pdb structures/7UKN/7ukn_ligand.pdb structures/7UKN/7ukn_ligand.cif structures/7UKN/7ukn_complex.pdb structures/7UKN/7ukn_complex.cif 7UKS classic SOS1 Na Na Na compound 15 "[""NL0""]" 1 Ki Ki = = 0.33 nM 0.33 [] unit_conversion 9.481486060122112 success True direct_binding SOS1 binding assay; initial C7-substituent SAR in Table 3. 4 Table 3 lists compound 15 with SOS1 binding Ki = 0.33 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7UKS\7UKS_metadata.json point structures/7UKS/7uks_protein.pdb structures/7UKS/7uks_pocket.pdb structures/7UKS/7uks_ligand.sdf structures/7UKS/7uks_ligand.pdb structures/7UKS/7uks_ligand.cif structures/7UKS/7uks_complex.pdb structures/7UKS/7uks_complex.cif 7UKZ classic CDK11B Homo sapiens CDK11B residues 72-380, p58 isoform Na OTS964 "[""NK3""]" 1 Kd Kd = = 65.4 ± 18 nM 65.4 [] unit_conversion 7.184422251675732 success True direct_binding Isothermal titration calorimetry (ITC) of OTS964 binding to CDK11 wild type; mean ± SD of two replicate experiments. 9 Table 2 reports for CDK11 wild type: K_D = 65.4 ± 18 nM for OTS964 binding. auto_single_measurement only accepted activity measurement [1] 1 structures\7UKZ\7UKZ_metadata.json point structures/7UKZ/7ukz_protein.pdb structures/7UKZ/7ukz_pocket.pdb structures/7UKZ/7ukz_ligand.sdf structures/7UKZ/7ukz_ligand.pdb structures/7UKZ/7ukz_ligand.cif structures/7UKZ/7ukz_complex.pdb structures/7UKZ/7ukz_complex.cif 7UOR extended cytochrome P450 enzyme CYP119 Na CYP119 mutant cloned into the 2B-T backbone with a histidine tag C317G, L155W, T213G, V254L methyliridium(III) mesoporphyrin (Ir(Me)-MPIX) "[""HIR""]" 1 Kd Kd = = 4.6 µM 4600.0 [] unit_conversion 5.337242168318426 success True direct_binding Fluorometric titration/binding of Ir(Me)-MPIX to apo-CYP119; the concentration-dependence experiment states that the selectivity transition is similar to the Kd value. 9 “There is a steep drop in selectivity at [Ir(Me)-CYP119] = 1.2 µM concentration which is similar to the Kd value of 4.6 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7UOR\7UOR_metadata.json point structures/7UOR/7uor_protein.pdb structures/7UOR/7uor_pocket.pdb structures/7UOR/7uor_ligand.pdb structures/7UOR/7uor_ligand.cif structures/7UOR/7uor_complex.pdb structures/7UOR/7uor_complex.cif 7UOY classic NDM-1 Na Na Na compound 14 "[""O0F""]" 1 IC50 IC50 = = 3.3 μM 3300.0 [] unit_conversion 5.481486060122112 success True biochemical_inhibition In vitro enzyme inhibition; CCF2 FA end-point assay. 4 Figure 3 reports compound 14 NDM-1 IC50 = 3.3 μM; Figure 6 maps compound 14/NDM-1 to PDB 7UOY. auto_single_measurement only accepted activity measurement [1] 1 structures\7UOY\7UOY_metadata.json point structures/7UOY/7uoy_protein.pdb structures/7UOY/7uoy_pocket.pdb structures/7UOY/7uoy_ligand.sdf structures/7UOY/7uoy_ligand.pdb structures/7UOY/7uoy_ligand.cif structures/7UOY/7uoy_complex.pdb structures/7UOY/7uoy_complex.cif 7UP1 classic NDM-1 Na Na Na compound 18 "[""NZR""]" 1 IC50 IC50 = = 3.9 nM 3.9 [] unit_conversion 8.4089353929735 success True biochemical_inhibition In vitro enzyme inhibition; CCF2 FA end-point assay. 6 Figure 7 reports compound 18 NDM-1 IC50 = 3.9 nM; Figure 6 maps compound 18/NDM-1 to PDB 7UP1. auto_single_measurement only accepted activity measurement [1] 1 structures\7UP1\7UP1_metadata.json point structures/7UP1/7up1_protein.pdb structures/7UP1/7up1_pocket.pdb structures/7UP1/7up1_ligand.sdf structures/7UP1/7up1_ligand.pdb structures/7UP1/7up1_ligand.cif structures/7UP1/7up1_complex.pdb structures/7UP1/7up1_complex.cif 7UP2 classic Na Na Na Na compound 18 "[""NZR""]" 1 IC50 IC50 = = 57.5 nM 57.5 [] unit_conversion 7.2403321553103694 success True biochemical_inhibition In vitro enzyme inhibition; CCF2 FA end-point assay. 6 Figure 7 reports compound 18 VIM-1 IC50 = 57.5 nM; Figure 8 explicitly maps compound 18/VIM-1 to PDB 7UP2. auto_single_measurement only accepted activity measurement [1] 1 structures\7UP2\7UP2_metadata.json point structures/7UP2/7up2_protein.pdb structures/7UP2/7up2_pocket.pdb structures/7UP2/7up2_ligand.sdf structures/7UP2/7up2_ligand.pdb structures/7UP2/7up2_ligand.cif structures/7UP2/7up2_complex.pdb structures/7UP2/7up2_complex.cif 7UQ2 classic Vs.4 Na Vs.4 residues 1-88 Na cGAMP (3'3'-cGAMP) "[""4BW""]" 1 Kd Kd = = 31.4 nM 31.4 [] unit_conversion 7.503070351926786 success True direct_binding Isothermal titration calorimetry of purified Vs.4 with cGAMP. 5 Fig. 3b reports that purified Vs.4 bound cGAMP by ITC with Kd 31.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7UQ2\7UQ2_metadata.json point structures/7UQ2/7uq2_protein.pdb structures/7UQ2/7uq2_pocket.pdb structures/7UQ2/7uq2_ligand.sdf structures/7UQ2/7uq2_ligand.pdb structures/7UQ2/7uq2_ligand.cif structures/7UQ2/7uq2_complex.pdb structures/7UQ2/7uq2_complex.cif 7UR3 classic Hsp90alpha Na Na Na KUNA-111 (5-fluoroisoindoline derivative of 23d) "[""OJ3""]" 1 IC50 IC50 = = 0.25 ± 0.01 μM 250.0 [] unit_conversion 6.6020599913279625 success True direct_binding Fluorescence polarization (FP) assay; Table 4. 4 Table 4 reports KUNA-111 IC50 = 0.25 ± 0.01 μM for Hsp90α. Figure 4 identifies KUNA-111 as the 5-fluoroisoindoline derivative of 23d bound to the Hsp90α NTD (PDB 7UR3). auto_single_measurement only accepted activity measurement [1] 1 structures\7UR3\7UR3_metadata.json point structures/7UR3/7ur3_protein.pdb structures/7UR3/7ur3_pocket.pdb structures/7UR3/7ur3_ligand.sdf structures/7UR3/7ur3_ligand.pdb structures/7UR3/7ur3_ligand.cif structures/7UR3/7ur3_complex.pdb structures/7UR3/7ur3_complex.cif 7UR9 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 SARS-CoV-2 Mpro residues 3264-3569, expressed as an N-terminal SUMO fusion with a C-terminal 6xHis tag Na CDD-1845 "[""O5F""]" 1 Ki Ki = = 3 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Purified Mpro fluorescent peptide proteolytic-cleavage inhibition assay; Fig. 2 states values are Ki values determined as described in Methods. 4 Fig. 2 labels CDD-1845 as 3 nM and states that the numbers indicate Ki values; Fig. 3 maps CDD-1845 to PDB 7UR9. auto_single_measurement only accepted activity measurement [1] 1 structures\7UR9\7UR9_metadata.json point structures/7UR9/7ur9_protein.pdb structures/7UR9/7ur9_pocket.pdb structures/7UR9/7ur9_ligand.sdf structures/7UR9/7ur9_ligand.pdb structures/7UR9/7ur9_ligand.cif structures/7UR9/7ur9_complex.pdb structures/7UR9/7ur9_complex.cif 7URB classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 SARS-CoV-2 Mpro residues 3264-3569, expressed as an N-terminal SUMO fusion with a C-terminal 6xHis tag Na CDD-1733 "[""O5O""]" 1 Ki Ki = = 12 nM 12.0 [] unit_conversion 7.920818753952375 success True biochemical_inhibition Purified Mpro fluorescent peptide proteolytic-cleavage inhibition assay. 3 The text states that CDD-1733, harboring the S-configuration, gave a Ki of 12 nM; Fig. 3 maps CDD-1733 to PDB 7URB. auto_single_measurement only accepted activity measurement [1] 1 structures\7URB\7URB_metadata.json point structures/7URB/7urb_protein.pdb structures/7URB/7urb_pocket.pdb structures/7URB/7urb_ligand.sdf structures/7URB/7urb_ligand.pdb structures/7URB/7urb_ligand.cif structures/7URB/7urb_complex.pdb structures/7URB/7urb_complex.cif 7US4 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 SARS-CoV-2 Mpro residues 3264-3569, expressed as an N-terminal SUMO fusion with a C-terminal 6xHis tag Na CDD-1819 "[""O69""]" 1 Ki Ki = = 5 nM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition Purified Mpro fluorescent peptide proteolytic-cleavage inhibition assay. 3 The text states that CDD-1819 gave a Ki of 5 nM; Fig. 3 maps CDD-1819 to PDB 7US4. auto_single_measurement only accepted activity measurement [1] 1 structures\7US4\7US4_metadata.json point structures/7US4/7us4_protein.pdb structures/7US4/7us4_pocket.pdb structures/7US4/7us4_ligand.sdf structures/7US4/7us4_ligand.pdb structures/7US4/7us4_ligand.cif structures/7US4/7us4_complex.pdb structures/7US4/7us4_complex.cif 7USO extended caspase-3 Na Na Na AcITVKD-CHO (compound 9) "[""CHAIN:F"", ""CHAIN:G""]" 1 pKi Ki = = 6.05 ± 0.06 unitless 891.2509381337459 [] p_metric_transform 6.05 success True biochemical_inhibition Fluorometric enzyme-inhibition assay; Table 2 pKi value for Casp3. 5 Table 2 lists AcITVKD-CHO (9) with Casp3 pKi 6.05 ± 0.06. The paper identifies compound 9 as a Casp3 crystallographic complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7USO\7USO_metadata.json point structures/7USO/7uso_protein.pdb structures/7USO/7uso_pocket.pdb structures/7USO/7uso_ligand.pdb structures/7USO/7uso_ligand.cif structures/7USO/7uso_complex.pdb structures/7USO/7uso_complex.cif 7USP extended caspase-3 Na Na Na AcITV(Orn)D-CHO (compound 20) "[""CHAIN:F"", ""CHAIN:G""]" 1 pKi Ki = = 5.68 ± 0.11 unitless 2089.2961308540407 [] p_metric_transform 5.68 success True biochemical_inhibition Fluorometric enzyme-inhibition assay; Table 2 pKi value for Casp3. 5 Table 2 lists AcITV(Orn)D-CHO (20) with Casp3 pKi 5.68 ± 0.11. auto_single_measurement only accepted activity measurement [1] 1 structures\7USP\7USP_metadata.json point structures/7USP/7usp_protein.pdb structures/7USP/7usp_pocket.pdb structures/7USP/7usp_ligand.pdb structures/7USP/7usp_ligand.cif structures/7USP/7usp_complex.pdb structures/7USP/7usp_complex.cif 7USQ extended caspase-3 Na Na Na AcDVPD-CHO (compound 16) "[""CHAIN:F"", ""CHAIN:G""]" 1 pKi Ki = = 8.18 ± 0.12 unitless 6.606934480075965 [] p_metric_transform 8.18 success True biochemical_inhibition Fluorometric enzyme-inhibition assay; Table 2 pKi value for Casp3. 5 Table 2 lists AcDVPD-CHO (16) with Casp3 pKi 8.18 ± 0.12. The paper identifies compound 16 as a Casp3 crystallographic complex. auto_single_measurement only accepted activity measurement [1] 1 structures\7USQ\7USQ_metadata.json point structures/7USQ/7usq_protein.pdb structures/7USQ/7usq_pocket.pdb structures/7USQ/7usq_ligand.pdb structures/7USQ/7usq_ligand.cif structures/7USQ/7usq_complex.pdb structures/7USQ/7usq_complex.cif 7UT3 classic G10C Fab mouse Fab fragment of G10C Na GalNAc-alpha-PNP (GalNAc-pNP) "[""TI0""]" 1 Kd Kd ~ ~ 10 nM 10.0 [] unit_conversion 8.0 success True direct_binding Isothermal titration calorimetry; monovalent binding to GalNAc-alpha-PNP. 4 “we used isothermal titration calorimetry to examine G10C’s binding affinity to 4-nitrophenyl-N-acetyl-α-D-galactosaminide (GalNAcα-PNP) ... G10C was found to have a KD of ~10 nM for monovalent binding to this monosaccharide derivative.” auto_single_measurement only accepted activity measurement [1] 1 structures\7UT3\7UT3_metadata.json point structures/7UT3/7ut3_protein.pdb structures/7UT3/7ut3_pocket.pdb structures/7UT3/7ut3_ligand.sdf structures/7UT3/7ut3_ligand.pdb structures/7UT3/7ut3_ligand.cif structures/7UT3/7ut3_complex.pdb structures/7UT3/7ut3_complex.cif 7UT5 classic Acinetobacter baumannii dihydroorotate dehydrogenase (AbDHODH) Acinetobacter baumannii Na Na DSM186 "[""OBR""]" 1 IC50 IC50 = = 0.028 ± 0.0038 μM 28.0 [] unit_conversion 7.552841968657781 success True biochemical_inhibition Steady-state assay against purified recombinant AbDHODH; Table 1 enzyme activity data. 3 Table 1 reports AbDHODH IC50 for DSM186 as 0.028 ± 0.0038 μM (n=7). auto_single_measurement only accepted activity measurement [1] 1 structures\7UT5\7UT5_metadata.json point structures/7UT5/7ut5_protein.pdb structures/7UT5/7ut5_pocket.pdb structures/7UT5/7ut5_ligand.sdf structures/7UT5/7ut5_ligand.pdb structures/7UT5/7ut5_ligand.cif structures/7UT5/7ut5_complex.pdb structures/7UT5/7ut5_complex.cif 7UTY classic BRD4 Na Na Na compound 2c "[""OFR""]" 1 IC50 IC50 = = 3.1 µM 3100.0 [] unit_conversion 5.508638306165727 success True biochemical_inhibition AlphaScreen assay; compounds tested once in duplicate. 4 Table 1 reports compound 2c IC50 = 3.1 µM for BRD4-1. The text identifies the BRD4-1/compound 2c co-crystal, and Figure 4a specifies the BRD4-1 structure with compound 2c. auto_single_measurement only accepted activity measurement [1] 1 structures\7UTY\7UTY_metadata.json point structures/7UTY/7uty_protein.pdb structures/7UTY/7uty_pocket.pdb structures/7UTY/7uty_ligand.sdf structures/7UTY/7uty_ligand.pdb structures/7UTY/7uty_ligand.cif structures/7UTY/7uty_complex.pdb structures/7UTY/7uty_complex.cif 7UUU classic BRDT Na Na Na compound 2c "[""OFR""]" 1 IC50 IC50 = = 4.7 µM 4700.0 [] unit_conversion 5.327902142064282 success True biochemical_inhibition AlphaScreen assay; compounds tested once in duplicate. 4 Table 1 reports compound 2c IC50 = 4.7 µM for BRDT-1. The text identifies the BRDT-1/compound 2c co-crystal, and Figure 4b specifies the BRDT-1 structure with compound 2c. auto_single_measurement only accepted activity measurement [1] 1 structures\7UUU\7UUU_metadata.json point structures/7UUU/7uuu_protein.pdb structures/7UUU/7uuu_pocket.pdb structures/7UUU/7uuu_ligand.sdf structures/7UUU/7uuu_ligand.pdb structures/7UUU/7uuu_ligand.cif structures/7UUU/7uuu_complex.pdb structures/7UUU/7uuu_complex.cif 7UVM classic human ClpP protease human Na Na TR-27 "[""OX0""]" 1 Kd Kd = = 23.7 ± 10.0 nM 23.7 [] unit_conversion 7.6252516539898965 success True biochemical_inhibition Apparent Kd derived from casein-FITC degradation activity assays with purified human ClpP; EC50 was measured across ClpP concentrations and extrapolated to zero ClpP concentration. 5 Table 1 reports TR-27 Kd, app = 23.7 ± 10.0 nM; the text states these values were obtained from the activity assay and are binding constants for TR compounds to ClpP. auto_single_measurement only accepted activity measurement [1] 1 structures\7UVM\7UVM_metadata.json point structures/7UVM/7uvm_protein.pdb structures/7UVM/7uvm_pocket.pdb structures/7UVM/7uvm_ligand.sdf structures/7UVM/7uvm_ligand.pdb structures/7UVM/7uvm_ligand.cif structures/7UVM/7uvm_complex.pdb structures/7UVM/7uvm_complex.cif 7UVN classic human ClpP protease human Na Na TR-57 "[""P3O""]" 1 Kd Kd = = 15.5 ± 12.0 nM 15.5 [] unit_conversion 7.809668301829708 success True biochemical_inhibition Apparent Kd derived from casein-FITC degradation activity assays with purified human ClpP; EC50 was measured across ClpP concentrations and extrapolated to zero ClpP concentration. 5 Table 1 reports TR-57 Kd, app = 15.5 ± 12.0 nM; the text states these values were obtained from the activity assay and are binding constants for TR compounds to ClpP. auto_single_measurement only accepted activity measurement [1] 1 structures\7UVN\7UVN_metadata.json point structures/7UVN/7uvn_protein.pdb structures/7UVN/7uvn_pocket.pdb structures/7UVN/7uvn_ligand.sdf structures/7UVN/7uvn_ligand.pdb structures/7UVN/7uvn_ligand.cif structures/7UVN/7uvn_complex.pdb structures/7UVN/7uvn_complex.cif 7UVR classic human ClpP protease human Na Na TR-65 "[""PJF""]" 1 Kd Kd = = 23.3 ± 9.1 nM 23.3 [] unit_conversion 7.632644078973981 success True biochemical_inhibition Apparent Kd derived from casein-FITC degradation activity assays with purified human ClpP; EC50 was measured across ClpP concentrations and extrapolated to zero ClpP concentration. 5 Table 1 reports TR-65 Kd, app = 23.3 ± 9.1 nM; the text states these values were obtained from the activity assay and are binding constants for TR compounds to ClpP. auto_single_measurement only accepted activity measurement [1] 1 structures\7UVR\7UVR_metadata.json point structures/7UVR/7uvr_protein.pdb structures/7UVR/7uvr_pocket.pdb structures/7UVR/7uvr_ligand.sdf structures/7UVR/7uvr_ligand.pdb structures/7UVR/7uvr_ligand.cif structures/7UVR/7uvr_complex.pdb structures/7UVR/7uvr_complex.cif 7UVU classic human ClpP protease human Na Na TR-107 "[""OY9""]" 1 Kd Kd = = 32.2 ± 6.3 nM 32.2 [] unit_conversion 7.492144128304169 success True biochemical_inhibition Apparent Kd derived from casein-FITC degradation activity assays with purified human ClpP; EC50 was measured across ClpP concentrations and extrapolated to zero ClpP concentration. 5 Table 1 reports TR-107 Kd, app = 32.2 ± 6.3 nM; the text states these values were obtained from the activity assay and are binding constants for TR compounds to ClpP. auto_single_measurement only accepted activity measurement [1] 1 structures\7UVU\7UVU_metadata.json point structures/7UVU/7uvu_protein.pdb structures/7UVU/7uvu_pocket.pdb structures/7UVU/7uvu_ligand.sdf structures/7UVU/7uvu_ligand.pdb structures/7UVU/7uvu_ligand.cif structures/7UVU/7uvu_complex.pdb structures/7UVU/7uvu_complex.cif 7UW0 classic human ClpP protease human Na Na TR-133 "[""P4I""]" 1 Kd Kd = = 29.1 ± 7.8 nM 29.1 [] unit_conversion 7.536107011014092 success True biochemical_inhibition Apparent Kd derived from casein-FITC degradation activity assays with purified human ClpP; EC50 was measured across ClpP concentrations and extrapolated to zero ClpP concentration. 5 Table 1 reports TR-133 Kd, app = 29.1 ± 7.8 nM; the text states these values were obtained from the activity assay and are binding constants for TR compounds to ClpP. auto_single_measurement only accepted activity measurement [1] 1 structures\7UW0\7UW0_metadata.json point structures/7UW0/7uw0_protein.pdb structures/7UW0/7uw0_pocket.pdb structures/7UW0/7uw0_ligand.sdf structures/7UW0/7uw0_ligand.pdb structures/7UW0/7uw0_ligand.cif structures/7UW0/7uw0_complex.pdb structures/7UW0/7uw0_complex.cif 7UW6 classic low molecular weight protein tyrosine phosphatase (LMW-PTP) human Na Na SPAA-2 "[""OIF""]" 1 IC50 IC50 = = 2.1 µM 2100.0 [] unit_conversion 5.6777807052660805 success True biochemical_inhibition Purified LMW-PTP inhibition assay; Table 2 reports LMW-PTP IC50 for SPAA-2. The methods state IC50 values were determined in an enzyme inhibition assay using pNPP substrate. 38 Table 2 lists SPAA-2 (R = H) with LMW-PTP IC50 = 2.1 µM. The paper explicitly identifies the SPAA-2/LMW-PTP crystal structure as PDB 7UW6. auto_single_measurement only accepted activity measurement [1] 1 structures\7UW6\7UW6_metadata.json point structures/7UW6/7uw6_protein.pdb structures/7UW6/7uw6_pocket.pdb structures/7UW6/7uw6_ligand.sdf structures/7UW6/7uw6_ligand.pdb structures/7UW6/7uw6_ligand.cif structures/7UW6/7uw6_complex.pdb structures/7UW6/7uw6_complex.cif 7UWI extended beta-catenin Na Na Na FP01567 "[""CHAIN:F""]" 1 Kd Kd = = 2.5 ± 0.50 µM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding Surface plasmon resonance (SPR); Figure 3 table. 5 The Figure 3 table reports FP01567 (C33): KD (µM, SPR) 2.5 ± 0.50. auto_single_measurement only accepted activity measurement [1] 1 structures\7UWI\7UWI_metadata.json point structures/7UWI/7uwi_protein.pdb structures/7UWI/7uwi_pocket.pdb structures/7UWI/7uwi_ligand.pdb structures/7UWI/7uwi_ligand.cif structures/7UWI/7uwi_complex.pdb structures/7UWI/7uwi_complex.cif 7UWO extended beta-catenin Na Na Na FP05874 "[""CHAIN:B""]" 1 Kd Kd = = 0.1 ± 0.02 µM 100.0 [] unit_conversion 7.0 success True direct_binding Surface plasmon resonance (SPR); Figure 3 table. 5 The Figure 3 table reports FP05874 (C35): KD (µM, SPR) 0.1 ± 0.02. auto_single_measurement only accepted activity measurement [1] 1 structures\7UWO\7UWO_metadata.json point structures/7UWO/7uwo_protein.pdb structures/7UWO/7uwo_pocket.pdb structures/7UWO/7uwo_ligand.pdb structures/7UWO/7uwo_ligand.cif structures/7UWO/7uwo_complex.pdb structures/7UWO/7uwo_complex.cif 7UY1 classic PRMT5:MEP50 complex human Na Na fragment hit 5 (compound 5) "[""PJ0""]" 1 Kd Kd = = 53.0 µM 53000.0 [] unit_conversion 4.275724130399211 success True direct_binding SPR binding assay with PRMT5 protein immobilized; PRMT5/MTA complex formed by adding MTA (20 µM). 2 Table 1 reports fragment hit 5, PDB 7UY1, PRMT5/MTA K_D = 53.0 µM; the text states the fragment library was screened by SPR against PRMT5/MTA. auto_single_measurement only accepted activity measurement [1] 1 structures\7UY1\7UY1_metadata.json point structures/7UY1/7uy1_protein.pdb structures/7UY1/7uy1_pocket.pdb structures/7UY1/7uy1_ligand.sdf structures/7UY1/7uy1_ligand.pdb structures/7UY1/7uy1_ligand.cif structures/7UY1/7uy1_complex.pdb structures/7UY1/7uy1_complex.cif 7UYF classic PRMT5:MEP50 complex human Na Na fragment hit 4 (compound 4) "[""PUI""]" 1 Kd Kd = = 62.0 µM 62000.0 [] unit_conversion 4.2076083105017466 success True direct_binding SPR binding assay with PRMT5 protein immobilized; PRMT5/MTA complex formed by adding MTA (20 µM). 2 Table 1 reports fragment hit 4, PDB 7UYF, PRMT5/MTA K_D = 62.0 µM; the text states the fragment library was screened by SPR against PRMT5/MTA. auto_single_measurement only accepted activity measurement [1] 1 structures\7UYF\7UYF_metadata.json point structures/7UYF/7uyf_protein.pdb structures/7UYF/7uyf_pocket.pdb structures/7UYF/7uyf_ligand.sdf structures/7UYF/7uyf_ligand.pdb structures/7UYF/7uyf_ligand.cif structures/7UYF/7uyf_complex.pdb structures/7UYF/7uyf_complex.cif 7UYK extended RNF31 Na RNF31 UBA domain Na FP06655 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 37 nM 37.0 [] unit_conversion 7.431798275933005 success True direct_binding Surface plasmon resonance (SPR) sensogram; Figure 4D. 6 Figure 4D explicitly labels FP06655 KD = 37 nM, and its caption identifies the sensogram as binding of FP06655 to the RNF31 UBA domain. auto_single_measurement only accepted activity measurement [1] 1 structures\7UYK\7UYK_metadata.json point structures/7UYK/7uyk_protein.pdb structures/7UYK/7uyk_pocket.pdb structures/7UYK/7uyk_ligand.pdb structures/7UYK/7uyk_ligand.cif structures/7UYK/7uyk_complex.pdb structures/7UYK/7uyk_complex.cif 7UYR classic TYK2 Na Na Na compound 12 "[""OVI""]" 1 Ki Ki = = 7.8 nM 7.8 [] unit_conversion 8.10790539730952 success True biochemical_inhibition Assayed in duplicate; Ki reported as geometric mean; assay carried out at 10 µM ATP. 3 Table 2 lists compound 12 with TYK2 Ki = 7.8 nM. The table footnote states duplicate assays, geometric-mean Ki, at 10 µM ATP; page 4 maps compound 12 to TYK2 PDB 7UYR. auto_single_measurement only accepted activity measurement [1] 1 structures\7UYR\7UYR_metadata.json point structures/7UYR/7uyr_protein.pdb structures/7UYR/7uyr_pocket.pdb structures/7UYR/7uyr_ligand.sdf structures/7UYR/7uyr_ligand.pdb structures/7UYR/7uyr_ligand.cif structures/7UYR/7uyr_complex.pdb structures/7UYR/7uyr_complex.cif 7UYS classic TYK2 Na Na Na compound 16 "[""OVC""]" 1 Ki Ki = = 8.6 nM 8.6 [] unit_conversion 8.065501548756432 success True biochemical_inhibition Assayed in duplicate; Ki reported as geometric mean; assay carried out at 10 µM ATP. 3 Table 2 lists compound 16 with TYK2 Ki = 8.6 nM. The table footnote states duplicate assays, geometric-mean Ki, at 10 µM ATP; page 4 maps compound 16 to TYK2 PDB 7UYS. auto_single_measurement only accepted activity measurement [1] 1 structures\7UYS\7UYS_metadata.json point structures/7UYS/7uys_protein.pdb structures/7UYS/7uys_pocket.pdb structures/7UYS/7uys_ligand.sdf structures/7UYS/7uys_ligand.pdb structures/7UYS/7uys_ligand.cif structures/7UYS/7uys_complex.pdb structures/7UYS/7uys_complex.cif 7UYT classic TYK2 Na Na Na compound 25 "[""OV5""]" 1 Ki Ki = = 1.1 nM 1.1 [] unit_conversion 8.958607314841775 success True biochemical_inhibition Ki value in Table 5; Table 5 defines selectivity indices as JAK Ki/TYK2 Ki. 5 Table 5 lists compound 25 with TYK2 Ki = 1.1 nM; page 4 maps compound 25 bound to TYK2 to PDB 7UYT. auto_single_measurement only accepted activity measurement [1] 1 structures\7UYT\7UYT_metadata.json point structures/7UYT/7uyt_protein.pdb structures/7UYT/7uyt_pocket.pdb structures/7UYT/7uyt_ligand.sdf structures/7UYT/7uyt_ligand.pdb structures/7UYT/7uyt_ligand.cif structures/7UYT/7uyt_complex.pdb structures/7UYT/7uyt_complex.cif 7UYU classic TYK2 Na Na Na compound 30 "[""OV0""]" 1 Ki Ki = = 0.51 nM 0.51 [] unit_conversion 9.292429823902063 success True biochemical_inhibition Ki value in Table 7; Table 7 defines selectivity indices as JAK Ki/TYK2 Ki. 6 Table 7 lists compound 30 with TYK2 Ki = 0.51 nM; page 7 maps compound 30 bound to TYK2 to PDB 7UYU. auto_single_measurement only accepted activity measurement [1] 1 structures\7UYU\7UYU_metadata.json point structures/7UYU/7uyu_protein.pdb structures/7UYU/7uyu_pocket.pdb structures/7UYU/7uyu_ligand.sdf structures/7UYU/7uyu_ligand.pdb structures/7UYU/7uyu_ligand.cif structures/7UYU/7uyu_complex.pdb structures/7UYU/7uyu_complex.cif 7UZN classic BRD4 human Na Na BMT-206059; compound 15 "[""PQF""]" 1 IC50 IC50 = = 0.9 ± 0.2 nM 0.9 [] unit_conversion 9.045757490560675 success True direct_binding FRET binding assay; BRD4 IC50 reported in Table 1. 3 Table 1 reports for compound 15: BRD4 IC50 = 0.9 ± 0.2 nM. The text identifies compound 15 as bound to BRD4-BD1, PDB code 7UZN. auto_single_measurement only accepted activity measurement [1] 1 structures\7UZN\7UZN_metadata.json point structures/7UZN/7uzn_protein.pdb structures/7UZN/7uzn_pocket.pdb structures/7UZN/7uzn_ligand.sdf structures/7UZN/7uzn_ligand.pdb structures/7UZN/7uzn_ligand.cif structures/7UZN/7uzn_complex.pdb structures/7UZN/7uzn_complex.cif 7V1A extended talin Na R7R8 domains Na S-TBS (stapled TBS peptide from RIAM) "[""CHAIN:B""]" 1 Kd Kd = = 2.6 µM 2600.0 [] unit_conversion 5.585026652029182 success True direct_binding Fluorescence-polarization binding assay using fluorophore-labeled peptides and recombinant talin R7R8 domains. 4 Table 1 reports S-TBS binding to talin rod (R7R8) with Kd 2.6 µM; Figure 1C caption identifies this as an FP assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7V1A\7V1A_metadata.json point structures/7V1A/7v1a_protein.pdb structures/7V1A/7v1a_pocket.pdb structures/7V1A/7v1a_ligand.pdb structures/7V1A/7v1a_ligand.cif structures/7V1A/7v1a_complex.pdb structures/7V1A/7v1a_complex.cif 7V75 classic thermostabilized human prestin (PresTS) human thermostabilized prestin (PresTS) Na salicylate "[""SAL""]" 1 Kd Kd = = 12.1 mM 12100000.0 [] unit_conversion 1.9172146296835502 success True direct_binding Isothermal titration calorimetry (ITC) of salicylate binding to digitonin detergent-extracted PresTS. 5 “The dissociation constants (Kd) of salicylate to digitonin detergent-extracted hPres and PresTS were determined by isothermal titration calorimetry (ITC) to be 7.08 and 12.1 mM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7V75\7V75_metadata.json point structures/7V75/7v75_protein.pdb structures/7V75/7v75_pocket.pdb structures/7V75/7v75_ligand.sdf structures/7V75/7v75_ligand.pdb structures/7V75/7v75_ligand.cif structures/7V75/7v75_complex.pdb structures/7V75/7v75_complex.cif 7VC1 classic Prolyl-tRNA synthetase (TgPRS) Toxoplasma gondii Na Na L95 "[""JE6""]" 1 IC50 IC50 = = 140 nM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the TgPRS IC50 for L95 as 140 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VC1\7VC1_metadata.json point structures/7VC1/7vc1_protein.pdb structures/7VC1/7vc1_pocket.pdb structures/7VC1/7vc1_ligand.sdf structures/7VC1/7vc1_ligand.pdb structures/7VC1/7vc1_ligand.cif structures/7VC1/7vc1_complex.pdb structures/7VC1/7vc1_complex.cif 7VC2 classic Prolyl-tRNA synthetase (TgPRS) Toxoplasma gondii Na Na L96 "[""1UI""]" 1 IC50 IC50 = = 79 nM 79.0 [] unit_conversion 7.102372908709558 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the TgPRS IC50 for L96 as 79 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VC2\7VC2_metadata.json point structures/7VC2/7vc2_protein.pdb structures/7VC2/7vc2_pocket.pdb structures/7VC2/7vc2_ligand.sdf structures/7VC2/7vc2_ligand.pdb structures/7VC2/7vc2_ligand.cif structures/7VC2/7vc2_complex.pdb structures/7VC2/7vc2_complex.cif 7VC3 classic Prolyl-tRNA synthetase (TgPRS) Toxoplasma gondii Na Na L97 "[""1XK""]" 1 IC50 IC50 = = 50 nM 50.0 [] unit_conversion 7.301029995663981 success True biochemical_inhibition Purified-enzyme aminoacylation inhibition assay; L-proline and ATP present at 1.5× their Km concentrations. 13 Fig. 5C reports the TgPRS IC50 for L97 as 50 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VC3\7VC3_metadata.json point structures/7VC3/7vc3_protein.pdb structures/7VC3/7vc3_pocket.pdb structures/7VC3/7vc3_ligand.sdf structures/7VC3/7vc3_ligand.pdb structures/7VC3/7vc3_ligand.cif structures/7VC3/7vc3_complex.pdb structures/7VC3/7vc3_complex.cif 7VC8 classic AtHPPD Na Na Na PyQ3 "[""6I1""]" 1 Kd Kd = = 1.20 ± 0.175 μmol/L 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding Binding force assay; PyQ3 adhesion force to HPPD. 6 “the adhesion force obtained for PyQ3 (Kd = 1.20 ± 0.175 μmol/L …)” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7VC8\7VC8_metadata.json point structures/7VC8/7vc8_protein.pdb structures/7VC8/7vc8_pocket.pdb structures/7VC8/7vc8_ligand.sdf structures/7VC8/7vc8_ligand.pdb structures/7VC8/7vc8_ligand.cif structures/7VC8/7vc8_complex.pdb structures/7VC8/7vc8_complex.cif 7VD4 classic BPTF bromodomain human BPTF residues 2914-3037 Na TP-248 (TP248) "[""6FI""]" 1 IC50 IC50 = = 85.1 ± 2.5 nM 85.1 [] unit_conversion 7.070070439915412 success True biochemical_inhibition HTRF assay; BPTF BRD inhibition by TP-248. Values are mean ± SD of three measurements. 2 TP-248 exhibited an IC50 of 85 nM for BPTF BRD in the HTRF assay; Fig. 2A prints BPTF IC50 = 85.1 ± 2.5 nM. The same value is tabulated in Table 1. auto_single_measurement only accepted activity measurement [1] 1 structures\7VD4\7VD4_metadata.json point structures/7VD4/7vd4_protein.pdb structures/7VD4/7vd4_pocket.pdb structures/7VD4/7vd4_ligand.sdf structures/7VD4/7vd4_ligand.pdb structures/7VD4/7vd4_ligand.cif structures/7VD4/7vd4_complex.pdb structures/7VD4/7vd4_complex.cif 7VDP classic CDK5/p25 Na Na Na Compound 1 "[""65L""]" 1 IC50 IC50 = = 16 nM 16.0 [] unit_conversion 7.795880017344075 success True biochemical_inhibition In vitro kinase activity assay; Table 1. 3 Table 1 reports Compound 1 CDK5/p25 IC50 16 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VDP\7VDP_metadata.json point structures/7VDP/7vdp_protein.pdb structures/7VDP/7vdp_pocket.pdb structures/7VDP/7vdp_ligand.sdf structures/7VDP/7vdp_ligand.pdb structures/7VDP/7vdp_ligand.cif structures/7VDP/7vdp_complex.pdb structures/7VDP/7vdp_complex.cif 7VDQ classic CDK5/p25 Na Na Na Compound 7 "[""64V""]" 1 IC50 IC50 = = 4.5 nM 4.5 [] unit_conversion 8.346787486224656 success True biochemical_inhibition In vitro kinase activity assay; Table 1. 3 Table 1 reports Compound 7 CDK5/p25 IC50 4.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VDQ\7VDQ_metadata.json point structures/7VDQ/7vdq_protein.pdb structures/7VDQ/7vdq_pocket.pdb structures/7VDQ/7vdq_ligand.sdf structures/7VDQ/7vdq_ligand.pdb structures/7VDQ/7vdq_ligand.cif structures/7VDQ/7vdq_complex.pdb structures/7VDQ/7vdq_complex.cif 7VDR classic CDK5/p25 Na Na Na Compound 13 "[""63I""]" 1 IC50 IC50 = = 0.8 nM 0.8 [] unit_conversion 9.096910013008056 success True biochemical_inhibition In vitro kinase activity assay; Table 2. 4 Table 2 reports Compound 13 CDK5/p25 IC50 0.8 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VDR\7VDR_metadata.json point structures/7VDR/7vdr_protein.pdb structures/7VDR/7vdr_pocket.pdb structures/7VDR/7vdr_ligand.sdf structures/7VDR/7vdr_ligand.pdb structures/7VDR/7vdr_ligand.cif structures/7VDR/7vdr_complex.pdb structures/7VDR/7vdr_complex.cif 7VDS classic CDK5/p25 Na Na Na Compound 24 "[""61U""]" 1 IC50 IC50 = = 2.0 nM 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition In vitro kinase activity assay; Table 3. 4 Table 3 reports Compound 24 CDK5/p25 IC50 2.0 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VDS\7VDS_metadata.json point structures/7VDS/7vds_protein.pdb structures/7VDS/7vds_pocket.pdb structures/7VDS/7vds_ligand.sdf structures/7VDS/7vds_ligand.pdb structures/7VDS/7vds_ligand.cif structures/7VDS/7vds_complex.pdb structures/7VDS/7vds_complex.cif 7VE0 classic Plasmepsin II (PMII) Plasmodium falciparum Recombinant soluble thioredoxin-tagged truncated PMII (Trx-tPMII) Na Ritonavir (RTV) "[""RIT""]" 1 Ki Ki = = 0.3 µM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition PMII hydrolysis of an Hb-based fluorogenic peptide substrate; HIV-1 protease inhibitors tested against PMII. 2 All five inhibitors were active against PMII; ritonavir showed the highest inhibitory activity, with Ki 0.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VE0\7VE0_metadata.json point structures/7VE0/7ve0_protein.pdb structures/7VE0/7ve0_pocket.pdb structures/7VE0/7ve0_ligand.sdf structures/7VE0/7ve0_ligand.pdb structures/7VE0/7ve0_ligand.cif structures/7VE0/7ve0_complex.pdb structures/7VE0/7ve0_complex.cif 7VE2 classic Plasmepsin II (PMII) Plasmodium falciparum Recombinant soluble thioredoxin-tagged truncated PMII (Trx-tPMII) Na Lopinavir (LPV) "[""AB1""]" 1 Ki Ki = = 0.7 µM 700.0 [] unit_conversion 6.154901959985743 success True biochemical_inhibition PMII hydrolysis of an Hb-based fluorogenic peptide substrate; HIV-1 protease inhibitors tested against PMII. 2 All five inhibitors were active against PMII; lopinavir had Ki 0.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VE2\7VE2_metadata.json point structures/7VE2/7ve2_protein.pdb structures/7VE2/7ve2_pocket.pdb structures/7VE2/7ve2_ligand.sdf structures/7VE2/7ve2_ligand.pdb structures/7VE2/7ve2_ligand.cif structures/7VE2/7ve2_complex.pdb structures/7VE2/7ve2_complex.cif 7VEC extended GABARAP Homo sapiens GABARAP residues 1-116 complexed with TEX264 LIR residues 269-278 Na TEX264 LIR phosphorylated at Ser271 and Ser272 "[""POLYMER_ENTITY:2""]" 1 Kd Kd range range 0.25–0.52 µM 250.0 520.0 [] range_unit_conversion success True direct_binding Isothermal titration calorimetry (ITC; n = 1) of TEX264 LIR peptides with GABARAP. The paper states that the doubly phosphorylated p-Ser271,p-Ser272 peptide yielded sub-µM Kd values within the reported 0.25–0.52 µM range. 4 “multiple phosphorylations (p-S271, p-S272 and p-S269, p-S271, p-S272) further strengthened the affinity of TEX264 to LC3B and GABARAP, resulting in sub-µM Kd values (0.25–0.52 µM).” Figure 4A identifies the p-S271,p-S272 TEX264 269–278 peptide in the ITC series. auto_single_measurement only accepted activity measurement [1] 1 structures\7VEC\7VEC_metadata.json interval structures/7VEC/7vec_protein.pdb structures/7VEC/7vec_pocket.pdb structures/7VEC/7vec_ligand.pdb structures/7VEC/7vec_ligand.cif structures/7VEC/7vec_complex.pdb structures/7VEC/7vec_complex.cif 7VHY classic EP300 Na Na Na compound (+)-3 "[""6QI""]" 1 IC50 IC50 = = 0.050 μM 50.0 [] unit_conversion 7.301029995663981 success True biochemical_inhibition HAT EP300 inhibition assay 2 Table 1 reports HAT EP300 IC50 = 0.050 μM for (+)-3; Figure 3 identifies (+)-3 bound to EP300 as PDB ID 7VHY. auto_single_measurement only accepted activity measurement [1] 1 structures\7VHY\7VHY_metadata.json point structures/7VHY/7vhy_protein.pdb structures/7VHY/7vhy_pocket.pdb structures/7VHY/7vhy_ligand.sdf structures/7VHY/7vhy_ligand.pdb structures/7VHY/7vhy_ligand.cif structures/7VHY/7vhy_complex.pdb structures/7VHY/7vhy_complex.cif 7VHZ classic EP300 Na Na Na compound 7 "[""6TI""]" 1 IC50 IC50 = = 0.18 μM 180.0 [] unit_conversion 6.7447274948966935 success True biochemical_inhibition HAT EP300 inhibition assay 3 Table 2 reports HAT EP300 IC50 = 0.18 μM for compound 7; the text and Figure 4 identify compound 7 bound to EP300 as PDB ID 7VHZ. auto_single_measurement only accepted activity measurement [1] 1 structures\7VHZ\7VHZ_metadata.json point structures/7VHZ/7vhz_protein.pdb structures/7VHZ/7vhz_pocket.pdb structures/7VHZ/7vhz_ligand.sdf structures/7VHZ/7vhz_ligand.pdb structures/7VHZ/7vhz_ligand.cif structures/7VHZ/7vhz_complex.pdb structures/7VHZ/7vhz_complex.cif 7VI0 classic EP300 Na Na Na compound 11 (DS17701585) "[""6YI""]" 1 IC50 IC50 = = 0.15 μM 150.0 [] unit_conversion 6.823908740944319 success True biochemical_inhibition HAT EP300 inhibition assay 3 Table 3 reports HAT EP300 IC50 = 0.15 μM for compound 11 (DS17701585). auto_single_measurement only accepted activity measurement [1] 1 structures\7VI0\7VI0_metadata.json point structures/7VI0/7vi0_protein.pdb structures/7VI0/7vi0_pocket.pdb structures/7VI0/7vi0_ligand.sdf structures/7VI0/7vi0_ligand.pdb structures/7VI0/7vi0_ligand.cif structures/7VI0/7vi0_complex.pdb structures/7VI0/7vi0_complex.cif 7VIC classic SARS-CoV-2 3CLpro Na Full-length SARS-CoV-2 3CLpro, codon-optimized and expressed in pET20b with a C-terminal 6xHis tag Na Oridonin "[""ODN""]" 2 Ki Ki = = 4.49 ± 0.86 µM 4490.0 [] unit_conversion 5.347753658996677 success True biochemical_inhibition Time-dependent enzyme-kinetic study of purified 3CLpro incubated with Oridonin; kobs was fitted against Oridonin concentration. 4 Figure 3d reports Ki = 4.49 ± 0.86 µM for Oridonin with 3CLpro. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7VIC\7VIC_metadata.json point structures/7VIC/7vic_protein.pdb structures/7VIC/7vic_pocket.pdb structures/7VIC/7vic_ligand.sdf structures/7VIC/7vic_ligand.pdb structures/7VIC/7vic_ligand.cif structures/7VIC/7vic_complex.pdb structures/7VIC/7vic_complex.cif 7VJV classic human AlkB homolog ALKBH6 human full-length ALKBH6 Na alpha-ketoglutarate (alpha-KG) "[""AKG""]" 1 Kd Kd = = 11.9 ± 0.7 µM 11900.0 [] unit_conversion 4.924453038607469 success True direct_binding Microscale thermophoresis measurement of fluorescently labelled ALKBH6 with alpha-KG at varied concentrations; assay buffer contained 5 µM MnCl2. 3 Figure 2C explicitly reports alpha-KG binding: WT ALKBH6 K_D (µM) = 11.9 ± 0.7. The figure caption states this is binding analysis of ALKBH6 with alpha-KG. auto_single_measurement only accepted activity measurement [1] 1 structures\7VJV\7VJV_metadata.json point structures/7VJV/7vjv_protein.pdb structures/7VJV/7vjv_pocket.pdb structures/7VJV/7vjv_ligand.sdf structures/7VJV/7vjv_ligand.pdb structures/7VJV/7vjv_ligand.cif structures/7VJV/7vjv_complex.pdb structures/7VJV/7vjv_complex.cif 7VKA classic GH3.6 Arabidopsis Na Na D4 "[""7IS""]" 1 Ki Ki = = 0.3 ± 0.02 µM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition In vitro kinetic inhibition of GH3.6 by D4; IAA-Asp production was detected by UPLC-MS and double-reciprocal initial-velocity plots were used. 7 Fig. 4F reports kinetic analysis of D4 inhibition of GH3.6 with “Ki = 0.3 ± 0.02 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7VKA\7VKA_metadata.json point structures/7VKA/7vka_protein.pdb structures/7VKA/7vka_pocket.pdb structures/7VKA/7vka_ligand.sdf structures/7VKA/7vka_ligand.pdb structures/7VKA/7vka_ligand.cif structures/7VKA/7vka_complex.pdb structures/7VKA/7vka_complex.cif 7VKG classic AF9 Na AF9 YEATS domain, residues 1-138 Na Compound 10 "[""7IV""]" 1 Kd Kd = = 0.038 ± 0.006 mM 38000.0 [] unit_conversion 4.42021640338319 success True direct_binding Dose-dependent 15N-AF9 YEATS chemical-shift-perturbation binding assay; Table 1 reports Kd values determined from dose-dependent CSPs. 4 Table 1 lists Compound 10 with Kd = 0.038 ± 0.006 mM; the footnote states Kd values were determined from dose-dependent chemical shift perturbations. auto_single_measurement only accepted activity measurement [1] 1 structures\7VKG\7VKG_metadata.json point structures/7VKG/7vkg_protein.pdb structures/7VKG/7vkg_pocket.pdb structures/7VKG/7vkg_ligand.sdf structures/7VKG/7vkg_ligand.pdb structures/7VKG/7vkg_ligand.cif structures/7VKG/7vkg_complex.pdb structures/7VKG/7vkg_complex.cif 7VKQ classic SAMTOR (dSAMTOR) Drosophila melanogaster Full-length WT dSAMTOR; crystal contains mainly the C-terminal MTase fragment WT (wild type) SAH (S-adenosyl-L-homocysteine) "[""SAH""]" 1 Kd Kd = = 13.10 ± 0.80 μM 13100.0 [] unit_conversion 4.882728704344236 success True direct_binding ITC of N-terminally truncated dSAMTOR (Δ1-64) with SAH; the crystallized material mainly comprises this C-terminal fragment. 4 Table 1 reports Δ1-64 dSAMTOR–SAH Kd = 13.10 ± 0.80 μM; the text identifies the crystals as mainly the C-terminal fragment corresponding to Δ1-64. auto_single_measurement only accepted activity measurement [1] 1 structures\7VKQ\7VKQ_metadata.json point structures/7VKQ/7vkq_protein.pdb structures/7VKQ/7vkq_pocket.pdb structures/7VKQ/7vkq_ligand.sdf structures/7VKQ/7vkq_ligand.pdb structures/7VKQ/7vkq_ligand.cif structures/7VKQ/7vkq_complex.pdb structures/7VKQ/7vkq_complex.cif 7VKR classic SAMTOR (dSAMTOR) Drosophila melanogaster Full-length WT dSAMTOR; crystal contains mainly the C-terminal MTase fragment WT (wild type) SAM (S-adenosylmethionine) "[""SAM""]" 1 Kd Kd = = 6.78 ± 0.75 μM 6780.0 [] unit_conversion 5.168770306132936 success True direct_binding ITC of N-terminally truncated dSAMTOR (Δ1-64) with SAM; the crystallized material mainly comprises this C-terminal fragment. 4 Table 1 reports Δ1-64 dSAMTOR–SAM Kd = 6.78 ± 0.75 μM; the text identifies the crystals as mainly the C-terminal fragment corresponding to Δ1-64. auto_single_measurement only accepted activity measurement [1] 1 structures\7VKR\7VKR_metadata.json point structures/7VKR/7vkr_protein.pdb structures/7VKR/7vkr_pocket.pdb structures/7VKR/7vkr_ligand.sdf structures/7VKR/7vkr_ligand.pdb structures/7VKR/7vkr_ligand.cif structures/7VKR/7vkr_complex.pdb structures/7VKR/7vkr_complex.cif 7VLN classic NSD2-PWWP1 Na NSD2-PWWP1 residues 211-350 expressed from pET-28 with an N-terminal His6 or SUMO tag Na compound 5 "[""7QC""]" 1 IC50 IC50 = = 4.44 ± 3.30 μM 4440.0 [] unit_conversion 5.35261702988538 success True biochemical_inhibition HTRF NSD2-PWWP1 binding assay; Table 1 reports mean ± SD from at least two separate determinations. 3 Table 1 lists compound 5 with NSD2 IC50 = 4.44 ± 3.30 μM; the accompanying text states that compound 5 showed binding affinity to the NSD2 PWWP1 domain. Figure 3 identifies the NSD2-PWWP1/compound 5 crystal structure as PDB 7VLN. auto_single_measurement only accepted activity measurement [1] 1 structures\7VLN\7VLN_metadata.json point structures/7VLN/7vln_protein.pdb structures/7VLN/7vln_pocket.pdb structures/7VLN/7vln_ligand.sdf structures/7VLN/7vln_ligand.pdb structures/7VLN/7vln_ligand.cif structures/7VLN/7vln_complex.pdb structures/7VLN/7vln_complex.cif 7VLP classic SARS-CoV-2 main protease SARS-CoV-2 Codon-optimized main protease fused with 6x His at the N terminus Na PF-07321332 "[""4WI""]" 1 IC50 IC50 = = 0.023 µM 23.0 [] unit_conversion 7.638272163982407 success True biochemical_inhibition Purified SARS-CoV-2 Mpro; fluorescence resonance energy transfer (FRET) enzymatic inhibition assay. Protein was preincubated with PF-07321332 for 30 min before addition of FRET substrate. 3 Figure 1B and accompanying Results text explicitly report that PF-07321332 inhibits SARS-CoV-2 Mpro with an IC50 of 0.023 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VLP\7VLP_metadata.json point structures/7VLP/7vlp_protein.pdb structures/7VLP/7vlp_pocket.pdb structures/7VLP/7vlp_ligand.sdf structures/7VLP/7vlp_ligand.pdb structures/7VLP/7vlp_ligand.cif structures/7VLP/7vlp_complex.pdb structures/7VLP/7vlp_complex.cif 7VLQ classic SARS-CoV-2 main protease SARS-CoV-2 Codon-optimized main protease fused with 6x His at the N terminus Na PF-07321332 "[""4WI""]" 1 IC50 IC50 = = 0.023 µM 23.0 [] unit_conversion 7.638272163982407 success True biochemical_inhibition Purified SARS-CoV-2 Mpro; fluorescence resonance energy transfer (FRET) enzymatic inhibition assay. Protein was preincubated with PF-07321332 for 30 min before addition of FRET substrate. 3 Figure 1B and accompanying Results text explicitly report that PF-07321332 inhibits SARS-CoV-2 Mpro with an IC50 of 0.023 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VLQ\7VLQ_metadata.json point structures/7VLQ/7vlq_protein.pdb structures/7VLQ/7vlq_pocket.pdb structures/7VLQ/7vlq_ligand.sdf structures/7VLQ/7vlq_ligand.pdb structures/7VLQ/7vlq_ligand.cif structures/7VLQ/7vlq_complex.pdb structures/7VLQ/7vlq_complex.cif 7VM5 classic urokinase-type plasminogen activator (uPA) human recombinant serine protease domain Na 4-guanidinobenzoic acid (GBA) "[""GBS""]" 1 IC50 IC50 = = 37.8 ± 8.7 µM 37800.0 [] unit_conversion 4.422508200162775 success True biochemical_inhibition Purified recombinant uPA serine protease; chromogenic-substrate inhibition assay under steady-state conditions. 4 Figure 3B visibly reports “IC50 = 37.8 ± 8.7 µM” for GBA against uPA. auto_single_measurement only accepted activity measurement [1] 1 structures\7VM5\7VM5_metadata.json point structures/7VM5/7vm5_protein.pdb structures/7VM5/7vm5_pocket.pdb structures/7VM5/7vm5_ligand.sdf structures/7VM5/7vm5_ligand.pdb structures/7VM5/7vm5_ligand.cif structures/7VM5/7vm5_complex.pdb structures/7VM5/7vm5_complex.cif 7VM6 classic urokinase-type plasminogen activator (uPA) human recombinant serine protease domain Na 6-amidino-2-naphthol (6A2N) "[""7R8""]" 1 IC50 IC50 = = 12.1 ± 2.4 µM 12100.0 [] unit_conversion 4.91721462968355 success True biochemical_inhibition Purified recombinant uPA serine protease; chromogenic-substrate inhibition assay under steady-state conditions. 4 Figure 3C visibly reports “IC50 = 12.1 ± 2.4 µM” for 6A2N against uPA. auto_single_measurement only accepted activity measurement [1] 1 structures\7VM6\7VM6_metadata.json point structures/7VM6/7vm6_protein.pdb structures/7VM6/7vm6_pocket.pdb structures/7VM6/7vm6_ligand.sdf structures/7VM6/7vm6_ligand.pdb structures/7VM6/7vm6_ligand.cif structures/7VM6/7vm6_complex.pdb structures/7VM6/7vm6_complex.cif 7VNH classic Drosophila AHR PAS-B domain Drosophila melanogaster PAS-B domain, residues 264-381 Na alpha-naphthoflavone (aNF) "[""BHF""]" 1 Kd Kd = = 232 nM 232.0 [] unit_conversion 6.634512015109101 success True direct_binding Microscale thermophoresis binding assay of purified dAHR PAS-B to αNF. 3 Fig. 2b prints “αNF Kd = 232 nM.” auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\7VNH\7VNH_metadata.json point structures/7VNH/7vnh_protein.pdb structures/7VNH/7vnh_pocket.pdb structures/7VNH/7vnh_ligand.sdf structures/7VNH/7vnh_ligand.pdb structures/7VNH/7vnh_ligand.cif structures/7VNH/7vnh_complex.pdb structures/7VNH/7vnh_complex.cif 7VOD classic 5-HT2AR Na Na Na cariprazine "[""7RU""]" 1 Kd Kd = = 6.40±0.96 nM 6.4 [] unit_conversion 8.193820026016112 success True direct_binding WT 5-HT2AR affinity measurement. 5 Supplementary Table 3 lists WT 5-HT2AR cariprazine Kd, 6.40±0.96 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7VOD\7VOD_metadata.json point structures/7VOD/7vod_protein.pdb structures/7VOD/7vod_pocket.pdb structures/7VOD/7vod_ligand.sdf structures/7VOD/7vod_ligand.pdb structures/7VOD/7vod_ligand.cif structures/7VOD/7vod_complex.pdb structures/7VOD/7vod_complex.cif 7VOE classic 5-HT2AR Na Na Na aripiprazole "[""9SC""]" 1 Kd Kd = = 6.40±0.96 nM 6.4 [] unit_conversion 8.193820026016112 success True direct_binding WT 5-HT2AR affinity measurement. 4 Supplementary Table 2 lists WT 5-HT2AR aripiprazole Kd, 6.40±0.96 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7VOE\7VOE_metadata.json point structures/7VOE/7voe_protein.pdb structures/7VOE/7voe_pocket.pdb structures/7VOE/7voe_ligand.sdf structures/7VOE/7voe_ligand.pdb structures/7VOE/7voe_ligand.cif structures/7VOE/7voe_complex.pdb structures/7VOE/7voe_complex.cif 7VPG extended human Rae1-Nup98 human Rae1 residues 1-368 with Nup98 GLEBS residues 157-213, complexed with SARS-CoV-1 Orf6 C-terminal tail peptide residues 42-63 Na SARS-CoV-1 Orf6 C-terminal tail peptide, residues 42-63 "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:X""]" 1 Kd Kd = = 277.8 nM 277.8 [] unit_conversion 6.556267758598404 success True direct_binding Isothermal titration calorimetry (ITC) of the SARS-CoV-1 Orf6 C-terminal-tail peptide with the Rae1–Nup98GLEBS complex; 1:1 binding. 4 Figure 1B and the accompanying text report that the SARS-CoV-1 Orf6CTT peptide bound Rae1–Nup98GLEBS with Kd = 277.8 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VPG\7VPG_metadata.json point structures/7VPG/7vpg_protein.pdb structures/7VPG/7vpg_pocket.pdb structures/7VPG/7vpg_ligand.pdb structures/7VPG/7vpg_ligand.cif structures/7VPG/7vpg_complex.pdb structures/7VPG/7vpg_complex.cif 7VPH extended human Rae1-Nup98 human Rae1 residues 1-368 with Nup98 GLEBS residues 157-213, complexed with SARS-CoV-2 Orf6 C-terminal tail peptide residues 41-61 Na SARS-CoV-2 Orf6 C-terminal tail peptide, residues 41-61 "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:X""]" 1 Kd Kd = = 141.6 nM 141.6 [] unit_conversion 6.84893674664625 success True direct_binding Isothermal titration calorimetry (ITC) of the SARS-CoV-2 Orf6 C-terminal-tail peptide with the Rae1–Nup98GLEBS complex; 1:1 binding. 4 Figure 1B and the accompanying text report that the SARS-CoV-2 Orf6CTT peptide bound Rae1–Nup98GLEBS with Kd = 141.6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VPH\7VPH_metadata.json point structures/7VPH/7vph_protein.pdb structures/7VPH/7vph_pocket.pdb structures/7VPH/7vph_ligand.pdb structures/7VPH/7vph_ligand.cif structures/7VPH/7vph_complex.pdb structures/7VPH/7vph_complex.cif 7VQF classic MopR Acinetobacter calcoaceticus NCIB8250 Sensor-domain construct, His-tagged G148P phenol "[""IPH""]" 1 Kd Kd = = 0.07 ± 0.02 µM 70.0 [] unit_conversion 7.154901959985743 success True direct_binding Isothermal titration calorimetry (ITC) of phenol with MopR G148P sensor-domain construct; the text reports a 7-fold higher affinity than WT. 6 “ITC studies show that MopRG148P exhibits a 7-fold higher binding affinity compared to MopRAB toward phenol ... with a Kd value of (0.07 ± 0.02 μM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7VQF\7VQF_metadata.json point structures/7VQF/7vqf_protein.pdb structures/7VQF/7vqf_pocket.pdb structures/7VQF/7vqf_ligand.sdf structures/7VQF/7vqf_ligand.pdb structures/7VQF/7vqf_ligand.cif structures/7VQF/7vqf_complex.pdb structures/7VQF/7vqf_complex.cif 7VRG classic OfChi-h (chitinase-h) Ostrinia furnacalis Na Na Lynamicin B "[""7U8""]" 2 Kd Kd = = 19.21 μM 19210.0 [] unit_conversion 4.716472635138306 success True direct_binding Tryptophan fluorescence spectroscopy monitoring Lynamicin B binding to OfChi-h. 3 “The Kd of lynamicin B for OfChi-h was determined to be 19.21 μM (Figure 2C, inset).” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7VRG\7VRG_metadata.json point structures/7VRG/7vrg_protein.pdb structures/7VRG/7vrg_pocket.pdb structures/7VRG/7vrg_ligand.sdf structures/7VRG/7vrg_ligand.pdb structures/7VRG/7vrg_ligand.cif structures/7VRG/7vrg_complex.pdb structures/7VRG/7vrg_complex.cif 7VTH classic SARS-CoV-2 3CL protease (3CLpro) Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) SARS-CoV-2 3CLpro residues 1-306, C-terminal His-tag free Na compound 1 "[""7XB""]" 1 IC50 IC50 = = 8.6 µM 8600.0 [] unit_conversion 5.065501548756432 success True biochemical_inhibition 3CL protease enzymatic inhibition assay. 3 Figure 3 reports compound 1 with SARS-CoV-2 3CLpro IC50 = 8.6 µM; the text identifies this as an enzymatic inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7VTH\7VTH_metadata.json point structures/7VTH/7vth_protein.pdb structures/7VTH/7vth_pocket.pdb structures/7VTH/7vth_ligand.sdf structures/7VTH/7vth_ligand.pdb structures/7VTH/7vth_ligand.cif structures/7VTH/7vth_complex.pdb structures/7VTH/7vth_complex.cif 7VU6 classic SARS-CoV-2 3CL protease (3CLpro) Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) SARS-CoV-2 3CLpro residues 1-306, N-terminal His-tag free Na compound 3 (S-217622) "[""7YY""]" 1 IC50 IC50 = = 0.013 µM 13.0 [] unit_conversion 7.886056647693163 success True biochemical_inhibition 3CL protease enzymatic inhibition assay. 3 Figure 3 reports compound 3 (S-217622) with SARS-CoV-2 3CLpro IC50 = 0.013 µM; the text identifies this as an enzymatic inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7VU6\7VU6_metadata.json point structures/7VU6/7vu6_protein.pdb structures/7VU6/7vu6_pocket.pdb structures/7VU6/7vu6_ligand.sdf structures/7VU6/7vu6_ligand.pdb structures/7VU6/7vu6_ligand.cif structures/7VU6/7vu6_complex.pdb structures/7VU6/7vu6_complex.cif 7VUN classic human PD-L1 Homo sapiens residues 18-134, C-terminal His tag Na P39 "[""8H7""]" 2 Kd Kd = = 24.4 ± 0.02 nmol/L 24.4 [] unit_conversion 7.61261017366127 success True direct_binding Microscale thermophoresis (MST) of P39 binding purified hPD-L1 ligand-binding domain. 6 The paper states that MST gave a KD of 24.4 ± 0.02 nmol/L for P39 binding to hPD-L1. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7VUN\7VUN_metadata.json point structures/7VUN/7vun_protein.pdb structures/7VUN/7vun_pocket.pdb structures/7VUN/7vun_ligand.sdf structures/7VUN/7vun_ligand.pdb structures/7VUN/7vun_ligand.cif structures/7VUN/7vun_complex.pdb structures/7VUN/7vun_complex.cif 7VVP classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 N-terminal 6xHis-tagged recombinant Mpro expressed from pET-28a; His tag removed by TEV protease Na PF-07304814 "[""80I""]" 1 IC50 IC50 = = 0.692 µM 692.0 [] unit_conversion 6.1598939055432425 success True biochemical_inhibition FRET-based enzymatic inhibition assay using purified SARS-CoV-2 Mpro. 3 Figure 1A prints “PF-07304814 against SARS-CoV-2 Mpro” and IC50 = 0.692 µM; Figure 1 caption identifies enzymatic inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7VVP\7VVP_metadata.json point structures/7VVP/7vvp_protein.pdb structures/7VVP/7vvp_pocket.pdb structures/7VVP/7vvp_ligand.sdf structures/7VVP/7vvp_ligand.pdb structures/7VVP/7vvp_ligand.cif structures/7VVP/7vvp_complex.pdb structures/7VVP/7vvp_complex.cif 7VXG classic SHP2 (non-receptor protein tyrosine phosphatase 2) human Residues Met1-Leu525 with an N-terminal 6xHis tag followed by a TEV protease cleavage site Na TK-453 "[""83Q""]" 1 Kd Kd = = 150 nM 150.0 [] unit_conversion 6.823908740944319 success True direct_binding Isothermal titration calorimetry of TK-453 with purified SHP2-WT protein. 5 “isothermal titration calorimetry (ITC) with compound TK-453 and SHP2-WT, and obtained a K_D value of 150 nM.” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7VXG\7VXG_metadata.json point structures/7VXG/7vxg_protein.pdb structures/7VXG/7vxg_pocket.pdb structures/7VXG/7vxg_ligand.sdf structures/7VXG/7vxg_ligand.pdb structures/7VXG/7vxg_ligand.cif structures/7VXG/7vxg_complex.pdb structures/7VXG/7vxg_complex.cif 7VXX classic Zika virus NS2B/NS3 protease (bZiPro) Zika virus NS3 residues 1-177 with an N-terminal His-tag plus NS2B residues 46-99; recombinant bZiPro C143S 4-amino benzamidine; compound 2 "[""PBZ""]" 1 IC50 IC50 = = 1136.0 ± 48.79 µM 1136000.0 [] unit_conversion 2.9446216686249995 success True biochemical_inhibition Purified bZiPro enzyme inhibition assay using Bz-Nle-Lys-Lys-Arg-AMC substrate; fluorescence monitored at 340/440 nm. 2 Fig. 1B visibly reports for compound 2: IC50 = 1136.0 ± 48.79 µM against ZIKV NS2B/NS3 protease. auto_single_measurement only accepted activity measurement [1] 1 structures\7VXX\7VXX_metadata.json point structures/7VXX/7vxx_protein.pdb structures/7VXX/7vxx_pocket.pdb structures/7VXX/7vxx_ligand.sdf structures/7VXX/7vxx_ligand.pdb structures/7VXX/7vxx_ligand.cif structures/7VXX/7vxx_complex.pdb structures/7VXX/7vxx_complex.cif 7VXY extended Zika virus NS2B/NS3 protease (bZiPro) Zika virus NS3 residues 1-177 with an N-terminal His-tag plus NS2B residues 46-99; recombinant bZiPro C143S D-RKOR; compound 1 "[""CHAIN:E""]" 2 Kd Kd = = 29.98 µM 29980.0 [] unit_conversion 4.523168371487739 success True direct_binding Isothermal titration calorimetry of compound 1 binding purified bZiPro; one-binding-site fitting model. 4 Table 1 visibly reports Kd = 29.98 µM for compound 1 binding to ZIKV NS2B/NS3 protease (bZiPro); the text identifies the tetrapeptide as compound 1 and reports the same Kd. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7VXY\7VXY_metadata.json point structures/7VXY/7vxy_protein.pdb structures/7VXY/7vxy_pocket.pdb structures/7VXY/7vxy_ligand.pdb structures/7VXY/7vxy_ligand.cif structures/7VXY/7vxy_complex.pdb structures/7VXY/7vxy_complex.cif 7VZ6 classic KasQ (non-hydrolyzing UDP-GlcNAc 2-epimerase) Streptomyces kasugaensis N-terminal His6-tagged KasQ WT UDP-glucose (UDP-Glc) "[""UPG""]" 1 Kd Kd = = 9.5 ± 0.3 µM 9500.0 [] unit_conversion 5.022276394711152 success True direct_binding Isothermal titration calorimetry (25 °C); KasQ versus UDP-Glc. 13 Table 4 reports KasQ binding to UDP-Glc with Kd 9.5 ± 0.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VZ6\7VZ6_metadata.json point structures/7VZ6/7vz6_protein.pdb structures/7VZ6/7vz6_pocket.pdb structures/7VZ6/7vz6_ligand.sdf structures/7VZ6/7vz6_ligand.pdb structures/7VZ6/7vz6_ligand.cif structures/7VZ6/7vz6_complex.pdb structures/7VZ6/7vz6_complex.cif 7VZA classic KasQ (non-hydrolyzing UDP-GlcNAc 2-epimerase) Streptomyces kasugaensis N-terminal His6-tagged KasQ WT UDP "[""UDP""]" 1 Kd Kd = = 32.2 ± 6.8 µM 32200.000000000004 [] unit_conversion 4.492144128304169 success True direct_binding Isothermal titration calorimetry (25 °C); KasQ versus UDP. 13 Table 4 reports KasQ binding to UDP with Kd 32.2 ± 6.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7VZA\7VZA_metadata.json point structures/7VZA/7vza_protein.pdb structures/7VZA/7vza_pocket.pdb structures/7VZA/7vza_ligand.sdf structures/7VZA/7vza_ligand.pdb structures/7VZA/7vza_ligand.cif structures/7VZA/7vza_complex.pdb structures/7VZA/7vza_complex.cif 7VZE extended Human protein tyrosine phosphatase non-receptor type 4 (PTPN4) PDZ domain human PTPN4 residues 500-604; N-terminal His10-GST tag removed before crystallization Na HPV16 E6 PBM peptide residues 152-158 (TRRETQL) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 Kd Kd = = 18.8 µM 18800.0 [] unit_conversion 4.72584215073632 success True direct_binding ITC using purified recombinant PTPN4 PDZ domain and synthetic 7-mer HPV16 E6 peptide; Fig. 1B/Table 1. 2 The table lists HPV16 E6(152–158), sequence TRRETQL, with KD 18.8 µM by ITC ('This study'). auto_single_measurement only accepted activity measurement [1] 1 structures\7VZE\7VZE_metadata.json point structures/7VZE/7vze_protein.pdb structures/7VZE/7vze_pocket.pdb structures/7VZE/7vze_ligand.pdb structures/7VZE/7vze_ligand.cif structures/7VZE/7vze_complex.pdb structures/7VZE/7vze_complex.cif 7W28 extended SETD3 human SETD3 residues 1-497 Na betaA-4PyrAla73 peptide "[""CHAIN:P""]" 1 Kd Kd = = 3.1 ± 0.7 µM 3100.0 [] unit_conversion 5.508638306165727 success True direct_binding ITC titration of SETD3(1–497) preincubated with SAH; βA-4PyrAla73 peptide titrated into the SETD3–SAH complex. 9 Figure 5c lists K_D = 3.1 ± 0.7 µM for βA-4PyrAla73 with hSETD3–SAH. The text identifies the 7W28 ternary complex as SETD3–βA-4PyrAla73–SAH. auto_single_measurement only accepted activity measurement [1] 1 structures\7W28\7W28_metadata.json point structures/7W28/7w28_protein.pdb structures/7W28/7w28_pocket.pdb structures/7W28/7w28_ligand.pdb structures/7W28/7w28_ligand.cif structures/7W28/7w28_complex.pdb structures/7W28/7w28_complex.cif 7W29 extended SETD3 human SETD3 residues 1-497 Na betaA-Orn73 peptide "[""CHAIN:P""]" 1 Kd Kd = = 7.2 ± 1.3 µM 7200.0 [] unit_conversion 5.142667503568731 success True direct_binding ITC titration of SETD3(1–497) preincubated with SAH; βA-Orn73 peptide titrated into the SETD3–SAH complex. 9 Figure 5c lists K_D = 7.2 ± 1.3 µM for βA-Orn73 with hSETD3–SAH. The text identifies the 7W29 ternary complex as SETD3–βA-Orn73–SAH. auto_single_measurement only accepted activity measurement [1] 1 structures\7W29\7W29_metadata.json point structures/7W29/7w29_protein.pdb structures/7W29/7w29_pocket.pdb structures/7W29/7w29_ligand.pdb structures/7W29/7w29_ligand.cif structures/7W29/7w29_complex.pdb structures/7W29/7w29_complex.cif 7W2P classic SMN Na SMN aa 82-147 Na compound 4 "[""8AI""]" 1 Kd Kd = = 13 ± 1 µM 13000.0 [] unit_conversion 4.886056647693163 success True direct_binding ITC measurement of compound 4 binding to purified SMN Tudor domain (SMN aa 82–147). 6 Table 2 reports compound 4 SMN Kd 13 ± 1 µM and states that the ITC data are representative of two independent experiments. Table 1 maps 7W2P to SMN–compound 4. auto_single_measurement only accepted activity measurement [1] 1 structures\7W2P\7W2P_metadata.json point structures/7W2P/7w2p_protein.pdb structures/7W2P/7w2p_pocket.pdb structures/7W2P/7w2p_ligand.sdf structures/7W2P/7w2p_ligand.pdb structures/7W2P/7w2p_ligand.cif structures/7W2P/7w2p_complex.pdb structures/7W2P/7w2p_complex.cif 7W30 classic SMN Na SMN aa 82-147 Na compound 6 "[""8AT""]" 1 Kd Kd = = 12 ± 2 µM 12000.0 [] unit_conversion 4.920818753952375 success True direct_binding ITC measurement of compound 6 binding to purified SMN Tudor domain (SMN aa 82–147). 6 Table 2 reports compound 6 SMN Kd 12 ± 2 µM and states that the ITC data are representative of two independent experiments. Table 1 maps 7W30 to SMN–compound 6. auto_single_measurement only accepted activity measurement [1] 1 structures\7W30\7W30_metadata.json point structures/7W30/7w30_protein.pdb structures/7W30/7w30_pocket.pdb structures/7W30/7w30_ligand.sdf structures/7W30/7w30_ligand.pdb structures/7W30/7w30_ligand.cif structures/7W30/7w30_complex.pdb structures/7W30/7w30_complex.cif 7W36 extended human ATG5 human ATG5(1-275)-His6 Na stapled peptide 7 "[""CHAIN:B""]" 1 Kd Kd = = 0.032±0.013 µM 32.0 [] unit_conversion 7.494850021680094 success True direct_binding Isothermal titration calorimetry (ITC) of purified ATG5 with peptide 7. 3 Table 1 reports peptide 7 Kd = 0.032±0.013 µM; the text states these affinities were evaluated toward purified ATG5 by ITC. Figure 5 maps peptide 7 bound to ATG5 to PDB 7W36. auto_single_measurement only accepted activity measurement [1] 1 structures\7W36\7W36_metadata.json point structures/7W36/7w36_protein.pdb structures/7W36/7w36_pocket.pdb structures/7W36/7w36_ligand.pdb structures/7W36/7w36_ligand.cif structures/7W36/7w36_complex.pdb structures/7W36/7w36_complex.cif 7W3S classic Larg1 (Lpg0081; Legionella ADP-ribose glycohydrolase 1) Legionella pneumophila Lpg0081/Larg1 residues 16-428 aa, expressed from a pET28a-SUMO construct Na ADPR (ADP-ribose) "[""AR6""]" 1 Kd Kd = = 3.868 µM 3868.0 [] unit_conversion 5.412513534589036 success True direct_binding Isothermal titration calorimetry of Larg1 binding to ADPR. 7 Figure 5C lists the WT Larg1–ADPR dissociation constant as 3.868 µM; the caption states binding affinity was evaluated using isothermal titration calorimetry. auto_single_measurement only accepted activity measurement [1] 1 structures\7W3S\7W3S_metadata.json point structures/7W3S/7w3s_protein.pdb structures/7W3S/7w3s_pocket.pdb structures/7W3S/7w3s_ligand.sdf structures/7W3S/7w3s_ligand.pdb structures/7W3S/7w3s_ligand.cif structures/7W3S/7w3s_complex.pdb structures/7W3S/7w3s_complex.cif 7W47 classic gastric H+,K+-ATPase pig N-terminally Flag- and GFP-tagged H+,K+-ATPase (Flag-GFP-TEVsite-Met48-H+,K+-ATPase) and WT beta-subunit Na tegoprazan "[""8BN""]" 1 IC50 IC50 = = 2.3 ± 0.57 µM 2300.0 [] unit_conversion 5.638272163982407 success True biochemical_inhibition Dose-dependent inhibition of recombinant H+,K+-ATPase activity at pH 7.0; membrane-fraction assay with 10 mM KCl. Table reports the WT value. 5 Table 1 reports WT tegoprazan IC50 = 2.3 ± 0.57 µM. Figure 2 maps tegoprazan-bound gastric H+,K+-ATPase to PDB 7W47; the experimental section describes recombinant pig H+,K+-ATPase activity assays. auto_single_measurement only accepted activity measurement [1] 1 structures\7W47\7W47_metadata.json point structures/7W47/7w47_protein.pdb structures/7W47/7w47_pocket.pdb structures/7W47/7w47_ligand.sdf structures/7W47/7w47_ligand.pdb structures/7W47/7w47_ligand.cif structures/7W47/7w47_complex.pdb structures/7W47/7w47_complex.cif 7W48 classic gastric H+,K+-ATPase pig N-terminally Flag- and GFP-tagged H+,K+-ATPase (Flag-GFP-TEVsite-Met48-H+,K+-ATPase) and WT beta-subunit Na PF-03716556 "[""8BZ""]" 1 IC50 IC50 = = 6.5 ± 0.68 µM 6500.0 [] unit_conversion 5.187086643357144 success True biochemical_inhibition Dose-dependent inhibition of recombinant H+,K+-ATPase activity at pH 7.0; membrane-fraction assay with 10 mM KCl. Table reports the WT value. 5 Table 1 reports WT PF-03716556 IC50 = 6.5 ± 0.68 µM. Figure 2 maps PF-03716556-bound gastric H+,K+-ATPase to PDB 7W48; the experimental section describes recombinant pig H+,K+-ATPase activity assays. auto_single_measurement only accepted activity measurement [1] 1 structures\7W48\7W48_metadata.json point structures/7W48/7w48_protein.pdb structures/7W48/7w48_pocket.pdb structures/7W48/7w48_ligand.sdf structures/7W48/7w48_ligand.pdb structures/7W48/7w48_ligand.cif structures/7W48/7w48_complex.pdb structures/7W48/7w48_complex.cif 7W49 classic gastric H+,K+-ATPase pig N-terminally Flag- and GFP-tagged H+,K+-ATPase (Flag-GFP-TEVsite-Met48-H+,K+-ATPase) and WT beta-subunit Na soraprazan "[""8CE""]" 1 IC50 IC50 = = 0.30 ± 0.023 µM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition Dose-dependent inhibition of recombinant H+,K+-ATPase activity at pH 7.0; membrane-fraction assay with 10 mM KCl. Table reports the WT value. 5 Table 1 reports WT soraprazan IC50 = 0.30 ± 0.023 µM. Figure 2 maps soraprazan-bound gastric H+,K+-ATPase to PDB 7W49; the experimental section describes recombinant pig H+,K+-ATPase activity assays. auto_single_measurement only accepted activity measurement [1] 1 structures\7W49\7W49_metadata.json point structures/7W49/7w49_protein.pdb structures/7W49/7w49_pocket.pdb structures/7W49/7w49_ligand.sdf structures/7W49/7w49_ligand.pdb structures/7W49/7w49_ligand.cif structures/7W49/7w49_complex.pdb structures/7W49/7w49_complex.cif 7W4X classic PDE4D Na Na Na 17 "[""8G7""]" 1 IC50 IC50 = = 0.4 ± 0.1 μM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition In vitro PDE4D catalytic-domain enzymatic inhibition assay; Table 2 reports racemic compound 17. 5 Table 2 lists compound 17 (rac) with PDE4D IC50 = 0.4 ± 0.1 μM. The paper identifies the PDE4D–17 co-crystal as PDB 7W4X. auto_single_measurement only accepted activity measurement [1] 1 structures\7W4X\7W4X_metadata.json point structures/7W4X/7w4x_protein.pdb structures/7W4X/7w4x_pocket.pdb structures/7W4X/7w4x_ligand.sdf structures/7W4X/7w4x_ligand.pdb structures/7W4X/7w4x_ligand.cif structures/7W4X/7w4x_complex.pdb structures/7W4X/7w4x_complex.cif 7W4Y classic PDE4D Na Na Na 33a "[""8GO""]" 1 IC50 IC50 = = 3.1 ± 0.6 nM 3.1 [] unit_conversion 8.508638306165727 success True biochemical_inhibition In vitro PDE4D catalytic-domain enzymatic inhibition assay; Table 4 reports enantiopure (2R,4S) compound 33a. 6 Table 4 lists compound 33a, configuration (2R,4S), with PDE4D IC50 = 3.1 ± 0.6 nM. The text identifies the PDE4D–33a co-crystal as PDB 7W4Y. auto_single_measurement only accepted activity measurement [1] 1 structures\7W4Y\7W4Y_metadata.json point structures/7W4Y/7w4y_protein.pdb structures/7W4Y/7w4y_pocket.pdb structures/7W4Y/7w4y_ligand.sdf structures/7W4Y/7w4y_ligand.pdb structures/7W4Y/7w4y_ligand.cif structures/7W4Y/7w4y_complex.pdb structures/7W4Y/7w4y_complex.cif 7W5M extended AtNASP Arabidopsis thaliana AtNASPcore, residues 58-398 with deletions of residues 148-200 and 334-353 Na histone H3 alpha3 helix peptide, residues 116-135 "[""CHAIN:B""]" 1 Kd Kd = = 0.4 µM 400.0 [] unit_conversion 6.3979400086720375 success True direct_binding Isothermal titration calorimetry (ITC) of AtNASPcore with the H3 α3 peptide. 2 “Our isothermal titration calorimetry (ITC) results revealed that AtNASPcore bound to the H3 α3 (a.a. 116–135) peptide … with Kds of 0.4 and 0.3 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7W5M\7W5M_metadata.json point structures/7W5M/7w5m_protein.pdb structures/7W5M/7w5m_pocket.pdb structures/7W5M/7w5m_ligand.pdb structures/7W5M/7w5m_ligand.cif structures/7W5M/7w5m_complex.pdb structures/7W5M/7w5m_complex.cif 7W61 classic farnesol dehydrogenase (HaFDL) Helicoverpa armigera Recombinant HaFDL with the N-terminal 6xHis tag removed by TEV protease Na NADP "[""NAP""]" 1 Kd Kd = = 3.43 µM 3430.0 [] unit_conversion 5.464705879957229 success True direct_binding Isothermal titration calorimetry (ITC) of NADP binding to recombinant HaFDL at 30 °C. 6 “In ITC, a high binding affinity (Kd, 3.43 μM) of NADP to the enzyme was observed”. auto_single_measurement only accepted activity measurement [1] 1 structures\7W61\7W61_metadata.json point structures/7W61/7w61_protein.pdb structures/7W61/7w61_pocket.pdb structures/7W61/7w61_ligand.sdf structures/7W61/7w61_ligand.pdb structures/7W61/7w61_ligand.cif structures/7W61/7w61_complex.pdb structures/7W61/7w61_complex.cif 7W81 extended IsdH Staphylococcus aureus linker-NEAT3 region; crystal contains linker residues Asn476-Val537 and NEAT3 residues Thr538-Asn656 Na heme (Fe(III)-PPIX) "[""HEM""]" 1 Kd Kd = = 0.51 ± 0.16 nM 0.51 [] unit_conversion 9.292429823902063 success True direct_binding Isothermal titration calorimetry of heme binding to linker-NEAT3 in PBS, pH 7.4, with 5% DMSO; Table 2 reports the fitted dissociation constant. 6 Table 2, “Thermodynamic and kinetic parameters corresponding to the binding of heme to IsdH,” reports linker-NEAT3 K_D = 0.51 ± 0.16 nM. The adjacent text identifies this as ITC measurement of heme binding. auto_single_measurement only accepted activity measurement [1] 1 structures\7W81\7W81_metadata.json point structures/7W81/7w81_protein.pdb structures/7W81/7w81_pocket.pdb structures/7W81/7w81_ligand.pdb structures/7W81/7w81_ligand.cif structures/7W81/7w81_complex.pdb structures/7W81/7w81_complex.cif 7WAA classic MCR-1-S Na MCR-1-S Na AgNO3 (Ag+) "[""AG""]" 1 Kd Kd = = 0.29 ± 0.09 μM 290.0 [] unit_conversion 6.537602002101044 success True direct_binding Isothermal titration calorimetry (ITC) measurement of AgNO3 binding to apo-MCR-1-S; sequential-binding model. 4 “The ITC data were fitted by a sequential-binding model, giving rise to an apparent dissociation constant (Kd) of 0.29 ± 0.09 μM and binding capacity (N) of 9.77 ± 0.43.” auto_single_measurement only accepted activity measurement [1] 1 structures\7WAA\7WAA_metadata.json point structures/7WAA/7waa_protein.pdb structures/7WAA/7waa_pocket.pdb structures/7WAA/7waa_ligand.sdf structures/7WAA/7waa_ligand.pdb structures/7WAA/7waa_ligand.cif structures/7WAA/7waa_complex.pdb structures/7WAA/7waa_complex.cif 7WCV classic FTO Na FTO truncated at the N-terminal 31 residues (FTODeltaN31) with a His-tag derived from pET28a Na 6e "[""943""]" 1 IC50 IC50 = = 1.5 ± 0.3 µM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition PAGE-based FTO demethylation inhibition assay; experiments performed in triplicate. 7 Figure 2B reports IC50 = 1.5 ± 0.3 µM for 6e, and Table 4 lists 6e: FTO IC50 1.5 ± 0.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7WCV\7WCV_metadata.json point structures/7WCV/7wcv_protein.pdb structures/7WCV/7wcv_pocket.pdb structures/7WCV/7wcv_ligand.sdf structures/7WCV/7wcv_ligand.pdb structures/7WCV/7wcv_ligand.cif structures/7WCV/7wcv_complex.pdb structures/7WCV/7wcv_complex.cif 7WCW classic FGFR4 kinase domain Na FGFR4 kinase domain residues 445-753 in modified pET28a with an N-terminal 6xHis tag and PreScission cleavage site V550L 7v "[""90F""]" 1 IC50 IC50 = = 0.25 nM 0.25 [] unit_conversion 9.602059991327963 success True biochemical_inhibition Biochemical kinase inhibition assay; 10 μM ATP. 7 Table 3 reports FGFR4V550L IC50 of 0.25 nM for 7v at 10 μM ATP. auto_single_measurement only accepted activity measurement [1] 1 structures\7WCW\7WCW_metadata.json point structures/7WCW/7wcw_protein.pdb structures/7WCW/7wcw_pocket.pdb structures/7WCW/7wcw_ligand.sdf structures/7WCW/7wcw_ligand.pdb structures/7WCW/7wcw_ligand.cif structures/7WCW/7wcw_complex.pdb structures/7WCW/7wcw_complex.cif 7WCX classic FGFR4 kinase domain Na FGFR4 kinase domain residues 445-753 in modified pET28a with an N-terminal 6xHis tag and PreScission cleavage site V550M 7v "[""90F""]" 1 IC50 IC50 = = 1.6 nM 1.6 [] unit_conversion 8.795880017344075 success True biochemical_inhibition Biochemical kinase inhibition assay; 10 μM ATP. 7 Table 3 reports FGFR4V550M IC50 of 1.6 nM for 7v at 10 μM ATP. auto_single_measurement only accepted activity measurement [1] 1 structures\7WCX\7WCX_metadata.json point structures/7WCX/7wcx_protein.pdb structures/7WCX/7wcx_pocket.pdb structures/7WCX/7wcx_ligand.sdf structures/7WCX/7wcx_ligand.pdb structures/7WCX/7wcx_ligand.cif structures/7WCX/7wcx_complex.pdb structures/7WCX/7wcx_complex.cif 7WEG extended PDZD7 and FCHSD2 Na PDZD7 PDZ3 residues 842-946 in complex with the FCHSD2 C-terminal tail residues 729-740 Na FCHSD2 C-terminal tail residues 729-740 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 1.51±0.10 μM 1510.0 [] unit_conversion 5.821023052706831 success True direct_binding Isothermal titration calorimetry (ITC) of purified FCHSD2 tail and PDZD7 PDZ3. 4 Figure 2 caption: “ITC analysis showing that FCHSD2 tail binds to PDZD7 PDZ3 with a Kd value of ~1.51 μM”; panel D prints “1.51±0.10 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7WEG\7WEG_metadata.json point structures/7WEG/7weg_protein.pdb structures/7WEG/7weg_pocket.pdb structures/7WEG/7weg_ligand.pdb structures/7WEG/7weg_ligand.cif structures/7WEG/7weg_complex.pdb structures/7WEG/7weg_complex.cif 7WEK extended mouse Wdr47 NTD mouse Wdr47-NTD, amino acids 1-315, in complex with the Camsap3 WBR peptide Na Camsap3 WBR peptide, residues 565-580 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 5.9 ± 0.5 µM 5900.0 [] unit_conversion 5.229147988357855 success True direct_binding ITC measurement of Wdr47-NTD binding to the chemically synthesized Camsap3 WBR peptide. 5 The paper states that the WBR peptide bound Wdr47-NTD with a high affinity, with a Kd of 5.9 ± 0.5 µM by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7WEK\7WEK_metadata.json point structures/7WEK/7wek_protein.pdb structures/7WEK/7wek_pocket.pdb structures/7WEK/7wek_ligand.pdb structures/7WEK/7wek_ligand.cif structures/7WEK/7wek_complex.pdb structures/7WEK/7wek_complex.cif 7WFY extended VAV2 SH2 domain human Vav2 SH2 domain residues 659-771 with an N-terminal 6xHis tag Na APP-pY682 peptide (QNG-pY-ENPT; APP695 residues 679-686) "[""CHAIN:A""]" 1 Kd Kd = = 0.86 ± 0.09 μM 860.0 [] unit_conversion 6.065501548756432 success True direct_binding Isothermal titration calorimetry (ITC) using recombinant Vav2-SH2 protein and synthesized phosphorylated APP-pY682 peptide. 2 “ITC reported a binding Kd of 0.86 μM for Vav2-SH2 in complex with APP-pY682 peptide and no binding of Vav2-SH2 and APP-Y682 peptide.” Figure 1 reports “Kd = 0.86 ± 0.09 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7WFY\7WFY_metadata.json point structures/7WFY/7wfy_protein.pdb structures/7WFY/7wfy_pocket.pdb structures/7WFY/7wfy_ligand.pdb structures/7WFY/7wfy_ligand.cif structures/7WFY/7wfy_complex.pdb structures/7WFY/7wfy_complex.cif 7WGT classic Drosophila melanogaster dopamine transporter dDAT_GAT Drosophila melanogaster ts5 dDAT_GAT crystallization construct with Delta1-20 and Delta162-202 deletions and C-terminal thrombin site LVPRGS replacement F43Y, D46G, A117S, V120L, D121N, F325L, V327S, S422Q, G425T, S426V; V74A, V275A, V311A, L415A, G538L; Delta1-20 and Delta162-202 deletions; residues 602-607 replaced by LVPRGS NO711 "[""9BC""]" 1 Kd Kd = = 10 µM 10000.0 [] unit_conversion 5.0 success True direct_binding Microscale thermophoresis measurement of purified ts5 dDAT_GAT in detergent micelles. 2 “The purified dDAT_GAT in detergent micelles displays weak interactions with the GAT1 inhibitors NO711 and SKF89976a with a Kd value of 10 and 34 µM using microscale thermophoresis measurements, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7WGT\7WGT_metadata.json point structures/7WGT/7wgt_protein.pdb structures/7WGT/7wgt_pocket.pdb structures/7WGT/7wgt_ligand.sdf structures/7WGT/7wgt_ligand.pdb structures/7WGT/7wgt_ligand.cif structures/7WGT/7wgt_complex.pdb structures/7WGT/7wgt_complex.cif 7WHU extended Human neutrophil elastase (hNE) Human Peptidase domain, residues 30-247 Na Ecotin-derived peptide Pep1 (77VSSPVSTM84) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 IC50 IC50 = = 1.9 µM 1900.0 [] unit_conversion 5.721246399047171 success True biochemical_inhibition Enzymatic hNE activity assay using chromogenic substrate; Pep1 inhibition of wild-type hNE. 3 Figure 1b reports: “Pep1 has the best IC50 of 1.9 µM”; the figure caption states the four peptides were evaluated against wild-type hNE. auto_single_measurement only accepted activity measurement [1] 1 structures\7WHU\7WHU_metadata.json point structures/7WHU/7whu_protein.pdb structures/7WHU/7whu_pocket.pdb structures/7WHU/7whu_ligand.pdb structures/7WHU/7whu_ligand.cif structures/7WHU/7whu_complex.pdb structures/7WHU/7whu_complex.cif 7WJ8 classic AtHPPD Na Na Na PyQ1 "[""0B8""]" 1 Kd Kd = = 0.643 ± 0.199 μmol/L 643.0 [] unit_conversion 6.191789027075778 success True direct_binding Microscale thermophoresis (MST) binding-force assay of PyQ1 with HPPD. 4 “The value of the binding constant (Kd) of PyQ1 with HPPD was 0.643 ± 0.199 μmol/L.” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7WJ8\7WJ8_metadata.json point structures/7WJ8/7wj8_protein.pdb structures/7WJ8/7wj8_pocket.pdb structures/7WJ8/7wj8_ligand.sdf structures/7WJ8/7wj8_ligand.pdb structures/7WJ8/7wj8_ligand.cif structures/7WJ8/7wj8_complex.pdb structures/7WJ8/7wj8_complex.cif 7WJH extended Bcl-xL mouse Bcl-xL residues 1-42 and 85-196 Na human Pxt1 BH3 domain peptide, residues 76-101 "[""CHAIN:B""]" 1 Kd Kd = = 233 nM 233.0 [] unit_conversion 6.632644078973981 success True direct_binding Isothermal titration calorimetry of recombinant Bcl-xL with synthetic human Pxt1(76–101) peptide. 2 Fig. 1B states that Bcl-xL binds human Pxt1(76–101) peptide with a dissociation constant (Kd) of 233 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7WJH\7WJH_metadata.json point structures/7WJH/7wjh_protein.pdb structures/7WJH/7wjh_pocket.pdb structures/7WJH/7wjh_ligand.pdb structures/7WJH/7wjh_ligand.cif structures/7WJH/7wjh_complex.pdb structures/7WJH/7wjh_complex.cif 7WJJ classic AtHPPD Na Na Na PyQ2 "[""0I0""]" 1 Kd Kd = = 71.044 ± 4.688 μmol/L 71044.0 [] unit_conversion 4.148472594399748 success True direct_binding Binding-force assay of PyQ2 with HPPD. 6 “the strong adhesion force found for PyQ1 with HPPD … compared with that obtained for PyQ2 with HPPD exhibited a 110-fold decrease (Kd = 71.044 ± 4.688 μmol/L …)” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7WJJ\7WJJ_metadata.json point structures/7WJJ/7wjj_protein.pdb structures/7WJJ/7wjj_pocket.pdb structures/7WJJ/7wjj_ligand.sdf structures/7WJJ/7wjj_ligand.pdb structures/7WJJ/7wjj_ligand.cif structures/7WJJ/7wjj_complex.pdb structures/7WJJ/7wjj_complex.cif 7WKU extended Porcine deltacoronavirus main protease (PDCoV Mpro) Porcine deltacoronavirus PDCoV Mpro expressed as a SUMO fusion; SUMO tag cleaved by ULP protease Na N3 "[""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L"", ""CHAIN:M""]" 1 Ki Ki = = 11.98 ± 0.13 μM 11980.0 [] unit_conversion 4.921543181946707 success True biochemical_inhibition Enzymatic inhibition assay of PDCoV Mpro; Ki obtained after addition of PDCoV Mpro. 8 “The calculated Ki and k3 were 11.98 ± 0.13 μM and 72.91 ± 7.05 (10−3 s−1), respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7WKU\7WKU_metadata.json point structures/7WKU/7wku_protein.pdb structures/7WKU/7wku_pocket.pdb structures/7WKU/7wku_ligand.pdb structures/7WKU/7wku_ligand.cif structures/7WKU/7wku_complex.pdb structures/7WKU/7wku_complex.cif 7WLW classic Drosophila melanogaster dopamine transporter dDAT_GAT Drosophila melanogaster ts5 dDAT_GAT crystallization construct with Delta1-20 and Delta162-202 deletions and C-terminal thrombin site LVPRGS replacement F43Y, D46G, A117S, V120L, D121N, F325L, V327S, S422Q, G425T, S426V; V74A, V275A, V311A, L415A, G538L; Delta1-20 and Delta162-202 deletions; residues 602-607 replaced by LVPRGS SKF89976a "[""1WR""]" 1 Kd Kd = = 34 µM 34000.0 [] unit_conversion 4.468521082957745 success True direct_binding Microscale thermophoresis measurement of purified ts5 dDAT_GAT in detergent micelles. 2 “The purified dDAT_GAT in detergent micelles displays weak interactions with the GAT1 inhibitors NO711 and SKF89976a with a Kd value of 10 and 34 µM using microscale thermophoresis measurements, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7WLW\7WLW_metadata.json point structures/7WLW/7wlw_protein.pdb structures/7WLW/7wlw_pocket.pdb structures/7WLW/7wlw_ligand.sdf structures/7WLW/7wlw_ligand.pdb structures/7WLW/7wlw_ligand.cif structures/7WLW/7wlw_complex.pdb structures/7WLW/7wlw_complex.cif 7WM7 classic Threonyl-tRNA synthetase (SeThrRS) Salmonella enterica N-terminal truncated SeThrRS, residues 242-642 Na compound 18a "[""9I6""]" 1 IC50 IC50 = = 5.68 ± 0.04 μM 5680.0 [] unit_conversion 5.245651664288982 success True biochemical_inhibition Luciferase ATP-consumption enzyme-inhibition assay; IC50 determined after screening with SeThrRS, ATP, L-threonine, and E. coli tRNAThr. 7 Table 1 reports compound 18a IC50 = 5.68 ± 0.04 μM; the table defines IC50 as the half-maximum inhibitory concentration. The assay procedure is specified on page 18. auto_single_measurement only accepted activity measurement [1] 1 structures\7WM7\7WM7_metadata.json point structures/7WM7/7wm7_protein.pdb structures/7WM7/7wm7_pocket.pdb structures/7WM7/7wm7_ligand.sdf structures/7WM7/7wm7_ligand.pdb structures/7WM7/7wm7_ligand.cif structures/7WM7/7wm7_complex.pdb structures/7WM7/7wm7_complex.cif 7WMF classic Threonyl-tRNA synthetase (SeThrRS) Salmonella enterica N-terminal truncated SeThrRS, residues 242-642 Na compound 36k "[""9I9""]" 1 IC50 IC50 = = 0.58 ± 0.16 μM 580.0 [] unit_conversion 6.236572006437063 success True biochemical_inhibition Luciferase ATP-consumption enzyme-inhibition assay; IC50 determined after screening with SeThrRS, ATP, L-threonine, and E. coli tRNAThr. 10 Table 4 reports compound 36k IC50 = 0.58 ± 0.16 μM; the table defines IC50 as the half-maximum inhibitory concentration. The assay procedure is specified on page 18. auto_single_measurement only accepted activity measurement [1] 1 structures\7WMF\7WMF_metadata.json point structures/7WMF/7wmf_protein.pdb structures/7WMF/7wmf_pocket.pdb structures/7WMF/7wmf_ligand.sdf structures/7WMF/7wmf_ligand.pdb structures/7WMF/7wmf_ligand.cif structures/7WMF/7wmf_complex.pdb structures/7WMF/7wmf_complex.cif 7WMI classic Threonyl-tRNA synthetase (SeThrRS) Salmonella enterica N-terminal truncated SeThrRS, residues 242-642 Na compound 36a "[""9IC""]" 1 IC50 IC50 = = 3.71 ± 0.40 μM 3710.0 [] unit_conversion 5.430626090384954 success True biochemical_inhibition Luciferase ATP-consumption enzyme-inhibition assay; IC50 determined after screening with SeThrRS, ATP, L-threonine, and E. coli tRNAThr. 8 Table 2 reports compound 36a IC50 = 3.71 ± 0.40 μM; the table defines IC50 as the half-maximum inhibitory concentration. The assay procedure is specified on page 18. auto_single_measurement only accepted activity measurement [1] 1 structures\7WMI\7WMI_metadata.json point structures/7WMI/7wmi_protein.pdb structures/7WMI/7wmi_pocket.pdb structures/7WMI/7wmi_ligand.sdf structures/7WMI/7wmi_ligand.pdb structures/7WMI/7wmi_ligand.cif structures/7WMI/7wmi_complex.pdb structures/7WMI/7wmi_complex.cif 7WO3 classic SARS-CoV-2 3CLPro SARS-CoV-2 Na Na TPM10 "[""59S""]" 1 IC50 IC50 = = 0.080 ± 0.002 μM 80.0 [] unit_conversion 7.096910013008056 success True biochemical_inhibition FRET-based enzymatic inhibition assay using purified SARS-CoV-2 3CLPro and fluorescent peptide substrate. 7 Figure 6A reports TPM10 IC50 = 0.080 ± 0.002 μM for SARS-CoV-2 3CLPro. auto_single_measurement only accepted activity measurement [1] 1 structures\7WO3\7WO3_metadata.json point structures/7WO3/7wo3_protein.pdb structures/7WO3/7wo3_pocket.pdb structures/7WO3/7wo3_ligand.sdf structures/7WO3/7wo3_ligand.pdb structures/7WO3/7wo3_ligand.cif structures/7WO3/7wo3_complex.pdb structures/7WO3/7wo3_complex.cif 7WPL classic Methionyl-tRNA synthetase (SaMetRS) Staphylococcus aureus C-terminal domain-truncated SaMetRS (SaMetRS-dC), residues 1-520, N-terminal His6-tagged Na ATP "[""ATP""]" 1 Kd Kd = = 52.0 ± 6.7 µM 52000.0 [] unit_conversion 4.2839966563652006 success True direct_binding Isothermal titration calorimetry of ATP into SaMetRS alone. 9 ITC titration of ATP to SaMetRS alone gave Kd = 52.0 ± 6.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7WPL\7WPL_metadata.json point structures/7WPL/7wpl_protein.pdb structures/7WPL/7wpl_pocket.pdb structures/7WPL/7wpl_ligand.sdf structures/7WPL/7wpl_ligand.pdb structures/7WPL/7wpl_ligand.cif structures/7WPL/7wpl_complex.pdb structures/7WPL/7wpl_complex.cif 7WQH classic HCoV-NL63 main protease (Mpro) HCoV-NL63 N-terminal 6xHis-tagged recombinant Mpro expressed from pET-28a; His tag removed by TEV protease Na PF-07304814 "[""80I""]" 1 IC50 IC50 = = 31.59 µM 31590.0 [] unit_conversion 4.500450374094851 success True biochemical_inhibition FRET-based enzymatic inhibition assay using purified HCoV-NL63 Mpro. 3 Figure 1G prints “PF-07304814 against HCoV-NL63 Mpro” and IC50 = 31.59 µM; Figure 1 caption identifies enzymatic inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7WQH\7WQH_metadata.json point structures/7WQH/7wqh_protein.pdb structures/7WQH/7wqh_pocket.pdb structures/7WQH/7wqh_ligand.sdf structures/7WQH/7wqh_ligand.pdb structures/7WQH/7wqh_ligand.cif structures/7WQH/7wqh_complex.pdb structures/7WQH/7wqh_complex.cif 7WQJ classic MERS-CoV main protease (Mpro) MERS-CoV N-terminal 6xHis-tagged recombinant Mpro expressed from pET-28a; His tag removed by TEV protease Na PF-07304814 "[""80I""]" 1 IC50 IC50 = = 9.507 µM 9507.0 [] unit_conversion 5.021956506090037 success True biochemical_inhibition FRET-based enzymatic inhibition assay using purified MERS-CoV Mpro. 3 Figure 1C prints “PF-07304814 against MERS-CoV Mpro” and IC50 = 9.507 µM; Figure 1 caption identifies enzymatic inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\7WQJ\7WQJ_metadata.json point structures/7WQJ/7wqj_protein.pdb structures/7WQJ/7wqj_pocket.pdb structures/7WQJ/7wqj_ligand.sdf structures/7WQJ/7wqj_ligand.pdb structures/7WQJ/7wqj_ligand.cif structures/7WQJ/7wqj_complex.pdb structures/7WQJ/7wqj_complex.cif 7WRM classic MCP2201 Comamonas testosteroni MCP2201 ligand-binding domain residues 58-203 with an N-terminal His6 tag Na L-malate (malate) "[""LMR""]" 1 Kd Kd = = 18.78 ± 7.45 μM 18780.0 [] unit_conversion 4.726304412069908 success True direct_binding Isothermal titration calorimetry of isolated MCP2201-LBD with L-malate. 5 The paper states that wild-type MCP2201-LBD has a Kd of 18.78 ± 7.45 μM for malate; the affinity was measured for isolated periplasmic domains. auto_single_measurement only accepted activity measurement [1] 1 structures\7WRM\7WRM_metadata.json point structures/7WRM/7wrm_protein.pdb structures/7WRM/7wrm_pocket.pdb structures/7WRM/7wrm_ligand.sdf structures/7WRM/7wrm_ligand.pdb structures/7WRM/7wrm_ligand.cif structures/7WRM/7wrm_complex.pdb structures/7WRM/7wrm_complex.cif 7WSM classic human glucose transporter GLUT4 human full-length human GLUT4 fused with an N-terminal FLAG tag wild-type cytochalasin B (CCB) "[""5RH""]" 1 IC50 IC50 = = 3.7 μM 3700.0 [] unit_conversion 5.431798275933005 success True biochemical_inhibition Proteoliposome-based counterflow assay; CCB inhibition of GLUT4 glucose transport activity. 2 “CCB inhibits the glucose transport activity of GLUT4 with an IC50 of 3.7 μM (Supplementary Fig. 2c).” auto_single_measurement only accepted activity measurement [1] 1 structures\7WSM\7WSM_metadata.json point structures/7WSM/7wsm_protein.pdb structures/7WSM/7wsm_pocket.pdb structures/7WSM/7wsm_ligand.sdf structures/7WSM/7wsm_ligand.pdb structures/7WSM/7wsm_ligand.cif structures/7WSM/7wsm_complex.pdb structures/7WSM/7wsm_complex.cif 7WSN classic human glucose transporter GLUT4 human full-length human GLUT4 fused with an N-terminal FLAG tag wild-type cytochalasin B (CCB) "[""5RH""]" 1 IC50 IC50 = = 3.7 μM 3700.0 [] unit_conversion 5.431798275933005 success True biochemical_inhibition Proteoliposome-based counterflow assay; CCB inhibition of GLUT4 glucose transport activity. 2 “CCB inhibits the glucose transport activity of GLUT4 with an IC50 of 3.7 μM (Supplementary Fig. 2c).” auto_single_measurement only accepted activity measurement [1] 1 structures\7WSN\7WSN_metadata.json point structures/7WSN/7wsn_protein.pdb structures/7WSN/7wsn_pocket.pdb structures/7WSN/7wsn_ligand.sdf structures/7WSN/7wsn_ligand.pdb structures/7WSN/7wsn_ligand.cif structures/7WSN/7wsn_complex.pdb structures/7WSN/7wsn_complex.cif 7WVK classic human WDR5 human WDR5 residues 22-334 with an N-terminal 6x His tag Na compound 19 "[""6IQ""]" 1 Kd Kd = = 36.8 μM 36800.0 [] unit_conversion 4.434152181326482 success True direct_binding Surface plasmon resonance (Biacore 8K) with recombinant WDR5; Figure 3c. 4 “Binding affinities of the four active compounds were identified by SPR, ranging from 16.8 μM to 36.8 μM (Fig. 3).” Figure 3c prints K_D = 36.8 μM for compound 19. auto_single_measurement only accepted activity measurement [1] 1 structures\7WVK\7WVK_metadata.json point structures/7WVK/7wvk_protein.pdb structures/7WVK/7wvk_pocket.pdb structures/7WVK/7wvk_ligand.sdf structures/7WVK/7wvk_ligand.pdb structures/7WVK/7wvk_ligand.cif structures/7WVK/7wvk_complex.pdb structures/7WVK/7wvk_complex.cif 7X0H classic CbpA (sugar-binding protein) Clostridium thermocellum Na Na glucose "[""BGC""]" 1 Kd Kd = = 240 ± 95 µM 240000.0 [] unit_conversion 3.6197887582883936 success True direct_binding Isothermal titration calorimetry (ITC). 6 Table 1 reports CbpA–glucose K_D = 240 ± 95 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7X0H\7X0H_metadata.json point structures/7X0H/7x0h_protein.pdb structures/7X0H/7x0h_pocket.pdb structures/7X0H/7x0h_ligand.sdf structures/7X0H/7x0h_ligand.pdb structures/7X0H/7x0h_ligand.cif structures/7X0H/7x0h_complex.pdb structures/7X0H/7x0h_complex.cif 7X0K extended CbpB (sugar-binding protein) Clostridium thermocellum Na Na cellotriose "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 1.17 ± 0.23 µM 1170.0 [] unit_conversion 5.931814138253838 success True direct_binding Isothermal titration calorimetry (ITC). 6 Table 1 reports CbpB–cellotriose K_D = 1.17 ± 0.23 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7X0K\7X0K_metadata.json point structures/7X0K/7x0k_protein.pdb structures/7X0K/7x0k_pocket.pdb structures/7X0K/7x0k_ligand.pdb structures/7X0K/7x0k_ligand.cif structures/7X0K/7x0k_complex.pdb structures/7X0K/7x0k_complex.cif 7X0L extended CbpB (sugar-binding protein) Clostridium thermocellum Na Na cellotetraose "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 0.56 ± 0.08 µM 560.0 [] unit_conversion 6.251811972993799 success True direct_binding Isothermal titration calorimetry (ITC). 6 Table 1 reports CbpB–cellotetraose K_D = 0.56 ± 0.08 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7X0L\7X0L_metadata.json point structures/7X0L/7x0l_protein.pdb structures/7X0L/7x0l_pocket.pdb structures/7X0L/7x0l_ligand.pdb structures/7X0L/7x0l_ligand.cif structures/7X0L/7x0l_complex.pdb structures/7X0L/7x0l_complex.cif 7X11 classic ME1 (malic enzyme 1) human Na Na AS1134900 "[""86I""]" 1 IC50 IC50 = = 0.73 μM 730.0 [] unit_conversion 6.136677139879544 success True biochemical_inhibition ME1/resazurin enzymatic assay; AS1134900 inhibition, with NADP+ and malate required for binding. 2 “AS1134900 … [has] an IC50 of 0.73 μM in the ME1/resazurin assay”; the paper maps the NADPH–AS1134900–ME1 complex to PDB entry 7X11. auto_single_measurement only accepted activity measurement [1] 1 structures\7X11\7X11_metadata.json point structures/7X11/7x11_protein.pdb structures/7X11/7x11_pocket.pdb structures/7X11/7x11_ligand.sdf structures/7X11/7x11_ligand.pdb structures/7X11/7x11_ligand.cif structures/7X11/7x11_complex.pdb structures/7X11/7x11_complex.cif 7X14 extended MIGA2; VAPB Mus musculus MIGA2 phosphorylated FFAT motif peptide residues 289-298 bound to VAPB MSP domain residues 1-125 Na phosphorylated MIGA2 FFAT motif peptide, residues 289-298 "[""CHAIN:B""]" 1 Kd Kd = = 1.7 ± 0.2 μM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding ITC measurement of mMIGA2pFFAT peptide binding to mVAPB. 9 Figure 5f reports Kd = 1.7 ± 0.2 μM for mMIGA2pFFAT binding mVAPB; methods specify the phosphorylated MIGA2 289–298 peptide and mVAPB MSP domain. auto_single_measurement only accepted activity measurement [1] 1 structures\7X14\7X14_metadata.json point structures/7X14/7x14_protein.pdb structures/7X14/7x14_pocket.pdb structures/7X14/7x14_ligand.pdb structures/7X14/7x14_ligand.cif structures/7X14/7x14_complex.pdb structures/7X14/7x14_complex.cif 7X5R classic 4-Hydroxyphenylpyruvate dioxygenase (AtHPPD) Arabidopsis thaliana Na Na Lancotrione "[""9P5""]" 1 IC50 IC50 = = 0.177 μM 177.0 [] unit_conversion 6.752026733638193 success True biochemical_inhibition HPPD activity/inhibition assay; lancotrione inhibition towards AtHPPD. 2 “Lancotrione ... shows safety for use in rice fields (IC50 = 0.177 μM)”. The section explicitly concerns binding of AtHPPD with lancotrione. auto_single_measurement only accepted activity measurement [1] 1 structures\7X5R\7X5R_metadata.json point structures/7X5R/7x5r_protein.pdb structures/7X5R/7x5r_pocket.pdb structures/7X5R/7x5r_ligand.sdf structures/7X5R/7x5r_ligand.pdb structures/7X5R/7x5r_ligand.cif structures/7X5R/7x5r_complex.pdb structures/7X5R/7x5r_complex.cif 7X5U classic 4-Hydroxyphenylpyruvate dioxygenase (AtHPPD) Arabidopsis thaliana Na Na Diketonitrile (DKN) "[""9R6""]" 1 IC50 IC50 = = 0.261 μM 261.0 [] unit_conversion 6.583359492661719 success True biochemical_inhibition HPPD activity/inhibition assay; DKN bound to AtHPPD. 2 “DKN (IC50 = 0.261 μM) bound to HPPD through its diketone system and a phenyl ring”. The section and figure identify the complex as AtHPPD–DKN. auto_single_measurement only accepted activity measurement [1] 1 structures\7X5U\7X5U_metadata.json point structures/7X5U/7x5u_protein.pdb structures/7X5U/7x5u_pocket.pdb structures/7X5U/7x5u_ligand.sdf structures/7X5U/7x5u_ligand.pdb structures/7X5U/7x5u_ligand.cif structures/7X5U/7x5u_complex.pdb structures/7X5U/7x5u_complex.cif 7X6Y extended TRIM7 Na Na Na C-terminal peptide of NSP5 "[""CHAIN:B""]" 1 Kd Kd = = 5.7 ± 2.6 μM 5700.0 [] unit_conversion 5.2441251443275085 success True direct_binding ITC measurement with a peptide derived from SARS-CoV-2 NSP5. 10 Supplementary Fig. 8 reports TRIM7 + NSP5, Kd 5.7 ± 2.6 μM; the caption specifies peptides derived from SARS-CoV-2 NSP proteins. auto_single_measurement only accepted activity measurement [1] 1 structures\7X6Y\7X6Y_metadata.json point structures/7X6Y/7x6y_protein.pdb structures/7X6Y/7x6y_pocket.pdb structures/7X6Y/7x6y_ligand.pdb structures/7X6Y/7x6y_ligand.cif structures/7X6Y/7x6y_complex.pdb structures/7X6Y/7x6y_complex.cif 7X6Z extended TRIM7 Na Na Na C-terminal peptide of NSP12 "[""CHAIN:B""]" 1 Kd Kd = = 15.6 ± 3.3 μM 15600.0 [] unit_conversion 4.806875401645539 success True direct_binding ITC measurement with a peptide derived from SARS-CoV-2 NSP12. 10 Supplementary Fig. 8 reports TRIM7 + NSP12, Kd 15.6 ± 3.3 μM; the caption specifies peptides derived from SARS-CoV-2 NSP proteins. auto_single_measurement only accepted activity measurement [1] 1 structures\7X6Z\7X6Z_metadata.json point structures/7X6Z/7x6z_protein.pdb structures/7X6Z/7x6z_pocket.pdb structures/7X6Z/7x6z_ligand.pdb structures/7X6Z/7x6z_ligand.cif structures/7X6Z/7x6z_complex.pdb structures/7X6Z/7x6z_complex.cif 7X70 extended TRIM7 Na Na Na C-terminal peptide of NSP8 "[""CHAIN:B""]" 1 Kd Kd = = 8.8 ± 1.5 μM 8800.0 [] unit_conversion 5.055517327849831 success True direct_binding ITC measurement with a peptide derived from SARS-CoV-2 NSP8. 10 Supplementary Fig. 8 reports TRIM7 + NSP8, Kd 8.8 ± 1.5 μM; the caption specifies peptides derived from SARS-CoV-2 NSP proteins. auto_single_measurement only accepted activity measurement [1] 1 structures\7X70\7X70_metadata.json point structures/7X70/7x70_protein.pdb structures/7X70/7x70_pocket.pdb structures/7X70/7x70_ligand.pdb structures/7X70/7x70_ligand.cif structures/7X70/7x70_complex.pdb structures/7X70/7x70_complex.cif 7X7N extended SARS-CoV-2 spike protein SARS-CoV-2 Na Na SIH-5 "[""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I""]" 2 Kd Kd = = 0.9 nM 0.9 [] unit_conversion 9.045757490560675 success True direct_binding Direct SIH-5–RBD binding affinity discussed together with its oligomeric state. 8 The text explicitly states: “SIH-5 (KD 0.9 nM, oligomeric state 2.4)”. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7X7N\7X7N_metadata.json point structures/7X7N/7x7n_protein.pdb structures/7X7N/7x7n_pocket.pdb structures/7X7N/7x7n_ligand.pdb structures/7X7N/7x7n_ligand.cif structures/7X7N/7x7n_complex.pdb structures/7X7N/7x7n_complex.cif 7X8H classic AtHPPD Arabidopsis thaliana Na Na (+)-Usnic acid "[""AIY""]" 1 Ki Ki = = 6.00 nM 6.0 [] unit_conversion 8.221848749616356 success True biochemical_inhibition In vitro AtHPPD inhibition kinetics; the paper states that (+)-usnic acid did not inhibit in a time-dependent manner. 2 “Its Ki value toward AtHPPD is 6.00 nM and IC50 value is 0.146 μM”. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\7X8H\7X8H_metadata.json point structures/7X8H/7x8h_protein.pdb structures/7X8H/7x8h_pocket.pdb structures/7X8H/7x8h_ligand.sdf structures/7X8H/7x8h_ligand.pdb structures/7X8H/7x8h_ligand.cif structures/7X8H/7x8h_complex.pdb structures/7X8H/7x8h_complex.cif 7X9E extended 76E1 Fab human Fab fragment generated by papain digestion of 76E1 antibody; heavy chain VH-CH1 and light chain VL-CL Na SARS-CoV-2 S peptide 809-833 "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 15.3 ± 5.8 nM 15.3 [] unit_conversion 7.815308569182401 success True direct_binding Isothermal titration calorimetry of 76E1 Fab with the crystallographic SARS-CoV-2 S peptide 809-833. 17 Extended Data Fig. 5c prints KD = 15.3 ± 5.8 nM for S peptide 809-833. auto_single_measurement only accepted activity measurement [1] 1 structures\7X9E\7X9E_metadata.json point structures/7X9E/7x9e_protein.pdb structures/7X9E/7x9e_pocket.pdb structures/7X9E/7x9e_ligand.pdb structures/7X9E/7x9e_ligand.cif structures/7X9E/7x9e_complex.pdb structures/7X9E/7x9e_complex.cif 7XAF classic TrkA kinase Na TRKA kinase domain, residues 485-795, with an N-terminal hexahistidine tag; expressed in Sf9 cells wild-type 7b "[""FKT""]" 1 IC50 IC50 = = 13.7 nM 13.7 [] unit_conversion 7.863279432843593 success True biochemical_inhibition Biochemical kinase inhibition assay against TRKA. 4 Table 1 reports compound 7b biochemical kinase inhibition IC50 against TRKA of 13.7 nM; Figure 4 identifies 7b in complex with wild-type TRKA (PDB 7XAF). auto_single_measurement only accepted activity measurement [1] 1 structures\7XAF\7XAF_metadata.json point structures/7XAF/7xaf_protein.pdb structures/7XAF/7xaf_pocket.pdb structures/7XAF/7xaf_ligand.sdf structures/7XAF/7xaf_ligand.pdb structures/7XAF/7xaf_ligand.cif structures/7XAF/7xaf_complex.pdb structures/7XAF/7xaf_complex.cif 7XB4 classic SARS-CoV-2 main protease (Mpro) D48N mutant SARS-CoV-2 Recombinant SARS-CoV-2 Mpro D48N mutant with an N-terminal 6xHis tag; His tag removed by TEV protease D48N PF-07321332 (PF07321332) "[""4WI""]" 1 IC50 IC50 = = 9.531 µM 9531.0 [] unit_conversion 5.020861530453191 success True biochemical_inhibition FRET-based enzymatic inhibition assay using purified SARS-CoV-2 Mpro D48N mutant; PF-07321332 inhibition curve. 5 “PF-07321332 had a potent inhibitory effect against SARS-CoV-2 Mpro D48N with an IC50 of 9.531 μM (Figure 2A).” auto_single_measurement only accepted activity measurement [1] 1 structures\7XB4\7XB4_metadata.json point structures/7XB4/7xb4_protein.pdb structures/7XB4/7xb4_pocket.pdb structures/7XB4/7xb4_ligand.sdf structures/7XB4/7xb4_ligand.pdb structures/7XB4/7xb4_ligand.cif structures/7XB4/7xb4_complex.pdb structures/7XB4/7xb4_complex.cif 7XDG classic human mitochondrial NAD(P)+-dependent malic enzyme (ME2) human Na Na MDSA (5,5'-methylenedisalicylic acid) "[""D5S""]" 1 IC50 IC50 = = 0.51 μM 510.0 [] unit_conversion 6.292429823902063 success True biochemical_inhibition Purified human ME2 inhibition by MDSA; text reports the inhibitor effect. 2 “5,5′-Methylenedisalicylic acid (MDSA) had a remarkable inhibitory effect on ME2 with an IC50 of 0.51 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7XDG\7XDG_metadata.json point structures/7XDG/7xdg_protein.pdb structures/7XDG/7xdg_pocket.pdb structures/7XDG/7xdg_ligand.sdf structures/7XDG/7xdg_ligand.pdb structures/7XDG/7xdg_ligand.cif structures/7XDG/7xdg_complex.pdb structures/7XDG/7xdg_complex.cif 7XFG extended p300 TAZ2 domain Na p300 TAZ2 domain in complex with BRD4-NUT F1c domain binding motif #1 Na BRD4-NUT F1c domain binding motif #1 "[""CHAIN:B""]" 1 Kd Kd = = 115 µM 115000.0 [] unit_conversion 3.939302159646388 success True direct_binding NMR chemical-shift perturbation titration of 15N-TAZ2 with the F1c peptide NUT residues 403–418. 2 The text explicitly states Kd ~115 µM for residues 403–418 and identifies this peptide as the essential binding motif within residues 377–418. The Methods state that the TAZ2/NUT peptide (403–418) complex was used for structure determination. auto_single_measurement only accepted activity measurement [1] 1 structures\7XFG\7XFG_metadata.json point structures/7XFG/7xfg_protein.pdb structures/7XFG/7xfg_pocket.pdb structures/7XFG/7xfg_ligand.pdb structures/7XFG/7xfg_ligand.cif structures/7XFG/7xfg_complex.pdb structures/7XFG/7xfg_complex.cif 7XG8 classic PstS protein cyanophage P-SSM2 Na Na PO4 (phosphate) "[""PO4""]" 1 Kd Kd = = 1.39 ± 0.22 µM 1390.0 [] unit_conversion 5.856985199745905 success True direct_binding Equilibrium dialysis measurement of phosphate-binding affinity using purified recombinant PstS protein and 32P-labelled orthophosphoric acid with cold phosphate; separate recombinant-protein batches were measured. 6 “The dissociation constants (Kd) of the host and phage PstS proteins were 0.82 ± 0.44 and 1.39 ± 0.22 µM respectively.” The preceding text identifies the phage protein as cyanophage P-SSM2 PstS. auto_single_measurement only accepted activity measurement [1] 1 structures\7XG8\7XG8_metadata.json point structures/7XG8/7xg8_protein.pdb structures/7XG8/7xg8_pocket.pdb structures/7XG8/7xg8_ligand.sdf structures/7XG8/7xg8_ligand.pdb structures/7XG8/7xg8_ligand.cif structures/7XG8/7xg8_complex.pdb structures/7XG8/7xg8_complex.cif 7XGX classic Lgt2 Legionella pneumophila, strain Philadelphia 1 6x His-tagged wild-type Lgt2 wild-type UDP-glucose (UPG) "[""UPG""]" 1 Kd Kd = = 10.88 ± 2.18 µM 10880.0 [] unit_conversion 4.963371104637839 success True direct_binding Purified His6-tagged wild-type Lgt2 binding to UDP-glucose determined by isothermal titration calorimetry (ITC). 3 Figure 2e lists the UPG-binding Kd of wild-type Lgt2 as 10.88 ± 2.18 µM; the figure caption states that binding was determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\7XGX\7XGX_metadata.json point structures/7XGX/7xgx_protein.pdb structures/7XGX/7xgx_pocket.pdb structures/7XGX/7xgx_ligand.sdf structures/7XGX/7xgx_ligand.pdb structures/7XGX/7xgx_ligand.cif structures/7XGX/7xgx_complex.pdb structures/7XGX/7xgx_complex.cif 7XHQ classic SHP2 Homo sapiens SHP2 residues Met1-Leu525, expressed from pET-15b with an N-terminal 6xHis tag and TEV cleavage site Na PB17-026-01 "[""FIZ""]" 1 IC50 IC50 = = 38.9 nM 38.9 [] unit_conversion 7.410050398674292 success True biochemical_inhibition Purified SHP2 phosphatase dose–response assay using the fluorescent surrogate substrate DiFMUP; the paper identifies the co-crystal as SHP2–PB17-026-01 (PDB ID 7XHQ). 3 “PB17-026-01 showed the highest inhibitory activity with a IC50 value of 38.9 nM”; the same paragraph states that the SHP2–PB17-026-01 co-crystal structure was studied (PDB-ID: 7XHQ). auto_single_measurement only accepted activity measurement [1] 1 structures\7XHQ\7XHQ_metadata.json point structures/7XHQ/7xhq_protein.pdb structures/7XHQ/7xhq_pocket.pdb structures/7XHQ/7xhq_ligand.sdf structures/7XHQ/7xhq_ligand.pdb structures/7XHQ/7xhq_ligand.cif structures/7XHQ/7xhq_complex.pdb structures/7XHQ/7xhq_complex.cif 7XHY classic MerTK Na N-terminal His6-tag thrombin-MerTK kinase domain, residues 571-864 wild type (WT) BMS794833 "[""E0X""]" 1 Ki Ki = = 22.4 ± 2.7 nM 22.4 [] unit_conversion 7.649751981665837 success True biochemical_inhibition HTRF-based MerTK kinase kinetic assay; ATP competition analysis. 5 “BMS794833 inhibits MERTK in an ATP competitive inhibition mode with a Ki value of 22.4 nM (Fig. 3a and Table 1).” Figure 3a prints Ki = 22.4 ± 2.7 nM. auto_metric_priority unique highest-priority metric family: Ki [1] 3 structures\7XHY\7XHY_metadata.json point structures/7XHY/7xhy_protein.pdb structures/7XHY/7xhy_pocket.pdb structures/7XHY/7xhy_ligand.sdf structures/7XHY/7xhy_ligand.pdb structures/7XHY/7xhy_ligand.cif structures/7XHY/7xhy_complex.pdb structures/7XHY/7xhy_complex.cif 7XM2 classic Keap1 human Keap1 Kelch domain, residues 322-609 Na NXPZ-2 "[""GFD""]" 1 Kd Kd = = 0.23±0.015 μM 230.0 [] unit_conversion 6.638272163982407 success True direct_binding Equilibrium dissociation constant determined by fluorescence anisotropy assay for Keap1 binding. 4 Table 1 reports NXPZ-2 K_D2 = 0.23±0.015 μM; footnote states equilibrium dissociation constants were determined using fluorescence anisotropy. auto_single_measurement only accepted activity measurement [1] 1 structures\7XM2\7XM2_metadata.json point structures/7XM2/7xm2_protein.pdb structures/7XM2/7xm2_pocket.pdb structures/7XM2/7xm2_ligand.sdf structures/7XM2/7xm2_ligand.pdb structures/7XM2/7xm2_ligand.cif structures/7XM2/7xm2_complex.pdb structures/7XM2/7xm2_complex.cif 7XM3 classic Keap1 human Keap1 Kelch domain, residues 322-609 Na 6k "[""GED""]" 1 Kd Kd = = 0.21±0.011 μM 210.0 [] unit_conversion 6.6777807052660805 success True direct_binding Equilibrium dissociation constant determined by fluorescence anisotropy assay for Keap1 binding. 4 Table 1 reports compound 6k K_D2 = 0.21±0.011 μM; footnote states equilibrium dissociation constants were determined using fluorescence anisotropy. auto_single_measurement only accepted activity measurement [1] 1 structures\7XM3\7XM3_metadata.json point structures/7XM3/7xm3_protein.pdb structures/7XM3/7xm3_pocket.pdb structures/7XM3/7xm3_ligand.sdf structures/7XM3/7xm3_ligand.pdb structures/7XM3/7xm3_ligand.cif structures/7XM3/7xm3_complex.pdb structures/7XM3/7xm3_complex.cif 7XM4 classic Keap1 human Keap1 Kelch domain, residues 322-609 Na 6e "[""GDJ""]" 1 Kd Kd = = 0.48±0.172 μM 480.0 [] unit_conversion 6.318758762624412 success True direct_binding Equilibrium dissociation constant determined by fluorescence anisotropy assay for Keap1 binding. 4 Table 1 reports compound 6e K_D2 = 0.48±0.172 μM; footnote states equilibrium dissociation constants were determined using fluorescence anisotropy. auto_single_measurement only accepted activity measurement [1] 1 structures\7XM4\7XM4_metadata.json point structures/7XM4/7xm4_protein.pdb structures/7XM4/7xm4_pocket.pdb structures/7XM4/7xm4_ligand.sdf structures/7XM4/7xm4_ligand.pdb structures/7XM4/7xm4_ligand.cif structures/7XM4/7xm4_complex.pdb structures/7XM4/7xm4_complex.cif 7XM5 classic Keap1 human Keap1 Kelch domain, residues 322-609 Na 6i "[""GCI""]" 1 Kd Kd = = 1.03±0.056 μM 1030.0 [] unit_conversion 5.987162775294828 success True direct_binding Equilibrium dissociation constant determined by fluorescence anisotropy assay for Keap1 binding. 4 Table 1 reports compound 6i K_D2 = 1.03±0.056 μM; footnote states equilibrium dissociation constants were determined using fluorescence anisotropy. auto_single_measurement only accepted activity measurement [1] 1 structures\7XM5\7XM5_metadata.json point structures/7XM5/7xm5_protein.pdb structures/7XM5/7xm5_pocket.pdb structures/7XM5/7xm5_ligand.sdf structures/7XM5/7xm5_ligand.pdb structures/7XM5/7xm5_ligand.cif structures/7XM5/7xm5_complex.pdb structures/7XM5/7xm5_complex.cif 7XNE classic CBP Na Na Na Y08284 (9g) "[""GHF""]" 2 Kd Kd = = 58 nM 58.0 [] unit_conversion 7.236572006437063 success True direct_binding Isothermal titration calorimetry (ITC) direct binding measurement. 7 Figure 5B reports an ITC Kd of 0.058 μM for 9g binding to CBP; Figure 8 restates this as 58 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7XNE\7XNE_metadata.json point structures/7XNE/7xne_protein.pdb structures/7XNE/7xne_pocket.pdb structures/7XNE/7xne_ligand.sdf structures/7XNE/7xne_ligand.pdb structures/7XNE/7xne_ligand.cif structures/7XNE/7xne_complex.pdb structures/7XNE/7xne_complex.cif 7XNT classic 4-Hydroxyphenylpyruvate dioxygenase (PfHPPD) Pseudomonas fluorescens Na Na Benquitrione (Y13161) "[""94L""]" 1 IC50 IC50 = = 859 nM 859.0 [] unit_conversion 6.066006836168757 success True biochemical_inhibition HPPD activity/inhibition assay; comparison of benquitrione and compound 7 towards PfHPPD. 6 “The IC50 value of benquitrione or compound 7 towards PfHPPD was 859 nM or 229 nM, respectively”. auto_single_measurement only accepted activity measurement [1] 1 structures\7XNT\7XNT_metadata.json point structures/7XNT/7xnt_protein.pdb structures/7XNT/7xnt_pocket.pdb structures/7XNT/7xnt_ligand.sdf structures/7XNT/7xnt_ligand.pdb structures/7XNT/7xnt_ligand.cif structures/7XNT/7xnt_complex.pdb structures/7XNT/7xnt_complex.cif 7XP1 classic PmiR Pseudomonas aeruginosa PmiR residues 15–232 Na 2-methylisocitrate (MIC; PDB component MIC) "[""MIC""]" 1 Kd Kd = = 62.9 μM 62900.0 [] unit_conversion 4.201349354554731 success True direct_binding ITC direct binding of truncated PmiR residues 15–232 to MIC. 5 The structural-characterization section reports that truncated PmiR residues 15–232 bind MIC with Kd 62.9 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7XP1\7XP1_metadata.json point structures/7XP1/7xp1_protein.pdb structures/7XP1/7xp1_pocket.pdb structures/7XP1/7xp1_ligand.sdf structures/7XP1/7xp1_ligand.pdb structures/7XP1/7xp1_ligand.cif structures/7XP1/7xp1_complex.pdb structures/7XP1/7xp1_complex.cif 7XPK extended rice ASI1 rice OsASI1-BAH residues 19 to 183 in complex with OsSUVH6N residues 287 to 304 Na OsSUVH6 N-terminal peptide (OsSUVH6N, residues 287 to 304) "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 183.8 ± 62.6 nM 183.8 [] unit_conversion 6.735654492949907 success True direct_binding Isothermal titration calorimetry (ITC), three repeats. 3 ITC of OsASI1-BAH residues 19–183 with OsSUVH6N residues 287–304 yielded a strong binding Kd of 183.8 ± 62.6 nM from three repeats. auto_single_measurement only accepted activity measurement [1] 1 structures\7XPK\7XPK_metadata.json point structures/7XPK/7xpk_protein.pdb structures/7XPK/7xpk_pocket.pdb structures/7XPK/7xpk_ligand.pdb structures/7XPK/7xpk_ligand.cif structures/7XPK/7xpk_complex.pdb structures/7XPK/7xpk_complex.cif 7XPS classic MtdL Marinactinospora thermotolerans Na WT GDP "[""GDP""]" 1 Kd Kd = = 0.2 ± 0.04 µM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Isothermal titration calorimetry of GDP into MtdL WT in buffer supplemented with 0.5 mM MnCl2. 5 Figure 3B prints “Kd = 0.2 ± 0.04 µM, N = 1.11” for GDP versus MtdL WT; the ITC methods specify 0.5 mM MnCl2. auto_single_measurement only accepted activity measurement [1] 1 structures\7XPS\7XPS_metadata.json point structures/7XPS/7xps_protein.pdb structures/7XPS/7xps_pocket.pdb structures/7XPS/7xps_ligand.sdf structures/7XPS/7xps_ligand.pdb structures/7XPS/7xps_ligand.cif structures/7XPS/7xps_complex.pdb structures/7XPS/7xps_complex.cif 7XQM classic short-chain dehydrogenase (scDH) Thermus thermophilus Delta scDH InDel mutant Ala15 deletion; Arg16 deletion; Arg20 deletion SAH (S-adenosyl homocysteine) "[""SAH""]" 1 Kd Kd = = 391.5 ± 175.75 µM 391500.0 [] unit_conversion 3.407268233606038 success True direct_binding Isothermal titration calorimetry (ITC), ΔscDH + SAH. 5 Figure 2 identifies PDB 7XQM as the ΔscDH mutant and states that SAH binding remains, with Kd = 391.5 ± 175.75 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7XQM\7XQM_metadata.json point structures/7XQM/7xqm_protein.pdb structures/7XQM/7xqm_pocket.pdb structures/7XQM/7xqm_ligand.sdf structures/7XQM/7xqm_ligand.pdb structures/7XQM/7xqm_ligand.cif structures/7XQM/7xqm_complex.pdb structures/7XQM/7xqm_complex.cif 7XRS classic SARS-CoV-2 main protease (Mpro) Na Full-length Mpro expressed from pET-28a with an N-terminal His6 tag and TEV cleavage site; the His tag was removed by TEV protease Na YH-53 "[""HUR""]" 1 IC50 IC50 = = 0.1240 μM 124.0 [] unit_conversion 6.906578314837764 success True biochemical_inhibition Purified Mpro fluorogenic FRET enzymatic inhibition assay; main protease was preincubated with YH-53 for 30 min at room temperature before FRET substrate addition. 4 “YH-53 has a potent inhibition against SARS-CoV-2 Mpro, with an IC50 value of 0.1240 μM (Figure 1a).” auto_single_measurement only accepted activity measurement [1] 1 structures\7XRS\7XRS_metadata.json point structures/7XRS/7xrs_protein.pdb structures/7XRS/7xrs_pocket.pdb structures/7XRS/7xrs_ligand.sdf structures/7XRS/7xrs_ligand.pdb structures/7XRS/7xrs_ligand.cif structures/7XRS/7xrs_complex.pdb structures/7XRS/7xrs_complex.cif 7XRY classic MERS-CoV main protease (Mpro) Na Full-length Mpro expressed from pET-28a with an N-terminal His6 tag and TEV cleavage site; the His tag was removed by TEV protease Na YH-53 "[""HUR""]" 1 IC50 IC50 = = 3.103 μM 3103.0 [] unit_conversion 5.508218224415835 success True biochemical_inhibition Purified Mpro fluorogenic FRET enzymatic inhibition assay; main protease was preincubated with YH-53 for 30 min at room temperature before FRET substrate addition. 4 “YH-53 inhibits Mpro of MERS-CoV with an IC50 value of 3.103 μM (Figure 1b).” auto_single_measurement only accepted activity measurement [1] 1 structures\7XRY\7XRY_metadata.json point structures/7XRY/7xry_protein.pdb structures/7XRY/7xry_pocket.pdb structures/7XRY/7xry_ligand.sdf structures/7XRY/7xry_ligand.pdb structures/7XRY/7xry_ligand.cif structures/7XRY/7xry_complex.pdb structures/7XRY/7xry_complex.cif 7XSV classic PIM1 kinase Na Na Na H3 (compound H3) "[""I4M""]" 1 IC50 IC50 = = 81.49 nM 81.49 [] unit_conversion 7.0888956821959646 success True biochemical_inhibition ADP-Glo kinase assay in vitro; Pim-1 inhibitory activity. 5 Table 1 reports compound H3 Pim-1 inhibitory activity IC50 = 81.49 nM. The text states that inhibitory potency was evaluated using a Pim-1 kinase ADP-Glo Kinase Assay, and identifies the crystal structure of Pim-1 kinase bound with compound H3 as PDB ID 7XSV. auto_single_measurement only accepted activity measurement [1] 1 structures\7XSV\7XSV_metadata.json point structures/7XSV/7xsv_protein.pdb structures/7XSV/7xsv_pocket.pdb structures/7XSV/7xsv_ligand.sdf structures/7XSV/7xsv_ligand.pdb structures/7XSV/7xsv_ligand.cif structures/7XSV/7xsv_complex.pdb structures/7XSV/7xsv_complex.cif 7XUB classic G9a (EHMT2/KMT1C) human G9a SET domain, residues 913-1193 Na compound 10d "[""I6L""]" 1 IC50 IC50 = = 1900 nM 1900.0 [] unit_conversion 5.721246399047171 success True biochemical_inhibition In vitro G9a inhibition; Table 1 SAR value, mean from three independent experiments in triplicate. 4 Table 1 reports compound 10d (S) with G9a IC50 = 1,900 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7XUB\7XUB_metadata.json point structures/7XUB/7xub_protein.pdb structures/7XUB/7xub_pocket.pdb structures/7XUB/7xub_ligand.sdf structures/7XUB/7xub_ligand.pdb structures/7XUB/7xub_ligand.cif structures/7XUB/7xub_complex.pdb structures/7XUB/7xub_complex.cif 7XUC classic G9a (EHMT2/KMT1C) human G9a SET domain, residues 913-1193 Na compound 11a "[""I6S""]" 1 IC50 IC50 = = 355 nM 355.0 [] unit_conversion 6.449771646944906 success True biochemical_inhibition In vitro G9a inhibition; Table 1 SAR value, mean from three independent experiments in triplicate. 4 Table 1 reports compound 11a (S) with G9a IC50 = 355 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7XUC\7XUC_metadata.json point structures/7XUC/7xuc_protein.pdb structures/7XUC/7xuc_pocket.pdb structures/7XUC/7xuc_ligand.sdf structures/7XUC/7xuc_ligand.pdb structures/7XUC/7xuc_ligand.cif structures/7XUC/7xuc_complex.pdb structures/7XUC/7xuc_complex.cif 7XUD classic G9a (EHMT2/KMT1C) human G9a SET domain, residues 913-1193 Na compound 26a "[""I6Z""]" 1 IC50 IC50 = = 39.6 ± 5.6 nM 39.6 [] unit_conversion 7.402304814074488 success True biochemical_inhibition In vitro G9a inhibition; Table 5 value, mean ± SD from three independent experiments in triplicate. 7 Table 5 reports compound 26a with G9a IC50 = 39.6 ± 5.6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7XUD\7XUD_metadata.json point structures/7XUD/7xud_protein.pdb structures/7XUD/7xud_pocket.pdb structures/7XUD/7xud_ligand.sdf structures/7XUD/7xud_ligand.pdb structures/7XUD/7xud_ligand.cif structures/7XUD/7xud_complex.pdb structures/7XUD/7xud_complex.cif 7XUV extended human RPA70N Homo sapiens RPA70N residues 1-120 fused to RMI1 residues 243-262; N-terminal 6-His-SUMO tag Na RMI1 peptide residues 243-262 "[""CHAIN:B""]" 1 Kd Kd = = 14.47 ± 0.54 μM 14470.0 [] unit_conversion 4.8395314688809625 success True direct_binding ITC titration of WT RMI1 peptide with RPA70N. 9 Figure 4F prints “RMI1 Kd=14.47±0.54 μM”. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\7XUV\7XUV_metadata.json point structures/7XUV/7xuv_protein.pdb structures/7XUV/7xuv_pocket.pdb structures/7XUV/7xuv_ligand.pdb structures/7XUV/7xuv_ligand.cif structures/7XUV/7xuv_complex.pdb structures/7XUV/7xuv_complex.cif 7XV0 extended human RPA70N Homo sapiens RPA70N residues 1-120 fused to BLMp1 residues 146-165; N-terminal 6-His-SUMO tag Na BLMp1 peptide residues 146-165 "[""CHAIN:B""]" 1 Kd Kd = = 16.75 ± 0.84 μM 16750.0 [] unit_conversion 4.775985188627136 success True direct_binding ITC titration of WT BLMp1 peptide with RPA70N. 7 Figure 3I prints “BLMp1 Kd=16.75±0.84 μM”. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\7XV0\7XV0_metadata.json point structures/7XV0/7xv0_protein.pdb structures/7XV0/7xv0_pocket.pdb structures/7XV0/7xv0_ligand.pdb structures/7XV0/7xv0_ligand.cif structures/7XV0/7xv0_complex.pdb structures/7XV0/7xv0_complex.cif 7XV1 extended human RPA70N Homo sapiens RPA70N residues 1-120 fused to HelB residues 496-519; N-terminal 6-His-SUMO tag Na HelB peptide residues 496-519 "[""CHAIN:B""]" 1 Kd Kd = = 3.94 ± 0.31 μM 3940.0 [] unit_conversion 5.404503778174426 success True direct_binding ITC titration of WT HelB peptide with RPA70N. 5 Figure 2G prints “HelB Kd:3.94±0.31 μM”. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\7XV1\7XV1_metadata.json point structures/7XV1/7xv1_protein.pdb structures/7XV1/7xv1_pocket.pdb structures/7XV1/7xv1_ligand.pdb structures/7XV1/7xv1_ligand.cif structures/7XV1/7xv1_complex.pdb structures/7XV1/7xv1_complex.cif 7XV4 extended human RPA70N Homo sapiens RPA70N residues 1-120 fused to ATRIP residues 53-69; N-terminal 6-His-SUMO tag Na ATRIP peptide residues 53-69 "[""CHAIN:B""]" 1 Kd Kd = = 10.40 ± 0.62 μM 10400.0 [] unit_conversion 4.982966660701219 success True direct_binding ITC titration of WT ATRIP peptide with RPA70N. 13 Figure 6E prints “ATRIP Kd=10.40±0.62 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\7XV4\7XV4_metadata.json point structures/7XV4/7xv4_protein.pdb structures/7XV4/7xv4_pocket.pdb structures/7XV4/7xv4_ligand.pdb structures/7XV4/7xv4_ligand.cif structures/7XV4/7xv4_complex.pdb structures/7XV4/7xv4_complex.cif 7XVU classic neuraminidase (NA) Wuhan spiny eel influenza-like virus neuraminidase ectodomain, residues 83 to 472, N2 numbering Na oseltamivir carboxylate "[""G39""]" 1 IC50 IC50 = = 13.85 ± 1.73 nM 13.85 [] unit_conversion 7.858550226599533 success True biochemical_inhibition MUNANA fluorescence NA-inhibition assay; Table 1 reports mean ± SEM from three independent experiments. 6 Table 1 reports Wuhan spiny eel NA IC50 for oseltamivir carboxylate as 13.85 ± 1.73 nM; page 10 maps 7XVU to eNA-oseltamivir carboxylate. auto_single_measurement only accepted activity measurement [1] 1 structures\7XVU\7XVU_metadata.json point structures/7XVU/7xvu_protein.pdb structures/7XVU/7xvu_pocket.pdb structures/7XVU/7xvu_ligand.sdf structures/7XVU/7xvu_ligand.pdb structures/7XVU/7xvu_ligand.cif structures/7XVU/7xvu_complex.pdb structures/7XVU/7xvu_complex.cif 7XVV classic neuraminidase (NA) Wuhan spiny eel influenza-like virus neuraminidase ectodomain, residues 83 to 472, N2 numbering Na zanamivir "[""ZMR""]" 1 IC50 IC50 = = 8.37 ± 3.68 nM 8.37 [] unit_conversion 8.07727454200674 success True biochemical_inhibition MUNANA fluorescence NA-inhibition assay; Table 1 reports mean ± SEM from three independent experiments. 6 Table 1 reports Wuhan spiny eel NA IC50 for zanamivir as 8.37 ± 3.68 nM; page 10 maps 7XVV to eNA-zanamivir. auto_single_measurement only accepted activity measurement [1] 1 structures\7XVV\7XVV_metadata.json point structures/7XVV/7xvv_protein.pdb structures/7XVV/7xvv_pocket.pdb structures/7XVV/7xvv_ligand.sdf structures/7XVV/7xvv_ligand.pdb structures/7XVV/7xvv_ligand.cif structures/7XVV/7xvv_complex.pdb structures/7XVV/7xvv_complex.cif 7XVW classic neuraminidase (NA) Wuhan spiny eel influenza-like virus neuraminidase ectodomain, residues 83 to 472, N2 numbering Na peramivir "[""BCZ""]" 1 IC50 IC50 = = 1.55 ± 0.21 nM 1.55 [] unit_conversion 8.809668301829708 success True biochemical_inhibition MUNANA fluorescence NA-inhibition assay; Table 1 reports mean ± SEM from three independent experiments. 6 Table 1 reports Wuhan spiny eel NA IC50 for peramivir as 1.55 ± 0.21 nM; page 10 maps 7XVW to eNA-peramivir. auto_single_measurement only accepted activity measurement [1] 1 structures\7XVW\7XVW_metadata.json point structures/7XVW/7xvw_protein.pdb structures/7XVW/7xvw_pocket.pdb structures/7XVW/7xvw_ligand.sdf structures/7XVW/7xvw_ligand.pdb structures/7XVW/7xvw_ligand.cif structures/7XVW/7xvw_complex.pdb structures/7XVW/7xvw_complex.cif 7XZP classic formate-tetrahydrofolate ligase (Ftl) Peptostreptococcus anaerobius Na Na berberine (BBR) "[""BER""]" 1 Kd Kd = = 674 nM 674.0 [] unit_conversion 6.17134010346468 success True direct_binding Bio-layer interferometry (BLI) direct binding of BBR to PaFtl. 3 The text reports direct binding of PaFtl with BBR by BLI (Kd = 674 nM). auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\7XZP\7XZP_metadata.json point structures/7XZP/7xzp_protein.pdb structures/7XZP/7xzp_pocket.pdb structures/7XZP/7xzp_ligand.sdf structures/7XZP/7xzp_ligand.pdb structures/7XZP/7xzp_ligand.cif structures/7XZP/7xzp_complex.pdb structures/7XZP/7xzp_complex.cif 7XZQ extended TNIK Na Na Na TP1 "[""CHAIN:B""]" 1 Kd Kd = = 6.0 ± 0.2 nM 6.0 [] unit_conversion 8.221848749616356 success True direct_binding Surface plasmon resonance measurement of synthesized TP1 binding to TNIK. 5 Figure 3b lists TP1 K_D = 6.0 ± 0.2 nM; text states binding affinities were characterized by surface plasmon resonance. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7XZQ\7XZQ_metadata.json point structures/7XZQ/7xzq_protein.pdb structures/7XZQ/7xzq_pocket.pdb structures/7XZQ/7xzq_ligand.pdb structures/7XZQ/7xzq_ligand.cif structures/7XZQ/7xzq_complex.pdb structures/7XZQ/7xzq_complex.cif 7Y0F classic TMPRSS2 human Ectodomain residues 109-492 with N-terminal GP64 signal peptide and C-terminal 10xHis tag; autoactivation sequence replaced by an enteroptidase cleavage site Na UK-371804 "[""I9V""]" 1 IC50 IC50 = = 4.59 ± 0.07 nM 4.59 [] unit_conversion 8.338187314462738 success True biochemical_inhibition Purified-protein fluorogenic enzymatic inhibition assay. 2 Fig. 1e prints TMPRSS2 IC50 = 4.59 ± 0.07 nM for UK-371804. auto_single_measurement only accepted activity measurement [1] 1 structures\7Y0F\7Y0F_metadata.json point structures/7Y0F/7y0f_protein.pdb structures/7Y0F/7y0f_pocket.pdb structures/7Y0F/7y0f_ligand.sdf structures/7Y0F/7y0f_ligand.pdb structures/7Y0F/7y0f_ligand.cif structures/7Y0F/7y0f_complex.pdb structures/7Y0F/7y0f_complex.cif 7Y0T extended P450 BM3 Bacillus megaterium heme domain F87A N-imidazolyl-hexanoyl-L-phenylalanyl-L-phenylalanine (Im-C6-Phe-Phe) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 3.1×10−7 M 310.0 [] unit_conversion 6.508638306165727 success True direct_binding Absorption spectral titration of the P450BM3 F87A heme domain with Im-DFSM-dipeps. 5 “The Kd value of Im-C6-Phe-Phe reached 3.1×10−7 M.” The preceding binding-affinity section identifies absorption spectral titration of the P450BM3 F87A heme domain. auto_single_measurement only accepted activity measurement [1] 1 structures\7Y0T\7Y0T_metadata.json point structures/7Y0T/7y0t_protein.pdb structures/7Y0T/7y0t_pocket.pdb structures/7Y0T/7y0t_ligand.pdb structures/7Y0T/7y0t_ligand.cif structures/7Y0T/7y0t_complex.pdb structures/7Y0T/7y0t_complex.cif 7Y1W classic human prolyl-tRNA synthetase 1 (PARS1) human Na Na DWN12088 "[""F9O""]" 1 Kd Kd = = 20.49 ± 8.58 µM 20490.0 [] unit_conversion 4.688458041598805 success True direct_binding Microscale thermophoresis (MST) binding measurement in sufficient ATP; Figure 6B reports mean ± SD. 12 Figure 6B visibly reports for DWN12088: “WT Kd = 20.49 ± 8.58”; the x-axis is DWN12088 concentration (µM). auto_single_measurement only accepted activity measurement [1] 1 structures\7Y1W\7Y1W_metadata.json point structures/7Y1W/7y1w_protein.pdb structures/7Y1W/7y1w_pocket.pdb structures/7Y1W/7y1w_ligand.sdf structures/7Y1W/7y1w_ligand.pdb structures/7Y1W/7y1w_ligand.cif structures/7Y1W/7y1w_complex.pdb structures/7Y1W/7y1w_complex.cif 7Y42 classic SARS-CoV-2 spike glycoprotein SARS-CoV-2 Prefusion S ectodomain residues 1-1208 with a C-terminal trimerization motif, HRV3C protease cleavage site, and Twin-Strep-tag Proline substitutions at residues 986 and 987; GSAS substitution at the furin cleavage site all-trans retinoic acid (ATRA) "[""REA""]" 1 Kd Kd = = 3.44 × 10^-6 M 3439.9999999999995 [] unit_conversion 5.46344155742847 success True direct_binding Surface plasmon resonance assay using purified SARS-CoV-2 spike protein and ATRA. 6 “ATRA directly interacted with the trimeric spike protein, with an equilibrium dissociation constant (Kd) of 3.44 × 10−6 M (Fig. 4A).” auto_single_measurement only accepted activity measurement [1] 1 structures\7Y42\7Y42_metadata.json point structures/7Y42/7y42_protein.pdb structures/7Y42/7y42_pocket.pdb structures/7Y42/7y42_ligand.sdf structures/7Y42/7y42_ligand.pdb structures/7Y42/7y42_ligand.cif structures/7Y42/7y42_complex.pdb structures/7Y42/7y42_complex.cif 7Y4U classic c-Met human c-Met residues 1038-1346 with an N-terminal His-SUMO tag and Ulp1 protease cleavage site wild-type compound 9Y "[""I94""]" 1 IC50 IC50 = = 4.8 nM 4.8 [] unit_conversion 8.318758762624412 success True biochemical_inhibition FRET-based Z′-Lyte biochemical c-Met kinase inhibition assay; 50 μM ATP. 6 Table 2 prints c-Met IC50 = 4.8 nM for 9y; the text identifies 9y as the c-Met cocrystal structure PDB 7Y4U. auto_single_measurement only accepted activity measurement [1] 1 structures\7Y4U\7Y4U_metadata.json point structures/7Y4U/7y4u_protein.pdb structures/7Y4U/7y4u_pocket.pdb structures/7Y4U/7y4u_ligand.sdf structures/7Y4U/7y4u_ligand.pdb structures/7Y4U/7y4u_ligand.cif structures/7Y4U/7y4u_complex.pdb structures/7Y4U/7y4u_complex.cif 7Y5T classic PS1-containing gamma-secretase human Na WT MRK-560 "[""IGD""]" 1 IC50 IC50 = = 33 ± 2 nM 33.0 [] unit_conversion 7.481486060122112 success True biochemical_inhibition Purified PS1 complex in an in vitro cleavage assay; AP40 production quantified by AlphaLISA. 2 “The IC50 of MRK-560 for PS1- or PS2-complex is estimated to be 33 ± 2 nM or 173 ± 24 nM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\7Y5T\7Y5T_metadata.json point structures/7Y5T/7y5t_protein.pdb structures/7Y5T/7y5t_pocket.pdb structures/7Y5T/7y5t_ligand.sdf structures/7Y5T/7y5t_ligand.pdb structures/7Y5T/7y5t_ligand.cif structures/7Y5T/7y5t_complex.pdb structures/7Y5T/7y5t_complex.cif 7Y74 classic Apostichopus japonicus ferritin mutant-D129A/E132A Apostichopus japonicus AjFER-D129A/E132A mutant (M3) D129A/E132A Fe2+ "[""FE""]" 1 Kd Kd = = 230.6 ± 9.1 nM 230.6 [] unit_conversion 6.637140697041319 success True direct_binding Microscale thermophoresis (MST) binding assay of Fe2+ to M3 protein. 13 “Kd = 230.6 ± 9.1 nM for the M3 protein” in MST binding assays of Fe2+ ions. auto_single_measurement only accepted activity measurement [1] 1 structures\7Y74\7Y74_metadata.json point structures/7Y74/7y74_protein.pdb structures/7Y74/7y74_pocket.pdb structures/7Y74/7y74_ligand.sdf structures/7Y74/7y74_ligand.pdb structures/7Y74/7y74_ligand.cif structures/7Y74/7y74_complex.pdb structures/7Y74/7y74_complex.cif 7Y8D extended BCL-X_L Na Na Na cp1 "[""CHAIN:B""]" 1 Kd Kd > > 12.14 µM 12140.0 [] unit_conversion 4.915781313260761 success True direct_binding SPR affinity fitting assay; Table 1. 4 Table 1 reports BCL-X_L–cp1 K_D >12.14 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Y8D\7Y8D_metadata.json point structures/7Y8D/7y8d_protein.pdb structures/7Y8D/7y8d_pocket.pdb structures/7Y8D/7y8d_ligand.pdb structures/7Y8D/7y8d_ligand.cif structures/7Y8D/7y8d_complex.pdb structures/7Y8D/7y8d_complex.cif 7Y90 extended BCL-2 Na Na Na cp1 "[""CHAIN:B""]" 1 Kd Kd = = 0.65 ± 0.14 µM 650.0 [] unit_conversion 6.187086643357144 success True direct_binding SPR affinity fitting assay; Table 1. 4 Table 1 reports BCL-2–cp1 K_D 0.65 ± 0.14 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Y90\7Y90_metadata.json point structures/7Y90/7y90_protein.pdb structures/7Y90/7y90_pocket.pdb structures/7Y90/7y90_ligand.pdb structures/7Y90/7y90_ligand.cif structures/7Y90/7y90_complex.pdb structures/7Y90/7y90_complex.cif 7Y9U classic PIN1 auxin exporter Arabidopsis thaliana Full-length PIN1 with an N-terminal Flag tag Na NPA (N-1-naphthylphthalamic acid) "[""E7O""]" 1 Kd Kd = = 0.15 ± 0.08 μM 150.0 [] unit_conversion 6.823908740944319 success True direct_binding Isothermal titration calorimetry of purified wild-type PIN1 with NPA at pH 7.0. 4 Fig. 4b reports ITC results for NPA binding to wild-type PIN1 with Kd = 0.15 ± 0.08 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Y9U\7Y9U_metadata.json point structures/7Y9U/7y9u_protein.pdb structures/7Y9U/7y9u_pocket.pdb structures/7Y9U/7y9u_ligand.sdf structures/7Y9U/7y9u_ligand.pdb structures/7Y9U/7y9u_ligand.cif structures/7Y9U/7y9u_complex.pdb structures/7Y9U/7y9u_complex.cif 7YAA extended BCL-X_L Na Na Na cp3 "[""CHAIN:B""]" 1 Kd Kd = = 0.09 ± 0.01 µM 90.0 [] unit_conversion 7.045757490560675 success True direct_binding SPR affinity fitting assay; Table 1. 4 Table 1 reports BCL-X_L–cp3 K_D 0.09 ± 0.01 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7YAA\7YAA_metadata.json point structures/7YAA/7yaa_protein.pdb structures/7YAA/7yaa_pocket.pdb structures/7YAA/7yaa_ligand.pdb structures/7YAA/7yaa_ligand.cif structures/7YAA/7yaa_complex.pdb structures/7YAA/7yaa_complex.cif 7YF6 extended HIV-1 protease Na Na Na compound 1 "[""CHAIN:C""]" 1 IC50 IC50 = = 8.05 nM 8.05 [] unit_conversion 8.094204119632131 success True biochemical_inhibition Fluorogenic peptide cleavage assay of HIV-1 protease. 2 Figure 2 prints for compound 1: IC50 (nM): 8.05; its footnote identifies a fluorogenic peptide cleavage assay of HIV-1 protease. auto_single_measurement only accepted activity measurement [1] 1 structures\7YF6\7YF6_metadata.json point structures/7YF6/7yf6_protein.pdb structures/7YF6/7yf6_pocket.pdb structures/7YF6/7yf6_ligand.pdb structures/7YF6/7yf6_ligand.cif structures/7YF6/7yf6_complex.pdb structures/7YF6/7yf6_complex.cif 7YGH extended Sso2081 Saccharolobus solfataricus Na Na cA4 (cyclic tetraadenylate) "[""CHAIN:C""]" 1 Kd Kd = = 5.7 ± 3.4 nM 5.7 [] unit_conversion 8.244125144327509 success True direct_binding Microscale thermophoresis (MST) binding assay using 50 nM labelled protein and varying cA4 concentrations. 7 Figure 5A reports cA4 binding to WT Sso2081 with K_D = 5.7 ± 3.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7YGH\7YGH_metadata.json point structures/7YGH/7ygh_protein.pdb structures/7YGH/7ygh_pocket.pdb structures/7YGH/7ygh_ligand.pdb structures/7YGH/7ygh_ligand.cif structures/7YGH/7ygh_complex.pdb structures/7YGH/7ygh_complex.cif 7YJP classic MCR-1 Na MCR-1-S, truncated soluble MCR-1 fragment, residues 200-541 Na AuCl "[""AU""]" 1 Kd Kd = = 0.8 ± 0.24 µM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Isothermal titration calorimetry of AuCl (Au+) into apo-MCR-1-S; sequential-binding model. 7 ITC showed Au+ (as AuCl) binding to apo-MCR-1-S with Kd = 0.8 ± 0.24 µM and N = 2.34 ± 0.33. auto_single_measurement only accepted activity measurement [1] 1 structures\7YJP\7YJP_metadata.json point structures/7YJP/7yjp_protein.pdb structures/7YJP/7yjp_pocket.pdb structures/7YJP/7yjp_ligand.sdf structures/7YJP/7yjp_ligand.pdb structures/7YJP/7yjp_ligand.cif structures/7YJP/7yjp_complex.pdb structures/7YJP/7yjp_complex.cif 7YKG extended MAGI2 mouse MAGI2 PDZ0-GK, His6 tag removed after 3C cleavage Na pSGEF "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.43 μM 430.0 [] unit_conversion 6.366531544420413 success True direct_binding ITC-based binding of synthesized phospho-SGEF peptide to MAGI2 PDZ0-GK. 7 The text reports pSGEF among peptides binding MAGI2 PDZ0-GK, with Kd 0.43 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\7YKG\7YKG_metadata.json point structures/7YKG/7ykg_protein.pdb structures/7YKG/7ykg_pocket.pdb structures/7YKG/7ykg_ligand.pdb structures/7YKG/7ykg_ligand.cif structures/7YKG/7ykg_complex.pdb structures/7YKG/7ykg_complex.cif 7YKH extended MAGI2 mouse MAGI2 PDZ0-GK, His6 tag removed after 3C cleavage Na pSAPAP1-GBR2 "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.07 ± 0.01 μM 70.0 [] unit_conversion 7.154901959985743 success True direct_binding ITC-based binding of MAGI2 PDZ0-GK to pSAPAP1-GBR2, Fig. 1D. 2 Fig. 1D labels “PDZ0-GK ~ pSAPAP1-GBR2, Kd: 0.07 ± 0.01 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7YKH\7YKH_metadata.json point structures/7YKH/7ykh_protein.pdb structures/7YKH/7ykh_pocket.pdb structures/7YKH/7ykh_ligand.pdb structures/7YKH/7ykh_ligand.cif structures/7YKH/7ykh_complex.pdb structures/7YKH/7ykh_complex.cif 7YKI extended MAGI2 mouse MAGI2 PDZ0-GK, His6 tag removed after 3C cleavage Na pSAPAP1-GBR3 "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd ~ ~ 0.08 μM 80.0 [] unit_conversion 7.096910013008056 success True direct_binding Direct binding of MAGI2 PDZ0-GK to pSAPAP1-GBR3; the text cites Fig. S2A. 3 The text states that MAGI2 PDZ0-GK bound pSAPAP1-GBR3 with similar affinity, “Kd of ~0.08 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7YKI\7YKI_metadata.json point structures/7YKI/7yki_protein.pdb structures/7YKI/7yki_pocket.pdb structures/7YKI/7yki_ligand.pdb structures/7YKI/7yki_ligand.cif structures/7YKI/7yki_complex.pdb structures/7YKI/7yki_complex.cif 7YLE classic RnDmpX Roseovarius nubinhibens ISM Na Na DMSP "[""DQY""]" 1 Kd Kd = = 474 nM 474.0 [] unit_conversion 6.324221658325914 success True direct_binding Isothermal titration calorimetry (Fig. S2); value stated in main text. 5 “The recombinant RnDmpX also presented a high binding affinity for DMSP, with a Kd of 474 nM (Fig. S2).” The RnDmpX/DMSP complex is deposited as PDB 7YLE. auto_single_measurement only accepted activity measurement [1] 1 structures\7YLE\7YLE_metadata.json point structures/7YLE/7yle_protein.pdb structures/7YLE/7yle_pocket.pdb structures/7YLE/7yle_ligand.sdf structures/7YLE/7yle_ligand.pdb structures/7YLE/7yle_ligand.cif structures/7YLE/7yle_complex.pdb structures/7YLE/7yle_complex.cif 7YM1 classic Staphylococcus aureus SsbA (SaSsbA) Staphylococcus aureus His-tagged SaSsbA Na 5-fluorouracil (5-FU) "[""URF""]" 1 Kd Kd = = 55.9 ± 0.7 μM 55900.0 [] unit_conversion 4.252588192113577 success True direct_binding Purified SaSsbA fluorescence-quenching titration with 5-FU; Kd determined from titration curves. 11 “K_d values of 497.6 ± 13.5 μM for R18A and 55.9 ± 0.7 μM for WT (Table 3).” auto_single_measurement only accepted activity measurement [1] 1 structures\7YM1\7YM1_metadata.json point structures/7YM1/7ym1_protein.pdb structures/7YM1/7ym1_pocket.pdb structures/7YM1/7ym1_ligand.sdf structures/7YM1/7ym1_ligand.pdb structures/7YM1/7ym1_ligand.cif structures/7YM1/7ym1_complex.pdb structures/7YM1/7ym1_complex.cif 7YMG classic BRD4 bromodomain 1 (BD1) Na BRD4 BD1 residues 44-168 with an N-terminal His6-TEV tag, cleaved before crystallization Na compound 12; 2-({3-ethyl-[1,2,4]triazolo[4,3-b]pyridazin-6-yl}amino)-3-(1H-indol-3-yl)propan-1-ol "[""JHO""]" 1 IC50 IC50 = = 25.2 (±4.6) µM 25200.0 [] unit_conversion 4.598599459218456 success True biochemical_inhibition AlphaScreen inhibition assay; Table 1, N=3 and standard deviations shown in parentheses. 5 Table 1 reports IC50 (BD1) for compound 12 as 25.2 (±4.6) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7YMG\7YMG_metadata.json point structures/7YMG/7ymg_protein.pdb structures/7YMG/7ymg_pocket.pdb structures/7YMG/7ymg_ligand.sdf structures/7YMG/7ymg_ligand.pdb structures/7YMG/7ymg_ligand.cif structures/7YMG/7ymg_complex.pdb structures/7YMG/7ymg_complex.cif 7YQ9 classic BRD4 bromodomain 1 (BD1) Na BRD4 BD1 residues 44-168 with an N-terminal His6-TEV tag, cleaved before crystallization Na compound 6; N-[2-(1H-indol-3-yl)ethyl]-3-(trifluoromethyl)[1,2,4]triazolo[4,3-b]pyridazin-6-amine "[""JLX""]" 1 IC50 IC50 = = 9.6 (±2.0) µM 9600.0 [] unit_conversion 5.017728766960431 success True biochemical_inhibition AlphaScreen inhibition assay; Table 1, N=3 and standard deviations shown in parentheses. 5 Table 1 reports IC50 (BD1) for compound 6 as 9.6 (±2.0) µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7YQ9\7YQ9_metadata.json point structures/7YQ9/7yq9_protein.pdb structures/7YQ9/7yq9_pocket.pdb structures/7YQ9/7yq9_ligand.sdf structures/7YQ9/7yq9_ligand.pdb structures/7YQ9/7yq9_ligand.cif structures/7YQ9/7yq9_complex.pdb structures/7YQ9/7yq9_complex.cif 7YQG extended GII.6 P domain Na P domain residues 224-551 wild-type H disaccharides "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 8.78 × 10^-6 M 8779.999999999998 [] unit_conversion 5.056505484093897 success True direct_binding Biolayer interferometry (Octet RED96) of GII.6 P particles with immobilized biotin-labeled H disaccharides; association and dissociation curves were measured. 4 The P domain bound H disaccharides with an affinity constant Kd of 8.78 μmol/L; Table/Fig. 2 prints Kd = 8.78 × 10^-6 M. auto_single_measurement only accepted activity measurement [1] 1 structures\7YQG\7YQG_metadata.json point structures/7YQG/7yqg_protein.pdb structures/7YQG/7yqg_pocket.pdb structures/7YQG/7yqg_ligand.pdb structures/7YQG/7yqg_ligand.cif structures/7YQG/7yqg_complex.pdb structures/7YQG/7yqg_complex.cif 7YUE extended scFv D31 human D31 single-chain variable fragment with a C-terminal 6XHis tag Amber stop codon TAG in CDR H2 mutated to glutamine (CAG) S2' 12-mer peptide epitope, RSFIEDLLFNKV "[""CHAIN:C""]" 1 Kd Kd = = 7.81 × 10⁻7 M 780.9999999999999 [] unit_conversion 6.1073489661227 success True direct_binding Biolayer interferometry (BLI) binding affinity of purified scFv D31 to immobilized BSA-S2′ epitope. 7 Table 1 reports scFv D31 K_D with peptide as 7.81 × 10⁻7 M; the text identifies BLI as the affinity method. auto_single_measurement only accepted activity measurement [1] 1 structures\7YUE\7YUE_metadata.json point structures/7YUE/7yue_protein.pdb structures/7YUE/7yue_pocket.pdb structures/7YUE/7yue_ligand.pdb structures/7YUE/7yue_ligand.cif structures/7YUE/7yue_complex.pdb structures/7YUE/7yue_complex.cif 7YV4 classic human UCHL3 human Na Na Farrerol "[""JXY""]" 1 Kd Kd = = 36.73 nM 36.73 [] unit_conversion 7.434979071654706 success True direct_binding SPR measurement using recombinant UCHL3 and farrerol at different concentrations. 2 “The results revealed a strong interaction between farrerol and UCHL3, and the dissociation constant (Kd) of farrerol to UCHL3 reached a low of 36.73 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7YV4\7YV4_metadata.json point structures/7YV4/7yv4_protein.pdb structures/7YV4/7yv4_pocket.pdb structures/7YV4/7yv4_ligand.sdf structures/7YV4/7yv4_ligand.pdb structures/7YV4/7yv4_ligand.cif structures/7YV4/7yv4_complex.pdb structures/7YV4/7yv4_complex.cif 7YWM classic Mycobacterium abscessus phosphopantetheine adenylyltransferase (PPAT) Mycobacterium abscessus Na Na ATP "[""ATP""]" 1 Kd Kd = = 20.1 ± 3.3 µM 20100.0 [] unit_conversion 4.696803942579511 success True direct_binding Isothermal titration calorimetry (ITC) of ATP binding to Mab PPAT. 10 The paper states that ATP has Kd 20.1 ± 3.3 µM for Mab PPAT; Figure 1A maps ATP-bound Mab PPAT to PDB 7YWM. auto_single_measurement only accepted activity measurement [1] 1 structures\7YWM\7YWM_metadata.json point structures/7YWM/7ywm_protein.pdb structures/7YWM/7ywm_pocket.pdb structures/7YWM/7ywm_ligand.sdf structures/7YWM/7ywm_ligand.pdb structures/7YWM/7ywm_ligand.cif structures/7YWM/7ywm_complex.pdb structures/7YWM/7ywm_complex.cif 7YWT extended Carbonic anhydrase II human Na Na compound 34a; 4-oxo-N-(4-sulfamoylphenyl)-1,3,4,6,7,11b-hexahydro-2H-pyrazino[2,1-a]isoquinoline-2-carboxamide "[""I6U""]" 1 Ki Ki = = 8.4 ± 0.8 nM 8.4 [] unit_conversion 8.075720713938118 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay. 7 Table 1 reports Ki = 8.4 ± 0.8 nM for compound 34a against hCA II. Figure 3 identifies hCA II–34a as PDB 7YWT. auto_single_measurement only accepted activity measurement [1] 1 structures\7YWT\7YWT_metadata.json point structures/7YWT/7ywt_ligand.sdf structures/7YWT/7ywt_ligand.cif structures/7YWT/7ywt_complex.cif 7YX1 classic Sandercyanin fluorescent protein (SFP) Canadian walleye (Stizostedion vitreum) Tetrameric SFP variant Y142A Biliverdin IX-alpha (BV) "[""BLA""]" 1 Kd Kd = = 4.1 ± 0.09 μM 4100.0 [] unit_conversion 5.3872161432802645 success True direct_binding Binding curve of BV to Y142A tetrameric SFP protein. 4 Fig. 2B caption prints: “The Kd of BV to wild-type protein is 7.06 μM (±0.71 μM), V71E, L135E, and Y142A have Kd values of 1.97 (±0.12) μM, 1.2 (±0.10) μM, and 4.1 (±0.09) μM, respectively.” The main text states all F55A, F106A, H108A, and Y142A variants are tetrameric on BV binding; page 7 maps PDB 7YX1 to Y142A. auto_single_measurement only accepted activity measurement [1] 1 structures\7YX1\7YX1_metadata.json point structures/7YX1/7yx1_protein.pdb structures/7YX1/7yx1_pocket.pdb structures/7YX1/7yx1_ligand.sdf structures/7YX1/7yx1_ligand.pdb structures/7YX1/7yx1_ligand.cif structures/7YX1/7yx1_complex.pdb structures/7YX1/7yx1_complex.cif 7YXI classic Drosophila melanogaster JMJD7 (dmJMJD7) Drosophila melanogaster Full-length dmJMJD7, residues 1-316, N-terminal His6-tagged Na N-oxalylglycine (NOG) "[""OGA""]" 1 IC50 IC50 = = 0.3 µM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition SPE-MS inhibition assay of His6-dmJMJD7 activity using a DRG1 peptide substrate. 4 The paper reports N-oxalylglycine (IC50 0.3 µM) for dmJMJD7. auto_single_measurement only accepted activity measurement [1] 1 structures\7YXI\7YXI_metadata.json point structures/7YXI/7yxi_protein.pdb structures/7YXI/7yxi_pocket.pdb structures/7YXI/7yxi_ligand.sdf structures/7YXI/7yxi_ligand.pdb structures/7YXI/7yxi_ligand.cif structures/7YXI/7yxi_complex.pdb structures/7YXI/7yxi_complex.cif 7YXJ classic Drosophila melanogaster JMJD7 (dmJMJD7) Drosophila melanogaster Full-length dmJMJD7, residues 1-316, N-terminal His6-tagged Na 2,4-PDCA "[""PD2""]" 1 IC50 IC50 = = 1.34 µM 1340.0 [] unit_conversion 5.872895201635192 success True biochemical_inhibition SPE-MS inhibition assay of His6-dmJMJD7 activity using a DRG1 peptide substrate. 4 The paper reports pyridine-2,4-dicarboxylate (2,4-PDCA; IC50 1.34 µM) for dmJMJD7. auto_single_measurement only accepted activity measurement [1] 1 structures\7YXJ\7YXJ_metadata.json point structures/7YXJ/7yxj_protein.pdb structures/7YXJ/7yxj_pocket.pdb structures/7YXJ/7yxj_ligand.sdf structures/7YXJ/7yxj_ligand.pdb structures/7YXJ/7yxj_ligand.cif structures/7YXJ/7yxj_complex.pdb structures/7YXJ/7yxj_complex.cif 7YXK classic Drosophila melanogaster JMJD7 (dmJMJD7) Drosophila melanogaster Full-length dmJMJD7, residues 1-316, N-terminal His6-tagged Na N-oxalyl-D-alanine (NODA) "[""I78""]" 1 IC50 IC50 = = 4.14 µM 4140.0 [] unit_conversion 5.3829996588791005 success True biochemical_inhibition SPE-MS inhibition assay of His6-dmJMJD7 activity using a DRG1 peptide substrate. 4 The paper reports N-oxalyl-D-alanine (IC50 4.14 µM) for dmJMJD7. auto_single_measurement only accepted activity measurement [1] 1 structures\7YXK\7YXK_metadata.json point structures/7YXK/7yxk_protein.pdb structures/7YXK/7yxk_pocket.pdb structures/7YXK/7yxk_ligand.sdf structures/7YXK/7yxk_ligand.pdb structures/7YXK/7yxk_ligand.cif structures/7YXK/7yxk_complex.pdb structures/7YXK/7yxk_complex.cif 7YXL classic Drosophila melanogaster JMJD7 (dmJMJD7) Drosophila melanogaster Full-length dmJMJD7, residues 1-316, N-terminal His6-tagged Na N-oxalyl-D-phenylalanine (NOFD) "[""NDF""]" 1 IC50 IC50 = = 1.34 µM 1340.0 [] unit_conversion 5.872895201635192 success True biochemical_inhibition SPE-MS inhibition assay of His6-dmJMJD7 activity using a DRG1 peptide substrate. 4 The paper reports N-oxalyl-D-phenylalanine (IC50 1.34 µM) for dmJMJD7. auto_single_measurement only accepted activity measurement [1] 1 structures\7YXL\7YXL_metadata.json point structures/7YXL/7yxl_protein.pdb structures/7YXL/7yxl_pocket.pdb structures/7YXL/7yxl_ligand.sdf structures/7YXL/7yxl_ligand.pdb structures/7YXL/7yxl_ligand.cif structures/7YXL/7yxl_complex.pdb structures/7YXL/7yxl_complex.cif 7YXZ classic Mycobacterium abscessus phosphopantetheine adenylyltransferase (PPAT) Mycobacterium abscessus Na Na Coenzyme A (CoA) "[""COA""]" 1 Kd Kd = = 8.2 ± 1.1 µM 8200.0 [] unit_conversion 5.086186147616283 success True direct_binding Isothermal titration calorimetry (ITC) of Coenzyme A binding to Mab PPAT. 6 Figure 2C reports Coenzyme A Kd (Mab PPAT) = 8.2 ± 1.1 µM; Figure 2A maps the CoA complex to PDB 7YXZ. auto_single_measurement only accepted activity measurement [1] 1 structures\7YXZ\7YXZ_metadata.json point structures/7YXZ/7yxz_protein.pdb structures/7YXZ/7yxz_pocket.pdb structures/7YXZ/7yxz_ligand.sdf structures/7YXZ/7yxz_ligand.pdb structures/7YXZ/7yxz_ligand.cif structures/7YXZ/7yxz_complex.pdb structures/7YXZ/7yxz_complex.cif 7YY2 classic Mycobacterium abscessus phosphopantetheine adenylyltransferase (PPAT) Mycobacterium abscessus Na Na Compound 20 "[""EP8""]" 1 Kd Kd = = 3.2 ± 0.8 µM 3200.0 [] unit_conversion 5.494850021680094 success True direct_binding Isothermal titration calorimetry (ITC) of Compound 20 binding to Mab PPAT. 9 Figure 4B reports thermodynamic (ITC) profiles of Compound 20 interaction with Mab PPAT and gives Kd (Mab PPAT) = 3.2 ± 0.8 µM; Figure 3 caption identifies Compound 20-bound Mab PPAT as PDB 7YY2. auto_single_measurement only accepted activity measurement [1] 1 structures\7YY2\7YY2_metadata.json point structures/7YY2/7yy2_protein.pdb structures/7YY2/7yy2_pocket.pdb structures/7YY2/7yy2_ligand.sdf structures/7YY2/7yy2_ligand.pdb structures/7YY2/7yy2_ligand.cif structures/7YY2/7yy2_complex.pdb structures/7YY2/7yy2_complex.cif 7YZH extended Carbonic anhydrase (SmCA) Schistosoma mansoni Na Na compound 35c; 4-oxo-N-(4-sulfamoylphenethyl)-1,3,4,6,7,11b-hexahydro-2H-pyrazino[2,1-a]isoquinoline-2-carbothioamide "[""HFF""]" 1 Ki Ki = = 4627 ± 1284 nM 4627.0 [] unit_conversion 5.334700500500103 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay. 7 Table 1 reports Ki = 4627 ± 1284 nM for compound 35c against SmCA. Figure 2 identifies SmCA–35c as PDB 7YZH. auto_single_measurement only accepted activity measurement [1] 1 structures\7YZH\7YZH_metadata.json point structures/7YZH/7yzh_ligand.sdf structures/7YZH/7yzh_ligand.cif structures/7YZH/7yzh_complex.cif 7YZM classic DCCP:DCCP-R complex Na Na Na MgADPNP "[""ANP""]" 1 Kd Kd = = 7.1 ± 1.1 µM 7100.0 [] unit_conversion 5.1487416512809245 success True direct_binding ITC nucleotide-binding experiment with DCCP additionally present in the titration cell; the stated affinity is for MgADPNP. 2 The text states that DCCP in the titration cell changed thermodynamic contributions but not affinity: “MgADPNP: Kd = 7.1 ± 1.1 µM.” Page 7 maps PDB 7YZM to DCCP:DCCP-R with MgADPNP. auto_single_measurement only accepted activity measurement [1] 1 structures\7YZM\7YZM_metadata.json point structures/7YZM/7yzm_protein.pdb structures/7YZM/7yzm_pocket.pdb structures/7YZM/7yzm_ligand.sdf structures/7YZM/7yzm_ligand.pdb structures/7YZM/7yzm_ligand.cif structures/7YZM/7yzm_complex.pdb structures/7YZM/7yzm_complex.cif 7Z14 extended Torpedo nicotinic acetylcholine receptor (nAChR) Na Native Torpedo muscle-type nAChR reconstituted in asolectin-MSP1E3D1 lipid nanodiscs Na ScNtx (consensus short-chain alpha-neurotoxin) "[""CHAIN:F"", ""CHAIN:G""]" 1 Kd Kd = = 28 nM 28.0 [] unit_conversion 7.552841968657781 success True direct_binding Microscale thermophoresis with fluorescently labelled ScNtx-NT647; binding affinity determined from normalized fluorescence versus Torpedo nAChR concentration. 2 The text reports an apparent affinity of 28 nM, and Fig. 1b explicitly labels “KD=28 nM” for ScNtx binding to Torpedo nAChR. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z14\7Z14_metadata.json point structures/7Z14/7z14_protein.pdb structures/7Z14/7z14_pocket.pdb structures/7Z14/7z14_ligand.pdb structures/7Z14/7z14_ligand.cif structures/7Z14/7z14_complex.pdb structures/7Z14/7z14_complex.cif 7Z1K extended SHARP (SPEN) human SHARP SPOC residues 3496-3664; N-terminal His6 fusion in pET M11 Na 1x5SP CTD peptide (RNA polymerase II CTD heptapeptide phosphorylated on Ser5) "[""CHAIN:B""]" 1 Kd Kd = = 23.8 ± 0.8 µM 23800.0 [] unit_conversion 4.623423042943488 success True direct_binding Fluorescence anisotropy binding assay of purified SHARP SPOC with a singly Ser5-phosphorylated RNA polymerase II CTD peptide. 4 The paper states that SHARP requires phosphorylation in a single repeat and reports Kd = 23.8 ± 0.8 µM for 1×S5P. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z1K\7Z1K_metadata.json point structures/7Z1K/7z1k_protein.pdb structures/7Z1K/7z1k_pocket.pdb structures/7Z1K/7z1k_ligand.pdb structures/7Z1K/7z1k_ligand.cif structures/7Z1K/7z1k_complex.pdb structures/7Z1K/7z1k_complex.cif 7Z24 classic HIV-1 reverse transcriptase HIV-1 p66/p51 RT heterodimer with 38-mer DNA-hairpin aptamer wild-type Nevirapine (NVP) "[""NVP""]" 1 IC50 IC50 = = 130 ± 10 nM 130.0 [] unit_conversion 6.886056647693163 success True biochemical_inhibition EnzChek Reverse Transcriptase Assay Kit; IC50 inhibition assay. 5 Table 1 reports wild-type RT IC50 for NVP as 130 ± 10 nM; text identifies this as the current study's enzymatic inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z24\7Z24_metadata.json point structures/7Z24/7z24_protein.pdb structures/7Z24/7z24_pocket.pdb structures/7Z24/7z24_ligand.sdf structures/7Z24/7z24_ligand.pdb structures/7Z24/7z24_ligand.cif structures/7Z24/7z24_complex.pdb structures/7Z24/7z24_complex.cif 7Z28 classic ERAP1 human Optimized ERAP1 construct with the exon 10 loop substituted by a GSG linker Exon 10 loop substituted by linker GSG Compound 30 (bestatin analogue inhibitor) "[""I88""]" 1 IC50 IC50 = = 1.2 µM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition Fluorogenic enzymatic inhibition assay using recombinant human ERAP1; Table 1. 5 Table 1 reports compound 30 IC50 = 1.2 µM against ERAP1. The structure is identified as ERAP1–30 (PDB 7Z28) on page 7, whereas the GSG exon-10-loop construct is stated for structural determination on page 17 and is not established for the inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z28\7Z28_metadata.json point structures/7Z28/7z28_protein.pdb structures/7Z28/7z28_pocket.pdb structures/7Z28/7z28_ligand.sdf structures/7Z28/7z28_ligand.pdb structures/7Z28/7z28_ligand.cif structures/7Z28/7z28_complex.pdb structures/7Z28/7z28_complex.cif 7Z29 classic HIV-1 reverse transcriptase HIV-1 p66/p51 RT heterodimer with 38-mer DNA-hairpin aptamer E138K in p51; M184I in p66 Nevirapine (NVP) "[""NVP""]" 1 IC50 IC50 = = 88 ± 17 nM 88.0 [] unit_conversion 7.055517327849831 success True biochemical_inhibition EnzChek Reverse Transcriptase Assay Kit; IC50 inhibition assay. 5 Table 1 reports E138K/M184I RT IC50 for NVP as 88 ± 17 nM (0.7-fold resistance). auto_single_measurement only accepted activity measurement [1] 1 structures\7Z29\7Z29_metadata.json point structures/7Z29/7z29_protein.pdb structures/7Z29/7z29_pocket.pdb structures/7Z29/7z29_ligand.sdf structures/7Z29/7z29_ligand.pdb structures/7Z29/7z29_ligand.cif structures/7Z29/7z29_complex.pdb structures/7Z29/7z29_complex.cif 7Z2D classic HIV-1 reverse transcriptase HIV-1 p66/p51 RT heterodimer with 38-mer DNA-hairpin aptamer wild-type Rilpivirine (RPV) "[""T27""]" 1 IC50 IC50 = = 3.9 ± 0.4 nM 3.9 [] unit_conversion 8.4089353929735 success True biochemical_inhibition EnzChek Reverse Transcriptase Assay Kit; IC50 inhibition assay. 5 Table 1 reports wild-type RT IC50 for RPV as 3.9 ± 0.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z2D\7Z2D_metadata.json point structures/7Z2D/7z2d_protein.pdb structures/7Z2D/7z2d_pocket.pdb structures/7Z2D/7z2d_ligand.sdf structures/7Z2D/7z2d_ligand.pdb structures/7Z2D/7z2d_ligand.cif structures/7Z2D/7z2d_complex.pdb structures/7Z2D/7z2d_complex.cif 7Z2E classic HIV-1 reverse transcriptase HIV-1 p66/p51 RT heterodimer with 38-mer DNA-hairpin aptamer E138K in p51; M184I in p66 Rilpivirine (RPV) "[""T27""]" 1 IC50 IC50 = = 8.9 ± 0.2 nM 8.9 [] unit_conversion 8.050609993355087 success True biochemical_inhibition EnzChek Reverse Transcriptase Assay Kit; IC50 inhibition assay. 5 Table 1 reports E138K/M184I RT IC50 for RPV as 8.9 ± 0.2 nM (2.3-fold resistance). auto_single_measurement only accepted activity measurement [1] 1 structures\7Z2E\7Z2E_metadata.json point structures/7Z2E/7z2e_protein.pdb structures/7Z2E/7z2e_pocket.pdb structures/7Z2E/7z2e_ligand.sdf structures/7Z2E/7z2e_ligand.pdb structures/7Z2E/7z2e_ligand.cif structures/7Z2E/7z2e_complex.pdb structures/7Z2E/7z2e_complex.cif 7Z2G classic HIV-1 reverse transcriptase HIV-1 p66/p51 RT heterodimer with 38-mer DNA-hairpin aptamer wild-type Doravirine (DOR) "[""2KW""]" 1 IC50 IC50 = = 11 ± 1 nM 11.0 [] unit_conversion 7.958607314841775 success True biochemical_inhibition EnzChek Reverse Transcriptase Assay Kit; IC50 inhibition assay. 5 Table 1 reports wild-type RT IC50 for DOR as 11 ± 1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z2G\7Z2G_metadata.json point structures/7Z2G/7z2g_protein.pdb structures/7Z2G/7z2g_pocket.pdb structures/7Z2G/7z2g_ligand.sdf structures/7Z2G/7z2g_ligand.pdb structures/7Z2G/7z2g_ligand.cif structures/7Z2G/7z2g_complex.pdb structures/7Z2G/7z2g_complex.cif 7Z2H classic HIV-1 reverse transcriptase HIV-1 p66/p51 RT heterodimer with 38-mer DNA-hairpin aptamer E138K in p51; M184I in p66 Doravirine (DOR) "[""2KW""]" 1 IC50 IC50 = = 26 ± 1 nM 26.0 [] unit_conversion 7.585026652029182 success True biochemical_inhibition EnzChek Reverse Transcriptase Assay Kit; IC50 inhibition assay. 5 Table 1 reports E138K/M184I RT IC50 for DOR as 26 ± 1 nM (2.4-fold resistance). auto_single_measurement only accepted activity measurement [1] 1 structures\7Z2H\7Z2H_metadata.json point structures/7Z2H/7z2h_protein.pdb structures/7Z2H/7z2h_pocket.pdb structures/7Z2H/7z2h_ligand.sdf structures/7Z2H/7z2h_ligand.pdb structures/7Z2H/7z2h_ligand.cif structures/7Z2H/7z2h_complex.pdb structures/7Z2H/7z2h_complex.cif 7Z3U extended SARS-CoV-2 Main Protease SARS-CoV-2 Na Na Sulfo-Calpeptin (S-Calpeptin), activated "[""CHAIN:F"", ""CHAIN:G""]" 1 Ki Ki = = 4500 (3900–5600) nM 4500.0 [] unit_conversion 5.346787486224656 success True biochemical_inhibition In vitro SARS-CoV-2 Mpro inhibition assay; Table 1 reports Ki with 95% confidence interval. 3 Table 1 prints the Calpeptin SARS-CoV-2 Mpro Ki as 4500 nM (3900–5600). The paper describes the activated S-Calpeptin-derived bound form as desulfonated Calpeptin, and Table 2 maps 7Z3U to Mpro with activated S-Calpeptin. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z3U\7Z3U_metadata.json point structures/7Z3U/7z3u_protein.pdb structures/7Z3U/7z3u_pocket.pdb structures/7Z3U/7z3u_ligand.pdb structures/7Z3U/7z3u_ligand.cif structures/7Z3U/7z3u_complex.pdb structures/7Z3U/7z3u_complex.cif 7Z4S extended SARS-CoV-2 Mpro SARS-CoV-2 Na Na GM4 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 5.2 nM 5.2 [] unit_conversion 8.2839966563652 success True direct_binding Surface plasmon resonance (SPR) binding affinity measurement. 3 Table 1 reports GM4 K_D = 5.2 nM; the text states GM1–GM7 binding affinities to Mpro were evaluated by SPR. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7Z4S\7Z4S_metadata.json point structures/7Z4S/7z4s_protein.pdb structures/7Z4S/7z4s_pocket.pdb structures/7Z4S/7z4s_ligand.pdb structures/7Z4S/7z4s_ligand.cif structures/7Z4S/7z4s_complex.pdb structures/7Z4S/7z4s_complex.cif 7Z5U classic Peptidase domain of collagenase G (ColG-PD) Clostridium histolyticum Peptidase domain of collagenase G Na Compound 27 "[""IFW""]" 1 Ki Ki = = 11.6 ± 0.4 μM 11600.0 [] unit_conversion 4.935542010773082 success True biochemical_inhibition In vitro FRET-based proteolytic inhibition assay; Table 4 reports inhibition constants against bacterial collagenases. 9 Table 4 lists compound 27 against C. histolyticum ColG-PD with Ki = 11.6 ± 0.4 μM. Figure 4 maps compound 27 in ColG-PD to PDB 7Z5U. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z5U\7Z5U_metadata.json point structures/7Z5U/7z5u_protein.pdb structures/7Z5U/7z5u_pocket.pdb structures/7Z5U/7z5u_ligand.sdf structures/7Z5U/7z5u_ligand.pdb structures/7Z5U/7z5u_ligand.cif structures/7Z5U/7z5u_complex.pdb structures/7Z5U/7z5u_complex.cif 7Z6C classic human dihydroorotate dehydrogenase (hDHODH) human N-terminally truncated hDHODH residues 31-395, expressed as an N-terminal GST fusion Na compound 4: 2-Hydroxy-N-(2-isopropyl-5-methyl-4-phenoxyphenyl)pyrazolo[1,5-a]pyridine-3-carboxamide "[""IEQ""]" 1 IC50 IC50 = = 0.0072 ± 0.0009 µM 7.2 [] unit_conversion 8.142667503568731 success True biochemical_inhibition In vitro recombinant hDHODH inhibition assay; DCPIP reduction monitored at 650 nm in a DHO/coenzyme Q10 reaction system. 4 Table 1 reports compound 4 hDHODH IC50 = 0.0072 ± 0.0009 µM; the surrounding Results text identifies compound 4 as the series' most potent hDHODH inhibitor. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z6C\7Z6C_metadata.json point structures/7Z6C/7z6c_protein.pdb structures/7Z6C/7z6c_pocket.pdb structures/7Z6C/7z6c_ligand.sdf structures/7Z6C/7z6c_ligand.pdb structures/7Z6C/7z6c_ligand.cif structures/7Z6C/7z6c_complex.pdb structures/7Z6C/7z6c_complex.cif 7Z6Z classic human angiotensin-1 converting enzyme human minimally glycosylated truncated N-domain (N389) Na fosinoprilat "[""KS8""]" 1 Ki Ki = = 4.11 ± 0.38 nM 4.11 [] unit_conversion 8.386158178123932 success True biochemical_inhibition Fosinoprilat inhibition characterised by inhibitory binding constant (Ki); assay methods use purified truncated human ACE domains and Z-FHL substrate. 3 “Fosinoprilat displayed low nanomolar inhibition of nACE (Ki = 4.11 ± 0.38 nM)” auto_single_measurement only accepted activity measurement [1] 1 structures\7Z6Z\7Z6Z_metadata.json point structures/7Z6Z/7z6z_protein.pdb structures/7Z6Z/7z6z_pocket.pdb structures/7Z6Z/7z6z_ligand.sdf structures/7Z6Z/7z6z_ligand.pdb structures/7Z6Z/7z6z_ligand.cif structures/7Z6Z/7z6z_complex.pdb structures/7Z6Z/7z6z_complex.cif 7Z70 classic human angiotensin-1 converting enzyme human truncated C-domain (g13), Ser-1 to Pro-633 Na fosinoprilat "[""KS8""]" 1 Ki Ki = = 0.15 ± 0.01 nM 0.15 [] unit_conversion 9.823908740944319 success True biochemical_inhibition Fosinoprilat inhibition characterised by inhibitory binding constant (Ki); assay methods use purified truncated human ACE domains and Z-FHL substrate. 3 “cACE (Ki = 0.15 ± 0.01 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\7Z70\7Z70_metadata.json point structures/7Z70/7z70_protein.pdb structures/7Z70/7z70_pocket.pdb structures/7Z70/7z70_ligand.sdf structures/7Z70/7z70_ligand.pdb structures/7Z70/7z70_ligand.cif structures/7Z70/7z70_complex.pdb structures/7Z70/7z70_complex.cif 7Z8O extended SARS-CoV-2 S RBD SARS-CoV-2 soluble spike receptor-binding domain (sRBD) Na E2 "[""CHAIN:B""]" 1 Kd Kd = = 650 nM 650.0 [] unit_conversion 6.187086643357144 success True direct_binding Surface plasmon resonance binding of E2 Bicycle to S1-RBD; Figure 1c matrix reports geometric-mean KD values. 3 Figure 1c reports E2 binding to S1-RBD at 650 nM; the caption states that geometric-mean KD values are indicated. auto_single_measurement only accepted activity measurement [1] 1 structures\7Z8O\7Z8O_metadata.json point structures/7Z8O/7z8o_protein.pdb structures/7Z8O/7z8o_pocket.pdb structures/7Z8O/7z8o_ligand.pdb structures/7Z8O/7z8o_ligand.cif structures/7Z8O/7z8o_complex.pdb structures/7Z8O/7z8o_complex.cif 7ZCZ classic aspartate transcarbamoylase (PfATC) Plasmodium falciparum truncated Na Fragment A; 1-(4-chlorophenyl)methanamine "[""C2B""]" 1 IC50 IC50 = = 10 µM 10000.0 [] unit_conversion 5.0 success True biochemical_inhibition In vitro enzyme assay against PfATC (50 nM, n = 3); paper maps Fragment A to PDB 7ZCZ. 2 “Enzymatic assays indicated an IC50 for these compounds of 10, 125, 150, and 145 μM, respectively”; Figure 1 caption maps 7ZCZ to Fragment A. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZCZ\7ZCZ_metadata.json point structures/7ZCZ/7zcz_protein.pdb structures/7ZCZ/7zcz_pocket.pdb structures/7ZCZ/7zcz_ligand.sdf structures/7ZCZ/7zcz_ligand.pdb structures/7ZCZ/7zcz_ligand.cif structures/7ZCZ/7zcz_complex.pdb structures/7ZCZ/7zcz_complex.cif 7ZEA classic aspartate transcarbamoylase (PfATC) Plasmodium falciparum truncated Na Fragment B; O-benzylhydroxylamine "[""OBZ""]" 1 IC50 IC50 = = 125 µM 125000.0 [] unit_conversion 3.9030899869919438 success True biochemical_inhibition In vitro enzyme assay against PfATC (50 nM, n = 3); paper maps Fragment B to PDB 7ZEA. 2 “Enzymatic assays indicated an IC50 for these compounds of 10, 125, 150, and 145 μM, respectively”; Figure 1 caption maps 7ZEA to Fragment B. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZEA\7ZEA_metadata.json point structures/7ZEA/7zea_protein.pdb structures/7ZEA/7zea_pocket.pdb structures/7ZEA/7zea_ligand.sdf structures/7ZEA/7zea_ligand.pdb structures/7ZEA/7zea_ligand.cif structures/7ZEA/7zea_complex.pdb structures/7ZEA/7zea_complex.cif 7ZED extended E. coli LptA E. coli LptAm, monomeric N-terminal truncated LptA Q62L compound 7 "[""CHAIN:B""]" 1 Ki Ki = = 17.2 ± 3.1 nM 17.2 [] unit_conversion 7.764471553092451 success True direct_binding Fluorescence-polarization direct binding assay; LptAmQ62L–compound 7 binary interaction. 4 “K_i = 17.2 ± 3.1 nM for LptAmQ62L.” The paper maps E. coli LptAmQ62L-7 to 7ZED. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZED\7ZED_metadata.json point structures/7ZED/7zed_protein.pdb structures/7ZED/7zed_pocket.pdb structures/7ZED/7zed_ligand.pdb structures/7ZED/7zed_ligand.cif structures/7ZED/7zed_complex.pdb structures/7ZED/7zed_complex.cif 7ZEG classic Human cytosolic 5' nucleotidase IIIB human Full-length residues 1-300; expressed with an N-terminal His6-Sumo tag, which was cleaved before crystallization Na 3,4-diF-Bn7GMP (compound 5d) "[""IOO""]" 1 IC50 IC50 = = 2.5 ± 0.2 µM 2500.0 [] unit_conversion 5.6020599913279625 success True biochemical_inhibition Malachite Green Phosphate assay; inhibition of m7GMP dephosphorylation by recombinant cN-IIIB. IC50 determined using a 12-point inhibitor dilution series. 8 Table 1 reports compound 5d IC50 ± SEM against cN-IIIB as 2.5 ± 0.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZEG\7ZEG_metadata.json point structures/7ZEG/7zeg_protein.pdb structures/7ZEG/7zeg_pocket.pdb structures/7ZEG/7zeg_ligand.sdf structures/7ZEG/7zeg_ligand.pdb structures/7ZEG/7zeg_ligand.cif structures/7ZEG/7zeg_complex.pdb structures/7ZEG/7zeg_complex.cif 7ZEZ extended Cyclophilin 33 (Cyp33); mixed-lineage leukemia 1 (MLL1) human Cyp33-RRMdelta alpha; structured residues 5-84, full chain A residues 3-90; MLL1-PHD3 residues 1568-1625, full chain B residues 1564-1627; H3K4me3 peptide residues 1-7, full chain C residues 1-13 Na H3K4me3 "[""CHAIN:D""]" 1 Kd Kd = = 24 μM 24000.0 [] unit_conversion 4.619788758288394 success True direct_binding ITC measurement of H3K4me3 binding to the Cyp33-RRMΔα/MLL1-PHD3 complex. 11 “We therefore measured the affinity of H3K4me3 to Cyp33 RRMΔα/MLL1 PHD3, which resulted in an unexpectedly higher affinity with a Kd value of 24 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7ZEZ\7ZEZ_metadata.json point structures/7ZEZ/7zez_protein.pdb structures/7ZEZ/7zez_pocket.pdb structures/7ZEZ/7zez_ligand.pdb structures/7ZEZ/7zez_ligand.cif structures/7ZEZ/7zez_complex.pdb structures/7ZEZ/7zez_complex.cif 7ZG9 classic Sec14p Na His8-Sec14 (octahistidine-tagged Sec14) Na himbacine "[""KO0""]" 1 IC50 IC50 = = 1.2 µM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition In vitro PtdIns-transfer activity inhibition assay. 2 “himbacine (IC50 = 1.2 µM)” among potent inhibitors of PtdIns transfer activity in vitro. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZG9\7ZG9_metadata.json point structures/7ZG9/7zg9_protein.pdb structures/7ZG9/7zg9_pocket.pdb structures/7ZG9/7zg9_ligand.sdf structures/7ZG9/7zg9_ligand.pdb structures/7ZG9/7zg9_ligand.cif structures/7ZG9/7zg9_complex.pdb structures/7ZG9/7zg9_complex.cif 7ZGC classic Sec14p Na His8-Sec14 (octahistidine-tagged Sec14) Na NPPM481 "[""IUO""]" 1 IC50 IC50 = = 0.2 µM 200.0 [] unit_conversion 6.698970004336019 success True biochemical_inhibition In vitro PtdIns-transfer activity inhibition assay. 2 “NPPM481 (IC50 = 0.2 µM)” among potent inhibitors of PtdIns transfer activity in vitro. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZGC\7ZGC_metadata.json point structures/7ZGC/7zgc_protein.pdb structures/7ZGC/7zgc_pocket.pdb structures/7ZGC/7zgc_ligand.sdf structures/7ZGC/7zgc_ligand.pdb structures/7ZGC/7zgc_ligand.cif structures/7ZGC/7zgc_complex.pdb structures/7ZGC/7zgc_complex.cif 7ZGD classic Sec14p Na His8-Sec14 (octahistidine-tagged Sec14) Na NPPM244 "[""IUC""]" 1 IC50 IC50 = = 0.1 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition In vitro PtdIns-transfer activity inhibition assay. 2 “NPPM244 (IC50 = 0.1 µM)” among potent inhibitors of PtdIns transfer activity in vitro. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZGD\7ZGD_metadata.json point structures/7ZGD/7zgd_protein.pdb structures/7ZGD/7zgd_pocket.pdb structures/7ZGD/7zgd_ligand.sdf structures/7ZGD/7zgd_ligand.pdb structures/7ZGD/7zgd_ligand.cif structures/7ZGD/7zgd_complex.pdb structures/7ZGD/7zgd_complex.cif 7ZGL classic CYP125A1 (Rv3545c) Mycobacterium tuberculosis N-terminally truncated CYP125A1 residues 18-433, pET21a construct with TEV-cleavable Twin-Strep/hexa-histidine tag; tag-free protein used for crystallography Na 5j "[""EIQ""]" 1 Kd Kd = = 0.27 ± 0.02 µM 270.0 [] unit_conversion 6.568636235841012 success True direct_binding Optical titration; Table 1 binding value for compound 5j. 5 Table 1 reports compound 5j K_D = 0.27 ± 0.02 µM for CYP125. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7ZGL\7ZGL_metadata.json point structures/7ZGL/7zgl_protein.pdb structures/7ZGL/7zgl_pocket.pdb structures/7ZGL/7zgl_ligand.sdf structures/7ZGL/7zgl_ligand.pdb structures/7ZGL/7zgl_ligand.cif structures/7ZGL/7zgl_complex.pdb structures/7ZGL/7zgl_complex.cif 7ZHF classic SaGPN (Saci_1281), GPN-loop GTPase Sulfolobus acidocaldarius residues Y2-A240; N-terminal His10 tag (MHHHHHHHHHHLELFGPGS) Na GppNHp "[""GNP""]" 1 Kd Kd = = 22.0 nM 22.0 [] unit_conversion 7.657577319177793 success True direct_binding Isothermal titration calorimetry at 65°C with purified SaGPN; GppNHp titration. 8 Figure 4D reports “K_D = 22.0 nM” for GppNHp at 65°C. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZHF\7ZHF_metadata.json point structures/7ZHF/7zhf_protein.pdb structures/7ZHF/7zhf_pocket.pdb structures/7ZHF/7zhf_ligand.sdf structures/7ZHF/7zhf_ligand.pdb structures/7ZHF/7zhf_ligand.cif structures/7ZHF/7zhf_complex.pdb structures/7ZHF/7zhf_complex.cif 7ZHI classic aspartate transcarbamoylase (PfATC) Plasmodium falciparum truncated Na Fragment D; indole "[""IND""]" 1 IC50 IC50 = = 145 µM 145000.0 [] unit_conversion 3.8386319977650247 success True biochemical_inhibition In vitro enzyme assay against PfATC (50 nM, n = 3); paper maps Fragment D to PDB 7ZHI. 2 “Enzymatic assays indicated an IC50 for these compounds of 10, 125, 150, and 145 μM, respectively”; Figure 1 caption maps 7ZHI to Fragment D. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZHI\7ZHI_metadata.json point structures/7ZHI/7zhi_protein.pdb structures/7ZHI/7zhi_pocket.pdb structures/7ZHI/7zhi_ligand.sdf structures/7ZHI/7zhi_ligand.pdb structures/7ZHI/7zhi_ligand.cif structures/7ZHI/7zhi_complex.pdb structures/7ZHI/7zhi_complex.cif 7ZIC classic CYP125A1 (Rv3545c) Mycobacterium tuberculosis N-terminally truncated CYP125A1 residues 18-433, pET21a construct with TEV-cleavable Twin-Strep/hexa-histidine tag; tag-free protein used for crystallography Na 5m "[""5YG""]" 1 Kd Kd = = 0.040 ± 0.041 µM 40.0 [] unit_conversion 7.3979400086720375 success True direct_binding Optical titration; Table 1 binding value for compound 5m. 5 Table 1 reports compound 5m K_D = 0.040 ± 0.041 µM for CYP125. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7ZIC\7ZIC_metadata.json point structures/7ZIC/7zic_protein.pdb structures/7ZIC/7zic_pocket.pdb structures/7ZIC/7zic_ligand.sdf structures/7ZIC/7zic_ligand.pdb structures/7ZIC/7zic_ligand.cif structures/7ZIC/7zic_complex.pdb structures/7ZIC/7zic_complex.cif 7ZIY classic HaloTag7 Na Na Na TMR-T5 "[""IYI""]" 1 Kd Kd = = 166 nM 166.0 [] unit_conversion 6.779891911959945 success True direct_binding Fluorescence-polarization binding assay; Table 1 reports KD 166 nM (95% CI 150–185 nM) for the HaloTag7/TMR-T5 pair. 3 Table 1 lists TMR-T5 with HaloTag7: KD 166 (150–185) nM. The text identifies the TMR-T5/HaloTag7 crystal structure as PDB-ID 7ZJY; the supplied 7ZIY title uniquely resolves this as the stated accession transposition. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZIY\7ZIY_metadata.json point structures/7ZIY/7ziy_protein.pdb structures/7ZIY/7ziy_pocket.pdb structures/7ZIY/7ziy_ligand.sdf structures/7ZIY/7ziy_ligand.pdb structures/7ZIY/7ziy_ligand.cif structures/7ZIY/7ziy_complex.pdb structures/7ZIY/7ziy_complex.cif 7ZJ0 classic HaloTag7 Na Na Na TMR-S5 "[""IYO""]" 1 Kd Kd = = 311 nM 311.0 [] unit_conversion 6.507239610973162 success True direct_binding Fluorescence-polarization binding assay; Table 1 reports KD 311 nM (95% CI 275–351 nM) for the HaloTag7/TMR-S5 pair. 3 Table 1 lists TMR-S5 with HaloTag7: KD 311 (275–351) nM. The preceding text identifies the HaloTag7/TMR-S5 crystal structure as PDB-ID 7ZJ0. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZJ0\7ZJ0_metadata.json point structures/7ZJ0/7zj0_protein.pdb structures/7ZJ0/7zj0_pocket.pdb structures/7ZJ0/7zj0_ligand.sdf structures/7ZJ0/7zj0_ligand.pdb structures/7ZJ0/7zj0_ligand.cif structures/7ZJ0/7zj0_complex.pdb structures/7ZJ0/7zj0_complex.cif 7ZJP classic TEAD1 human residues 209-426 Na MSC-4106; compound 23 "[""JJU""]" 1 Kd Kd = = 0.12 µM 120.0 [] unit_conversion 6.920818753952375 success True direct_binding Surface plasmon resonance (SPR) direct-binding measurement reported for MSC-4106 against TEAD1. 10 Table 7, “PhysChem, ADME, and PK Profile of MSC-4106”, reports SPR K_D [µM] values; TEAD1 = 0.12. The text identifies optimized derivative 23 as MSC-4106. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZJP\7ZJP_metadata.json point structures/7ZJP/7zjp_protein.pdb structures/7ZJP/7zjp_pocket.pdb structures/7ZJP/7zjp_ligand.sdf structures/7ZJP/7zjp_ligand.pdb structures/7ZJP/7zjp_ligand.cif structures/7ZJP/7zjp_complex.pdb structures/7ZJP/7zjp_complex.cif 7ZK3 classic mouse TMEM16A (mTMEM16A(ac)) mouse Na wild-type 1PBC "[""JRF""]" 2 Kd Kd = = 3.6 ± 0.29 µM 3600.0 [] unit_conversion 5.443697499232712 success True biochemical_inhibition Apparent affinity from a global open-channel-block model fitted to concentration-response data; zero mV. 3 “a global fit to an open-channel block mechanism … with estimated parameters Kd 1PBC = 3.6 ± 0.29 µM at zero mV and apparent valence δb = 0.27 ± 0.025.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7ZK3\7ZK3_metadata.json point structures/7ZK3/7zk3_protein.pdb structures/7ZK3/7zk3_pocket.pdb structures/7ZK3/7zk3_ligand.sdf structures/7ZK3/7zk3_ligand.pdb structures/7ZK3/7zk3_ligand.cif structures/7ZK3/7zk3_complex.pdb structures/7ZK3/7zk3_complex.cif 7ZKS classic SRPK1 Na Na Na 5i "[""IXQ""]" 1 IC50 IC50 = = 0.032 μM 32.0 [] unit_conversion 7.494850021680094 success True biochemical_inhibition Biochemical kinase assay with radioactive assay format. 4 Table 1 reports compound 5i with SRPK1 IC50 = 0.032 μM; Figure 5 identifies SRPK1 PDB 7ZKS in complex with 5i. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZKS\7ZKS_metadata.json point structures/7ZKS/7zks_protein.pdb structures/7ZKS/7zks_pocket.pdb structures/7ZKS/7zks_ligand.sdf structures/7ZKS/7zks_ligand.pdb structures/7ZKS/7zks_ligand.cif structures/7ZKS/7zks_complex.pdb structures/7ZKS/7zks_complex.cif 7ZKT classic Moss spermine/spermidine N-acetyl transferase (PpSSAT) Physcomitrium patens 214-aa recombinant PpSSAT with an N-terminal His-tag (pET28b construct) Na lysine (Lys) "[""LYS""]" 1 Kd Kd = = 2.3 ± 0.2 mM 2300000.0 [] unit_conversion 2.638272163982407 success True direct_binding Microscale thermophoresis, PpSSAT–CoA complex. 6 Table 3 reports PpSSAT Lys K_D[CoA] = 2.3 ± 0.2 mM; its note defines the CoA-bound enzyme condition. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZKT\7ZKT_metadata.json point structures/7ZKT/7zkt_protein.pdb structures/7ZKT/7zkt_pocket.pdb structures/7ZKT/7zkt_ligand.sdf structures/7ZKT/7zkt_ligand.pdb structures/7ZKT/7zkt_ligand.cif structures/7ZKT/7zkt_complex.pdb structures/7ZKT/7zkt_complex.cif 7ZKX classic SRPK2 Na Na Na 5i "[""IXQ""]" 1 IC50 IC50 = = 0.67 μM 670.0 [] unit_conversion 6.173925197299173 success True biochemical_inhibition Biochemical kinase assay with radioactive assay format. 4 Table 1 reports compound 5i with SRPK2 IC50 = 0.67 μM; Figure 5 identifies SRPK2 PDB 7ZKX in complex with 5i. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZKX\7ZKX_metadata.json point structures/7ZKX/7zkx_protein.pdb structures/7ZKX/7zkx_pocket.pdb structures/7ZKX/7zkx_ligand.sdf structures/7ZKX/7zkx_ligand.pdb structures/7ZKX/7zkx_ligand.cif structures/7ZKX/7zkx_complex.pdb structures/7ZKX/7zkx_complex.cif 7ZLC classic Unlinked NS2B/NS3 protease Zika virus Unlinked NS2B/NS3 protease Na MI-2224; inhibitor 3 "[""IXU""]" 2 Kd Kd = = 2700 ± 90 nM 2700.0 [] unit_conversion 5.568636235841012 success True direct_binding Isothermal titration calorimetry (ITC); Table 1 identifies inhibitor 3 Kd. The paper maps PDB 7ZLC to inhibitor 3. 2 Table 1 reports inhibitor 3: Kd = 2700 ± 90 nM; page 9 maps deposited PDB 7ZLC to compound 3. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7ZLC\7ZLC_metadata.json point structures/7ZLC/7zlc_protein.pdb structures/7ZLC/7zlc_pocket.pdb structures/7ZLC/7zlc_ligand.sdf structures/7ZLC/7zlc_ligand.pdb structures/7ZLC/7zlc_ligand.cif structures/7ZLC/7zlc_complex.pdb structures/7ZLC/7zlc_complex.cif 7ZLD classic Unlinked NS2B/NS3 protease Zika virus Unlinked NS2B/NS3 protease Na MI-2223; inhibitor 2 "[""IY3""]" 2 Kd Kd = = 2120 ± 440 nM 2120.0 [] unit_conversion 5.673664139071249 success True direct_binding Isothermal titration calorimetry (ITC); Table 1 identifies inhibitor 2 Kd. The paper maps PDB 7ZLD to inhibitor 2. 2 Table 1 reports inhibitor 2: Kd = 2120 ± 440 nM; page 9 maps deposited PDB 7ZLD to compound 2. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7ZLD\7ZLD_metadata.json point structures/7ZLD/7zld_protein.pdb structures/7ZLD/7zld_pocket.pdb structures/7ZLD/7zld_ligand.sdf structures/7ZLD/7zld_ligand.pdb structures/7ZLD/7zld_ligand.cif structures/7ZLD/7zld_complex.pdb structures/7ZLD/7zld_complex.cif 7ZLL classic Catalytic domain of UDP-Glucose Glycoprotein Glucosyltransferase (CtUGGT_GT24) Chaetomium thermophilum CtUGGT_GT24 catalytic domain without its C-terminal ER-retrieval motif Na 5-[(morpholin-4-yl)methyl]quinolin-8-ol (5M-8OH-Q) "[""JM3""]" 1 Kd Kd = = 47 ± 2 μM 47000.0 [] unit_conversion 4.327902142064283 success True direct_binding Ligand-enhanced fluorescence (LEF) measurement of N-NHS-RED-labeled CtUGGT_GT24 binding to 5M-8OH-Q in vitro. 6 “The equilibrium dissociation constant of the N-NHS-RED-CtUGGT_GT24:5M-8OH-Q complex is estimated as Kd^5M-8OH-Q = 47 ± 2 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\7ZLL\7ZLL_metadata.json point structures/7ZLL/7zll_protein.pdb structures/7ZLL/7zll_pocket.pdb structures/7ZLL/7zll_ligand.sdf structures/7ZLL/7zll_ligand.pdb structures/7ZLL/7zll_ligand.cif structures/7ZLL/7zll_complex.pdb structures/7ZLL/7zll_complex.cif 7ZMI classic Unlinked NS2B/NS3 protease Zika virus Unlinked NS2B/NS3 protease Na MI-2113; inhibitor 4 "[""IXJ""]" 2 Kd Kd = = 8220 ± 250 nM 8220.0 [] unit_conversion 5.0851281824599495 success True direct_binding Isothermal titration calorimetry (ITC); Table 1 identifies inhibitor 4 Kd. The paper maps PDB 7ZMI to inhibitor 4. 2 Table 1 reports inhibitor 4: Kd = 8220 ± 250 nM; page 9 maps deposited PDB 7ZMI to compound 4. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7ZMI\7ZMI_metadata.json point structures/7ZMI/7zmi_protein.pdb structures/7ZMI/7zmi_pocket.pdb structures/7ZMI/7zmi_ligand.sdf structures/7ZMI/7zmi_ligand.pdb structures/7ZMI/7zmi_ligand.cif structures/7ZMI/7zmi_complex.pdb structures/7ZMI/7zmi_complex.cif 7ZP2 classic aspartate transcarbamoylase (PfATC) Plasmodium falciparum truncated Na BDA-04 "[""EJG""]" 2 Kd Kd = = 66.3 nM 66.3 [] unit_conversion 7.178486471595226 success True direct_binding Microscale thermophoresis binding assay with PfATC (50 nM, n = 3); Figure 3E. 4 Figure 3E labels “Kd = 66.3 nM”; caption: “MST result showing the binding affinity of PfATC (50 nM, n = 3) with BDA-04.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7ZP2\7ZP2_metadata.json point structures/7ZP2/7zp2_protein.pdb structures/7ZP2/7zp2_pocket.pdb structures/7ZP2/7zp2_ligand.sdf structures/7ZP2/7zp2_ligand.pdb structures/7ZP2/7zp2_ligand.cif structures/7ZP2/7zp2_complex.pdb structures/7ZP2/7zp2_complex.cif 7ZPY extended Influenza polymerase A PA subunit (CPA) Na CPA residues 257-716 Na PB1-19 "[""CHAIN:B""]" 2 Kd Kd = = 1.7 ± 0.3 nM 1.7 [] unit_conversion 8.769551078621726 success True direct_binding Isothermal titration calorimetry of PB1-19 binding to CPA at 25 °C; Fig. 3B used a c-value of 440. 4 The text reports that the dissociation constant of PB1-19 binding to CPA was estimated as 1.7 nM, and Fig. 3B prints Kd = 1.7 ± 0.3 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\7ZPY\7ZPY_metadata.json point structures/7ZPY/7zpy_protein.pdb structures/7ZPY/7zpy_pocket.pdb structures/7ZPY/7zpy_ligand.pdb structures/7ZPY/7zpy_ligand.cif structures/7ZPY/7zpy_complex.pdb structures/7ZPY/7zpy_complex.cif 7ZQX classic Human galectin-3 Human C-terminal domain (galectin-3C) Na 11d (GB1211) "[""JU0""]" 1 Kd Kd = = 0.025 ± 0.0017 µM 25.0 [] unit_conversion 7.6020599913279625 success True direct_binding Fluorescence-polarization galectin-3 binding assay; Table 3. 5 Table 3 reports galectin-3 Kd for 11d as 0.025 ± 0.0017 µM; footnote states Kd was determined by fluorescence polarization. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZQX\7ZQX_metadata.json point structures/7ZQX/7zqx_protein.pdb structures/7ZQX/7zqx_pocket.pdb structures/7ZQX/7zqx_ligand.sdf structures/7ZQX/7zqx_ligand.pdb structures/7ZQX/7zqx_ligand.cif structures/7ZQX/7zqx_complex.pdb structures/7ZQX/7zqx_complex.cif 7ZRP extended calmodulin (CaM) Homo sapiens CaM-WT WT (wild type) CaMKII delta residues 294-315 peptide "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.052 ± 0.008 µM 52.0 [] unit_conversion 7.2839966563652006 success True direct_binding Isothermal titration calorimetry of Ca2+/CaM-WT with CaMKIIδ294–315 peptide; 5 mM CaCl2. 3 ITC determined the dissociation constant of Ca2+/CaM for CaMKIIδ294–315 as 0.052 ± 0.008 µM (n = 8); Figure 2 caption identifies CaM–CaMKIIδ294–315 binding. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZRP\7ZRP_metadata.json point structures/7ZRP/7zrp_protein.pdb structures/7ZRP/7zrp_pocket.pdb structures/7ZRP/7zrp_ligand.pdb structures/7ZRP/7zrp_ligand.cif structures/7ZRP/7zrp_complex.pdb structures/7ZRP/7zrp_complex.cif 7ZRQ extended calmodulin (CaM) Homo sapiens CaM-E140G E140G CaMKII delta residues 294-315 peptide "[""CHAIN:B""]" 1 Kd Kd = = 0.097 ± 0.008 µM 97.0 [] unit_conversion 7.013228265733755 success True direct_binding Isothermal titration calorimetry of Ca2+/CaM-E140G with CaMKIIδ294–315 peptide; 5 mM CaCl2. 3 ITC determined the dissociation constant for the E140G variant as 0.097 ± 0.008 µM (n = 5) for CaMKIIδ294–315; Figure 2 caption identifies CaM–CaMKIIδ294–315 binding. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZRQ\7ZRQ_metadata.json point structures/7ZRQ/7zrq_protein.pdb structures/7ZRQ/7zrq_pocket.pdb structures/7ZRQ/7zrq_ligand.pdb structures/7ZRQ/7zrq_ligand.cif structures/7ZRQ/7zrq_complex.pdb structures/7ZRQ/7zrq_complex.cif 7ZTK classic NME1 mouse Na Na CoA "[""COA""]" 1 Kd Kd = = 17.5 ± 5.9 μM 17500.0 [] unit_conversion 4.756961951313706 success True direct_binding Isothermal titration calorimetry of CoA binding to recombinant murine NME1; data fit using a single-site binding model. 4 Figure 2E reports an ITC profile for CoA binding by NME1 with Kd = 17.5 ± 5.9 μM; the text identifies this as the NME1:CoA interaction. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZTK\7ZTK_metadata.json point structures/7ZTK/7ztk_protein.pdb structures/7ZTK/7ztk_pocket.pdb structures/7ZTK/7ztk_ligand.sdf structures/7ZTK/7ztk_ligand.pdb structures/7ZTK/7ztk_ligand.cif structures/7ZTK/7ztk_complex.pdb structures/7ZTK/7ztk_complex.cif 7ZUP classic PRMT5:MEP50 complex human Na Na compound 18 (fragment hit 3 analog) "[""JYX""]" 1 Kd Kd = = 28.0 µM 28000.0 [] unit_conversion 4.552841968657781 success True direct_binding SPR PRMT5/MTA direct-binding K_D determination. 8 The text reports compound 18 PRMT5/MTA K_D = 28.0 µM and identifies its PRMT5/MTA X-ray co-crystal structure as PDB 7ZUP. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZUP\7ZUP_metadata.json point structures/7ZUP/7zup_protein.pdb structures/7ZUP/7zup_pocket.pdb structures/7ZUP/7zup_ligand.sdf structures/7ZUP/7zup_ligand.pdb structures/7ZUP/7zup_ligand.cif structures/7ZUP/7zup_complex.pdb structures/7ZUP/7zup_complex.cif 7ZUY extended PRMT5:MEP50 complex human Na Na compound 26 "[""UNL""]" 1 Kd Kd = = 0.179 µM 179.0 [] unit_conversion 6.747146969020107 success True direct_binding SPR PRMT5/MTA direct-binding K_D determination. 10 The text reports compound 26 PRMT5/MTA K_D = 0.179 µM, and Fig. 12 identifies its PRMT5/MTA X-ray co-crystal structure as PDB 7ZUY. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZUY\7ZUY_metadata.json point structures/7ZUY/7zuy_protein.pdb structures/7ZUY/7zuy_pocket.pdb structures/7ZUY/7zuy_ligand.pdb structures/7ZUY/7zuy_ligand.cif structures/7ZUY/7zuy_complex.pdb structures/7ZUY/7zuy_complex.cif 7ZV2 extended PRMT5:MEP50 complex human Na Na compound 22 "[""UNL""]" 1 Kd Kd = = 1.48 µM 1480.0 [] unit_conversion 5.8297382846050425 success True direct_binding SPR PRMT5/MTA direct-binding K_D determination. 10 The text reports compound 22 PRMT5/MTA K_D = 1.48 µM, and Fig. 12 identifies its PRMT5/MTA X-ray co-crystal structure as PDB 7ZV2. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZV2\7ZV2_metadata.json point structures/7ZV2/7zv2_protein.pdb structures/7ZV2/7zv2_pocket.pdb structures/7ZV2/7zv2_ligand.pdb structures/7ZV2/7zv2_ligand.cif structures/7ZV2/7zv2_complex.pdb structures/7ZV2/7zv2_complex.cif 7ZVU extended PRMT5:MEP50 complex human Na Na compound 25 "[""UNL""]" 1 Kd Kd = = 0.205 µM 205.0 [] unit_conversion 6.688246138944246 success True direct_binding SPR PRMT5/MTA direct-binding K_D determination. 10 The text reports compound 25 PRMT5/MTA K_D = 0.205 µM, and Fig. 12 identifies its PRMT5/MTA X-ray co-crystal structure as PDB 7ZVU. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZVU\7ZVU_metadata.json point structures/7ZVU/7zvu_protein.pdb structures/7ZVU/7zvu_pocket.pdb structures/7ZVU/7zvu_ligand.pdb structures/7ZVU/7zvu_ligand.cif structures/7ZVU/7zvu_complex.pdb structures/7ZVU/7zvu_complex.cif 7ZW3 extended human MAO B human Na Na compound 19; (Z)-N-benzyl-1-(8-hydroxyquinolin-2-yl)methanimine oxide "[""AI0""]" 2 Ki Ki = = 355.6 ± 72.2 nmol/L 355.6 [] unit_conversion 6.449038247701823 success True biochemical_inhibition Direct MMTB steady-state kinetic assay on purified recombinant hMAO-B; competitive-inhibition model. 9 The text states that direct MMTB assay on purified recombinant hMAO-B gave compound 19 Ki = 355.6 ± 72.2 nmol/L. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\7ZW3\7ZW3_metadata.json point structures/7ZW3/7zw3_ligand.sdf structures/7ZW3/7zw3_ligand.cif structures/7ZW3/7zw3_complex.cif 7ZW8 classic cKIT (KIT) Na Na wild-type compound 32; M4205/IDRX-42 "[""K3R""]" 1 IC50 IC50 = = 44 nM 44.0 [] unit_conversion 7.356547323513812 success True biochemical_inhibition Kinase inhibition panel for compound 32; Table 5 reports KIT inhibition. 6 Table 5, “Kinase Inhibition of 32”, lists KIT IC50 = 44 nM; the text identifies 32 as M4205 and describes the wild-type KIT kinase-domain complex (PDB-ID 7ZW8). auto_single_measurement only accepted activity measurement [1] 1 structures\7ZW8\7ZW8_metadata.json point structures/7ZW8/7zw8_protein.pdb structures/7ZW8/7zw8_pocket.pdb structures/7ZW8/7zw8_ligand.sdf structures/7ZW8/7zw8_ligand.pdb structures/7ZW8/7zw8_ligand.cif structures/7ZW8/7zw8_complex.pdb structures/7ZW8/7zw8_complex.cif 7ZWB extended human Carbonic Anhydrase II (hCA II) human Na Na 8a (4-(((2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)thio)benzenesulfonamide) "[""K7P""]" 1 Ki Ki = = 7.5 nM 7.5 [] unit_conversion 8.1249387366083 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay on hCA II. 4 Table 1 reports compound 8a with Ki = 7.5 nM for hCA II; Figure 1 identifies the hCA II/8a crystal complex as PDB 7ZWB. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZWB\7ZWB_metadata.json point structures/7ZWB/7zwb_ligand.sdf structures/7ZWB/7zwb_ligand.cif structures/7ZWB/7zwb_complex.cif 7ZWG classic CK2alpha Na Na Na RO4493940; RO4493940-000 "[""R7W""]" 1 IC50 IC50 = = 67 nM 67.0 [] unit_conversion 7.173925197299173 success True biochemical_inhibition Recombinant kinase activity assay; table reports activity IC50 for CK2 inhibitors. 19 Extended Data Fig. 6 table reports RO4493940-000 activity IC50 of 67 nM for CSNK2A1; the caption identifies recombinant kinase activity assays. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZWG\7ZWG_metadata.json point structures/7ZWG/7zwg_protein.pdb structures/7ZWG/7zwg_pocket.pdb structures/7ZWG/7zwg_ligand.sdf structures/7ZWG/7zwg_ligand.pdb structures/7ZWG/7zwg_ligand.cif structures/7ZWG/7zwg_complex.pdb structures/7ZWG/7zwg_complex.cif 7ZWV classic human BCL6 human BCL6 5-129 product with purification tag removed Na compound 17 "[""KA9""]" 1 Kd Kd = = 49 µM 49000.0 [] unit_conversion 4.309803919971486 success True direct_binding SPR direct binding to the BCL6 BTB domain; Langmuir isotherm. 4 Figure 2C prints “Compound 17: K_D = 49 µM”; page 3 states SPR tested direct binding to the BCL6 BTB domain. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7ZWV\7ZWV_metadata.json point structures/7ZWV/7zwv_protein.pdb structures/7ZWV/7zwv_pocket.pdb structures/7ZWV/7zwv_ligand.sdf structures/7ZWV/7zwv_ligand.pdb structures/7ZWV/7zwv_ligand.cif structures/7ZWV/7zwv_complex.pdb structures/7ZWV/7zwv_complex.cif 7ZWY classic human BCL6 human BCL6 5-129 product with purification tag removed Na compound 21 "[""K6R""]" 1 Kd Kd = = 81 µM 81000.0 [] unit_conversion 4.0915149811213505 success True direct_binding SPR direct binding to the BCL6 BTB domain; Langmuir isotherm. 4 Figure 2C prints “Compound 21: K_D = 81 µM”; page 3 states SPR tested direct binding to the BCL6 BTB domain. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\7ZWY\7ZWY_metadata.json point structures/7ZWY/7zwy_protein.pdb structures/7ZWY/7zwy_pocket.pdb structures/7ZWY/7zwy_ligand.sdf structures/7ZWY/7zwy_ligand.pdb structures/7ZWY/7zwy_ligand.cif structures/7ZWY/7zwy_complex.pdb structures/7ZWY/7zwy_complex.cif 7ZX1 extended DNA polymerase theta (Pol theta) polymerase domain Na Pol theta-PD Delta insert2, residues 1820-2590; expressed as an N-His6-SUMO3 fusion with the tag removed before crystallization Deletion of insert 2 residues 2261-2306, replaced with a single glycine compound 22 (ART558) "[""K8I""]" 1 Kd Kd = = 4.8 nM 4.8 [] unit_conversion 8.318758762624412 success True direct_binding Endpoint TR-FRET direct-binding assay with Tb-labeled Polθ polymerase domain and DNA substrate. 6 Table 5 reports Polθ Kd = 4.8 nM for compound 22. The experimental section describes the Tb-labeled polymerase-domain TR-FRET binding assay and the Polθ-PDΔinsert2 construct. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZX1\7ZX1_metadata.json point structures/7ZX1/7zx1_ligand.sdf structures/7ZX1/7zx1_ligand.cif structures/7ZX1/7zx1_complex.cif 7ZYF classic Insulin-regulated aminopeptidase (IRAP) Na Na Na Compound 32e (alpha-hydroxy-beta-amino-acid-based inhibitor) "[""KFR""]" 1 IC50 IC50 = = 0.0065 µM 6.5 [] unit_conversion 8.187086643357144 success True biochemical_inhibition Fluorogenic enzymatic inhibition assay using recombinant IRAP; Table 1. 5 Table 1 reports compound 32e IC50 = 0.0065 µM against IRAP. Figure 2 identifies the IRAP–32e crystal structure as PDB 7ZYF on page 8. auto_single_measurement only accepted activity measurement [1] 1 structures\7ZYF\7ZYF_metadata.json point structures/7ZYF/7zyf_protein.pdb structures/7ZYF/7zyf_pocket.pdb structures/7ZYF/7zyf_ligand.sdf structures/7ZYF/7zyf_ligand.pdb structures/7ZYF/7zyf_ligand.cif structures/7ZYF/7zyf_complex.pdb structures/7ZYF/7zyf_complex.cif 8A0I classic PtGSTU20 (poplar glutathione transferase U20) Populus trichocarpa untagged recombinant protein Na glutathionylphenylacetophenone (GS-PAP) "[""CNZ""]" 1 Ki Ki = = 5.1 ± 2.1 μM 5100.0 [] unit_conversion 5.292429823902063 success True biochemical_inhibition Inhibition constant determined toward the GSH-conjugation reaction using PITC as substrate; Table 3. 10 Table 3 reports PtGSTU20 GS-PAP Ki = 5.1 ± 2.1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8A0I\8A0I_metadata.json point structures/8A0I/8a0i_protein.pdb structures/8A0I/8a0i_pocket.pdb structures/8A0I/8a0i_ligand.sdf structures/8A0I/8a0i_ligand.pdb structures/8A0I/8a0i_ligand.cif structures/8A0I/8a0i_complex.pdb structures/8A0I/8a0i_complex.cif 8A0O classic PtGSTU20 (poplar glutathione transferase U20) Populus trichocarpa untagged recombinant protein Na galangin "[""KMC""]" 1 Ki Ki = = 43.8 ± 0.6 μM 43800.0 [] unit_conversion 4.3585258894959 success True biochemical_inhibition Inhibition constant determined toward the GSH-conjugation reaction using PITC as substrate; Table 3. 10 Table 3 reports PtGSTU20 galangin Ki = 43.8 ± 0.6 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8A0O\8A0O_metadata.json point structures/8A0O/8a0o_protein.pdb structures/8A0O/8a0o_pocket.pdb structures/8A0O/8a0o_ligand.sdf structures/8A0O/8a0o_ligand.pdb structures/8A0O/8a0o_ligand.cif structures/8A0O/8a0o_complex.pdb structures/8A0O/8a0o_complex.cif 8A0P classic PtGSTU20 (poplar glutathione transferase U20) Populus trichocarpa untagged recombinant protein Na morin "[""MRI""]" 1 Ki Ki = = 16.0 ± 0.9 μM 16000.0 [] unit_conversion 4.795880017344075 success True biochemical_inhibition Inhibition constant determined toward the GSH-conjugation reaction using PITC as substrate; Table 3. 10 Table 3 reports PtGSTU20 morin Ki = 16.0 ± 0.9 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8A0P\8A0P_metadata.json point structures/8A0P/8a0p_protein.pdb structures/8A0P/8a0p_pocket.pdb structures/8A0P/8a0p_ligand.sdf structures/8A0P/8a0p_ligand.pdb structures/8A0P/8a0p_ligand.cif structures/8A0P/8a0p_complex.pdb structures/8A0P/8a0p_complex.cif 8A0Q classic PtGSTU20 (poplar glutathione transferase U20) Populus trichocarpa untagged recombinant protein Na baicalein "[""3WL""]" 1 Ki Ki = = 7.1 ± 0.6 μM 7100.0 [] unit_conversion 5.1487416512809245 success True biochemical_inhibition Inhibition constant determined toward the GSH-conjugation reaction using PITC as substrate; Table 3. 10 Table 3 reports PtGSTU20 baicalein Ki = 7.1 ± 0.6 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8A0Q\8A0Q_metadata.json point structures/8A0Q/8a0q_protein.pdb structures/8A0Q/8a0q_pocket.pdb structures/8A0Q/8a0q_ligand.sdf structures/8A0Q/8a0q_ligand.pdb structures/8A0Q/8a0q_ligand.cif structures/8A0Q/8a0q_complex.pdb structures/8A0Q/8a0q_complex.cif 8A0R classic PtGSTU20 (poplar glutathione transferase U20) Populus trichocarpa untagged recombinant protein Na pinocembrin "[""KML""]" 1 Ki Ki = = 61.2 ± 10.5 μM 61200.0 [] unit_conversion 4.213248577854439 success True biochemical_inhibition Inhibition constant determined toward the GSH-conjugation reaction using PITC as substrate; Table 3. 10 Table 3 reports PtGSTU20 pinocembrin Ki = 61.2 ± 10.5 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8A0R\8A0R_metadata.json point structures/8A0R/8a0r_protein.pdb structures/8A0R/8a0r_pocket.pdb structures/8A0R/8a0r_ligand.sdf structures/8A0R/8a0r_ligand.pdb structures/8A0R/8a0r_ligand.cif structures/8A0R/8a0r_complex.pdb structures/8A0R/8a0r_complex.cif 8A1Q classic HIV-1 integrase Human immunodeficiency virus type 1 (HIV-1) HIV-1 isolate NL4-3 integrase residues 220-288 linked to residues 50-212 via a flexible linker; NTD absent F185K and W243E STP0404 (Pirmitegravir); PIR "[""WBV""]" 1 Kd Kd ~ ~ 5 nM 5.0 [] unit_conversion 8.301029995663981 success True direct_binding Surface plasmon resonance measurement of PIR binding to the engineered CTD-CCD fusion construct. 4 “the affinity of PIR for the CTD-CCD fusion (K_D ≈ 5 nM)” auto_single_measurement only accepted activity measurement [1] 1 structures\8A1Q\8A1Q_metadata.json point structures/8A1Q/8a1q_protein.pdb structures/8A1Q/8a1q_pocket.pdb structures/8A1Q/8a1q_ligand.sdf structures/8A1Q/8a1q_ligand.pdb structures/8A1Q/8a1q_ligand.cif structures/8A1Q/8a1q_complex.pdb structures/8A1Q/8a1q_complex.cif 8A1R classic thioredoxin glutathione reductase Na Na Na compound 9 "[""KW2""]" 1 IC50 IC50 = = 57.5 ± 2.46 μM 57500.0 [] unit_conversion 4.2403321553103694 success True biochemical_inhibition Recombinant S. mansoni TGR biochemical inhibition assay; IC50 determined after 15 min preincubation. 4 Table 1 reports compound 9 S. mansoni TGR IC50 = 57.5 ± 2.46 μM. The table footnote states IC50 values are after 15 min preincubation. The paper maps cryo-EM PDB 8A1R to TGR bound to compound 9. auto_single_measurement only accepted activity measurement [1] 1 structures\8A1R\8A1R_metadata.json point structures/8A1R/8a1r_protein.pdb structures/8A1R/8a1r_pocket.pdb structures/8A1R/8a1r_ligand.sdf structures/8A1R/8a1r_ligand.pdb structures/8A1R/8a1r_ligand.cif structures/8A1R/8a1r_complex.pdb structures/8A1R/8a1r_complex.cif 8A3Q classic human plasma kallikrein human Na Na 14w; Sebetralstat (KVD900) "[""A1J3F""]" 1 Ki Ki = = 3.0 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Competitive, reversible inhibition of PKa. 8 “Sebetralstat, 14w, is a potent, competitive, and reversible inhibitor of PKa (Ki = 3.0 nM)” auto_metric_priority unique highest-priority metric family: Ki [1] 3 structures\8A3Q\8A3Q_metadata.json point structures/8A3Q/8a3q_protein.pdb structures/8A3Q/8a3q_pocket.pdb structures/8A3Q/8a3q_ligand.sdf structures/8A3Q/8a3q_ligand.pdb structures/8A3Q/8a3q_ligand.cif structures/8A3Q/8a3q_complex.pdb structures/8A3Q/8a3q_complex.cif 8A46 classic KEAP1 human Na Na S217879 "[""L5F""]" 1 Kd Kd = = 4.15 nM 4.15 [] unit_conversion 8.381951903287908 success True direct_binding Direct surface plasmon resonance assay. 7 “Binding to KEAP1 Kelch domain was confirmed with a direct surface plasmon resonance assay (Kd = 4.15 nM; Table S1).” Compound 3 is referred to as S217879 throughout the manuscript. auto_single_measurement only accepted activity measurement [1] 1 structures\8A46\8A46_metadata.json point structures/8A46/8a46_protein.pdb structures/8A46/8a46_pocket.pdb structures/8A46/8a46_ligand.sdf structures/8A46/8a46_ligand.pdb structures/8A46/8a46_ligand.cif structures/8A46/8a46_complex.pdb structures/8A46/8a46_complex.cif 8A4D classic 1-deoxy-D-xylulose 5-phosphate synthase Pseudomonas aeruginosa Optimized paDXPS construct with the loop corresponding to residues 206-245 replaced by a six-glycine unit Residues 206-245 replaced by six glycine residues thiamine analog inhibitor (2-{3-[(4-Amino-2-Methylpyrimidin-5-yl)methyl]phenyl}ethanol) "[""26G""]" 1 IC50 IC50 = = 197 µM 197000.0 [] unit_conversion 3.7055337738384067 success True biochemical_inhibition Inhibition assay of paDXPS with the co-crystallized thiamine analog inhibitor. 6 The co-crystallized thiamine analog is named on this page and “showed a half-maximal inhibitory concentration (IC50) of 197 μM for paDXPS”; PDB ID 8A4D is explicitly given for its paDXPS co-crystal structure. auto_single_measurement only accepted activity measurement [1] 1 structures\8A4D\8A4D_metadata.json point structures/8A4D/8a4d_protein.pdb structures/8A4D/8a4d_pocket.pdb structures/8A4D/8a4d_ligand.sdf structures/8A4D/8a4d_ligand.pdb structures/8A4D/8a4d_ligand.cif structures/8A4D/8a4d_complex.pdb structures/8A4D/8a4d_complex.cif 8A4Q classic SARS-CoV-2 Mpro SARS-CoV-2 Na Na 13b-H (12), diastereomer (R,S,S)-13b "[""V9R""]" 1 IC50 IC50 > > 5 µM 5000.0 [] unit_conversion 5.301029995663981 success True biochemical_inhibition FRET-based recombinant Mpro cleavage assay. 3 “Compounds 12 and 13 inhibited SARS-CoV-2 Mpro with IC50 values of >5 μM and 0.12 ± 0.03 μM, respectively.” Compound 12 is 13b-H. auto_single_measurement only accepted activity measurement [1] 1 structures\8A4Q\8A4Q_metadata.json point structures/8A4Q/8a4q_protein.pdb structures/8A4Q/8a4q_pocket.pdb structures/8A4Q/8a4q_ligand.sdf structures/8A4Q/8a4q_ligand.pdb structures/8A4Q/8a4q_ligand.cif structures/8A4Q/8a4q_complex.pdb structures/8A4Q/8a4q_complex.cif 8A4Y classic SARS-CoV-2 non-structural protein 1 (Nsp1) SARS-CoV-2 N-terminal domain, residues Glu10-Asn126 (E10-N126) Na N-(2,3-dihydro-1H-inden-5-yl)acetamide; 2E10 "[""QO6""]" 1 Kd Kd = = 15.1 ± 5.7 mM 15100000.0 [] unit_conversion 1.8210230527068303 success True direct_binding Microscale thermophoresis (MST) measurement of fragment hit 2E10 binding to SARS-CoV-2 Nsp1N pocket 1. 7 The paper states: “2E10 binds to Nsp1N pocket 1 with a KD value of 15.1±5.7 mM.” Figure 6 identifies 2E10 as N-(2,3-dihydro-1H-inden-5-yl)acetamide; the data-availability section identifies the corresponding crystallographic structure as 8A4Y. auto_single_measurement only accepted activity measurement [1] 1 structures\8A4Y\8A4Y_metadata.json point structures/8A4Y/8a4y_protein.pdb structures/8A4Y/8a4y_pocket.pdb structures/8A4Y/8a4y_ligand.sdf structures/8A4Y/8a4y_ligand.pdb structures/8A4Y/8a4y_ligand.cif structures/8A4Y/8a4y_complex.pdb structures/8A4Y/8a4y_complex.cif 8A51 extended HSF2BP; BRME1 human HSF2BP helix alpha1 peptide, residues E19-V50, with BRME1-M peptide, residues E602-K641; crystallized HSF2BP fragment E19-G48 Na Na "[""CHAIN:B""]" 1 Kd Kd = = 2.5 × 10^-8 M 25.0 [] unit_conversion 7.6020599913279625 success True direct_binding ITC at 303 K; HSF2BP α1 versus BRME1-M. 7 Table 1 reports HSF2BP α1 versus BRME1-M: Kd 2.5 × 10^-8 M (±0.3 × 10^-8) at 303 K; Fig. 4B on page 6 labels Kd = 25 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8A51\8A51_metadata.json point structures/8A51/8a51_protein.pdb structures/8A51/8a51_pocket.pdb structures/8A51/8a51_ligand.pdb structures/8A51/8a51_ligand.cif structures/8A51/8a51_complex.pdb structures/8A51/8a51_complex.cif 8A5B extended human Cathepsin L human Recombinant procathepsin L expressed in Komagataella pastoris and processed to activated Cathepsin L Thr110Ala (T110A; active cathepsin numbering) MG-101 "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 Ki Ki = = 64.5 ± 7 pM 0.0645 [] unit_conversion 10.190440285364732 success True biochemical_inhibition CatL inhibition assay; residual activity versus linear MG-101 concentration. 5 Figure 3C prints “Ki = 64.5 ± 7 pM” for MG-101; Figure 5 maps MG-101 to PDB 8A5B. The experimental section identifies the recombinant CatL preparation as T110A. auto_single_measurement only accepted activity measurement [1] 1 structures\8A5B\8A5B_metadata.json point structures/8A5B/8a5b_protein.pdb structures/8A5B/8a5b_pocket.pdb structures/8A5B/8a5b_ligand.pdb structures/8A5B/8a5b_ligand.cif structures/8A5B/8a5b_complex.pdb structures/8A5B/8a5b_complex.cif 8A5L extended TRIM7 PRYSPRY Na His-tagged TRIM7 PRYSPRY domain, residues 342-511 Na 2BC peptide TIEALFQ "[""CHAIN:B""]" 1 Kd Kd = = 11.2 ± 4.2 µM 11200.0 [] unit_conversion 4.950781977329818 success True direct_binding ITC titration of the TIEALFQ peptide with hisTRIM7-PRYSPRY. 11 Figure 2E prints TIEALFQ with KD = 11.2 ± 4.2 µM; the caption identifies these as ITC-derived peptide binding values. Figure 2C caption maps 8A5L to the TRIM7:2BC complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8A5L\8A5L_metadata.json point structures/8A5L/8a5l_protein.pdb structures/8A5L/8a5l_pocket.pdb structures/8A5L/8a5l_ligand.pdb structures/8A5L/8a5l_ligand.cif structures/8A5L/8a5l_complex.pdb structures/8A5L/8a5l_complex.cif 8A5W classic human phosphoserine aminotransferase (PSAT) human PSAT-beta expressed from pET28b with a hexahistidine tag wild-type O-phosphoserine (OPS) "[""SEP""]" 1 Ki Ki = = 3.4 ± 2.0 mM 3400000.0 [] unit_conversion 2.4685210829577446 success True biochemical_inhibition Substrate-inhibition constant for OPS in the reverse PSAT reaction; Table 1 conditions: 37°C, 50 mM HEPES, 100 mM KCl, 1 mM DTT, 0.17 mM PLP, pH 7.0. 6 Table 1 explicitly reports for the reverse reaction: OPS, Ki (mM) = 3.4 ± 2.0. The paper identifies 8A5W as OPS-bound PSAT. auto_single_measurement only accepted activity measurement [1] 1 structures\8A5W\8A5W_metadata.json point structures/8A5W/8a5w_protein.pdb structures/8A5W/8a5w_pocket.pdb structures/8A5W/8a5w_ligand.sdf structures/8A5W/8a5w_ligand.pdb structures/8A5W/8a5w_ligand.cif structures/8A5W/8a5w_complex.pdb structures/8A5W/8a5w_complex.cif 8A6H extended 14-3-3 sigma Na Na Na compound 7 "[""L6L""]" 1 Kd Kd = = 294 nM 294.0 [] unit_conversion 6.531652669587842 success True direct_binding Protein titration (50 μM BME); apparent Kd for C-RAF phosphopeptide binding to 14-3-3σ in the presence of compound 7. 8 Table 3 lists compound 7 protein-titration K_D,app = 294 nM; Figure 5 reports a 77-fold increase in 14-3-3σ/C-RAF binding. auto_single_measurement only accepted activity measurement [1] 1 structures\8A6H\8A6H_metadata.json point structures/8A6H/8a6h_protein.pdb structures/8A6H/8a6h_pocket.pdb structures/8A6H/8a6h_ligand.pdb structures/8A6H/8a6h_ligand.cif structures/8A6H/8a6h_complex.pdb structures/8A6H/8a6h_complex.cif 8A76 classic NDM-1 metallo-beta-lactamase Na NDM-1 without signal peptide, residues 28-270 Na compound 26 "[""L82""]" 1 Ki Ki = = 0.57 ± 0.08 μM 570.0 [] unit_conversion 6.2441251443275085 success True biochemical_inhibition Purified NDM-1 inhibition assay; Table 3 reports Ki values (triplicate assays). 6 Table 3 lists compound 26 with NDM-1 Ki = 0.57 ± 0.08 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8A76\8A76_metadata.json point structures/8A76/8a76_protein.pdb structures/8A76/8a76_pocket.pdb structures/8A76/8a76_ligand.sdf structures/8A76/8a76_ligand.pdb structures/8A76/8a76_ligand.cif structures/8A76/8a76_complex.pdb structures/8A76/8a76_complex.cif 8A92 classic p53-Y220C core domain Na T-p53C-Y220C crystallization construct, residues 94-312 Y220C compound 1151; bromo-trifluoro-pyrazole-amine "[""LE9""]" 1 Kd Kd > > 1 mM 1000000.0 [] unit_conversion 3.0 success True direct_binding ITC; stated as non-fittable ITC data. 4 “Even though the compound has a low K_D value (>1 mM, based on non-fittable ITC data) it stabilizes T-p53C-Y220C by about 0.8 °C.” The preceding text identifies this compound as 1151, and the paper maps compound 1151 to PDB 8A92. auto_single_measurement only accepted activity measurement [1] 1 structures\8A92\8A92_metadata.json point structures/8A92/8a92_protein.pdb structures/8A92/8a92_pocket.pdb structures/8A92/8a92_ligand.sdf structures/8A92/8a92_ligand.pdb structures/8A92/8a92_ligand.cif structures/8A92/8a92_complex.pdb structures/8A92/8a92_complex.cif 8AAP classic PDZ tandem of syntenin Na 6xHis-Syntenin, residues 113-273 Na SYNTi (compound 118) "[""LLV""]" 1 Kd Kd = = 1.8 ± 0.7 µM 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding Isothermal titration calorimetry of SYNTi directly interacting with syntenin; three independent experiments. Syntenin samples prepared for crystallography were directly used for ITC. 11 Three independent experiments gave an average KD of 1.8 ± 0.7 µM for SYNTi-syntenin interaction by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8AAP\8AAP_metadata.json point structures/8AAP/8aap_protein.pdb structures/8AAP/8aap_pocket.pdb structures/8AAP/8aap_ligand.sdf structures/8AAP/8aap_ligand.pdb structures/8AAP/8aap_ligand.cif structures/8AAP/8aap_complex.pdb structures/8AAP/8aap_complex.cif 8AB5 extended E. coli GlpG Escherichia coli GlpG core prepared from a C-terminally His-tagged GFP fusion, GlpG-[TEV protease cleavage site]-GFP-His8; GFP-His8 and TEV were removed and the GlpG core was chymotrypsin-treated Na compound 5; Ac-VRHA-conh-[4-(4-butyl)-phenoxy-1-phenyl-2-butyl] "[""CHAIN:C"", ""CHAIN:D""]" 2 Ki Ki = = 0.7 ± 0.3 nM 0.7 [] unit_conversion 9.154901959985743 success True biochemical_inhibition Apparent inhibition constant (Kiapp) determined from activity measurements at different inhibitor concentrations under tight-binding inhibition conditions using Morrison’s equation. 4 Table 1 visibly reports compound 5 Kiapp = 0.7 ± 0.3 nM for E. coli GlpG; the table states values were calculated using Eq. 1. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8AB5\8AB5_metadata.json point structures/8AB5/8ab5_protein.pdb structures/8AB5/8ab5_pocket.pdb structures/8AB5/8ab5_ligand.pdb structures/8AB5/8ab5_ligand.cif structures/8AB5/8ab5_complex.pdb structures/8AB5/8ab5_complex.cif 8ACD classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na GA-17S "[""LQ6""]" 1 IC50 IC50 = = 0.40 ± 0.03 μM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition Enzymatic Mpro inhibition assay; Figure 3 reports the S-enantiomer GA-17S. 6 Figure 3 prints: “GA-17S IC50 = 0.40 ± 0.03 μM (SARS-CoV-2)”. auto_single_measurement only accepted activity measurement [1] 1 structures\8ACD\8ACD_metadata.json point structures/8ACD/8acd_protein.pdb structures/8ACD/8acd_pocket.pdb structures/8ACD/8acd_ligand.sdf structures/8ACD/8acd_ligand.pdb structures/8ACD/8acd_ligand.cif structures/8ACD/8acd_complex.pdb structures/8ACD/8acd_complex.cif 8ACL classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na GC-14 "[""LQL""]" 1 IC50 IC50 = = 0.40 μM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition Abstract summary of GC-14 inhibition of SARS-CoV-2 Mpro. 1 The abstract states: “The optimized compound GC-14 inhibits Mpro with high potency (IC50 = 0.40 μM)”. auto_single_measurement only accepted activity measurement [1] 1 structures\8ACL\8ACL_metadata.json point structures/8ACL/8acl_protein.pdb structures/8ACL/8acl_pocket.pdb structures/8ACL/8acl_ligand.sdf structures/8ACL/8acl_ligand.pdb structures/8ACL/8acl_ligand.cif structures/8ACL/8acl_complex.pdb structures/8ACL/8acl_complex.cif 8AEU classic human MDM2 human residues 18-125 wild-type Nutlin-3a-aa (compound 3) "[""M0L""]" 1 IC50 IC50 = = 0.21 ± 0.02 µM 210.0 [] unit_conversion 6.6777807052660805 success True biochemical_inhibition Fluorescence-polarization assay measuring inhibition of p53-derived peptide binding to wild-type MDM2. 3 Figure 3C reports for compound 3 against wild-type MDM2: IC50 = 0.21 ± 0.02 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8AEU\8AEU_metadata.json point structures/8AEU/8aeu_protein.pdb structures/8AEU/8aeu_pocket.pdb structures/8AEU/8aeu_ligand.sdf structures/8AEU/8aeu_ligand.pdb structures/8AEU/8aeu_ligand.cif structures/8AEU/8aeu_complex.pdb structures/8AEU/8aeu_complex.cif 8AFB classic KRAS Na Na G12C BI-0474 (compound 23) "[""GDP""]" 1 Ki Ki = = 2.5±0.7 µM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding MS-based covalent-modification kinetic assay; Table 4 reports KI for BI-0474. 5 Table 4 reports KI (MS assay) = 2.5±0.7 µM for BI-0474 (23). auto_single_measurement only accepted activity measurement [1] 1 structures\8AFB\8AFB_metadata.json point structures/8AFB/8afb_protein.pdb structures/8AFB/8afb_pocket.pdb structures/8AFB/8afb_ligand.sdf structures/8AFB/8afb_ligand.pdb structures/8AFB/8afb_ligand.cif structures/8AFB/8afb_complex.pdb structures/8AFB/8afb_complex.cif 8AHG classic PAK4 Homo sapiens PAK4 residues 300-591; GST expression tag cleaved before crystallization Na compound 7 "[""M4I""]" 1 Kd Kd = = 290 µM 290000.0 [] unit_conversion 3.5376020021010435 success True direct_binding SPR measurement; Fig. 6 reports the Kd for PAK4 hit 7 as measured by SPR. 5 Fig. 6 lists compound 7 with “PAK4 K_D 290 μM”; its caption states that K_D values for 5, 6 and 7 were measured by SPR. Data deposition maps 8AHG to compound 7 bound to PAK4. auto_single_measurement only accepted activity measurement [1] 1 structures\8AHG\8AHG_metadata.json point structures/8AHG/8ahg_protein.pdb structures/8AHG/8ahg_pocket.pdb structures/8AHG/8ahg_ligand.sdf structures/8AHG/8ahg_ligand.pdb structures/8AHG/8ahg_ligand.cif structures/8AHG/8ahg_complex.pdb structures/8AHG/8ahg_complex.cif 8AHH classic PAK4 Homo sapiens PAK4 residues 300-591; GST expression tag cleaved before crystallization Na compound 5 "[""M4X""]" 1 Kd Kd = = 15 µM 15000.0 [] unit_conversion 4.823908740944319 success True direct_binding SPR measurement; Fig. 6 reports the Kd for PAK4 hit 5 as measured by SPR. 5 Fig. 6 lists compound 5 with “PAK4 K_D 15 μM”; its caption states that K_D values for 5, 6 and 7 were measured by SPR. Data deposition maps 8AHH to compound 5 bound to PAK4. auto_single_measurement only accepted activity measurement [1] 1 structures\8AHH\8AHH_metadata.json point structures/8AHH/8ahh_protein.pdb structures/8AHH/8ahh_pocket.pdb structures/8AHH/8ahh_ligand.sdf structures/8AHH/8ahh_ligand.pdb structures/8AHH/8ahh_ligand.cif structures/8AHH/8ahh_complex.pdb structures/8AHH/8ahh_complex.cif 8AIJ extended LecB lectin from Pseudomonas aeruginosa strain PAO1 Pseudomonas aeruginosa strain PAO1 Na Na N-(alpha-L-Fucopyranosyl)benzamide (6) "[""M9I""]" 2 Kd Kd = = 2310 ± 350 nM 2310.0 [] unit_conversion 5.636388020107855 success True direct_binding Isothermal titration calorimetry of LecB with α-fucosyl benzamide 6. 5 Table 2 reports ITC for compound 6: Kd = 2310 ± 350 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8AIJ\8AIJ_metadata.json point structures/8AIJ/8aij_ligand.sdf structures/8AIJ/8aij_ligand.cif structures/8AIJ/8aij_complex.cif 8AIY extended LecB lectin from Pseudomonas aeruginosa strain PAO1 Pseudomonas aeruginosa strain PAO1 Na Na N-(beta-L-Fucopyranosyl)-biphenyl-3-carboxamide (4i) "[""MJO""]" 1 IC50 IC50 = = 85 ± 16 nM 85.0 [] unit_conversion 7.070581074285707 success True biochemical_inhibition Competitive fluorescence-polarization binding assay; L-fucose positive reference. 4 Table 1 reports compound 4i (mPh-C6H4-substituted β-fucosyl amide), IC50 = 85 ± 16 nM, for LecBPAO1 in a competitive binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8AIY\8AIY_metadata.json point structures/8AIY/8aiy_ligand.sdf structures/8AIY/8aiy_ligand.cif structures/8AIY/8aiy_complex.cif 8AJM extended DDB1-DCAF12 Homo sapiens His6-DDB1-Strep(II)-DCAF12-His6-CCT5 Na CCT5 C-terminal di-Glu degron peptide (CCT5 residues 537-541) "[""CHAIN:C""]" 1 IC50 IC50 = = 24.64 µM 24640.0 [] unit_conversion 4.608359296507612 success True direct_binding TR-FRET competition titration of unlabeled CCT5 C-terminal peptides against pre-assembled TbDDB1-DCAF12^488; Figure 1D. 3 Figure 1D lists the CCT5_5 peptide sequence GESEE, corresponding to degron positions −5 to −1 (CCT5 residues 537–541), with IC50 = 24.64 µM. The caption identifies this as TR-FRET counter-titration of unlabeled CCT5 C-terminal peptides into TbDDB1-DCAF12^488. auto_single_measurement only accepted activity measurement [1] 1 structures\8AJM\8AJM_metadata.json point structures/8AJM/8ajm_protein.pdb structures/8AJM/8ajm_pocket.pdb structures/8AJM/8ajm_ligand.pdb structures/8AJM/8ajm_ligand.cif structures/8AJM/8ajm_complex.pdb structures/8AJM/8ajm_complex.cif 8ALX extended PD-L1 human Na Na pAC65 "[""CHAIN:B""]" 1 IC50 IC50 = = 1.80±0.16 nM 1.8 [] unit_conversion 8.744727494896694 success True biochemical_inhibition Commercial homogeneous time-resolved fluorescence (HTRF) assay assessing pAC65-mediated dissociation of the PD-1/PD-L1 complex. 6 “The pAC65 peptide dose-dependently dissociated the PD-1/PD-L1 complex with an IC50 value of 1.80±0.16 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ALX\8ALX_metadata.json point structures/8ALX/8alx_protein.pdb structures/8ALX/8alx_pocket.pdb structures/8ALX/8alx_ligand.pdb structures/8ALX/8alx_ligand.cif structures/8ALX/8alx_complex.pdb structures/8ALX/8alx_complex.cif 8AN8 classic c-MET Na Na wild-type compound 7 "[""MDI""]" 1 Kd Kd = = 7.2 ± 0.7 µM 7200.0 [] unit_conversion 5.142667503568731 success True direct_binding Surface plasmon resonance (SPR), wild-type c-MET. 2 Table 1 reports a Kd (SPR) of 7.2 ± 0.7 µM for compound 7 (R), wild-type c-MET; Figure 2 identifies PDB 8AN8 as wild-type c-MET bound by compound 7. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8AN8\8AN8_metadata.json point structures/8AN8/8an8_protein.pdb structures/8AN8/8an8_pocket.pdb structures/8AN8/8an8_ligand.sdf structures/8AN8/8an8_ligand.pdb structures/8AN8/8an8_ligand.cif structures/8AN8/8an8_complex.pdb structures/8AN8/8an8_complex.cif 8AO0 classic nanoFAST Na nanoFAST, a FAST variant lacking the N-terminal domain Na HBR-DOM2 "[""O1F""]" 1 Kd Kd = = 0.85 µM 850.0 [] unit_conversion 6.070581074285707 success True direct_binding Spectrofluorometric titration of purified nanoFAST by fluorogen; 25 °C, pH 7.4 PBS; protein concentration 0.10 µM. 8 “its dissociation constant with nanoFAST is 0.85 µM”; the direct titration method is specified on page 10. auto_single_measurement only accepted activity measurement [1] 1 structures\8AO0\8AO0_metadata.json point structures/8AO0/8ao0_protein.pdb structures/8AO0/8ao0_pocket.pdb structures/8AO0/8ao0_ligand.sdf structures/8AO0/8ao0_ligand.pdb structures/8AO0/8ao0_ligand.cif structures/8AO0/8ao0_complex.pdb structures/8AO0/8ao0_complex.cif 8APT classic TrmD Haemophilus influenzae Na Na Compound 13 "[""NN9""]" 1 IC50 IC50 = = 1.4 µM 1400.0 [] unit_conversion 5.853871964321762 success True biochemical_inhibition TrmD enzyme inhibition assay; values determined from at least two technical replicates. 3 Table 1 lists Compound 13 with TrmD IC50 = 1.4 µM; the paper identifies PDB 8APT as the co-crystal structure of Compound 13. auto_single_measurement only accepted activity measurement [1] 1 structures\8APT\8APT_metadata.json point structures/8APT/8apt_protein.pdb structures/8APT/8apt_pocket.pdb structures/8APT/8apt_ligand.sdf structures/8APT/8apt_ligand.pdb structures/8APT/8apt_ligand.cif structures/8APT/8apt_complex.pdb structures/8APT/8apt_complex.cif 8APU classic TrmD Haemophilus influenzae Na Na Compound 14 "[""NMV""]" 1 IC50 IC50 = = 2.3 µM 2300.0 [] unit_conversion 5.638272163982407 success True biochemical_inhibition TrmD enzyme inhibition assay; values determined from at least two technical replicates. 3 Table 1 lists Compound 14 with TrmD IC50 = 2.3 µM; the paper identifies PDB 8APU as the co-crystal structure of Compound 14. auto_single_measurement only accepted activity measurement [1] 1 structures\8APU\8APU_metadata.json point structures/8APU/8apu_protein.pdb structures/8APU/8apu_pocket.pdb structures/8APU/8apu_ligand.sdf structures/8APU/8apu_ligand.pdb structures/8APU/8apu_ligand.cif structures/8APU/8apu_complex.pdb structures/8APU/8apu_complex.cif 8APV classic TrmD Haemophilus influenzae Na Na Compound 27 "[""NLL""]" 1 IC50 IC50 = = 1.9 µM 1900.0 [] unit_conversion 5.721246399047171 success True biochemical_inhibition TrmD enzyme inhibition assay; values determined from at least two technical replicates. 5 Table 2 lists Compound 27 with TrmD IC50 = 1.9 µM. The text identifies its X-ray crystal structure as PDB 8APV. auto_single_measurement only accepted activity measurement [1] 1 structures\8APV\8APV_metadata.json point structures/8APV/8apv_protein.pdb structures/8APV/8apv_pocket.pdb structures/8APV/8apv_ligand.sdf structures/8APV/8apv_ligand.pdb structures/8APV/8apv_ligand.cif structures/8APV/8apv_complex.pdb structures/8APV/8apv_complex.cif 8APW classic TrmD Haemophilus influenzae Na Na Compound 30 "[""NL1""]" 1 IC50 IC50 = = 6.5 µM 6500.0 [] unit_conversion 5.187086643357144 success True biochemical_inhibition TrmD enzyme inhibition assay; values determined from at least two technical replicates. 5 Table 2 lists Compound 30 with TrmD IC50 = 6.5 µM. The text identifies its X-ray crystal structure as PDB 8APW. auto_single_measurement only accepted activity measurement [1] 1 structures\8APW\8APW_metadata.json point structures/8APW/8apw_protein.pdb structures/8APW/8apw_pocket.pdb structures/8APW/8apw_ligand.sdf structures/8APW/8apw_ligand.pdb structures/8APW/8apw_ligand.cif structures/8APW/8apw_complex.pdb structures/8APW/8apw_complex.cif 8ARE extended OppA Bacillus subtilis Residues 17-525 with an N-terminal HRV 3C-cleavable hexahistidine tag; cleavage leaves a vestigial GPA sequence Na Ser-Arg-Asn-Val-Thr (SRNVT) "[""CHAIN:B""]" 1 Kd Kd = = 2.16±0.8 µM 2160.0 [] unit_conversion 5.665546248849069 success True direct_binding Isothermal titration calorimetry; experiments in triplicate at 298 K. 9 Table 5 reports peptide binding to BsOppA measured by ITC: SRVNT (PhrE), Kd 2.16±0.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8ARE\8ARE_metadata.json point structures/8ARE/8are_protein.pdb structures/8ARE/8are_pocket.pdb structures/8ARE/8are_ligand.pdb structures/8ARE/8are_ligand.cif structures/8ARE/8are_complex.pdb structures/8ARE/8are_complex.cif 8ARN extended OppA Bacillus subtilis Residues 17-525 with an N-terminal HRV 3C-cleavable hexahistidine tag; cleavage leaves a vestigial GPA sequence Na Ser-Asn-Ser-Ser (SNSS) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.43±0.03 µM 430.0 [] unit_conversion 6.366531544420413 success True direct_binding Isothermal titration calorimetry; experiments in triplicate at 298 K. 9 Table 5 reports peptide binding to BsOppA measured by ITC: SNSS, Kd 0.43±0.03 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8ARN\8ARN_metadata.json point structures/8ARN/8arn_protein.pdb structures/8ARN/8arn_pocket.pdb structures/8ARN/8arn_ligand.pdb structures/8ARN/8arn_ligand.cif structures/8ARN/8arn_complex.pdb structures/8ARN/8arn_complex.cif 8ATB extended IRAK4 Na Na Na compound 16 "[""O0H""]" 1 IC50 IC50 = = 5 nM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition Biochemical potency of IRAK4 inhibition at 1 mM ATP. 4 Table 2 reports compound 16 IRAK4 IC50 = 5 nM; its footnote specifies 1 mM ATP. The accession-code list maps PDB 8ATB to compound 16 (page 16). auto_single_measurement only accepted activity measurement [1] 1 structures\8ATB\8ATB_metadata.json point structures/8ATB/8atb_ligand.sdf structures/8ATB/8atb_ligand.cif structures/8ATB/8atb_complex.cif 8ATL extended IRAK4 Na Na Na compound 23 "[""O6X""]" 1 IC50 IC50 = = 9 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition Biochemical potency of IRAK4 inhibition at 1 mM ATP. 4 Table 2 reports compound 23 IRAK4 IC50 = 9 nM; its footnote specifies 1 mM ATP. The accession-code list maps PDB 8ATL to compound 23 (page 16). auto_single_measurement only accepted activity measurement [1] 1 structures\8ATL\8ATL_metadata.json point structures/8ATL/8atl_ligand.sdf structures/8ATL/8atl_ligand.cif structures/8ATL/8atl_complex.cif 8ATN extended IRAK4 Na Na Na compound 38 "[""O06""]" 1 IC50 IC50 = = 11 nM 11.0 [] unit_conversion 7.958607314841775 success True biochemical_inhibition Biochemical potency of IRAK4 inhibition at 1 mM ATP. 8 Table 8 reports compound 38 IRAK4 IC50 = 11 nM; its footnote specifies 1 mM ATP. Figure 5 identifies PDB 8ATN as the IRAK4 cocrystal structure of compound 38 (page 9), and the accession-code list confirms this mapping (page 16). auto_single_measurement only accepted activity measurement [1] 1 structures\8ATN\8ATN_metadata.json point structures/8ATN/8atn_ligand.sdf structures/8ATN/8atn_ligand.cif structures/8ATN/8atn_complex.cif 8AU3 classic c-MET Na MET kinase domain, residues 1051-1349 Y1234E; Y1235E Tepotinib "[""3E8""]" 1 Kd Kd = = 2.9 nM 2.9 [] unit_conversion 8.537602002101044 success True direct_binding SPR with recombinant MET Y1234E/Y1235E. 3 “SPR studies with MET Y1234E/Y1235E (Table 1) showed a similar binding affinity (KD = 2.9 nM) ... for tepotinib.” auto_single_measurement only accepted activity measurement [1] 1 structures\8AU3\8AU3_metadata.json point structures/8AU3/8au3_protein.pdb structures/8AU3/8au3_pocket.pdb structures/8AU3/8au3_ligand.sdf structures/8AU3/8au3_ligand.pdb structures/8AU3/8au3_ligand.cif structures/8AU3/8au3_complex.pdb structures/8AU3/8au3_complex.cif 8AUZ classic GSK-3 beta Na Recombinant kinase domain containing a C-terminal His-tag Na FL-291 "[""O9C""]" 1 IC50 IC50 = = 25 nM 25.0 [] unit_conversion 7.6020599913279625 success True biochemical_inhibition Kinase inhibition assay; Fig. 1 reports the GSK-3β IC50 for FL-291. Table 2 identifies the assay kinases as human unless otherwise specified. 2 Fig. 1(d) visibly reports for FL-291: IC50 (GSK-3β): 25 nM. The experimental section maps PDB 8AUZ to FL-291 (page 15). auto_single_measurement only accepted activity measurement [1] 1 structures\8AUZ\8AUZ_metadata.json point structures/8AUZ/8auz_protein.pdb structures/8AUZ/8auz_pocket.pdb structures/8AUZ/8auz_ligand.sdf structures/8AUZ/8auz_ligand.pdb structures/8AUZ/8auz_ligand.cif structures/8AUZ/8auz_complex.pdb structures/8AUZ/8auz_complex.cif 8AV1 classic GSK-3 beta Na Recombinant kinase domain containing a C-terminal His-tag Na CD-07 "[""O9L""]" 1 IC50 IC50 = = 22 nM 22.0 [] unit_conversion 7.657577319177793 success True biochemical_inhibition Kinase inhibition assay; Fig. 1 reports the GSK-3β IC50 for CD-07. Table 2 identifies the assay kinases as human unless otherwise specified. 2 Fig. 1(d) visibly reports for CD-07: IC50 (GSK-3β): 22 nM. The experimental section maps PDB 8AV1 to CD-07 (page 15). auto_single_measurement only accepted activity measurement [1] 1 structures\8AV1\8AV1_metadata.json point structures/8AV1/8av1_protein.pdb structures/8AV1/8av1_pocket.pdb structures/8AV1/8av1_ligand.sdf structures/8AV1/8av1_ligand.pdb structures/8AV1/8av1_ligand.cif structures/8AV1/8av1_complex.pdb structures/8AV1/8av1_complex.cif 8AVQ classic A075L Paramecium bursaria chlorella virus-1 (PBCV-1) Na Na UDP-alpha-D-Xyl (compound 1; UDP-xylose) "[""UDX""]" 1 Kd Kd = = 31.2e-6 ± 3.54e-6 M 31200.0 [] unit_conversion 4.505845405981558 success True direct_binding ITC of A075L with UDP-alpha-D-Xyl (1); Figure 3 caption specifies MgCl2. 5 Figure 3a prints “KD(M)=31.2e-6 ± 3.54e-6” for UDP-Xyl–A075L. auto_single_measurement only accepted activity measurement [1] 1 structures\8AVQ\8AVQ_metadata.json point structures/8AVQ/8avq_protein.pdb structures/8AVQ/8avq_pocket.pdb structures/8AVQ/8avq_ligand.sdf structures/8AVQ/8avq_ligand.pdb structures/8AVQ/8avq_ligand.cif structures/8AVQ/8avq_complex.pdb structures/8AVQ/8avq_complex.cif 8AW1 classic c-MET Na MET kinase domain, residues 1051-1349 Y1235D Tepotinib "[""3E8""]" 1 Kd Kd = = 2.3 nM 2.3 [] unit_conversion 8.638272163982407 success True direct_binding SPR with recombinant nonphosphorylated Y1235D MET protein. 2 Table 1 lists Y1235D with KD 2.3 nM; the Results state recombinant Y1235D was obtained in nonphosphorylated form. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8AW1\8AW1_metadata.json point structures/8AW1/8aw1_protein.pdb structures/8AW1/8aw1_pocket.pdb structures/8AW1/8aw1_ligand.sdf structures/8AW1/8aw1_ligand.pdb structures/8AW1/8aw1_ligand.cif structures/8AW1/8aw1_complex.pdb structures/8AW1/8aw1_complex.cif 8AYS classic SARS-CoV-2 non-structural protein 1 (nsp1) SARS-CoV-2 residues 10-126 Na 4-(2-aminothiazol-4-yl)phenol; 10B6 "[""92G""]" 1 Kd Kd = = 0.56 ± 0.19 mM 560000.0 [] unit_conversion 3.2518119729937993 success True direct_binding Microscale thermophoresis (MST); fragment affinity reported in Table 3. 8 Table 3 reports 10B6, binding site I, MST Kd 0.56 ± 0.19 mM for SARS-CoV-2 nsp1(10-126). auto_single_measurement only accepted activity measurement [1] 1 structures\8AYS\8AYS_metadata.json point structures/8AYS/8ays_protein.pdb structures/8AYS/8ays_pocket.pdb structures/8AYS/8ays_ligand.sdf structures/8AYS/8ays_ligand.pdb structures/8AYS/8ays_ligand.cif structures/8AYS/8ays_complex.pdb structures/8AYS/8ays_complex.cif 8AZ8 classic SARS-CoV-2 non-structural protein 1 (nsp1) SARS-CoV-2 residues 10-126 Na 2-(benzylamino)ethan-1-ol; 8E6 "[""OEI""]" 1 Kd Kd = = 8.32 ± 3.32 mM 8320000.0 [] unit_conversion 2.0798766737092764 success True direct_binding Microscale thermophoresis (MST); fragment affinity reported in Table 3. 8 Table 3 reports 8E6, binding site II, MST Kd 8.32 ± 3.32 mM for SARS-CoV-2 nsp1(10-126). auto_single_measurement only accepted activity measurement [1] 1 structures\8AZ8\8AZ8_metadata.json point structures/8AZ8/8az8_protein.pdb structures/8AZ8/8az8_pocket.pdb structures/8AZ8/8az8_ligand.sdf structures/8AZ8/8az8_ligand.pdb structures/8AZ8/8az8_ligand.cif structures/8AZ8/8az8_complex.pdb structures/8AZ8/8az8_complex.cif 8AZV classic KRAS Na KRAS residues 1-169, UniProt P01116 WT BI-2865 "[""OFU""]" 1 Kd Kd = = 6.9 nM 6.9 [] unit_conversion 8.161150909262744 success True direct_binding Isothermal titration calorimetry; GDP-loaded KRAS. 2 Fig. 1c prints: “Kd 6.9 nM (WT)”. The text states that BI-2865 bound GDP-loaded WT KRAS with high affinity as determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8AZV\8AZV_metadata.json point structures/8AZV/8azv_protein.pdb structures/8AZV/8azv_pocket.pdb structures/8AZV/8azv_ligand.sdf structures/8AZV/8azv_ligand.pdb structures/8AZV/8azv_ligand.cif structures/8AZV/8azv_complex.pdb structures/8AZV/8azv_complex.cif 8AZX classic KRAS Na KRAS residues 1-169, UniProt P01116 G12C BI-2865 "[""OFU""]" 1 Kd Kd = = 4.5 nM 4.5 [] unit_conversion 8.346787486224656 success True direct_binding Isothermal titration calorimetry; GDP-loaded KRAS. 2 Fig. 1c prints: “Kd ... 4.5 nM (G12C)”. The text states that BI-2865 bound GDP-loaded G12C KRAS with high affinity as determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8AZX\8AZX_metadata.json point structures/8AZX/8azx_protein.pdb structures/8AZX/8azx_pocket.pdb structures/8AZX/8azx_ligand.sdf structures/8AZX/8azx_ligand.pdb structures/8AZX/8azx_ligand.cif structures/8AZX/8azx_complex.pdb structures/8AZX/8azx_complex.cif 8AZY classic KRAS Na KRAS residues 1-169, UniProt P01116 G12D BI-2865 "[""OFU""]" 1 Kd Kd = = 32 nM 32.0 [] unit_conversion 7.494850021680094 success True direct_binding Isothermal titration calorimetry; GDP-loaded KRAS. 2 Fig. 1c prints: “Kd ... 32 nM (G12D)”. The text states that BI-2865 bound GDP-loaded G12D KRAS with high affinity as determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8AZY\8AZY_metadata.json point structures/8AZY/8azy_protein.pdb structures/8AZY/8azy_pocket.pdb structures/8AZY/8azy_ligand.sdf structures/8AZY/8azy_ligand.pdb structures/8AZY/8azy_ligand.cif structures/8AZY/8azy_complex.pdb structures/8AZY/8azy_complex.cif 8AZZ classic KRAS Na KRAS residues 1-169, UniProt P01116 G12V BI-2865 "[""OFU""]" 1 Kd Kd = = 26 nM 26.0 [] unit_conversion 7.585026652029182 success True direct_binding Isothermal titration calorimetry; GDP-loaded KRAS. 2 Fig. 1c prints: “Kd ... 26 nM (G12V)”. The text states that BI-2865 bound GDP-loaded G12V KRAS with high affinity as determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8AZZ\8AZZ_metadata.json point structures/8AZZ/8azz_protein.pdb structures/8AZZ/8azz_pocket.pdb structures/8AZZ/8azz_ligand.sdf structures/8AZZ/8azz_ligand.pdb structures/8AZZ/8azz_ligand.cif structures/8AZZ/8azz_complex.pdb structures/8AZZ/8azz_complex.cif 8B00 classic KRAS Na KRAS residues 1-169, UniProt P01116 G13D BI-2865 "[""OFU""]" 1 Kd Kd = = 4.3 nM 4.3 [] unit_conversion 8.366531544420413 success True direct_binding Isothermal titration calorimetry; GDP-loaded KRAS. 2 Fig. 1c prints: “Kd ... 4.3 nM (G13D)”. The text states that BI-2865 bound GDP-loaded G13D KRAS with high affinity as determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8B00\8B00_metadata.json point structures/8B00/8b00_protein.pdb structures/8B00/8b00_pocket.pdb structures/8B00/8b00_ligand.sdf structures/8B00/8b00_ligand.pdb structures/8B00/8b00_ligand.cif structures/8B00/8b00_complex.pdb structures/8B00/8b00_complex.cif 8B07 classic monkeypox virus methyltransferase VP39 Monkeypox virus (MPXV) Recombinant VP39 expressed in E. coli from a pSUMO construct with an 8xHis-SUMO tag; tag cleaved before crystallization Na sinefungin (SFG) "[""SFG""]" 1 IC50 IC50 = = 2.33 ± 0.064 µM 2330.0 [] unit_conversion 5.632644078973981 success True biochemical_inhibition VP39 2′-O-methyltransferase inhibition assay; Fig. 4 reports mean ± SEM (n=2 independent measurements). 5 Fig. 4 labels sinefungin (SFG) with IC50 2.33 ± 0.064 µM; its caption identifies MTase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8B07\8B07_metadata.json point structures/8B07/8b07_protein.pdb structures/8B07/8b07_pocket.pdb structures/8B07/8b07_ligand.sdf structures/8B07/8b07_ligand.pdb structures/8B07/8b07_ligand.cif structures/8B07/8b07_complex.pdb structures/8B07/8b07_complex.cif 8B1W classic NDM-1 metallo-beta-lactamase Na Na Na CP35 "[""OQU""]" 1 Ki Ki = = 25.8 ± 0.7 µM 25800.0 [] unit_conversion 4.58838029403677 success True biochemical_inhibition Purified NDM-1 enzymatic inhibition assay using meropenem reporter substrate; Ki determined with Dixon plots. 7 Table 2 reports CP 35 NDM-1 Ki = 25.8 ± 0.7 µM; its footnote states Ki was determined with Dixon plots. The paper maps CP 35 to PDB 8B1W. auto_single_measurement only accepted activity measurement [1] 1 structures\8B1W\8B1W_metadata.json point structures/8B1W/8b1w_protein.pdb structures/8B1W/8b1w_pocket.pdb structures/8B1W/8b1w_ligand.sdf structures/8B1W/8b1w_ligand.pdb structures/8B1W/8b1w_ligand.cif structures/8B1W/8b1w_complex.pdb structures/8B1W/8b1w_complex.cif 8B1Z classic NDM-1 metallo-beta-lactamase Na Na Na CP56 "[""ORL""]" 1 Ki Ki = = 24.5 ± 0.5 µM 24500.0 [] unit_conversion 4.610833915635467 success True biochemical_inhibition Purified NDM-1 enzymatic inhibition assay using meropenem reporter substrate; best inhibitors, including CP 56, were evaluated by Dixon plots. 8 Table 2 reports CP 56 NDM-1 Ki = 24.5 ± 0.5 µM. The paper identifies the CP 56 NDM-1 structure as PDB 8B1Z. auto_single_measurement only accepted activity measurement [1] 1 structures\8B1Z\8B1Z_metadata.json point structures/8B1Z/8b1z_protein.pdb structures/8B1Z/8b1z_pocket.pdb structures/8B1Z/8b1z_ligand.sdf structures/8B1Z/8b1z_ligand.pdb structures/8B1Z/8b1z_ligand.cif structures/8B1Z/8b1z_complex.pdb structures/8B1Z/8b1z_complex.cif 8B20 classic NDM-1 metallo-beta-lactamase Na Na Na CP57 "[""OQK""]" 1 Ki Ki = = 5.6 ± 0.8 µM 5600.0 [] unit_conversion 5.251811972993799 success True biochemical_inhibition Purified NDM-1 enzymatic inhibition assay using meropenem reporter substrate; Ki determined for best inhibitors by Dixon plots. 8 Table 2 reports CP 57 NDM-1 Ki = 5.6 ± 0.8 µM. The paper identifies the CP 57 NDM-1 structure as PDB 8B20. auto_single_measurement only accepted activity measurement [1] 1 structures\8B20\8B20_metadata.json point structures/8B20/8b20_protein.pdb structures/8B20/8b20_pocket.pdb structures/8B20/8b20_ligand.sdf structures/8B20/8b20_ligand.pdb structures/8B20/8b20_ligand.cif structures/8B20/8b20_complex.pdb structures/8B20/8b20_complex.cif 8B2C extended type I dehydroquinase (DHQ1) Salmonella typhi Na Na compound 8 (epoxide derivative) "[""OVU""]" 1 IC50 IC50 > > 2 mM 2000000.0 [] unit_conversion 2.6989700043360187 success True biochemical_inhibition Reversible competitive inhibition assay; enzyme activity was measured with increasing ligand concentration. 5 Compound 8 was reported as a reversible competitive inhibitor with IC50 values > 2 mM for both enzymes, including St-DHQ1. auto_single_measurement only accepted activity measurement [1] 1 structures\8B2C\8B2C_metadata.json point structures/8B2C/8b2c_ligand.sdf structures/8B2C/8b2c_ligand.cif structures/8B2C/8b2c_complex.cif 8B4J extended Rfa1 N-terminal domain S. cerevisiae Rfa1-NTD in complex with phosphorylated Ddc2 peptide, residues 4-24 Na phosphorylated Ddc2 peptide (pS11-Ddc2 peptide) "[""CHAIN:P""]" 1 Kd Kd = = 1.7 ± 0.2 µM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding MST specific Site II binding of pS11-Ddc2 peptide to Rfa1-NTD with ZnCl2 added. 5 Fig. 3H prints “pS11-Ddc2 + ZnCl2, K_D = 1.7 ± 0.2 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8B4J\8B4J_metadata.json point structures/8B4J/8b4j_protein.pdb structures/8B4J/8b4j_pocket.pdb structures/8B4J/8b4j_ligand.pdb structures/8B4J/8b4j_ligand.cif structures/8B4J/8b4j_complex.pdb structures/8B4J/8b4j_complex.cif 8B4X extended furin (PCSK3) Na Na Na Guanidinomethyl-Phac-R-Tle-K-6-(aminomethyl)-3-amino-isoindol (inhibitor 15) "[""CHAIN:B""]" 1 Ki Ki = = 4.78 ± 0.19 pM 0.00478 [] unit_conversion 11.320572103387882 success True biochemical_inhibition Enzyme kinetic measurement with soluble human furin and Ac-Arg-Arg-Tle-Arg-Arg-AMC substrate. 4 Table 1 lists inhibitor 15 with Ki = 4.78 ± 0.19 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\8B4X\8B4X_metadata.json point structures/8B4X/8b4x_protein.pdb structures/8B4X/8b4x_pocket.pdb structures/8B4X/8b4x_ligand.pdb structures/8B4X/8b4x_ligand.cif structures/8B4X/8b4x_complex.pdb structures/8B4X/8b4x_complex.cif 8B58 extended TgCyp23 Toxoplasma gondii Full-length TgCyp285760 (TgCyp23) recombinant protein with an N-terminal His6 tag and TEV cleavage site; the tag was removed before crystallization Na Cyclosporin A (CsA) "[""CHAIN:C"", ""CHAIN:D""]" 2 Kd Kd = = 82 ± 15 nM 82.0 [] unit_conversion 7.086186147616283 success True direct_binding Isothermal titration calorimetry of CsA binding to purified recombinant TgCyp23; one-site, 1:1 CsA/protein stoichiometry. 5 Table 3 reports “TgCyp23 + CsA” Kd = “82 ± 15” nM; the text states that CsA binding was measured by ITC and showed a single 1:1 binding event. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8B58\8B58_metadata.json point structures/8B58/8b58_protein.pdb structures/8B58/8b58_pocket.pdb structures/8B58/8b58_ligand.pdb structures/8B58/8b58_ligand.cif structures/8B58/8b58_complex.pdb structures/8B58/8b58_complex.cif 8B5A extended BRD3 Human BRD3(2), expressed and purified without fluorescent tags Na H4K20ApmTri "[""CHAIN:B""]" 1 Kd Kd = = 6.5 ± 0.5 μM 6500.0 [] unit_conversion 5.187086643357144 success True direct_binding Microscale thermophoresis (MST) assay with BRD3(2) and H4K20ApmTri peptide. 4 “The recorded K_D values of BRD3(2) bound to H4K20ac and H4K20ApmTri were 3.2±0.3 μM and 6.5±0.5 μM, respectively (Figure 2c).” auto_single_measurement only accepted activity measurement [1] 1 structures\8B5A\8B5A_metadata.json point structures/8B5A/8b5a_protein.pdb structures/8B5A/8b5a_pocket.pdb structures/8B5A/8b5a_ligand.pdb structures/8B5A/8b5a_ligand.cif structures/8B5A/8b5a_complex.pdb structures/8B5A/8b5a_complex.cif 8B5B extended BRD4 Human BRD4(1), expressed and purified without fluorescent tags Na H4K5acK8ApmTri "[""CHAIN:D"", ""CHAIN:E""]" 1 Kd Kd = = 6.7 ± 0.5 μM 6700.0 [] unit_conversion 5.173925197299173 success True direct_binding Microscale thermophoresis (MST) assay with BRD4(1) and the mixed H4 peptide bearing native K5 acetyllysine and K8 ApmTri. 4 Figure 2d labels the blue ligand as H4K5acK8ApmTri and prints K_D = 6.7 ± 0.5 μM; the text identifies the mixed probe as native Kac at position 5 and ApmTri at position 8. auto_single_measurement only accepted activity measurement [1] 1 structures\8B5B\8B5B_metadata.json point structures/8B5B/8b5b_protein.pdb structures/8B5B/8b5b_pocket.pdb structures/8B5B/8b5b_ligand.pdb structures/8B5B/8b5b_ligand.cif structures/8B5B/8b5b_complex.pdb structures/8B5B/8b5b_complex.cif 8B5Y classic SHP2 Na Na Na Compound 8 "[""P8O""]" 2 Kd Kd = = 0.6 nM 0.6 [] unit_conversion 9.221848749616356 success True direct_binding Surface plasmon resonance (SPR) measurement of compound 8 binding to SHP2. 3 “Compound 8 binding was studied by surface plasmon resonance (SPR): the measured KD = 0.6 nM”; the same passage identifies the compound 8–SHP2 crystallization structure as PDB 8B5Y. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8B5Y\8B5Y_metadata.json point structures/8B5Y/8b5y_protein.pdb structures/8B5Y/8b5y_pocket.pdb structures/8B5Y/8b5y_ligand.sdf structures/8B5Y/8b5y_ligand.pdb structures/8B5Y/8b5y_ligand.cif structures/8B5Y/8b5y_complex.pdb structures/8B5Y/8b5y_complex.cif 8B6M classic Tankyrase 2 (TNKS2) Na Na Na compound 6 "[""OY6""]" 1 Ki Ki = = 0.0085 μM 8.5 [] unit_conversion 8.070581074285707 success True biochemical_inhibition TNKS2 biochemical inhibition assay; Table 3 reports compound 6. The paper describes the assay as measuring unreacted NAD+ conversion and calculating Ki from IC50 values. 7 Table 3 lists compound 6 with Ki = 0.0085 μM. Its footnote states Ki values are for TNKS2 inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\8B6M\8B6M_metadata.json point structures/8B6M/8b6m_protein.pdb structures/8B6M/8b6m_pocket.pdb structures/8B6M/8b6m_ligand.sdf structures/8B6M/8b6m_ligand.pdb structures/8B6M/8b6m_ligand.cif structures/8B6M/8b6m_complex.pdb structures/8B6M/8b6m_complex.cif 8B8V extended Rabies virus nucleoprotein (N) and phosphoprotein (P) rabies virus (RABV), CVS-11 strain NDelta23 nucleoprotein (residues 24-450) in complex with P68 phosphoprotein (residues 1-68) Na Na "[""CHAIN:B""]" 1 Kd Kd = = 8.2 ± 0.6 nM 8.2 [] unit_conversion 8.086186147616283 success True direct_binding Equilibrium competition fluorescence-anisotropy binding assay of the NΔ23–P68 complex; values fitted with Kd* fixed at 0.5 nM. 15 Table 2 reports P68 Kd = 8.2 ± 0.6 nM; the preceding text identifies the assay as equilibrium competition binding of fluorescent NΔ23–P42-G41C complex with unlabeled P68. auto_single_measurement only accepted activity measurement [1] 1 structures\8B8V\8B8V_metadata.json point structures/8B8V/8b8v_protein.pdb structures/8B8V/8b8v_pocket.pdb structures/8B8V/8b8v_ligand.pdb structures/8B8V/8b8v_ligand.cif structures/8B8V/8b8v_complex.pdb structures/8B8V/8b8v_complex.cif 8B9U extended ClpC1 Mycobacterium tuberculosis N-terminal domain (NTD) Na Ecu** "[""CHAIN:C""]" 1 Kd Kd = = 50 μM 50000.0 [] unit_conversion 4.301029995663981 success True direct_binding Binding of the short linear ecumicin-fragment peptide mimic Ecu** to ClpC1 NTD; the paper then co-crystallized this complex (8B9U). 7 “Upon confirming the binding of the short Ecu** peptide mimic ... to ClpC1NTD (KD = 50 μM, Table S2), we co-crystallized the protein-peptide complex and determined its crystal structure.” auto_single_measurement only accepted activity measurement [1] 1 structures\8B9U\8B9U_metadata.json point structures/8B9U/8b9u_protein.pdb structures/8B9U/8b9u_pocket.pdb structures/8B9U/8b9u_ligand.pdb structures/8B9U/8b9u_ligand.cif structures/8B9U/8b9u_complex.pdb structures/8B9U/8b9u_complex.cif 8BAN extended Secretagogin mouse Mouse secretagogin with GFP carrying the SNAP-25-derived target peptide as a C-terminal tag Na SNAP-25-derived peptide (construct residues 155-179; modeled bound segment 155-171) "[""POLYMER_ENTITY:1""]" 1 Kd Kd = = 8 nM 8.0 [] unit_conversion 8.096910013008056 success True direct_binding ITC measurement of mSCGN binding to the C-terminal helix of mouse SNAP-25. 4 Fig. 2 caption: “Kd = 8 nM was calculated for the interaction between mSCGN and the C-terminal helix of mouse SNAP-25 by ITC.” auto_single_measurement only accepted activity measurement [1] 1 structures\8BAN\8BAN_metadata.json point structures/8BAN/8ban_protein.pdb structures/8BAN/8ban_pocket.pdb structures/8BAN/8ban_ligand.pdb structures/8BAN/8ban_ligand.cif structures/8BAN/8ban_complex.pdb structures/8BAN/8ban_complex.cif 8BBJ extended Secretagogin mouse Mouse secretagogin BC module (residues 90-276) with GFP fused to the Syntaxin-4-derived peptide Na Syntaxin-4-derived peptide (residues 82-109) "[""CHAIN:A"", ""CHAIN:B""]" 1 Kd Kd = = 826 nM 826.0 [] unit_conversion 6.083019952679617 success True direct_binding Binding of mSCGN to a GFP-fusion construct carrying the 28-amino-acid syntaxin-4 peptide. 5 “A 28 AA-long peptide (82-GLQN...-109; as GFP-fusion tag termed GFPmSTX4Hb10) was the shortest segment that still exhibited nM binding (Kd = 826 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8BBJ\8BBJ_metadata.json point structures/8BBJ/8bbj_protein.pdb structures/8BBJ/8bbj_pocket.pdb structures/8BBJ/8bbj_ligand.pdb structures/8BBJ/8bbj_ligand.cif structures/8BBJ/8bbj_complex.pdb structures/8BBJ/8bbj_complex.cif 8BBS classic Human aldoketo reductase 1C3 (AKR1C3) human AKR1C3 residues 6-323 in chain A and 6-319 in chain B; recombinant N-terminal His6-tagged construct subjected to thrombin cleavage before crystallization Na Compound 2, a bile acid fused tetrazole inhibitor "[""QBO""]" 1 IC50 IC50 ~ ~ 7 µM 7000.0 [] unit_conversion 5.154901959985743 success True biochemical_inhibition NADPH fluorescence spectroscopy dose-response assay monitoring AKR1C3 reduction of 9,10-phenanthrenequinone; compound 2 tested from 0 to 100 µM. 3 “compound 2 inhibits AKR1C3 reduction of PQ in a dose-dependent manner, with a resulting calculated IC50 value of ~7 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8BBS\8BBS_metadata.json point structures/8BBS/8bbs_protein.pdb structures/8BBS/8bbs_pocket.pdb structures/8BBS/8bbs_ligand.sdf structures/8BBS/8bbs_ligand.pdb structures/8BBS/8bbs_ligand.cif structures/8BBS/8bbs_complex.pdb structures/8BBS/8bbs_complex.cif 8BC7 extended Cereblon isoform 4 Magnetospirillum gryphiswaldense isoform 4 Na KFFEQMQcQ peptide; C-terminal aminoglutarimide degron peptide "[""CHAIN:D""]" 2 Ki Ki = = 3.82 ± 1.34 μM 3820.0 [] unit_conversion 5.417936637088291 success True direct_binding Competitive microscale thermophoresis assay against BODIPY-uracil reporter. 5 Fig. 3B explicitly reports Ki = 3.82 ± 1.34 μM for KFFEQMQcQ with MsCI4. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8BC7\8BC7_metadata.json point structures/8BC7/8bc7_protein.pdb structures/8BC7/8bc7_pocket.pdb structures/8BC7/8bc7_ligand.pdb structures/8BC7/8bc7_ligand.cif structures/8BC7/8bc7_complex.pdb structures/8BC7/8bc7_complex.cif 8BDI classic VCB Na Na Na compound 32 "[""QF7""]" 2 Kd Kd = = 0.052 µM 52.0 [] unit_conversion 7.2839966563652006 success True direct_binding ITC equilibrium binding to VHL 6 Table 6 reports compound 32: Kd 0.052 µM; Table 1 footnote specifies Kd values were determined by ITC. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8BDI\8BDI_metadata.json point structures/8BDI/8bdi_protein.pdb structures/8BDI/8bdi_pocket.pdb structures/8BDI/8bdi_ligand.sdf structures/8BDI/8bdi_ligand.pdb structures/8BDI/8bdi_ligand.cif structures/8BDI/8bdi_complex.pdb structures/8BDI/8bdi_complex.cif 8BDJ classic VCB Na Na Na compound 30 "[""QE0""]" 2 Kd Kd = = 0.093 µM 93.0 [] unit_conversion 7.031517051446065 success True direct_binding ITC equilibrium binding to VHL 4 Table 5 reports compound 30: Kd 0.093 µM; the paper defines its Kd values as ITC determinations. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8BDJ\8BDJ_metadata.json point structures/8BDJ/8bdj_protein.pdb structures/8BDJ/8bdj_pocket.pdb structures/8BDJ/8bdj_ligand.sdf structures/8BDJ/8bdj_ligand.pdb structures/8BDJ/8bdj_ligand.cif structures/8BDJ/8bdj_complex.pdb structures/8BDJ/8bdj_complex.cif 8BDL classic VCB Na Na Na compound 27 "[""QF3""]" 2 Kd Kd = = 0.003 µM 3.0 [] unit_conversion 8.522878745280337 success True direct_binding ITC equilibrium binding to VHL 4 Table 5 reports compound 27: Kd 0.003 µM; Kd values are defined as ITC determinations. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8BDL\8BDL_metadata.json point structures/8BDL/8bdl_protein.pdb structures/8BDL/8bdl_pocket.pdb structures/8BDL/8bdl_ligand.sdf structures/8BDL/8bdl_ligand.pdb structures/8BDL/8bdl_ligand.cif structures/8BDL/8bdl_complex.pdb structures/8BDL/8bdl_complex.cif 8BDM classic VCB Na Na Na compound 26 "[""QE9""]" 2 Kd Kd = = 0.006 µM 6.0 [] unit_conversion 8.221848749616356 success True direct_binding ITC equilibrium binding to VHL 4 Table 5 reports compound 26: Kd 0.006 µM; Kd values are defined as ITC determinations. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8BDM\8BDM_metadata.json point structures/8BDM/8bdm_protein.pdb structures/8BDM/8bdm_pocket.pdb structures/8BDM/8bdm_ligand.sdf structures/8BDM/8bdm_ligand.pdb structures/8BDM/8bdm_ligand.cif structures/8BDM/8bdm_complex.pdb structures/8BDM/8bdm_complex.cif 8BDO classic VCB Na Na Na compound 21 "[""QFF""]" 2 Kd Kd = = 0.11 µM 110.0 [] unit_conversion 6.958607314841775 success True direct_binding ITC equilibrium binding to VHL 3 Table 4 reports compound 21: Kd 0.11 µM; the paper defines Kd values as ITC determinations. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8BDO\8BDO_metadata.json point structures/8BDO/8bdo_protein.pdb structures/8BDO/8bdo_pocket.pdb structures/8BDO/8bdo_ligand.sdf structures/8BDO/8bdo_ligand.pdb structures/8BDO/8bdo_ligand.cif structures/8BDO/8bdo_complex.pdb structures/8BDO/8bdo_complex.cif 8BGC classic Human Casein Kinase II subunit alpha (CK2a1) human Na Na compound 2 (AA-CS-9-003) "[""QIA""]" 1 IC50 IC50 = = 3.0 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Enzymatic CK2α assay; Figure 2 nested table reports the enzymatic and NanoBRET IC50 values separately as 3.0 and 920 nM, respectively. 3 Figure 2 lists CK2α, assay format “Enzymatic and NB”, with “IC50 value (nM)” of “3.0 and 920”; the enzymatic value is 3.0 nM and the NanoBRET value is cellular and excluded. auto_single_measurement only accepted activity measurement [1] 1 structures\8BGC\8BGC_metadata.json point structures/8BGC/8bgc_protein.pdb structures/8BGC/8bgc_pocket.pdb structures/8BGC/8bgc_ligand.sdf structures/8BGC/8bgc_ligand.pdb structures/8BGC/8bgc_ligand.cif structures/8BGC/8bgc_complex.pdb structures/8BGC/8bgc_complex.cif 8BI7 extended 14-3-3sigma Na Na Na PKR phosphopeptide "[""CHAIN:B""]" 1 Kd Kd = = 180 nM 180.0 [] unit_conversion 6.7447274948966935 success True direct_binding Binary phosphopeptide affinity obtained from fluorescence-anisotropy studies and used in the competitive-environment equilibrium model. 9 “The highest-affinity peptide, PKR (KD = 180 nM), occupied 61% of the total 14-3-3 population.” The paper states the peptide affinities used in this model were based on FA studies. auto_single_measurement only accepted activity measurement [1] 1 structures\8BI7\8BI7_metadata.json point structures/8BI7/8bi7_protein.pdb structures/8BI7/8bi7_pocket.pdb structures/8BI7/8bi7_ligand.pdb structures/8BI7/8bi7_ligand.cif structures/8BI7/8bi7_complex.pdb structures/8BI7/8bi7_complex.cif 8BJD classic Legionella pneumophila MIP (LpMIP) Legionella pneumophila LpMIP residues 1-213 (full length) Na JK095 "[""9QN""]" 1 Kd Kd = = 1.27 ± 0.14 µM 1270.0 [] unit_conversion 5.896196279044043 success True direct_binding Isothermal titration calorimetry (ITC) of JK095 binding to full-length LpMIP. 2 “ITC confirmed that JK095 indeed interacts with microbial MIP proteins and LpMIP variants ... and binds to full-length LpMIP with a dissociation constant of 1.27 ± 0.14 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\8BJD\8BJD_metadata.json point structures/8BJD/8bjd_protein.pdb structures/8BJD/8bjd_pocket.pdb structures/8BJD/8bjd_ligand.sdf structures/8BJD/8bjd_ligand.pdb structures/8BJD/8bjd_ligand.cif structures/8BJD/8bjd_complex.pdb structures/8BJD/8bjd_complex.cif 8BJE classic Legionella pneumophila MIP (LpMIP) Legionella pneumophila LpMIP residues 77-213 Na JK236 "[""WRL""]" 1 Kd Kd = = 123.5 ± 47.4 nM 123.5 [] unit_conversion 6.9083330424043154 success True direct_binding ITC binding measurement for methylated inhibitor JK236 and LpMIP77–213. 8 “the binding affinity of JK236 to LpMIP77–213 ... was increased by roughly one order of magnitude with the methylated (Kd = 123.5 ± 47.4 nM ...)”. auto_single_measurement only accepted activity measurement [1] 1 structures\8BJE\8BJE_metadata.json point structures/8BJE/8bje_protein.pdb structures/8BJE/8bje_pocket.pdb structures/8BJE/8bje_ligand.sdf structures/8BJE/8bje_ligand.pdb structures/8BJE/8bje_ligand.cif structures/8BJE/8bje_complex.pdb structures/8BJE/8bje_complex.cif 8BJK classic histone deacetylase 6 (HDAC6) Danio rerio zHDAC6 residues 440-798 Na compound 4 (hydrolysis product; CPD11352/PDB component QXF) "[""QXF""]" 1 IC50 IC50 = = 3866 ± 1644 nM 3866.0 [] unit_conversion 5.412738150307465 success True biochemical_inhibition Purified zebrafish HDAC6 catalytic DD2-domain inhibition assay. 3 Table 1 reports compound 4 IC50 3866 ± 1644 nM for wild-type zHDAC6. auto_single_measurement only accepted activity measurement [1] 1 structures\8BJK\8BJK_metadata.json point structures/8BJK/8bjk_protein.pdb structures/8BJK/8bjk_pocket.pdb structures/8BJK/8bjk_ligand.sdf structures/8BJK/8bjk_ligand.pdb structures/8BJK/8bjk_ligand.cif structures/8BJK/8bjk_complex.pdb structures/8BJK/8bjk_complex.cif 8BJU classic human WEE1 kinase human Na Na compound 20; 1-[6-(1-hydroxy-1-methyl-ethyl)-pyridin-2-yl]-2-(2-methoxy-phenyl)-6-[4-(4-methyl-piperazin-1-yl)-phenylamino]-1,2-dihydro-pyrazolo[3,4-d]pyrimidin-3-one "[""QT9""]" 1 IC50 IC50 = = 9.6 nM 9.6 [] unit_conversion 8.017728766960431 success True biochemical_inhibition Wee1 enzymatic IC50 reported in Table 1 for compound 20. 4 Table 1 reports compound 20: Wee1 IC50 = 9.6 nM. Page 5 identifies PDB 8BJU as Wee1 with compound 20 bound in the ATP pocket. auto_single_measurement only accepted activity measurement [1] 1 structures\8BJU\8BJU_metadata.json point structures/8BJU/8bju_protein.pdb structures/8BJU/8bju_pocket.pdb structures/8BJU/8bju_ligand.sdf structures/8BJU/8bju_ligand.pdb structures/8BJU/8bju_ligand.cif structures/8BJU/8bju_complex.pdb structures/8BJU/8bju_complex.cif 8BJX extended human Carbonic anhydrase II human Na Na (R)-37a; (R)-4-(3-(1-(6-nitropyridin-2-yl)pyrrolidin-3-yl)thioureido)benzenesulfonamide "[""QKO""]" 1 Ki Ki = = 6.7 nM 6.7 [] unit_conversion 8.173925197299173 success True biochemical_inhibition Stopped-flow CO2 hydration inhibition assay. 6 Table 1 reports Ki = 6.7 nM for compound 37a against hCA II; the table title identifies a stopped-flow CO2 hydrase assay. Figure 3 identifies 8BJX as hCA II bound to (R)-37a. auto_single_measurement only accepted activity measurement [1] 1 structures\8BJX\8BJX_metadata.json point structures/8BJX/8bjx_ligand.sdf structures/8BJX/8bjx_ligand.cif structures/8BJX/8bjx_complex.cif 8BK5 classic Legionella pneumophila MIP (LpMIP) Legionella pneumophila LpMIP residues 77-213 Na JK095 "[""9QN""]" 1 Kd Kd = = 2.27 ± 0.01 µM 2270.0 [] unit_conversion 5.6439741428068775 success True direct_binding ITC binding measurement for JK095 and LpMIP77–213. 4 “LpMIP100–213 (Kd = 20.47 ± 4.48 μM) compared to LpMIP77–213 (Kd = 2.27 ± 0.01 μM) and full-length LpMIP (Kd = 1.27 ± 0.14 μM)”. auto_single_measurement only accepted activity measurement [1] 1 structures\8BK5\8BK5_metadata.json point structures/8BK5/8bk5_protein.pdb structures/8BK5/8bk5_pocket.pdb structures/8BK5/8bk5_ligand.sdf structures/8BK5/8bk5_ligand.pdb structures/8BK5/8bk5_ligand.cif structures/8BK5/8bk5_complex.pdb structures/8BK5/8bk5_complex.cif 8BM2 classic JAK2 human kinase domain, amino acids 840-1132 Na gandotinib "[""QQC""]" 1 Kd Kd = = 11 nM 11.0 [] unit_conversion 7.958607314841775 success True direct_binding Fluorescence-polarization binding assay; Table 1. 2 Table 1 reports JAK2 binding Kd = 11 nM for gandotinib. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 3] 3 structures\8BM2\8BM2_metadata.json point structures/8BM2/8bm2_protein.pdb structures/8BM2/8bm2_pocket.pdb structures/8BM2/8bm2_ligand.sdf structures/8BM2/8bm2_ligand.pdb structures/8BM2/8bm2_ligand.cif structures/8BM2/8bm2_complex.pdb structures/8BM2/8bm2_complex.cif 8BO4 extended coagulation factor XI protease domain human Na Na compound 1 "[""QVI""]" 1 IC50 IC50 = = 9 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition FXIa inhibition. 2 Figure 1 labels compound 1 as “FXIa IC50 = 9 nM” and identifies its human FXIa complex as PDB 8BO4. auto_single_measurement only accepted activity measurement [1] 1 structures\8BO4\8BO4_metadata.json point structures/8BO4/8bo4_ligand.cif structures/8BO4/8bo4_complex.cif 8BO5 extended coagulation factor XI protease domain human Na Na compound 3 "[""QVO""]" 1 IC50 IC50 = = 930 nM 930.0 [] unit_conversion 6.031517051446064 success True biochemical_inhibition FXIa inhibition. 4 Figure 3 labels hit 3 as “FXIa IC50 = 930 nM” and identifies the human FXIa cocrystal structure as PDB 8BO5. auto_single_measurement only accepted activity measurement [1] 1 structures\8BO5\8BO5_metadata.json point structures/8BO5/8bo5_ligand.cif structures/8BO5/8bo5_complex.cif 8BO6 extended coagulation factor XI protease domain human Na Na compound 2 "[""QW0""]" 1 IC50 IC50 = = 4 nM 4.0 [] unit_conversion 8.397940008672037 success True biochemical_inhibition FXIa inhibition. 3 Figure 2 labels compound 2 as “FXIa IC50 = 4 nM” and identifies its human FXIa complex as PDB 8BO6. auto_single_measurement only accepted activity measurement [1] 1 structures\8BO6\8BO6_metadata.json point structures/8BO6/8bo6_ligand.cif structures/8BO6/8bo6_complex.cif 8BO7 extended coagulation factor XI protease domain human Na Na compound 34 "[""QW6""]" 1 IC50 IC50 = = 0.5 nM 0.5 [] unit_conversion 9.301029995663981 success True biochemical_inhibition Direct, reversible FXIa inhibition in buffer. 8 The text states that compound 34 inhibited human FXIa directly, reversibly, potently, and selectively with IC50 of 0.5 nM in buffer; Figure 5 identifies its complex as PDB 8BO7. auto_single_measurement only accepted activity measurement [1] 1 structures\8BO7\8BO7_metadata.json point structures/8BO7/8bo7_ligand.sdf structures/8BO7/8bo7_ligand.cif structures/8BO7/8bo7_complex.cif 8BO8 classic glutamate carboxypeptidase II (GCPII) human extracellular part of human PSMA, amino acids 44-750 Na P17 "[""QWF""]" 1 IC50 IC50 = = 0.30 ± 0.04 nM 0.3 [] unit_conversion 9.522878745280337 success True biochemical_inhibition HPLC-based in vitro PSMA enzyme assay using fluorescein-γ-Glu-Glu substrate. 3 Table 2 reports a PSMA IC50 of 0.30 ± 0.04 nM for P17; the text specifies recombinant human PSMA and an HPLC-based assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8BO8\8BO8_metadata.json point structures/8BO8/8bo8_protein.pdb structures/8BO8/8bo8_pocket.pdb structures/8BO8/8bo8_ligand.sdf structures/8BO8/8bo8_ligand.pdb structures/8BO8/8bo8_ligand.cif structures/8BO8/8bo8_complex.pdb structures/8BO8/8bo8_complex.cif 8BOL classic glutamate carboxypeptidase II (GCPII) human extracellular part of human PSMA, amino acids 44-750 Na P18 "[""A1J0C""]" 1 IC50 IC50 = = 0.45 ± 0.09 nM 0.45 [] unit_conversion 9.346787486224656 success True biochemical_inhibition HPLC-based in vitro PSMA enzyme assay using fluorescein-γ-Glu-Glu substrate. 3 Table 2 reports a PSMA IC50 of 0.45 ± 0.09 nM for P18; the text specifies recombinant human PSMA and an HPLC-based assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8BOL\8BOL_metadata.json point structures/8BOL/8bol_protein.pdb structures/8BOL/8bol_pocket.pdb structures/8BOL/8bol_ligand.sdf structures/8BOL/8bol_ligand.pdb structures/8BOL/8bol_ligand.cif structures/8BOL/8bol_complex.pdb structures/8BOL/8bol_complex.cif 8BOW classic glutamate carboxypeptidase II (GCPII) human extracellular part of human PSMA, amino acids 44-750 Na 617 (PSMA-617) "[""QYF""]" 1 IC50 IC50 = = 0.05 ± 0.03 nM 0.05 [] unit_conversion 10.301029995663981 success True biochemical_inhibition HPLC-based in vitro PSMA enzyme assay using fluorescein-γ-Glu-Glu substrate. 3 Table 2 reports a PSMA IC50 of 0.05 ± 0.03 nM for PSMA-617; the text specifies recombinant human PSMA and an HPLC-based assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8BOW\8BOW_metadata.json point structures/8BOW/8bow_protein.pdb structures/8BOW/8bow_pocket.pdb structures/8BOW/8bow_ligand.sdf structures/8BOW/8bow_ligand.pdb structures/8BOW/8bow_ligand.cif structures/8BOW/8bow_complex.pdb structures/8BOW/8bow_complex.cif 8BPY classic PDE9A Na Na Na Inhibitor 13A "[""R4I""]" 1 IC50 IC50 = = 3 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition PDE9A inhibition; Figure 4 labels inhibitor 13A with PDE9A-IC50 3 nM. The paper states IC50 values versus human PDE9A were measured using a scintillation proximity assay with 3H-cGMP substrate. 4 Figure 4: “Inhibitor 13A PDE9A-IC50 3 nM”; caption identifies the X-ray cocrystal structure of 13A in PDE9A, deposited as PDB 8BPY. auto_single_measurement only accepted activity measurement [1] 1 structures\8BPY\8BPY_metadata.json point structures/8BPY/8bpy_protein.pdb structures/8BPY/8bpy_pocket.pdb structures/8BPY/8bpy_ligand.sdf structures/8BPY/8bpy_ligand.pdb structures/8BPY/8bpy_ligand.cif structures/8BPY/8bpy_complex.pdb structures/8BPY/8bpy_complex.cif 8BR5 extended IRAK4 Na Na Na compound 41 "[""R73""]" 1 IC50 IC50 = = 43 nM 43.0 [] unit_conversion 7.366531544420414 success True biochemical_inhibition Biochemical potency of IRAK4 inhibition at 1 mM ATP. 10 Table 9 reports compound 41 IRAK4 IC50 = 43 nM; its footnote specifies 1 mM ATP. The accession-code list maps PDB 8BR5 to compound 41 (page 16). auto_single_measurement only accepted activity measurement [1] 1 structures\8BR5\8BR5_metadata.json point structures/8BR5/8br5_ligand.cif structures/8BR5/8br5_complex.cif 8BR6 extended IRAK4 Na Na Na compound 40 "[""R6I""]" 1 IC50 IC50 = = 8 nM 8.0 [] unit_conversion 8.096910013008056 success True biochemical_inhibition Biochemical potency of IRAK4 inhibition at 1 mM ATP. 10 Table 9 reports compound 40 IRAK4 IC50 = 8 nM; its footnote specifies 1 mM ATP. Figure 5 identifies PDB 8BR6 as the IRAK4 cocrystal structure of compound 40 (page 9), and the accession-code list confirms this mapping (page 16). auto_single_measurement only accepted activity measurement [1] 1 structures\8BR6\8BR6_metadata.json point structures/8BR6/8br6_ligand.sdf structures/8BR6/8br6_ligand.cif structures/8BR6/8br6_complex.cif 8BR7 extended IRAK4 Na Na Na compound 5 "[""R6R""]" 1 IC50 IC50 = = 212 nM 212.0 [] unit_conversion 6.673664139071249 success True biochemical_inhibition Biochemical potency of IRAK4 inhibition at 1 mM ATP. 3 Table 1 reports compound 5 IRAK4 IC50 = 212 nM; its footnote specifies 1 mM ATP. The accession-code list maps PDB 8BR7 to compound 5 (page 16). auto_single_measurement only accepted activity measurement [1] 1 structures\8BR7\8BR7_metadata.json point structures/8BR7/8br7_ligand.sdf structures/8BR7/8br7_ligand.cif structures/8BR7/8br7_complex.cif 8BRO classic BC2L-C lectin Burkholderia cenocepacia N-terminal domain, residues 1-131 Na compound 3 (synthetic beta-L-fucosylamide) "[""R7E""]" 1 Kd Kd = = 159 ± 7 μM 159000.0 [] unit_conversion 3.7986028756795482 success True direct_binding Isothermal titration calorimetry at 25 °C; Table 1 affinity measurement. 7 Table 1 reports ligand 3 with K_D 159 ± 7 μM. The text identifies compound 3 as the ligand in the BC2L-C-Nt complex deposited as PDB 8BRO. auto_single_measurement only accepted activity measurement [1] 1 structures\8BRO\8BRO_metadata.json point structures/8BRO/8bro_protein.pdb structures/8BRO/8bro_pocket.pdb structures/8BRO/8bro_ligand.sdf structures/8BRO/8bro_ligand.pdb structures/8BRO/8bro_ligand.cif structures/8BRO/8bro_complex.pdb structures/8BRO/8bro_complex.cif 8BRV classic methionyl-tRNA synthetase Escherichia coli Na L13M,I297C beta3-methionine "[""B3M""]" 1 Kd Kd = = 0.9 (3) mM 900000.0 [] unit_conversion 3.045757490560675 success True direct_binding Fluorescence equilibrium dissociation-constant measurement for MAC MetRS. 5 Table 2 reports Kd (β-Met) = 0.9 (3) mM for MAC; MAC is L13M,I297C. auto_single_measurement only accepted activity measurement [1] 1 structures\8BRV\8BRV_metadata.json point structures/8BRV/8brv_protein.pdb structures/8BRV/8brv_pocket.pdb structures/8BRV/8brv_ligand.sdf structures/8BRV/8brv_ligand.pdb structures/8BRV/8brv_ligand.cif structures/8BRV/8brv_complex.pdb structures/8BRV/8brv_complex.cif 8BRX classic methionyl-tRNA synthetase Escherichia coli Na L13C,I297C beta-3-methionine "[""B3M""]" 1 Kd Kd = = 0.9 (2) mM 900000.0 [] unit_conversion 3.045757490560675 success True direct_binding Fluorescence equilibrium dissociation-constant measurement for CAC MetRS. 5 Table 2 reports Kd (β-Met) = 0.9 (2) mM for CAC; CAC is L13C,I297C. auto_single_measurement only accepted activity measurement [1] 1 structures\8BRX\8BRX_metadata.json point structures/8BRX/8brx_protein.pdb structures/8BRX/8brx_pocket.pdb structures/8BRX/8brx_ligand.sdf structures/8BRX/8brx_ligand.pdb structures/8BRX/8brx_ligand.cif structures/8BRX/8brx_complex.pdb structures/8BRX/8brx_complex.cif 8BSK classic human GLS human Na Na compound 3 "[""04A""]" 1 IC50 IC50 = = 0.135 μM 135.0 [] unit_conversion 6.8696662315049934 success True biochemical_inhibition GLS1 enzyme inhibition assay; Table 1 states the biochemical assay employs the KGA GLS1 splice variant. 12 Table 1 reports GLS1 enzyme IC50 = 0.135 μM for (BPTES) compound 3. auto_single_measurement only accepted activity measurement [1] 1 structures\8BSK\8BSK_metadata.json point structures/8BSK/8bsk_protein.pdb structures/8BSK/8bsk_pocket.pdb structures/8BSK/8bsk_ligand.sdf structures/8BSK/8bsk_ligand.pdb structures/8BSK/8bsk_ligand.cif structures/8BSK/8bsk_complex.pdb structures/8BSK/8bsk_complex.cif 8BSL classic human GLS human Na Na compound 12 "[""R90""]" 1 IC50 IC50 = = 0.014 μM 14.0 [] unit_conversion 7.853871964321762 success True biochemical_inhibition GLS1 enzyme inhibition assay; the Table 2 series follows the stated KGA GLS1 biochemical assay. 13 Table 2 reports GLS1 enzyme IC50 = 0.014 μM for compound 12. auto_single_measurement only accepted activity measurement [1] 1 structures\8BSL\8BSL_metadata.json point structures/8BSL/8bsl_protein.pdb structures/8BSL/8bsl_pocket.pdb structures/8BSL/8bsl_ligand.sdf structures/8BSL/8bsl_ligand.pdb structures/8BSL/8bsl_ligand.cif structures/8BSL/8bsl_complex.pdb structures/8BSL/8bsl_complex.cif 8BSM classic human GLS human Na Na compound 18 "[""5XX""]" 1 IC50 IC50 = = 0.347 μM 347.0 [] unit_conversion 6.459670525209127 success True biochemical_inhibition GLS1 enzyme inhibition assay reported in Table 4. 17 Table 4 reports GLS1 enzyme IC50 = 0.347 μM for compound 18. auto_single_measurement only accepted activity measurement [1] 1 structures\8BSM\8BSM_metadata.json point structures/8BSM/8bsm_protein.pdb structures/8BSM/8bsm_pocket.pdb structures/8BSM/8bsm_ligand.sdf structures/8BSM/8bsm_ligand.pdb structures/8BSM/8bsm_ligand.cif structures/8BSM/8bsm_complex.pdb structures/8BSM/8bsm_complex.cif 8BU1 extended DDB1-CDK12-cyclin K Homo sapiens Na Na DS17 "[""RQL""]" 1 Kd Kd < < 1 nM 1.0 [] unit_conversion 9.0 success True direct_binding TR-FRET ternary-complex assay; 50 nM CDK12-cyclin K and 100 nM DDB1. 21 Extended Data Fig. 6b reports DS17 TR-FRET Kd <1 nM at 50 nM CDK12-cyclin K + 100 nM DDB1. auto_single_measurement only accepted activity measurement [1] 1 structures\8BU1\8BU1_metadata.json point structures/8BU1/8bu1_protein.pdb structures/8BU1/8bu1_pocket.pdb structures/8BU1/8bu1_ligand.pdb structures/8BU1/8bu1_ligand.cif structures/8BU1/8bu1_complex.pdb structures/8BU1/8bu1_complex.cif 8BUN classic DDB1-CDK12-cyclin K complex Homo sapiens DDB1DeltaBPB with residues 396-705 deleted; CDK12 residues 713-1052; cyclin K residues 1-267; affinity tags removed for crystallography Na DS16 (compound 2) "[""RNF""]" 1 Kd Kd = = 6 ± 2 nM 6.0 [] unit_conversion 8.221848749616356 success True direct_binding TR-FRET complex-formation assay with 50 nM CDK12–cyclin K and 100 nM DDB1. 21 Extended Data Fig. 6b prints “TR-FRET Kd [nM]” and lists DS16 as 6 ± 2 in the 50 nM CDK12–cyclin K + 100 nM DDB1 assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8BUN\8BUN_metadata.json point structures/8BUN/8bun_protein.pdb structures/8BUN/8bun_pocket.pdb structures/8BUN/8bun_ligand.sdf structures/8BUN/8bun_ligand.pdb structures/8BUN/8bun_ligand.cif structures/8BUN/8bun_complex.pdb structures/8BUN/8bun_complex.cif 8BV1 extended ASF1A histone chaperone Human ASF1A_N, N-terminal conserved domain Na P4 "[""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I"", ""CHAIN:K"", ""CHAIN:L"", ""CHAIN:N""]" 1 Kd Kd = = 0.20 ± 0.09 µM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Isothermal titration calorimetry (ITC) measurement of peptide P4 binding to ASF1A_N. 2 Peptide P4 is reported with K_D = 0.20 ± 0.09 µM; Figure 2 states that displayed K_D values were determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8BV1\8BV1_metadata.json point structures/8BV1/8bv1_protein.pdb structures/8BV1/8bv1_pocket.pdb structures/8BV1/8bv1_ligand.pdb structures/8BV1/8bv1_ligand.cif structures/8BV1/8bv1_complex.pdb structures/8BV1/8bv1_complex.cif 8BWU classic SARS-CoV-2 nsp14 methyltransferase domain SARS-CoV-2 nsp14 methyltransferase domain, residues 300-527, with N-terminal His6-SUMO-TELSAM fusion tags Na SS148 "[""6NR""]" 1 IC50 IC50 = = 70 ± 6 nM 70.0 [] unit_conversion 7.154901959985743 success True biochemical_inhibition Radiometric MTase-activity inhibition assay; SS148 is reported as a potent inhibitor of nsp14 methyltransferase activity. 1 “SS148 (PDB:8BWU), a potent inhibitor of methyltransferase activity at the nanomolar level (IC50 value of 70 ± 6 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8BWU\8BWU_metadata.json point structures/8BWU/8bwu_protein.pdb structures/8BWU/8bwu_pocket.pdb structures/8BWU/8bwu_ligand.sdf structures/8BWU/8bwu_ligand.pdb structures/8BWU/8bwu_ligand.cif structures/8BWU/8bwu_complex.pdb structures/8BWU/8bwu_complex.cif 8BXY extended FimH fimbrial adhesin Escherichia coli FimH lectin domain, residues Phe1-Thr158 Na alpha1,6 core-fucosylated oligomannose-3 (Man3Gn2F1[6]) "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 118 nM 118.0 [] unit_conversion 6.928117992693874 success True direct_binding SPR binding to immobilized glycan ligand; Langmuir 1:1 fit. 5 Table 1 reports Kd = 118 nM for glycan Man3Gn2F1[6]. Data availability identifies 8BXY as the STARANISO processing entry for the same FimH–Man3Gn2F1[6] structure as 7BHD. auto_single_measurement only accepted activity measurement [1] 1 structures\8BXY\8BXY_metadata.json point structures/8BXY/8bxy_protein.pdb structures/8BXY/8bxy_pocket.pdb structures/8BXY/8bxy_ligand.pdb structures/8BXY/8bxy_ligand.cif structures/8BXY/8bxy_complex.pdb structures/8BXY/8bxy_complex.cif 8BZ7 classic RmlT Listeria monocytogenes full-length RmlT wild-type TDP-rhamnose "[""TRH""]" 2 Kd Kd = = 4.71 ± 2.34 µM 4710.0 [] unit_conversion 5.326979092871104 success True direct_binding ITC measurement of recombinant RmlT/donor-substrate interactions; MgCl2 was present in the dialysis buffer. 8 Fig. 5b prints the RmlT/TDP-rhamnose ITC fit K_D as 4.71 ± 2.34 µM. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\8BZ7\8BZ7_metadata.json point structures/8BZ7/8bz7_protein.pdb structures/8BZ7/8bz7_pocket.pdb structures/8BZ7/8bz7_ligand.sdf structures/8BZ7/8bz7_ligand.pdb structures/8BZ7/8bz7_ligand.cif structures/8BZ7/8bz7_complex.pdb structures/8BZ7/8bz7_complex.cif 8BZP classic JNK3 (Mitogen-activated protein kinase 10) Na JNK3 residues 39-402 Na compound 23 "[""SWM""]" 1 Kd Kd = = 17 ± 2 µM 17000.0 [] unit_conversion 4.769551078621726 success True direct_binding ITC validation against purified JNK3; Table 6 reports compound 23. 13 Table 6 reports compound 23 (Br) with JNK3 Kd = 17 ± 2 µM. The table is titled biophysical measurements using STD NMR and ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8BZP\8BZP_metadata.json point structures/8BZP/8bzp_protein.pdb structures/8BZP/8bzp_pocket.pdb structures/8BZP/8bzp_ligand.sdf structures/8BZP/8bzp_ligand.pdb structures/8BZP/8bzp_ligand.cif structures/8BZP/8bzp_complex.pdb structures/8BZP/8bzp_complex.cif 8BZS classic rabbit muscle glycogen phosphorylase b (rmGPb) rabbit Na Na baicalein "[""3WL""]" 1 Ki Ki = = 5.66 ± 0.18 µM 5660.0 [] unit_conversion 5.247183568811728 success True biochemical_inhibition Purified rmGPb kinetic inhibition assay in the direction of glycogen synthesis. 2 Table 1 reports baicalein Ki = 5.66 ± 0.18 µM for rmGPb; the table footnote identifies this as the glycogen-synthesis direction. auto_single_measurement only accepted activity measurement [1] 1 structures\8BZS\8BZS_metadata.json point structures/8BZS/8bzs_protein.pdb structures/8BZS/8bzs_pocket.pdb structures/8BZS/8bzs_ligand.sdf structures/8BZS/8bzs_ligand.pdb structures/8BZS/8bzs_ligand.cif structures/8BZS/8bzs_complex.pdb structures/8BZS/8bzs_complex.cif 8BZX classic 1-deoxy-D-xylulose 5-phosphate synthase (DXPS; kpDXPS) Klebsiella pneumoniae Na Na compound 8b (thiamine monophosphate analog) "[""SW6""]" 1 Ki Ki = = 60 nM 60.0 [] unit_conversion 7.221848749616356 success True biochemical_inhibition ThDP-competitive inhibition; Table 2 DXPS determination. Ki calculated using [ThDP]/IC50 = Km(ThDP)/Ki; DXPS assay used 50 nM ThDP. 5 Table 2 reports compound 8b (R = Et) with DXPS Ki = 60 nM. Its footnote states that Ki values were calculated for ThDP-competitive inhibitors and gives the DXPS ThDP concentration; the text identifies the crystallized 8b complex as Klebsiella pneumoniae DXPS. auto_single_measurement only accepted activity measurement [1] 1 structures\8BZX\8BZX_metadata.json point structures/8BZX/8bzx_protein.pdb structures/8BZX/8bzx_pocket.pdb structures/8BZX/8bzx_ligand.sdf structures/8BZX/8bzx_ligand.pdb structures/8BZX/8bzx_ligand.cif structures/8BZX/8bzx_complex.pdb structures/8BZX/8bzx_complex.cif 8BZZ extended human carbonic anhydrase II (hCA II) human Na Na compound 4; 4-(dimethylamino)-N-nitrobenzenesulfonamide "[""SVO""]" 1 Ki Ki = = 64.2 µM 64200.0 [] unit_conversion 4.192464971931146 success True biochemical_inhibition CO₂ hydrase inhibition assay; Table 1 reports inhibition data for human CA isoforms, with values stated as means from three assays by stopped-flow technique. 3 Table 1 lists compound 4 with Ki = 64.2 µM against hCA II. The table caption specifies human CA isoforms and the footnote states values are means from three stopped-flow assays. auto_single_measurement only accepted activity measurement [1] 1 structures\8BZZ\8BZZ_metadata.json point structures/8BZZ/8bzz_ligand.sdf structures/8BZZ/8bzz_ligand.cif structures/8BZZ/8bzz_complex.cif 8C15 classic Aurora A kinase Na Na Na compound 3 (TPX2-inhibitor 3) "[""T4C""]" 1 Kd Kd = = 1.26 µM 1260.0 [] unit_conversion 5.899629454882437 success True direct_binding Competitive fluorescence-polarization assay; Figure 2. 3 Figure 2 prints for compound 3: FP K_D = 1.26 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8C15\8C15_metadata.json point structures/8C15/8c15_protein.pdb structures/8C15/8c15_pocket.pdb structures/8C15/8c15_ligand.sdf structures/8C15/8c15_ligand.pdb structures/8C15/8c15_ligand.cif structures/8C15/8c15_complex.pdb structures/8C15/8c15_complex.cif 8C17 extended TEAD4 human TEAD4 residues 217-434 Na peptide 1 "[""CHAIN:B""]" 1 Kd Kd = = 59 ± 1 nM 59.0 [] unit_conversion 7.229147988357855 success True direct_binding Surface-plasmon-resonance affinity measurement for peptide 1 binding immobilized TEAD4. 2 Table 1 reports compound 1 Kd = 59 ± 1 nM; the text identifies SPR as the method used to determine Kd values. auto_single_measurement only accepted activity measurement [1] 1 structures\8C17\8C17_metadata.json point structures/8C17/8c17_protein.pdb structures/8C17/8c17_pocket.pdb structures/8C17/8c17_ligand.pdb structures/8C17/8c17_ligand.cif structures/8C17/8c17_complex.pdb structures/8C17/8c17_complex.cif 8C1D classic Aurora A kinase Na Na Na Na "[""T2F""]" 1 Kd Kd = = 158 nM 158.0 [] unit_conversion 6.801342913045577 success True direct_binding Competitive fluorescence-polarization assay; Figure 2. 3 Figure 2 maps compound 4 to PDB 8C1D and prints FP K_D = 158 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8C1D\8C1D_metadata.json point structures/8C1D/8c1d_protein.pdb structures/8C1D/8c1d_pocket.pdb structures/8C1D/8c1d_ligand.sdf structures/8C1D/8c1d_ligand.pdb structures/8C1D/8c1d_ligand.cif structures/8C1D/8c1d_complex.pdb structures/8C1D/8c1d_complex.cif 8C1F classic Aurora A kinase Na Na Na compound 6 (TPX2-inhibitor 6) "[""T2O""]" 1 Kd Kd = = 200 nM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Competitive fluorescence-polarization assay; Figure 2. 3 Figure 2 prints for compound 6: FP K_D = 200 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8C1F\8C1F_metadata.json point structures/8C1F/8c1f_protein.pdb structures/8C1F/8c1f_pocket.pdb structures/8C1F/8c1f_ligand.sdf structures/8C1F/8c1f_ligand.pdb structures/8C1F/8c1f_ligand.cif structures/8C1F/8c1f_complex.pdb structures/8C1F/8c1f_complex.cif 8C1I classic Aurora A kinase Na Na Na compound 10 (TPX2-inhibitor 10) "[""T1L""]" 1 Kd Kd = = 18 nM 18.0 [] unit_conversion 7.7447274948966935 success True direct_binding Competitive fluorescence-polarization assay; Figure 2. 3 Figure 2 prints for compound 10: FP K_D = 18 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8C1I\8C1I_metadata.json point structures/8C1I/8c1i_protein.pdb structures/8C1I/8c1i_pocket.pdb structures/8C1I/8c1i_ligand.sdf structures/8C1I/8c1i_ligand.pdb structures/8C1I/8c1i_ligand.cif structures/8C1I/8c1i_complex.pdb structures/8C1I/8c1i_complex.cif 8C3C classic 14-3-3 sigma Na 14-3-3 sigma DeltaC (C-terminally truncated) Na Fusicoccin A (FC-A) "[""FSC""]" 1 Kd Kd = = 2.9 ± 0.2 µM 2900.0 [] unit_conversion 5.537602002101044 success True direct_binding td-FA assay at pH 7.5; FC-A used as a non-covalent control stabilizer. 2 In the presence of FC-A, rapid stabilization of the 14-3-3/Pin1 complex was observed (apparent KD = 2.9 ± 0.2 µM). auto_single_measurement only accepted activity measurement [1] 1 structures\8C3C\8C3C_metadata.json point structures/8C3C/8c3c_protein.pdb structures/8C3C/8c3c_pocket.pdb structures/8C3C/8c3c_ligand.sdf structures/8C3C/8c3c_ligand.pdb structures/8C3C/8c3c_ligand.cif structures/8C3C/8c3c_complex.pdb structures/8C3C/8c3c_complex.cif 8C3U classic human interleukin-1beta (hIL-1beta) human mature, proteolytically processed hIL-1beta starting at Ala1 (Ala117 of unprocessed protein) Na (S)-2 "[""T9C""]" 1 Kd Kd = = 1.1 ± 0.1 (N = 3) µM 1100.0 [] unit_conversion 5.958607314841775 success True direct_binding Surface plasmon resonance (SPR) binding of compound (S)-2 to hIL-1β. 3 Table 1 reports for (S)-2: SPR 1.1 ± 0.1 µM (N = 3). auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8C3U\8C3U_metadata.json point structures/8C3U/8c3u_protein.pdb structures/8C3U/8c3u_pocket.pdb structures/8C3U/8c3u_ligand.sdf structures/8C3U/8c3u_ligand.pdb structures/8C3U/8c3u_ligand.cif structures/8C3U/8c3u_complex.pdb structures/8C3U/8c3u_complex.cif 8C4P classic CdaA (Lm CdaA) Listeria monocytogenes Truncated Delta100CdaA; N-terminal GST fusion used for expression and removed during purification Na compound 7 "[""TJ9""]" 1 Kd Kd = = 16.3 ± 2.5 µM 16300.0 [] unit_conversion 4.787812395596042 success True direct_binding Isothermal titration calorimetry (ITC), 25°C; 50 µM CdaA in sample cell; compound 7 titrated in 20 mM Tris-HCl pH 7.5, 300 mM NaCl, with 2% DMSO; data fit with a 1:1 binding model. 8 Figure 4 caption states that ITC analysis of compound 7 binding to CdaA yielded a dissociation constant of Kd = 16.3 ± 2.5 µM; the page text confirms compound 7 binds CdaA. auto_single_measurement only accepted activity measurement [1] 1 structures\8C4P\8C4P_metadata.json point structures/8C4P/8c4p_protein.pdb structures/8C4P/8c4p_pocket.pdb structures/8C4P/8c4p_ligand.sdf structures/8C4P/8c4p_ligand.pdb structures/8C4P/8c4p_ligand.cif structures/8C4P/8c4p_complex.pdb structures/8C4P/8c4p_complex.cif 8C5Q classic CK2alpha (CK2a) Na Na Na AB668 "[""TL0""]" 1 Kd Kd = = 86 ± 20 nM 86.0 [] unit_conversion 7.0655015487564325 success True direct_binding KINOMEscan active-site-directed competition binding assay; affinity determined for CK2α. 4 “The affinity of AB668 for CK2α was 86 ± 20 nM, as determined by the KINOMEscan profiling assay.” Figure 1D reports “Kd (nM) = 86 ± 20.” auto_single_measurement only accepted activity measurement [1] 1 structures\8C5Q\8C5Q_metadata.json point structures/8C5Q/8c5q_protein.pdb structures/8C5Q/8c5q_pocket.pdb structures/8C5Q/8c5q_ligand.sdf structures/8C5Q/8c5q_ligand.pdb structures/8C5Q/8c5q_ligand.cif structures/8C5Q/8c5q_complex.pdb structures/8C5Q/8c5q_complex.cif 8C85 classic human transthyretin (TTR) human wild-type human transthyretin wild-type 3-O-methyltolcapone analogue 1 (compound 1) "[""U1F""]" 1 Kd Kd = = 71 ± 26 nM 71.0 [] unit_conversion 7.1487416512809245 success True direct_binding Isothermal titration calorimetry (ITC); single-binding-site model. 9 Table 3 reports compound 1 Kd = 71 ± 26 nM; Figure 5 identifies ITC data for TTR with compound 1. Figure 6 maps TTR/1 to PDB 8C85. auto_single_measurement only accepted activity measurement [1] 1 structures\8C85\8C85_metadata.json point structures/8C85/8c85_protein.pdb structures/8C85/8c85_pocket.pdb structures/8C85/8c85_ligand.sdf structures/8C85/8c85_ligand.pdb structures/8C85/8c85_ligand.cif structures/8C85/8c85_complex.pdb structures/8C85/8c85_complex.cif 8C86 classic human transthyretin (TTR) human wild-type human transthyretin wild-type 3-O-methyltolcapone analogue 2 (compound 2) "[""TQ0""]" 1 Kd Kd = = 25 ± 5 nM 25.0 [] unit_conversion 7.6020599913279625 success True direct_binding Isothermal titration calorimetry (ITC); single-binding-site model. 9 Table 3 reports compound 2 Kd = 25 ± 5 nM; Figure 5 identifies ITC data for TTR with compound 2. Figure 6 maps TTR/2 to PDB 8C86. auto_single_measurement only accepted activity measurement [1] 1 structures\8C86\8C86_metadata.json point structures/8C86/8c86_protein.pdb structures/8C86/8c86_pocket.pdb structures/8C86/8c86_ligand.sdf structures/8C86/8c86_ligand.pdb structures/8C86/8c86_ligand.cif structures/8C86/8c86_complex.pdb structures/8C86/8c86_complex.cif 8C8B classic human DNA cross-link repair 1A (SNM1A) human Na Na compound 20 "[""U1L""]" 1 IC50 IC50 = = 84 µM 84000.0 [] unit_conversion 4.075720713938118 success True biochemical_inhibition Biochemical inhibition assay. 2 The supplement maps 8C8B to compound 20 and reports IC50 84 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8C8B\8C8B_metadata.json point structures/8C8B/8c8b_protein.pdb structures/8C8B/8c8b_pocket.pdb structures/8C8B/8c8b_ligand.sdf structures/8C8B/8c8b_ligand.pdb structures/8C8B/8c8b_ligand.cif structures/8C8B/8c8b_complex.pdb structures/8C8B/8c8b_complex.cif 8C8D classic human DNA cross-link repair 1A (SNM1A) human Na Na compound 19 "[""U2C""]" 1 IC50 IC50 = = 44 µM 44000.0 [] unit_conversion 4.356547323513812 success True biochemical_inhibition Biochemical inhibition assay. 2 The supplement maps 8C8D to compound 19 and reports IC50 44 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8C8D\8C8D_metadata.json point structures/8C8D/8c8d_protein.pdb structures/8C8D/8c8d_pocket.pdb structures/8C8D/8c8d_ligand.sdf structures/8C8D/8c8d_ligand.pdb structures/8C8D/8c8d_ligand.cif structures/8C8D/8c8d_complex.pdb structures/8C8D/8c8d_complex.cif 8C8S classic human DNA cross-link repair 1A (SNM1A) human Na Na compound 13 "[""U2O""]" 1 IC50 IC50 = = 0.8 µM 800.0 [] unit_conversion 6.096910013008056 success True biochemical_inhibition Biochemical inhibition assay. 2 The supplement maps 8C8S to compound 13 and reports IC50 0.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8C8S\8C8S_metadata.json point structures/8C8S/8c8s_protein.pdb structures/8C8S/8c8s_pocket.pdb structures/8C8S/8c8s_ligand.sdf structures/8C8S/8c8s_ligand.pdb structures/8C8S/8c8s_ligand.cif structures/8C8S/8c8s_complex.pdb structures/8C8S/8c8s_complex.cif 8C8U classic isoleucyl-tRNA synthetase 2 (IleRS2) Priestia megaterium Na wild-type (wt-HVGH) mupirocin "[""MRC""]" 1 Ki Ki = = 1.08 ± 0.06 µM 1080.0 [] unit_conversion 5.96657624451305 success True biochemical_inhibition ATP-PPi exchange activation assay; mupirocin Ki. 4 Table 1 reports Ki(MUP)Ile = 1.08 ± 0.06 µM for wt-HVGH PmIleRS2; page 10 maps 8C8U to wt-HVGH-PmIleRS2:mupirocin. auto_single_measurement only accepted activity measurement [1] 1 structures\8C8U\8C8U_metadata.json point structures/8C8U/8c8u_protein.pdb structures/8C8U/8c8u_pocket.pdb structures/8C8U/8c8u_ligand.sdf structures/8C8U/8c8u_ligand.pdb structures/8C8U/8c8u_ligand.cif structures/8C8U/8c8u_complex.pdb structures/8C8U/8c8u_complex.cif 8C9G classic isoleucyl-tRNA synthetase 1 (IleRS1) Priestia megaterium Na wild-type (wt-HMGH) mupirocin "[""MRC""]" 1 Ki Ki = = 0.00029 ± 0.00002 µM 0.29 [] unit_conversion 9.537602002101044 success True biochemical_inhibition ATP-PPi exchange activation assay; mupirocin Ki. 4 Table 1 reports Ki(MUP)Ile = 0.00029 ± 0.00002 µM for wt-HMGH PmIleRS1; page 10 maps 8C9G to wt-HMGH-PmIleRS1:mupirocin. auto_single_measurement only accepted activity measurement [1] 1 structures\8C9G\8C9G_metadata.json point structures/8C9G/8c9g_protein.pdb structures/8C9G/8c9g_pocket.pdb structures/8C9G/8c9g_ligand.sdf structures/8C9G/8c9g_ligand.pdb structures/8C9G/8c9g_ligand.cif structures/8C9G/8c9g_complex.pdb structures/8C9G/8c9g_complex.cif 8CAK classic NADPH-Oxidase 5 (NOX5) Cylindrospermum stagnale Na Na M41 (compound 3) "[""U4F""]" 2 Kd Kd = = 3.3 ± 1.2 µM 3300.0 [] unit_conversion 5.481486060122112 success True direct_binding Thermophoresis with 200 nM protein; inhibitor titrated to 100 µM; n = 3 independent experiments. 14 Supplementary Fig. 9 reports Kd compound 3 = 3.3 ± 1.2 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8CAK\8CAK_metadata.json point structures/8CAK/8cak_protein.pdb structures/8CAK/8cak_pocket.pdb structures/8CAK/8cak_ligand.sdf structures/8CAK/8cak_ligand.pdb structures/8CAK/8cak_ligand.cif structures/8CAK/8cak_complex.pdb structures/8CAK/8cak_complex.cif 8CAL classic NADPH-Oxidase 5 (NOX5) Cylindrospermum stagnale Na Na M34 (compound 2) "[""U45""]" 1 Ki Ki = = 1.5 ± 0.1 µM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition Ki determination on purified dehydrogenase domain; nonlinear regression of apparent kcat versus NADPH (0–100 µM). 5 Supplementary Table 1 reports compound 2 Ki DH csNOX5 = 1.5 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CAL\8CAL_metadata.json point structures/8CAL/8cal_protein.pdb structures/8CAL/8cal_pocket.pdb structures/8CAL/8cal_ligand.sdf structures/8CAL/8cal_ligand.pdb structures/8CAL/8cal_ligand.cif structures/8CAL/8cal_complex.pdb structures/8CAL/8cal_complex.cif 8CAO classic NADPH-Oxidase 5 (NOX5) Cylindrospermum stagnale Na Na CA24 (compound 4) "[""U40""]" 1 Ki Ki = = 3.3 ± 0.6 µM 3300.0 [] unit_conversion 5.481486060122112 success True biochemical_inhibition Ki determination on purified dehydrogenase domain; nonlinear regression of apparent kcat versus NADPH (0–100 µM). 5 Supplementary Table 1 reports compound 4 Ki DH csNOX5 = 3.3 ± 0.6 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CAO\8CAO_metadata.json point structures/8CAO/8cao_protein.pdb structures/8CAO/8cao_pocket.pdb structures/8CAO/8cao_ligand.sdf structures/8CAO/8cao_ligand.pdb structures/8CAO/8cao_ligand.cif structures/8CAO/8cao_complex.pdb structures/8CAO/8cao_complex.cif 8CAP classic NADPH-Oxidase 5 (NOX5) Cylindrospermum stagnale Na Na CB28 (compound 6) "[""U4O""]" 1 Ki Ki = = 19.2 ± 2.3 µM 19200.0 [] unit_conversion 4.716698771296451 success True biochemical_inhibition Ki determination on purified dehydrogenase domain; nonlinear regression of apparent kcat versus NADPH (0–100 µM). 5 Supplementary Table 1 reports compound 6 Ki DH csNOX5 = 19.2 ± 2.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CAP\8CAP_metadata.json point structures/8CAP/8cap_protein.pdb structures/8CAP/8cap_pocket.pdb structures/8CAP/8cap_ligand.sdf structures/8CAP/8cap_ligand.pdb structures/8CAP/8cap_ligand.cif structures/8CAP/8cap_complex.pdb structures/8CAP/8cap_complex.cif 8CB0 classic NADPH-Oxidase 5 (NOX5) Cylindrospermum stagnale Na Na M41 (compound 3) "[""U4F""]" 1 Ki Ki = = 0.52 ± 0.05 µM 520.0 [] unit_conversion 6.2839966563652006 success True biochemical_inhibition Ki determination on purified dehydrogenase domain; nonlinear regression of apparent kcat versus NADPH (0–100 µM). 5 Supplementary Table 1 reports compound 3 Ki DH csNOX5 = 0.52 ± 0.05 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CB0\8CB0_metadata.json point structures/8CB0/8cb0_protein.pdb structures/8CB0/8cb0_pocket.pdb structures/8CB0/8cb0_ligand.sdf structures/8CB0/8cb0_ligand.pdb structures/8CB0/8cb0_ligand.cif structures/8CB0/8cb0_complex.pdb structures/8CB0/8cb0_complex.cif 8CB1 classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (Myozyme) Na N-PNT-DNM 15 "[""U4X""]" 1 IC50 IC50 = = 0.11 ± 0.08 µM 110.0 [] unit_conversion 6.958607314841775 success True biochemical_inhibition In vitro inhibition of recombinant human lysosomal α-glucosidase GAA (Myozyme); Table 1 reports mean ± standard deviation from three technical replicates. 5 Table 1 lists compound 15 with GAA IC50 0.11 ± 0.08 µM; the text identifies compound 15 as N-PNT-DNM 15 and describes its rhGAA co-crystal structure. auto_single_measurement only accepted activity measurement [1] 1 structures\8CB1\8CB1_metadata.json point structures/8CB1/8cb1_protein.pdb structures/8CB1/8cb1_pocket.pdb structures/8CB1/8cb1_ligand.sdf structures/8CB1/8cb1_ligand.pdb structures/8CB1/8cb1_ligand.cif structures/8CB1/8cb1_complex.pdb structures/8CB1/8cb1_complex.cif 8CB4 extended PrfA transcriptional regulator Listeria monocytogenes Full-length recombinant PrfA with two additional N-terminal residues GA after TEV cleavage; expressed from pET28a with a 6xHis-TEV construct wild-type PrfA LLL (Leu-Leu-Leu) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 5 μM 5000.0 [] unit_conversion 5.301029995663981 success True direct_binding Isothermal titration calorimetry (ITC) of purified recombinant PrfA with inhibitory peptide; integrated heat-peak analysis. 3 “peptides LLL and LL have the strongest affinity, with dissociation constants (K_Ds) in the low micromolar range, approximately 2 and 5 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CB4\8CB4_metadata.json point structures/8CB4/8cb4_protein.pdb structures/8CB4/8cb4_pocket.pdb structures/8CB4/8cb4_ligand.pdb structures/8CB4/8cb4_ligand.cif structures/8CB4/8cb4_complex.pdb structures/8CB4/8cb4_complex.cif 8CB5 extended PrfA transcriptional regulator Listeria monocytogenes Full-length recombinant PrfA with two additional N-terminal residues GA after TEV cleavage; expressed from pET28a with a 6xHis-TEV construct wild-type PrfA EVF (Glu-Val-Phe) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 12 μM 12000.0 [] unit_conversion 4.920818753952375 success True direct_binding Isothermal titration calorimetry (ITC) of purified recombinant PrfA with inhibitory peptide; integrated heat-peak analysis. 3 “Peptides EVF and EVFL had K_D values of approximately 12 and 15 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CB5\8CB5_metadata.json point structures/8CB5/8cb5_protein.pdb structures/8CB5/8cb5_pocket.pdb structures/8CB5/8cb5_ligand.pdb structures/8CB5/8cb5_ligand.cif structures/8CB5/8cb5_complex.pdb structures/8CB5/8cb5_complex.cif 8CB7 extended PrfA transcriptional regulator Listeria monocytogenes Full-length recombinant PrfA with two additional N-terminal residues GA after TEV cleavage; expressed from pET28a with a 6xHis-TEV construct wild-type PrfA EVFL (Glu-Val-Phe-Leu) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 15 μM 15000.0 [] unit_conversion 4.823908740944319 success True direct_binding Isothermal titration calorimetry (ITC) of purified recombinant PrfA with inhibitory peptide; integrated heat-peak analysis. 3 “Peptides EVF and EVFL had K_D values of approximately 12 and 15 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CB7\8CB7_metadata.json point structures/8CB7/8cb7_protein.pdb structures/8CB7/8cb7_pocket.pdb structures/8CB7/8cb7_ligand.pdb structures/8CB7/8cb7_ligand.cif structures/8CB7/8cb7_complex.pdb structures/8CB7/8cb7_complex.cif 8CB8 extended PrfA transcriptional regulator Listeria monocytogenes Full-length recombinant PrfA with two additional N-terminal residues GA after TEV cleavage; expressed from pET28a with a 6xHis-TEV construct wild-type PrfA STLL (Ser-Thr-Leu-Leu) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 28 μM 28000.0 [] unit_conversion 4.552841968657781 success True direct_binding Isothermal titration calorimetry (ITC) of purified recombinant PrfA with inhibitory peptide; integrated heat-peak analysis. 3 “peptides STLL and RGLL showed weaker binding with K_D values of approximately 28 and 90 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CB8\8CB8_metadata.json point structures/8CB8/8cb8_protein.pdb structures/8CB8/8cb8_pocket.pdb structures/8CB8/8cb8_ligand.pdb structures/8CB8/8cb8_ligand.cif structures/8CB8/8cb8_complex.pdb structures/8CB8/8cb8_complex.cif 8CBG extended PrfA transcriptional regulator Listeria monocytogenes Full-length recombinant PrfA with two additional N-terminal residues GA after TEV cleavage; expressed from pET28a with a 6xHis-TEV construct wild-type PrfA RGLL (Arg-Gly-Leu-Leu) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 90 μM 90000.0 [] unit_conversion 4.045757490560675 success True direct_binding Isothermal titration calorimetry (ITC) of purified recombinant PrfA with inhibitory peptide; integrated heat-peak analysis. 3 “peptides STLL and RGLL showed weaker binding with K_D values of approximately 28 and 90 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CBG\8CBG_metadata.json point structures/8CBG/8cbg_protein.pdb structures/8CBG/8cbg_pocket.pdb structures/8CBG/8cbg_ligand.pdb structures/8CBG/8cbg_ligand.cif structures/8CBG/8cbg_complex.pdb structures/8CBG/8cbg_complex.cif 8CBY classic anti-cortisol (17) Fab fragment murine Fab fragment with a six-histidine tag; C-terminal His-tag residues were unmodeled Ser56-H to Arg56-H cortisol "[""HCY""]" 1 Kd Kd = = 7.17 ± 0.80 nM 7.17 [] unit_conversion 8.1444808443322 success True direct_binding SPR on a Biacore T200 instrument using a Sensor Chip CM5; affinity of anti-cortisol (17) Fab to cortisol. 4 Table 1 reports cortisol K_D = 7.17 ± 0.80 nM; the text states the binding properties were characterized by SPR using a Biacore T200. auto_single_measurement only accepted activity measurement [1] 1 structures\8CBY\8CBY_metadata.json point structures/8CBY/8cby_protein.pdb structures/8CBY/8cby_pocket.pdb structures/8CBY/8cby_ligand.sdf structures/8CBY/8cby_ligand.pdb structures/8CBY/8cby_ligand.cif structures/8CBY/8cby_complex.pdb structures/8CBY/8cby_complex.cif 8CBZ classic anti-cortisol (17) Fab fragment murine Fab fragment with a six-histidine tag; C-terminal His-tag residues were unmodeled Ser56-H to Arg56-H corticosterone "[""C0R""]" 1 Kd Kd = = 30.85 ± 2.26 nM 30.85 [] unit_conversion 7.510744831630739 success True direct_binding SPR on a Biacore T200 instrument using a Sensor Chip CM5; cross-reactivity binding measurement of anti-cortisol (17) Fab to corticosterone. 4 Table 1 reports corticosterone K_D = 30.85 ± 2.26 nM; the text states SPR was also applied in cross-reactivity studies. auto_single_measurement only accepted activity measurement [1] 1 structures\8CBZ\8CBZ_metadata.json point structures/8CBZ/8cbz_protein.pdb structures/8CBZ/8cbz_pocket.pdb structures/8CBZ/8cbz_ligand.sdf structures/8CBZ/8cbz_ligand.pdb structures/8CBZ/8cbz_ligand.cif structures/8CBZ/8cbz_complex.pdb structures/8CBZ/8cbz_complex.cif 8CC0 classic anti-cortisol (17) Fab fragment murine Fab fragment with a six-histidine tag; C-terminal His-tag residues were unmodeled Ser56-H to Arg56-H cortisone "[""UQC""]" 1 Kd Kd = = 32.45 ± 2.32 nM 32.45 [] unit_conversion 7.488785298863612 success True direct_binding SPR on a Biacore T200 instrument using a Sensor Chip CM5; cross-reactivity binding measurement of anti-cortisol (17) Fab to cortisone. 4 Table 1 reports cortisone K_D = 32.45 ± 2.32 nM; the text states SPR was also applied in cross-reactivity studies. auto_single_measurement only accepted activity measurement [1] 1 structures\8CC0\8CC0_metadata.json point structures/8CC0/8cc0_protein.pdb structures/8CC0/8cc0_pocket.pdb structures/8CC0/8cc0_ligand.sdf structures/8CC0/8cc0_ligand.pdb structures/8CC0/8cc0_ligand.cif structures/8CC0/8cc0_complex.pdb structures/8CC0/8cc0_complex.cif 8CC1 classic anti-cortisol (17) Fab fragment murine Fab fragment with a six-histidine tag; C-terminal His-tag residues were unmodeled Ser56-H to Arg56-H prednisolone "[""TUA""]" 1 Kd Kd = = 12.72 ± 0.90 nM 12.72 [] unit_conversion 7.895512888687605 success True direct_binding SPR on a Biacore T200 instrument using a Sensor Chip CM5; cross-reactivity binding measurement of anti-cortisol (17) Fab to prednisolone. 4 Table 1 reports prednisolone K_D = 12.72 ± 0.90 nM; the text states SPR was also applied in cross-reactivity studies. auto_single_measurement only accepted activity measurement [1] 1 structures\8CC1\8CC1_metadata.json point structures/8CC1/8cc1_protein.pdb structures/8CC1/8cc1_pocket.pdb structures/8CC1/8cc1_ligand.sdf structures/8CC1/8cc1_ligand.pdb structures/8CC1/8cc1_ligand.cif structures/8CC1/8cc1_complex.pdb structures/8CC1/8cc1_complex.cif 8CD3 extended human Scribble PDZ1 domain human Scribble PDZ1 domain complexed with the human TMIGD1 C-terminal 8-mer peptide Na TMIGD1 C-terminal peptide DPHSETAL "[""CHAIN:A""]" 1 Kd Kd = = 18.17 ± 1.80 μM 18170.0 [] unit_conversion 4.740645072691966 success True direct_binding Isothermal titration calorimetry of purified Scribble PDZ1 domain with TMIGD1/WT peptide. 7 Table 2 reports TMIGD1/WT DPHSETAL binding to Scrib-PDZ1: 18.17 ± 1.80 μM; the Fig. 4 legend identifies these as ITC interaction profiles of human Scribble PDZ domains with hTMIGD1 peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\8CD3\8CD3_metadata.json point structures/8CD3/8cd3_protein.pdb structures/8CD3/8cd3_pocket.pdb structures/8CD3/8cd3_ligand.pdb structures/8CD3/8cd3_ligand.cif structures/8CD3/8cd3_complex.pdb structures/8CD3/8cd3_complex.cif 8CD8 classic ulilysin C269A Methanosarcina acetivorans Residues M1-R342, N-terminal His6-tagged expression construct; modeled residues R61-A322 C269A AEBSF (4-(2-aminoethyl)benzenesulfonyl fluoride) "[""AES""]" 1 Ki Ki = = 4.0 ± 0.4 µM 4000.0 [] unit_conversion 5.3979400086720375 success True biochemical_inhibition Fluorogenic peptide-cleavage inhibition assay; apparent Ki determined after 1 h preincubation with AEBSF. Figure reports a dose-dependent, competitive, reversible inhibition measurement. 4 Fig. 1E explicitly prints “Ki = 4.0 ± 0.4 µM”; its caption identifies AEBSF inhibition of ulilysin cleavage and graphical determination of the apparent inhibition constant. Methods identify the activity/inhibition experiments as using ulilysin C269A. auto_single_measurement only accepted activity measurement [1] 1 structures\8CD8\8CD8_metadata.json point structures/8CD8/8cd8_protein.pdb structures/8CD8/8cd8_pocket.pdb structures/8CD8/8cd8_ligand.sdf structures/8CD8/8cd8_ligand.pdb structures/8CD8/8cd8_ligand.cif structures/8CD8/8cd8_complex.pdb structures/8CD8/8cd8_complex.cif 8CDX extended human carbonic anhydrase I human Na Na 4-(3-ethylureido)benzenesulfonamide; compound 8 "[""UE7""]" 1 Ki Ki = = 871.6 nM 871.6 [] unit_conversion 6.059682778425782 success True biochemical_inhibition Stopped-flow enzyme-inhibition experiment; Table 1 reports Ki values for hCA I, II, IX, and XII. 4 Table 1 lists compound 8 with hCA I Ki = 871.6 nM; the preceding text states compounds 1–15 were screened through stopped-flow experiments employing hCA I, hCA II, hCA IX, and hCA XII. Figure 6 identifies compound 8 in the hCA I active site, and the paper deposits 8CDX/8CDZ. auto_single_measurement only accepted activity measurement [1] 1 structures\8CDX\8CDX_metadata.json point structures/8CDX/8cdx_ligand.sdf structures/8CDX/8cdx_ligand.cif structures/8CDX/8cdx_complex.cif 8CDZ extended human carbonic anhydrase I human Na Na 4-(3-butylureido)benzenesulfonamide; compound 10 "[""U7M""]" 1 Ki Ki = = 86.2 nM 86.2 [] unit_conversion 7.064492734175287 success True biochemical_inhibition Stopped-flow enzyme-inhibition experiment; Table 1 reports Ki values for hCA I, II, IX, and XII. 4 Table 1 lists compound 10 with hCA I Ki = 86.2 nM; the preceding text states compounds 1–15 were screened through stopped-flow experiments employing hCA I, hCA II, hCA IX, and hCA XII. Figure 7 identifies compound 10 in the hCA I active site, and the paper deposits 8CDX/8CDZ. auto_single_measurement only accepted activity measurement [1] 1 structures\8CDZ\8CDZ_metadata.json point structures/8CDZ/8cdz_ligand.sdf structures/8CDZ/8cdz_ligand.cif structures/8CDZ/8cdz_complex.cif 8CEQ classic monkeypox virus methyltransferase VP39 Monkeypox virus (MPXV) Recombinant VP39 expressed in E. coli from a pSUMO construct with an 8xHis-SUMO tag; tag cleaved before crystallization Na TO427 "[""UF9""]" 1 IC50 IC50 = = 0.115 ± 0.0004 µM 115.0 [] unit_conversion 6.939302159646388 success True biochemical_inhibition VP39 2′-O-methyltransferase inhibition assay; Fig. 4 reports mean ± SEM (n=2 independent measurements). 5 Fig. 4 labels TO427 with IC50 0.115 ± 0.0004 µM; its caption identifies MTase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CEQ\8CEQ_metadata.json point structures/8CEQ/8ceq_protein.pdb structures/8CEQ/8ceq_pocket.pdb structures/8CEQ/8ceq_ligand.sdf structures/8CEQ/8ceq_ligand.pdb structures/8CEQ/8ceq_ligand.cif structures/8CEQ/8ceq_complex.pdb structures/8CEQ/8ceq_complex.cif 8CER classic monkeypox virus methyltransferase VP39 Monkeypox virus (MPXV) Recombinant VP39 expressed in E. coli from a pSUMO construct with an 8xHis-SUMO tag; tag cleaved before crystallization Na TO494 "[""UEM""]" 1 IC50 IC50 = = 0.145 ± 0.049 µM 145.0 [] unit_conversion 6.838631997765026 success True biochemical_inhibition VP39 2′-O-methyltransferase inhibition assay; Fig. 4 reports mean ± SEM (n=2 independent measurements). 5 Fig. 4 labels TO494 with IC50 0.145 ± 0.049 µM; its caption identifies MTase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CER\8CER_metadata.json point structures/8CER/8cer_protein.pdb structures/8CER/8cer_pocket.pdb structures/8CER/8cer_ligand.sdf structures/8CER/8cer_ligand.pdb structures/8CER/8cer_ligand.cif structures/8CER/8cer_complex.pdb structures/8CER/8cer_complex.cif 8CES classic monkeypox virus methyltransferase VP39 Monkeypox virus (MPXV) Recombinant VP39 expressed in E. coli from a pSUMO construct with an 8xHis-SUMO tag; tag cleaved before crystallization Na TO500 "[""UH2""]" 1 IC50 IC50 = = 0.169 ± 0.004 µM 169.0 [] unit_conversion 6.772113295386326 success True biochemical_inhibition VP39 2′-O-methyltransferase inhibition assay; Fig. 4 reports mean ± SEM (n=2 independent measurements). 5 Fig. 4 labels TO500 with IC50 0.169 ± 0.004 µM; its caption identifies MTase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CES\8CES_metadata.json point structures/8CES/8ces_protein.pdb structures/8CES/8ces_pocket.pdb structures/8CES/8ces_ligand.sdf structures/8CES/8ces_ligand.pdb structures/8CES/8ces_ligand.cif structures/8CES/8ces_complex.pdb structures/8CES/8ces_complex.cif 8CET classic monkeypox virus methyltransferase VP39 Monkeypox virus (MPXV) Recombinant VP39 expressed in E. coli from a pSUMO construct with an 8xHis-SUMO tag; tag cleaved before crystallization Na TO507 "[""UGR""]" 1 IC50 IC50 = = 0.117 ± 0.014 µM 117.0 [] unit_conversion 6.931814138253838 success True biochemical_inhibition VP39 2′-O-methyltransferase inhibition assay; Fig. 4 reports mean ± SEM (n=2 independent measurements). 5 Fig. 4 labels TO507 with IC50 0.117 ± 0.014 µM; its caption identifies MTase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CET\8CET_metadata.json point structures/8CET/8cet_protein.pdb structures/8CET/8cet_pocket.pdb structures/8CET/8cet_ligand.sdf structures/8CET/8cet_ligand.pdb structures/8CET/8cet_ligand.cif structures/8CET/8cet_complex.pdb structures/8CET/8cet_complex.cif 8CEV classic monkeypox virus methyltransferase VP39 Monkeypox virus (MPXV) Recombinant VP39 expressed in E. coli from a pSUMO construct with an 8xHis-SUMO tag; tag cleaved before crystallization Na TO1119 "[""UG9""]" 1 IC50 IC50 = = 0.128 ± 0.034 µM 128.0 [] unit_conversion 6.892790030352131 success True biochemical_inhibition VP39 2′-O-methyltransferase inhibition assay; Fig. 4 reports mean ± SEM (n=2 independent measurements). 5 Fig. 4 labels TO1119 with IC50 0.128 ± 0.034 µM; its caption identifies MTase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CEV\8CEV_metadata.json point structures/8CEV/8cev_protein.pdb structures/8CEV/8cev_pocket.pdb structures/8CEV/8cev_ligand.sdf structures/8CEV/8cev_ligand.pdb structures/8CEV/8cev_ligand.cif structures/8CEV/8cev_complex.pdb structures/8CEV/8cev_complex.cif 8CGO classic human butyrylcholinesterase (hBChE) human Recombinant human BuChE without the tetramerization C-terminal domain and with four deleted N-glycosylation sites Four N-glycosylation-site Asn-to-Gln substitutions compound 87; N-{[2-(benzyloxy)-3-methoxyphenyl]methyl}-N-[3-(2-fluorophenyl)propyl]cyclobutanamine "[""XB8""]" 2 Ki Ki = = 4.04 ± 0.52 nM 4.04 [] unit_conversion 8.393618634889394 success True biochemical_inhibition Modified Ellman kinetic study; competitive inhibition of hBChE by compound 87. 6 The kinetic-study text states that compound 87 competes directly with substrate at the hBChE active site and reports Ki = 4.04 ± 0.52 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8CGO\8CGO_metadata.json point structures/8CGO/8cgo_protein.pdb structures/8CGO/8cgo_pocket.pdb structures/8CGO/8cgo_ligand.sdf structures/8CGO/8cgo_ligand.pdb structures/8CGO/8cgo_ligand.cif structures/8CGO/8cgo_complex.pdb structures/8CGO/8cgo_complex.cif 8CHI classic FKBP12 human Na Na compound 6a; (1S,5S,6R)-10-((S)-3,5-dichloro-N-methylphenylsulfonimidoyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,10-diazabicyclo[4.3.1]decan-2-one "[""UMR""]" 1 Kd Kd = = 1,390 ± 190 nM 1390.0 [] unit_conversion 5.856985199745905 success True direct_binding Competitive fluorescence-polarization assay using sulfonamide 1 as reference; Table 1 FKBP12 measurement. 4 Table 1 lists compound 6a (vinyl, N-methyl sulfonimidamide) with K_D for FKBP12 of 1,390 ± 190 nM. Figure 2 maps compound 6a to PDB 8CHI. auto_single_measurement only accepted activity measurement [1] 1 structures\8CHI\8CHI_metadata.json point structures/8CHI/8chi_protein.pdb structures/8CHI/8chi_pocket.pdb structures/8CHI/8chi_ligand.sdf structures/8CHI/8chi_ligand.pdb structures/8CHI/8chi_ligand.cif structures/8CHI/8chi_complex.pdb structures/8CHI/8chi_complex.cif 8CHJ classic FKBP12 human Na Na (1S,5S,6R)-10-((R)-(3,5-dichlorophenyl)sulfonimidoyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,10-diazabicyclo[4.3.1]decan-2-one "[""UQI""]" 1 Kd Kd = = 283 ± 24 nM 283.0 [] unit_conversion 6.548213564475709 success True direct_binding Competitive fluorescence-polarization assay using sulfonamide 1 as reference; Table 1 FKBP12 measurement. 4 Table 1 lists compound 5b with K_D for FKBP12 of 283 ± 24 nM; the R-configured, N-unsubstituted sulfonimidamide matches the supplied 8CHJ ligand title. auto_single_measurement only accepted activity measurement [1] 1 structures\8CHJ\8CHJ_metadata.json point structures/8CHJ/8chj_protein.pdb structures/8CHJ/8chj_pocket.pdb structures/8CHJ/8chj_ligand.sdf structures/8CHJ/8chj_ligand.pdb structures/8CHJ/8chj_ligand.cif structures/8CHJ/8chj_complex.pdb structures/8CHJ/8chj_complex.cif 8CHK classic FKBP12 human Na Na (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfonimidoyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,10-diazabicyclo[4.3.1]decan-2-one "[""UUI""]" 1 Kd Kd = = 360 ± 27 nM 360.0 [] unit_conversion 6.443697499232712 success True direct_binding Competitive fluorescence-polarization assay using sulfonamide 1 as reference; Table 1 FKBP12 measurement. 4 Table 1 lists compound 5a with K_D for FKBP12 of 360 ± 27 nM; the S-configured, N-unsubstituted sulfonimidamide matches the supplied 8CHK ligand title. auto_single_measurement only accepted activity measurement [1] 1 structures\8CHK\8CHK_metadata.json point structures/8CHK/8chk_protein.pdb structures/8CHK/8chk_pocket.pdb structures/8CHK/8chk_ligand.sdf structures/8CHK/8chk_ligand.pdb structures/8CHK/8chk_ligand.cif structures/8CHK/8chk_complex.pdb structures/8CHK/8chk_complex.cif 8CHL classic FKBP12 human Na Na compound 1; (1S,5S,6R)-9-((3,5-dichlorophenyl)sulfonyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,9-diazabicyclo[4.2.1]nonan-2-one "[""USV""]" 1 Kd Kd = = 2.6 ± 0.2 nM 2.6 [] unit_conversion 8.585026652029182 success True direct_binding Competitive fluorescence-polarization assay using sulfonamide 1 as reference; Table 1 FKBP12 measurement. 4 Table 1 lists compound 1 with K_D for FKBP12 of 2.6 ± 0.2 nM. Figure 2 maps compound 1 to PDB 8CHL. auto_single_measurement only accepted activity measurement [1] 1 structures\8CHL\8CHL_metadata.json point structures/8CHL/8chl_protein.pdb structures/8CHL/8chl_pocket.pdb structures/8CHL/8chl_ligand.sdf structures/8CHL/8chl_ligand.pdb structures/8CHL/8chl_ligand.cif structures/8CHL/8chl_complex.pdb structures/8CHL/8chl_complex.cif 8CHM classic FKBP12 human Na Na compound 4b; (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfinyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,10-diazabicyclo[4.3.1]decan-2-one "[""UT6""]" 1 Kd Kd = = 67 ± 5 nM 67.0 [] unit_conversion 7.173925197299173 success True direct_binding Competitive fluorescence-polarization assay using sulfonamide 1 as reference; Table 1 FKBP12 measurement. 4 Table 1 lists compound 4b with K_D for FKBP12 of 67 ± 5 nM. Figure 2 maps compound 4b to PDB 8CHM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CHM\8CHM_metadata.json point structures/8CHM/8chm_protein.pdb structures/8CHM/8chm_pocket.pdb structures/8CHM/8chm_ligand.sdf structures/8CHM/8chm_ligand.pdb structures/8CHM/8chm_ligand.cif structures/8CHM/8chm_complex.pdb structures/8CHM/8chm_complex.cif 8CIR extended moesin (MSN) human MSN residues 1-345 Na C3P-pd peptide (EDGGSWKYPDAFELSG) "[""CHAIN:C"", ""CHAIN:D""]" 2 Kd Kd = = 258.4 ± 3.5 nM 258.4 [] unit_conversion 6.587707490676953 success True direct_binding Isothermal titration calorimetry of C3P-pd binding to MSN. 6 Figure 3L reports C3P-pd KD = 258.4 ± 3.5 nM for binding to MSN. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8CIR\8CIR_metadata.json point structures/8CIR/8cir_protein.pdb structures/8CIR/8cir_pocket.pdb structures/8CIR/8cir_ligand.pdb structures/8CIR/8cir_ligand.cif structures/8CIR/8cir_complex.pdb structures/8CIR/8cir_complex.cif 8CJ1 extended ASF1A histone chaperone Human ASF1A_N, N-terminal conserved domain Na c3u_3 "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L""]" 1 Kd Kd = = 7.7 ± 2.0 µM 7700.0 [] unit_conversion 5.113509274827518 success True direct_binding Isothermal titration calorimetry (ITC) measurement of c3u_3 chimera binding to ASF1A_N. 2 Figure 2 prints 7.7 ± 2.0 µM for c3u_3 and states that K_D values for ASF1 were determined by ITC; the text identifies c3u_3 as binding ASF1A_N. auto_single_measurement only accepted activity measurement [1] 1 structures\8CJ1\8CJ1_metadata.json point structures/8CJ1/8cj1_protein.pdb structures/8CJ1/8cj1_pocket.pdb structures/8CJ1/8cj1_ligand.pdb structures/8CJ1/8cj1_ligand.cif structures/8CJ1/8cj1_complex.pdb structures/8CJ1/8cj1_complex.cif 8CJ2 extended ASF1A histone chaperone Human ASF1A_N, N-terminal conserved domain Na c3u_5 "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 Kd Kd = = 4.0 ± 0.2 µM 4000.0 [] unit_conversion 5.3979400086720375 success True direct_binding Isothermal titration calorimetry (ITC) measurement of c3u_5 chimera binding to ASF1A_N. 2 Figure 2 prints 4.0 ± 0.2 µM for c3u_5 and states that K_D values for ASF1 were determined by ITC; the text reports c3u_5 binding to ASF1A_N. auto_single_measurement only accepted activity measurement [1] 1 structures\8CJ2\8CJ2_metadata.json point structures/8CJ2/8cj2_protein.pdb structures/8CJ2/8cj2_pocket.pdb structures/8CJ2/8cj2_ligand.pdb structures/8CJ2/8cj2_ligand.cif structures/8CJ2/8cj2_complex.pdb structures/8CJ2/8cj2_complex.cif 8CJ3 extended ASF1A histone chaperone Human ASF1A_N, N-terminal conserved domain Na c3u_7 "[""CHAIN:B""]" 1 Kd Kd = = 12 ± 2 µM 12000.0 [] unit_conversion 4.920818753952375 success True direct_binding Isothermal titration calorimetry (ITC) measurement of c3u_7 chimera binding to ASF1A_N. 2 Figure 2 prints 12 ± 2 µM for c3u_7 and states that K_D values for ASF1 were determined by ITC; the text reports c3u_7 binding to ASF1A_N. auto_single_measurement only accepted activity measurement [1] 1 structures\8CJ3\8CJ3_metadata.json point structures/8CJ3/8cj3_protein.pdb structures/8CJ3/8cj3_pocket.pdb structures/8CJ3/8cj3_ligand.pdb structures/8CJ3/8cj3_ligand.cif structures/8CJ3/8cj3_complex.pdb structures/8CJ3/8cj3_complex.cif 8CK7 classic avidin chicken egg white avidin Na theophylline (TEP; 1,3-dimethylxanthine) "[""TEP""]" 1 Kd Kd = = 440 μM 440000.0 [] unit_conversion 3.356547323513812 success True direct_binding Isothermal titration calorimetry (ITC) of avidin–TEP at 25 °C in PBS pH 7.4; TEP was titrated into avidin. 5 “ITC measurements on the avidin-TEP complex (Figure 2) showed that the binding constant Kd is 440 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CK7\8CK7_metadata.json point structures/8CK7/8ck7_protein.pdb structures/8CK7/8ck7_pocket.pdb structures/8CK7/8ck7_ligand.sdf structures/8CK7/8ck7_ligand.pdb structures/8CK7/8ck7_ligand.cif structures/8CK7/8ck7_complex.pdb structures/8CK7/8ck7_complex.cif 8CMB extended Human Leukocyte Antigen class II allotype DR1 (HLA-DR1) Human HLA-DRA*0101/HLA-DRB1*0101 heterodimer Na S486-505 "[""CHAIN:C""]" 1 IC50 IC50 = = 3046.2 nM 3046.2 [] unit_conversion 5.516241586211752 success True direct_binding Purified HLA-DR1 competitive peptide-binding assay. 6 Figure 1B prints an IC50 of 3046.2 nM for S486-505 in the HLA-DR1 binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CMB\8CMB_metadata.json point structures/8CMB/8cmb_protein.pdb structures/8CMB/8cmb_pocket.pdb structures/8CMB/8cmb_ligand.pdb structures/8CMB/8cmb_ligand.cif structures/8CMB/8cmb_complex.pdb structures/8CMB/8cmb_complex.cif 8CMC extended Human Leukocyte Antigen class II allotype DR1 (HLA-DR1) Human HLA-DRA*0101/HLA-DRB1*0101 heterodimer Na S511-530 "[""CHAIN:C""]" 1 IC50 IC50 = = 2624.3 nM 2624.3 [] unit_conversion 5.580986519564192 success True direct_binding Purified HLA-DR1 competitive peptide-binding assay. 6 Figure 1B prints an IC50 of 2624.3 nM for S511-530 in the HLA-DR1 binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CMC\8CMC_metadata.json point structures/8CMC/8cmc_protein.pdb structures/8CMC/8cmc_pocket.pdb structures/8CMC/8cmc_ligand.pdb structures/8CMC/8cmc_ligand.cif structures/8CMC/8cmc_complex.pdb structures/8CMC/8cmc_complex.cif 8CMD extended Human Leukocyte Antigen class II allotype DR1 (HLA-DR1) Human HLA-DRA*0101/HLA-DRB1*0101 heterodimer Na S761-775 "[""CHAIN:C"", ""CHAIN:F"", ""CHAIN:I""]" 1 IC50 IC50 > > 10 µM 10000.0 [] unit_conversion 5.0 success True direct_binding Purified HLA-DR1 competitive peptide-binding assay. 6 Figure 1B prints IC50 >10 µM for S761-775 in the HLA-DR1 binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CMD\8CMD_metadata.json point structures/8CMD/8cmd_protein.pdb structures/8CMD/8cmd_pocket.pdb structures/8CMD/8cmd_ligand.pdb structures/8CMD/8cmd_ligand.cif structures/8CMD/8cmd_complex.pdb structures/8CMD/8cmd_complex.cif 8CME extended Human Leukocyte Antigen class II allotype DR1 (HLA-DR1) Human HLA-DRA*0101/HLA-DRB1*0101 heterodimer Na M176-190 "[""POLYMER_ENTITY:3""]" 1 IC50 IC50 = = 7.9 nM 7.9 [] unit_conversion 8.102372908709558 success True direct_binding Purified HLA-DR1 competitive peptide-binding assay. 6 Figure 1B prints an IC50 of 7.9 nM for M176-190 in the HLA-DR1 binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CME\8CME_metadata.json point structures/8CME/8cme_protein.pdb structures/8CME/8cme_pocket.pdb structures/8CME/8cme_ligand.pdb structures/8CME/8cme_ligand.cif structures/8CME/8cme_complex.pdb structures/8CME/8cme_complex.cif 8CMF extended Human Leukocyte Antigen class II allotype DR1 (HLA-DR1) Human HLA-DRA*0101/HLA-DRB1*0101 heterodimer Na nsp3_1350-1364 "[""CHAIN:C"", ""CHAIN:F""]" 1 IC50 IC50 = = 139.7 nM 139.7 [] unit_conversion 6.854803593885818 success True direct_binding Purified HLA-DR1 competitive peptide-binding assay. 6 Figure 1B prints an IC50 of 139.7 nM for nsp3_1350-1364 in the HLA-DR1 binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CMF\8CMF_metadata.json point structures/8CMF/8cmf_protein.pdb structures/8CMF/8cmf_pocket.pdb structures/8CMF/8cmf_ligand.pdb structures/8CMF/8cmf_ligand.cif structures/8CMF/8cmf_complex.pdb structures/8CMF/8cmf_complex.cif 8CMG extended Human Leukocyte Antigen class II allotype DR1 (HLA-DR1) Human HLA-DRA*0101/HLA-DRB1*0101 heterodimer Na nsp14_6420-6434 "[""CHAIN:C""]" 1 IC50 IC50 = = 541.6 nM 541.6 [] unit_conversion 6.266321344322912 success True direct_binding Purified HLA-DR1 competitive peptide-binding assay. 6 Figure 1B prints an IC50 of 541.6 nM for nsp14_6420-6434 in the HLA-DR1 binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CMG\8CMG_metadata.json point structures/8CMG/8cmg_protein.pdb structures/8CMG/8cmg_pocket.pdb structures/8CMG/8cmg_ligand.pdb structures/8CMG/8cmg_ligand.cif structures/8CMG/8cmg_complex.pdb structures/8CMG/8cmg_complex.cif 8CMH extended Human Leukocyte Antigen class II allotype DR1 (HLA-DR1) Human HLA-DRA*0101/HLA-DRB1*0101 heterodimer F486V; Q493R; G496S; Q498R; N501Y; Y505H S486-505 Omicron (BA.1) "[""CHAIN:C""]" 1 IC50 IC50 = = 753.6 nM 753.6 [] unit_conversion 6.122859110215179 success True direct_binding Purified HLA-DR1 competitive peptide-binding assay of the Omicron (BA.1) variant peptide. 10 Figure 4E prints an IC50 of 753.6 nM for the Omicron (BA.1) S486-505 peptide in the HLA-DR1 binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CMH\8CMH_metadata.json point structures/8CMH/8cmh_protein.pdb structures/8CMH/8cmh_pocket.pdb structures/8CMH/8cmh_ligand.pdb structures/8CMH/8cmh_ligand.cif structures/8CMH/8cmh_complex.pdb structures/8CMH/8cmh_complex.cif 8CMI extended Human Leukocyte Antigen class II allotype DR1 (HLA-DR1) Human HLA-DRA*0101/HLA-DRB1*0101 heterodimer N764K S761-775 Omicron (BA.1) "[""POLYMER_ENTITY:3""]" 1 IC50 IC50 = = 677.2 nM 677.2 [] unit_conversion 6.169283050563102 success True direct_binding Purified HLA-DR1 competitive peptide-binding assay of the Omicron (BA.1) variant peptide. 10 Figure 4E prints an IC50 of 677.2 nM for the Omicron (BA.1) S761-775 peptide in the HLA-DR1 binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CMI\8CMI_metadata.json point structures/8CMI/8cmi_protein.pdb structures/8CMI/8cmi_pocket.pdb structures/8CMI/8cmi_ligand.pdb structures/8CMI/8cmi_ligand.cif structures/8CMI/8cmi_complex.pdb structures/8CMI/8cmi_complex.cif 8CMK extended Transportin-3 (TNPO3) Homo sapiens TNPO3 C511A with CIRBP RSY-region peptide, residues 157-172 TNPO3 C511A CIRBP RSY region (mCIRBPRSY), residues 157-172 "[""CHAIN:C"", ""CHAIN:D"", ""CHAIN:E""]" 1 Kd Kd = = 5.78 ± 1.63 µM 5780.0 [] unit_conversion 5.2380721615794705 success True direct_binding Isothermal titration calorimetry at 25 °C; synthetic CIRBP 157–172 peptide binding to TNPO3 C511A. 7 Table 1 reports WT CIRBP motif GGSYRDSYDSYATHNE with Kd = 5.78 ± 1.63 µM. Methods state that CIRBP (157–172) peptide studies were performed with TNPO3 C511A. auto_single_measurement only accepted activity measurement [1] 1 structures\8CMK\8CMK_metadata.json point structures/8CMK/8cmk_protein.pdb structures/8CMK/8cmk_pocket.pdb structures/8CMK/8cmk_ligand.pdb structures/8CMK/8cmk_ligand.cif structures/8CMK/8cmk_complex.pdb structures/8CMK/8cmk_complex.cif 8CN6 extended CD59 Na CD59 ectodomain Na CP-06 "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 11.3 ± 0.0 nM 11.3 [] unit_conversion 7.94692155651658 success True direct_binding Surface plasmon resonance (SPR) with immobilized CD59; reported as mean of three technical replicates ± SEM. 3 Table in Figure 2 lists CP-06 K_D = 11.3 ± 0.0 nM; caption identifies SPR with immobilized CD59. auto_single_measurement only accepted activity measurement [1] 1 structures\8CN6\8CN6_metadata.json point structures/8CN6/8cn6_protein.pdb structures/8CN6/8cn6_pocket.pdb structures/8CN6/8cn6_ligand.pdb structures/8CN6/8cn6_ligand.cif structures/8CN6/8cn6_complex.pdb structures/8CN6/8cn6_complex.cif 8CO0 classic human carbonic anhydrase IX (hCA IX) human Na Na compound 35 "[""V8O""]" 1 Ki Ki = = 29.8 nM 29.8 [] unit_conversion 7.525783735923745 success True biochemical_inhibition Stopped-flow CO2 hydration inhibition assay. 5 Table 1 reports compound 35 Ki = 29.8 nM against hCA IX; Figure 5 maps compound 35 bound to hCA IX to PDB 8CO0. auto_single_measurement only accepted activity measurement [1] 1 structures\8CO0\8CO0_metadata.json point structures/8CO0/8co0_protein.pdb structures/8CO0/8co0_pocket.pdb structures/8CO0/8co0_ligand.sdf structures/8CO0/8co0_ligand.pdb structures/8CO0/8co0_ligand.cif structures/8CO0/8co0_complex.pdb structures/8CO0/8co0_complex.cif 8CO3 classic human carbonic anhydrase XII (hCA XII) human catalytic domain residues 30-291, expressed as a 6xHis-tagged maltose-binding protein fusion Na compound 35 "[""V8O""]" 1 Ki Ki = = 86.3 nM 86.3 [] unit_conversion 7.06398920428479 success True biochemical_inhibition Stopped-flow CO2 hydration inhibition assay. 5 Table 1 reports compound 35 Ki = 86.3 nM against hCA XII; Figure 5 maps compound 35 bound to hCA XII to PDB 8CO3. auto_single_measurement only accepted activity measurement [1] 1 structures\8CO3\8CO3_metadata.json point structures/8CO3/8co3_protein.pdb structures/8CO3/8co3_pocket.pdb structures/8CO3/8co3_ligand.sdf structures/8CO3/8co3_ligand.pdb structures/8CO3/8co3_ligand.cif structures/8CO3/8co3_complex.pdb structures/8CO3/8co3_complex.cif 8COY extended Plasmodium vivax subtilisin-like protease 1 (PvS1/Sub1) Plasmodium vivax Catalytic domain (PvS1Cat-Tryps), with C-terminal residues 612-617 extension Na MAM-117 "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 225.5 ±32.8 nM 225.5 [] unit_conversion 6.64685345378602 success True biochemical_inhibition IC50 determination of MAM-117 for recombinant PvS1Cat-Tryps active enzyme. 3 Figure S3A explicitly reports an IC50 of 225.5 ±32.8 nM for MAM-117 with PvS1Cat-Tryps; Figure S4 identifies the PvS1Cat-Tryps inhibitor complex as MAM-117. auto_single_measurement only accepted activity measurement [1] 1 structures\8COY\8COY_metadata.json point structures/8COY/8coy_protein.pdb structures/8COY/8coy_pocket.pdb structures/8COY/8coy_ligand.pdb structures/8COY/8coy_ligand.cif structures/8COY/8coy_complex.pdb structures/8COY/8coy_complex.cif 8CP7 classic HiSiaP Haemophilus influenzae HiSiaP CLOSED #2 disulfide-locked construct S15C/A194C Neu5Ac (N-acetylneuraminic acid) "[""SLB""]" 1 Kd Kd ~ ~ 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True direct_binding Isothermal titration calorimetry of HiSiaP CLOSED #2 with Neu5Ac; biphasic binding, with one resolved reaction having an average Kd of approximately 2 µM. 3 “One of the reactions was fully resolved and the average Kd was determined to be in the micromolar range (~2 µM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8CP7\8CP7_metadata.json point structures/8CP7/8cp7_protein.pdb structures/8CP7/8cp7_pocket.pdb structures/8CP7/8cp7_ligand.sdf structures/8CP7/8cp7_ligand.pdb structures/8CP7/8cp7_ligand.cif structures/8CP7/8cp7_complex.pdb structures/8CP7/8cp7_complex.cif 8CQY extended protein tyrosine phosphatase non-receptor type 3 (PTPN3) human N-terminal GST-tagged PTPN3-PDZ, residues 504-597 Na PBM-TACE; sequence RQNRVDSKETEC "[""CHAIN:B""]" 1 Kd Kd = = 30 ± 17 μM 30000.0 [] unit_conversion 4.522878745280337 success True direct_binding 1H,15N HSQC NMR peptide titration of PTPN3-PDZ with PBM-TACE; KD reported in Table 1. 8 “The PBM-TACE peptide binds to PTPN3-PDZ with a KD value of 30 μM” and Table 1 reports PBM-TACE KD “30 ± 17*.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CQY\8CQY_metadata.json point structures/8CQY/8cqy_protein.pdb structures/8CQY/8cqy_pocket.pdb structures/8CQY/8cqy_ligand.pdb structures/8CQY/8cqy_ligand.cif structures/8CQY/8cqy_complex.pdb structures/8CQY/8cqy_complex.cif 8CR0 extended human carbonic anhydrase II human Na Na compound 20 (6-(4-((4-fluorophenoxy)methyl)-1H-1,2,3-triazol-1-yl)benzo[c][1,2]oxaborol-1(3H)-ol) "[""VI6""]" 1 Ki Ki = = 185.8 ± 11.4 nM 185.8 [] unit_conversion 6.7309542903423765 success True biochemical_inhibition Stopped-flow CO2 hydration assay; Table 3. 6 Table 3 reports compound 20 Ki = 185.8 ± 11.4 nM against hCA II. The paper explicitly identifies the deposited hCA II/20 complex as PDB 8CR0. auto_single_measurement only accepted activity measurement [1] 1 structures\8CR0\8CR0_metadata.json point structures/8CR0/8cr0_protein.pdb structures/8CR0/8cr0_pocket.pdb structures/8CR0/8cr0_ligand.pdb structures/8CR0/8cr0_ligand.cif structures/8CR0/8cr0_complex.pdb structures/8CR0/8cr0_complex.cif 8CRH classic Candida auris dihydrofolate reductase (CauDHFR) Candida auris His-tag-free CauDHFR with the N-terminal His tag removed Na cycloguanil (CYG) "[""VIL""]" 1 IC50 IC50 = = 401 µM 401000.0 [] unit_conversion 3.396855627379818 success True biochemical_inhibition NADPH-consumption assay monitoring CauDHFR activity at 340 nm; Table 2 reports biochemical data for CauDHFR with cycloguanil. The 8CRH structure is the CauDHFR–NADPH–CYG ternary complex. 10 Table 2 prints CYG IC50 = 401 µM. The accompanying text states that NADPH-oxidation assays gave CYG an IC50 of 401 µM; Table 1/Figure 1 map 8CRH to CauDHFR–NADPH–CYG. auto_single_measurement only accepted activity measurement [1] 1 structures\8CRH\8CRH_metadata.json point structures/8CRH/8crh_protein.pdb structures/8CRH/8crh_pocket.pdb structures/8CRH/8crh_ligand.sdf structures/8CRH/8crh_ligand.pdb structures/8CRH/8crh_ligand.cif structures/8CRH/8crh_complex.pdb structures/8CRH/8crh_complex.cif 8CRI classic LplA1 Listeria monocytogenes Na Na lipoic acid (LA; R-LA) "[""LPA""]" 1 Kd Kd = = 1.9 ± 0.1 μM 1900.0 [] unit_conversion 5.721246399047171 success True direct_binding ITC with recombinant L. monocytogenes LplA1. 7 Figure 4C reports an ITC KD value of 1.9 μM ± 0.1 μM for LA with L. monocytogenes LplA1. auto_single_measurement only accepted activity measurement [1] 1 structures\8CRI\8CRI_metadata.json point structures/8CRI/8cri_protein.pdb structures/8CRI/8cri_pocket.pdb structures/8CRI/8cri_ligand.sdf structures/8CRI/8cri_ligand.pdb structures/8CRI/8cri_ligand.cif structures/8CRI/8cri_complex.pdb structures/8CRI/8cri_complex.cif 8CRL classic LplA1 Listeria monocytogenes Na Na C3 "[""VK9""]" 1 Kd Kd = = 3.2 ± 0.1 μM 3200.0 [] unit_conversion 5.494850021680094 success True direct_binding ITC with recombinant L. monocytogenes LplA1. 7 Figure 4C reports an ITC KD value of 3.2 μM ± 0.1 μM for C3 with L. monocytogenes LplA1. auto_single_measurement only accepted activity measurement [1] 1 structures\8CRL\8CRL_metadata.json point structures/8CRL/8crl_protein.pdb structures/8CRL/8crl_pocket.pdb structures/8CRL/8crl_ligand.sdf structures/8CRL/8crl_ligand.pdb structures/8CRL/8crl_ligand.cif structures/8CRL/8crl_complex.pdb structures/8CRL/8crl_complex.cif 8CSG classic PRMT5:MEP50 complex human Na Na fragment hit 1 (compound 1) "[""PWL""]" 1 Kd Kd = = 0.74 µM 740.0 [] unit_conversion 6.130768280269024 success True direct_binding SPR binding assay with PRMT5 protein immobilized; PRMT5/MTA complex formed by adding MTA (20 µM). 3 The text reports fragment hit 1 PRMT5/MTA K_D = 0.74 µM and identifies its PRMT5/MTA X-ray co-crystal structure as PDB 8CSG. auto_single_measurement only accepted activity measurement [1] 1 structures\8CSG\8CSG_metadata.json point structures/8CSG/8csg_protein.pdb structures/8CSG/8csg_pocket.pdb structures/8CSG/8csg_ligand.sdf structures/8CSG/8csg_ligand.pdb structures/8CSG/8csg_ligand.cif structures/8CSG/8csg_complex.pdb structures/8CSG/8csg_complex.cif 8CTB classic PRMT5:MEP50 complex human Na Na fragment hit 3 (compound 3) "[""PWX""]" 1 Kd Kd = = 12.0 µM 12000.0 [] unit_conversion 4.920818753952375 success True direct_binding SPR binding assay with PRMT5 protein immobilized; PRMT5/MTA complex formed by adding MTA (20 µM). 3 The text reports fragment hit 3 PRMT5/MTA K_D = 12.0 µM and identifies its PRMT5/MTA X-ray co-crystal structure as PDB 8CTB. auto_single_measurement only accepted activity measurement [1] 1 structures\8CTB\8CTB_metadata.json point structures/8CTB/8ctb_protein.pdb structures/8CTB/8ctb_pocket.pdb structures/8CTB/8ctb_ligand.sdf structures/8CTB/8ctb_ligand.pdb structures/8CTB/8ctb_ligand.cif structures/8CTB/8ctb_complex.pdb structures/8CTB/8ctb_complex.cif 8CUB classic ABCG5/G8 human Na WT (wild-type) cholesterol "[""CLR""]" 1 Kd Kd = = 1.46 ± 0.28 µM 1460.0 [] unit_conversion 5.835647144215563 success True direct_binding Purified His-tagged WT ABCG5/G8 direct cholesterol-binding assay. 5 Figure 2 caption reports cholesterol binding by WT ABCG5/G8 measured with [3H]-cholesterol, with KD = 1.46 ± 0.28 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CUB\8CUB_metadata.json point structures/8CUB/8cub_protein.pdb structures/8CUB/8cub_pocket.pdb structures/8CUB/8cub_ligand.sdf structures/8CUB/8cub_ligand.pdb structures/8CUB/8cub_ligand.cif structures/8CUB/8cub_complex.pdb structures/8CUB/8cub_complex.cif 8CV7 extended BRD2 human BRD2 BD2 residues 347-455; crystallography construct expressed as an N-terminal GST fusion and GST-cleaved Na cyclic peptide 2.2E "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 2 nM 2.0 [] unit_conversion 8.698970004336019 success True direct_binding SPR binding of cyclic peptide 2.2E to BRD2-BD2; Figure 1 gives the representative sensorgram and K_D. 4 Figure 1B explicitly reports K_D = 2 nM for peptide 2.2E binding BRD2-BD2; the text identifies the corresponding complex structure as PDB 8CV7. auto_single_measurement only accepted activity measurement [1] 1 structures\8CV7\8CV7_metadata.json point structures/8CV7/8cv7_protein.pdb structures/8CV7/8cv7_pocket.pdb structures/8CV7/8cv7_ligand.pdb structures/8CV7/8cv7_ligand.cif structures/8CV7/8cv7_complex.pdb structures/8CV7/8cv7_complex.cif 8CVN classic 15-PGDH human Na Na SW209415 ((+)-SW209415) "[""SWL""]" 1 IC50 IC50 = = 0.43 nM 0.43 [] unit_conversion 9.366531544420413 success True biochemical_inhibition Inhibition of purified wild-type 15-PGDH activity; 2 nM protein, 300 µM NAD+, 40 µM PGE2; percent inhibition fitted to a dose-response curve. 7 Fig. 5 caption: “IC50 values for (+)-SW209415 for wild type and Y217A are 0.43 and 0.86 nM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CVN\8CVN_metadata.json point structures/8CVN/8cvn_protein.pdb structures/8CVN/8cvn_pocket.pdb structures/8CVN/8cvn_ligand.sdf structures/8CVN/8cvn_ligand.pdb structures/8CVN/8cvn_ligand.cif structures/8CVN/8cvn_complex.pdb structures/8CVN/8cvn_complex.cif 8CWL classic 15-PGDH human Na Na SW222746 "[""RLD""]" 1 IC50 IC50 = = 1.2 nM 1.2 [] unit_conversion 8.920818753952375 success True biochemical_inhibition Inhibition of purified wild-type 15-PGDH activity; 2 nM protein, 300 µM NAD+, 40 µM PGE2; percent inhibition fitted to a dose-response curve. 7 Fig. 5 caption: “IC50 values for SW222746 for wild type and Y217A are 1.2 and 8.5 nM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CWL\8CWL_metadata.json point structures/8CWL/8cwl_protein.pdb structures/8CWL/8cwl_pocket.pdb structures/8CWL/8cwl_ligand.sdf structures/8CWL/8cwl_ligand.pdb structures/8CWL/8cwl_ligand.cif structures/8CWL/8cwl_complex.pdb structures/8CWL/8cwl_complex.cif 8CX8 classic Stx2A1 Na Stx2A1 residues 1-252 Na BTB13086 "[""P1U""]" 1 Kd Kd = = 554 ± 30 μM 554000.0 [] unit_conversion 3.2564902352715706 success True direct_binding Surface plasmon resonance using Biacore 8K+; P6 peptide control. 4 “The equilibrium dissociation constant (K_D) of BTB13086 was 554 μM.” Figure 4 reports “K_D = 554 ± 30 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8CX8\8CX8_metadata.json point structures/8CX8/8cx8_protein.pdb structures/8CX8/8cx8_pocket.pdb structures/8CX8/8cx8_ligand.sdf structures/8CX8/8cx8_ligand.pdb structures/8CX8/8cx8_ligand.cif structures/8CX8/8cx8_complex.pdb structures/8CX8/8cx8_complex.cif 8CXR classic MraY_AA Aquifex aeolicus MraY_AA expressed as a His10x-MBP fusion with a PreScission protease site; fusion tag cleaved before crystallization Na SPM-1 "[""P5L""]" 1 IC50 IC50 = = 0.17 μM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition UMP-Glo biochemical inhibition assay against purified MraY_AA. 7 “SPM-1 and SPM-2 inhibit MraY_AA with IC50 values of 0.17 μM and 9.2 μM, respectively.” Figure 7a labels SPM-1 IC50 0.17 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXR\8CXR_metadata.json point structures/8CXR/8cxr_protein.pdb structures/8CXR/8cxr_pocket.pdb structures/8CXR/8cxr_ligand.sdf structures/8CXR/8cxr_ligand.pdb structures/8CXR/8cxr_ligand.cif structures/8CXR/8cxr_complex.pdb structures/8CXR/8cxr_complex.cif 8CXS classic CamA adenine methyltransferase Na Na Na MTA "[""MTA""]" 1 IC50 IC50 = = 18 μM 18000.0 [] unit_conversion 4.7447274948966935 success True biochemical_inhibition MTase-Glo inhibition assay; 40 μM SAM co-substrate and DNA substrate. 6 Figure 2A prints “MTA IC50 = 18 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXS\8CXS_metadata.json point structures/8CXS/8cxs_protein.pdb structures/8CXS/8cxs_pocket.pdb structures/8CXS/8cxs_ligand.sdf structures/8CXS/8cxs_ligand.pdb structures/8CXS/8cxs_ligand.cif structures/8CXS/8cxs_complex.pdb structures/8CXS/8cxs_complex.cif 8CXT classic CamA adenine methyltransferase Na Na Na N6-benzyladenosine (Compound 1) "[""Q8C""]" 1 IC50 IC50 = = 15±3 μM 15000.0 [] unit_conversion 4.823908740944319 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 3 table. 7 Figure 3B reports compound 1 IC50 ± SEM = 15±3 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXT\8CXT_metadata.json point structures/8CXT/8cxt_protein.pdb structures/8CXT/8cxt_pocket.pdb structures/8CXT/8cxt_ligand.sdf structures/8CXT/8cxt_ligand.pdb structures/8CXT/8cxt_ligand.cif structures/8CXT/8cxt_complex.pdb structures/8CXT/8cxt_complex.cif 8CXU classic CamA adenine methyltransferase Na Na Na Compound 2 "[""T96""]" 1 IC50 IC50 = = 10±1 μM 10000.0 [] unit_conversion 5.0 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 3 table. 7 Figure 3B reports compound 2 IC50 ± SEM = 10±1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXU\8CXU_metadata.json point structures/8CXU/8cxu_protein.pdb structures/8CXU/8cxu_pocket.pdb structures/8CXU/8cxu_ligand.sdf structures/8CXU/8cxu_ligand.pdb structures/8CXU/8cxu_ligand.cif structures/8CXU/8cxu_complex.pdb structures/8CXU/8cxu_complex.cif 8CXV classic CamA adenine methyltransferase Na Na Na Compound 3 "[""T9R""]" 1 IC50 IC50 = = 4.8±0.6 μM 4800.0 [] unit_conversion 5.318758762624412 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 3 table. 7 Figure 3B reports compound 3 IC50 ± SEM = 4.8±0.6 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXV\8CXV_metadata.json point structures/8CXV/8cxv_protein.pdb structures/8CXV/8cxv_pocket.pdb structures/8CXV/8cxv_ligand.sdf structures/8CXV/8cxv_ligand.pdb structures/8CXV/8cxv_ligand.cif structures/8CXV/8cxv_complex.pdb structures/8CXV/8cxv_complex.cif 8CXW classic CamA adenine methyltransferase Na Na Na piclidenoson (Compound 4) "[""Q8L""]" 1 IC50 IC50 = = 8±1 μM 8000.0 [] unit_conversion 5.096910013008056 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 3 table. 7 Figure 3B reports compound 4 IC50 ± SEM = 8±1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXW\8CXW_metadata.json point structures/8CXW/8cxw_protein.pdb structures/8CXW/8cxw_pocket.pdb structures/8CXW/8cxw_ligand.sdf structures/8CXW/8cxw_ligand.pdb structures/8CXW/8cxw_ligand.cif structures/8CXW/8cxw_complex.pdb structures/8CXW/8cxw_complex.cif 8CXX classic CamA adenine methyltransferase Na Na Na Compound 6 "[""T9I""]" 1 IC50 IC50 = = 43±8 μM 43000.0 [] unit_conversion 4.366531544420414 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 3 table. 7 Figure 3B reports compound 6 IC50 ± SEM = 43±8 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXX\8CXX_metadata.json point structures/8CXX/8cxx_protein.pdb structures/8CXX/8cxx_pocket.pdb structures/8CXX/8cxx_ligand.sdf structures/8CXX/8cxx_ligand.pdb structures/8CXX/8cxx_ligand.cif structures/8CXX/8cxx_complex.pdb structures/8CXX/8cxx_complex.cif 8CXY classic CamA adenine methyltransferase Na Na Na N6-(2-Phenethyl)adenosine (Compound 8) "[""Q8R""]" 1 IC50 IC50 = = 2.5±0.4 μM 2500.0 [] unit_conversion 5.6020599913279625 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 4 table. 8 Figure 4B reports compound 8 IC50 ± SEM = 2.5±0.4 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXY\8CXY_metadata.json point structures/8CXY/8cxy_protein.pdb structures/8CXY/8cxy_pocket.pdb structures/8CXY/8cxy_ligand.sdf structures/8CXY/8cxy_ligand.pdb structures/8CXY/8cxy_ligand.cif structures/8CXY/8cxy_complex.pdb structures/8CXY/8cxy_complex.cif 8CXZ classic CamA adenine methyltransferase Na Na Na N6-(3-Phenylpropyl)adenosine (Compound 14) "[""Q8Y""]" 1 IC50 IC50 = = 0.7±0.1 μM 700.0 [] unit_conversion 6.154901959985743 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 4 table. 8 Figure 4B reports compound 14 IC50 ± SEM = 0.7±0.1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CXZ\8CXZ_metadata.json point structures/8CXZ/8cxz_protein.pdb structures/8CXZ/8cxz_pocket.pdb structures/8CXZ/8cxz_ligand.sdf structures/8CXZ/8cxz_ligand.pdb structures/8CXZ/8cxz_ligand.cif structures/8CXZ/8cxz_complex.pdb structures/8CXZ/8cxz_complex.cif 8CY1 classic CamA adenine methyltransferase Na Na Na Compound 19 "[""QBU""]" 1 IC50 IC50 = = 1.3±0.2 μM 1300.0 [] unit_conversion 5.886056647693163 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 4 table. 8 Figure 4B reports compound 19 IC50 ± SEM = 1.3±0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CY1\8CY1_metadata.json point structures/8CY1/8cy1_protein.pdb structures/8CY1/8cy1_pocket.pdb structures/8CY1/8cy1_ligand.sdf structures/8CY1/8cy1_ligand.pdb structures/8CY1/8cy1_ligand.cif structures/8CY1/8cy1_complex.pdb structures/8CY1/8cy1_complex.cif 8CY3 classic CamA adenine methyltransferase Na Na Na Compound 15 "[""TAI""]" 1 IC50 IC50 = = 1.4±0.2 μM 1400.0 [] unit_conversion 5.853871964321762 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 5 table. 9 Figure 5B reports compound 15 IC50 ± SEM = 1.4±0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CY3\8CY3_metadata.json point structures/8CY3/8cy3_protein.pdb structures/8CY3/8cy3_pocket.pdb structures/8CY3/8cy3_ligand.sdf structures/8CY3/8cy3_ligand.pdb structures/8CY3/8cy3_ligand.cif structures/8CY3/8cy3_complex.pdb structures/8CY3/8cy3_complex.cif 8CY4 classic CamA adenine methyltransferase Na Na Na Compound 16 "[""QA6""]" 1 IC50 IC50 = = 0.51±0.05 μM 510.0 [] unit_conversion 6.292429823902063 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 5 table. 9 Figure 5B reports compound 16 IC50 ± SEM = 0.51±0.05 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CY4\8CY4_metadata.json point structures/8CY4/8cy4_protein.pdb structures/8CY4/8cy4_pocket.pdb structures/8CY4/8cy4_ligand.sdf structures/8CY4/8cy4_ligand.pdb structures/8CY4/8cy4_ligand.cif structures/8CY4/8cy4_complex.pdb structures/8CY4/8cy4_complex.cif 8CY5 classic CamA adenine methyltransferase Na Na Na Compound 39 "[""T8Q""]" 1 IC50 IC50 = = 0.39±0.02 μM 390.0 [] unit_conversion 6.4089353929735005 success True biochemical_inhibition MTase-Glo inhibition assay, Figure 6 table. 10 Figure 6B reports compound 39 IC50 ± SEM = 0.39±0.02 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CY5\8CY5_metadata.json point structures/8CY5/8cy5_protein.pdb structures/8CY5/8cy5_pocket.pdb structures/8CY5/8cy5_ligand.sdf structures/8CY5/8cy5_ligand.pdb structures/8CY5/8cy5_ligand.cif structures/8CY5/8cy5_complex.pdb structures/8CY5/8cy5_complex.cif 8CYI classic human PRMT5:MEP50 complex Homo sapiens Full-length human PRMT5 residues 1-637 and human MEP50 residues 2-342, co-expressed in Sf9 cells Na 11-2F "[""P2R""]" 1 Kd Kd = = 82.1 nM 82.1 [] unit_conversion 7.085656842880559 success True direct_binding SPR binding of 11-2F to PRMT5:MEP50 saturated with 25 μM MTA. 3 Fig. 1c and its caption print KD = 82.1 nM for PRMT5:MEP50 saturated with 25 μM MTA plus 11-2F. auto_single_measurement only accepted activity measurement [1] 1 structures\8CYI\8CYI_metadata.json point structures/8CYI/8cyi_protein.pdb structures/8CYI/8cyi_pocket.pdb structures/8CYI/8cyi_ligand.sdf structures/8CYI/8cyi_ligand.pdb structures/8CYI/8cyi_ligand.cif structures/8CYI/8cyi_complex.pdb structures/8CYI/8cyi_complex.cif 8CYU classic SARS-CoV-2 Mpro SARS-CoV-2 Na Na C5 "[""P5X""]" 2 Kd Kd = = 0.24 ± 0.1 µM 240.0 [] unit_conversion 6.619788758288394 success True direct_binding Microscale thermophoresis inhibitory Kd measurement. 9 Figure 2 panel I reports Kd = 0.24 ± 0.1 µM for C5. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8CYU\8CYU_metadata.json point structures/8CYU/8cyu_protein.pdb structures/8CYU/8cyu_pocket.pdb structures/8CYU/8cyu_ligand.sdf structures/8CYU/8cyu_ligand.pdb structures/8CYU/8cyu_ligand.cif structures/8CYU/8cyu_complex.pdb structures/8CYU/8cyu_complex.cif 8CYZ classic SARS-CoV-2 Mpro SARS-CoV-2 Na Na C4 "[""P6I""]" 2 Kd Kd = = 1.4 ± 0.5 µM 1400.0 [] unit_conversion 5.853871964321762 success True direct_binding Microscale thermophoresis inhibitory Kd measurement. 9 Figure 2 panel H reports Kd = 1.4 ± 0.5 µM for C4. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8CYZ\8CYZ_metadata.json point structures/8CYZ/8cyz_protein.pdb structures/8CYZ/8cyz_pocket.pdb structures/8CYZ/8cyz_ligand.sdf structures/8CYZ/8cyz_ligand.pdb structures/8CYZ/8cyz_ligand.cif structures/8CYZ/8cyz_complex.pdb structures/8CYZ/8cyz_complex.cif 8CZ4 classic SARS-CoV-2 Mpro SARS-CoV-2 Na Na C3 "[""P6R""]" 2 Kd Kd = = 1.9 ± 0.2 µM 1900.0 [] unit_conversion 5.721246399047171 success True direct_binding Microscale thermophoresis inhibitory Kd measurement. 9 Figure 2 panel G reports Kd = 1.9 ± 0.2 µM for C3. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8CZ4\8CZ4_metadata.json point structures/8CZ4/8cz4_protein.pdb structures/8CZ4/8cz4_pocket.pdb structures/8CZ4/8cz4_ligand.sdf structures/8CZ4/8cz4_ligand.pdb structures/8CZ4/8cz4_ligand.cif structures/8CZ4/8cz4_complex.pdb structures/8CZ4/8cz4_complex.cif 8CZ7 classic SARS-CoV-2 Mpro SARS-CoV-2 Na Na C2 "[""P7L""]" 2 Kd Kd = = 1.5 ± 0.3 µM 1500.0 [] unit_conversion 5.823908740944319 success True direct_binding Microscale thermophoresis inhibitory Kd measurement. 9 Figure 2 panel F reports Kd = 1.5 ± 0.3 µM for C2. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8CZ7\8CZ7_metadata.json point structures/8CZ7/8cz7_protein.pdb structures/8CZ7/8cz7_pocket.pdb structures/8CZ7/8cz7_ligand.sdf structures/8CZ7/8cz7_ligand.pdb structures/8CZ7/8cz7_ligand.cif structures/8CZ7/8cz7_complex.pdb structures/8CZ7/8cz7_complex.cif 8CZ9 extended SH2B3 (LNK) mouse SH2B3 SH2 domain, residues 324-446 E372K JAK2 pY813 phosphopeptide "[""CHAIN:C""]" 1 IC50 IC50 = = 685 nM 685.0 [] unit_conversion 6.164309428507575 success True biochemical_inhibition SPR competition assay: E372K SH2B3 SH2 domain binding to JAK2 pY813 peptide, competing with immobilized IL6ST pY757 peptide. 2 “E372K IC50 = 685 nM compared with WT = 127 nM” for the JAK2 pY813 interaction measured by competition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8CZ9\8CZ9_metadata.json point structures/8CZ9/8cz9_protein.pdb structures/8CZ9/8cz9_pocket.pdb structures/8CZ9/8cz9_ligand.pdb structures/8CZ9/8cz9_ligand.cif structures/8CZ9/8cz9_complex.pdb structures/8CZ9/8cz9_complex.cif 8CZA classic BRDT human Na Na GXH-IV-075 "[""ZN1""]" 1 Kd Kd = = 0.16 ± 0.021 nM 0.16 [] unit_conversion 9.795880017344075 success True direct_binding Single qPCR BromoScan binding assay, duplicate (±SD). 3 Table 1 reports GXH-IV-075 Kd for BRDT-1 as 0.16 ± 0.021 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8CZA\8CZA_metadata.json point structures/8CZA/8cza_protein.pdb structures/8CZA/8cza_pocket.pdb structures/8CZA/8cza_ligand.sdf structures/8CZA/8cza_ligand.pdb structures/8CZA/8cza_ligand.cif structures/8CZA/8cza_complex.pdb structures/8CZA/8cza_complex.cif 8D0E classic Human SARM1 TIR domain human SARM1 residues 559-700 Na NB-7 "[""Q0C""]" 1 Kd Kd > > 100 μM 100000.0 [] unit_conversion 4.0 success True direct_binding SPR measurement in the absence of NAD. 4 NB-7 did not bind tightly to the TIR domain, with K_D >100 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8D0E\8D0E_metadata.json point structures/8D0E/8d0e_protein.pdb structures/8D0E/8d0e_pocket.pdb structures/8D0E/8d0e_ligand.sdf structures/8D0E/8d0e_ligand.pdb structures/8D0E/8d0e_ligand.cif structures/8D0E/8d0e_complex.pdb structures/8D0E/8d0e_complex.cif 8D19 classic Human LanCL1 human Na Na GSH "[""GSH""]" 1 Kd Kd = = 9.6 ± 0.6 µM 9600.0 [] unit_conversion 5.017728766960431 success True direct_binding ITC; GSH binding to LanCL1. 4 “we determined the binding affinity of LanCL1 for GSH by isothermal titration calorimetry (ITC), providing a KD,GSH of 9.6 ± 0.6 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8D19\8D19_metadata.json point structures/8D19/8d19_protein.pdb structures/8D19/8d19_pocket.pdb structures/8D19/8d19_ligand.sdf structures/8D19/8d19_ligand.pdb structures/8D19/8d19_ligand.cif structures/8D19/8d19_complex.pdb structures/8D19/8d19_complex.cif 8D6C classic PKMYT1 (Myt1) human Na Na compound 28 "[""QGR""]" 1 IC50 IC50 < < 0.003 µM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition PKMYT1 enzymatic assay; luminescent ADP-detection assay using human recombinant PKMYT1. 3 Table 4 reports compound 28 PKMYT1 enzymatic IC50 <0.003 µM. The experimental assay description identifies human recombinant PKMYT1; the paper maps PDB 8D6C to compound 28. auto_single_measurement only accepted activity measurement [1] 1 structures\8D6C\8D6C_metadata.json point structures/8D6C/8d6c_protein.pdb structures/8D6C/8d6c_pocket.pdb structures/8D6C/8d6c_ligand.sdf structures/8D6C/8d6c_ligand.pdb structures/8D6C/8d6c_ligand.cif structures/8D6C/8d6c_complex.pdb structures/8D6C/8d6c_complex.cif 8D6O classic saxiphilin Nanorana parkeri Na Na F-STX "[""QDX""]" 1 Kd Kd = = 0.5 ± 0.3 nM 0.5 [] unit_conversion 9.301029995663981 success True direct_binding Fluorescence-polarization binding assay. 10 Table 2 prints NpSxph Kd = 0.5 ± 0.3 nM; the text identifies the FP measurements as F-STX binding. auto_single_measurement only accepted activity measurement [1] 1 structures\8D6O\8D6O_metadata.json point structures/8D6O/8d6o_protein.pdb structures/8D6O/8d6o_pocket.pdb structures/8D6O/8d6o_ligand.sdf structures/8D6O/8d6o_ligand.pdb structures/8D6O/8d6o_ligand.cif structures/8D6O/8d6o_complex.pdb structures/8D6O/8d6o_complex.cif 8D6U classic saxiphilin Rana catesbeiana Na Na F-STX "[""QDX""]" 1 Kd Kd = = 7.4 ± 2.6 nM 7.4 [] unit_conversion 8.130768280269024 success True direct_binding Fluorescence-polarization binding assay with fluorescein-labelled STX (F-STX). 3 The Results text explicitly reports RcSxph:F-STX fluorescence-polarization Kd = 7.4 ± 2.6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8D6U\8D6U_metadata.json point structures/8D6U/8d6u_protein.pdb structures/8D6U/8d6u_pocket.pdb structures/8D6U/8d6u_ligand.sdf structures/8D6U/8d6u_ligand.pdb structures/8D6U/8d6u_ligand.cif structures/8D6U/8d6u_complex.pdb structures/8D6U/8d6u_complex.cif 8D95 classic Complement Factor D Na Na Na compound 1 "[""QIE""]" 1 IC50 IC50 = = 35 µM 35000.0 [] unit_conversion 4.455931955649724 success True biochemical_inhibition Esterolytic assay of purified recombinant human Complement Factor D using a synthetic peptide substrate. 4 Table 1 reports compound 1: Esterolytic IC50 = 35 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8D95\8D95_metadata.json point structures/8D95/8d95_protein.pdb structures/8D95/8d95_pocket.pdb structures/8D95/8d95_ligand.sdf structures/8D95/8d95_ligand.pdb structures/8D95/8d95_ligand.cif structures/8D95/8d95_complex.pdb structures/8D95/8d95_complex.cif 8D98 classic histone deacetylase 6 (HDAC6) Danio rerio HDAC6 catalytic domain 2 encoded in the His6-MBP-TEV-HDAC6-pET28a-(+) vector wild-type compound 5 (3,5-difluorophenylhydroxamic acid; meta-difluorophenylhydroxamate) "[""QHX""]" 1 IC50 IC50 = = 1600 ± 100 nM 1600.0 [] unit_conversion 5.795880017344075 success True biochemical_inhibition Fluor-de-Lys fluorogenic-substrate inhibition assay using Danio rerio HDAC6 catalytic domain 2. 4 Table 2 reports zebrafish HDAC6 CD2 IC50 = 1600 ± 100 nM for inhibitor 5; the Methods describe the fluorogenic biochemical inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8D98\8D98_metadata.json point structures/8D98/8d98_protein.pdb structures/8D98/8d98_pocket.pdb structures/8D98/8d98_ligand.sdf structures/8D98/8d98_ligand.pdb structures/8D98/8d98_ligand.cif structures/8D98/8d98_complex.pdb structures/8D98/8d98_complex.cif 8D99 classic histone deacetylase 6 (HDAC6) Danio rerio HDAC6 catalytic domain 2 encoded in the His6-MBP-TEV-HDAC6-pET28a-(+) vector wild-type compound 7 (2,3,6-trifluorophenylhydroxamic acid) "[""QH7""]" 1 IC50 IC50 > > 20,000 nM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition Fluor-de-Lys fluorogenic-substrate inhibition assay using Danio rerio HDAC6 catalytic domain 2. 4 Table 2 reports zebrafish HDAC6 CD2 IC50 >20,000 nM for inhibitor 7; the Methods describe the fluorogenic biochemical inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8D99\8D99_metadata.json point structures/8D99/8d99_protein.pdb structures/8D99/8d99_pocket.pdb structures/8D99/8d99_ligand.sdf structures/8D99/8d99_ligand.pdb structures/8D99/8d99_ligand.cif structures/8D99/8d99_complex.pdb structures/8D99/8d99_complex.cif 8D9A classic histone deacetylase 6 (HDAC6) Danio rerio HDAC6 catalytic domain 2 encoded in the His6-MBP-TEV-HDAC6-pET28a-(+) vector wild-type compound 8 (2,3,5-trifluorophenylhydroxamic acid) "[""QHO""]" 1 IC50 IC50 = = 4600 ± 500 nM 4600.0 [] unit_conversion 5.337242168318426 success True biochemical_inhibition Fluor-de-Lys fluorogenic-substrate inhibition assay using Danio rerio HDAC6 catalytic domain 2. 4 Table 2 reports zebrafish HDAC6 CD2 IC50 = 4600 ± 500 nM for inhibitor 8; the Methods describe the fluorogenic biochemical inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8D9A\8D9A_metadata.json point structures/8D9A/8d9a_protein.pdb structures/8D9A/8d9a_pocket.pdb structures/8D9A/8d9a_ligand.sdf structures/8D9A/8d9a_ligand.pdb structures/8D9A/8d9a_ligand.cif structures/8D9A/8d9a_complex.pdb structures/8D9A/8d9a_complex.cif 8D9B classic histone deacetylase 6 (HDAC6) Danio rerio HDAC6 catalytic domain 2 encoded in the His6-MBP-TEV-HDAC6-pET28a-(+) vector wild-type compound 9 (2,3,5,6-tetrafluorophenylhydroxamic acid) "[""QI8""]" 1 IC50 IC50 > > 20,000 nM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition Fluor-de-Lys fluorogenic-substrate inhibition assay using Danio rerio HDAC6 catalytic domain 2. 4 Table 2 reports zebrafish HDAC6 CD2 IC50 >20,000 nM for inhibitor 9; the Methods describe the fluorogenic biochemical inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8D9B\8D9B_metadata.json point structures/8D9B/8d9b_protein.pdb structures/8D9B/8d9b_pocket.pdb structures/8D9B/8d9b_ligand.sdf structures/8D9B/8d9b_ligand.pdb structures/8D9B/8d9b_ligand.cif structures/8D9B/8d9b_complex.pdb structures/8D9B/8d9b_complex.cif 8D9C classic histone deacetylase 6 (HDAC6) Danio rerio HDAC6 catalytic domain 2 encoded in the His6-MBP-TEV-HDAC6-pET28a-(+) vector wild-type compound 10 (2,3,4,5,6-pentafluorophenylhydroxamic acid) "[""QI5""]" 1 IC50 IC50 > > 20,000 nM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition Fluor-de-Lys fluorogenic-substrate inhibition assay using Danio rerio HDAC6 catalytic domain 2. 4 Table 2 reports zebrafish HDAC6 CD2 IC50 >20,000 nM for inhibitor 10; the Methods describe the fluorogenic biochemical inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8D9C\8D9C_metadata.json point structures/8D9C/8d9c_protein.pdb structures/8D9C/8d9c_pocket.pdb structures/8D9C/8d9c_ligand.sdf structures/8D9C/8d9c_ligand.pdb structures/8D9C/8d9c_ligand.cif structures/8D9C/8d9c_complex.pdb structures/8D9C/8d9c_complex.cif 8DBB classic D-DT (D-dopachrome tautomerase) Na Na Na 2,5-pyridinedicarboxylic acid (compound 1) "[""R3K""]" 2 Kd Kd = = 36 µM 36000.0 [] unit_conversion 4.443697499232713 success True direct_binding Isothermal titration calorimetry of the D-DT–compound 1 interaction. 4 “Our ITC findings demonstrate a 1:1 interaction of ligand to D-DT with a dissociation constant (KD) of 36 µM.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8DBB\8DBB_metadata.json point structures/8DBB/8dbb_protein.pdb structures/8DBB/8dbb_pocket.pdb structures/8DBB/8dbb_ligand.sdf structures/8DBB/8dbb_ligand.pdb structures/8DBB/8dbb_ligand.cif structures/8DBB/8dbb_complex.pdb structures/8DBB/8dbb_complex.cif 8DCH classic Highly resistant HIV-1 protease clinical isolate PR10x HIV-1 (human immunodeficiency virus type 1) Optimized recombinant protease PR10x PR10x has 20 mutations; explicitly named substitutions include L10F, V32I, M46I, I54L, L63P, A71V, L76V, I84V, L89V, L90M, K20T, M36I, I93L, Q7K, L33I, C95A, T74S, C67E, T91S, and E35N GRL-0519 (GRL-519) "[""G52""]" 1 Ki Ki = = 26 ± 2 nM 26.0 [] unit_conversion 7.585026652029182 success True biochemical_inhibition Purified-protease FRET continuous assay; Ki calculated from dose-response IC50 values for tight-binding inhibitors. 12 Table 1 reports Ki PR10x = 26 ± 2 nM for GRL-519. auto_single_measurement only accepted activity measurement [1] 1 structures\8DCH\8DCH_metadata.json point structures/8DCH/8dch_protein.pdb structures/8DCH/8dch_pocket.pdb structures/8DCH/8dch_ligand.sdf structures/8DCH/8dch_ligand.pdb structures/8DCH/8dch_ligand.cif structures/8DCH/8dch_complex.pdb structures/8DCH/8dch_complex.cif 8DEA classic Complement Factor D Na Na Na compound 3 "[""R7X""]" 1 IC50 IC50 = = 3.4 µM 3400.0 [] unit_conversion 5.468521082957745 success True biochemical_inhibition Esterolytic assay of purified recombinant human Complement Factor D using a synthetic peptide substrate. 4 Table 1 reports compound 3: Esterolytic IC50 = 3.4 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8DEA\8DEA_metadata.json point structures/8DEA/8dea_protein.pdb structures/8DEA/8dea_pocket.pdb structures/8DEA/8dea_ligand.sdf structures/8DEA/8dea_ligand.pdb structures/8DEA/8dea_ligand.cif structures/8DEA/8dea_complex.pdb structures/8DEA/8dea_complex.cif 8DGH extended calmodulin Na Ca2+-bound calmodulin C-lobe bound to CaM2 peptide, CNGB1 residues 1120-1147 Na CaM2 (CNGB1 residues 1120-1147) "[""CHAIN:B""]" 1 Kd Kd = = 100 ± 20 nM 100.0 [] unit_conversion 7.0 success True direct_binding ITC of isolated CaM C-lobe with CaM2 peptide. 5 “CaM2 peptide binds ... to an isolated CaM C-lobe fragment ... with Kd equal to 100 ± 20 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8DGH\8DGH_metadata.json point structures/8DGH/8dgh_protein.pdb structures/8DGH/8dgh_pocket.pdb structures/8DGH/8dgh_ligand.pdb structures/8DGH/8dgh_ligand.cif structures/8DGH/8dgh_complex.pdb structures/8DGH/8dgh_complex.cif 8DGK extended calmodulin Na Ca2+-bound calmodulin N-lobe bound to CaM1 peptide, CNGB1 residues 565-589 Na CaM1 (CNGB1 residues 565-589) "[""CHAIN:B""]" 1 Kd Kd = = 5.7 ± 1 μM 5700.0 [] unit_conversion 5.2441251443275085 success True direct_binding ITC of isolated CaM N-lobe with CaM1 peptide. 5 “CaM1 binding to an isolated CaM N-lobe fragment ... is exothermic ... with Kd of 5.7 ± 1 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8DGK\8DGK_metadata.json point structures/8DGK/8dgk_protein.pdb structures/8DGK/8dgk_pocket.pdb structures/8DGK/8dgk_ligand.pdb structures/8DGK/8dgk_ligand.cif structures/8DGK/8dgk_complex.pdb structures/8DGK/8dgk_complex.cif 8DGO extended Growth factor receptor-bound protein 2 (Grb2) human Full-length Grb2, residues 1-217 Na PEAK3 SH2-pY peptide (TpYSNLGQ; pY24) "[""CHAIN:C""]" 1 Kd Kd = = 4.6 μM 4600.0 [] unit_conversion 5.337242168318426 success True direct_binding SPR affinity of PEAK phosphopeptides; Fig. 2e, consensus pY motif TpYSNLGQ against Grb2 full length. 4 Fig. 2e reports K_D 4.6 μM for the consensus pY motif TpYSNLGQ binding Grb2FL. auto_single_measurement only accepted activity measurement [1] 1 structures\8DGO\8DGO_metadata.json point structures/8DGO/8dgo_protein.pdb structures/8DGO/8dgo_pocket.pdb structures/8DGO/8dgo_ligand.pdb structures/8DGO/8dgo_ligand.cif structures/8DGO/8dgo_complex.pdb structures/8DGO/8dgo_complex.cif 8DGQ extended p120RasGAP human SH2-SH3-SH2 region, residues 174-444, expressed with an N-terminal His6 tag and TEV protease site C236S, C261S, C372S, C402S p190RhoGAP doubly phosphorylated peptide, pY-1087 and pY-1105 "[""CHAIN:U"", ""CHAIN:V""]" 1 Kd Kd = = 10 ± 6 nM 10.0 [] unit_conversion 8.0 success True direct_binding Isothermal titration calorimetry (ITC) of p120RasGAP SH2-SH3-SH2 with the doubly phosphorylated p190RhoGAP peptide. 4 Table 1 reports Kd = 10 ± 6 nM for “SH2-SH3-SH2/pYpY”; the Results text identifies this as ITC binding of the human p120RasGAP SH2-SH3-SH2 region to the doubly phosphorylated p190RhoGAP-A peptide. Methods specify the four Cys-to-Ser construct mutations. auto_single_measurement only accepted activity measurement [1] 1 structures\8DGQ\8DGQ_metadata.json point structures/8DGQ/8dgq_protein.pdb structures/8DGQ/8dgq_pocket.pdb structures/8DGQ/8dgq_ligand.pdb structures/8DGQ/8dgq_ligand.cif structures/8DGQ/8dgq_complex.pdb structures/8DGQ/8dgq_complex.cif 8DI4 classic PDE10A Na PDE10A catalytic domain, residues 439-779 Na compound 18; MK-8189 "[""S9I""]" 1 Ki Ki = = 0.029 nM 0.029 [] unit_conversion 10.537602002101044 success True biochemical_inhibition In vitro PDE biochemical assay; apparent Ki for MK-8189/compound 18 against human PDE10A using cGMP substrate. 6 “The functional Ki of 18 on the human PDE10A enzyme is 0.029 nM.” The assay methods state that apparent Ki values for MK-8189 against PDE enzymes were determined in duplicate at room temperature. auto_single_measurement only accepted activity measurement [1] 1 structures\8DI4\8DI4_metadata.json point structures/8DI4/8di4_protein.pdb structures/8DI4/8di4_pocket.pdb structures/8DI4/8di4_ligand.sdf structures/8DI4/8di4_ligand.pdb structures/8DI4/8di4_ligand.cif structures/8DI4/8di4_complex.pdb structures/8DI4/8di4_complex.cif 8DIG classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound '5548 (Z4929615548) "[""U26""]" 1 IC50 IC50 = = 30 μM 30000.0 [] unit_conversion 4.522878745280337 success True biochemical_inhibition Mpro enzyme inhibition assay; DMSO condition 9 Figure 2e labels Z4929615548 with IC50[DMSO] = 30 μM and identifies it as '5548; its caption maps '5548 to PDB 8DIG. auto_single_measurement only accepted activity measurement [1] 1 structures\8DIG\8DIG_metadata.json point structures/8DIG/8dig_protein.pdb structures/8DIG/8dig_pocket.pdb structures/8DIG/8dig_ligand.sdf structures/8DIG/8dig_ligand.pdb structures/8DIG/8dig_ligand.cif structures/8DIG/8dig_complex.pdb structures/8DIG/8dig_complex.cif 8DIH classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound '6111 (Z4929616111) "[""U2B""]" 1 IC50 IC50 = = 25 μM 25000.0 [] unit_conversion 4.6020599913279625 success True biochemical_inhibition Mpro enzyme inhibition assay; DMSO condition 9 Figure 2f labels Z4929616111 with IC50[DMSO] = 25 μM and identifies it as '6111; its caption maps '6111 to PDB 8DIH. auto_single_measurement only accepted activity measurement [1] 1 structures\8DIH\8DIH_metadata.json point structures/8DIH/8dih_protein.pdb structures/8DIH/8dih_pocket.pdb structures/8DIH/8dih_ligand.sdf structures/8DIH/8dih_ligand.pdb structures/8DIH/8dih_ligand.cif structures/8DIH/8dih_complex.pdb structures/8DIH/8dih_complex.cif 8DII classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na SG-0001 "[""U2I""]" 1 IC50 IC50 = = 55 μM 55000.0 [] unit_conversion 4.259637310505756 success True biochemical_inhibition Mpro enzyme inhibition assay 9 The Figure 2 caption reports SG-0001 IC50 = 55 μM and identifies its crystal structure as PDB 8DII. auto_single_measurement only accepted activity measurement [1] 1 structures\8DII\8DII_metadata.json point structures/8DII/8dii_protein.pdb structures/8DII/8dii_pocket.pdb structures/8DII/8dii_ligand.sdf structures/8DII/8dii_ligand.pdb structures/8DII/8dii_ligand.cif structures/8DII/8dii_complex.pdb structures/8DII/8dii_complex.cif 8DJ3 classic Caspase-7 Na Na Na inhibitor 2 "[""SE1""]" 2 Ki Ki = = 128.8 ± 25.3 µM 128800.00000000001 [] unit_conversion 3.8900841369762063 success True biochemical_inhibition Fluorometric steady-state kinetics assay; Table 1, C7 wt; Ki determined using a noncompetitive-inhibitor equation. 2 Table 1 prints the inhibitor 2 Ki for Caspase-7 wt as 128.8 ± 25.3 µM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8DJ3\8DJ3_metadata.json point structures/8DJ3/8dj3_protein.pdb structures/8DJ3/8dj3_pocket.pdb structures/8DJ3/8dj3_ligand.sdf structures/8DJ3/8dj3_ligand.pdb structures/8DJ3/8dj3_ligand.cif structures/8DJ3/8dj3_complex.pdb structures/8DJ3/8dj3_complex.cif 8DJH extended SUMO1 human SUMO1 residues 2-97; complexed with PML-SIM-4SD peptide residues 547-573 SUMO1 C52A; PML-SIM-4SD S560D, S561D, S562D, S565D PML-SIM-4SD "[""CHAIN:B""]" 1 Kd Kd = = 0.57 ± 0.08 μM 570.0 [] unit_conversion 6.2441251443275085 success True direct_binding ITC in the presence of 1 mM ZnSO4; SUMO1:PML-SIM-4SD:Zn ternary binding condition. 12 Figure 6B reports PML-SIM-4SD Kd of 0.57 ± 0.08 μM with ZnSO4. auto_single_measurement only accepted activity measurement [1] 1 structures\8DJH\8DJH_metadata.json point structures/8DJH/8djh_protein.pdb structures/8DJH/8djh_pocket.pdb structures/8DJH/8djh_ligand.pdb structures/8DJH/8djh_ligand.cif structures/8DJH/8djh_complex.pdb structures/8DJH/8djh_complex.cif 8DJI extended SUMO1 human SUMO1 residues 2-97; complexed with PML-SIM peptide residues 547-573 SUMO1 C52A PML-SIM "[""CHAIN:B""]" 1 Kd Kd = = 42 ± 8.0 μM 42000.0 [] unit_conversion 4.376750709602099 success True direct_binding ITC in the presence of 1 mM ZnSO4; SUMO1:PML-SIM:Zn ternary binding condition. 12 Figure 6B reports PML-SIM Kd of 42 ± 8.0 μM with ZnSO4. auto_single_measurement only accepted activity measurement [1] 1 structures\8DJI\8DJI_metadata.json point structures/8DJI/8dji_protein.pdb structures/8DJI/8dji_pocket.pdb structures/8DJI/8dji_ligand.pdb structures/8DJI/8dji_ligand.cif structures/8DJI/8dji_complex.pdb structures/8DJI/8dji_complex.cif 8DKS classic IRAK4 Na Na Na compound 3 "[""SO9""]" 1 IC50 IC50 = = 0.003 µM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition IRAK4 biochemical assay; Table 1. 2 Table 1 reports compound 3 with IRAK4 IC50 = 0.003 µM. The text states compound 3 has IRAK4 biochemical potency and describes its co-crystal structure with IRAK4. auto_single_measurement only accepted activity measurement [1] 1 structures\8DKS\8DKS_metadata.json point structures/8DKS/8dks_protein.pdb structures/8DKS/8dks_pocket.pdb structures/8DKS/8dks_ligand.sdf structures/8DKS/8dks_ligand.pdb structures/8DKS/8dks_ligand.cif structures/8DKS/8dks_complex.pdb structures/8DKS/8dks_complex.cif 8DML classic VtrA/VtrC complex Vibrio parahaemolyticus VtrC residues 31-161 and VtrA residues 161-253; VtrC N-terminal hexahistidine tag Na chenodeoxycholate (CDC) "[""JN3""]" 1 Kd Kd = = 310.3 nM 310.3 [] unit_conversion 6.508218224415835 success True direct_binding ITC of purified VtrA–VtrC periplasmic-domain complex; 25 °C, assay buffer 50 mM Tris pH 8.0 and 100 mM NaCl. 3 Table 1 reports WT VtrA–VtrC binding CDC with KD 310.3 nM; the text identifies this as ITC-measured CDC binding. auto_single_measurement only accepted activity measurement [1] 1 structures\8DML\8DML_metadata.json point structures/8DML/8dml_protein.pdb structures/8DML/8dml_pocket.pdb structures/8DML/8dml_ligand.sdf structures/8DML/8dml_ligand.pdb structures/8DML/8dml_ligand.cif structures/8DML/8dml_complex.pdb structures/8DML/8dml_complex.cif 8DMM classic MsbA Na Na Na KDL "[""KDL""]" 1 Kd Kd = = 0.3 μM 300.0 [] unit_conversion 6.522878745280337 success True direct_binding Native-MS equilibrium lipid-binding analysis of copper(II)-bound, ADP- and vanadate-trapped MsbA; the trapped state is the state used for the 8DMM KDL complex. 4 “the binding affinity for KDL (K_D1 = 0.3 μM) significantly increased by two-fold compared to the non-trapped protein”. auto_single_measurement only accepted activity measurement [1] 1 structures\8DMM\8DMM_metadata.json point structures/8DMM/8dmm_protein.pdb structures/8DMM/8dmm_pocket.pdb structures/8DMM/8dmm_ligand.sdf structures/8DMM/8dmm_ligand.pdb structures/8DMM/8dmm_ligand.cif structures/8DMM/8dmm_complex.pdb structures/8DMM/8dmm_complex.cif 8DNQ extended BRD2 human BRD2 BD1 residues 65-194; crystallography construct expressed as an N-terminal GST fusion and GST-cleaved Na cyclic peptide 2.2B "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.4 nM 0.4 [] unit_conversion 9.397940008672037 success True direct_binding SPR panel measuring peptide 2.2B across BET bromodomains; the BRD2-BD1 value is shown in Figure 1C. 4 Figure 1C gives the BRD2-BD1 K_D for peptide 2.2B as 0.4 nM; the adjacent text identifies the BRD2-BD1:2.2B crystal structure as PDB 8DNQ. auto_single_measurement only accepted activity measurement [1] 1 structures\8DNQ\8DNQ_metadata.json point structures/8DNQ/8dnq_protein.pdb structures/8DNQ/8dnq_pocket.pdb structures/8DNQ/8dnq_ligand.pdb structures/8DNQ/8dnq_ligand.cif structures/8DNQ/8dnq_complex.pdb structures/8DNQ/8dnq_complex.cif 8DP7 classic EgtU Helicobacter pylori EgtU soluble-binding domain, residues R282-L553 Na ergothioneine (EGT) "[""LW8""]" 1 Kd Kd = = 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True direct_binding Isothermal titration calorimetry of purified H. pylori EgtU SBD binding EGT. 5 The paper reports that the purified EgtU SBD bound EGT with low-micromolar affinity (Kd = 2 µM; Figure 2G). auto_single_measurement only accepted activity measurement [1] 1 structures\8DP7\8DP7_metadata.json point structures/8DP7/8dp7_protein.pdb structures/8DP7/8dp7_pocket.pdb structures/8DP7/8dp7_ligand.sdf structures/8DP7/8dp7_ligand.pdb structures/8DP7/8dp7_ligand.cif structures/8DP7/8dp7_complex.pdb structures/8DP7/8dp7_complex.cif 8DQF classic Neisseria gonorrhoeae alpha-carbonic anhydrase (alpha-NgCA) Neisseria gonorrhoeae Na Na 3; N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)cyclohexanecarboxamide "[""VGV""]" 1 Ki Ki = = 9.8 ± 0.4 nM 9.8 [] unit_conversion 8.008773924307505 success True biochemical_inhibition CO2 hydration assay inhibition; Table 1 reports mean of one experiment in triplicate, with standard error. 2 Table 1 lists compound 3 with Ki 9.8 ± 0.4 nM against α-NgCA; the text identifies the structure of 3 as PDB 8DQF. auto_single_measurement only accepted activity measurement [1] 1 structures\8DQF\8DQF_metadata.json point structures/8DQF/8dqf_protein.pdb structures/8DQF/8dqf_pocket.pdb structures/8DQF/8dqf_ligand.sdf structures/8DQF/8dqf_ligand.pdb structures/8DQF/8dqf_ligand.cif structures/8DQF/8dqf_complex.pdb structures/8DQF/8dqf_complex.cif 8DRB classic Neisseria gonorrhoeae alpha-carbonic anhydrase (alpha-NgCA) Neisseria gonorrhoeae Na Na 8; 3-phenyl-N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)propanamide "[""TBW""]" 1 Ki Ki = = 8.3 ± 0.4 nM 8.3 [] unit_conversion 8.080921907623926 success True biochemical_inhibition CO2 hydration assay inhibition; Table 1 reports mean of one experiment in triplicate, with standard error. 2 Table 1 lists compound 8 with Ki 8.3 ± 0.4 nM against α-NgCA; Figure 4 identifies the structure of 8 as PDB 8DRB. auto_single_measurement only accepted activity measurement [1] 1 structures\8DRB\8DRB_metadata.json point structures/8DRB/8drb_protein.pdb structures/8DRB/8drb_pocket.pdb structures/8DRB/8drb_ligand.sdf structures/8DRB/8drb_ligand.pdb structures/8DRB/8drb_ligand.cif structures/8DRB/8drb_complex.pdb structures/8DRB/8drb_complex.cif 8DSF classic cIAP1 Na cIAP1 Bir3 domain, residues 260-352 Na BCCov "[""TO0""]" 1 Kd Kd <= <= 10 nM 10.0 [] unit_conversion 8.0 success True direct_binding Biolayer interferometry of the cIAP1Bir3–BCCov binary complex. 5 The paper states that, despite difficulty determining the absolute Kd, it can “confidently assign an affinity of ≤10 nM” for BCCov in the cIAP1–BCCov binary-binding discussion. auto_single_measurement only accepted activity measurement [1] 1 structures\8DSF\8DSF_metadata.json point structures/8DSF/8dsf_protein.pdb structures/8DSF/8dsf_pocket.pdb structures/8DSF/8dsf_ligand.sdf structures/8DSF/8dsf_ligand.pdb structures/8DSF/8dsf_ligand.cif structures/8DSF/8dsf_complex.pdb structures/8DSF/8dsf_complex.cif 8DSY classic PPARgamma Na Na Na H3B-343 "[""TJC""]" 1 IC50 IC50 = = 9.2 ± 7 nM 9.2 [] unit_conversion 8.036212172654444 success True direct_binding TR-FRET Fluormone competition assay 7 Table 1 reports H3B-343 IC50 9.2 ± 7 nM; table notes IC50 refers to the Fluormone assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8DSY\8DSY_metadata.json point structures/8DSY/8dsy_protein.pdb structures/8DSY/8dsy_pocket.pdb structures/8DSY/8dsy_ligand.sdf structures/8DSY/8dsy_ligand.pdb structures/8DSY/8dsy_ligand.cif structures/8DSY/8dsy_complex.pdb structures/8DSY/8dsy_complex.cif 8DSZ classic PPARgamma Na Na Na H3B-487 "[""TJO""]" 1 IC50 IC50 = = 220 ± 47 nM 220.0 [] unit_conversion 6.657577319177793 success True direct_binding TR-FRET Fluormone competition assay 7 Table 1 reports H3B-487 IC50 220 ± 47 nM; table notes IC50 refers to the Fluormone assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8DSZ\8DSZ_metadata.json point structures/8DSZ/8dsz_protein.pdb structures/8DSZ/8dsz_pocket.pdb structures/8DSZ/8dsz_ligand.sdf structures/8DSZ/8dsz_ligand.pdb structures/8DSZ/8dsz_ligand.cif structures/8DSZ/8dsz_complex.pdb structures/8DSZ/8dsz_complex.cif 8DVL extended LRP6 Na LRP6 E3E4, residues E631-Q1253 Na disulfide constrained peptide E3.18 "[""CHAIN:B""]" 1 Kd Kd = = 28 ± 4.2 nM 28.0 [] unit_conversion 7.552841968657781 success True direct_binding Surface plasmon resonance binding to immobilized LRP6 E3E4; average dissociation constant, Kd ± SD (N = 3). 2 Figure 1c lists E3.18 with Kd 28 ± 4.2 nM; the caption states these are selective-binder dissociation constants against immobilized LRP6 E3E4 determined by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\8DVL\8DVL_metadata.json point structures/8DVL/8dvl_protein.pdb structures/8DVL/8dvl_pocket.pdb structures/8DVL/8dvl_ligand.pdb structures/8DVL/8dvl_ligand.cif structures/8DVL/8dvl_complex.pdb structures/8DVL/8dvl_complex.cif 8DVM extended LRP6 Na LRP6 E3E4, residues E631-Q1253 Na disulfide constrained peptide E3.6 "[""CHAIN:B""]" 1 Kd Kd = = 247 ± 76.5 nM 247.0 [] unit_conversion 6.607303046740334 success True direct_binding Surface plasmon resonance binding to immobilized LRP6 E3E4; average dissociation constant, Kd ± SD (N = 3). 2 Figure 1c lists E3.6 with Kd 247 ± 76.5 nM; the caption states these are selective-binder dissociation constants against immobilized LRP6 E3E4 determined by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\8DVM\8DVM_metadata.json point structures/8DVM/8dvm_protein.pdb structures/8DVM/8dvm_pocket.pdb structures/8DVM/8dvm_ligand.pdb structures/8DVM/8dvm_ligand.cif structures/8DVM/8dvm_complex.pdb structures/8DVM/8dvm_complex.cif 8DVN extended LRP6 Na LRP6 E3E4, residues E631-Q1253 Na disulfide constrained peptide E3.10 "[""CHAIN:B""]" 1 Kd Kd = = 24 ± 4.5 nM 24.0 [] unit_conversion 7.619788758288394 success True direct_binding Surface plasmon resonance binding to immobilized LRP6 E3E4; average dissociation constant, Kd ± SD (N = 3). 2 Figure 1c lists E3.10 with Kd 24 ± 4.5 nM; the caption states these are selective-binder dissociation constants against immobilized LRP6 E3E4 determined by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\8DVN\8DVN_metadata.json point structures/8DVN/8dvn_protein.pdb structures/8DVN/8dvn_pocket.pdb structures/8DVN/8dvn_ligand.pdb structures/8DVN/8dvn_ligand.cif structures/8DVN/8dvn_complex.pdb structures/8DVN/8dvn_complex.cif 8DYB classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na T252A 4-methylthiobenzoic acid "[""4MI""]" 1 Kd Kd = = 1.4 ± 0.1 µM 1400.0 [] unit_conversion 5.853871964321762 success True direct_binding UV-vis substrate-binding/Soret-shift analysis; Table 1. 7 Table 1 reports Kd = 1.4 ± 0.1 µM for 4-methylthioBA/T252A. auto_single_measurement only accepted activity measurement [1] 1 structures\8DYB\8DYB_metadata.json point structures/8DYB/8dyb_protein.pdb structures/8DYB/8dyb_pocket.pdb structures/8DYB/8dyb_ligand.sdf structures/8DYB/8dyb_ligand.pdb structures/8DYB/8dyb_ligand.cif structures/8DYB/8dyb_complex.pdb structures/8DYB/8dyb_complex.cif 8DYG classic IL17A homodimer Na Na Na Compound 7 "[""U5Q""]" 1 Kd Kd = = 40 μM 40000.0 [] unit_conversion 4.3979400086720375 success True direct_binding SPR binding to IL17A 6 Figure 4 prints “SPR K_D 40 μM” for Compound 7. auto_single_measurement only accepted activity measurement [1] 1 structures\8DYG\8DYG_metadata.json point structures/8DYG/8dyg_protein.pdb structures/8DYG/8dyg_pocket.pdb structures/8DYG/8dyg_ligand.sdf structures/8DYG/8dyg_ligand.pdb structures/8DYG/8dyg_ligand.cif structures/8DYG/8dyg_complex.pdb structures/8DYG/8dyg_complex.cif 8DYH classic IL17A homodimer Na Na Na Compound 6 "[""U5X""]" 1 Kd Kd = = 72 μM 72000.0 [] unit_conversion 4.142667503568732 success True direct_binding SPR binding to IL17A 6 Figure 4 prints “SPR K_D 72 μM” for Compound 6. auto_single_measurement only accepted activity measurement [1] 1 structures\8DYH\8DYH_metadata.json point structures/8DYH/8dyh_protein.pdb structures/8DYH/8dyh_pocket.pdb structures/8DYH/8dyh_ligand.sdf structures/8DYH/8dyh_ligand.pdb structures/8DYH/8dyh_ligand.cif structures/8DYH/8dyh_complex.pdb structures/8DYH/8dyh_complex.cif 8DYI extended IL17A homodimer Na Na Na Compound 5 "[""U6C""]" 1 Kd Kd = = 12 μM 12000.0 [] unit_conversion 4.920818753952375 success True direct_binding 2D NMR titration binding to IL17A 4 The text states that Compound 5 displayed an NMR K_D of 12 μM upon titration. auto_single_measurement only accepted activity measurement [1] 1 structures\8DYI\8DYI_metadata.json point structures/8DYI/8dyi_protein.pdb structures/8DYI/8dyi_pocket.pdb structures/8DYI/8dyi_ligand.pdb structures/8DYI/8dyi_ligand.cif structures/8DYI/8dyi_complex.pdb structures/8DYI/8dyi_complex.cif 8DYJ classic human methylmalonyl-CoA mutase human Na Na ADP; cob(II)alamin "[""ADP""]" 1 Kd Kd = = 44 ± 4.2 µM 44000.0 [] unit_conversion 4.356547323513812 success True direct_binding Metabolite binding to purified MCM•cob(II)alamin; dissociation constants determined from absorbance changes at 460 nm. 3 Table 1 reports ADP Kd = 44 ± 4.2 µM for human MCM•cob(II)alamin; the text states dissociation constants were determined for metabolites binding this complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8DYJ\8DYJ_metadata.json point structures/8DYJ/8dyj_protein.pdb structures/8DYJ/8dyj_pocket.pdb structures/8DYJ/8dyj_ligand.sdf structures/8DYJ/8dyj_ligand.pdb structures/8DYJ/8dyj_ligand.cif structures/8DYJ/8dyj_complex.pdb structures/8DYJ/8dyj_complex.cif 8DYQ classic Neisseria gonorrhoeae alpha-carbonic anhydrase (alpha-NgCA) Neisseria gonorrhoeae Na Na Acetazolamide (AZM) "[""AZM""]" 1 Ki Ki = = 74.1 ± 3.2 nM 74.1 [] unit_conversion 7.130181792020672 success True biochemical_inhibition CO2 hydration assay inhibition; Table 1 reports mean of one experiment in triplicate, with standard error. 2 Table 1 lists AZM with Ki 74.1 ± 3.2 nM against α-NgCA; Figure 1 identifies the AZM-bound α-NgCA structure as PDB 8DYQ. auto_single_measurement only accepted activity measurement [1] 1 structures\8DYQ\8DYQ_metadata.json point structures/8DYQ/8dyq_protein.pdb structures/8DYQ/8dyq_pocket.pdb structures/8DYQ/8dyq_ligand.sdf structures/8DYQ/8dyq_ligand.pdb structures/8DYQ/8dyq_ligand.cif structures/8DYQ/8dyq_complex.pdb structures/8DYQ/8dyq_complex.cif 8DZ0 classic SARS-CoV-2 Main protease SARS-CoV-2 Na WT Ensitrelvir "[""7YY""]" 2 Ki Ki = = 8.9 ± 0.71 nM 8.9 [] unit_conversion 8.050609993355087 success True biochemical_inhibition Purified-protein FRET inhibition assay. 5 Table 2 reports WT ensitrelvir Ki = 8.9 ± 0.71 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8DZ0\8DZ0_metadata.json point structures/8DZ0/8dz0_protein.pdb structures/8DZ0/8dz0_pocket.pdb structures/8DZ0/8dz0_ligand.sdf structures/8DZ0/8dz0_ligand.pdb structures/8DZ0/8dz0_ligand.cif structures/8DZ0/8dz0_complex.pdb structures/8DZ0/8dz0_complex.cif 8DZ1 classic SARS-CoV-2 Main protease SARS-CoV-2 Na M49I Ensitrelvir "[""7YY""]" 2 Ki Ki = = 54.2 ± 7.8 nM 54.2 [] unit_conversion 7.266000713461613 success True biochemical_inhibition Purified-protein FRET inhibition assay. 5 Table 2 reports M49I ensitrelvir Ki = 54.2 ± 7.8 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8DZ1\8DZ1_metadata.json point structures/8DZ1/8dz1_protein.pdb structures/8DZ1/8dz1_pocket.pdb structures/8DZ1/8dz1_ligand.sdf structures/8DZ1/8dz1_ligand.pdb structures/8DZ1/8dz1_ligand.cif structures/8DZ1/8dz1_complex.pdb structures/8DZ1/8dz1_complex.cif 8DZV extended Chicken anti-cardiac troponin I single-chain variable fragment (scFv) antibody Chicken Peptide-bound single-chain variable fragment (scFv) Na cTnI peptide (KISASRKLQLKT) "[""CHAIN:C""]" 1 Kd Kd = = 1.05 nM 1.05 [] unit_conversion 8.978810700930062 success True direct_binding Bio-layer interferometry affinity measurement for WT scFv binding to cTnI peptide. 7 The paper states that affinities measured by bio-layer interferometry for WT and L27c-Y mutants were 1.05 and 2.94 nM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\8DZV\8DZV_metadata.json point structures/8DZV/8dzv_protein.pdb structures/8DZV/8dzv_pocket.pdb structures/8DZV/8dzv_ligand.pdb structures/8DZV/8dzv_ligand.cif structures/8DZV/8dzv_complex.pdb structures/8DZV/8dzv_complex.cif 8E1O classic TEAD2 Homo sapiens TEAD2-YBD, residues A217-D447 Na Compound A (methoxypyridine lipid pocket binder) "[""Y2S""]" 1 IC50 IC50 = = 0.01 µM 10.0 [] unit_conversion 8.0 success True direct_binding TEAD lipid-pocket TR-FRET competitive binding assay; IC50 fitted using a nonlinear four-parameter curve. 43 Figure 5C explicitly lists for Compound A: “TEAD2 IC50: 0.01 µM.” The methods state that TEAD lipid-pocket binder potency was determined from TR-FRET displacement using IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\8E1O\8E1O_metadata.json point structures/8E1O/8e1o_protein.pdb structures/8E1O/8e1o_pocket.pdb structures/8E1O/8e1o_ligand.sdf structures/8E1O/8e1o_ligand.pdb structures/8E1O/8e1o_ligand.cif structures/8E1O/8e1o_complex.pdb structures/8E1O/8e1o_complex.cif 8E5J classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na Na 4-n-butylbenzoic acid "[""HX1""]" 1 Kd Kd = = 0.39 ± 0.04 μM 390.0 [] unit_conversion 6.4089353929735005 success True direct_binding UV-visible spectroscopic substrate-binding titration of CYP199A4; dissociation constants reported in Table 1. 6 Table 1 reports Kd = 0.39 ± 0.04 μM for 4-n-butylBA; the text identifies this table as substrate-binding data for CYP199A4. auto_single_measurement only accepted activity measurement [1] 1 structures\8E5J\8E5J_metadata.json point structures/8E5J/8e5j_protein.pdb structures/8E5J/8e5j_pocket.pdb structures/8E5J/8e5j_ligand.sdf structures/8E5J/8e5j_ligand.pdb structures/8E5J/8e5j_ligand.cif structures/8E5J/8e5j_complex.pdb structures/8E5J/8e5j_complex.cif 8E9F classic WD repeat-containing protein 5 (WDR5) Na Na Na compound 10 "[""UY9""]" 1 Ki Ki < < 0.02 nM 0.02 [] unit_conversion 10.698970004336019 success True direct_binding TR-FRET WDR5 binding assay 5 Table 1 reports compound 10 TR-FRET Ki for WDR5 as <0.02 nM; Fig. 3 identifies compound 10 bound to WDR5 as PDB ID 8E9F. auto_single_measurement only accepted activity measurement [1] 1 structures\8E9F\8E9F_metadata.json point structures/8E9F/8e9f_protein.pdb structures/8E9F/8e9f_pocket.pdb structures/8E9F/8e9f_ligand.sdf structures/8E9F/8e9f_ligand.pdb structures/8E9F/8e9f_ligand.cif structures/8E9F/8e9f_complex.pdb structures/8E9F/8e9f_complex.cif 8EBM extended KLHDC2 Na KLHDC2 substrate-binding domain (b-propeller fold-only domain), residues 15-361 Na KLHDC2's C-degron mimic (C-terminal peptide) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 1.40 µM 1400.0 [] unit_conversion 5.853871964321762 success True direct_binding Surface plasmon resonance of KLHDC2 SBD with the WT KLHDC2-derived peptide. 5 Figure 2C reports KD = 1.40 µM for the WT KLHDC2 peptide; the text identifies this as the wild-type KLHDC2-derived peptide bound to KLHDC2 SBD. auto_single_measurement only accepted activity measurement [1] 1 structures\8EBM\8EBM_metadata.json point structures/8EBM/8ebm_protein.pdb structures/8EBM/8ebm_pocket.pdb structures/8EBM/8ebm_ligand.pdb structures/8EBM/8ebm_ligand.cif structures/8EBM/8ebm_complex.pdb structures/8EBM/8ebm_complex.cif 8EI3 extended VHL-ELOBC complex human VHL residues 54-213 with N-terminal 6xHis-TEV tag; ELOB residues 1-118; ELOC residues 17-112 Na H313 (Helicon polypeptide) "[""CHAIN:G""]" 1 Kd Kd = = 4.1 µM 4100.0 [] unit_conversion 5.3872161432802645 success True direct_binding SPR specificity measurement of H313 binding to VHL-ELOBC. 5 “Using SPR, we confirmed the specificity of H313 for VHL-ELOBC over SOCS2-ELOBC and measured the K_D for the former to be 4.1 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8EI3\8EI3_metadata.json point structures/8EI3/8ei3_protein.pdb structures/8EI3/8ei3_pocket.pdb structures/8EI3/8ei3_ligand.pdb structures/8EI3/8ei3_ligand.cif structures/8EI3/8ei3_complex.pdb structures/8EI3/8ei3_complex.cif 8EIP classic cyanophycin dipeptide hydrolase CphZ (AbCphZ) Acinetobacter baylyi DSM587 Na E251A beta-Asp-Arg "[""7ID""]" 1 Kd Kd = = 7.6 ± 0.1 μM 7600.0 [] unit_conversion 5.119186407719209 success True direct_binding Isothermal titration calorimetry binding assay using purified AbCphZ E251A and β-Asp-Arg. 3 “Isothermal titration calorimetry (ITC) binding assays with β-Asp-Arg, Asn, and Arg shows CphZ_E251A has good affinity for the substrate β-Asp-Arg (K_D = 7.6 ± 0.1 μM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8EIP\8EIP_metadata.json point structures/8EIP/8eip_protein.pdb structures/8EIP/8eip_pocket.pdb structures/8EIP/8eip_ligand.sdf structures/8EIP/8eip_ligand.pdb structures/8EIP/8eip_ligand.cif structures/8EIP/8eip_complex.pdb structures/8EIP/8eip_complex.cif 8EJV classic PcaR transcription factor Pseudomonas putida Recombinant tag-free PcaR after removal of the N-terminal His6 tag by TEV protease Na succinate "[""SIN""]" 1 Kd Kd = = 1.3 mM 1300000.0 [] unit_conversion 2.886056647693163 success True direct_binding Differential scanning fluorimetry (DSF) of purified PcaR with dicarboxylic-acid ligands; dissociation constants calculated from the unfolded fraction at 52 °C. 3 “The calculated dissociation constant (Kd) indicates that PcaR with succinate has the smallest dissociation constant at 1.3 mM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8EJV\8EJV_metadata.json point structures/8EJV/8ejv_protein.pdb structures/8EJV/8ejv_pocket.pdb structures/8EJV/8ejv_ligand.sdf structures/8EJV/8ejv_ligand.pdb structures/8EJV/8ejv_ligand.cif structures/8EJV/8ejv_complex.pdb structures/8EJV/8ejv_complex.cif 8ENW extended beta'-COPI WD40 domain S. cerevisiae recombinant beta'-COPI WD40 domain Thr1273Glu in the SARS-CoV-2 S tail heptapeptide clientized SARS-CoV-2 spike tail heptapeptide (Thr1273Glu) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 2.3 ± 0.23 μM 2300.0 [] unit_conversion 5.638272163982407 success True direct_binding Biolayer interferometry of purified β′WD40 domain with clientized S heptapeptide. 6 Table 1 lists GVKLHYE with β′WD40: equilibrium KD 2.3 ± 0.23 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8ENW\8ENW_metadata.json point structures/8ENW/8enw_protein.pdb structures/8ENW/8enw_pocket.pdb structures/8ENW/8enw_ligand.pdb structures/8ENW/8enw_ligand.cif structures/8ENW/8enw_complex.pdb structures/8ENW/8enw_complex.cif 8ESE extended Human VPS29 Homo sapiens VPS29 bound to VPS35L peptide residues 16-38 Na VPS35L peptide residues 16-38 "[""CHAIN:X""]" 1 Kd Kd = = 1.87 ± 0.8 µM 1870.0 [] unit_conversion 5.7281583934635005 success True direct_binding ITC titration of synthetic VPS35L peptide (16-38) into VPS29; fitted to a 1:1 binding model. 5 Figure 2 legend states that VPS35L (16-38) had an affinity of 1.87 µM ± 0.8 µM for VPS29 by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8ESE\8ESE_metadata.json point structures/8ESE/8ese_protein.pdb structures/8ESE/8ese_pocket.pdb structures/8ESE/8ese_ligand.pdb structures/8ESE/8ese_ligand.cif structures/8ESE/8ese_complex.pdb structures/8ESE/8ese_complex.cif 8ESM classic Human triacylglycerol synthesizing enzyme DGAT1 Homo sapiens Human DGAT1 expressed with an N-terminal maltose-binding protein and TEV cleavage site; MBP tag cleaved before cryo-EM preparation Na T863 "[""WS0""]" 1 IC50 IC50 = = 1.4 ± 0.2 µM 1400.0 [] unit_conversion 5.853871964321762 success True biochemical_inhibition Dose-dependent inhibition of purified human DGAT1; IC50 and standard deviation calculated from three independent experiments (n = 3). 2 Fig. 1c legend: “T863 (IC50: 1.4 ± 0.2 µM)” and states both compounds inhibit purified human DGAT1. auto_single_measurement only accepted activity measurement [1] 1 structures\8ESM\8ESM_metadata.json point structures/8ESM/8esm_protein.pdb structures/8ESM/8esm_pocket.pdb structures/8ESM/8esm_ligand.sdf structures/8ESM/8esm_ligand.pdb structures/8ESM/8esm_ligand.cif structures/8ESM/8esm_complex.pdb structures/8ESM/8esm_complex.cif 8ESX classic HIV-1 protease Na Na wild-type BOL-darunavir (3) "[""X7B""]" 1 Ki Ki = = 10 ± 2 pM 0.01 [] unit_conversion 11.0 success True biochemical_inhibition Inhibition of cleavage of RE(EDANS)SGIFLETSK(DABCYL)R in sodium acetate buffer, pH 5.0, containing NaCl (0.10 M) and DMF (2% v/v). 3 “Benzoxaborolone 3 proved to be an effective inhibitor of catalysis by HIV protease… we obtained an inhibitory constant (Ki) of 10 ± 2 pM with the wild-type enzyme.” Figure 2 maps BOL-darunavir (3) bound to wild-type HIV-1 protease to PDB entry 8ESX. auto_single_measurement only accepted activity measurement [1] 1 structures\8ESX\8ESX_metadata.json point structures/8ESX/8esx_protein.pdb structures/8ESX/8esx_pocket.pdb structures/8ESX/8esx_ligand.sdf structures/8ESX/8esx_ligand.pdb structures/8ESX/8esx_ligand.cif structures/8ESX/8esx_complex.pdb structures/8ESX/8esx_complex.cif 8ESY classic HIV-1 protease Na Na D30N BOL-darunavir (3) "[""X7B""]" 1 Ki Ki = = 7 ± 5 pM 0.007 [] unit_conversion 11.154901959985743 success True biochemical_inhibition HIV-1 protease inhibition assay; the page does not restate the substrate/buffer details for this D30N determination. 3 “we did not observe a decrease in affinity of BOL-darunavir to the D30N variant (Ki = 7 ± 5 pM; Figure S2).” Figure 2 maps BOL-darunavir (3) bound to D30N HIV-1 protease to PDB entry 8ESY. auto_single_measurement only accepted activity measurement [1] 1 structures\8ESY\8ESY_metadata.json point structures/8ESY/8esy_protein.pdb structures/8ESY/8esy_pocket.pdb structures/8ESY/8esy_ligand.sdf structures/8ESY/8esy_ligand.pdb structures/8ESY/8esy_ligand.cif structures/8ESY/8esy_complex.pdb structures/8ESY/8esy_complex.cif 8ETM classic Human triacylglycerol synthesizing enzyme DGAT1 Homo sapiens Human DGAT1 expressed with an N-terminal maltose-binding protein and TEV cleavage site; MBP tag cleaved before cryo-EM preparation Na DGAT1IN1 "[""WTT""]" 1 IC50 IC50 = = 3.2 ± 1.1 µM 3200.0 [] unit_conversion 5.494850021680094 success True biochemical_inhibition Dose-dependent inhibition of purified human DGAT1; IC50 and standard deviation calculated from three independent experiments (n = 3). 2 Fig. 1c legend: “DGAT1IN1 (IC50: 3.2 ± 1.1 µM)” and states both compounds inhibit purified human DGAT1. auto_single_measurement only accepted activity measurement [1] 1 structures\8ETM\8ETM_metadata.json point structures/8ETM/8etm_protein.pdb structures/8ETM/8etm_pocket.pdb structures/8ETM/8etm_ligand.sdf structures/8ETM/8etm_ligand.pdb structures/8ETM/8etm_ligand.cif structures/8ETM/8etm_complex.pdb structures/8ETM/8etm_complex.cif 8EUL classic cytochrome P450terp (CYP108A1) Na Na F188A alpha-terpineol "[""XGE""]" 1 Kd Kd = = 33.6 ± 4.1 µM 33600.0 [] unit_conversion 4.473660722610156 success True direct_binding ITC, single-binding-site model incorporating the slow re-equilibration contribution. 11 For F188A, the ITC binding curve was best fit to a single-site model with K_D of 33.6 µM; Table 1 prints 33.6 ± 4.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8EUL\8EUL_metadata.json point structures/8EUL/8eul_protein.pdb structures/8EUL/8eul_pocket.pdb structures/8EUL/8eul_ligand.sdf structures/8EUL/8eul_ligand.pdb structures/8EUL/8eul_ligand.cif structures/8EUL/8eul_complex.pdb structures/8EUL/8eul_complex.cif 8EV7 extended 70S ribosome Thermus thermophilus Na Na kanamycin "[""KAN""]" 1 Ki Ki ~ ~ 0.8 µM 800.0 [] unit_conversion 6.096910013008056 success True biochemical_inhibition EF-G-catalyzed mRNA–tRNA translocation inhibition. 4 The text explicitly states that KAN showed weaker inhibition of translocation with “Kᵢ ~ 0.8 µM” (Supplementary Fig. 6d). auto_single_measurement only accepted activity measurement [1] 1 structures\8EV7\8EV7_metadata.json point structures/8EV7/8ev7_ligand.sdf structures/8EV7/8ev7_ligand.cif structures/8EV7/8ev7_complex.cif 8EVF classic Human DNA polymerase eta human Residues 1-432; N-terminal 6xHis tag and PreScission protease recognition site; pET28a expression construct Na 6-oxo-M1dG "[""DCP""]" 1 Ki Ki = = 650 ± 225 µM 650000.0 [] unit_conversion 3.1870866433571443 success True biochemical_inhibition Steady-state nucleotide-incorporation assay using purified hPol η and a 6-oxo-M1dG oligonucleotide primer-template duplex; dCTP substrate inhibition was fitted using the substrate-inhibition model. 4 Table 1 lists the 6-Oxo-M1dG oligonucleotide dCTP Ki as 650 ± 225 µM; the text states that Ki values for substrate inhibition were measured for all nucleotides. auto_single_measurement only accepted activity measurement [1] 1 structures\8EVF\8EVF_metadata.json point structures/8EVF/8evf_protein.pdb structures/8EVF/8evf_pocket.pdb structures/8EVF/8evf_ligand.sdf structures/8EVF/8evf_ligand.pdb structures/8EVF/8evf_ligand.cif structures/8EVF/8evf_complex.pdb structures/8EVF/8evf_complex.cif 8EWD extended CYP3A4 Na Na Na Δ,Λ-(L)-6 "[""WZN""]" 1 Kd Kd = = 21 ± 6 nM 21.0 [] unit_conversion 7.6777807052660805 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWD to Δ,Λ-(L)-6; Table 4 reports Kd 21 ± 6 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWD\8EWD_metadata.json point structures/8EWD/8ewd_protein.pdb structures/8EWD/8ewd_pocket.pdb structures/8EWD/8ewd_ligand.pdb structures/8EWD/8ewd_ligand.cif structures/8EWD/8ewd_complex.pdb structures/8EWD/8ewd_complex.cif 8EWE extended CYP3A4 Na Na Na Δ,Λ-(D)-6 "[""X0E""]" 1 Kd Kd = = 28 ± 6 nM 28.0 [] unit_conversion 7.552841968657781 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWE to Δ,Λ-(D)-6; Table 4 reports Kd 28 ± 6 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWE\8EWE_metadata.json point structures/8EWE/8ewe_protein.pdb structures/8EWE/8ewe_pocket.pdb structures/8EWE/8ewe_ligand.pdb structures/8EWE/8ewe_ligand.cif structures/8EWE/8ewe_complex.pdb structures/8EWE/8ewe_complex.cif 8EWL extended CYP3A4 Na Na Na Δ,Λ-7 "[""X1C""]" 1 Kd Kd = = 133 ± 5 nM 133.0 [] unit_conversion 6.876148359032914 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWL to Δ,Λ-7; Table 4 reports Kd 133 ± 5 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWL\8EWL_metadata.json point structures/8EWL/8ewl_protein.pdb structures/8EWL/8ewl_pocket.pdb structures/8EWL/8ewl_ligand.pdb structures/8EWL/8ewl_ligand.cif structures/8EWL/8ewl_complex.pdb structures/8EWL/8ewl_complex.cif 8EWM extended CYP3A4 Na Na Na Δ,Λ-(L)-9 "[""X1I""]" 1 Kd Kd = = 13 ± 2 nM 13.0 [] unit_conversion 7.886056647693163 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWM to Δ,Λ-(L)-9; Table 4 reports Kd 13 ± 2 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWM\8EWM_metadata.json point structures/8EWM/8ewm_protein.pdb structures/8EWM/8ewm_pocket.pdb structures/8EWM/8ewm_ligand.pdb structures/8EWM/8ewm_ligand.cif structures/8EWM/8ewm_complex.pdb structures/8EWM/8ewm_complex.cif 8EWN extended CYP3A4 Na Na Na Δ,Λ-10 "[""X1O""]" 1 Kd Kd = = 356 ± 44 nM 356.0 [] unit_conversion 6.448550002027124 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWN to Δ,Λ-10; Table 4 reports Kd 356 ± 44 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWN\8EWN_metadata.json point structures/8EWN/8ewn_protein.pdb structures/8EWN/8ewn_pocket.pdb structures/8EWN/8ewn_ligand.pdb structures/8EWN/8ewn_ligand.cif structures/8EWN/8ewn_complex.pdb structures/8EWN/8ewn_complex.cif 8EWP extended CYP3A4 Na Na Na Δ,Λ-12 "[""X2Q""]" 1 Kd Kd = = 24 ± 1 nM 24.0 [] unit_conversion 7.619788758288394 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWP to Δ,Λ-12; Table 4 reports Kd 24 ± 1 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWP\8EWP_metadata.json point structures/8EWP/8ewp_protein.pdb structures/8EWP/8ewp_pocket.pdb structures/8EWP/8ewp_ligand.pdb structures/8EWP/8ewp_ligand.cif structures/8EWP/8ewp_complex.pdb structures/8EWP/8ewp_complex.cif 8EWQ extended CYP3A4 Na Na Na Δ,Λ-(L)-14 "[""X2B""]" 1 Kd Kd = = 26 ± 5 nM 26.0 [] unit_conversion 7.585026652029182 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWQ to Δ,Λ-(L)-14; Table 4 reports Kd 26 ± 5 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWQ\8EWQ_metadata.json point structures/8EWQ/8ewq_protein.pdb structures/8EWQ/8ewq_pocket.pdb structures/8EWQ/8ewq_ligand.pdb structures/8EWQ/8ewq_ligand.cif structures/8EWQ/8ewq_complex.pdb structures/8EWQ/8ewq_complex.cif 8EWR extended CYP3A4 Na Na Na Λ-(L)-6 "[""WZN""]" 1 Kd Kd = = 22 ± 5 nM 22.0 [] unit_conversion 7.657577319177793 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWR to Λ-(L)-6; Table 4 reports Kd 22 ± 5 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWR\8EWR_metadata.json point structures/8EWR/8ewr_protein.pdb structures/8EWR/8ewr_pocket.pdb structures/8EWR/8ewr_ligand.pdb structures/8EWR/8ewr_ligand.cif structures/8EWR/8ewr_complex.pdb structures/8EWR/8ewr_complex.cif 8EWS extended CYP3A4 Na Na Na Λ-12 "[""X2Q""]" 1 Kd Kd = = 52 ± 1 nM 52.0 [] unit_conversion 7.2839966563652006 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EWS to Λ-12; Table 4 reports Kd 52 ± 1 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EWS\8EWS_metadata.json point structures/8EWS/8ews_protein.pdb structures/8EWS/8ews_pocket.pdb structures/8EWS/8ews_ligand.pdb structures/8EWS/8ews_ligand.cif structures/8EWS/8ews_complex.pdb structures/8EWS/8ews_complex.cif 8EXB extended CYP3A4 Na Na Na Δ-13 "[""X4E""]" 1 Kd Kd = = 29 ± 3 nM 29.0 [] unit_conversion 7.537602002101044 success True direct_binding Direct-binding titration with CYP3A4. 35 Supporting Information page S42 maps 8EXB to Δ-13; Table 4 reports Kd 29 ± 3 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EXB\8EXB_metadata.json point structures/8EXB/8exb_protein.pdb structures/8EXB/8exb_pocket.pdb structures/8EXB/8exb_ligand.pdb structures/8EXB/8exb_ligand.cif structures/8EXB/8exb_complex.pdb structures/8EXB/8exb_complex.cif 8EYM classic NagB-II phosphosugar isomerase (SdNagBII) Shewanella denitrificans OS217 Recombinant untagged SdNagBII Na Glucitolamine-6-phosphate (GlcNol6P); N-acetylglucosamine-6-phosphate (GlcNAc6P) "[""AGP""]" 1 Kd Kd = = (1.54 ± 0.17) E−04 M 154000.0 [] unit_conversion 3.8124792791635373 success True direct_binding ITC titration of GlcNAc6P-saturated SdNagBII with GlcNol6P. 5 Table 2 lists Kd for reaction [3], MA + L ⇌ MAL, as (1.54 ± 0.17) E−04 M. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8EYM\8EYM_metadata.json point structures/8EYM/8eym_protein.pdb structures/8EYM/8eym_pocket.pdb structures/8EYM/8eym_ligand.sdf structures/8EYM/8eym_ligand.pdb structures/8EYM/8eym_ligand.cif structures/8EYM/8eym_complex.pdb structures/8EYM/8eym_complex.cif 8EYZ extended glutamine-binding protein (GlnBP) Na GlnBP lacking the 22-aa leader sequence; T72C single-Cys variant T72C Gln; Co(dmgH)2(N3) "[""GLN""]" 1 Kd Kd = = 730 ± 50 nM 730.0 [] unit_conversion 6.136677139879544 success True direct_binding Isothermal titration calorimetry of Gln binding to the cobaloxime-installed T72C GlnBP holo complex. 5 Table 2 lists [Co(N3)]-GlnBP ITC Kd = 730 ± 50 nM; the surrounding text identifies this as the installed-metal-cofactor construct. auto_single_measurement only accepted activity measurement [1] 1 structures\8EYZ\8EYZ_metadata.json point structures/8EYZ/8eyz_protein.pdb structures/8EYZ/8eyz_pocket.pdb structures/8EYZ/8eyz_ligand.pdb structures/8EYZ/8eyz_ligand.cif structures/8EYZ/8eyz_complex.pdb structures/8EYZ/8eyz_complex.cif 8F0F classic HIV-1 protease HIV-1 Na wild type GRL-110-19A (inhibitor 4a) "[""X7H""]" 1 Ki Ki = = 4.4 pM 0.0044 [] unit_conversion 11.356547323513812 success True biochemical_inhibition Enzyme-inhibitory assay; Table 1 reports inhibitor 4a activity. 4 Table 1 lists inhibitor 4a with Ki 4.4 pM; the text states that chloroacetamide derivative 4a exhibited potent protease-inhibitory activity. auto_single_measurement only accepted activity measurement [1] 1 structures\8F0F\8F0F_metadata.json point structures/8F0F/8f0f_protein.pdb structures/8F0F/8f0f_pocket.pdb structures/8F0F/8f0f_ligand.sdf structures/8F0F/8f0f_ligand.pdb structures/8F0F/8f0f_ligand.cif structures/8F0F/8f0f_complex.pdb structures/8F0F/8f0f_complex.cif 8F1Z classic EGFR (epidermal growth factor receptor) kinase Homo sapiens EGFR kinase domain residues 696-1022 (WT numbering), expressed as an N-10x His C-TwinStrep fusion; affinity tags cleaved before crystallization WT Bayer #33 (BAY-33) "[""X9B""]" 1 IC50 IC50 > > 1000 nM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition Purified recombinant EGFR kinase; HTRF biochemical inhibition assay at 1 mM ATP; mean ± SD, n=3 independent experiments performed in triplicate. 3 Table 2 reports BAY-33 IC50 against WT EGFR as >1,000 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F1Z\8F1Z_metadata.json point structures/8F1Z/8f1z_protein.pdb structures/8F1Z/8f1z_pocket.pdb structures/8F1Z/8f1z_ligand.sdf structures/8F1Z/8f1z_ligand.pdb structures/8F1Z/8f1z_ligand.cif structures/8F1Z/8f1z_complex.pdb structures/8F1Z/8f1z_complex.cif 8F2Q extended Mouse importin alpha2 (IMPalpha2DeltaIBB) bound to human parvovirus B19 NS1 cNLS peptide Human parvovirus B19 and mouse N-terminally truncated mouse IMPalpha2DeltaIBB, residues 71-529, lacking the IBB domain, with a 6xHis tag Na B19V NS1 cNLS peptide, residues 172-182, sequence GACHAKKPRIT "[""CHAIN:B"", ""CHAIN:C""]" 1 Kd Kd = = 0.9 μM 900.0 [] unit_conversion 6.045757490560675 success True direct_binding Fluorescence-polarization assay using purified recombinant mouse IMPα2ΔIBB and FITC-labelled NS1(172–182) peptide. 9 Fig. 4E explicitly reports for “NS1 NLS” a Kd of 0.9 μM (SEM 0.1); Fig. 4 caption identifies the fluorescence-polarization assay with FITC-labelled B19V NS1(172–182) peptide and bacterially purified IMPα2ΔIBB. auto_single_measurement only accepted activity measurement [1] 1 structures\8F2Q\8F2Q_metadata.json point structures/8F2Q/8f2q_protein.pdb structures/8F2Q/8f2q_pocket.pdb structures/8F2Q/8f2q_ligand.pdb structures/8F2Q/8f2q_ligand.cif structures/8F2Q/8f2q_complex.pdb structures/8F2Q/8f2q_complex.cif 8F4B extended Bovine multidrug resistance protein 1 (MRP1) Bovine MRP1 construct with a C-terminal eGFP tag Na CPI1 (cyclic peptide inhibitor 1) "[""CHAIN:B""]" 1 Ki Ki = = 70 ± 29 nM 70.0 [] unit_conversion 7.154901959985743 success True biochemical_inhibition bMRP1 ATPase inhibition assay, in the absence of LTC4. 3 “The Ki values of CPI1 against bMRP1 were determined to be 70 ± 29 nM and 95 ± 46 nM in the absence and presence of 3.5 μM LTC4, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8F4B\8F4B_metadata.json point structures/8F4B/8f4b_protein.pdb structures/8F4B/8f4b_pocket.pdb structures/8F4B/8f4b_ligand.pdb structures/8F4B/8f4b_ligand.cif structures/8F4B/8f4b_complex.pdb structures/8F4B/8f4b_complex.cif 8F5F classic human branched-chain ketoacid dehydrogenase kinase (BDK) human Na Na PF-07247685 "[""XGG""]" 2 Kd Kd = = 0.68 ± 0.38 nM 0.68 [] unit_conversion 9.167491087293763 success True direct_binding BDK SPR binding assay 3 Table 1 reports BDK SPR Kd of 0.68 ± 0.38 nM for PF-07247685. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8F5F\8F5F_metadata.json point structures/8F5F/8f5f_protein.pdb structures/8F5F/8f5f_pocket.pdb structures/8F5F/8f5f_ligand.sdf structures/8F5F/8f5f_ligand.pdb structures/8F5F/8f5f_ligand.cif structures/8F5F/8f5f_complex.pdb structures/8F5F/8f5f_complex.cif 8F5J classic human branched-chain ketoacid dehydrogenase kinase (BDK) human Na Na PF-07208254 "[""XER""]" 3 Kd Kd = = 84 ± 8.7 nM 84.0 [] unit_conversion 7.075720713938118 success True direct_binding BDK SPR binding assay 3 Table 1 reports BDK SPR Kd of 84 ± 8.7 nM for PF-07208254. auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\8F5J\8F5J_metadata.json point structures/8F5J/8f5j_protein.pdb structures/8F5J/8f5j_pocket.pdb structures/8F5J/8f5j_ligand.sdf structures/8F5J/8f5j_ligand.pdb structures/8F5J/8f5j_ligand.cif structures/8F5J/8f5j_complex.pdb structures/8F5J/8f5j_complex.cif 8F5Q extended human PCNA Homo sapiens Full-length human PCNA; untagged protein used for crystallization Na FBH1 PIP peptide, residues 55-68 "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F""]" 1 Kd Kd = = 7.8 ± 3.7 μM 7800.0 [] unit_conversion 5.107905397309519 success True direct_binding NMR titration of PCNA with FBH1 PIP peptide at 35°C; fitted using 10 PCNA signals. 3 “fitting analysis of CSPs for 10 PCNA signals yielded a dissociation constant (Kd) of 7.8 ± 3.7 μM (Figures 1B and 1D).” The preceding text identifies the added ligand as FBH1 PIP peptide (residues 55–68). auto_single_measurement only accepted activity measurement [1] 1 structures\8F5Q\8F5Q_metadata.json point structures/8F5Q/8f5q_protein.pdb structures/8F5Q/8f5q_pocket.pdb structures/8F5Q/8f5q_ligand.pdb structures/8F5Q/8f5q_ligand.cif structures/8F5Q/8f5q_complex.pdb structures/8F5Q/8f5q_complex.cif 8F6S classic LSD1-CoREST human His6-tagged human LSD1(Delta150, residues 151-852)-CoREST(Delta307, residues 308-485) Na compound 2 "[""XHX""]" 1 IC50 IC50 = = 231 ± 1 nM 231.0 [] unit_conversion 6.636388020107855 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8F6S to compound 2 and reports IC50 231 ± 1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F6S\8F6S_metadata.json point structures/8F6S/8f6s_protein.pdb structures/8F6S/8f6s_pocket.pdb structures/8F6S/8f6s_ligand.sdf structures/8F6S/8f6s_ligand.pdb structures/8F6S/8f6s_ligand.cif structures/8F6S/8f6s_complex.pdb structures/8F6S/8f6s_complex.cif 8F78 classic procaspase-6 Na Na Na compound 1 "[""2J6""]" 1 Kd Kd = = 0.27 ± 0.30 µM 270.0 [] unit_conversion 6.568636235841012 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 1 K_D = 0.27 ± 0.30 µM; the table footnote states values are means of three determinations ± SD. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8F78\8F78_metadata.json point structures/8F78/8f78_protein.pdb structures/8F78/8f78_pocket.pdb structures/8F78/8f78_ligand.sdf structures/8F78/8f78_ligand.pdb structures/8F78/8f78_ligand.cif structures/8F78/8f78_complex.pdb structures/8F78/8f78_complex.cif 8F8Y extended PHF2 human PHF2(1-451) fragment Na VRK1(1-12)K4me3 peptide "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 0.042±0.005 µM 42.0 [] unit_conversion 7.376750709602099 success True direct_binding Isothermal titration calorimetry of PHF2(1-451) with VRK1 K4me3 peptide; 25 °C. 2 Figure 1I and accompanying text report PHF2(1-451) binding to the VRK1 K4me3 peptide with KD = 0.042±0.005 µM; page 7 maps PDB 8F8Y to the VRK1-bound PHF2 structure. auto_single_measurement only accepted activity measurement [1] 1 structures\8F8Y\8F8Y_metadata.json point structures/8F8Y/8f8y_protein.pdb structures/8F8Y/8f8y_pocket.pdb structures/8F8Y/8f8y_ligand.pdb structures/8F8Y/8f8y_ligand.cif structures/8F8Y/8f8y_complex.pdb structures/8F8Y/8f8y_complex.cif 8F8Z extended PHF2 human PHF2(1-451) fragment Na H3(1-12)K4me3 peptide "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 0.16±0.02 µM 160.0 [] unit_conversion 6.795880017344075 success True direct_binding Isothermal titration calorimetry of PHF2(1-451) with H3 K4me3 peptide; 25 °C. 2 Figure 1I and accompanying text report PHF2(1-451) binding to the H3 K4me3 peptide with KD = 0.16±0.02 µM; page 7 maps PDB 8F8Z to the H3-bound PHF2 structure. auto_single_measurement only accepted activity measurement [1] 1 structures\8F8Z\8F8Z_metadata.json point structures/8F8Z/8f8z_protein.pdb structures/8F8Z/8f8z_pocket.pdb structures/8F8Z/8f8z_ligand.pdb structures/8F8Z/8f8z_ligand.cif structures/8F8Z/8f8z_complex.pdb structures/8F8Z/8f8z_complex.cif 8F96 classic procaspase-6 Na Na Na compound 3 "[""XLW""]" 1 Kd Kd = = 0.85 ± 0.13 µM 850.0 [] unit_conversion 6.070581074285707 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 3 K_D = 0.85 ± 0.13 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F96\8F96_metadata.json point structures/8F96/8f96_protein.pdb structures/8F96/8f96_pocket.pdb structures/8F96/8f96_ligand.sdf structures/8F96/8f96_ligand.pdb structures/8F96/8f96_ligand.cif structures/8F96/8f96_complex.pdb structures/8F96/8f96_complex.cif 8F97 classic procaspase-6 Na Na Na compound 5 "[""XM6""]" 1 Kd Kd = = 95.3 ± 6.3 µM 95300.0 [] unit_conversion 4.020907099361674 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 5 K_D = 95.3 ± 6.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F97\8F97_metadata.json point structures/8F97/8f97_protein.pdb structures/8F97/8f97_pocket.pdb structures/8F97/8f97_ligand.sdf structures/8F97/8f97_ligand.pdb structures/8F97/8f97_ligand.cif structures/8F97/8f97_complex.pdb structures/8F97/8f97_complex.cif 8F98 classic procaspase-6 Na Na Na compound 8 "[""XML""]" 1 Kd Kd = = 4.01 ± 1.5 µM 4010.0 [] unit_conversion 5.396855627379818 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 8 K_D = 4.01 ± 1.5 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F98\8F98_metadata.json point structures/8F98/8f98_protein.pdb structures/8F98/8f98_pocket.pdb structures/8F98/8f98_ligand.sdf structures/8F98/8f98_ligand.pdb structures/8F98/8f98_ligand.cif structures/8F98/8f98_complex.pdb structures/8F98/8f98_complex.cif 8F99 classic procaspase-6 Na Na Na compound 10 "[""XMR""]" 1 Kd Kd = = 1.19 ± 0.074 µM 1190.0 [] unit_conversion 5.924453038607469 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 10 K_D = 1.19 ± 0.074 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F99\8F99_metadata.json point structures/8F99/8f99_protein.pdb structures/8F99/8f99_pocket.pdb structures/8F99/8f99_ligand.sdf structures/8F99/8f99_ligand.pdb structures/8F99/8f99_ligand.cif structures/8F99/8f99_complex.pdb structures/8F99/8f99_complex.cif 8F9A classic procaspase-6 Na Na Na compound 11 "[""XMX""]" 1 Kd Kd = = 980 µM 980000.0 [] unit_conversion 3.008773924307505 success True direct_binding SPR using catalytically dead C163A procaspase-6; weak-binding estimate (†). 5 Table 1 reports compound 11 K_D = 980† µM; the footnote identifies daggered weak-binding values as estimates. auto_single_measurement only accepted activity measurement [1] 1 structures\8F9A\8F9A_metadata.json point structures/8F9A/8f9a_protein.pdb structures/8F9A/8f9a_pocket.pdb structures/8F9A/8f9a_ligand.sdf structures/8F9A/8f9a_ligand.pdb structures/8F9A/8f9a_ligand.cif structures/8F9A/8f9a_complex.pdb structures/8F9A/8f9a_complex.cif 8F9B classic procaspase-6 Na Na Na compound 19 "[""XN5""]" 1 Kd Kd = = 21.2 ± 1.2 µM 21200.0 [] unit_conversion 4.673664139071248 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 19 K_D = 21.2 ± 1.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F9B\8F9B_metadata.json point structures/8F9B/8f9b_protein.pdb structures/8F9B/8f9b_pocket.pdb structures/8F9B/8f9b_ligand.sdf structures/8F9B/8f9b_ligand.pdb structures/8F9B/8f9b_ligand.cif structures/8F9B/8f9b_complex.pdb structures/8F9B/8f9b_complex.cif 8F9C classic procaspase-6 Na Na Na compound 20 "[""XN9""]" 1 Kd Kd = = 1.22 ± 0.041 µM 1220.0 [] unit_conversion 5.913640169325252 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 20 K_D = 1.22 ± 0.041 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F9C\8F9C_metadata.json point structures/8F9C/8f9c_protein.pdb structures/8F9C/8f9c_pocket.pdb structures/8F9C/8f9c_ligand.sdf structures/8F9C/8f9c_ligand.pdb structures/8F9C/8f9c_ligand.cif structures/8F9C/8f9c_complex.pdb structures/8F9C/8f9c_complex.cif 8F9D classic procaspase-6 Na Na Na compound 21 "[""XNK""]" 1 Kd Kd = = 1.16 ± 0.80 µM 1160.0 [] unit_conversion 5.935542010773082 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 21 K_D = 1.16 ± 0.80 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8F9D\8F9D_metadata.json point structures/8F9D/8f9d_protein.pdb structures/8F9D/8f9d_pocket.pdb structures/8F9D/8f9d_ligand.sdf structures/8F9D/8f9d_ligand.pdb structures/8F9D/8f9d_ligand.cif structures/8F9D/8f9d_complex.pdb structures/8F9D/8f9d_complex.cif 8FAL classic carbonic anhydrase II (hCAII) Homo sapiens Na Na compound 4; benzo[d]thiazole-2(3H)-thione "[""XO9""]" 1 IC50 IC50 = = 68.27 ± 10.69 µM 68270.0 [] unit_conversion 4.1657700971483225 success True biochemical_inhibition IC50 inhibition assay against hCAII; 95% confidence interval indicated. 13 Table 1 reports compound 4 IC50 against hCAII as 68.27 ± 10.69 µM; Figure 4 maps compound 4 bound to hCAII to PDB 8FAL. auto_single_measurement only accepted activity measurement [1] 1 structures\8FAL\8FAL_metadata.json point structures/8FAL/8fal_protein.pdb structures/8FAL/8fal_pocket.pdb structures/8FAL/8fal_ligand.sdf structures/8FAL/8fal_ligand.pdb structures/8FAL/8fal_ligand.cif structures/8FAL/8fal_complex.pdb structures/8FAL/8fal_complex.cif 8FAU classic carbonic anhydrase II (hCAII) Homo sapiens Na Na compound 7; 4-phenylthiazole-2(3H)-thione "[""Y3E""]" 1 IC50 IC50 = = 4.56 ± 0.62 µM 4560.0 [] unit_conversion 5.341035157335565 success True biochemical_inhibition IC50 inhibition assay against hCAII; 95% confidence interval indicated. 13 Table 1 reports compound 7 IC50 against hCAII as 4.56 ± 0.62 µM; Figure 4 maps compound 7 bound to hCAII to PDB 8FAU. auto_single_measurement only accepted activity measurement [1] 1 structures\8FAU\8FAU_metadata.json point structures/8FAU/8fau_protein.pdb structures/8FAU/8fau_pocket.pdb structures/8FAU/8fau_ligand.sdf structures/8FAU/8fau_ligand.pdb structures/8FAU/8fau_ligand.cif structures/8FAU/8fau_complex.pdb structures/8FAU/8fau_complex.cif 8FBM classic Cryptosporidium parvum N-myristoyltransferase Cryptosporidium parvum A10, residues 40-466 Na inhibitor 1 (Compound 1) "[""XOF""]" 1 IC50 IC50 = = 3.5 μM 3500.0 [] unit_conversion 5.455931955649724 success True biochemical_inhibition Fluorescence-based recombinant CpNMT enzymatic inhibition assay; assay conditions include MyrCoA and PfARF-peptide. 3 Figure 1 visibly reports “CpNMT IC50 = 3.5 μM” for compound 1; the figure caption states these are CpNMT values from resynthesized compounds in this work. auto_single_measurement only accepted activity measurement [1] 1 structures\8FBM\8FBM_metadata.json point structures/8FBM/8fbm_protein.pdb structures/8FBM/8fbm_pocket.pdb structures/8FBM/8fbm_ligand.sdf structures/8FBM/8fbm_ligand.pdb structures/8FBM/8fbm_ligand.cif structures/8FBM/8fbm_complex.pdb structures/8FBM/8fbm_complex.cif 8FBQ extended Plasmodium vivax glycylpeptide N-tetradecanoyltransferase (N-myristoyltransferase, NMT) Plasmodium vivax PvNMT residues 27-410 Na inhibitor 12b "[""XOQ""]" 1 IC50 IC50 = = 80.15 nM 80.15 [] unit_conversion 7.096096473309837 success True biochemical_inhibition Purified PvNMT enzymatic activity assay; Table 1 reports mean values from two or more determinations. The assay detects free CoA using a thiol-reactive fluorescent probe. 4 Table 1 lists compound 12b: PvNMT IC50 = 80.15 nM. Methods describe the purified PvNMT activity assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8FBQ\8FBQ_metadata.json point structures/8FBQ/8fbq_protein.pdb structures/8FBQ/8fbq_pocket.pdb structures/8FBQ/8fbq_ligand.pdb structures/8FBQ/8fbq_ligand.cif structures/8FBQ/8fbq_complex.pdb structures/8FBQ/8fbq_complex.cif 8FBV classic procaspase-6 Na Na Na compound 7 "[""XOW""]" 1 Kd Kd = = 1.15 ± 0.14 µM 1150.0 [] unit_conversion 5.939302159646388 success True direct_binding SPR using catalytically dead C163A procaspase-6; mean of three determinations ± SD. 5 Table 1 reports compound 7 K_D = 1.15 ± 0.14 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FBV\8FBV_metadata.json point structures/8FBV/8fbv_protein.pdb structures/8FBV/8fbv_pocket.pdb structures/8FBV/8fbv_ligand.sdf structures/8FBV/8fbv_ligand.pdb structures/8FBV/8fbv_ligand.cif structures/8FBV/8fbv_complex.pdb structures/8FBV/8fbv_complex.cif 8FDA classic Human cytochrome P450 17A1 (CYP17A1) human Na Na 3beta-formyl-5alpha-pregnanolone-(R)-20-isonitrile (compound 1; 20-(R)-1) "[""XPK""]" 1 Kd Kd = = 149 aM 1.49e-07 [] unit_conversion 15.826813731587727 success True direct_binding CYP17A1 optical titration/tight-binding equation; reported alongside abiraterone comparison. 2 “tight binding equation fitting this data estimates of 44 pM ... for abiraterone and 149 aM ... for 1, respectively.” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8FDA\8FDA_metadata.json point structures/8FDA/8fda_protein.pdb structures/8FDA/8fda_pocket.pdb structures/8FDA/8fda_ligand.sdf structures/8FDA/8fda_ligand.pdb structures/8FDA/8fda_ligand.cif structures/8FDA/8fda_complex.pdb structures/8FDA/8fda_complex.cif 8FE8 classic HIV-1 reverse transcriptase (RT) Human immunodeficiency virus type 1 (HIV-1) Na wild-type (WT) 18b1 "[""XRB""]" 1 IC50 IC50 = = 0.093 ± 0.017 μM 93.0 [] unit_conversion 7.031517051446065 success True biochemical_inhibition Inhibition of biotin deoxyuridine triphosphate incorporation into HIV-1 IIIB RT by 50% (mean ± SD, n = 2). 7 Table 3, “Inhibitory activity against WT HIV-1 RT,” reports 18b1 IC50 = 0.093 ± 0.017 μM; its footnote defines the RT biochemical inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8FE8\8FE8_metadata.json point structures/8FE8/8fe8_protein.pdb structures/8FE8/8fe8_pocket.pdb structures/8FE8/8fe8_ligand.sdf structures/8FE8/8fe8_ligand.pdb structures/8FE8/8fe8_ligand.cif structures/8FE8/8fe8_complex.pdb structures/8FE8/8fe8_complex.cif 8FET classic flavanone 4-reductase (SbFNR1) Sorghum bicolor SbFNR1 cDNA cloned into pET-30a(+) Na NADP+ "[""NAP""]" 1 Kd Kd = = 13.91 ± 2.72 µM 13910.0 [] unit_conversion 4.856672870007953 success True direct_binding Isothermal titration calorimetry (Table 2). 8 Table 2 reports SbFNR1–NADP+ Kd of 13.91 ± 2.72 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FET\8FET_metadata.json point structures/8FET/8fet_protein.pdb structures/8FET/8fet_pocket.pdb structures/8FET/8fet_ligand.sdf structures/8FET/8fet_ligand.pdb structures/8FET/8fet_ligand.cif structures/8FET/8fet_complex.pdb structures/8FET/8fet_complex.cif 8FFF classic Staphylococcus aureus D-alanine D-alanine ligase Staphylococcus aureus Na Na acetate "[""ACT""]" 1 IC50 IC50 = = 400.3 ± 8 mM 400300000.0 [] unit_conversion 0.3976144098948957 success True biochemical_inhibition In-vitro kinetic inhibition of purified recombinant 6×His-tagged S. aureus Ddl by sodium acetate; IC50 curve reported for Ddl activity. 14 The paper states that varying acetate concentrations inhibited Ddl in vitro and reports an IC50 of 400.3 ± 8 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FFF\8FFF_metadata.json point structures/8FFF/8fff_protein.pdb structures/8FFF/8fff_pocket.pdb structures/8FFF/8fff_ligand.sdf structures/8FFF/8fff_ligand.pdb structures/8FFF/8fff_ligand.cif structures/8FFF/8fff_complex.pdb structures/8FFF/8fff_complex.cif 8FFS classic Klebsiella pneumoniae AcrB multidrug efflux pump Klebsiella pneumoniae Full-length KpAcrB with an N-terminal 6xHis tag; modeled residues 1-1033 of 1048 Na erythromycin (Ery; C37H67NO13) "[""ERY""]" 1 Kd Kd = = 14.4 ± 2.6 µM 14400.0 [] unit_conversion 4.841637507904751 success True direct_binding Microscale thermophoresis interaction assay between KpAcrB and erythromycin. 5 “The equilibrium dissociation constant (K_D) for KpAcrB and Ery interaction is 14.4 ± 2.6 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8FFS\8FFS_metadata.json point structures/8FFS/8ffs_protein.pdb structures/8FFS/8ffs_pocket.pdb structures/8FFS/8ffs_ligand.sdf structures/8FFS/8ffs_ligand.pdb structures/8FFS/8ffs_ligand.cif structures/8FFS/8ffs_complex.pdb structures/8FFS/8ffs_complex.cif 8FG1 extended Human diaphanous 1 (DIAPH1), diaphanous inhibitory domain (DID) Human DIAPH1 DID residues 142-380 bound to a 29-residue DAD peptide corresponding to residues 1194-1222 DAD M1199L DAD M1199L peptide "[""CHAIN:B""]" 1 Kd Kd = = 270 ± 100 nM 270.0 [] unit_conversion 6.568636235841012 success True direct_binding Tryptophan fluorescence spectroscopy measurement of the 1:1 DID-DAD M1199L interaction. 3 “The strength of the DID–DAD M1199L interaction was measured using tryptophan fluorescence spectroscopy and yielded a macroscopic binding constant of 270 ± 100 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8FG1\8FG1_metadata.json point structures/8FG1/8fg1_protein.pdb structures/8FG1/8fg1_pocket.pdb structures/8FG1/8fg1_ligand.pdb structures/8FG1/8fg1_ligand.cif structures/8FG1/8fg1_complex.pdb structures/8FG1/8fg1_complex.cif 8FG9 classic neuronal nitric oxide synthase rat heme domain Na compound 16; 6-(5-(2-(dimethylamino)ethyl)-2,3-difluorophenethyl)pyridin-2-amine "[""XVO""]" 1 Ki Ki = = 1108 nM 1108.0 [] unit_conversion 5.955460239607589 success True biochemical_inhibition Purified rat nNOS inhibition assay; Ki calculated from IC50 dose-response curves. 46 Table 1 lists compound 16·2HCl: rat nNOS Ki 1108 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FG9\8FG9_metadata.json point structures/8FG9/8fg9_protein.pdb structures/8FG9/8fg9_pocket.pdb structures/8FG9/8fg9_ligand.sdf structures/8FG9/8fg9_ligand.pdb structures/8FG9/8fg9_ligand.cif structures/8FG9/8fg9_complex.pdb structures/8FG9/8fg9_complex.cif 8FGA classic neuronal nitric oxide synthase rat heme domain Na compound 17; 6-(5-(2-(dimethylamino)ethyl)-2,3-difluorophenethyl)-4-methylpyridin-2-amine "[""XVU""]" 1 Ki Ki = = 15 nM 15.0 [] unit_conversion 7.823908740944319 success True biochemical_inhibition Purified rat nNOS inhibition assay; Ki calculated from IC50 dose-response curves. 46 Table 1 lists compound 17·2HCl: rat nNOS Ki 15 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FGA\8FGA_metadata.json point structures/8FGA/8fga_protein.pdb structures/8FGA/8fga_pocket.pdb structures/8FGA/8fga_ligand.sdf structures/8FGA/8fga_ligand.pdb structures/8FGA/8fga_ligand.cif structures/8FGA/8fga_complex.pdb structures/8FGA/8fga_complex.cif 8FGB classic neuronal nitric oxide synthase rat heme domain Na compound 19; 4-(5-(2-(dimethylamino)ethyl)-2,3-difluorophenethyl)-6-methylpyrimidin-2-amine "[""V80""]" 1 Ki Ki = = 6577 nM 6577.0 [] unit_conversion 5.181972158140743 success True biochemical_inhibition Purified rat nNOS inhibition assay; Ki calculated from IC50 dose-response curves. 46 Table 1 lists compound 19·2HCl: rat nNOS Ki 6577 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FGB\8FGB_metadata.json point structures/8FGB/8fgb_protein.pdb structures/8FGB/8fgb_pocket.pdb structures/8FGB/8fgb_ligand.sdf structures/8FGB/8fgb_ligand.pdb structures/8FGB/8fgb_ligand.cif structures/8FGB/8fgb_complex.pdb structures/8FGB/8fgb_complex.cif 8FGC classic neuronal nitric oxide synthase rat heme domain Na compound 20; 6-(5-(2-aminoethyl)-2,3-difluorophenethyl)-4-methylpyridin-2-amine "[""XVZ""]" 1 Ki Ki = = 60 nM 60.0 [] unit_conversion 7.221848749616356 success True biochemical_inhibition Purified rat nNOS inhibition assay; Ki calculated from IC50 dose-response curves. 46 Table 1 lists compound 20·2HCl: rat nNOS Ki 60 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FGC\8FGC_metadata.json point structures/8FGC/8fgc_protein.pdb structures/8FGC/8fgc_pocket.pdb structures/8FGC/8fgc_ligand.sdf structures/8FGC/8fgc_ligand.pdb structures/8FGC/8fgc_ligand.cif structures/8FGC/8fgc_complex.pdb structures/8FGC/8fgc_complex.cif 8FGN classic endothelial nitric oxide synthase human heme domain Na compound 16; 6-(5-(2-(dimethylamino)ethyl)-2,3-difluorophenethyl)pyridin-2-amine "[""XVO""]" 1 Ki Ki = = 61362 nM 61362.0 [] unit_conversion 4.212100493667803 success True biochemical_inhibition Human eNOS inhibition assay; Ki calculated from IC50 dose-response curves. 46 Table 1 lists compound 16·2HCl: human eNOS Ki 61362 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FGN\8FGN_metadata.json point structures/8FGN/8fgn_protein.pdb structures/8FGN/8fgn_pocket.pdb structures/8FGN/8fgn_ligand.sdf structures/8FGN/8fgn_ligand.pdb structures/8FGN/8fgn_ligand.cif structures/8FGN/8fgn_complex.pdb structures/8FGN/8fgn_complex.cif 8FGO classic endothelial nitric oxide synthase human heme domain Na compound 17; 6-(5-(2-(dimethylamino)ethyl)-2,3-difluorophenethyl)-4-methylpyridin-2-amine "[""XVU""]" 1 Ki Ki = = 20423 nM 20423.0 [] unit_conversion 4.68988046265319 success True biochemical_inhibition Human eNOS inhibition assay; Ki calculated from IC50 dose-response curves. 46 Table 1 lists compound 17·2HCl: human eNOS Ki 20423 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FGO\8FGO_metadata.json point structures/8FGO/8fgo_protein.pdb structures/8FGO/8fgo_pocket.pdb structures/8FGO/8fgo_ligand.sdf structures/8FGO/8fgo_ligand.pdb structures/8FGO/8fgo_ligand.cif structures/8FGO/8fgo_complex.pdb structures/8FGO/8fgo_complex.cif 8FHM classic RNase A Na Na Na uridine 5'-hexaphosphate (p6U) "[""U6F""]" 1 Ki Ki = = 1.1 ± 0.2 μM 1100.0 [] unit_conversion 5.958607314841775 success True biochemical_inhibition RNase A ribonucleolytic-inhibition assay using a FRET-tagged chimeric oligonucleotide substrate; 40 pM RNase A, 15 min incubation, n = 4 wells. 4 Figure 5A prints Ki = 1.1 ± 0.2 μM for p6U; Table 1 also lists p6U, Ki 1.1 ± 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FHM\8FHM_metadata.json point structures/8FHM/8fhm_protein.pdb structures/8FHM/8fhm_pocket.pdb structures/8FHM/8fhm_ligand.sdf structures/8FHM/8fhm_ligand.pdb structures/8FHM/8fhm_ligand.cif structures/8FHM/8fhm_complex.pdb structures/8FHM/8fhm_complex.cif 8FIC classic CYP114 Erwinia tracheiphila EtCYP114 with N-terminal His-tag Na ent-kaurenoic acid (KA) "[""NE4""]" 1 Kd Kd = = 65 ± 7 nM 65.0 [] unit_conversion 7.187086643357144 success True direct_binding UV–Vis spectral binding assay of purified EtCYP114 with KA. 3 “quite tight binding was observed, with the measured Kd = 65 ± 7 nM.” The same page states that EtCYP114 was cocrystallized with KA; page 6 maps Crystal Form 1 to 8FIC. auto_single_measurement only accepted activity measurement [1] 1 structures\8FIC\8FIC_metadata.json point structures/8FIC/8fic_protein.pdb structures/8FIC/8fic_pocket.pdb structures/8FIC/8fic_ligand.sdf structures/8FIC/8fic_ligand.pdb structures/8FIC/8fic_ligand.cif structures/8FIC/8fic_complex.pdb structures/8FIC/8fic_complex.cif 8FID classic CYP114 Erwinia tracheiphila EtCYP114 with N-terminal His-tag Na ent-kaurenoic acid (KA) "[""NE4""]" 1 Kd Kd = = 65 ± 7 nM 65.0 [] unit_conversion 7.187086643357144 success True direct_binding UV–Vis spectral binding assay of purified EtCYP114 with KA. 3 “quite tight binding was observed, with the measured Kd = 65 ± 7 nM.” The same page states that EtCYP114 was cocrystallized with KA; page 6 maps Crystal Form 2 to 8FID. auto_single_measurement only accepted activity measurement [1] 1 structures\8FID\8FID_metadata.json point structures/8FID/8fid_protein.pdb structures/8FID/8fid_pocket.pdb structures/8FID/8fid_ligand.sdf structures/8FID/8fid_ligand.pdb structures/8FID/8fid_ligand.cif structures/8FID/8fid_complex.pdb structures/8FID/8fid_complex.cif 8FJ4 classic LSD1-CoREST human His6-tagged human LSD1(Delta150, residues 151-852)-CoREST(Delta307, residues 308-485) Na compound 15 "[""XZU""]" 1 IC50 IC50 = = 333 ± 1 nM 333.0 [] unit_conversion 6.47755576649368 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8FJ4 to compound 15 and reports IC50 333 ± 1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FJ4\8FJ4_metadata.json point structures/8FJ4/8fj4_protein.pdb structures/8FJ4/8fj4_pocket.pdb structures/8FJ4/8fj4_ligand.sdf structures/8FJ4/8fj4_ligand.pdb structures/8FJ4/8fj4_ligand.cif structures/8FJ4/8fj4_complex.pdb structures/8FJ4/8fj4_complex.cif 8FPE classic pregnane X receptor (PXR) Na Na Na T0-BP "[""Y5B""]" 1 IC50 IC50 = = 158.8 ± 26.2 nM 158.8 [] unit_conversion 6.799149501908922 success True direct_binding TR-FRET PXR competitive binding assay; T0901317-analogue binding table. 6 Figure 4 reports T0-BP IC50 = 158.8 ± 26.2 nM. Page 9 states that the T0-BP structure is deposited as PDB ID 8FPE. auto_single_measurement only accepted activity measurement [1] 1 structures\8FPE\8FPE_metadata.json point structures/8FPE/8fpe_protein.pdb structures/8FPE/8fpe_pocket.pdb structures/8FPE/8fpe_ligand.sdf structures/8FPE/8fpe_ligand.pdb structures/8FPE/8fpe_ligand.cif structures/8FPE/8fpe_complex.pdb structures/8FPE/8fpe_complex.cif 8FQX classic Carbonic Anhydrase II Na Na Na 3g "[""N84""]" 1 Ki Ki = = 463 nM 463.0 [] unit_conversion 6.334419008982047 success True biochemical_inhibition Stopped-flow CO2 hydrase assay; recombinant CA isoforms; inhibition constants obtained by nonlinear least-squares methods. 3 Table 1 reports compound 3g Ki = 463 nM for CA II; page 10 describes the stopped-flow CO2 hydrase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8FQX\8FQX_metadata.json point structures/8FQX/8fqx_protein.pdb structures/8FQX/8fqx_pocket.pdb structures/8FQX/8fqx_ligand.sdf structures/8FQX/8fqx_ligand.pdb structures/8FQX/8fqx_ligand.cif structures/8FQX/8fqx_complex.pdb structures/8FQX/8fqx_complex.cif 8FQY classic Carbonic Anhydrase II Na Na Na 3h "[""N8A""]" 1 Ki Ki = = 331 nM 331.0 [] unit_conversion 6.480172006224281 success True biochemical_inhibition Stopped-flow CO2 hydrase assay; recombinant CA isoforms; inhibition constants obtained by nonlinear least-squares methods. 3 Table 1 reports compound 3h Ki = 331 nM for CA II; page 10 describes the stopped-flow CO2 hydrase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8FQY\8FQY_metadata.json point structures/8FQY/8fqy_protein.pdb structures/8FQY/8fqy_pocket.pdb structures/8FQY/8fqy_ligand.sdf structures/8FQY/8fqy_ligand.pdb structures/8FQY/8fqy_ligand.cif structures/8FQY/8fqy_complex.pdb structures/8FQY/8fqy_complex.cif 8FQZ classic Carbonic Anhydrase II Na Na Na 3j "[""N7S""]" 1 Ki Ki = = 75.9 nM 75.9 [] unit_conversion 7.11975822410452 success True biochemical_inhibition Stopped-flow CO2 hydrase assay; recombinant CA isoforms; inhibition constants obtained by nonlinear least-squares methods. 3 Table 1 reports compound 3j Ki = 75.9 nM for CA II; page 10 describes the stopped-flow CO2 hydrase inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8FQZ\8FQZ_metadata.json point structures/8FQZ/8fqz_protein.pdb structures/8FQZ/8fqz_pocket.pdb structures/8FQZ/8fqz_ligand.sdf structures/8FQZ/8fqz_ligand.pdb structures/8FQZ/8fqz_ligand.cif structures/8FQZ/8fqz_complex.pdb structures/8FQZ/8fqz_complex.cif 8FR3 classic EF-Tu Escherichia coli (E. coli) 6His-tagged EF-Tu expressed from pQE60-tufA-6xHis Na KKL-55 "[""Y7C""]" 1 Kd Kd = = 1.6 ± 0.02 µM 1600.0 [] unit_conversion 5.795880017344075 success True direct_binding Microscale thermophoresis binding of purified EF-Tu·GDP to KKL-55. 5 Fig. 2B reports: “EF-Tu GDP, Kd = 1.6 ± 0.02 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8FR3\8FR3_metadata.json point structures/8FR3/8fr3_protein.pdb structures/8FR3/8fr3_pocket.pdb structures/8FR3/8fr3_ligand.sdf structures/8FR3/8fr3_ligand.pdb structures/8FR3/8fr3_ligand.cif structures/8FR3/8fr3_complex.pdb structures/8FR3/8fr3_complex.cif 8FRL classic LptB2FG Acinetobacter baylyi LptB2FG Na compound 3 (RO7075573) "[""Y75""]" 1 Ki Ki = = 56 ± 8 nM 56.0 [] unit_conversion 7.251811972993799 success True direct_binding Scintillation-proximity competitive binding assay: displacement of radiolabelled compound 2 from His-tagged LptB2FG in the presence of E. coli LPS and absence of LptC. 4 Fig. 4g reports Ki = 56 ± 8 nM for compound 3; its legend states active compounds bind LptB2FG through SPA in the presence of LPS. auto_single_measurement only accepted activity measurement [1] 1 structures\8FRL\8FRL_metadata.json point structures/8FRL/8frl_protein.pdb structures/8FRL/8frl_pocket.pdb structures/8FRL/8frl_ligand.sdf structures/8FRL/8frl_ligand.pdb structures/8FRL/8frl_ligand.cif structures/8FRL/8frl_complex.pdb structures/8FRL/8frl_complex.cif 8FRN classic LptB2FG Acinetobacter baylyi LptB2FG Na compound 2 (Zosurabalpin) "[""VB6""]" 1 Ki Ki = = 35 ± 2 nM 35.0 [] unit_conversion 7.455931955649724 success True direct_binding Scintillation-proximity competitive binding assay: radiolabelled compound 2 binding to His-tagged LptB2FG in the presence of E. coli LPS and absence of LptC. 4 Fig. 4g reports Ki = 35 ± 2 nM for compound 2; the caption describes LPS-dependent SPA binding to LptB2FG. auto_single_measurement only accepted activity measurement [1] 1 structures\8FRN\8FRN_metadata.json point structures/8FRN/8frn_protein.pdb structures/8FRN/8frn_pocket.pdb structures/8FRN/8frn_ligand.sdf structures/8FRN/8frn_ligand.pdb structures/8FRN/8frn_ligand.cif structures/8FRN/8frn_complex.pdb structures/8FRN/8frn_complex.cif 8FRO classic LptB2FG Acinetobacter baylyi LptB2FG Na compound 1 (R07196472) "[""MG3""]" 1 Ki Ki = = 35 ± 7 nM 35.0 [] unit_conversion 7.455931955649724 success True direct_binding Scintillation-proximity competitive binding assay: compound 1 displacement of radiolabelled compound 2 from His-tagged LptB2FG in the presence of E. coli LPS and absence of LptC. 4 Fig. 4g reports Ki = 35 ± 7 nM for compound 1; the caption states binding was measured by SPA in the presence of LPS. auto_single_measurement only accepted activity measurement [1] 1 structures\8FRO\8FRO_metadata.json point structures/8FRO/8fro_protein.pdb structures/8FRO/8fro_pocket.pdb structures/8FRO/8fro_ligand.sdf structures/8FRO/8fro_ligand.pdb structures/8FRO/8fro_ligand.cif structures/8FRO/8fro_complex.pdb structures/8FRO/8fro_complex.cif 8FS1 classic CamA adenine methyltransferase Clostridioides difficile Na Na 11a (YD905) "[""YB0""]" 2 Ki Ki = = 0.09 ± 0.01 µM 90.0 [] unit_conversion 7.045757490560675 success True biochemical_inhibition CamA methylation kinetics varying SAM and 11a; Figure 2E inset. 3 Figure 2E reports Ki = 0.09 ± 0.01 µM for 11a and states competitive inhibition with respect to SAM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8FS1\8FS1_metadata.json point structures/8FS1/8fs1_protein.pdb structures/8FS1/8fs1_pocket.pdb structures/8FS1/8fs1_ligand.sdf structures/8FS1/8fs1_ligand.pdb structures/8FS1/8fs1_ligand.cif structures/8FS1/8fs1_complex.pdb structures/8FS1/8fs1_complex.cif 8FS2 classic CamA adenine methyltransferase Clostridioides difficile Na Na 11b (YD907) "[""YB5""]" 1 IC50 IC50 = = 0.27±0.02 µM 270.0 [] unit_conversion 6.568636235841012 success True biochemical_inhibition CamA-mediated methylation inhibition; Figure 2C table. 3 Figure 2C reports CamA IC50 = 0.27±0.02 µM for 11b (YD907). auto_single_measurement only accepted activity measurement [1] 1 structures\8FS2\8FS2_metadata.json point structures/8FS2/8fs2_protein.pdb structures/8FS2/8fs2_pocket.pdb structures/8FS2/8fs2_ligand.sdf structures/8FS2/8fs2_ligand.pdb structures/8FS2/8fs2_ligand.cif structures/8FS2/8fs2_complex.pdb structures/8FS2/8fs2_complex.cif 8FSQ extended YejA Escherichia coli YejA lacking the predicted N-terminal 19-residue signaling peptide wild-type Microcin C7 (McC) "[""CHAIN:B""]" 1 Ki Ki = = 0.95 µM 950.0 [] unit_conversion 6.022276394711152 success True direct_binding Fluorescence-polarization competition assay using fMccA_GGK-FITC recognition by YejA; McC was the competitor. 2 Fig. 1F visibly prints “Ki = 0.95 µM” for McC; the caption identifies panels D–F as FP competition assays for fMccA_GGK-FITC recognition by YejA. auto_single_measurement only accepted activity measurement [1] 1 structures\8FSQ\8FSQ_metadata.json point structures/8FSQ/8fsq_protein.pdb structures/8FSQ/8fsq_pocket.pdb structures/8FSQ/8fsq_ligand.pdb structures/8FSQ/8fsq_ligand.cif structures/8FSQ/8fsq_complex.pdb structures/8FSQ/8fsq_complex.cif 8FSR extended YejA Escherichia coli YejA lacking the predicted N-terminal 19-residue signaling peptide wild-type fMccA "[""CHAIN:B""]" 1 Ki Ki = = 0.12 µM 120.0 [] unit_conversion 6.920818753952375 success True direct_binding Fluorescence-polarization competition assay using fMccA_GGK-FITC recognition by YejA; fMccA was the competitor. 2 Fig. 1D visibly prints “Ki = 0.12 µM” for fMccA; the caption identifies panels D–F as FP competition assays for fMccA_GGK-FITC recognition by YejA. auto_single_measurement only accepted activity measurement [1] 1 structures\8FSR\8FSR_metadata.json point structures/8FSR/8fsr_protein.pdb structures/8FSR/8fsr_pocket.pdb structures/8FSR/8fsr_ligand.pdb structures/8FSR/8fsr_ligand.cif structures/8FSR/8fsr_complex.pdb structures/8FSR/8fsr_complex.cif 8FU3 classic Respiratory syncytial virus L + P polymerase complex Human respiratory syncytial virus, strain A2 Codon-optimized RSV L protein with N-terminal twin StrepTag and RSV P protein with C-terminal 6x His-tag Na JNJ-8003 "[""YBK""]" 4 Kd Kd = = 0.84 nM 0.84 [] unit_conversion 9.075720713938118 success True direct_binding Surface plasmon resonance measurement of JNJ-8003 binding to RSV L + P complex. 3 “Surface plasmon resonance (SPR) demonstrated JNJ-8003 bound to the RSV L + P complex with a Kd of 0.84 nM.” auto_metric_priority unique highest-priority metric family: Kd [4] 4 structures\8FU3\8FU3_metadata.json point structures/8FU3/8fu3_protein.pdb structures/8FU3/8fu3_pocket.pdb structures/8FU3/8fu3_ligand.sdf structures/8FU3/8fu3_ligand.pdb structures/8FU3/8fu3_ligand.cif structures/8FU3/8fu3_complex.pdb structures/8FU3/8fu3_complex.cif 8FU5 classic carotenoid oxygenase 1 (CAO1) Neurospora crassa Na wild-type piceatannol "[""PIT""]" 1 Kd Kd = = 0.05 ± 0.16 µM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding Anaerobic piceatannol titration of wild-type Fe(II)-CAO1, monitored by UV–visible absorption and CD; one-site quadratic binding fit. 3 Least-squares fitting of the saturable feature to a one-site quadratic binding equation resulted in a dissociation constant (Kd) of 0.05 ± 0.16 µM for piceatannol binding to the wildtype Fe(II)-CAO1 active site. auto_single_measurement only accepted activity measurement [1] 1 structures\8FU5\8FU5_metadata.json point structures/8FU5/8fu5_protein.pdb structures/8FU5/8fu5_pocket.pdb structures/8FU5/8fu5_ligand.sdf structures/8FU5/8fu5_ligand.pdb structures/8FU5/8fu5_ligand.cif structures/8FU5/8fu5_complex.pdb structures/8FU5/8fu5_complex.cif 8FUI classic HIV-1 protease HIV-1 Na wild type GRL-02519A (inhibitor 5b) "[""Y9R""]" 1 Ki Ki = = 0.17 nM 0.17 [] unit_conversion 9.769551078621726 success True biochemical_inhibition Enzyme-inhibitory assay of HIV-1 protease; Ki values represent at least 5 data points. 6 Table 1 lists inhibitor 5b with Ki = 0.17 nM; the text identifies 5b as an HIV-1 protease inhibitor and states the enzyme-inhibitory assay was reported by Toth and Marshall. auto_single_measurement only accepted activity measurement [1] 1 structures\8FUI\8FUI_metadata.json point structures/8FUI/8fui_protein.pdb structures/8FUI/8fui_pocket.pdb structures/8FUI/8fui_ligand.sdf structures/8FUI/8fui_ligand.pdb structures/8FUI/8fui_ligand.cif structures/8FUI/8fui_complex.pdb structures/8FUI/8fui_complex.cif 8FUJ classic HIV-1 protease HIV-1 Na wild type GRL-03419A (inhibitor 5c) "[""Y9N""]" 1 Ki Ki = = 0.58 nM 0.58 [] unit_conversion 9.236572006437063 success True biochemical_inhibition Enzyme-inhibitory assay of HIV-1 protease; Ki values represent at least 5 data points. 6 Table 1 lists inhibitor 5c with Ki = 0.58 nM; the text identifies 5c as an HIV-1 protease inhibitor and states the enzyme-inhibitory assay was reported by Toth and Marshall. auto_single_measurement only accepted activity measurement [1] 1 structures\8FUJ\8FUJ_metadata.json point structures/8FUJ/8fuj_protein.pdb structures/8FUJ/8fuj_pocket.pdb structures/8FUJ/8fuj_ligand.sdf structures/8FUJ/8fuj_ligand.pdb structures/8FUJ/8fuj_ligand.cif structures/8FUJ/8fuj_complex.pdb structures/8FUJ/8fuj_complex.cif 8FV2 classic CBP Na CBP bromodomain residues 1081-1197 Na CCS-1477 (CCS1477) "[""JHL""]" 1 Kd Kd = = 4.0 ± 6.7 nM 4.0 [] unit_conversion 8.397940008672037 success True direct_binding Isothermal titration calorimetry (ITC); Table 1. 7 Table 1 lists CCS1477 Kd for CBP as 4.0 ± 6.7 nM; the table notes this is a single ITC experiment fit ± SEM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FV2\8FV2_metadata.json point structures/8FV2/8fv2_protein.pdb structures/8FV2/8fv2_pocket.pdb structures/8FV2/8fv2_ligand.sdf structures/8FV2/8fv2_ligand.pdb structures/8FV2/8fv2_ligand.cif structures/8FV2/8fv2_complex.pdb structures/8FV2/8fv2_complex.cif 8FVF classic EP300 Na EP300 bromodomain residues 1048-1161 Na CCS-1477 (CCS1477) "[""JHL""]" 1 Kd Kd = = 25.5 ± 46.3 nM 25.5 [] unit_conversion 7.5934598195660445 success True direct_binding Isothermal titration calorimetry (ITC); Table 1. 7 Table 1 lists CCS1477 Kd for EP300 as 25.5 ± 46.3 nM; the table notes this is a single ITC experiment fit ± SEM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FVF\8FVF_metadata.json point structures/8FVF/8fvf_protein.pdb structures/8FVF/8fvf_pocket.pdb structures/8FVF/8fvf_ligand.sdf structures/8FVF/8fvf_ligand.pdb structures/8FVF/8fvf_ligand.cif structures/8FVF/8fvf_complex.pdb structures/8FVF/8fvf_complex.cif 8FVK classic BRD4 Na BRD4-BD1 residues 44-168 Na CCS-1477 (CCS1477) "[""JHL""]" 1 Kd Kd = = 403 ± 137 nM 403.0 [] unit_conversion 6.39469495385889 success True direct_binding Isothermal titration calorimetry (ITC); Table 1. 7 Table 1 lists CCS1477 Kd for BRD4-1 as 403 ± 137 nM; the table notes this is a single ITC experiment fit ± SEM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FVK\8FVK_metadata.json point structures/8FVK/8fvk_protein.pdb structures/8FVK/8fvk_pocket.pdb structures/8FVK/8fvk_ligand.sdf structures/8FVK/8fvk_ligand.pdb structures/8FVK/8fvk_ligand.cif structures/8FVK/8fvk_complex.pdb structures/8FVK/8fvk_complex.cif 8FVS classic CBP Na CBP bromodomain residues 1081-1197 Na CCS1477int (CCS1477int1; compound 1) "[""YBE""]" 1 Kd Kd = = 1550 ± 600 nM 1550.0 [] unit_conversion 5.809668301829708 success True direct_binding Isothermal titration calorimetry (ITC); Table 1. 7 Table 1 identifies compound 1 as CCS1477int1 and lists its CBP Kd as 1550 ± 600 nM; the table notes this is a single ITC experiment fit ± SEM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FVS\8FVS_metadata.json point structures/8FVS/8fvs_protein.pdb structures/8FVS/8fvs_pocket.pdb structures/8FVS/8fvs_ligand.sdf structures/8FVS/8fvs_ligand.pdb structures/8FVS/8fvs_ligand.cif structures/8FVS/8fvs_complex.pdb structures/8FVS/8fvs_complex.cif 8FW0 classic MtrR Neisseria gonorrhoeae Na Na beta-Estradiol "[""EST""]" 1 Kd Kd = = 1.67 ± 1.1 µM 1670.0 [] unit_conversion 5.777283528852417 success True direct_binding Isothermal titration calorimetry (ITC) of purified MtrR with β-estradiol. 3 ITC studies found that β-estradiol binds MtrR with a Kd of 1.67 ± 1.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FW0\8FW0_metadata.json point structures/8FW0/8fw0_protein.pdb structures/8FW0/8fw0_pocket.pdb structures/8FW0/8fw0_ligand.sdf structures/8FW0/8fw0_ligand.pdb structures/8FW0/8fw0_ligand.cif structures/8FW0/8fw0_complex.pdb structures/8FW0/8fw0_complex.cif 8FW8 classic MtrR Neisseria gonorrhoeae Na Na Progesterone "[""STR""]" 1 Kd Kd = = 2.75 ± 0.7 µM 2750.0 [] unit_conversion 5.560667306169737 success True direct_binding Isothermal titration calorimetry (ITC) of purified MtrR with progesterone. 3 ITC studies found that progesterone binds MtrR with a Kd of 2.75 ± 0.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FW8\8FW8_metadata.json point structures/8FW8/8fw8_protein.pdb structures/8FW8/8fw8_pocket.pdb structures/8FW8/8fw8_ligand.sdf structures/8FW8/8fw8_ligand.pdb structures/8FW8/8fw8_ligand.cif structures/8FW8/8fw8_complex.pdb structures/8FW8/8fw8_complex.cif 8FXA classic CBP Na CBP bromodomain residues 1081-1197 Na iCBP4 (compound 4) "[""YJY""]" 1 Kd Kd = = 116 ± 68 nM 116.0 [] unit_conversion 6.935542010773082 success True direct_binding Isothermal titration calorimetry (ITC); Table 1. 7 Table 1 identifies compound 4 as iCBP-4 and lists its CBP Kd as 116 ± 68 nM; the table notes this is a single ITC experiment fit ± SEM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FXA\8FXA_metadata.json point structures/8FXA/8fxa_protein.pdb structures/8FXA/8fxa_pocket.pdb structures/8FXA/8fxa_ligand.sdf structures/8FXA/8fxa_ligand.pdb structures/8FXA/8fxa_ligand.cif structures/8FXA/8fxa_complex.pdb structures/8FXA/8fxa_complex.cif 8FXE classic CBP Na CBP bromodomain residues 1081-1197 Na iCBP6 (compound 6) "[""YID""]" 1 Kd Kd = = 30.0 ± 21.6 nM 30.0 [] unit_conversion 7.522878745280337 success True direct_binding Isothermal titration calorimetry (ITC); Table 1. 7 Table 1 identifies compound 6 as iCBP-6 and lists its CBP Kd as 30.0 ± 21.6 nM; the table notes this is a single ITC experiment fit ± SEM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FXE\8FXE_metadata.json point structures/8FXE/8fxe_protein.pdb structures/8FXE/8fxe_pocket.pdb structures/8FXE/8fxe_ligand.sdf structures/8FXE/8fxe_ligand.pdb structures/8FXE/8fxe_ligand.cif structures/8FXE/8fxe_complex.pdb structures/8FXE/8fxe_complex.cif 8FXO classic CBP Na CBP bromodomain residues 1081-1197 Na iCBP8 (compound 7) "[""YN5""]" 1 Kd Kd = = 16.9 ± 10.2 nM 16.9 [] unit_conversion 7.772113295386326 success True direct_binding Isothermal titration calorimetry (ITC); Table 1. 7 Table 1 identifies compound 7 as iCBP-8 and lists its CBP Kd as 16.9 ± 10.2 nM; the table notes this is a single ITC experiment fit ± SEM. auto_single_measurement only accepted activity measurement [1] 1 structures\8FXO\8FXO_metadata.json point structures/8FXO/8fxo_protein.pdb structures/8FXO/8fxo_pocket.pdb structures/8FXO/8fxo_ligand.sdf structures/8FXO/8fxo_ligand.pdb structures/8FXO/8fxo_ligand.cif structures/8FXO/8fxo_complex.pdb structures/8FXO/8fxo_complex.cif 8FYU extended CHIP (C-terminus of Hsc70-interacting protein) human CHIP TPR domain, amino acids 22-154 Na Ac-SSTGSIDMVD-OH (10mer acetylated tau peptide) "[""CHAIN:C"", ""CHAIN:E""]" 1 Ki Ki = = 0.15 ± 0.02 µM 150.0 [] unit_conversion 6.823908740944319 success True direct_binding Fluorescence-polarization competition assay using synthetic 10-mer tauC3-derived peptide; inhibition constant derived from peptide displacement. 3 “Ki WT tauC3 = 0.15 ± 0.02 µM”; the preceding text identifies the tested material as a 10-mer acetylated tauC3 C-terminal peptide. The 8FYU structure is stated to contain Ac-SSTGSIDMVD-OH. auto_single_measurement only accepted activity measurement [1] 1 structures\8FYU\8FYU_metadata.json point structures/8FYU/8fyu_protein.pdb structures/8FYU/8fyu_pocket.pdb structures/8FYU/8fyu_ligand.pdb structures/8FYU/8fyu_ligand.cif structures/8FYU/8fyu_complex.pdb structures/8FYU/8fyu_complex.cif 8FYV classic Salmonella enterica serovar Typhimurium chemoreceptor Tsr Salmonella enterica serovar Typhimurium Soluble periplasmic Tsr ligand-binding domain, residues 32-187, with an N-terminal TEV-cleavage tag Na L-serine "[""SER""]" 1 Kd Kd ~ ~ 5 µM 5000.0 [] unit_conversion 5.301029995663981 success True direct_binding Isothermal titration calorimetry (ITC) of purified recombinant SeTsr LBD with L-serine. 15 “L-serine produces a robust exothermic binding curve, exhibiting a KD of approximately 5 μM (Figure 7K).” auto_single_measurement only accepted activity measurement [1] 1 structures\8FYV\8FYV_metadata.json point structures/8FYV/8fyv_protein.pdb structures/8FYV/8fyv_pocket.pdb structures/8FYV/8fyv_ligand.sdf structures/8FYV/8fyv_ligand.pdb structures/8FYV/8fyv_ligand.cif structures/8FYV/8fyv_complex.pdb structures/8FYV/8fyv_complex.cif 8G07 classic Mycobacterium smegmatis ATP synthase Mycobacterium smegmatis Na Na SQ31f "[""SQC""]" 2 IC50 IC50 = = 38 nM 38.0 [] unit_conversion 7.42021640338319 success True biochemical_inhibition ATP-synthesis assay in wild-type M. smegmatis inverted membrane vesicles with a proton motive force established and ATP production monitored by luciferase. 6 “the IC50 for SQ31f inhibition of ATP synthesis was 38 nM.” auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\8G07\8G07_metadata.json point structures/8G07/8g07_protein.pdb structures/8G07/8g07_pocket.pdb structures/8G07/8g07_ligand.sdf structures/8G07/8g07_ligand.pdb structures/8G07/8g07_ligand.cif structures/8G07/8g07_complex.pdb structures/8G07/8g07_complex.cif 8G08 classic Mycobacterium smegmatis ATP synthase Mycobacterium smegmatis Na Na SQ31f "[""SQC""]" 2 IC50 IC50 = = 38 nM 38.0 [] unit_conversion 7.42021640338319 success True biochemical_inhibition ATP-synthesis assay in wild-type M. smegmatis inverted membrane vesicles with a proton motive force established and ATP production monitored by luciferase. 6 “the IC50 for SQ31f inhibition of ATP synthesis was 38 nM.” auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\8G08\8G08_metadata.json point structures/8G08/8g08_protein.pdb structures/8G08/8g08_pocket.pdb structures/8G08/8g08_ligand.sdf structures/8G08/8g08_ligand.pdb structures/8G08/8g08_ligand.cif structures/8G08/8g08_complex.pdb structures/8G08/8g08_complex.cif 8G09 classic Mycobacterium smegmatis ATP synthase Mycobacterium smegmatis Na Na SQ31f "[""SQC""]" 2 IC50 IC50 = = 38 nM 38.0 [] unit_conversion 7.42021640338319 success True biochemical_inhibition ATP-synthesis assay in wild-type M. smegmatis inverted membrane vesicles with a proton motive force established and ATP production monitored by luciferase. 6 “the IC50 for SQ31f inhibition of ATP synthesis was 38 nM.” auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\8G09\8G09_metadata.json point structures/8G09/8g09_protein.pdb structures/8G09/8g09_pocket.pdb structures/8G09/8g09_ligand.sdf structures/8G09/8g09_ligand.pdb structures/8G09/8g09_ligand.cif structures/8G09/8g09_complex.pdb structures/8G09/8g09_complex.cif 8G0A classic Mycobacterium smegmatis ATP synthase Mycobacterium smegmatis Na Na SQ31f "[""SQC""]" 2 IC50 IC50 = = 38 nM 38.0 [] unit_conversion 7.42021640338319 success True biochemical_inhibition ATP-synthesis assay in wild-type M. smegmatis inverted membrane vesicles with a proton motive force established and ATP production monitored by luciferase. 6 “the IC50 for SQ31f inhibition of ATP synthesis was 38 nM.” auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\8G0A\8G0A_metadata.json point structures/8G0A/8g0a_protein.pdb structures/8G0A/8g0a_pocket.pdb structures/8G0A/8g0a_ligand.sdf structures/8G0A/8g0a_ligand.pdb structures/8G0A/8g0a_ligand.cif structures/8G0A/8g0a_complex.pdb structures/8G0A/8g0a_complex.cif 8G0T classic CnAcs1 acetyl-CoA synthetase Cryptococcus neoformans H99 Na Na cyclopropyl-AMP ester "[""YHK""]" 1 IC50 IC50 = = 9 µM 9000.0 [] unit_conversion 5.045757490560675 success True biochemical_inhibition Purified CnAcs1 enzyme inhibition assay. 9 “the IC50 of the cyclopropyl-AMP ester (9 µM)” toward CnAcs1. auto_single_measurement only accepted activity measurement [1] 1 structures\8G0T\8G0T_metadata.json point structures/8G0T/8g0t_protein.pdb structures/8G0T/8g0t_pocket.pdb structures/8G0T/8g0t_ligand.sdf structures/8G0T/8g0t_ligand.pdb structures/8G0T/8g0t_ligand.cif structures/8G0T/8g0t_complex.pdb structures/8G0T/8g0t_complex.cif 8G2H classic PRMT4 human PRMT4 residues 140-480 Na YD1113 "[""YVU""]" 1 IC50 IC50 = = 138 ± 12.9 nmol/L 138.0 [] unit_conversion 6.860120913598763 success True biochemical_inhibition PRMT-family inhibition determination at physiological SAM and substrate values by Reaction Biology Corp. 5 Figure 3f prints “PRMT4 138 ± 12.9” under IC50 (nmol/L) for YD1113. auto_single_measurement only accepted activity measurement [1] 1 structures\8G2H\8G2H_metadata.json point structures/8G2H/8g2h_protein.pdb structures/8G2H/8g2h_pocket.pdb structures/8G2H/8g2h_ligand.sdf structures/8G2H/8g2h_ligand.pdb structures/8G2H/8g2h_ligand.cif structures/8G2H/8g2h_complex.pdb structures/8G2H/8g2h_complex.cif 8G2I classic PRMT4 human PRMT4 residues 140-480 Na YD1290 "[""I0B""]" 1 IC50 IC50 < < 1 nmol/L 1.0 [] unit_conversion 9.0 success True biochemical_inhibition Panel of PRMT inhibition values for YD1290 under the same assay conditions; experiments performed in duplicate. 8 Figure 6 lists YD1290 for PRMT4 as “<1” under IC50 (nmol/L); the Figure 6 caption identifies these as inhibition activity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8G2I\8G2I_metadata.json point structures/8G2I/8g2i_protein.pdb structures/8G2I/8g2i_pocket.pdb structures/8G2I/8g2i_ligand.sdf structures/8G2I/8g2i_ligand.pdb structures/8G2I/8g2i_ligand.cif structures/8G2I/8g2i_complex.pdb structures/8G2I/8g2i_complex.cif 8G3S classic Mcl-1 Na N-terminal maltose-binding protein (MBP) fusion tag Na compound 11 "[""YLT""]" 1 Ki Ki = = 0.47 nM 0.47 [] unit_conversion 9.327902142064282 success True direct_binding HTRF competitive binding assay: displacement of Cy5-labeled Bim BH3 peptide from terbium-labeled Mcl-1. 5 Table 1 reports Mcl-1 Ki = 0.47 nM for compound 11; its footnote defines the HTRF Mcl-1/Bim BH3 displacement binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8G3S\8G3S_metadata.json point structures/8G3S/8g3s_protein.pdb structures/8G3S/8g3s_pocket.pdb structures/8G3S/8g3s_ligand.sdf structures/8G3S/8g3s_ligand.pdb structures/8G3S/8g3s_ligand.cif structures/8G3S/8g3s_complex.pdb structures/8G3S/8g3s_complex.cif 8G3T classic Mcl-1 Na N-terminal maltose-binding protein (MBP) fusion tag Na compound 12 "[""YLK""]" 1 Ki Ki = = 0.22 nM 0.22 [] unit_conversion 9.657577319177793 success True direct_binding HTRF competitive binding assay: displacement of Cy5-labeled Bim BH3 peptide from terbium-labeled Mcl-1. 5 Table 1 reports Mcl-1 Ki = 0.22 nM for compound 12; its footnote defines the HTRF Mcl-1/Bim BH3 displacement binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8G3T\8G3T_metadata.json point structures/8G3T/8g3t_protein.pdb structures/8G3T/8g3t_pocket.pdb structures/8G3T/8g3t_ligand.sdf structures/8G3T/8g3t_ligand.pdb structures/8G3T/8g3t_ligand.cif structures/8G3T/8g3t_complex.pdb structures/8G3T/8g3t_complex.cif 8G3U classic Mcl-1 Na N-terminal maltose-binding protein (MBP) fusion tag Na compound 21 "[""YKT""]" 1 Ki Ki = = 0.014 nM 0.014 [] unit_conversion 10.853871964321762 success True direct_binding HTRF competitive binding assay: displacement of Cy5-labeled Bim BH3 peptide from terbium-labeled Mcl-1. 7 Table 2 reports Mcl-1 Ki = 0.014 nM for compound 21; its footnote defines the HTRF Mcl-1/Bim BH3 displacement binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8G3U\8G3U_metadata.json point structures/8G3U/8g3u_protein.pdb structures/8G3U/8g3u_pocket.pdb structures/8G3U/8g3u_ligand.sdf structures/8G3U/8g3u_ligand.pdb structures/8G3U/8g3u_ligand.cif structures/8G3U/8g3u_complex.pdb structures/8G3U/8g3u_complex.cif 8G3W classic Mcl-1 Na N-terminal maltose-binding protein (MBP) fusion tag Na compound 28 "[""YKX""]" 1 Ki Ki = = 0.011 nM 0.011 [] unit_conversion 10.958607314841775 success True direct_binding HTRF competitive binding assay: displacement of Cy5-labeled Bim BH3 peptide from terbium-labeled Mcl-1. 9 Table 3 reports Mcl-1 Ki = 0.011 nM for compound 28; its footnote defines the HTRF Mcl-1/Bim BH3 displacement binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8G3W\8G3W_metadata.json point structures/8G3W/8g3w_protein.pdb structures/8G3W/8g3w_pocket.pdb structures/8G3W/8g3w_ligand.sdf structures/8G3W/8g3w_ligand.pdb structures/8G3W/8g3w_ligand.cif structures/8G3W/8g3w_complex.pdb structures/8G3W/8g3w_complex.cif 8G3X classic Mcl-1 Na N-terminal maltose-binding protein (MBP) fusion tag Na compound 32 "[""YLF""]" 1 Ki Ki = = 0.011 nM 0.011 [] unit_conversion 10.958607314841775 success True direct_binding HTRF competitive binding assay: displacement of Cy5-labeled Bim BH3 peptide from terbium-labeled Mcl-1. 9 Table 3 reports Mcl-1 Ki = 0.011 nM for compound 32; its footnote defines the HTRF Mcl-1/Bim BH3 displacement binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8G3X\8G3X_metadata.json point structures/8G3X/8g3x_protein.pdb structures/8G3X/8g3x_pocket.pdb structures/8G3X/8g3x_ligand.sdf structures/8G3X/8g3x_ligand.pdb structures/8G3X/8g3x_ligand.cif structures/8G3X/8g3x_complex.pdb structures/8G3X/8g3x_complex.cif 8G3Y classic Mcl-1 Na N-terminal maltose-binding protein (MBP) fusion tag Na compound 34 "[""YKL""]" 1 Ki Ki = = 0.014 nM 0.014 [] unit_conversion 10.853871964321762 success True direct_binding HTRF competitive binding assay: displacement of Cy5-labeled Bim BH3 peptide from terbium-labeled Mcl-1. 9 Table 3 reports Mcl-1 Ki = 0.014 nM for compound 34; its footnote defines the HTRF Mcl-1/Bim BH3 displacement binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8G3Y\8G3Y_metadata.json point structures/8G3Y/8g3y_protein.pdb structures/8G3Y/8g3y_pocket.pdb structures/8G3Y/8g3y_ligand.sdf structures/8G3Y/8g3y_ligand.pdb structures/8G3Y/8g3y_ligand.cif structures/8G3Y/8g3y_complex.pdb structures/8G3Y/8g3y_complex.cif 8G43 classic HDAC6 Na HDAC6 residues 1109-1213, tag-free crystal construct Na compound 9 (3-(3-(2-(methylamino)-2-oxoethyl)-4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid) "[""ZU6""]" 1 Kd Kd = = 14 ± 5.8 μM 14000.0 [] unit_conversion 4.853871964321762 success True direct_binding Fluorescence-polarization binding assay. 4 Table 1 reports HDAC6 FP Kdisp = 14 ± 5.8 μM for compound 9; Figure 2 maps compound 9 to HDAC6-UBD PDB 8G43. auto_single_measurement only accepted activity measurement [1] 1 structures\8G43\8G43_metadata.json point structures/8G43/8g43_protein.pdb structures/8G43/8g43_pocket.pdb structures/8G43/8g43_ligand.sdf structures/8G43/8g43_ligand.pdb structures/8G43/8g43_ligand.cif structures/8G43/8g43_complex.pdb structures/8G43/8g43_complex.cif 8G44 classic HDAC6 Na HDAC6 residues 1109-1213, tag-free crystal construct Na compound 15 (3-(3-(2-(benzylamino)-2-oxoethyl)-4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid) "[""ZU9""]" 1 Kd Kd = = 0.62 ± 0.39 μM 620.0 [] unit_conversion 6.207608310501746 success True direct_binding Fluorescence-polarization binding assay. 4 Table 1 reports HDAC6 FP Kdisp = 0.62 ± 0.39 μM for compound 15; Figure 3 maps compound 15 to HDAC6-UBD PDB 8G44. auto_single_measurement only accepted activity measurement [1] 1 structures\8G44\8G44_metadata.json point structures/8G44/8g44_protein.pdb structures/8G44/8g44_pocket.pdb structures/8G44/8g44_ligand.sdf structures/8G44/8g44_ligand.pdb structures/8G44/8g44_ligand.cif structures/8G44/8g44_complex.pdb structures/8G44/8g44_complex.cif 8G4Y extended ZNRF3 human ZNRF3 residues K56-M219 with a C-terminal Flag tag Na MK1-3.6.10 "[""CHAIN:B""]" 1 Kd Kd = = 38 nM 38.0 [] unit_conversion 7.42021640338319 success True direct_binding Apparent binding affinity measured by SPR using single-cycle kinetics; Figure 3D identifies MK1-3.6.10 monomer as 38 nM. 8 Figure 3D lists “MK1-3.6.10” with valency “monomer” and app K_D (nM) of 38; the figure legend states apparent binding affinity was measured by single-cycle kinetics. auto_single_measurement only accepted activity measurement [1] 1 structures\8G4Y\8G4Y_metadata.json point structures/8G4Y/8g4y_protein.pdb structures/8G4Y/8g4y_pocket.pdb structures/8G4Y/8g4y_ligand.pdb structures/8G4Y/8g4y_ligand.cif structures/8G4Y/8g4y_complex.pdb structures/8G4Y/8g4y_complex.cif 8G63 classic EGFR Na EGFR kinase domain residues 696-1022, cloned into pTriEx with an N-terminal 6xHis-GST fusion tag followed by a TEV protease cleavage site wild-type Ralimetinib (LY2228820) "[""YXT""]" 1 IC50 IC50 = = 0.180 µM 180.0 [] unit_conversion 6.7447274948966935 success True biochemical_inhibition In vitro recombinant kinase assay; Figure 3A, “Ralimetinib: EGFR inhibition.” 6 Figure 3A visibly prints “IC50: 0.180 µM” for ralimetinib inhibition of wild-type EGFR; the legend identifies these as in vitro kinase assays. auto_single_measurement only accepted activity measurement [1] 1 structures\8G63\8G63_metadata.json point structures/8G63/8g63_protein.pdb structures/8G63/8g63_pocket.pdb structures/8G63/8g63_ligand.sdf structures/8G63/8g63_ligand.pdb structures/8G63/8g63_ligand.cif structures/8G63/8g63_complex.pdb structures/8G63/8g63_complex.cif 8G6Z classic JAK2 Na JAK2 active kinase spanning residues 837-1132 with an N-terminal hexaHis tag Na Compound 13 "[""YSI""]" 1 IC50 IC50 = = 0.98 nM 0.98 [] unit_conversion 9.008773924307505 success True biochemical_inhibition In vitro kinase assay at 0.5 μM ATP; Table 1 reports JAK2 IC50 values averaged from assays performed at least twice. 3 Table 1 lists compound 13 with JAK2 IC50 = 0.98 nM; the table footnote states compounds were assayed at 0.5 μM ATP at least twice and IC50 values were averaged. auto_single_measurement only accepted activity measurement [1] 1 structures\8G6Z\8G6Z_metadata.json point structures/8G6Z/8g6z_protein.pdb structures/8G6Z/8g6z_pocket.pdb structures/8G6Z/8g6z_ligand.sdf structures/8G6Z/8g6z_ligand.pdb structures/8G6Z/8g6z_ligand.cif structures/8G6Z/8g6z_complex.pdb structures/8G6Z/8g6z_complex.cif 8G8N extended anti-CTLA-4 mAb XTX100 Fab Na Fab Na CPGKGLPSC "[""CHAIN:C"", ""CHAIN:F"", ""CHAIN:J"", ""CHAIN:P"", ""CHAIN:R"", ""CHAIN:Z""]" 1 Kd Kd = = 1.04E-06 M 1040.0 [] unit_conversion 5.982966660701219 success True direct_binding SPR with peptide flowed over immobilized XTX100 Fab at 37 °C. 8 Figure 1B reports KD 1.04E-06 M for CPGKGLPSC binding XTX100; the PDB antibody annotation identifies CPGKGLPSC as the 8G8N antigen sequence. auto_single_measurement only accepted activity measurement [1] 1 structures\8G8N\8G8N_metadata.json point structures/8G8N/8g8n_protein.pdb structures/8G8N/8g8n_pocket.pdb structures/8G8N/8g8n_ligand.pdb structures/8G8N/8g8n_ligand.cif structures/8G8N/8g8n_complex.pdb structures/8G8N/8g8n_complex.cif 8G8O classic JAK2 Na JAK2 active kinase spanning residues 837-1132 with an N-terminal hexaHis tag Na Compound 31 "[""YT0""]" 1 IC50 IC50 = = 3.9 nM 3.9 [] unit_conversion 8.4089353929735 success True biochemical_inhibition In vitro kinase assay at 0.5 μM ATP; Table 3 reports JAK2 IC50 values averaged from assays performed at least twice. 8 Table 3 lists compound 31 with JAK2 IC50 = 3.9 nM; the table footnote states compounds were assayed at 0.5 μM ATP at least twice and IC50 values were averaged. auto_single_measurement only accepted activity measurement [1] 1 structures\8G8O\8G8O_metadata.json point structures/8G8O/8g8o_protein.pdb structures/8G8O/8g8o_pocket.pdb structures/8G8O/8g8o_ligand.sdf structures/8G8O/8g8o_ligand.pdb structures/8G8O/8g8o_ligand.cif structures/8G8O/8g8o_complex.pdb structures/8G8O/8g8o_complex.cif 8G8X classic JAK2 Na JAK2 active kinase spanning residues 837-1132 with an N-terminal hexaHis tag Na Compound 27 "[""YT8""]" 1 IC50 IC50 = = 2.5 nM 2.5 [] unit_conversion 8.602059991327963 success True biochemical_inhibition In vitro kinase assay at 0.5 μM ATP; Table 3 reports JAK2 IC50 values averaged from assays performed at least twice. 8 Table 3 lists compound 27 with JAK2 IC50 = 2.5 nM; the table footnote states compounds were assayed at 0.5 μM ATP at least twice and IC50 values were averaged. auto_single_measurement only accepted activity measurement [1] 1 structures\8G8X\8G8X_metadata.json point structures/8G8X/8g8x_protein.pdb structures/8G8X/8g8x_pocket.pdb structures/8G8X/8g8x_ligand.sdf structures/8G8X/8g8x_ligand.pdb structures/8G8X/8g8x_ligand.cif structures/8G8X/8g8x_complex.pdb structures/8G8X/8g8x_complex.cif 8GA2 classic CBP Na CBP bromodomain residues 1081-1197 Na iCBP5 (compound 5) "[""YVK""]" 1 Kd Kd = = 31.4 ± 14.2 nM 31.4 [] unit_conversion 7.503070351926786 success True direct_binding Isothermal titration calorimetry (ITC); Table 1. 7 Table 1 identifies compound 5 as iCBP-5 and lists its CBP Kd as 31.4 ± 14.2 nM; the table notes this is a single ITC experiment fit ± SEM. auto_single_measurement only accepted activity measurement [1] 1 structures\8GA2\8GA2_metadata.json point structures/8GA2/8ga2_protein.pdb structures/8GA2/8ga2_pocket.pdb structures/8GA2/8ga2_ligand.sdf structures/8GA2/8ga2_ligand.pdb structures/8GA2/8ga2_ligand.cif structures/8GA2/8ga2_complex.pdb structures/8GA2/8ga2_complex.cif 8GAJ extended E. coli LptA Escherichia coli (LptA); Podisus maculiventris (thanatin) His6-SUMO-LptA-GSGGSGSG-AviTag; monomeric LptA construct lacking residues 1-27 and 159-185 Delta1-27 and Delta159-185 Podisus maculiventris thanatin "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 1.8 ± 0.2 nM 1.8 [] unit_conversion 8.744727494896694 success True direct_binding Bio-layer interferometry binding assay; steady-state 1:1 binding fit of thanatin to biotinylated E. coli LptA. 3 The steady-state binding association yielded KD = 1.8 ± 0.2 nM for P. maculiventris thanatin; Fig. 2C reports the BLI comparison. auto_single_measurement only accepted activity measurement [1] 1 structures\8GAJ\8GAJ_metadata.json point structures/8GAJ/8gaj_protein.pdb structures/8GAJ/8gaj_pocket.pdb structures/8GAJ/8gaj_ligand.pdb structures/8GAJ/8gaj_ligand.cif structures/8GAJ/8gaj_complex.pdb structures/8GAJ/8gaj_complex.cif 8GAK extended E. coli LptA Escherichia coli (LptA); Chinavia ubica (thanatin) His6-SUMO-LptA-GSGGSGSG-AviTag; monomeric LptA construct lacking residues 1-27 and 159-185 Delta1-27 and Delta159-185 Chinavia ubica thanatin "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.5 ± 0.1 nM 0.5 [] unit_conversion 9.301029995663981 success True direct_binding Bio-layer interferometry binding assay; steady-state 1:1 binding fit of thanatin to biotinylated E. coli LptA. 5 C. ubica thanatin has KD of 0.5 ± 0.1 nM; the paper identifies Fig. 2C as the BLI binding comparison. auto_single_measurement only accepted activity measurement [1] 1 structures\8GAK\8GAK_metadata.json point structures/8GAK/8gak_protein.pdb structures/8GAK/8gak_pocket.pdb structures/8GAK/8gak_ligand.pdb structures/8GAK/8gak_ligand.cif structures/8GAK/8gak_complex.pdb structures/8GAK/8gak_complex.cif 8GAL extended E. coli LptA Escherichia coli (LptA); Murgantia histrionica (thanatin) His6-SUMO-LptA-GSGGSGSG-AviTag; monomeric LptA construct lacking residues 1-27 and 159-185 Delta1-27 and Delta159-185 Murgantia histrionica thanatin "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.8 ± 0.1 nM 0.8 [] unit_conversion 9.096910013008056 success True direct_binding Bio-layer interferometry binding assay; steady-state 1:1 binding fit of thanatin to biotinylated E. coli LptA. 5 M. histrionica thanatin has KD of 0.8 ± 0.1 nM; the paper identifies Fig. 2C as the BLI binding comparison. auto_single_measurement only accepted activity measurement [1] 1 structures\8GAL\8GAL_metadata.json point structures/8GAL/8gal_protein.pdb structures/8GAL/8gal_pocket.pdb structures/8GAL/8gal_ligand.pdb structures/8GAL/8gal_ligand.cif structures/8GAL/8gal_complex.pdb structures/8GAL/8gal_complex.cif 8GB1 classic SAMHD1 Na Na Na 5a; deoxyguanosine-linked inhibitor "[""YWI""]" 1 Kd Kd = = 5.2 ± 1.2 µM 5200.0 [] unit_conversion 5.2839966563652006 success True direct_binding Competitive fluorescence-anisotropy probe-displacement assay using purified 5a; reported relative Kd. 5 “Purified 5a (Kd = 5.2 ± 1.2 µM) binds…” auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\8GB1\8GB1_metadata.json point structures/8GB1/8gb1_protein.pdb structures/8GB1/8gb1_pocket.pdb structures/8GB1/8gb1_ligand.sdf structures/8GB1/8gb1_ligand.pdb structures/8GB1/8gb1_ligand.cif structures/8GB1/8gb1_complex.pdb structures/8GB1/8gb1_complex.cif 8GC9 classic RNase A Na Na Na uridine 5'-heptaphosphate (p7U) "[""YWQ""]" 1 Ki Ki = = 1.0 ± 0.2 μM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition RNase A ribonucleolytic-inhibition assay using a FRET-tagged chimeric oligonucleotide substrate; 40 pM RNase A, 15 min incubation, n = 4 wells. 4 Figure 5B prints Ki = 1.0 ± 0.2 μM for p7U; Table 1 also lists p7U, Ki 1.0 ± 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8GC9\8GC9_metadata.json point structures/8GC9/8gc9_protein.pdb structures/8GC9/8gc9_pocket.pdb structures/8GC9/8gc9_ligand.sdf structures/8GC9/8gc9_ligand.pdb structures/8GC9/8gc9_ligand.cif structures/8GC9/8gc9_complex.pdb structures/8GC9/8gc9_complex.cif 8GD2 classic human cellular retinol binding protein 1 (CRBP1) human recombinant human CRBP1 with six additional C-terminal His residues Na N-methyl-1-{3-[1-(4-methylphenyl)cyclopentyl]-1,2,4-oxadiazol-5-yl}-N-(2-thienylmethyl)methanamine "[""Z5H""]" 1 Ki Ki = = 9.0 ± 4.1 µM 9000.0 [] unit_conversion 5.045757490560675 success True direct_binding Purified holo CRBP1/atROL fluorescence-replacement titration; apparent Ki fitted using a one-site saturation model with a nonspecific binding component. 4 Table 1 reports inhibitor 1 Ki = 9.0 ± 4.1 µM; the paper identifies inhibitor 1 as PDB 8GD2. auto_single_measurement only accepted activity measurement [1] 1 structures\8GD2\8GD2_metadata.json point structures/8GD2/8gd2_protein.pdb structures/8GD2/8gd2_pocket.pdb structures/8GD2/8gd2_ligand.sdf structures/8GD2/8gd2_ligand.pdb structures/8GD2/8gd2_ligand.cif structures/8GD2/8gd2_complex.pdb structures/8GD2/8gd2_complex.cif 8GDM classic human cellular retinol binding protein 1 (CRBP1) human recombinant human CRBP1 with six additional C-terminal His residues Na {[3-(diphenylmethyl)-1,2,4-oxadiazol-5-yl]methyl}(methyl)[1-(thiophen-2-yl)ethyl]amine "[""ZA6""]" 1 Ki Ki = = 10.6 ± 2.5 µM 10600.0 [] unit_conversion 4.97469413473523 success True direct_binding Purified holo CRBP1/atROL fluorescence-replacement titration; apparent Ki fitted using a one-site saturation model with a nonspecific binding component. 4 Table 1 reports the matching diphenylmethyl/thiophenyl inhibitor (inhibitor 5) Ki = 10.6 ± 2.5 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8GDM\8GDM_metadata.json point structures/8GDM/8gdm_protein.pdb structures/8GDM/8gdm_pocket.pdb structures/8GDM/8gdm_ligand.sdf structures/8GDM/8gdm_ligand.pdb structures/8GDM/8gdm_ligand.cif structures/8GDM/8gdm_complex.pdb structures/8GDM/8gdm_complex.cif 8GEM classic human cellular retinol binding protein 1 (CRBP1) human recombinant human CRBP1 with six additional C-terminal His residues Na N-ethyl-N-({3-[1-(4-methylphenyl)cyclopentyl]-1,2,4-oxadiazol-5-yl}methyl)-2-(1H-pyrazol-1-yl)ethanamine "[""ZDF""]" 1 Ki Ki = = 7.1 ± 2.7 µM 7100.0 [] unit_conversion 5.1487416512809245 success True direct_binding Purified holo CRBP1/atROL fluorescence-replacement titration; apparent Ki fitted using a one-site saturation model with a nonspecific binding component. 4 Table 1 reports inhibitor 2 Ki = 7.1 ± 2.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8GEM\8GEM_metadata.json point structures/8GEM/8gem_protein.pdb structures/8GEM/8gem_pocket.pdb structures/8GEM/8gem_ligand.sdf structures/8GEM/8gem_ligand.pdb structures/8GEM/8gem_ligand.cif structures/8GEM/8gem_complex.pdb structures/8GEM/8gem_complex.cif 8GEU classic human cellular retinol binding protein 1 (CRBP1) human recombinant human CRBP1 with six additional C-terminal His residues Na methyl({3-[1-(4-methylphenyl)cyclopentyl]-1,2,4-oxadiazol-5-yl}methyl)[(1-methylpyrazol-4-yl)methyl]amine "[""ZCF""]" 1 Ki Ki = = 10.7 ± 4.5 µM 10700.0 [] unit_conversion 4.97061622231479 success True direct_binding Purified holo CRBP1/atROL fluorescence-replacement titration; apparent Ki fitted using a one-site saturation model with a nonspecific binding component. 4 Table 1 reports the matching 1-methylpyrazolyl inhibitor (inhibitor 6) Ki = 10.7 ± 4.5 µM. Figure 3 identifies inhibitor 6 as PDB 8GEU. auto_single_measurement only accepted activity measurement [1] 1 structures\8GEU\8GEU_metadata.json point structures/8GEU/8geu_protein.pdb structures/8GEU/8geu_pocket.pdb structures/8GEU/8geu_ligand.sdf structures/8GEU/8geu_ligand.pdb structures/8GEU/8geu_ligand.cif structures/8GEU/8geu_complex.pdb structures/8GEU/8geu_complex.cif 8GEV classic human cellular retinol binding protein 1 (CRBP1) human recombinant human CRBP1 with six additional C-terminal His residues Na 1-{[3-(diphenylmethyl)-1,2,4-oxadiazol-5-yl]methyl}-4-(methoxymethyl)piperidine "[""ZDK""]" 1 Ki Ki = = 8.3 ± 2.8 µM 8300.0 [] unit_conversion 5.080921907623926 success True direct_binding Purified holo CRBP1/atROL fluorescence-replacement titration; apparent Ki fitted using a one-site saturation model with a nonspecific binding component. 4 Table 1 reports inhibitor 3 Ki = 8.3 ± 2.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8GEV\8GEV_metadata.json point structures/8GEV/8gev_protein.pdb structures/8GEV/8gev_pocket.pdb structures/8GEV/8gev_ligand.sdf structures/8GEV/8gev_ligand.pdb structures/8GEV/8gev_ligand.cif structures/8GEV/8gev_complex.pdb structures/8GEV/8gev_complex.cif 8GEY classic human cellular retinol binding protein 1 (CRBP1) human recombinant human CRBP1 with six additional C-terminal His residues Na 4-(hydroxymethyl)-1-[(4-methoxy-5,6,7,8-tetrahydronaphthalen-1-yl)sulfonyl]piperidin-4-ol "[""ZE2""]" 1 Ki Ki = = 9.5 ± 3.7 µM 9500.0 [] unit_conversion 5.022276394711152 success True direct_binding Purified holo CRBP1/atROL fluorescence-replacement titration; apparent Ki fitted using a one-site saturation model with a nonspecific binding component. 4 Table 1 reports inhibitor 4 Ki = 9.5 ± 3.7 µM. Figure 3 identifies inhibitor 4 as PDB 8GEY. auto_single_measurement only accepted activity measurement [1] 1 structures\8GEY\8GEY_metadata.json point structures/8GEY/8gey_protein.pdb structures/8GEY/8gey_pocket.pdb structures/8GEY/8gey_ligand.sdf structures/8GEY/8gey_ligand.pdb structures/8GEY/8gey_ligand.cif structures/8GEY/8gey_complex.pdb structures/8GEY/8gey_complex.cif 8GFR classic SARS-CoV-2 main protease SARS-CoV-2 truncated residues 1-304 C145A NBH2 "[""ZGO""]" 1 Kd Kd = = 2.3 ± 0.9 µM 2300.0 [] unit_conversion 5.638272163982407 success True direct_binding Isothermal titration calorimetry; Table 1, protein in buffer C at pH 7.2 and 28 °C. 4 Table 1 reports MProC145A + NBH2: Kd 2.3 ± 0.9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8GFR\8GFR_metadata.json point structures/8GFR/8gfr_protein.pdb structures/8GFR/8gfr_pocket.pdb structures/8GFR/8gfr_ligand.sdf structures/8GFR/8gfr_ligand.pdb structures/8GFR/8gfr_ligand.cif structures/8GFR/8gfr_complex.pdb structures/8GFR/8gfr_complex.cif 8GGG classic RNase A Na Na Na adenosine 5'-hexaphosphate (p6A) "[""ZF9""]" 1 Ki Ki = = 3.6 ± 0.6 μM 3600.0 [] unit_conversion 5.443697499232712 success True biochemical_inhibition RNase A inhibition assay; Table 1 reports inhibition constants for 5'-nucleoside oligophosphates. 3 Table 1 lists p6A with Ki = 3.6 ± 0.6 μM (this work). auto_single_measurement only accepted activity measurement [1] 1 structures\8GGG\8GGG_metadata.json point structures/8GGG/8ggg_protein.pdb structures/8GGG/8ggg_pocket.pdb structures/8GGG/8ggg_ligand.sdf structures/8GGG/8ggg_ligand.pdb structures/8GGG/8ggg_ligand.cif structures/8GGG/8ggg_complex.pdb structures/8GGG/8ggg_complex.cif 8GHE classic human arachidonate 12S-lipoxygenase (12-LOX) human full-length 12-LOX, residues G2 to I663 Na oleoyl-CoA "[""3VV""]" 1 IC50 IC50 = = 32 ± 4 μM 32000.0 [] unit_conversion 4.494850021680094 success True biochemical_inhibition Panel of long-chain fatty-acyl-CoAs tested for inhibition of 12-LOX catalysis; oleoyl-CoA was the most potent. 8 “The 12-LOX inhibition by acyl-CoAs depends on both their length and saturation status, with oleoyl-CoA (18:1) being the most potent inhibitor with an IC50 of 32 ± 4 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8GHE\8GHE_metadata.json point structures/8GHE/8ghe_protein.pdb structures/8GHE/8ghe_pocket.pdb structures/8GHE/8ghe_ligand.sdf structures/8GHE/8ghe_ligand.pdb structures/8GHE/8ghe_ligand.cif structures/8GHE/8ghe_complex.pdb structures/8GHE/8ghe_complex.cif 8GIA classic SARS-CoV-2 Nsp3 macrodomain (Macro1) SARS-CoV-2 (Covid-19) Na Na TFMU-ADPr "[""ZJ3""]" 1 IC50 IC50 = = 0.59 ± 0.05 µM 590.0 [] unit_conversion 6.229147988357855 success True direct_binding Fluorescence-polarization competitive binding assay using TAMRA-ADPr tracer; IC50 of TFMU-ADPr against SARS-CoV-2 Macro1. 4 Figure 4C lists the TFMU-ADPr IC50 for SARS Macro1 as 0.59 ± 0.05 µM; the text identifies the SARS-CoV-2 Macro1 IC50 as 0.59 µM and links the Macro1–TFMU-ADPr complex to PDB 8GIA. auto_single_measurement only accepted activity measurement [1] 1 structures\8GIA\8GIA_metadata.json point structures/8GIA/8gia_protein.pdb structures/8GIA/8gia_pocket.pdb structures/8GIA/8gia_ligand.sdf structures/8GIA/8gia_ligand.pdb structures/8GIA/8gia_ligand.cif structures/8GIA/8gia_complex.pdb structures/8GIA/8gia_complex.cif 8GJ5 extended afumPCNA Aspergillus fumigatus recombinant afumPCNA Na p21mu-afumRFC "[""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 94.84 ± 8.76 nM 94.84 [] unit_conversion 7.02300845469385 success True direct_binding SPR, candidate fungal peptide tested against afumPCNA in triplicate 10 Table 3 reports p21μafumRFC affinity against afumPCNA: KD 94.84 ± 8.76 nM; the text identifies the 8GJ5 co-crystal as afumPCNA bound to p21μ-afumRFC. auto_single_measurement only accepted activity measurement [1] 1 structures\8GJ5\8GJ5_metadata.json point structures/8GJ5/8gj5_protein.pdb structures/8GJ5/8gj5_pocket.pdb structures/8GJ5/8gj5_ligand.pdb structures/8GJ5/8gj5_ligand.cif structures/8GJ5/8gj5_complex.pdb structures/8GJ5/8gj5_complex.cif 8GJF extended afumPCNA Aspergillus fumigatus recombinant afumPCNA Na p21mu "[""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 265.1 ± 5.9 nM 265.1 [] unit_conversion 6.576590272266907 success True direct_binding SPR, p21 peptide library tested against afumPCNA 5 Table 1 reports p21μ affinity against afumPCNA: KD 265.1 ± 5.9 nM. The paper assigns PDB 8GJF to afumPCNA bound with p21μ. auto_single_measurement only accepted activity measurement [1] 1 structures\8GJF\8GJF_metadata.json point structures/8GJF/8gjf_protein.pdb structures/8GJF/8gjf_pocket.pdb structures/8GJF/8gjf_ligand.pdb structures/8GJF/8gjf_ligand.cif structures/8GJF/8gjf_complex.pdb structures/8GJF/8gjf_complex.cif 8GJG extended GCG binder Na Na Na GCG (glucagon peptide) "[""CHAIN:B""]" 1 Kd Kd = = 231 nM 231.0 [] unit_conversion 6.636388020107855 success True direct_binding Fluorescence-polarization titration (n=4) of the tightest inpainted GCG binder. 3 The text reports generation of “a 231-nM-affinity binder for GCG”; Extended Data Fig. 1 identifies the inpainted GCG binder as Kd = ~231 nM, measured by FP. auto_single_measurement only accepted activity measurement [1] 1 structures\8GJG\8GJG_metadata.json point structures/8GJG/8gjg_protein.pdb structures/8GJG/8gjg_pocket.pdb structures/8GJG/8gjg_ligand.pdb structures/8GJG/8gjg_ligand.cif structures/8GJG/8gjg_complex.pdb structures/8GJG/8gjg_complex.cif 8GJI extended GCG binder Na Na Na GCG (glucagon peptide) "[""CHAIN:B""]" 1 Kd Kd < < 500 pM 0.5 [] unit_conversion 9.301029995663981 success True direct_binding Fluorescence-polarization measurements (n=4) of the partially diffused GCG binder. 4 Fig. 2b states that FP measurements indicate “a subnanomolar binding affinity to GCG”; the plotted label gives GCG Kd < 500 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\8GJI\8GJI_metadata.json point structures/8GJI/8gji_protein.pdb structures/8GJI/8gji_pocket.pdb structures/8GJI/8gji_ligand.pdb structures/8GJI/8gji_ligand.cif structures/8GJI/8gji_complex.pdb structures/8GJI/8gji_complex.cif 8GK3 classic human cytochrome P450 3A7 (CYP3A7) human N-terminal transmembrane helix truncated; C-terminal six-residue histidine tag; hexamutant CYP3A7 K421A/K422A/K424A/R69G/C77G/K244E dehydroepiandrosterone 3-sulfate (DHEA-S) "[""ZWY""]" 1 Kd Kd = = 130 µM 130000.0 [] unit_conversion 3.886056647693163 success True direct_binding Purified recombinant hexamutant CYP3A7; DHEA-S titration monitored by CYP3A7 heme absorbance spectral shifts and fit to a one-site specific-binding equation. 3 Figure 1E reports DHEA-S ligand-binding Kd for the hexamutant as 130 µM (95% confidence interval 110–150 µM). auto_single_measurement only accepted activity measurement [1] 1 structures\8GK3\8GK3_metadata.json point structures/8GK3/8gk3_protein.pdb structures/8GK3/8gk3_pocket.pdb structures/8GK3/8gk3_ligand.sdf structures/8GK3/8gk3_ligand.pdb structures/8GK3/8gk3_ligand.cif structures/8GK3/8gk3_complex.pdb structures/8GK3/8gk3_complex.cif 8GMC classic Adaptor protein 2-associated kinase 1 (AAK1) Na Na Na Compound 2; 5-[(4-aminopiperidin-1-yl)methyl]-N-{3-[5-(propan-2-yl)-1,3,4-thiadiazol-2-yl]phenyl}pyrrolo[2,1-f][1,2,4]triazin-4-amine "[""YFV""]" 1 IC50 IC50 = = 57 (±9) nM 57.0 [] unit_conversion 7.2441251443275085 success True biochemical_inhibition AAK1 IC50; mean of two or more experiments, standard deviation in parentheses. 4 Table 1 reports Compound 2, AAK1 IC50 57 (±9) nM; Fig. 2 identifies PDB ID 8GMC as compound 2 bound to AAK1. auto_single_measurement only accepted activity measurement [1] 1 structures\8GMC\8GMC_metadata.json point structures/8GMC/8gmc_protein.pdb structures/8GMC/8gmc_pocket.pdb structures/8GMC/8gmc_ligand.sdf structures/8GMC/8gmc_ligand.pdb structures/8GMC/8gmc_ligand.cif structures/8GMC/8gmc_complex.pdb structures/8GMC/8gmc_complex.cif 8GMD classic Adaptor protein 2-associated kinase 1 (AAK1) Na Na Na Compound 30; (5P)-3-({(8R)-5-[(4-aminopiperidin-1-yl)methyl]pyrrolo[2,1-f][1,2,4]triazin-4-yl}amino)-5-[2-(propan-2-yl)-2H-tetrazol-5-yl]phenol "[""ZRR""]" 1 IC50 IC50 = = 3.8 (±1.1) nM 3.8 [] unit_conversion 8.42021640338319 success True biochemical_inhibition AAK1 IC50; mean of two or more experiments, standard deviation in parentheses. 5 Table 3 reports Compound 30, AAK1 IC50 3.8 (±1.1) nM; Fig. 3 identifies PDB ID 8GMD as compound 30 bound to AAK1. auto_single_measurement only accepted activity measurement [1] 1 structures\8GMD\8GMD_metadata.json point structures/8GMD/8gmd_protein.pdb structures/8GMD/8gmd_pocket.pdb structures/8GMD/8gmd_ligand.sdf structures/8GMD/8gmd_ligand.pdb structures/8GMD/8gmd_ligand.cif structures/8GMD/8gmd_complex.pdb structures/8GMD/8gmd_complex.cif 8GOD classic Human protein-arginine deiminase type-4 (PAD4) human Full-length hPAD4, amino acids 1-663, with an N-terminal hexahistidine tag Na JBI-589 "[""K3X""]" 1 IC50 IC50 = = 0.122 µM 122.0 [] unit_conversion 6.913640169325252 success True biochemical_inhibition Ammonia-release assay using recombinant full-length human PAD4; dose-dependent enzymatic inhibition by JBI-589. 2 “JBI-589 was screened against recombinant human PAD4 enzyme in ammonia release assay… with a half-maximum inhibitory concentration (IC50) of 0.122 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8GOD\8GOD_metadata.json point structures/8GOD/8god_protein.pdb structures/8GOD/8god_pocket.pdb structures/8GOD/8god_ligand.sdf structures/8GOD/8god_ligand.pdb structures/8GOD/8god_ligand.cif structures/8GOD/8god_complex.pdb structures/8GOD/8god_complex.cif 8GOM extended SARS-CoV-2 specific private TCR RLQ7 Na TCR alpha residues 1-206 and beta residues 1-245, with engineered interchain disulfide Na RLQ peptide (RLQSLQTYV) "[""CHAIN:C""]" 1 Kd Kd = = 49.0 µM 49000.0 [] unit_conversion 4.309803919971486 success True direct_binding Surface plasmon resonance measurement of RLQ7 binding to WT RLQ–HLA-A2. 2 “RLQ7 binds T1006I–HLA-A2 with a dissociation constant (KD) of 62.8 μM ... nearly identical to its KD for WT RLQ (49.0 μM).” Page 8 maps 8GOM to RLQ7–RLQ–HLA-A2. auto_single_measurement only accepted activity measurement [1] 1 structures\8GOM\8GOM_metadata.json point structures/8GOM/8gom_protein.pdb structures/8GOM/8gom_pocket.pdb structures/8GOM/8gom_ligand.pdb structures/8GOM/8gom_ligand.cif structures/8GOM/8gom_complex.pdb structures/8GOM/8gom_complex.cif 8GON extended SARS-CoV-2 specific private TCR RLQ7 Na TCR alpha residues 1-206 and beta residues 1-245, with engineered interchain disulfide T1006I in the RLQ peptide T1006I peptide (RLQSLQIYV) "[""CHAIN:C""]" 1 Kd Kd = = 62.8 µM 62800.0 [] unit_conversion 4.2020403562628035 success True direct_binding Surface plasmon resonance measurement of RLQ7 binding to T1006I–HLA-A2. 2 “RLQ7 binds T1006I–HLA-A2 with a dissociation constant (KD) of 62.8 μM.” Page 8 maps 8GON to RLQ7–T1006I–HLA-A2. auto_single_measurement only accepted activity measurement [1] 1 structures\8GON\8GON_metadata.json point structures/8GON/8gon_protein.pdb structures/8GON/8gon_pocket.pdb structures/8GON/8gon_ligand.pdb structures/8GON/8gon_ligand.cif structures/8GON/8gon_complex.pdb structures/8GON/8gon_complex.cif 8GSV extended human BAK (Bcl-2 antagonist/killer) human BAK residues 23-185; Pxt1 residues 76-101 BAK C166S human Pxt1 BH3 domain (residues 76-101) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 15.4 µM 15400.0 [] unit_conversion 4.812479279163537 success True direct_binding Isothermal titration calorimetry of recombinant BAK(23–185;C166S) with human Pxt1(76–101) peptide. 4 “their dissociation constant (K_D) was quantified as 15.4 μM (Fig 1D).” auto_single_measurement only accepted activity measurement [1] 1 structures\8GSV\8GSV_metadata.json point structures/8GSV/8gsv_protein.pdb structures/8GSV/8gsv_pocket.pdb structures/8GSV/8gsv_ligand.pdb structures/8GSV/8gsv_ligand.cif structures/8GSV/8gsv_complex.pdb structures/8GSV/8gsv_complex.cif 8GTV classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na JZD-07 "[""KAE""]" 2 Kd Kd = = 117 nM 117.0 [] unit_conversion 6.931814138253838 success True direct_binding Biolayer interferometry (BLI) binding analysis; JZD-07 is stated as the lead-compound comparator. 11 The BLI discussion states that JZD-07 has KD = 117 nM and koff = 0.028 s−1. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8GTV\8GTV_metadata.json point structures/8GTV/8gtv_protein.pdb structures/8GTV/8gtv_pocket.pdb structures/8GTV/8gtv_ligand.sdf structures/8GTV/8gtv_ligand.pdb structures/8GTV/8gtv_ligand.cif structures/8GTV/8gtv_complex.pdb structures/8GTV/8gtv_complex.cif 8GUE classic Cytochrome P450 PikC (CYP107L1) Streptomyces venezuelae ATCC 15439 PikC with p-acetyl-L-phenylalanine incorporated at position 238 His238 to p-acetyl-L-phenylalanine (H238pAcF) narbomycin (compound 5) "[""NRB""]" 1 Kd Kd = = 87.1 µM 87100.0 [] unit_conversion 4.059981844992337 success True direct_binding Purified-protein substrate-binding affinity determined by spectral changes during substrate titration. 4 “The affinity of PikC_H238pAcF to 5 also increased by 3.3-fold (K_D = 87.1 μM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8GUE\8GUE_metadata.json point structures/8GUE/8gue_protein.pdb structures/8GUE/8gue_pocket.pdb structures/8GUE/8gue_ligand.sdf structures/8GUE/8gue_ligand.pdb structures/8GUE/8gue_ligand.cif structures/8GUE/8gue_complex.pdb structures/8GUE/8gue_complex.cif 8GVJ classic c-Met human c-Met residues 1038-1346 with an N-terminal His-SUMO tag and Ulp1 protease cleavage site wild-type D6808 "[""KGL""]" 1 IC50 IC50 = = 2.9 nM 2.9 [] unit_conversion 8.537602002101044 success True biochemical_inhibition Biochemical c-Met kinase inhibition assay; 50 μM ATP. 10 Table 5 prints c-Met IC50 = 2.9 nM for compound 14 (D6808); the text identifies the D6808 c-Met cocrystal structure as PDB 8GVJ. auto_single_measurement only accepted activity measurement [1] 1 structures\8GVJ\8GVJ_metadata.json point structures/8GVJ/8gvj_protein.pdb structures/8GVJ/8gvj_pocket.pdb structures/8GVJ/8gvj_ligand.sdf structures/8GVJ/8gvj_ligand.pdb structures/8GVJ/8gvj_ligand.cif structures/8GVJ/8gvj_complex.pdb structures/8GVJ/8gvj_complex.cif 8GVZ classic human CAD protein dihydroorotase domain (huDHOase) human huDHOase residues 1456-1846 of human CAD protein with a C-terminal His tag Na 5-fluorouracil (5-FU) "[""URF""]" 1 Kd Kd = = 91.2 ± 1.7 µM 91200.0 [] unit_conversion 4.0400051616715835 success True direct_binding Fluorescence-quenching titration of purified huDHOase with 5-FU; Table 3 reports the Kd value. 10 Table 3 lists huDHOase with 5-FU: Kd Value 91.2 ± 1.7 µM. The preceding text identifies fluorescence quenching as the binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8GVZ\8GVZ_metadata.json point structures/8GVZ/8gvz_protein.pdb structures/8GVZ/8gvz_pocket.pdb structures/8GVZ/8gvz_ligand.sdf structures/8GVZ/8gvz_ligand.pdb structures/8GVZ/8gvz_ligand.cif structures/8GVZ/8gvz_complex.pdb structures/8GVZ/8gvz_complex.cif 8GW4 extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 residues 1-302 C145A peptide 8-1 (TSVKLQAEFRKM) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 6.03 µM 6030.0 [] unit_conversion 5.219682687859849 success True direct_binding Isothermal titration calorimetry (ITC) measurement of peptide 8-1 binding to Mpro C145A mutant. 2 The paper reports that peptide 8 had Kd 6.03 µM; the following text identifies peptide 8-1 as TSVKLQAEFRKM. Figure 2 identifies peptide 8-1 as the ligand in PDB 8GW4 with Mpro 1-302/C145A. auto_single_measurement only accepted activity measurement [1] 1 structures\8GW4\8GW4_metadata.json point structures/8GW4/8gw4_protein.pdb structures/8GW4/8gw4_pocket.pdb structures/8GW4/8gw4_ligand.pdb structures/8GW4/8gw4_ligand.cif structures/8GW4/8gw4_complex.pdb structures/8GW4/8gw4_complex.cif 8GWH extended PTPN21 Na PTP domain residues 872-1174 C1108S Src pY530 peptide "[""CHAIN:E""]" 1 Kd Kd = = 2.933 ± 0.988 µM 2933.0 [] unit_conversion 5.532687937019448 success True direct_binding MST binding-affinity measurement using fluorescent PTP C1108S-EGFP and increasing Src pY530 peptide. 4 Fig. 2D prints PTP C1108S-EGFP KD = 2.933 ± 0.988 µM for Src pY530 peptide; the caption identifies this as MST binding affinity measurement. auto_single_measurement only accepted activity measurement [1] 1 structures\8GWH\8GWH_metadata.json point structures/8GWH/8gwh_protein.pdb structures/8GWH/8gwh_pocket.pdb structures/8GWH/8gwh_ligand.pdb structures/8GWH/8gwh_ligand.cif structures/8GWH/8gwh_complex.pdb structures/8GWH/8gwh_complex.cif 8GWS extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 residues 1-302 C145A peptide 4 (VKLQAIFR) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 3.89 ± 0.58 µM 3890.0 [] unit_conversion 5.410050398674292 success True direct_binding Isothermal titration calorimetry (ITC) measurement of peptide 4 binding to Mpro C145A mutant. 3 Figure 1C reports peptide 4 (VKLQAIFR), Kd = 3.89 ± 0.58 µM; its caption states binding Kds were determined by ITC with SARS-CoV-2 Mpro C145A. Figure 2 maps peptide 4 to PDB 8GWS. auto_single_measurement only accepted activity measurement [1] 1 structures\8GWS\8GWS_metadata.json point structures/8GWS/8gws_protein.pdb structures/8GWS/8gws_pocket.pdb structures/8GWS/8gws_ligand.pdb structures/8GWS/8gws_ligand.cif structures/8GWS/8gws_complex.pdb structures/8GWS/8gws_complex.cif 8GY9 classic Alongshan virus methyltransferase Alongshan virus Methyltransferase residues E42-R313 Na S-adenosyl-L-methionine (SAM) "[""SAM""]" 1 Kd Kd = = 12.5 ± 3.6 μM 12500.0 [] unit_conversion 4.903089986991944 success True direct_binding ITC measurement of native ALSV MTase with SAM. 3 “The binding affinities for SAM and SAH were determined to be 12.5 ± 3.6 μM and 12.7 ± 3.9 μM, respectively.” Figure 1 identifies the native ALSV MTase/SAM ITC determination. auto_single_measurement only accepted activity measurement [1] 1 structures\8GY9\8GY9_metadata.json point structures/8GY9/8gy9_protein.pdb structures/8GY9/8gy9_pocket.pdb structures/8GY9/8gy9_ligand.sdf structures/8GY9/8gy9_ligand.pdb structures/8GY9/8gy9_ligand.cif structures/8GY9/8gy9_complex.pdb structures/8GY9/8gy9_complex.cif 8GYA classic Alongshan virus methyltransferase Alongshan virus Methyltransferase residues E42-R313 Na Sinefungin (SIN) "[""SFG""]" 1 Kd Kd = = 12.6 ± 2.8 μM 12600.0 [] unit_conversion 4.8996294548824375 success True direct_binding ITC measurement of ALSV MTase with sinefungin. 12 Figure 6B prints “Kd = 12.6 ± 2.8 μM” for “SIN to ALSV MTase”; the text identifies this as ITC binding of SIN to ALSV MTase. auto_single_measurement only accepted activity measurement [1] 1 structures\8GYA\8GYA_metadata.json point structures/8GYA/8gya_protein.pdb structures/8GYA/8gya_pocket.pdb structures/8GYA/8gya_ligand.sdf structures/8GYA/8gya_ligand.pdb structures/8GYA/8gya_ligand.cif structures/8GYA/8gya_complex.pdb structures/8GYA/8gya_complex.cif 8GYB classic Alongshan virus methyltransferase Alongshan virus Methyltransferase residues E42-R313 Na S-adenosyl-L-homocysteine (SAH) "[""SAH""]" 1 Kd Kd = = 12.7 ± 3.9 μM 12700.0 [] unit_conversion 4.896196279044043 success True direct_binding ITC measurement of native ALSV MTase with SAH. 3 “The binding affinities for SAM and SAH were determined to be 12.5 ± 3.6 μM and 12.7 ± 3.9 μM, respectively.” Figure 1 identifies the native ALSV MTase/SAH ITC determination. auto_single_measurement only accepted activity measurement [1] 1 structures\8GYB\8GYB_metadata.json point structures/8GYB/8gyb_protein.pdb structures/8GYB/8gyb_pocket.pdb structures/8GYB/8gyb_ligand.sdf structures/8GYB/8gyb_ligand.pdb structures/8GYB/8gyb_ligand.cif structures/8GYB/8gyb_complex.pdb structures/8GYB/8gyb_complex.cif 8GYD classic Schistosoma japonicum glutathione S-transferase (SjGST) Schistosoma japonicum Residues 1-218 with an N-terminal His-tag Na Compound 16 "[""0IH""]" 1 IC50 IC50 = = 1.55 ± 0.02 μM 1550.0 [] unit_conversion 5.809668301829708 success True biochemical_inhibition In vitro GST inhibition assay using CDNB as electrophilic substrate; Figure 7 reports mean of at least twice enzyme activity assays. 9 Figure 7 lists compound 16 with IC50 ± SD of 1.55 ± 0.02 μM against SjGST. The paper identifies the 16/SjGST cocrystal as PDB 8GYD. auto_single_measurement only accepted activity measurement [1] 1 structures\8GYD\8GYD_metadata.json point structures/8GYD/8gyd_protein.pdb structures/8GYD/8gyd_pocket.pdb structures/8GYD/8gyd_ligand.sdf structures/8GYD/8gyd_ligand.pdb structures/8GYD/8gyd_ligand.cif structures/8GYD/8gyd_complex.pdb structures/8GYD/8gyd_complex.cif 8H2J classic Acb2 Pseudomonas phage PaMx33 Full-length Acb2 expressed as a His6-SUMO fusion; tag-cleaved before purification Na 3',3'-cGAMP "[""4BW""]" 1 Kd Kd = = 87.0 ± 22.4 nM 87.0 [] unit_conversion 7.060480747381382 success True direct_binding Isothermal titration calorimetry (ITC) of purified Acb2 with cyclic dinucleotides. 31 Figure 3C reports Acb2 binding to 3',3'-cGAMP with KD 87.0 ± 22.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8H2J\8H2J_metadata.json point structures/8H2J/8h2j_protein.pdb structures/8H2J/8h2j_pocket.pdb structures/8H2J/8h2j_ligand.sdf structures/8H2J/8h2j_ligand.pdb structures/8H2J/8h2j_ligand.cif structures/8H2J/8h2j_complex.pdb structures/8H2J/8h2j_complex.cif 8H2T classic IadD/E dioxygenase complex Variovorax paradoxus Na Na IAA "[""IAC""]" 1 Kd Kd = = 16.6 ± 3.1 μM 16600.0 [] unit_conversion 4.779891911959945 success True direct_binding ITC measurement of IAA binding to the IadD/E complex; mean ± SEM from 3 or more independent measurements. 7 Fig. 3A reports an ITC Kd of 16.6 ± 3.1 μM for IadD/E + IAA. auto_single_measurement only accepted activity measurement [1] 1 structures\8H2T\8H2T_metadata.json point structures/8H2T/8h2t_protein.pdb structures/8H2T/8h2t_pocket.pdb structures/8H2T/8h2t_ligand.sdf structures/8H2T/8h2t_ligand.pdb structures/8H2T/8h2t_ligand.cif structures/8H2T/8h2t_complex.pdb structures/8H2T/8h2t_complex.cif 8H39 classic Acb2 Pseudomonas phage PaMx33 Full-length Acb2 expressed as a His6-SUMO fusion; tag-cleaved before purification Na c-di-AMP "[""2BA""]" 1 Kd Kd = = 66.1 ± 18.3 nM 66.1 [] unit_conversion 7.17979854051436 success True direct_binding Isothermal titration calorimetry (ITC) of purified Acb2 with cyclic dinucleotides. 31 Figure 3C reports Acb2 binding to c-di-AMP with KD 66.1 ± 18.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8H39\8H39_metadata.json point structures/8H39/8h39_protein.pdb structures/8H39/8h39_pocket.pdb structures/8H39/8h39_ligand.sdf structures/8H39/8h39_ligand.pdb structures/8H39/8h39_ligand.cif structures/8H39/8h39_complex.pdb structures/8H39/8h39_complex.cif 8H3C extended antibody scFv Na scFv Na M2e influenza peptide; extended U1 peptide epitope "[""CHAIN:F"", ""CHAIN:G""]" 1 Kd Kd = = 9.4×10⁻7 M 940.0 [] unit_conversion 6.026872146400301 success True direct_binding Bio-layer interferometry of purified AU1 scFv binding the U1 peptide. 8 Fig. 3C prints K_D = 9.4×10⁻7 for AU1; page 9 identifies the crystallized complex as scFv AU1 with the extended U1 peptide, and page 13 assigns the scFv–M2e peptide complex to PDB 8H3C. auto_single_measurement only accepted activity measurement [1] 1 structures\8H3C\8H3C_metadata.json point structures/8H3C/8h3c_protein.pdb structures/8H3C/8h3c_pocket.pdb structures/8H3C/8h3c_ligand.pdb structures/8H3C/8h3c_ligand.cif structures/8H3C/8h3c_complex.pdb structures/8H3C/8h3c_complex.cif 8H3E classic SARS-CoV-2 spike protein SARS-CoV-2 S-Trimer fusion protein containing the spike protein ectodomain (residues 1-1211), fused to T4 fibritin trimerization domain, 8x histidine tag, and Protein C tag R682S; R683G; R685G; K986P; V987P SPC-14 "[""Q83""]" 1 Kd Kd = = 9.5 µM 9500.0 [] unit_conversion 5.022276394711152 success True direct_binding Surface plasmon resonance binding assay of SPC-14 to trimeric prototypic SARS-CoV-2 spike protein at 25 °C. 5 Table 1 reports SPC-14 K_D = 9.5 µM; its footnote states that, unless otherwise noted, K_D values are against prototypic SARS-CoV-2 spike protein. The SPR method is described on PDF page 8, and the prototypic spike construct with R682S/R683G/R685G/K986P/V987P is specified there. auto_single_measurement only accepted activity measurement [1] 1 structures\8H3E\8H3E_metadata.json point structures/8H3E/8h3e_protein.pdb structures/8H3E/8h3e_pocket.pdb structures/8H3E/8h3e_ligand.sdf structures/8H3E/8h3e_ligand.pdb structures/8H3E/8h3e_ligand.cif structures/8H3E/8h3e_complex.pdb structures/8H3E/8h3e_complex.cif 8H59 classic Mps1 Magnaporthe oryzae Na Na A378-0 "[""KR9""]" 1 Kd Kd = = 69.2 μM 69200.0 [] unit_conversion 4.1598939055432425 success True direct_binding In vitro surface plasmon resonance (SPR) measurement of synthesized A378-0 binding to recombinant Mps1. 3 “SPR assays showed that the in vitro binding affinity (represented by the dissociation equilibrium constant [K_D]) between A378-0 and Mps1 is 69.2 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8H59\8H59_metadata.json point structures/8H59/8h59_protein.pdb structures/8H59/8h59_pocket.pdb structures/8H59/8h59_ligand.sdf structures/8H59/8h59_ligand.pdb structures/8H59/8h59_ligand.cif structures/8H59/8h59_complex.pdb structures/8H59/8h59_complex.cif 8H5A classic YhaJ transcription factor Escherichia coli YhaJ effector-binding domain, residues 96-298 Na methylhydroquinone (MHQ) "[""7DV""]" 1 Kd Kd = = 11.0 ± 3.7 mM 11000000.0 [] unit_conversion 1.9586073148417746 success True direct_binding Microscale thermophoresis measurement of purified YhaJ-EBD binding to MHQ. 8 Table 2 reports the WT YhaJ-EBD dissociation constant for MHQ as 11.0 ± 3.7 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8H5A\8H5A_metadata.json point structures/8H5A/8h5a_protein.pdb structures/8H5A/8h5a_pocket.pdb structures/8H5A/8h5a_ligand.sdf structures/8H5A/8h5a_ligand.pdb structures/8H5A/8h5a_ligand.cif structures/8H5A/8h5a_complex.pdb structures/8H5A/8h5a_complex.cif 8H6P classic CDK2/Cyclin E1 Na Na Na compound 19 "[""WZU""]" 1 IC50 IC50 = = 0.090 nM 0.09 [] unit_conversion 10.045757490560675 success True biochemical_inhibition CDK2/E1 enzymatic IC50 reported in Table 2. 4 Table 2 lists compound 19 with CDK2/E1 IC50 = 0.090 nM; the text identifies compound 19 as the starting molecule and Figure 4 maps its CDK2/Cyclin E1 cocrystal to PDB 8H6P. auto_single_measurement only accepted activity measurement [1] 1 structures\8H6P\8H6P_metadata.json point structures/8H6P/8h6p_protein.pdb structures/8H6P/8h6p_pocket.pdb structures/8H6P/8h6p_ligand.sdf structures/8H6P/8h6p_ligand.pdb structures/8H6P/8h6p_ligand.cif structures/8H6P/8h6p_complex.pdb structures/8H6P/8h6p_complex.cif 8H6T classic CDK2/Cyclin E1 Na Na Na compound 13 "[""WZZ""]" 1 IC50 IC50 = = 0.0081 µM 8.1 [] unit_conversion 8.09151498112135 success True biochemical_inhibition CDK2/E1 enzymatic IC50 reported in Table 1. 2 Table 1 lists compound 13 with CDK2/E1 IC50 = 0.0081 µM; Figure 2 identifies the compound 13 CDK2/Cyclin E1 cocrystal as PDB 8H6T. auto_single_measurement only accepted activity measurement [1] 1 structures\8H6T\8H6T_metadata.json point structures/8H6T/8h6t_protein.pdb structures/8H6T/8h6t_pocket.pdb structures/8H6T/8h6t_ligand.sdf structures/8H6T/8h6t_ligand.pdb structures/8H6T/8h6t_ligand.cif structures/8H6T/8h6t_complex.pdb structures/8H6T/8h6t_complex.cif 8H7I classic nanobody 11A Na Na Na quinalphos "[""WYN""]" 2 Kd Kd = = 14.3±0.4 nM 14.3 [] unit_conversion 7.844663962534938 success True direct_binding ITC measurement of Nb-11A/pesticide binding. 6 “The KD for Nb-11A binding to quinalphos… [was] 14.3±0.4 nM.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8H7I\8H7I_metadata.json point structures/8H7I/8h7i_protein.pdb structures/8H7I/8h7i_pocket.pdb structures/8H7I/8h7i_ligand.sdf structures/8H7I/8h7i_ligand.pdb structures/8H7I/8h7i_ligand.cif structures/8H7I/8h7i_complex.pdb structures/8H7I/8h7i_complex.cif 8H7M classic nanobody 11A Na Na Na parathion "[""WYS""]" 2 Kd Kd = = 16.7±0.7 nM 16.7 [] unit_conversion 7.777283528852417 success True direct_binding ITC measurement of Nb-11A/pesticide binding. 6 “The KD for Nb-11A binding to… parathion… [was] 16.7±0.7 nM.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8H7M\8H7M_metadata.json point structures/8H7M/8h7m_protein.pdb structures/8H7M/8h7m_pocket.pdb structures/8H7M/8h7m_ligand.sdf structures/8H7M/8h7m_ligand.pdb structures/8H7M/8h7m_ligand.cif structures/8H7M/8h7m_complex.pdb structures/8H7M/8h7m_complex.cif 8H7N classic nanobody 11A Na Na Na triazophos "[""WYW""]" 2 Kd Kd = = 11.1±0.5 nM 11.1 [] unit_conversion 7.954677021213342 success True direct_binding ITC measurement of Nb-11A/pesticide binding. 6 “The KD for Nb-11A binding to… triazophos [was] 11.1±0.5 nM.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8H7N\8H7N_metadata.json point structures/8H7N/8h7n_protein.pdb structures/8H7N/8h7n_pocket.pdb structures/8H7N/8h7n_ligand.sdf structures/8H7N/8h7n_ligand.pdb structures/8H7N/8h7n_ligand.cif structures/8H7N/8h7n_complex.pdb structures/8H7N/8h7n_complex.cif 8H7R classic nanobody 11A Na Na Na coumaphos "[""WZ0""]" 2 Kd Kd = = 174.0±1.3 nM 174.0 [] unit_conversion 6.7594507517174005 success True direct_binding ITC measurement of Nb-11A/pesticide binding. 6 “The KD for Nb-11A binding to coumaphos [was] 174.0±1.3 nM.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8H7R\8H7R_metadata.json point structures/8H7R/8h7r_protein.pdb structures/8H7R/8h7r_pocket.pdb structures/8H7R/8h7r_ligand.sdf structures/8H7R/8h7r_ligand.pdb structures/8H7R/8h7r_ligand.cif structures/8H7R/8h7r_complex.pdb structures/8H7R/8h7r_complex.cif 8HCK classic MDA-9 PDZ1 domain Na MDA-9 PDZ1 domain, residues 113-192 Na PI1B "[""P1Z""]" 1 Kd Kd = = 0.34 mM 340000.0 [] unit_conversion 3.4685210829577446 success True direct_binding NMR chemical-shift-perturbation titration of MDA-9 PDZ1 with PI1B. 2 “PI1A and PI1B bound to the MDA-9 PDZ1 domain with an affinity of 0.11 and 0.34 mM, respectively, determined from the dose-dependent CSPs.” The PI1B–PDZ1 crystal structure is identified as PDB ID 8HCK. auto_single_measurement only accepted activity measurement [1] 1 structures\8HCK\8HCK_metadata.json point structures/8HCK/8hck_protein.pdb structures/8HCK/8hck_pocket.pdb structures/8HCK/8hck_ligand.sdf structures/8HCK/8hck_ligand.pdb structures/8HCK/8hck_ligand.cif structures/8HCK/8hck_complex.pdb structures/8HCK/8hck_complex.cif 8HE1 classic Pst_13661 Puccinia striiformis f. sp. tritici Na Na BHA (benzo-hydroxamic acid) "[""BHO""]" 1 Ki Ki = = 9.83 μM 9830.0 [] unit_conversion 5.007446482167865 success True biochemical_inhibition Recombinant-enzyme inhibition assay; Ki determined using Dixon plots. 6 Table 2 reports Pst_13661 Ki = 9.83 μM for compound 1 (BHA); the structure-determination text assigns Pst_13661-BHA to PDB 8HE1. auto_single_measurement only accepted activity measurement [1] 1 structures\8HE1\8HE1_metadata.json point structures/8HE1/8he1_protein.pdb structures/8HE1/8he1_pocket.pdb structures/8HE1/8he1_ligand.sdf structures/8HE1/8he1_ligand.pdb structures/8HE1/8he1_ligand.cif structures/8HE1/8he1_complex.pdb structures/8HE1/8he1_complex.cif 8HE2 classic Pst_13661 Puccinia striiformis f. sp. tritici Na Na compound 2 "[""LMI""]" 1 Ki Ki = = 10.75 μM 10750.0 [] unit_conversion 4.968591535748375 success True biochemical_inhibition Recombinant-enzyme inhibition assay; Ki determined using Dixon plots. 6 Table 2 reports Pst_13661 Ki = 10.75 μM for compound 2; the structure-determination text assigns the Pst_13661-compound 2 complex to PDB 8HE2. auto_single_measurement only accepted activity measurement [1] 1 structures\8HE2\8HE2_metadata.json point structures/8HE2/8he2_protein.pdb structures/8HE2/8he2_pocket.pdb structures/8HE2/8he2_ligand.sdf structures/8HE2/8he2_ligand.pdb structures/8HE2/8he2_ligand.cif structures/8HE2/8he2_complex.pdb structures/8HE2/8he2_complex.cif 8HE4 classic Pst_13661 Puccinia striiformis f. sp. tritici Na Na compound 3 "[""8GK""]" 1 Ki Ki = = 27.58 μM 27580.0 [] unit_conversion 4.559405738160169 success True biochemical_inhibition Recombinant-enzyme inhibition assay; Ki determined using Dixon plots. 6 Table 2 reports Pst_13661 Ki = 27.58 μM for compound 3; the structure-determination text assigns the Pst_13661-compound 3 complex to PDB 8HE4. auto_single_measurement only accepted activity measurement [1] 1 structures\8HE4\8HE4_metadata.json point structures/8HE4/8he4_protein.pdb structures/8HE4/8he4_pocket.pdb structures/8HE4/8he4_ligand.sdf structures/8HE4/8he4_ligand.pdb structures/8HE4/8he4_ligand.cif structures/8HE4/8he4_complex.pdb structures/8HE4/8he4_complex.cif 8HE7 classic ADP-ribosyltransferase 1 (PARP-1) Na PARP-1 catalytic domain (catPARP-1) Na Cpd36 "[""1WI""]" 2 Kd Kd = = 0.83 nM 0.83 [] unit_conversion 9.080921907623926 success True direct_binding Surface plasmon resonance binding-kinetic assay using catPARP-1. 8 Table 4 reports Cpd36 KD = 0.83 nM for catPARP-1; the text identifies this as an SPR assay. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8HE7\8HE7_metadata.json point structures/8HE7/8he7_protein.pdb structures/8HE7/8he7_pocket.pdb structures/8HE7/8he7_ligand.sdf structures/8HE7/8he7_ligand.pdb structures/8HE7/8he7_ligand.cif structures/8HE7/8he7_complex.pdb structures/8HE7/8he7_complex.cif 8HE8 classic ADP-ribosyltransferase 2 (PARP-2) human PARP-2 catalytic domain, catPARP-2SE 349TEKQSP354 -> 349SERQGL354 Cpd36 "[""1WI""]" 1 Kd Kd = = 0.75 nM 0.75 [] unit_conversion 9.1249387366083 success True direct_binding Surface plasmon resonance binding-kinetic assay using catPARP-2. 8 Table 4 reports Cpd36 KD = 0.75 nM for catPARP-2; the text identifies this as an SPR assay. The paper's crystallography methods specify the mutated catPARP-2 construct used for 8HE8. auto_single_measurement only accepted activity measurement [1] 1 structures\8HE8\8HE8_metadata.json point structures/8HE8/8he8_protein.pdb structures/8HE8/8he8_pocket.pdb structures/8HE8/8he8_ligand.sdf structures/8HE8/8he8_ligand.pdb structures/8HE8/8he8_ligand.cif structures/8HE8/8he8_complex.pdb structures/8HE8/8he8_complex.cif 8HE9 classic CTSB human Residues 18-333; codon-optimized pET28a expression construct Na K777 "[""DMS""]" 1 IC50 IC50 = = 244.26 ± 20.94 nM 244.26 [] unit_conversion 6.612147647236957 success True biochemical_inhibition Purified-protein fluorogenic enzymatic inhibition assay. 2 Figure 1i reports CTSB IC50 244.26 ± 20.94 nM for K777. auto_single_measurement only accepted activity measurement [1] 1 structures\8HE9\8HE9_metadata.json point structures/8HE9/8he9_protein.pdb structures/8HE9/8he9_pocket.pdb structures/8HE9/8he9_ligand.sdf structures/8HE9/8he9_ligand.pdb structures/8HE9/8he9_ligand.cif structures/8HE9/8he9_complex.pdb structures/8HE9/8he9_complex.cif 8HEF classic SARS-CoV-2 3CLpro (main protease/Mpro) SARS-CoV-2 3CLpro residues 1-306 with an N-terminal 6xHis tag and TEV cleavage site Na YY-278 (C11-d2-S-217622; deuterated S-217622/Ensitrelvir) "[""7YY""]" 1 IC50 IC50 = = 9 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition FRET enzymatic inhibition assay using full-length SARS-CoV-2 3CLpro and a fluorogenic 10-peptide substrate. 6 Table 1 reports YY-278 with SARS-CoV-2 3CLpro IC50 of 9 nM; the text describes the FRET full-length 3CLpro assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8HEF\8HEF_metadata.json point structures/8HEF/8hef_protein.pdb structures/8HEF/8hef_pocket.pdb structures/8HEF/8hef_ligand.sdf structures/8HEF/8hef_ligand.pdb structures/8HEF/8hef_ligand.cif structures/8HEF/8hef_complex.pdb structures/8HEF/8hef_complex.cif 8HEN classic CTSB human Residues 18-333; codon-optimized pET28a expression construct Na 212-148 "[""DMS""]" 1 IC50 IC50 = = 64.07 ± 3.72 nM 64.07 [] unit_conversion 7.19334527600814 success True biochemical_inhibition Purified-protein fluorogenic enzymatic inhibition assay. 7 Figure 5c reports CTSB IC50 64.07 ± 3.72 nM for 212-148. auto_single_measurement only accepted activity measurement [1] 1 structures\8HEN\8HEN_metadata.json point structures/8HEN/8hen_protein.pdb structures/8HEN/8hen_pocket.pdb structures/8HEN/8hen_ligand.sdf structures/8HEN/8hen_ligand.pdb structures/8HEN/8hen_ligand.cif structures/8HEN/8hen_complex.pdb structures/8HEN/8hen_complex.cif 8HFV classic CTSL human Residues 18-333; codon-optimized pET28a expression construct Na K777 "[""CAC""]" 1 IC50 IC50 = = 88.85 ± 2.57 nM 88.85 [] unit_conversion 7.051342567858679 success True biochemical_inhibition Purified-protein fluorogenic enzymatic inhibition assay. 2 Figure 1h reports CTSL IC50 88.85 ± 2.57 nM for K777. auto_single_measurement only accepted activity measurement [1] 1 structures\8HFV\8HFV_metadata.json point structures/8HFV/8hfv_protein.pdb structures/8HFV/8hfv_pocket.pdb structures/8HFV/8hfv_ligand.sdf structures/8HFV/8hfv_ligand.pdb structures/8HFV/8hfv_ligand.cif structures/8HFV/8hfv_complex.pdb structures/8HFV/8hfv_complex.cif 8HI9 classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na Robinetin "[""LKR""]" 1 IC50 IC50 = = 0.96 µM 960.0 [] unit_conversion 6.017728766960431 success True biochemical_inhibition Purified recombinant SARS-CoV-2 Mpro FRET protease inhibition assay using fluorogenic substrate Dacyl-KTSAVLQSGFRKME-Edans; initial velocities used for IC50 determination. 6 Table 1 reports Robinetin, 86.13% inhibition at 10 µM and IC50 0.96 µM. The paper identifies the Robinetin complex as PDB 8HI9 (pages 10 and 20). auto_single_measurement only accepted activity measurement [1] 1 structures\8HI9\8HI9_metadata.json point structures/8HI9/8hi9_protein.pdb structures/8HI9/8hi9_pocket.pdb structures/8HI9/8hi9_ligand.sdf structures/8HI9/8hi9_ligand.pdb structures/8HI9/8hi9_ligand.cif structures/8HI9/8hi9_complex.pdb structures/8HI9/8hi9_complex.cif 8HJA classic Syn_CdgR Synechocystis sp. PCC 6803 Na Na c-di-GMP "[""C2E""]" 1 Kd Kd = = 1.68 ± 0.468 µM 1680.0 [] unit_conversion 5.774690718274137 success True direct_binding LSR analysis of Syn_CdgR binding to c-di-GMP. 2 “LSR analysis showed that c-di-GMP binds to Syn_CdgR with a Kd of 1.68 ± 0.468 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8HJA\8HJA_metadata.json point structures/8HJA/8hja_protein.pdb structures/8HJA/8hja_pocket.pdb structures/8HJA/8hja_ligand.sdf structures/8HJA/8hja_ligand.pdb structures/8HJA/8hja_ligand.cif structures/8HJA/8hja_complex.pdb structures/8HJA/8hja_complex.cif 8HKS classic ADP-ribosyltransferase 2 (PARP2) human catPARP-2 catalytic-domain fragment covering residues 231-581 of Q9UGN5 catPARP-2SE: T349S, L351R, S353G, P354L (349TELQSP354 -> 349SERQGL354) Pamiparib (BGB-290) "[""DS9""]" 1 Kd Kd = = 1.3 nM 1.3 [] unit_conversion 8.886056647693163 success True direct_binding Fluorescence-polarization assay; Kd reported toward catPARP-2SE. 3 “the Kd values were determined to be 1.5/1.3 nM ... toward catPARP-1/catPARP-2SE for BGB290” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8HKS\8HKS_metadata.json point structures/8HKS/8hks_protein.pdb structures/8HKS/8hks_pocket.pdb structures/8HKS/8hks_ligand.sdf structures/8HKS/8hks_ligand.pdb structures/8HKS/8hks_ligand.cif structures/8HKS/8hks_complex.pdb structures/8HKS/8hks_complex.cif 8HLO extended ASAP1-SH3; MICAL1-PRM mouse (ASAP1); human (MICAL1) ASAP1-SH3 residues 1087-1147; MICAL1-PRM residues 828-842 Na MICAL1-PRM (residues 828-842) "[""CHAIN:C""]" 1 Kd Kd = = 0.8 ± 0.03 μM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding ITC-based affinity measurement of ASAP1-SH3 with MICAL1-PRM (Figure 1E). 3 Figure 1E reports ITC binding of ASAP1-SH3 and MICAL1-PRM with Kd = 0.8 ± 0.03 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8HLO\8HLO_metadata.json point structures/8HLO/8hlo_protein.pdb structures/8HLO/8hlo_pocket.pdb structures/8HLO/8hlo_ligand.pdb structures/8HLO/8hlo_ligand.cif structures/8HLO/8hlo_complex.pdb structures/8HLO/8hlo_complex.cif 8HOG classic BCL2 human BCL2 residues 6-207, with residues 35-91 replaced by residues 33-48 of BCL-xL wild-type sonrotoclax "[""98I""]" 1 Kd Kd = = 0.046 ± 0.015 nM 0.046 [] unit_conversion 10.337242168318426 success True direct_binding SPR binding of sonrotoclax to immobilized His-tagged BCL2; Kd fit to a 1:1 binding model. 2 “the K_D of sonrotoclax to BCL2 was 0.046 nM” and Figure 1 reports K_D = 0.046 ± 0.015 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8HOG\8HOG_metadata.json point structures/8HOG/8hog_protein.pdb structures/8HOG/8hog_pocket.pdb structures/8HOG/8hog_ligand.sdf structures/8HOG/8hog_ligand.pdb structures/8HOG/8hog_ligand.cif structures/8HOG/8hog_complex.pdb structures/8HOG/8hog_complex.cif 8HOH classic BCL2 human BCL2 residues 6-207, with residues 35-91 replaced by residues 33-48 of BCL-xL G101V sonrotoclax "[""98I""]" 1 Kd Kd = = 0.24 ± 0.081 nM 0.24 [] unit_conversion 9.619788758288394 success True direct_binding SPR binding of sonrotoclax to BCL2 G101V. 7 Figure 4A reports K_D = 0.24 ± 0.081 nM for sonrotoclax binding to the BCL2 G101V mutant. auto_single_measurement only accepted activity measurement [1] 1 structures\8HOH\8HOH_metadata.json point structures/8HOH/8hoh_protein.pdb structures/8HOH/8hoh_pocket.pdb structures/8HOH/8hoh_ligand.sdf structures/8HOH/8hoh_ligand.pdb structures/8HOH/8hoh_ligand.cif structures/8HOH/8hoh_complex.pdb structures/8HOH/8hoh_complex.cif 8HOI classic BCL2 human BCL2 residues 6-207, with residues 35-91 replaced by residues 33-48 of BCL-xL D103Y sonrotoclax "[""98I""]" 1 Kd Kd = = 0.52 ± 0.14 nM 0.52 [] unit_conversion 9.2839966563652 success True direct_binding SPR binding of sonrotoclax to the BCL2 D103Y variant. 9 Figure 6A reports K_D = 0.52 ± 0.14 nM for sonrotoclax binding to D103Y. auto_single_measurement only accepted activity measurement [1] 1 structures\8HOI\8HOI_metadata.json point structures/8HOI/8hoi_protein.pdb structures/8HOI/8hoi_pocket.pdb structures/8HOI/8hoi_ligand.sdf structures/8HOI/8hoi_ligand.pdb structures/8HOI/8hoi_ligand.cif structures/8HOI/8hoi_complex.pdb structures/8HOI/8hoi_complex.cif 8HOM classic SARS-CoV-2 Omicron Main Protease (Mpro) Na Na P132H ensitrelvir "[""7YY""]" 1 IC50 IC50 = = 0.048 ± 0.001 µM 48.0 [] unit_conversion 7.318758762624412 success True biochemical_inhibition FRET-based in vitro enzyme-inhibition assay; Fig. 3a. 4 Fig. 3a prints P132H IC50 = 0.048 ± 0.001 µM for ensitrelvir; page 6 maps 8HOM to P132H-ensitrelvir. auto_single_measurement only accepted activity measurement [1] 1 structures\8HOM\8HOM_metadata.json point structures/8HOM/8hom_protein.pdb structures/8HOM/8hom_pocket.pdb structures/8HOM/8hom_ligand.sdf structures/8HOM/8hom_ligand.pdb structures/8HOM/8hom_ligand.cif structures/8HOM/8hom_complex.pdb structures/8HOM/8hom_complex.cif 8HOQ extended P450 BM3 Bacillus megaterium heme domain F87A Im-C6-Phe(4CF3)-Tyr "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 1.4×10−8 M 14.0 [] unit_conversion 7.853871964321762 success True direct_binding Absorption spectral titration of the P450BM3 F87A heme domain with Im-DFSM-dipeps. 5 “Im-C6-Phe(4CF3)-Tyr exhibited the strongest affinity for P450BM3 (Kd=1.4×10−8 M).” Figure 2 maps this ligand to PDB 8HOQ. auto_single_measurement only accepted activity measurement [1] 1 structures\8HOQ\8HOQ_metadata.json point structures/8HOQ/8hoq_protein.pdb structures/8HOQ/8hoq_pocket.pdb structures/8HOQ/8hoq_ligand.pdb structures/8HOQ/8hoq_ligand.cif structures/8HOQ/8hoq_complex.pdb structures/8HOQ/8hoq_complex.cif 8HQQ classic SAR11_0769 Candidatus Pelagibacter ubique HTCC1062 Signal sequence removed; N-terminal His6 and thrombin tags Na D-glucose "[""BGC""]" 1 Kd Kd = = 238 nM 238.0 [] unit_conversion 6.623423042943488 success True direct_binding ITC-confirmed SAR11_0769–D-glucose interaction; value printed in Fig. 2. 4 Fig. 2 labels the SAR11_0769 glucose interaction as “238 nM”; its legend states labelled protein–ligand interactions were verified by ITC and labels give measured Kd. auto_single_measurement only accepted activity measurement [1] 1 structures\8HQQ\8HQQ_metadata.json point structures/8HQQ/8hqq_protein.pdb structures/8HQQ/8hqq_pocket.pdb structures/8HQQ/8hqq_ligand.sdf structures/8HQQ/8hqq_ligand.pdb structures/8HQQ/8hqq_ligand.cif structures/8HQQ/8hqq_complex.pdb structures/8HQQ/8hqq_complex.cif 8HQR classic SAR11_1210 Candidatus Pelagibacter ubique HTCC1062 Signal sequence removed; N-terminal His6 and thrombin tags Na L-arginine "[""ARG""]" 1 Kd Kd = = 32 pM 0.032 [] unit_conversion 10.494850021680094 success True direct_binding Competitive ITC using L-arginine, with Salmonella enterica ArgT as competing arginine-binding protein. 3 Fitting the protein–protein competition experiment yielded a Kd of 32 pM for the interaction between SAR11_1210 and L-arginine. auto_single_measurement only accepted activity measurement [1] 1 structures\8HQR\8HQR_metadata.json point structures/8HQR/8hqr_protein.pdb structures/8HQR/8hqr_pocket.pdb structures/8HQR/8hqr_ligand.sdf structures/8HQR/8hqr_ligand.pdb structures/8HQR/8hqr_ligand.cif structures/8HQR/8hqr_complex.pdb structures/8HQR/8hqr_complex.cif 8HQV extended beta'-COP Saccharomyces cerevisiae N-terminal beta-propeller domain, residues 1-301, with N-terminal 6xHis-SUMO tag Na HCoV-OC43 Spike peptide KTSHDD, residues 1348-1353, KTSHxx sorting motif "[""CHAIN:B""]" 1 Kd Kd = = 202.4 ± 26.6 µmol/L 202400.0 [] unit_conversion 3.6937894918322387 success True direct_binding ITC affinity measurement of the HCoV-OC43 S retrieval signal with β′-COP. 4 Figure 2F lists HCoV-OC43 S, KTSHDD, K_D 202.4 ± 26.6 µmol/L; Figure 1 identifies 8HQV as the β′-COP complex with KTSHDD. auto_single_measurement only accepted activity measurement [1] 1 structures\8HQV\8HQV_metadata.json point structures/8HQV/8hqv_protein.pdb structures/8HQV/8hqv_pocket.pdb structures/8HQV/8hqv_ligand.pdb structures/8HQV/8hqv_ligand.cif structures/8HQV/8hqv_complex.pdb structures/8HQV/8hqv_complex.cif 8HQX extended beta'-COP Saccharomyces cerevisiae N-terminal beta-propeller domain, residues 1-301, with N-terminal 6xHis-SUMO tag Na TAT-WDM peptide "[""CHAIN:B""]" 1 Kd Kd = = 1.8 ± 0.6 µmol/L 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding ITC affinity measurement of TAT-WDM with β′-COP. 4 Figure 2F lists TAT-WDM, sequence TAT-AKEKSD, K_D 1.8 ± 0.6 µmol/L; the text and Figure 2 identify the β′-COP/TAT-WDM complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8HQX\8HQX_metadata.json point structures/8HQX/8hqx_protein.pdb structures/8HQX/8hqx_pocket.pdb structures/8HQX/8hqx_ligand.pdb structures/8HQX/8hqx_ligand.cif structures/8HQX/8hqx_complex.pdb structures/8HQX/8hqx_complex.cif 8HSV extended rat beta-arrestin1 Rattus norvegicus beta-arrestin1 residues 1-394 in complex with an Mdm2 peptide Na Mdm2ABR peptide residues 210-227 "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 1.09 ± 0.05 µM 1090.0 [] unit_conversion 5.962573502059376 success True direct_binding Isothermal titration calorimetry; Mdm2_210–227 peptide binding to β-arrestin1, monophasic 1:1 stoichiometry. 2 “The Mdm2_210–227 peptide exhibited a similar binding affinity to βarr1 (KD of 1.09 ± 0.05 µM) ... as measured by isothermal titration calorimetry (ITC), exhibiting a monophasic binding with 1:1 binding stoichiometry.” auto_single_measurement only accepted activity measurement [1] 1 structures\8HSV\8HSV_metadata.json point structures/8HSV/8hsv_protein.pdb structures/8HSV/8hsv_pocket.pdb structures/8HSV/8hsv_ligand.pdb structures/8HSV/8hsv_ligand.cif structures/8HSV/8hsv_complex.pdb structures/8HSV/8hsv_complex.cif 8HTS classic Bcl-2 human Bcl-2 residues 6-34 and 92-207; expressed with His6-SUMO tag and purified after tag removal Na S-10r "[""N2L""]" 1 IC50 IC50 = = 0.039 nM 0.039 [] unit_conversion 10.4089353929735 success True biochemical_inhibition TR-FRET biochemical competitive Bcl-2:BAK disruption assay; Table 3. 7 Table 3 reports S-10r Bcl-2 WT biochemical IC50 = 0.039 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8HTS\8HTS_metadata.json point structures/8HTS/8hts_protein.pdb structures/8HTS/8hts_pocket.pdb structures/8HTS/8hts_ligand.sdf structures/8HTS/8hts_ligand.pdb structures/8HTS/8hts_ligand.cif structures/8HTS/8hts_complex.pdb structures/8HTS/8hts_complex.cif 8HTV classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Full-length SARS-CoV-2 3CLpro expressed with an N-terminal 6xHis-SUMO2 fusion tag; the tag was cleaved before crystallization Na compound 3a "[""UZF""]" 2 Ki Ki = = 43.64 µM 43640.0 [] unit_conversion 4.360115258083696 success True biochemical_inhibition Enzymatic kinetic study; reported as the noncovalent binding-affinity Ki for compound 3a. 7 The text states that enzymatic kinetic studies of 3a, 3c, and 3h gave Ki values of 43.64, 24.86, and 18.07 µM, respectively. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8HTV\8HTV_metadata.json point structures/8HTV/8htv_protein.pdb structures/8HTV/8htv_pocket.pdb structures/8HTV/8htv_ligand.sdf structures/8HTV/8htv_ligand.pdb structures/8HTV/8htv_ligand.cif structures/8HTV/8htv_complex.pdb structures/8HTV/8htv_complex.cif 8HVK classic SARS-CoV-2 main protease SARS-CoV-2 full-length Mpro mutant construct G15S PF07321332 (nirmatrelvir) "[""4WI""]" 1 IC50 IC50 = = 0.0592 μM 59.2 [] unit_conversion 7.22767829327708 success True biochemical_inhibition Purified mutant Mpro FRET-based cleavage/inhibition assay; nirmatrelvir preincubated for 30 min at room temperature. 5 Figure 3A explicitly reports IC50 = 0.0592 μM for nirmatrelvir against Mpro G15S. auto_single_measurement only accepted activity measurement [1] 1 structures\8HVK\8HVK_metadata.json point structures/8HVK/8hvk_protein.pdb structures/8HVK/8hvk_pocket.pdb structures/8HVK/8hvk_ligand.sdf structures/8HVK/8hvk_ligand.pdb structures/8HVK/8hvk_ligand.cif structures/8HVK/8hvk_complex.pdb structures/8HVK/8hvk_complex.cif 8HVL classic SARS-CoV-2 main protease SARS-CoV-2 full-length Mpro mutant construct M49I PF07321332 (nirmatrelvir) "[""4WI""]" 1 IC50 IC50 = = 0.1243 μM 124.3 [] unit_conversion 6.905528871358355 success True biochemical_inhibition Purified mutant Mpro FRET-based cleavage/inhibition assay; nirmatrelvir preincubated for 30 min at room temperature. 5 Figure 3G explicitly reports IC50 = 0.1243 μM for nirmatrelvir against Mpro M49I. auto_single_measurement only accepted activity measurement [1] 1 structures\8HVL\8HVL_metadata.json point structures/8HVL/8hvl_protein.pdb structures/8HVL/8hvl_pocket.pdb structures/8HVL/8hvl_ligand.sdf structures/8HVL/8hvl_ligand.pdb structures/8HVL/8hvl_ligand.cif structures/8HVL/8hvl_complex.pdb structures/8HVL/8hvl_complex.cif 8HVM classic SARS-CoV-2 main protease SARS-CoV-2 full-length Mpro mutant construct K90R PF07321332 (nirmatrelvir) "[""4WI""]" 1 IC50 IC50 = = 0.047 μM 47.0 [] unit_conversion 7.327902142064282 success True biochemical_inhibition Purified mutant Mpro FRET-based cleavage/inhibition assay; nirmatrelvir preincubated for 30 min at room temperature. 5 Figure 3J explicitly reports IC50 = 0.047 μM for nirmatrelvir against Mpro K90R. auto_single_measurement only accepted activity measurement [1] 1 structures\8HVM\8HVM_metadata.json point structures/8HVM/8hvm_protein.pdb structures/8HVM/8hvm_pocket.pdb structures/8HVM/8hvm_ligand.sdf structures/8HVM/8hvm_ligand.pdb structures/8HVM/8hvm_ligand.cif structures/8HVM/8hvm_complex.pdb structures/8HVM/8hvm_complex.cif 8HVN classic SARS-CoV-2 main protease SARS-CoV-2 full-length Mpro mutant construct P132H PF07321332 (nirmatrelvir) "[""4WI""]" 1 IC50 IC50 = = 0.0559 μM 55.9 [] unit_conversion 7.252588192113577 success True biochemical_inhibition Purified mutant Mpro FRET-based cleavage/inhibition assay; nirmatrelvir preincubated for 30 min at room temperature. 5 Figure 3K explicitly reports IC50 = 0.0559 μM for nirmatrelvir against Mpro P132H. auto_single_measurement only accepted activity measurement [1] 1 structures\8HVN\8HVN_metadata.json point structures/8HVN/8hvn_protein.pdb structures/8HVN/8hvn_pocket.pdb structures/8HVN/8hvn_ligand.sdf structures/8HVN/8hvn_ligand.pdb structures/8HVN/8hvn_ligand.cif structures/8HVN/8hvn_complex.pdb structures/8HVN/8hvn_complex.cif 8HVO classic SARS-CoV-2 main protease SARS-CoV-2 full-length Mpro mutant construct V186F PF07321332 (nirmatrelvir) "[""4WI""]" 1 IC50 IC50 = = 0.0453 μM 45.3 [] unit_conversion 7.343901797987169 success True biochemical_inhibition Purified mutant Mpro FRET-based cleavage/inhibition assay; nirmatrelvir preincubated for 30 min at room temperature. 5 Figure 3M explicitly reports IC50 = 0.0453 μM for nirmatrelvir against Mpro V186F. auto_single_measurement only accepted activity measurement [1] 1 structures\8HVO\8HVO_metadata.json point structures/8HVO/8hvo_protein.pdb structures/8HVO/8hvo_pocket.pdb structures/8HVO/8hvo_ligand.sdf structures/8HVO/8hvo_ligand.pdb structures/8HVO/8hvo_ligand.cif structures/8HVO/8hvo_complex.pdb structures/8HVO/8hvo_complex.cif 8HX5 classic VIM-2 Na Na Na compound 15 (2-amino-5-(4-methoxybenzyl)thiazole-4-carboxylic acid) "[""4YJ""]" 1 IC50 IC50 = = 0.79 μM 790.0 [] unit_conversion 6.102372908709558 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 2, B1 MBL VIM-2 column. 5 Table 2 reports compound 15 with VIM-2 IC50/LE of 0.79 μM/0.47; Figure 2 maps compound 15 to VIM-2 structure 8HX5. auto_single_measurement only accepted activity measurement [1] 1 structures\8HX5\8HX5_metadata.json point structures/8HX5/8hx5_protein.pdb structures/8HX5/8hx5_pocket.pdb structures/8HX5/8hx5_ligand.sdf structures/8HX5/8hx5_ligand.pdb structures/8HX5/8hx5_ligand.cif structures/8HX5/8hx5_complex.pdb structures/8HX5/8hx5_complex.cif 8HXE classic L1 Na residues 22-290 Na compound 18 (2-amino-5-(4-propylbenzyl)thiazole-4-carboxylic acid) "[""51I""]" 1 IC50 IC50 = = 5.31 μM 5310.0 [] unit_conversion 5.274905478918531 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 2, B3 MBL L1 column. 5 Table 2 reports compound 18 with L1 IC50/LE of 5.31 μM/0.39; Figure 3 and the accession list map compound 18 to L1 structure 8HXE. auto_single_measurement only accepted activity measurement [1] 1 structures\8HXE\8HXE_metadata.json point structures/8HXE/8hxe_protein.pdb structures/8HXE/8hxe_pocket.pdb structures/8HXE/8hxe_ligand.sdf structures/8HXE/8hxe_ligand.pdb structures/8HXE/8hxe_ligand.cif structures/8HXE/8hxe_complex.pdb structures/8HXE/8hxe_complex.cif 8HXI classic L1 Na residues 22-290 Na compound 19 (2-amino-5-(4-isopropylbenzyl)thiazole-4-carboxylic acid) "[""5A5""]" 1 IC50 IC50 = = 13.58 μM 13580.0 [] unit_conversion 4.8671002300555175 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 2, B3 MBL L1 column. 5 Table 2 reports compound 19 with L1 IC50/LE of 13.58 μM/0.36; Figure 3 and the accession list map compound 19 to L1 structure 8HXI. auto_single_measurement only accepted activity measurement [1] 1 structures\8HXI\8HXI_metadata.json point structures/8HXI/8hxi_protein.pdb structures/8HXI/8hxi_pocket.pdb structures/8HXI/8hxi_ligand.sdf structures/8HXI/8hxi_ligand.pdb structures/8HXI/8hxi_ligand.cif structures/8HXI/8hxi_complex.pdb structures/8HXI/8hxi_complex.cif 8HXN classic Sfh-I Na residues 3-234 Na compound 24 (2-amino-5-(4-(but-3-en-1-yloxy)benzyl)thiazole-4-carboxylic acid) "[""5I6""]" 1 IC50 IC50 = = 13.76 μM 13760.0 [] unit_conversion 4.8613815661005075 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 2, B2 MBL Sfh-I column. 5 Table 2 reports compound 24 with Sfh-I IC50/LE of 13.76 μM/0.32; Figure 4 and the accession list map compound 24 to Sfh-I structure 8HXN. auto_single_measurement only accepted activity measurement [1] 1 structures\8HXN\8HXN_metadata.json point structures/8HXN/8hxn_protein.pdb structures/8HXN/8hxn_pocket.pdb structures/8HXN/8hxn_ligand.sdf structures/8HXN/8hxn_ligand.pdb structures/8HXN/8hxn_ligand.cif structures/8HXN/8hxn_complex.pdb structures/8HXN/8hxn_complex.cif 8HXO classic VIM-2 Na Na Na compound 32 (2-amino-5-isobutylthiazole-4-carboxylic acid) "[""5IY""]" 1 IC50 IC50 = = 5.00 μM 5000.0 [] unit_conversion 5.301029995663981 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL VIM-2 column. 8 Table 3 reports compound 32 with VIM-2 IC50/LE of 5.00 μM/0.50; Figure 5 and the accession list map compound 32 to VIM-2 structure 8HXO. auto_single_measurement only accepted activity measurement [1] 1 structures\8HXO\8HXO_metadata.json point structures/8HXO/8hxo_protein.pdb structures/8HXO/8hxo_pocket.pdb structures/8HXO/8hxo_ligand.sdf structures/8HXO/8hxo_ligand.pdb structures/8HXO/8hxo_ligand.cif structures/8HXO/8hxo_complex.pdb structures/8HXO/8hxo_complex.cif 8HXP classic VIM-2 Na Na Na compound 34 (2-amino-5-(but-3-en-1-yl)thiazole-4-carboxylic acid) "[""5YT""]" 1 IC50 IC50 = = 1.32 μM 1320.0 [] unit_conversion 5.8794260687941495 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL VIM-2 column. 8 Table 3 reports compound 34 with VIM-2 IC50/LE of 1.32 μM/0.63; Figure 6 and the accession list map compound 34 to VIM-2 structure 8HXP. auto_single_measurement only accepted activity measurement [1] 1 structures\8HXP\8HXP_metadata.json point structures/8HXP/8hxp_protein.pdb structures/8HXP/8hxp_pocket.pdb structures/8HXP/8hxp_ligand.sdf structures/8HXP/8hxp_ligand.pdb structures/8HXP/8hxp_ligand.cif structures/8HXP/8hxp_complex.pdb structures/8HXP/8hxp_complex.cif 8HXU classic VIM-2 Na Na Na compound 35 (2-amino-5-pentylthiazole-4-carboxylic acid) "[""5Z2""]" 1 IC50 IC50 = = 0.48 μM 480.0 [] unit_conversion 6.318758762624412 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL VIM-2 column. 8 Table 3 reports compound 35 with VIM-2 IC50/LE of 0.48 μM/0.63; Figure 6 and the accession list map compound 35 to VIM-2 structure 8HXU. auto_single_measurement only accepted activity measurement [1] 1 structures\8HXU\8HXU_metadata.json point structures/8HXU/8hxu_protein.pdb structures/8HXU/8hxu_pocket.pdb structures/8HXU/8hxu_ligand.sdf structures/8HXU/8hxu_ligand.pdb structures/8HXU/8hxu_ligand.cif structures/8HXU/8hxu_complex.pdb structures/8HXU/8hxu_complex.cif 8HXV classic VIM-2 Na Na Na compound 36 (2-amino-5-hexylthiazole-4-carboxylic acid) "[""5ZD""]" 1 IC50 IC50 = = 0.43 μM 430.0 [] unit_conversion 6.366531544420413 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL VIM-2 column. 8 Table 3 reports compound 36 with VIM-2 IC50/LE of 0.43 μM/0.59; Figure 6 and the accession list map compound 36 to VIM-2 structure 8HXV. auto_single_measurement only accepted activity measurement [1] 1 structures\8HXV\8HXV_metadata.json point structures/8HXV/8hxv_protein.pdb structures/8HXV/8hxv_pocket.pdb structures/8HXV/8hxv_ligand.sdf structures/8HXV/8hxv_ligand.pdb structures/8HXV/8hxv_ligand.cif structures/8HXV/8hxv_complex.pdb structures/8HXV/8hxv_complex.cif 8HXW classic VIM-2 Na Na Na compound 37 (2-amino-5-heptylthiazole-4-carboxylic acid) "[""5ZR""]" 1 IC50 IC50 = = 0.26 μM 260.0 [] unit_conversion 6.585026652029182 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL VIM-2 column. 8 Table 3 reports compound 37 with VIM-2 IC50/LE of 0.26 μM/0.57; Figure 6 and the accession list map compound 37 to VIM-2 structure 8HXW. auto_single_measurement only accepted activity measurement [1] 1 structures\8HXW\8HXW_metadata.json point structures/8HXW/8hxw_protein.pdb structures/8HXW/8hxw_pocket.pdb structures/8HXW/8hxw_ligand.sdf structures/8HXW/8hxw_ligand.pdb structures/8HXW/8hxw_ligand.cif structures/8HXW/8hxw_complex.pdb structures/8HXW/8hxw_complex.cif 8HY1 classic VIM-2 Na Na Na compound 39 (2-amino-5-(thiophen-2-ylmethyl)thiazole-4-carboxylic acid) "[""5ZU""]" 1 IC50 IC50 = = 3.30 μM 3300.0 [] unit_conversion 5.481486060122112 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL VIM-2 column. 8 Table 3 reports compound 39 with VIM-2 IC50/LE of 3.30 μM/0.51; Figure 7 and the accession list map compound 39 to VIM-2 structure 8HY1. auto_single_measurement only accepted activity measurement [1] 1 structures\8HY1\8HY1_metadata.json point structures/8HY1/8hy1_protein.pdb structures/8HY1/8hy1_pocket.pdb structures/8HY1/8hy1_ligand.sdf structures/8HY1/8hy1_ligand.pdb structures/8HY1/8hy1_ligand.cif structures/8HY1/8hy1_complex.pdb structures/8HY1/8hy1_complex.cif 8HY2 classic VIM-2 Na Na Na compound 41 (2-amino-5-phenethylthiazole-4-carboxylic acid) "[""5ZX""]" 1 IC50 IC50 = = 0.68 μM 680.0 [] unit_conversion 6.167491087293763 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL VIM-2 column. 8 Table 3 reports compound 41 with VIM-2 IC50/LE of 0.68 μM/0.51; Figure 8 and the accession list map compound 41 to VIM-2 structure 8HY2. auto_single_measurement only accepted activity measurement [1] 1 structures\8HY2\8HY2_metadata.json point structures/8HY2/8hy2_protein.pdb structures/8HY2/8hy2_pocket.pdb structures/8HY2/8hy2_ligand.sdf structures/8HY2/8hy2_ligand.pdb structures/8HY2/8hy2_ligand.cif structures/8HY2/8hy2_complex.pdb structures/8HY2/8hy2_complex.cif 8HY5 classic D-amino acid oxidase (DAO) human Na R38H FAD "[""BEZ""]" 1 Kd Kd = = 3010 ± 798 µM 3010000.0 [] unit_conversion 2.521433504406157 success True direct_binding Spectrophotometric benzoate-binding assay at 493 nm using holoenzyme containing 40 µM FAD. 8 Table 2 reports R38H benzoate Kd = 3010 ± 798 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8HY5\8HY5_metadata.json point structures/8HY5/8hy5_protein.pdb structures/8HY5/8hy5_pocket.pdb structures/8HY5/8hy5_ligand.sdf structures/8HY5/8hy5_ligand.pdb structures/8HY5/8hy5_ligand.cif structures/8HY5/8hy5_complex.pdb structures/8HY5/8hy5_complex.cif 8HY6 classic NDM-1 Na Na Na compound 41 (2-amino-5-phenethylthiazole-4-carboxylic acid) "[""5ZX""]" 1 IC50 IC50 = = 0.17 μM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL NDM-1 column. 8 Table 3 reports compound 41 with NDM-1 IC50/LE of 0.17 μM/0.56; Figure 8 and the accession list map compound 41 to NDM-1 structure 8HY6. auto_single_measurement only accepted activity measurement [1] 1 structures\8HY6\8HY6_metadata.json point structures/8HY6/8hy6_protein.pdb structures/8HY6/8hy6_pocket.pdb structures/8HY6/8hy6_ligand.sdf structures/8HY6/8hy6_ligand.pdb structures/8HY6/8hy6_ligand.cif structures/8HY6/8hy6_complex.pdb structures/8HY6/8hy6_complex.cif 8HY9 classic Riemerella anatipestifer STING (RiSTING) Riemerella anatipestifer Na Na 3'3'-c-di-GMP (cGG) "[""C2E""]" 1 Kd Kd = = 0.1 nM 0.1 [] unit_conversion 10.0 success True direct_binding Isothermal titration calorimetry (ITC) of cGG binding to RiSTING. 5 Fig. 2 caption explicitly states: “ITC analysis of cGG binding to RiSTING. The dissociation constant was determined to be 0.1 nM.” The data-availability section maps RiSTING_cGG to PDB 8HY9. auto_single_measurement only accepted activity measurement [1] 1 structures\8HY9\8HY9_metadata.json point structures/8HY9/8hy9_protein.pdb structures/8HY9/8hy9_pocket.pdb structures/8HY9/8hy9_ligand.sdf structures/8HY9/8hy9_ligand.pdb structures/8HY9/8hy9_ligand.cif structures/8HY9/8hy9_complex.pdb structures/8HY9/8hy9_complex.cif 8HYD classic VIM-2 Na Na Na compound 45 (2-amino-5-(2-(thiophen-2-yl)ethyl)thiazole-4-carboxylic acid) "[""60J""]" 1 IC50 IC50 = = 0.13 μM 130.0 [] unit_conversion 6.886056647693163 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL VIM-2 column. 8 Table 3 reports compound 45 with VIM-2 IC50/LE of 0.13 μM/0.60; Figure 9 and the accession list map compound 45 to VIM-2 structure 8HYD. auto_single_measurement only accepted activity measurement [1] 1 structures\8HYD\8HYD_metadata.json point structures/8HYD/8hyd_protein.pdb structures/8HYD/8hyd_pocket.pdb structures/8HYD/8hyd_ligand.sdf structures/8HYD/8hyd_ligand.pdb structures/8HYD/8hyd_ligand.cif structures/8HYD/8hyd_complex.pdb structures/8HYD/8hyd_complex.cif 8HZR classic SARS-CoV-2 main protease SARS-CoV-2 full-length Mpro mutant construct S46F PF07321332 (nirmatrelvir) "[""4WI""]" 1 IC50 IC50 = = 0.0721 μM 72.1 [] unit_conversion 7.142064735280571 success True biochemical_inhibition Purified mutant Mpro FRET-based cleavage/inhibition assay; nirmatrelvir preincubated for 30 min at room temperature. 5 Figure 3D explicitly reports IC50 = 0.0721 μM for nirmatrelvir against Mpro S46F. auto_single_measurement only accepted activity measurement [1] 1 structures\8HZR\8HZR_metadata.json point structures/8HZR/8hzr_protein.pdb structures/8HZR/8hzr_pocket.pdb structures/8HZR/8hzr_ligand.sdf structures/8HZR/8hzr_ligand.pdb structures/8HZR/8hzr_ligand.cif structures/8HZR/8hzr_complex.pdb structures/8HZR/8hzr_complex.cif 8I2A classic tryptophanyl-tRNA synthetase (TrpRS) Escherichia coli K-12 full-length EcTrpRS with a C-terminal hexahistidine tag Na M1-109 "[""5OB""]" 1 Kd Kd = = 26.1 ± 4.4 µM 26100.0 [] unit_conversion 4.583359492661719 success True direct_binding ITC binding of M1-109 to the asymmetric ‘open-closed’ EcTrpRS state containing TrpAMP. 9 The paper states that M1-109 had a binding affinity of 26.1 ± 4.4 µM to ‘open-closed’ EcTrpRS by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8I2A\8I2A_metadata.json point structures/8I2A/8i2a_protein.pdb structures/8I2A/8i2a_pocket.pdb structures/8I2A/8i2a_ligand.sdf structures/8I2A/8i2a_ligand.pdb structures/8I2A/8i2a_ligand.cif structures/8I2A/8i2a_complex.pdb structures/8I2A/8i2a_complex.cif 8I3F extended Eaf3-Rco1 complex Na Eaf3 MRG domain residues 218-401; Rco1 PHD1-SID residues 240-376 Na H3K4me0 histone H3 N-terminal peptide "[""CHAIN:C""]" 1 Kd Kd = = 22 μM 22000.0 [] unit_conversion 4.657577319177793 success True direct_binding Isothermal titration calorimetry (ITC) with Eaf3 MRG–Rco1 PHD1–SID. 1 ITC found H3K4me0 peptide binding to the Eaf3MRG–Rco1PHD1–SID complex with KD 22 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8I3F\8I3F_metadata.json point structures/8I3F/8i3f_protein.pdb structures/8I3F/8i3f_pocket.pdb structures/8I3F/8i3f_ligand.pdb structures/8I3F/8i3f_ligand.cif structures/8I3F/8i3f_complex.pdb structures/8I3F/8i3f_complex.cif 8I4I classic tryptophanyl-tRNA synthetase (TrpRS) Escherichia coli K-12 full-length EcTrpRS with a C-terminal hexahistidine tag Na TrpAMP; L-Trp "[""TRP""]" 1 Kd Kd = = 37.6 ± 3.5 µM 37600.0 [] unit_conversion 4.424812155072339 success True direct_binding ITC binding of L-Trp to ‘open-closed’ asymmetric EcTrpRS, whose other active site is occupied by TrpAMP. 6 Figure 2A prints Kd = 37.6 ± 3.5 µM for L-Trp binding to ‘open-closed’ EcTrpRS; the text identifies this as the TrpAMP-bound asymmetric state. auto_single_measurement only accepted activity measurement [1] 1 structures\8I4I\8I4I_metadata.json point structures/8I4I/8i4i_protein.pdb structures/8I4I/8i4i_pocket.pdb structures/8I4I/8i4i_ligand.sdf structures/8I4I/8i4i_ligand.pdb structures/8I4I/8i4i_ligand.cif structures/8I4I/8i4i_complex.pdb structures/8I4I/8i4i_complex.cif 8I4S classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 SARS-CoV-2 Mpro cloned into pET-28a(+) with N-terminal SAVLQ-SGFRK and C-terminal SGVTFQ-GP protease cleavage sites Na D8 "[""OU3""]" 1 IC50 IC50 = = 0.100 ± 0.012 μM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition FRET protease activity assay against SARS-CoV-2 Mpro. 13 Table 4 reports D8 IC50 = 0.100 ± 0.012 μM; its footnote states inhibition against SARS-CoV-2 Mpro was determined using the FRET protease activity assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8I4S\8I4S_metadata.json point structures/8I4S/8i4s_protein.pdb structures/8I4S/8i4s_pocket.pdb structures/8I4S/8i4s_ligand.sdf structures/8I4S/8i4s_ligand.pdb structures/8I4S/8i4s_ligand.cif structures/8I4S/8i4s_complex.pdb structures/8I4S/8i4s_complex.cif 8I60 extended GAS41 human GAS41 YEATS domain, residues 11-150 Na histone H3K27cr peptide, residues 21-33 "[""CHAIN:A"", ""CHAIN:B""]" 1 Kd Kd = = 22.9 µM 22900.0 [] unit_conversion 4.640164517660112 success True direct_binding Isothermal titration calorimetry and NMR spectroscopy confirmed preferential GAS41 YEATS-domain binding to H3K27cr; the reported Kd for H3K27cr was 22.9 µM. 5 “GAS41 YEATS domain binding preference for H3K27cr over H3K27ac was confirmed by isothermal titration calorimetry (Figure S2B) and NMR ... showing that the binding affinity to H3K27cr was about 2-fold ... (Kd of 22.9 µM vs. 51.5 µM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8I60\8I60_metadata.json point structures/8I60/8i60_protein.pdb structures/8I60/8i60_pocket.pdb structures/8I60/8i60_ligand.pdb structures/8I60/8i60_ligand.cif structures/8I60/8i60_complex.pdb structures/8I60/8i60_complex.cif 8I7T classic human ABL1 kinase Homo sapiens kinase domain Na ABL1-B4 (B4) "[""6I5""]" 1 Ki Ki = = 0.19 × 10^-6 M 189.99999999999997 [] unit_conversion 6.721246399047171 success True direct_binding Time- and concentration-dependent kinetic analysis of the ABL kinase domain/B4 covalent reaction by intact-protein MS. 8 Fig. 3G prints K_I = 0.19 × 10^-6 M; its caption states this kinetic analysis of the time-dependent ABL kinase domain/B4 reaction determined k_inact and K_I by intact protein MS. auto_single_measurement only accepted activity measurement [1] 1 structures\8I7T\8I7T_metadata.json point structures/8I7T/8i7t_protein.pdb structures/8I7T/8i7t_pocket.pdb structures/8I7T/8i7t_ligand.sdf structures/8I7T/8i7t_ligand.pdb structures/8I7T/8i7t_ligand.cif structures/8I7T/8i7t_complex.pdb structures/8I7T/8i7t_complex.cif 8IBQ classic BRD4 Na BRD4 BD1, residues K57-E168 Na compound 21 "[""OWO""]" 1 Ki Ki = = 0.031 ± 0.003 μM 31.0 [] unit_conversion 7.508638306165727 success True biochemical_inhibition Fluorescence-polarization competitive assay; BRD4 BD1 Ki for compound 21. 4 Table 1 reports compound 21 BRD4(1) Ki = 0.031 ± 0.003 μM. Figure 3 caption maps compound 21 bound to BRD4 BD1 to PDB 8IBQ; the paper describes recombinant human BRD4 BD1/BD2 and the FP competitive assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8IBQ\8IBQ_metadata.json point structures/8IBQ/8ibq_protein.pdb structures/8IBQ/8ibq_pocket.pdb structures/8IBQ/8ibq_ligand.sdf structures/8IBQ/8ibq_ligand.pdb structures/8IBQ/8ibq_ligand.cif structures/8IBQ/8ibq_complex.pdb structures/8IBQ/8ibq_complex.cif 8IDH classic BRD4 Na BRD4 BD2, residues E352-M457 Na compound 21 "[""OWO""]" 1 Ki Ki = = 0.092 ± 0.006 μM 92.0 [] unit_conversion 7.036212172654444 success True biochemical_inhibition Fluorescence-polarization competitive assay; BRD4 BD2 Ki for compound 21. 4 Table 1 reports compound 21 BRD4(2) Ki = 0.092 ± 0.006 μM. Figure 3 caption maps compound 21 bound to BRD4 BD2 to PDB 8IDH; the paper describes recombinant human BRD4 BD1/BD2 and the FP competitive assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8IDH\8IDH_metadata.json point structures/8IDH/8idh_protein.pdb structures/8IDH/8idh_pocket.pdb structures/8IDH/8idh_ligand.sdf structures/8IDH/8idh_ligand.pdb structures/8IDH/8idh_ligand.cif structures/8IDH/8idh_complex.pdb structures/8IDH/8idh_complex.cif 8IF3 classic human alpha2delta1 human R677-8His-K678 Na mirogabalin "[""8X9""]" 1 Kd Kd = = 10.6 ± 3.78 nM 10.6 [] unit_conversion 7.97469413473523 success True direct_binding Microscale thermophoresis (MST) binding assay of purified α2δ1 R677-8His-K678 for mirogabalin. 3 “The Kd value of mirogabalin was 10.6 ± 3.78 nM for the purified α2δ1.” auto_single_measurement only accepted activity measurement [1] 1 structures\8IF3\8IF3_metadata.json point structures/8IF3/8if3_protein.pdb structures/8IF3/8if3_pocket.pdb structures/8IF3/8if3_ligand.sdf structures/8IF3/8if3_ligand.pdb structures/8IF3/8if3_ligand.cif structures/8IF3/8if3_complex.pdb structures/8IF3/8if3_complex.cif 8IFP classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na compound 1 "[""OZ6""]" 1 IC50 IC50 = = 9 ± 1 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition FRET-based enzymatic inhibition assay. 3 Fig. 1c prints IC50 = 9 ± 1 nM for compound 1. auto_single_measurement only accepted activity measurement [1] 1 structures\8IFP\8IFP_metadata.json point structures/8IFP/8ifp_protein.pdb structures/8IFP/8ifp_pocket.pdb structures/8IFP/8ifp_ligand.sdf structures/8IFP/8ifp_ligand.pdb structures/8IFP/8ifp_ligand.cif structures/8IFP/8ifp_complex.pdb structures/8IFP/8ifp_complex.cif 8IFQ classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na compound 2 "[""I1Z""]" 1 IC50 IC50 = = 20 ± 4 nM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition FRET-based enzymatic inhibition assay. 3 Fig. 1c prints IC50 = 20 ± 4 nM for compound 2. auto_single_measurement only accepted activity measurement [1] 1 structures\8IFQ\8IFQ_metadata.json point structures/8IFQ/8ifq_protein.pdb structures/8IFQ/8ifq_pocket.pdb structures/8IFQ/8ifq_ligand.sdf structures/8IFQ/8ifq_ligand.pdb structures/8IFQ/8ifq_ligand.cif structures/8IFQ/8ifq_complex.pdb structures/8IFQ/8ifq_complex.cif 8IFR classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na compound 3 "[""P0O""]" 1 IC50 IC50 = = 14 ± 2 nM 14.0 [] unit_conversion 7.853871964321762 success True biochemical_inhibition FRET-based enzymatic inhibition assay. 3 Fig. 1c prints IC50 = 14 ± 2 nM for compound 3. auto_single_measurement only accepted activity measurement [1] 1 structures\8IFR\8IFR_metadata.json point structures/8IFR/8ifr_protein.pdb structures/8IFR/8ifr_pocket.pdb structures/8IFR/8ifr_ligand.sdf structures/8IFR/8ifr_ligand.pdb structures/8IFR/8ifr_ligand.cif structures/8IFR/8ifr_complex.pdb structures/8IFR/8ifr_complex.cif 8IFS classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na compound 7 "[""OZL""]" 1 IC50 IC50 = = 23 ± 3 nM 23.0 [] unit_conversion 7.638272163982407 success True biochemical_inhibition FRET-based enzymatic inhibition assay. 3 Fig. 1d prints IC50 = 23 ± 3 nM for compound 7. auto_single_measurement only accepted activity measurement [1] 1 structures\8IFS\8IFS_metadata.json point structures/8IFS/8ifs_protein.pdb structures/8IFS/8ifs_pocket.pdb structures/8IFS/8ifs_ligand.sdf structures/8IFS/8ifs_ligand.pdb structures/8IFS/8ifs_ligand.cif structures/8IFS/8ifs_complex.pdb structures/8IFS/8ifs_complex.cif 8IFT classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na compound 10 "[""OZB""]" 1 IC50 IC50 = = 10 ± 2 nM 10.0 [] unit_conversion 8.0 success True biochemical_inhibition FRET-based enzymatic inhibition assay. 3 Fig. 1e prints IC50 = 10 ± 2 nM for compound 10. auto_single_measurement only accepted activity measurement [1] 1 structures\8IFT\8IFT_metadata.json point structures/8IFT/8ift_protein.pdb structures/8IFT/8ift_pocket.pdb structures/8IFT/8ift_ligand.sdf structures/8IFT/8ift_ligand.pdb structures/8IFT/8ift_ligand.cif structures/8IFT/8ift_complex.pdb structures/8IFT/8ift_complex.cif 8IG1 classic transthyretin (TTR) human N-terminal hexahistidine-tagged WT-TTR wild-type (WT) rafoxanide "[""OX9""]" 1 Kd Kd = = 3.6 ± 0.51 μM 3600.0 [] unit_conversion 5.443697499232712 success True direct_binding Tryptophan intrinsic-fluorescence quenching assay using 2 μM WT-TTR; apparent dissociation constant (Kd,app). 3 “rafoxanide quenched the intrinsic fluorescence of TTR with a Kd,app of 3.6 μM” and Table 1 reports 3.6 ± 0.51 μM for rafoxanide. auto_single_measurement only accepted activity measurement [1] 1 structures\8IG1\8IG1_metadata.json point structures/8IG1/8ig1_protein.pdb structures/8IG1/8ig1_pocket.pdb structures/8IG1/8ig1_ligand.sdf structures/8IG1/8ig1_ligand.pdb structures/8IG1/8ig1_ligand.cif structures/8IG1/8ig1_complex.pdb structures/8IG1/8ig1_complex.cif 8IGC extended B-cell lymphoma-2 antagonist/killer (Bak) Human Bak residues 23-185; N-terminal His10 tag removed; C-terminal His6-tagged, in complex with Bnip5 residues 244-269 peptide Bak C166S Bnip5 BH3 peptide, residues 244-269 "[""CHAIN:B""]" 1 Kd Kd = = 775 nM 775.0 [] unit_conversion 6.110698297493689 success True direct_binding Isothermal titration calorimetry; Bnip5 peptide 0.8 mM and recombinant Bak 80 µM. 5 Figure 2B explicitly reports K_D = 775 nM for Human Bnip5 (244–269) titrated against Bak(23–185;C166S)–His6. auto_single_measurement only accepted activity measurement [1] 1 structures\8IGC\8IGC_metadata.json point structures/8IGC/8igc_protein.pdb structures/8IGC/8igc_pocket.pdb structures/8IGC/8igc_ligand.pdb structures/8IGC/8igc_ligand.cif structures/8IGC/8igc_complex.pdb structures/8IGC/8igc_complex.cif 8IGX classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na compound 9; simnotrelvir; SIM0417; SSD8432 "[""PQL""]" 1 IC50 IC50 = = 9 ± 1 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition FRET-based enzymatic inhibition assay. 3 Fig. 1e identifies compound 9 as simnotrelvir and prints IC50 = 9 ± 1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8IGX\8IGX_metadata.json point structures/8IGX/8igx_protein.pdb structures/8IGX/8igx_pocket.pdb structures/8IGX/8igx_ligand.sdf structures/8IGX/8igx_ligand.pdb structures/8IGX/8igx_ligand.cif structures/8IGX/8igx_complex.pdb structures/8IGX/8igx_complex.cif 8IHO extended SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 6x His-SUMO2-SARS-CoV-2 PLpro construct, with the tag cleaved before crystallization Na compound 2 "[""CHAIN:D"", ""CHAIN:E""]" 1 IC50 IC50 = = 0.46 ± 0.06 µM 460.0 [] unit_conversion 6.337242168318426 success True biochemical_inhibition Purified-protein enzymatic inhibition using RLRGG-AMC substrate. 4 Figure 2A reports for compound 2: “RLRGG-AMC: IC50 = 0.46 ± 0.06 µM”. auto_single_measurement only accepted activity measurement [1] 1 structures\8IHO\8IHO_metadata.json point structures/8IHO/8iho_protein.pdb structures/8IHO/8iho_pocket.pdb structures/8IHO/8iho_ligand.pdb structures/8IHO/8iho_ligand.cif structures/8IHO/8iho_complex.pdb structures/8IHO/8iho_complex.cif 8IHZ classic Factor inhibiting HIF-1 alpha (FIH) Na Na Na compound 1; (5-(1-(3-(4-chlorophenyl)propyl)-1H-1,2,3-triazol-4-yl)-3-hydroxypicolinoyl)glycine "[""P1X""]" 2 Ki Ki = = 240.4 ± 3.1 nM 240.4 [] unit_conversion 6.619065536669298 success True direct_binding Competitive affinity-based fluorescence-polarisation assay. 2 The text reports that compound 1 binds FIH with Ki = 240.4 ± 3.1 nM in FP studies. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8IHZ\8IHZ_metadata.json point structures/8IHZ/8ihz_protein.pdb structures/8IHZ/8ihz_pocket.pdb structures/8IHZ/8ihz_ligand.sdf structures/8IHZ/8ihz_ligand.pdb structures/8IHZ/8ihz_ligand.cif structures/8IHZ/8ihz_complex.pdb structures/8IHZ/8ihz_complex.cif 8II0 classic Factor inhibiting HIF-1 alpha (FIH) Na Na Na ZG-2291; (5-(3-(3-chlorophenyl)isoxazol-5-yl)-3-hydroxypicolinoyl)glycine "[""P5I""]" 2 Kd Kd = = 99.7 ± 20.2 nM 99.7 [] unit_conversion 7.001304841688344 success True direct_binding Isothermal titration calorimetry (ITC). 3 The text reports that ZG-2291 has high affinity for FIH with Kd = 99.7 ± 20.2 nM by ITC. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8II0\8II0_metadata.json point structures/8II0/8ii0_protein.pdb structures/8II0/8ii0_pocket.pdb structures/8II0/8ii0_ligand.sdf structures/8II0/8ii0_ligand.pdb structures/8II0/8ii0_ligand.cif structures/8II0/8ii0_complex.pdb structures/8II0/8ii0_complex.cif 8IIY extended GAS41 human MBP-fused GAS41 YEATS domain, residues 19-159 Na H3K14ac peptide, residues 1-19 "[""CHAIN:B"", ""CHAIN:C""]" 1 Kd Kd = = 3.5 ± 0.25 µM 3500.0 [] unit_conversion 5.455931955649724 success True direct_binding Isothermal titration calorimetry (ITC) of GAS41YEATS with H3K14ac H3-tail peptide (residues 1-19). 2 “The KD value between GAS41YEATS and the H3K14ac peptide (residues 1 to 19) was 3.5 ± 0.25 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8IIY\8IIY_metadata.json point structures/8IIY/8iiy_protein.pdb structures/8IIY/8iiy_pocket.pdb structures/8IIY/8iiy_ligand.pdb structures/8IIY/8iiy_ligand.cif structures/8IIY/8iiy_complex.pdb structures/8IIY/8iiy_complex.cif 8IIZ extended GAS41 human MBP-fused GAS41 YEATS domain, residues 19-159 Na H3K27ac peptide, residues 1-32 "[""CHAIN:B"", ""CHAIN:C""]" 1 Kd Kd = = 7.6 ± 0.79 µM 7600.0 [] unit_conversion 5.119186407719209 success True direct_binding Isothermal titration calorimetry (ITC) of GAS41YEATS with H3K27ac H3-tail peptide (residues 1-32). 2 “the H3K27ac peptide (1 to 32; 7.6 ± 0.79 µM)” auto_single_measurement only accepted activity measurement [1] 1 structures\8IIZ\8IIZ_metadata.json point structures/8IIZ/8iiz_protein.pdb structures/8IIZ/8iiz_pocket.pdb structures/8IIZ/8iiz_ligand.pdb structures/8IIZ/8iiz_ligand.cif structures/8IIZ/8iiz_complex.pdb structures/8IIZ/8iiz_complex.cif 8IJV classic gastric H+,K+-ATPase pig Alpha subunit with N-terminal Flag (DYKDDDDK), hexahistidine, EGFP, and TEV protease recognition sequence inserted before Met48; wild-type beta subunit Na DQ-02 "[""PWI""]" 1 IC50 IC50 = = 39.9 ± 3.3 µM 39900.0 [] unit_conversion 4.399027104313252 success True biochemical_inhibition Dose-dependent ATPase-activity inhibition using H+,K+-ATPase-enriched membrane fractions purified from pig stomach. 4 DQ-02 inhibited H+,K+-ATPase with apparent affinity IC50,DQ02 = 39.9 ± 3.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8IJV\8IJV_metadata.json point structures/8IJV/8ijv_protein.pdb structures/8IJV/8ijv_pocket.pdb structures/8IJV/8ijv_ligand.sdf structures/8IJV/8ijv_ligand.pdb structures/8IJV/8ijv_ligand.cif structures/8IJV/8ijv_complex.pdb structures/8IJV/8ijv_complex.cif 8IJW classic gastric H+,K+-ATPase pig Alpha subunit with N-terminal Flag (DYKDDDDK), hexahistidine, EGFP, and TEV protease recognition sequence inserted before Met48; wild-type beta subunit Na DQ-06 "[""PXR""]" 2 Ki Ki = = 93.8 nM 93.8 [] unit_conversion 7.027797161620936 success True biochemical_inhibition ATPase inhibition; the paper states DQ-06 is purely competitive with K+. 4 DQ-06 inhibition is purely competitive with K+ (Ki,DQ06 = 93.8 nM). auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8IJW\8IJW_metadata.json point structures/8IJW/8ijw_protein.pdb structures/8IJW/8ijw_pocket.pdb structures/8IJW/8ijw_ligand.sdf structures/8IJW/8ijw_ligand.pdb structures/8IJW/8ijw_ligand.cif structures/8IJW/8ijw_complex.pdb structures/8IJW/8ijw_complex.cif 8IJX classic gastric H+,K+-ATPase pig Alpha subunit with N-terminal Flag (DYKDDDDK), hexahistidine, EGFP, and TEV protease recognition sequence inserted before Met48; wild-type beta subunit Na DQ-18 "[""PZ0""]" 2 Ki Ki = = 47.6 nM 47.6 [] unit_conversion 7.3223930472795065 success True biochemical_inhibition ATPase inhibition; the paper confirms K+-competitive inhibition. 5 The paper confirms the K+-competitive inhibition mode of DQ-18 (Ki,DQ18 = 47.6 nM). auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8IJX\8IJX_metadata.json point structures/8IJX/8ijx_protein.pdb structures/8IJX/8ijx_pocket.pdb structures/8IJX/8ijx_ligand.sdf structures/8IJX/8ijx_ligand.pdb structures/8IJX/8ijx_ligand.cif structures/8IJX/8ijx_complex.pdb structures/8IJX/8ijx_complex.cif 8ILR classic PI3Kalpha Na p110alpha/p85alpha complex expressed using a baculovirus FastBac dual vector; N-terminal 6xHis tag on p110alpha WT (wild-type) compound 16 (cpd16) "[""7TZ""]" 1 Kd Kd = = 915 nM 915.0 [] unit_conversion 6.0385789059335515 success True direct_binding Surface plasmon resonance (SPR) measurement using purified PI3Kα complex. 4 Fig. 3 caption: “SPR sensorgrams demonstrate that cpd16 ... bind[s] to PI3Kα with binding affinities of 915 nM ... respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ILR\8ILR_metadata.json point structures/8ILR/8ilr_protein.pdb structures/8ILR/8ilr_pocket.pdb structures/8ILR/8ilr_ligand.sdf structures/8ILR/8ilr_ligand.pdb structures/8ILR/8ilr_ligand.cif structures/8ILR/8ilr_complex.pdb structures/8ILR/8ilr_complex.cif 8ILS classic PI3Kalpha Na p110alpha/p85alpha complex expressed using a baculovirus FastBac dual vector; N-terminal 6xHis tag on p110alpha WT (wild-type) compound 17 (cpd17) "[""7U5""]" 1 Kd Kd = = 347 nM 347.0 [] unit_conversion 6.459670525209127 success True direct_binding Surface plasmon resonance (SPR) measurement using purified PI3Kα complex. 3 Text states that SPR “demonstrated that cpd17 binds to PI3Kα with an affinity (K_D) of 347 nM”; Fig. 2 caption also states a binding affinity of 347 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8ILS\8ILS_metadata.json point structures/8ILS/8ils_protein.pdb structures/8ILS/8ils_pocket.pdb structures/8ILS/8ils_ligand.sdf structures/8ILS/8ils_ligand.pdb structures/8ILS/8ils_ligand.cif structures/8ILS/8ils_complex.pdb structures/8ILS/8ils_complex.cif 8ILV classic PI3Kalpha Na p110alpha/p85alpha complex expressed using a baculovirus FastBac dual vector; N-terminal 6xHis tag on p110alpha WT (wild-type) compound 18 (cpd18) "[""L2V""]" 1 Kd Kd = = 6.30 μM 6300.0 [] unit_conversion 5.200659450546418 success True direct_binding Surface plasmon resonance (SPR) measurement using purified PI3Kα complex. 4 Fig. 3 caption: “SPR sensorgrams demonstrate that cpd16 (A) and cpd18 (B) bind to PI3Kα with binding affinities of 915 nM and 6.30 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ILV\8ILV_metadata.json point structures/8ILV/8ilv_protein.pdb structures/8ILV/8ilv_pocket.pdb structures/8ILV/8ilv_ligand.sdf structures/8ILV/8ilv_ligand.pdb structures/8ILV/8ilv_ligand.cif structures/8ILV/8ilv_complex.pdb structures/8ILV/8ilv_complex.cif 8IM2 classic human HPPD human recombinant human HPPD wild type NTBC "[""NTD""]" 2 Ki Ki = = 6.06 ± 0.44 nM 6.06 [] unit_conversion 8.217527375833713 success True biochemical_inhibition Slow-binding inhibition kinetics of human HPPD with NTBC. 6 The inhibition-kinetics text reports for NTBC: Ki = 6.06 ± 0.44 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8IM2\8IM2_metadata.json point structures/8IM2/8im2_protein.pdb structures/8IM2/8im2_pocket.pdb structures/8IM2/8im2_ligand.sdf structures/8IM2/8im2_ligand.pdb structures/8IM2/8im2_ligand.cif structures/8IM2/8im2_complex.pdb structures/8IM2/8im2_complex.cif 8IM3 classic human HPPD human recombinant human HPPD wild type compound a10 "[""92U""]" 2 Ki Ki = = 0.88 ± 0.07 nM 0.88 [] unit_conversion 9.05551732784983 success True biochemical_inhibition Slow-binding inhibition kinetics of human HPPD with compound a10. 6 The inhibition-kinetics text reports for compound a10: Ki = 0.88 ± 0.07 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8IM3\8IM3_metadata.json point structures/8IM3/8im3_protein.pdb structures/8IM3/8im3_pocket.pdb structures/8IM3/8im3_ligand.sdf structures/8IM3/8im3_ligand.pdb structures/8IM3/8im3_ligand.cif structures/8IM3/8im3_complex.pdb structures/8IM3/8im3_complex.cif 8INX classic SARS-CoV-2 Main Protease (Mpro) Na Na G15S ensitrelvir "[""7YY""]" 1 IC50 IC50 = = 0.048 ± 0.002 µM 48.0 [] unit_conversion 7.318758762624412 success True biochemical_inhibition FRET-based in-vitro enzyme-inhibition assay of SARS-CoV-2 Mpro G15S. 4 Figure 3a reports G15S ensitrelvir IC50 0.048 ± 0.002 µM, and page 6 explicitly maps 8INX to G15S-ensitrelvir. auto_single_measurement only accepted activity measurement [1] 1 structures\8INX\8INX_metadata.json point structures/8INX/8inx_protein.pdb structures/8INX/8inx_pocket.pdb structures/8INX/8inx_ligand.sdf structures/8INX/8inx_ligand.pdb structures/8INX/8inx_ligand.cif structures/8INX/8inx_complex.pdb structures/8INX/8inx_complex.cif 8INY classic SARS-CoV-2 Main Protease (Mpro) Na Na K90R ensitrelvir "[""7YY""]" 1 IC50 IC50 = = 0.048 ± 0.001 µM 48.0 [] unit_conversion 7.318758762624412 success True biochemical_inhibition FRET-based in vitro enzyme-inhibition assay; Fig. 3a. 4 Fig. 3a prints K90R IC50 = 0.048 ± 0.001 µM for ensitrelvir; page 6 maps 8INY to K90R-ensitrelvir. auto_single_measurement only accepted activity measurement [1] 1 structures\8INY\8INY_metadata.json point structures/8INY/8iny_protein.pdb structures/8INY/8iny_pocket.pdb structures/8INY/8iny_ligand.sdf structures/8INY/8iny_ligand.pdb structures/8INY/8iny_ligand.cif structures/8INY/8iny_complex.pdb structures/8INY/8iny_complex.cif 8IPK classic human mitochondrial methyltransferase METTL15 Homo sapiens METTL15 residues 70-407 Na S-adenosyl methionine (SAM) "[""SAM""]" 1 Kd Kd = = 2.99 ± 0.36 µM 2990.0 [] unit_conversion 5.52432881167557 success True direct_binding ITC measurement of SAM binding to WT METTL15; Table 2 reports METTL15WT with SAM. 5 Table 2 lists METTL15WT with SAM and K_D 2.99 ± 0.36 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8IPK\8IPK_metadata.json point structures/8IPK/8ipk_protein.pdb structures/8IPK/8ipk_pocket.pdb structures/8IPK/8ipk_ligand.sdf structures/8IPK/8ipk_ligand.pdb structures/8IPK/8ipk_ligand.cif structures/8IPK/8ipk_complex.pdb structures/8IPK/8ipk_complex.cif 8IPW classic MavL Legionella pneumophila MavL residues 40-404 Na ADPR "[""AR6""]" 1 Kd Kd = = 25.01 ± 3.24 µM 25010.0 [] unit_conversion 4.601886308269497 success True direct_binding Low-volume Nano ITC at 20 °C; wild-type MavL binding to ADPR. 2 Table c prints MavL_WT/ADPR Kd = 25.01 ± 3.24 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8IPW\8IPW_metadata.json point structures/8IPW/8ipw_protein.pdb structures/8IPW/8ipw_pocket.pdb structures/8IPW/8ipw_ligand.sdf structures/8IPW/8ipw_ligand.pdb structures/8IPW/8ipw_ligand.cif structures/8IPW/8ipw_complex.pdb structures/8IPW/8ipw_complex.cif 8IR2 extended SLF1 Na SLF1 tBRCT residues 1-199; Rad18 peptide Na Rad18-2P (Rad18 peptide containing pS442 and pS444) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.015 ± 0.003 µM 15.0 [] unit_conversion 7.823908740944319 success True direct_binding Isothermal titration calorimetry (ITC) of WT SLF1 tBRCT with Rad18-2P. 3 Table 1 reports WT SLF1 tBRCT with Rad18-2P: KD 0.015 ± 0.003 µM; page 9 maps the SLF1 tBRCT–Rad18-2P structure to PDB 8IR2. auto_single_measurement only accepted activity measurement [1] 1 structures\8IR2\8IR2_metadata.json point structures/8IR2/8ir2_protein.pdb structures/8IR2/8ir2_pocket.pdb structures/8IR2/8ir2_ligand.pdb structures/8IR2/8ir2_ligand.cif structures/8IR2/8ir2_complex.pdb structures/8IR2/8ir2_complex.cif 8IR4 extended SLF1 Na SLF1 tBRCT residues 1-199; Rad18 peptide Na Rad18-pS442 (Rad18 peptide containing pS442) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.156 ± 0.005 µM 156.0 [] unit_conversion 6.806875401645538 success True direct_binding Isothermal titration calorimetry (ITC) of WT SLF1 tBRCT with Rad18-pS442. 3 Table 1 reports WT SLF1 tBRCT with Rad18-pS442: KD 0.156 ± 0.005 µM; page 9 maps the SLF1 tBRCT–Rad18-pS442 structure to PDB 8IR4. auto_single_measurement only accepted activity measurement [1] 1 structures\8IR4\8IR4_metadata.json point structures/8IR4/8ir4_protein.pdb structures/8IR4/8ir4_pocket.pdb structures/8IR4/8ir4_ligand.pdb structures/8IR4/8ir4_ligand.cif structures/8IR4/8ir4_complex.pdb structures/8IR4/8ir4_complex.cif 8ISN extended HLA-A24 Na FLAG-tagged HLA-A24 ectodomain co-expressed with beta-2 microglobulin Met2P to Tyr2P substitution in the mWT1 peptide modified 9mer WT1 peptide (mWT1; CYTWNQMNL) "[""CHAIN:C"", ""CHAIN:F""]" 1 Kd Kd = = 483 nM 483.0 [] unit_conversion 6.316052869248487 success True direct_binding ITC measurement of mWT1 peptide binding to A24 at 298 K. 8 “This experimental affinity was determined by ITC … dissociation constant, Kd = 483 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ISN\8ISN_metadata.json point structures/8ISN/8isn_protein.pdb structures/8ISN/8isn_pocket.pdb structures/8ISN/8isn_ligand.pdb structures/8ISN/8isn_ligand.cif structures/8ISN/8isn_complex.pdb structures/8ISN/8isn_complex.cif 8IT9 classic FTO Na FTOΔN31 Na compound 22 "[""ZL6""]" 1 IC50 IC50 = = 16.8 ± 0.9 μM 16800.0 [] unit_conversion 4.774690718274137 success True biochemical_inhibition PAGE-based FTO RNA-demethylase inhibition assay using FTOΔN31. 7 Figure 2A explicitly reports “IC50 = 16.8 ± 0.9 μM” for compound 22; the caption identifies this as FTO inhibition in a PAGE-based assay. Figure 4 identifies compound 22 as the ligand in the FTO/22 complex (PDB 8IT9). auto_single_measurement only accepted activity measurement [1] 1 structures\8IT9\8IT9_metadata.json point structures/8IT9/8it9_protein.pdb structures/8IT9/8it9_pocket.pdb structures/8IT9/8it9_ligand.sdf structures/8IT9/8it9_ligand.pdb structures/8IT9/8it9_ligand.cif structures/8IT9/8it9_complex.pdb structures/8IT9/8it9_complex.cif 8IV3 classic SARS-CoV-2 N protein N-terminal domain (N-NTD) SARS-CoV-2 N-NTD fragment, residues 41-174 Na P3; 5-benzyloxygramine "[""DJU""]" 1 Kd Kd = = 47.07 µM 47070.0 [] unit_conversion 4.327255801693401 success True direct_binding Fluorescence-quenching titration of purified SARS-CoV-2 N-NTD with P3; binding constant fitted using the Hill equation. 5 “The KD values for the SARS-CoV-2 N protein and N-NTD were 23.18 µM and 47.07 µM, respectively (Fig. 2).” Figure 2A identifies the N-NTD measurement as KD = 47.07 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8IV3\8IV3_metadata.json point structures/8IV3/8iv3_protein.pdb structures/8IV3/8iv3_pocket.pdb structures/8IV3/8iv3_ligand.sdf structures/8IV3/8iv3_ligand.pdb structures/8IV3/8iv3_ligand.cif structures/8IV3/8iv3_complex.pdb structures/8IV3/8iv3_complex.cif 8IVG classic Keap1 Na Na Na compound 9 "[""SGO""]" 1 IC50 IC50 = = 39 µM 39000.0 [] unit_conversion 4.4089353929735005 success True biochemical_inhibition Biacore Keap1–Nrf2 PPI inhibition assay; mean from four replicates. 2 Table 1 lists compound 9 with IC50 39 µM; the table footnote states values were determined using a Biacore assay. Figure 2 identifies compound 9 as PDB 8IVG. auto_single_measurement only accepted activity measurement [1] 1 structures\8IVG\8IVG_metadata.json point structures/8IVG/8ivg_protein.pdb structures/8IVG/8ivg_pocket.pdb structures/8IVG/8ivg_ligand.sdf structures/8IVG/8ivg_ligand.pdb structures/8IVG/8ivg_ligand.cif structures/8IVG/8ivg_complex.pdb structures/8IVG/8ivg_complex.cif 8IVR classic Keap1 Na Na Na compound 13 "[""SIU""]" 1 IC50 IC50 = = 2.8 µM 2800.0 [] unit_conversion 5.552841968657781 success True biochemical_inhibition Biacore Keap1–Nrf2 PPI inhibition assay; mean from four replicates. 3 Table 2 lists compound 13 with IC50 2.8 µM; its footnote specifies the Biacore assay. Figure 3 identifies compound 13 as PDB 8IVR. auto_single_measurement only accepted activity measurement [1] 1 structures\8IVR\8IVR_metadata.json point structures/8IVR/8ivr_protein.pdb structures/8IVR/8ivr_pocket.pdb structures/8IVR/8ivr_ligand.sdf structures/8IVR/8ivr_ligand.pdb structures/8IVR/8ivr_ligand.cif structures/8IVR/8ivr_complex.pdb structures/8IVR/8ivr_complex.cif 8IVU classic NAMPT human NAMPT residues 8-142 and 153-483 Na A4276 "[""SJ6""]" 1 IC50 IC50 = = 492 nM 492.0 [] unit_conversion 6.308034897232639 success True biochemical_inhibition Purified NAMPT activity assay measuring concentration-dependent inhibition of NAD+ synthesis by A4276. 5 Figure 2A visibly prints “IC₅₀ = 492 nM”; its caption states that the assay confirms concentration-dependent inhibition of NAD+ synthesis by A4276. The main text identifies this as purified NAMPT treated with A4276. auto_single_measurement only accepted activity measurement [1] 1 structures\8IVU\8IVU_metadata.json point structures/8IVU/8ivu_protein.pdb structures/8IVU/8ivu_pocket.pdb structures/8IVU/8ivu_ligand.sdf structures/8IVU/8ivu_ligand.pdb structures/8IVU/8ivu_ligand.cif structures/8IVU/8ivu_complex.pdb structures/8IVU/8ivu_complex.cif 8IX9 classic PaKPR2 (ketopantoate reductase 2) Pseudomonas aeruginosa Second panE copy from P. aeruginosa UCB(A) PA-14, cloned into pET28a(+) and expressed in E. coli BL21(DE3) wild-type NADPH "[""NDP""]" 1 Kd Kd = = 7.68 ± 0.5 µM 7680.0 [] unit_conversion 5.114638779968487 success True direct_binding Isothermal titration calorimetry of wild-type PaKPR2 with NADPH; binary protein-ligand interaction at 25 °C (Table 3). 8 Table 3 reports PaKPR2–NADPH Kd = 7.68 ± 0.5 µM. The ITC methods describe direct binding measurements of wild-type PaKPR2 and ligands. auto_single_measurement only accepted activity measurement [1] 1 structures\8IX9\8IX9_metadata.json point structures/8IX9/8ix9_protein.pdb structures/8IX9/8ix9_pocket.pdb structures/8IX9/8ix9_ligand.sdf structures/8IX9/8ix9_ligand.pdb structures/8IX9/8ix9_ligand.cif structures/8IX9/8ix9_complex.pdb structures/8IX9/8ix9_complex.cif 8IXH classic PaKPR2 (ketopantoate reductase 2) Pseudomonas aeruginosa Second panE copy from P. aeruginosa UCB(A) PA-14, cloned into pET28a(+) and expressed in E. coli BL21(DE3) wild-type 3-methyl-2-oxovalerate (3-methyl-2-ketopentanoate; KIL) "[""1QQ""]" 1 Kd Kd = = 15.41 ± 3.7 µM 15410.0 [] unit_conversion 4.812197361281581 success True direct_binding Isothermal titration calorimetry of wild-type PaKPR2 with 3-methyl-2-ketopentanoate/KIL; binary protein-ligand interaction at 25 °C (Table 3). 8 Table 3 reports PaKPR2–3-methyl-2-ketopentanoate Kd = 15.41 ± 3.7 µM. The paper identifies KIL as 3-methyl-2-ketopentanoate and maps its binary complex to PDB 8IXH. auto_single_measurement only accepted activity measurement [1] 1 structures\8IXH\8IXH_metadata.json point structures/8IXH/8ixh_protein.pdb structures/8IXH/8ixh_pocket.pdb structures/8IXH/8ixh_ligand.sdf structures/8IXH/8ixh_ligand.pdb structures/8IXH/8ixh_ligand.cif structures/8IXH/8ixh_complex.pdb structures/8IXH/8ixh_complex.cif 8IXS classic Keap1 Na Na Na compound 25 "[""T6I""]" 1 IC50 IC50 = = 0.089 µM 89.0 [] unit_conversion 7.050609993355087 success True biochemical_inhibition Biacore Keap1–Nrf2 PPI inhibition assay; mean from four replicates. 5 Table 3 lists compound 25 with IC50 0.089 µM; its footnote specifies the Biacore assay. Figure 5 identifies compound 25 as PDB 8IXS. auto_single_measurement only accepted activity measurement [1] 1 structures\8IXS\8IXS_metadata.json point structures/8IXS/8ixs_protein.pdb structures/8IXS/8ixs_pocket.pdb structures/8IXS/8ixs_ligand.sdf structures/8IXS/8ixs_ligand.pdb structures/8IXS/8ixs_ligand.cif structures/8IXS/8ixs_complex.pdb structures/8IXS/8ixs_complex.cif 8IXZ classic Acb2 Pseudomonas aeruginosa phage PaMx33 Na Na 3',2'-cGAMP "[""4UR""]" 1 Kd Kd = = 297.7 ± 56.1 nM 297.7 [] unit_conversion 6.526221165353276 success True direct_binding ITC binding assay 19 Figure 1A reports the ITC K_D for 3',2'-cGAMP binding to PaMx33-Acb2 as 297.7 ± 56.1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8IXZ\8IXZ_metadata.json point structures/8IXZ/8ixz_protein.pdb structures/8IXZ/8ixz_pocket.pdb structures/8IXZ/8ixz_ligand.sdf structures/8IXZ/8ixz_ligand.pdb structures/8IXZ/8ixz_ligand.cif structures/8IXZ/8ixz_complex.pdb structures/8IXZ/8ixz_complex.cif 8IY0 classic Acb2 Pseudomonas aeruginosa phage PaMx33 Na Na cAAA (cA3; 3',3',3'-cAAA) "[""3AM""]" 1 Kd Kd = = 1.5 ± 0.3 nM 1.5 [] unit_conversion 8.823908740944319 success True direct_binding ITC binding assay 20 Figure 2A reports cA3 binding to PaMx33-Acb2 with K_D 1.5 ± 0.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8IY0\8IY0_metadata.json point structures/8IY0/8iy0_protein.pdb structures/8IY0/8iy0_pocket.pdb structures/8IY0/8iy0_ligand.sdf structures/8IY0/8iy0_ligand.pdb structures/8IY0/8iy0_ligand.cif structures/8IY0/8iy0_complex.pdb structures/8IY0/8iy0_complex.cif 8J2V classic NbUGT72AY1 Nicotiana benthamiana NbUGT72AY1 expressed as an N-terminal GST fusion; GST tag removed before crystallization Na scopoletin "[""T83""]" 1 Kd Kd = = 4.5 ± 1.1 µM 4500.0 [] unit_conversion 5.346787486224656 success True direct_binding Isothermal titration calorimetry of purified NbUGT72AY1 and scopoletin; 1:1 protein:scopoletin stoichiometry. 7 “Isothermal titration calorimetry (ITC) measurements confirmed a 1:1 stoichiometry of protein and scopoletin and yielded a K_D of 4.5 ± 1.1 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8J2V\8J2V_metadata.json point structures/8J2V/8j2v_protein.pdb structures/8J2V/8j2v_pocket.pdb structures/8J2V/8j2v_ligand.sdf structures/8J2V/8j2v_ligand.pdb structures/8J2V/8j2v_ligand.cif structures/8J2V/8j2v_complex.pdb structures/8J2V/8j2v_complex.cif 8J2W classic SasPcob Saccharothrix syringae Na Na AdoCbl (adenosylcobalamin); biliverdin IX alpha (BV) "[""BLA""]" 1 Kd Kd = = 0.7 ± 0.04 μM 700.0 [] unit_conversion 6.154901959985743 success True direct_binding BV absorbance titration at 700 nm with AdoCbl-pre-bound SasPcob; Fig. 3e. 4 Fig. 3e prints “Kd = 0.7 ± 0.04 μM”; its caption specifies BV binding with AdoCbl pre-bound. auto_single_measurement only accepted activity measurement [1] 1 structures\8J2W\8J2W_metadata.json point structures/8J2W/8j2w_protein.pdb structures/8J2W/8j2w_pocket.pdb structures/8J2W/8j2w_ligand.sdf structures/8J2W/8j2w_ligand.pdb structures/8J2W/8j2w_ligand.cif structures/8J2W/8j2w_complex.pdb structures/8J2W/8j2w_complex.cif 8J3S extended human cytomegalovirus protease (HCMVPro) human cytomegalovirus Na Na macrocyclic peptide 1 "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G""]" 1 IC50 IC50 = = 0.0015 µM 1.5 [] unit_conversion 8.823908740944319 success True biochemical_inhibition Cell-free HCMVPro inhibition assay. 3 “peptide 1 was identified as a hit peptide that exhibited cell-free IC50 = 0.0015 µM”. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\8J3S\8J3S_metadata.json point structures/8J3S/8j3s_protein.pdb structures/8J3S/8j3s_pocket.pdb structures/8J3S/8j3s_ligand.pdb structures/8J3S/8j3s_ligand.cif structures/8J3S/8j3s_complex.pdb structures/8J3S/8j3s_complex.cif 8J3T classic human cytomegalovirus protease (HCMVPro) human cytomegalovirus Na Na compound 19 "[""T1F""]" 1 IC50 IC50 = = 2.5 µM 2500.0 [] unit_conversion 5.6020599913279625 success True biochemical_inhibition Cell-free HCMVPro inhibition assay. 5 Table 1 reports compound 19 HCMVPro cell-free IC50 “2.5” µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8J3T\8J3T_metadata.json point structures/8J3T/8j3t_protein.pdb structures/8J3T/8j3t_pocket.pdb structures/8J3T/8j3t_ligand.sdf structures/8J3T/8j3t_ligand.pdb structures/8J3T/8j3t_ligand.cif structures/8J3T/8j3t_complex.pdb structures/8J3T/8j3t_complex.cif 8J40 classic CatB8 chloramphenicol acetyltransferase Acinetobacter baumannii Full-length CatB8 with a C-terminal His6 tag Na chloramphenicol (chl) "[""CLM""]" 1 Kd Kd = = 250.3 ± 40.87 μM 250300.0 [] unit_conversion 3.601539150391777 success True direct_binding Isothermal titration calorimetry (ITC) measurement of CatB8 wild type binding to chloramphenicol; Figure 6 panel A. 5 Figure 6 caption states: “Binding affinity of CatB8 with chloride was measured by isothermal titration calorimetry (ITC). Compared to the equilibrium dissociation constant (Kd) of the CatB8 wt (A), 250.3 ± 40.87 μM …” The figure and surrounding text identify the ligand as chl (chloramphenicol). auto_single_measurement only accepted activity measurement [1] 1 structures\8J40\8J40_metadata.json point structures/8J40/8j40_protein.pdb structures/8J40/8j40_pocket.pdb structures/8J40/8j40_ligand.sdf structures/8J40/8j40_ligand.pdb structures/8J40/8j40_ligand.cif structures/8J40/8j40_complex.pdb structures/8J40/8j40_complex.cif 8J4H classic ferric ion-binding protein A (FbpA) Vibrio metschnikovii Na Na Danshensu (DSS) "[""TO9""]" 1 Kd Kd = = 0.9 ± 0.2 µM 900.0 [] unit_conversion 6.045757490560675 success True direct_binding ITC analysis of DSS binding to VmFbpA at 298 K in 20 mM HEPES, pH 8.0, 50 mM NaCl. 7 Figure 6 labels the DSS ITC determination: K_D: 0.9 ± 0.2 µM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8J4H\8J4H_metadata.json point structures/8J4H/8j4h_protein.pdb structures/8J4H/8j4h_pocket.pdb structures/8J4H/8j4h_ligand.sdf structures/8J4H/8j4h_ligand.pdb structures/8J4H/8j4h_ligand.cif structures/8J4H/8j4h_complex.pdb structures/8J4H/8j4h_complex.cif 8J5W classic TrkA Na Na F589L compound 10g; N-(3-cyclopropyl-5-((4-methylpiperazin-1-yl)methyl)phenyl)-4^6-methyl-14-oxo-5-oxa-13-aza-1(3,6)-imidazo[1,2-b]pyridazina-4(1,3)-benzenacyclotetradecaphan-2-yne-4^5-carboxamide "[""A4U""]" 1 IC50 IC50 = = 6.13 ± 0.66 nM 6.13 [] unit_conversion 8.212539525481585 success True biochemical_inhibition FRET-based Z′-LYTE biochemical kinase-inhibition assay. 6 Table 3 reports compound 10g biochemical TRKA F589L IC50 = 6.13 ± 0.66 nM; page 5 maps the TRKA F589L–10g crystal complex to PDB 8J5W. auto_single_measurement only accepted activity measurement [1] 1 structures\8J5W\8J5W_metadata.json point structures/8J5W/8j5w_protein.pdb structures/8J5W/8j5w_pocket.pdb structures/8J5W/8j5w_ligand.sdf structures/8J5W/8j5w_ligand.pdb structures/8J5W/8j5w_ligand.cif structures/8J5W/8j5w_complex.pdb structures/8J5W/8j5w_complex.cif 8J5X classic TrkA Na Na G595R compound 10g; N-(3-cyclopropyl-5-((4-methylpiperazin-1-yl)methyl)phenyl)-4^6-methyl-14-oxo-5-oxa-13-aza-1(3,6)-imidazo[1,2-b]pyridazina-4(1,3)-benzenacyclotetradecaphan-2-yne-4^5-carboxamide "[""A4U""]" 1 IC50 IC50 = = 6.77 ± 0.44 nM 6.77 [] unit_conversion 8.169411331314855 success True biochemical_inhibition FRET-based Z′-LYTE biochemical kinase-inhibition assay. 6 Table 3 reports compound 10g biochemical TRKA G595R IC50 = 6.77 ± 0.44 nM; page 5 maps the TRKA G595R–10g crystal complex to PDB 8J5X. auto_single_measurement only accepted activity measurement [1] 1 structures\8J5X\8J5X_metadata.json point structures/8J5X/8j5x_protein.pdb structures/8J5X/8j5x_pocket.pdb structures/8J5X/8j5x_ligand.sdf structures/8J5X/8j5x_ligand.pdb structures/8J5X/8j5x_ligand.cif structures/8J5X/8j5x_complex.pdb structures/8J5X/8j5x_complex.cif 8J61 classic TrkA Na Na wild-type compound 8f; 4^6-methyl-N-(3-(4-methyl-1H-imidazol-1-yl)-5-(trifluoromethyl)phenyl)-14-oxo-5-oxa-13-aza-1(3,6)-imidazo[1,2-b]pyridazina-4(1,3)-benzenacyclotetradecaphan-2-yne-4^5-carboxamide "[""A0X""]" 1 IC50 IC50 = = 33.36 nM 33.36 [] unit_conversion 7.476773958034299 success True biochemical_inhibition FRET-based Z′-LYTE biochemical kinase-inhibition assay. 3 Table 1 reports compound 8f biochemical wild-type TRKA IC50 = 33.36 nM; page 4 identifies the wild-type TRKA–8f crystal structure as PDB 8J61. auto_single_measurement only accepted activity measurement [1] 1 structures\8J61\8J61_metadata.json point structures/8J61/8j61_protein.pdb structures/8J61/8j61_pocket.pdb structures/8J61/8j61_ligand.sdf structures/8J61/8j61_ligand.pdb structures/8J61/8j61_ligand.cif structures/8J61/8j61_complex.pdb structures/8J61/8j61_complex.cif 8J63 classic TrkA Na Na wild-type compound 8c; 4^6-methyl-N-(3-(4-methyl-1H-imidazol-1-yl)-5-(trifluoromethyl)phenyl)-11-oxo-5-oxa-10,14-diaza-1(3,6)-imidazo[1,2-b]pyridazina-4(1,3)-benzenacyclotetradecaphan-2-yne-4^5-carboxamide "[""A6X""]" 1 IC50 IC50 = = 21.03 nM 21.03 [] unit_conversion 7.677160727313678 success True biochemical_inhibition FRET-based Z′-LYTE biochemical kinase-inhibition assay. 3 Table 1 reports compound 8c biochemical wild-type TRKA IC50 = 21.03 nM; page 4 identifies the wild-type TRKA–8c crystal structure as PDB 8J63. auto_single_measurement only accepted activity measurement [1] 1 structures\8J63\8J63_metadata.json point structures/8J63/8j63_protein.pdb structures/8J63/8j63_pocket.pdb structures/8J63/8j63_ligand.sdf structures/8J63/8j63_ligand.pdb structures/8J63/8j63_ligand.cif structures/8J63/8j63_complex.pdb structures/8J63/8j63_complex.cif 8J8E extended human serum albumin human Na Na 5b "[""U5U""]" 1 Kd Kd = = 3.28 μM 3280.0 [] unit_conversion 5.484126156288321 success True direct_binding Surface plasmon resonance (SPR); equilibrium dissociation constant for 5b binding to HSA. 4 “The results of SPR showed that 5b binds to HSA, yielding the equilibrium dissociation constant K_D = 3.28 μM (Figure 3A,B).” auto_single_measurement only accepted activity measurement [1] 1 structures\8J8E\8J8E_metadata.json point structures/8J8E/8j8e_protein.pdb structures/8J8E/8j8e_pocket.pdb structures/8J8E/8j8e_ligand.pdb structures/8J8E/8j8e_ligand.cif structures/8J8E/8j8e_complex.pdb structures/8J8E/8j8e_complex.cif 8J8J classic Rv3806c membrane-bound phosphoribosyltransferase (PRTase) Mycobacterium tuberculosis Na Na PRPP (5-phospho-alpha-D-ribose-1-diphosphate) "[""PRP""]" 1 Kd Kd = = 12.87 ± 3.33 µM 12870.0 [] unit_conversion 4.890421453095613 success True direct_binding Microscale thermophoresis (MST), Rv3806c + PRPP + Mg2+. 19 Extended Data Fig. 6a reports “Rv3806c+PRPP+Mg2+ 12.87 ± 3.33 µM”. auto_single_measurement only accepted activity measurement [1] 1 structures\8J8J\8J8J_metadata.json point structures/8J8J/8j8j_protein.pdb structures/8J8J/8j8j_pocket.pdb structures/8J8J/8j8j_ligand.sdf structures/8J8J/8j8j_ligand.pdb structures/8J8J/8j8j_ligand.cif structures/8J8J/8j8j_complex.pdb structures/8J8J/8j8j_complex.cif 8J8M classic LAT1-4F2hc complex human Full-length human LAT1 with N-terminal FLAG tag coexpressed with human 4F2hc isoform b bearing an N-terminal 10xHis tag Na L-tryptophan (L-Trp) "[""TRP""]" 1 Kd Kd = = 61.25 ± 17.98 μM 61250.0 [] unit_conversion 4.21289390696343 success True direct_binding Microscale thermophoresis using purified WT LAT1 coexpressed with 4F2hc; Trp was serially diluted from a 30 mM stock to 16 concentrations, mixtures equilibrated at 4 °C for 10 min; n = 3. 5 Figure 3D explicitly reports “WT K_D: 61.25±17.98 μM” for Trp; the Figure 3 caption identifies this as an affinity measurement for WT LAT1 protein, and the methods describe the MST assay with LAT1 coexpressed with 4F2hc. auto_single_measurement only accepted activity measurement [1] 1 structures\8J8M\8J8M_metadata.json point structures/8J8M/8j8m_protein.pdb structures/8J8M/8j8m_pocket.pdb structures/8J8M/8j8m_ligand.sdf structures/8J8M/8j8m_ligand.pdb structures/8J8M/8j8m_ligand.cif structures/8J8M/8j8m_complex.pdb structures/8J8M/8j8m_complex.cif 8JAO classic IMP-1 Na Na Na compound 41 (2-amino-5-phenethylthiazole-4-carboxylic acid) "[""5ZX""]" 1 IC50 IC50 = = 0.38 μM 380.0 [] unit_conversion 6.42021640338319 success True biochemical_inhibition Purified-enzyme inhibition assay; Table 3, B1 MBL IMP-1 column. 8 Table 3 reports compound 41 with IMP-1 IC50/LE of 0.38 μM/0.50; Figure 8 and the accession list map compound 41 to IMP-1 structure 8JAO. auto_single_measurement only accepted activity measurement [1] 1 structures\8JAO\8JAO_metadata.json point structures/8JAO/8jao_protein.pdb structures/8JAO/8jao_pocket.pdb structures/8JAO/8jao_ligand.sdf structures/8JAO/8jao_ligand.pdb structures/8JAO/8jao_ligand.cif structures/8JAO/8jao_complex.pdb structures/8JAO/8jao_complex.cif 8JBA classic PD-L1 Na PD-L1 residues 18-134 with a C-terminal His tag Na LP23 "[""AU9""]" 1 Kd Kd = = 11.4 nM 11.4 [] unit_conversion 7.943095148663527 success True direct_binding SPR binding assay between LP23 and human PD-L1. 6 Figure 3A and accompanying text report: “LP23-Human PD-L1 K_D = 11.4 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8JBA\8JBA_metadata.json point structures/8JBA/8jba_protein.pdb structures/8JBA/8jba_pocket.pdb structures/8JBA/8jba_ligand.sdf structures/8JBA/8jba_ligand.pdb structures/8JBA/8jba_ligand.cif structures/8JBA/8jba_complex.pdb structures/8JBA/8jba_complex.cif 8JBN classic Vascular endothelial protein tyrosine phosphatase (VE-PTP) Human VE-PTP residues 1686-1971 with N-terminal 6xHis-GST tags and HRV 3C cleavage sequence; fusion tag cleaved before final purification Na Cpd-1 "[""U7C""]" 2 Kd Kd = = 39 µM 39000.0 [] unit_conversion 4.4089353929735005 success True direct_binding Protein-observed 15N–1H HSQC NMR chemical-shift perturbation analysis. 4 The selected shifted amino-acid peaks yielded a KD of 39 µM from chemical-shift perturbation analysis for Cpd-1 binding to VE-PTP. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8JBN\8JBN_metadata.json point structures/8JBN/8jbn_protein.pdb structures/8JBN/8jbn_pocket.pdb structures/8JBN/8jbn_ligand.sdf structures/8JBN/8jbn_ligand.pdb structures/8JBN/8jbn_ligand.cif structures/8JBN/8jbn_complex.pdb structures/8JBN/8jbn_complex.cif 8JBW classic ZtHPPD (4-hydroxyphenylpyruvate dioxygenase) Zymoseptoria tritici Na Na (+)-Usnic acid "[""AIY""]" 2 Ki Ki = = 113 ± 11 nM 113.0 [] unit_conversion 6.94692155651658 success True biochemical_inhibition ZtHPPD inhibitor kinetic assay fitted using the corresponding equations; Table 2 kinetic parameters. 6 Table 2, “Inhibitory Kinetic Parameters of Inhibitors on ZtHPPD,” reports (+)-Usnic acid Ki = 113 ± 11 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8JBW\8JBW_metadata.json point structures/8JBW/8jbw_protein.pdb structures/8JBW/8jbw_pocket.pdb structures/8JBW/8jbw_ligand.sdf structures/8JBW/8jbw_ligand.pdb structures/8JBW/8jbw_ligand.cif structures/8JBW/8jbw_complex.pdb structures/8JBW/8jbw_complex.cif 8JBY classic Vascular endothelial protein tyrosine phosphatase (VE-PTP) Human VE-PTP residues 1686-1971 with N-terminal 6xHis-GST tags and HRV 3C cleavage sequence; fusion tag cleaved before final purification Na Cpd-2 "[""U7L""]" 1 IC50 IC50 = = 0.91 µM 910.0 [] unit_conversion 6.040958607678906 success True biochemical_inhibition Fluorescence-based VE-PTP enzyme-activity assay. 5 Table 1 reports a VE-PTP IC50 of 0.91 µM for Cpd-2; the table footnote states that inhibitory activities were measured by the fluorescence-based assay described in Materials and Methods. auto_single_measurement only accepted activity measurement [1] 1 structures\8JBY\8JBY_metadata.json point structures/8JBY/8jby_protein.pdb structures/8JBY/8jby_pocket.pdb structures/8JBY/8jby_ligand.sdf structures/8JBY/8jby_ligand.pdb structures/8JBY/8jby_ligand.cif structures/8JBY/8jby_complex.pdb structures/8JBY/8jby_complex.cif 8JF4 classic AURKA human Na Na compound 9 "[""C0N""]" 1 IC50 IC50 = = 26.8 nM 26.8 [] unit_conversion 7.5718652059712115 success True biochemical_inhibition In vitro AURKA inhibition potency shown in Figure 5A. 6 Figure 5A labels compound 9 as “9 (26.8 nM)”; the caption identifies this as in vitro inhibition potency. Figure 5C caption maps AURKA kinase domain–9 to PDB ID 8JF4. auto_single_measurement only accepted activity measurement [1] 1 structures\8JF4\8JF4_metadata.json point structures/8JF4/8jf4_protein.pdb structures/8JF4/8jf4_pocket.pdb structures/8JF4/8jf4_ligand.sdf structures/8JF4/8jf4_ligand.pdb structures/8JF4/8jf4_ligand.cif structures/8JF4/8jf4_complex.pdb structures/8JF4/8jf4_complex.cif 8JFA classic 3-oxoacyl-ACP reductase FabG Helicobacter pylori full-length recombinant FabG Na NADPH "[""NAP""]" 1 Kd Kd = = 22.8 µM 22800.0 [] unit_conversion 4.642065152999546 success True direct_binding ITC measurement of NADPH binding to FabG in the absence of ACP. 3 FabG preferentially recognized NADPH; the reported FabG NADPH Kd was 22.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8JFA\8JFA_metadata.json point structures/8JFA/8jfa_protein.pdb structures/8JFA/8jfa_pocket.pdb structures/8JFA/8jfa_ligand.sdf structures/8JFA/8jfa_ligand.pdb structures/8JFA/8jfa_ligand.cif structures/8JFA/8jfa_complex.pdb structures/8JFA/8jfa_complex.cif 8JG8 classic AURKA human Na Na compound 25 "[""C74""]" 1 IC50 IC50 = = 1905 nM 1905.0 [] unit_conversion 5.720105019988361 success True biochemical_inhibition In vitro AURKA inhibition potency shown in Figure 5A. 6 Figure 5A labels compound 25 as “25 (1905 nM)”; the caption identifies this as in vitro inhibition potency. Figure 5D caption maps AURKA kinase domain–25 to PDB ID 8JG8. auto_single_measurement only accepted activity measurement [1] 1 structures\8JG8\8JG8_metadata.json point structures/8JG8/8jg8_protein.pdb structures/8JG8/8jg8_pocket.pdb structures/8JG8/8jg8_ligand.sdf structures/8JG8/8jg8_ligand.pdb structures/8JG8/8jg8_ligand.cif structures/8JG8/8jg8_complex.pdb structures/8JG8/8jg8_complex.cif 8JIG classic UHRF1 human SRA domain, residues 414-617, with a C-terminal His tag Na H93 "[""8JA""]" 1 Kd Kd = = 0.44 ± 0.04 μM 440.0 [] unit_conversion 6.356547323513812 success True direct_binding Isothermal titration calorimetry (ITC) of H93 with UHRF1_SRA. 2 “H93 exhibited strong binding to UHRF1_SRA, with a dissociation constant (Kd) of 0.44 ± 0.04 μM (Fig. 3a).” auto_single_measurement only accepted activity measurement [1] 1 structures\8JIG\8JIG_metadata.json point structures/8JIG/8jig_protein.pdb structures/8JIG/8jig_pocket.pdb structures/8JIG/8jig_ligand.sdf structures/8JIG/8jig_ligand.pdb structures/8JIG/8jig_ligand.cif structures/8JIG/8jig_complex.pdb structures/8JIG/8jig_complex.cif 8JJQ classic SenB Variovorax paradoxus Na Na UDP-GalNAc "[""UD2""]" 1 Kd Kd = = 0.39±0.078 µM 390.0 [] unit_conversion 6.4089353929735005 success True direct_binding Microscale thermophoresis (MST) binding assay of purified SenB with UDP-GalNAc. 2 Fig. 2c prints Kd = 0.39±0.078 µM for UDP-GalNAc; Methods describe MST binding-affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8JJQ\8JJQ_metadata.json point structures/8JJQ/8jjq_protein.pdb structures/8JJQ/8jjq_pocket.pdb structures/8JJQ/8jjq_ligand.sdf structures/8JJQ/8jjq_ligand.pdb structures/8JJQ/8jjq_ligand.cif structures/8JJQ/8jjq_complex.pdb structures/8JJQ/8jjq_complex.cif 8JJT classic SenB Variovorax paradoxus Na Na UDP-GlcNAc "[""UD1""]" 1 Kd Kd = = 0.082±0.028 µM 82.0 [] unit_conversion 7.086186147616283 success True direct_binding Microscale thermophoresis (MST) binding assay of purified SenB with UDP-GlcNAc. 2 Fig. 2c prints Kd = 0.082±0.028 µM for UDP-GlcNAc; Methods describe MST binding-affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8JJT\8JJT_metadata.json point structures/8JJT/8jjt_protein.pdb structures/8JJT/8jjt_pocket.pdb structures/8JJT/8jjt_ligand.sdf structures/8JJT/8jjt_ligand.pdb structures/8JJT/8jjt_ligand.cif structures/8JJT/8jjt_complex.pdb structures/8JJT/8jjt_complex.cif 8JJV extended DeltaNterNb-alpha-syn01 camel N-terminal truncated nanobody, with the first 8 residues removed Na alpha-synuclein peptide (residues 43-56) "[""CHAIN:B""]" 1 Kd Kd = = 76 ± 22.7 nM 76.0 [] unit_conversion 7.119186407719209 success True direct_binding ITC at 25 °C; truncated nanobody–α-syn peptide interaction. 6 “dissociation constants (Kd) at 25°C of 809 ± 8.4 and 76 ± 22.7 nM, for Nbα-syn01 and ΔNterNbα-syn01, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8JJV\8JJV_metadata.json point structures/8JJV/8jjv_protein.pdb structures/8JJV/8jjv_pocket.pdb structures/8JJV/8jjv_ligand.pdb structures/8JJV/8jjv_ligand.cif structures/8JJV/8jjv_complex.pdb structures/8JJV/8jjv_complex.cif 8JLY extended Nb-alpha-syn01 camel Full-length nanobody Nb-alpha-syn01 Na alpha-synuclein peptide (residues 43-56) "[""CHAIN:B""]" 1 Kd Kd = = 809 ± 8.4 nM 809.0 [] unit_conversion 6.092051478387727 success True direct_binding ITC at 25 °C; full-length nanobody–α-syn peptide interaction. 6 “dissociation constants (Kd) at 25°C of 809 ± 8.4 and 76 ± 22.7 nM, for Nbα-syn01 and ΔNterNbα-syn01, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8JLY\8JLY_metadata.json point structures/8JLY/8jly_protein.pdb structures/8JLY/8jly_pocket.pdb structures/8JLY/8jly_ligand.pdb structures/8JLY/8jly_ligand.cif structures/8JLY/8jly_complex.pdb structures/8JLY/8jly_complex.cif 8JMJ extended Helicobacter pylori Soj/ParA (HpParAD41A) with Spo0J/ParB N-terminal peptide Helicobacter pylori HpParA D41A mutant with HpParB N-terminal peptide residues 1-10 (HpParBN10) D41A in HpParA ATP "[""CHAIN:K"", ""CHAIN:L"", ""CHAIN:M"", ""CHAIN:N""]" 1 Kd Kd = = 5.3 ± 1.1 µM 5300.0 [] unit_conversion 5.275724130399211 success True direct_binding Microscale thermophoresis of HpParAD41A–DNA complex with HpParBN10 peptide; the reported Kd is for their interaction. 7 “the interaction between HpParAD41A and HpParBN10 can be measured, with the calculated Kd value of 5.3 ± 1.1 µM (Figure 3B).” auto_single_measurement only accepted activity measurement [1] 1 structures\8JMJ\8JMJ_metadata.json point structures/8JMJ/8jmj_protein.pdb structures/8JMJ/8jmj_pocket.pdb structures/8JMJ/8jmj_ligand.pdb structures/8JMJ/8jmj_ligand.cif structures/8JMJ/8jmj_complex.pdb structures/8JMJ/8jmj_complex.cif 8JMN classic gastric H+,K+-ATPase pig Alpha subunit with N-terminal Flag (DYKDDDDK), hexahistidine, EGFP, and TEV protease recognition sequence inserted before Met48; wild-type beta subunit Na DQ-21 "[""UOU""]" 1 IC50 IC50 = = 0.28 ± 0.02 µM 280.0 [] unit_conversion 6.552841968657781 success True biochemical_inhibition Dose-dependent ATPase-activity inhibition using H+,K+-ATPase-enriched membrane fractions purified from pig stomach. 7 DQ-21 shows an apparent affinity IC50,DQ21 = 0.28 ± 0.02 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8JMN\8JMN_metadata.json point structures/8JMN/8jmn_protein.pdb structures/8JMN/8jmn_pocket.pdb structures/8JMN/8jmn_ligand.sdf structures/8JMN/8jmn_ligand.pdb structures/8JMN/8jmn_ligand.cif structures/8JMN/8jmn_complex.pdb structures/8JMN/8jmn_complex.cif 8JOQ extended human Plk1 polo-box domain (Plk1_PBD) human (Plk1); human papillomavirus type 18 (L2) Plk1 PBD residues 371-594; expressed with an N-terminal His10-MBP tag that was removed by TEV protease Na HPV18 L2 residues 209-215 phosphopeptide with pThr213 "[""CHAIN:B""]" 1 Kd Kd = = 0.763 µM 763.0 [] unit_conversion 6.117475462045119 success True direct_binding Isothermal titration calorimetry (ITC) of HPV18 L2(209–215;pThr213) with His6–MBP–Plk1(371–594). 5 Figure 1C lists HPV18 L2(209–215;pThr213), measured by ITC in this study, with KD 0.763 µM; Figure 1B identifies the WT Plk1(371–594) binding experiment. Table 1 maps the Plk1PBD–HPV18 L2(pThr213) structure to PDB 8JOQ. auto_single_measurement only accepted activity measurement [1] 1 structures\8JOQ\8JOQ_metadata.json point structures/8JOQ/8joq_protein.pdb structures/8JOQ/8joq_pocket.pdb structures/8JOQ/8joq_ligand.pdb structures/8JOQ/8joq_ligand.cif structures/8JOQ/8joq_complex.pdb structures/8JOQ/8joq_complex.cif 8JOW extended rabbit antibody A4 rabbit single-chain variable fragment (scFv) light-chain Cys80Ser phosphorylated Akt peptide (RPHFPQF[pS]YSAS) "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 3.34 ± 0.63 nM 3.34 [] unit_conversion 8.476253533188435 success True direct_binding ITC; A4 WT interacting with phosphopeptide. 4 Table 1 reports A4 WT K_D = 3.34 ± 0.63 nM for phosphopeptides; the paper states binding was quantified by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8JOW\8JOW_metadata.json point structures/8JOW/8jow_protein.pdb structures/8JOW/8jow_pocket.pdb structures/8JOW/8jow_ligand.pdb structures/8JOW/8jow_ligand.cif structures/8JOW/8jow_complex.pdb structures/8JOW/8jow_complex.cif 8JOY extended human Plk1 polo-box domain (Plk1_PBD) human (Plk1); human papillomavirus type 4 (L2) Plk1 PBD residues 371-594; expressed with an N-terminal His10-MBP tag that was removed by TEV protease Na HPV4 L2 residues 251-257 phosphopeptide with pThr255 "[""CHAIN:B""]" 1 Kd Kd = = 1.01 µM 1010.0 [] unit_conversion 5.995678626217357 success True direct_binding Isothermal titration calorimetry (ITC) of HPV4 L2(251–257;pThr255) with His6–MBP–Plk1(371–594). 6 Figure 2B explicitly reports KD = 1.01 µM for HPV4 L2(251–257;pThr255) binding to His6–MBP–Plk1(371–594) by ITC. Table 1 maps the Plk1PBD–HPV4 L2(pThr255) structure to PDB 8JOY. auto_single_measurement only accepted activity measurement [1] 1 structures\8JOY\8JOY_metadata.json point structures/8JOY/8joy_protein.pdb structures/8JOY/8joy_pocket.pdb structures/8JOY/8joy_ligand.pdb structures/8JOY/8joy_ligand.cif structures/8JOY/8joy_complex.pdb structures/8JOY/8joy_complex.cif 8JPQ extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na D-5-96 "[""CHAIN:B""]" 1 IC50 IC50 = = 1.14 ± 0.16 µM 1140.0 [] unit_conversion 5.943095148663527 success True biochemical_inhibition Fluorescence resonance energy transfer (FRET) assay using an Mpro substrate to test in vitro inhibitory activity. 5 The Figure 3B table reports D-5-96 IC50 = 1.14 ± 0.16 µM. Figure 3 caption identifies these as IC50 values; the preceding text states the FRET assay tested in vitro inhibitory activity against SARS-CoV-2 Mpro. auto_single_measurement only accepted activity measurement [1] 1 structures\8JPQ\8JPQ_metadata.json point structures/8JPQ/8jpq_protein.pdb structures/8JPQ/8jpq_pocket.pdb structures/8JPQ/8jpq_ligand.pdb structures/8JPQ/8jpq_ligand.cif structures/8JPQ/8jpq_complex.pdb structures/8JPQ/8jpq_complex.cif 8JSK classic PsPycTIR_CNBD Pseudovibrio sp. N-terminal CNBD truncation, residues 1-150, with a C-terminal His6 tag Na cUMP "[""6SY""]" 1 Kd Kd = = 1.0 × 10⁻⁹ M 1.0 [] unit_conversion 9.0 success True direct_binding Isothermal titration calorimetry of purified N-terminal CNBD truncation with cUMP; 1:1 binding stoichiometry reported. 7 Table 1 reports PsPycTIR_CNBD K_D = 1.0 × 10⁻⁹ M for cUMP; text states nanomolar cUMP binding at 1:1 stoichiometry. auto_single_measurement only accepted activity measurement [1] 1 structures\8JSK\8JSK_metadata.json point structures/8JSK/8jsk_protein.pdb structures/8JSK/8jsk_pocket.pdb structures/8JSK/8jsk_ligand.sdf structures/8JSK/8jsk_ligand.pdb structures/8JSK/8jsk_ligand.cif structures/8JSK/8jsk_complex.pdb structures/8JSK/8jsk_complex.cif 8JUC classic UBE2T Na UBE2T residues 1-154 Na ETC-6705 "[""V23""]" 1 Kd Kd = = 3.20 ± 1.21 mM 3200000.0 [] unit_conversion 2.4948500216800937 success True direct_binding Protein-observed solution NMR titration / 1H-15N-HSQC chemical-shift perturbation experiment. 7 “ETC-6705 interacted with UBE2T with an affinity of approximately 3.2 mM based on a titration experiment monitoring the CSP in the 1H-15N-HSQC spectra of UBE2T.” Figure 1 prints Kd = 3.20 ± 1.21 mM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8JUC\8JUC_metadata.json point structures/8JUC/8juc_protein.pdb structures/8JUC/8juc_pocket.pdb structures/8JUC/8juc_ligand.sdf structures/8JUC/8juc_ligand.pdb structures/8JUC/8juc_ligand.cif structures/8JUC/8juc_complex.pdb structures/8JUC/8juc_complex.cif 8JVD classic UBE2T Na UBE2T residues 1-154 Na ETC-0097 "[""V2R""]" 1 Kd Kd = = 1.20 mM 1200000.0 [] unit_conversion 2.920818753952375 success True direct_binding Solution NMR fragment-binding measurement. 3 Figure 1 explicitly prints for ETC-0097: “Kd = 1.20 mM.” The caption states that dissociation constants were determined using solution NMR spectroscopy. auto_single_measurement only accepted activity measurement [1] 1 structures\8JVD\8JVD_metadata.json point structures/8JVD/8jvd_protein.pdb structures/8JVD/8jvd_pocket.pdb structures/8JVD/8jvd_ligand.sdf structures/8JVD/8jvd_ligand.pdb structures/8JVD/8jvd_ligand.cif structures/8JVD/8jvd_complex.pdb structures/8JVD/8jvd_complex.cif 8JYC classic BTN3A1 and BTN2A1 human intracellular B30.2 domains of BTN3A1 and BTN2A1 Na DMAPP "[""DMA""]" 1 Kd Kd = = 34.5 µM 34500.0 [] unit_conversion 4.462180904926726 success True direct_binding ITC of DMAPP binding to the preconditioned human BTN2A1 B30.2–BTN3A1 B30.2 complex. 6 Fig. 5b and its caption report DMAPP binding to the preconditioned BTN2A1–BTN3A1 B30.2 complex, KD = 34.5 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8JYC\8JYC_metadata.json point structures/8JYC/8jyc_protein.pdb structures/8JYC/8jyc_pocket.pdb structures/8JYC/8jyc_ligand.sdf structures/8JYC/8jyc_ligand.pdb structures/8JYC/8jyc_ligand.cif structures/8JYC/8jyc_complex.pdb structures/8JYC/8jyc_complex.cif 8JYE classic BTN3A1 and BTN2A1 human intracellular B30.2 domains of BTN3A1 and BTN2A1 Na HMBPP "[""H6P""]" 1 Kd Kd = = 46.8 nM 46.8 [] unit_conversion 7.329754146925876 success True direct_binding ITC of HMBPP binding to the preconditioned human BTN2A1 B30.2–BTN3A1 B30.2 complex. 6 Fig. 5b and its caption report HMBPP binding to the preconditioned BTN2A1–BTN3A1 B30.2 complex, KD = 46.8 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8JYE\8JYE_metadata.json point structures/8JYE/8jye_protein.pdb structures/8JYE/8jye_pocket.pdb structures/8JYE/8jye_ligand.sdf structures/8JYE/8jye_ligand.pdb structures/8JYE/8jye_ligand.cif structures/8JYE/8jye_complex.pdb structures/8JYE/8jye_complex.cif 8JYL classic AasS (acyl-ACP synthetase) Vibrio harveyi Full-length AasS, 533 aa Na C10-AMS "[""VUL""]" 6 Kd Kd = = 14.13±3.82 nM 14.13 [] unit_conversion 7.849857838151442 success True direct_binding Isothermal titration calorimetry of C10-AMS binding to AasS; reported stoichiometry n = 0.97 ± 0.16. 7 The text states that C10-AMS binds AasS with Kd 14.13±3.82 nM; Fig. 3C on page 8 displays the same value. auto_metric_priority unique highest-priority metric family: Kd [6] 6 structures\8JYL\8JYL_metadata.json point structures/8JYL/8jyl_protein.pdb structures/8JYL/8jyl_pocket.pdb structures/8JYL/8jyl_ligand.sdf structures/8JYL/8jyl_ligand.pdb structures/8JYL/8jyl_ligand.cif structures/8JYL/8jyl_complex.pdb structures/8JYL/8jyl_complex.cif 8JZG classic S-adenosylmethionine synthase (CgMetK) Corynebacterium glutamicum metK gene cloned into pET30a and expressed in Escherichia coli BL21(DE3)-T1R Na Adenosine; triphosphate; SAM "[""SAM""]" 1 Ki Ki = = 0.024 mM 24000.0 [] unit_conversion 4.619788758288394 success True biochemical_inhibition Mixed-inhibition kinetic analysis of purified CgMetKWT with SAM; ATP fixed at 5 mM and methionine varied. 7 Table 2 prints Ki = 0.024 mM for CgMetKWT; the text states SAM inhibits CgMetK competitively and noncompetitively. auto_single_measurement only accepted activity measurement [1] 1 structures\8JZG\8JZG_metadata.json point structures/8JZG/8jzg_protein.pdb structures/8JZG/8jzg_pocket.pdb structures/8JZG/8jzg_ligand.sdf structures/8JZG/8jzg_ligand.pdb structures/8JZG/8jzg_ligand.cif structures/8JZG/8jzg_complex.pdb structures/8JZG/8jzg_complex.cif 8JZV extended human RPA70N Homo sapiens RPA70N residues 1-120 fused to ETAA1 residues 599-622; N-terminal 6-His-SUMO tag Na ETAA1 peptide residues 599-622 "[""CHAIN:B""]" 1 Kd Kd = = 4.76 ± 0.43 μM 4760.0 [] unit_conversion 5.3223930472795065 success True direct_binding ITC titration of WT ETAA1 peptide with RPA70N. 18 Figure 9C prints “ETAA1 Kd=4.76±0.43 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\8JZV\8JZV_metadata.json point structures/8JZV/8jzv_protein.pdb structures/8JZV/8jzv_pocket.pdb structures/8JZV/8jzv_ligand.pdb structures/8JZV/8jzv_ligand.cif structures/8JZV/8jzv_complex.pdb structures/8JZV/8jzv_complex.cif 8JZY extended human RPA70N Homo sapiens RPA70N residues 1-120 fused to RAD9 residues 296-314; N-terminal 6-His-SUMO tag Na RAD9 peptide residues 296-314 "[""CHAIN:B""]" 1 Kd Kd = = 20.49 ± 0.48 μM 20490.0 [] unit_conversion 4.688458041598805 success True direct_binding ITC titration of WT RAD9 CRD peptide with RPA70N. 16 Figure 8D prints “RAD9 Kd=20.49±0.48 μM”. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\8JZY\8JZY_metadata.json point structures/8JZY/8jzy_protein.pdb structures/8JZY/8jzy_pocket.pdb structures/8JZY/8jzy_ligand.pdb structures/8JZY/8jzy_ligand.cif structures/8JZY/8jzy_complex.pdb structures/8JZY/8jzy_complex.cif 8K00 extended human RPA70N Homo sapiens RPA70N residues 1-120 fused to MRE11 residues 538-563; N-terminal 6-His-SUMO tag Na MRE11 peptide residues 538-563 "[""CHAIN:B""]" 1 Kd Kd = = 16.21 ± 0.44 μM 16210.0 [] unit_conversion 4.790216985151485 success True direct_binding ITC titration of WT MRE11 peptide with RPA70N. 15 Figure 7C prints “MRE11 Kd=16.21±0.44 μM”. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\8K00\8K00_metadata.json point structures/8K00/8k00_protein.pdb structures/8K00/8k00_pocket.pdb structures/8K00/8k00_ligand.pdb structures/8K00/8k00_ligand.cif structures/8K00/8k00_complex.pdb structures/8K00/8k00_complex.cif 8K17 extended Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer human Na Na collagen alpha-1(I) chain, COL1A1 residues 1154-1174 synthetic peptide "[""CHAIN:E""]" 1 Kd Kd ~ ~ 0.2 mM 200000.0 [] unit_conversion 3.6989700043360187 success True direct_binding Isothermal titration calorimetry (ITC) of purified PCP complex with synthetic COL1A1(1154-1174) peptide. 5 “COL1A1 1154-1174 demonstrates an affinity for the purified PCP complex with an apparent dissociation constant (Kd) of approximately 0.2 mM.” The deposited PCP/COL1A1 quaternary complex is identified as 8K17 on page 12. auto_single_measurement only accepted activity measurement [1] 1 structures\8K17\8K17_metadata.json point structures/8K17/8k17_protein.pdb structures/8K17/8k17_pocket.pdb structures/8K17/8k17_ligand.pdb structures/8K17/8k17_ligand.cif structures/8K17/8k17_complex.pdb structures/8K17/8k17_complex.cif 8K1K classic KtrA Bacillus subtilis Na Na ATP "[""ATP""]" 1 Kd Kd = = 1.7 ± 0.3 μM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding ITC ATP binding to BsKtrA in the presence of 200 mM Na+. 4 ITC revealed dissociation constants in the presence and absence of 200 mM Na+ of 1.7 ± 0.3 μM and 5.5 ± 1.0 μM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\8K1K\8K1K_metadata.json point structures/8K1K/8k1k_protein.pdb structures/8K1K/8k1k_pocket.pdb structures/8K1K/8k1k_ligand.sdf structures/8K1K/8k1k_ligand.pdb structures/8K1K/8k1k_ligand.cif structures/8K1K/8k1k_complex.pdb structures/8K1K/8k1k_complex.cif 8K5Q classic STM0435 (YajQ family protein) Salmonella Typhimurium Full-length STM0435, 163 residues Na c-di-GMP "[""C2E""]" 1 Kd Kd = = 8.383 µM 8383.0 [] unit_conversion 5.076600533841283 success True direct_binding SPR assay of purified STM0435 with concentration series of c-di-GMP injected over an STM0435-coated sensor chip. 9 Figure 4 and accompanying text state that c-di-GMP bound STM0435 with a Kd of 8.383 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8K5Q\8K5Q_metadata.json point structures/8K5Q/8k5q_protein.pdb structures/8K5Q/8k5q_pocket.pdb structures/8K5Q/8k5q_ligand.sdf structures/8K5Q/8k5q_ligand.pdb structures/8K5Q/8k5q_ligand.cif structures/8K5Q/8k5q_complex.pdb structures/8K5Q/8k5q_complex.cif 8K5S classic EntE Na Na N235G compound 38 / 3-prop-2-ynoxybenzoic acid-AMS / 3-(prop-2-yn-1-yloxy)benzoic acid sulfamoyl adenosine "[""VPT""]" 1 Ki Ki = = 0.034 ± 0.003 µM 34.0 [] unit_conversion 7.468521082957745 success True biochemical_inhibition Apparent inhibition constant (Kiapp) from concentration-response plots fitted to the Morrison equation for N235G EntE. 7 Table 2 reports N235G EntE Kiapp for compound 38 as 0.034 ± 0.003 µM; the text states that inhibition constants were measured for EntE (wt) and the N235G mutant. auto_single_measurement only accepted activity measurement [1] 1 structures\8K5S\8K5S_metadata.json point structures/8K5S/8k5s_protein.pdb structures/8K5S/8k5s_pocket.pdb structures/8K5S/8k5s_ligand.sdf structures/8K5S/8k5s_ligand.pdb structures/8K5S/8k5s_ligand.cif structures/8K5S/8k5s_complex.pdb structures/8K5S/8k5s_complex.cif 8K5T classic EntE Na Na N235G compound 35 / 3-chloro-2-methylbenzoic acid-AMS / 2-methyl-3-chloro-benzoic acid sulfamoyl adenosine "[""VQ5""]" 1 Ki Ki = = 0.15 ± 0.04 µM 150.0 [] unit_conversion 6.823908740944319 success True biochemical_inhibition Apparent inhibition constant (Kiapp) from concentration-response plots fitted to the Morrison equation for N235G EntE. 7 Table 2 reports N235G EntE Kiapp for compound 35 as 0.15 ± 0.04 µM; the text states that inhibition constants were measured for EntE (wt) and the N235G mutant. auto_single_measurement only accepted activity measurement [1] 1 structures\8K5T\8K5T_metadata.json point structures/8K5T/8k5t_protein.pdb structures/8K5T/8k5t_pocket.pdb structures/8K5T/8k5t_ligand.sdf structures/8K5T/8k5t_ligand.pdb structures/8K5T/8k5t_ligand.cif structures/8K5T/8k5t_complex.pdb structures/8K5T/8k5t_complex.cif 8K62 classic ALKBH1 Na Na Na 13h "[""IAU""]" 1 Kd Kd = = 0.112 ± 0.017 μM 112.0 [] unit_conversion 6.950781977329818 success True direct_binding Isothermal titration calorimetry of 13h with ALKBH1; assay buffer contained 1 mM MnCl2. 3 “In the ITC assay, 13h displayed a KD value of 0.112 ± 0.017 μM (Figure 2C).” auto_single_measurement only accepted activity measurement [1] 1 structures\8K62\8K62_metadata.json point structures/8K62/8k62_protein.pdb structures/8K62/8k62_pocket.pdb structures/8K62/8k62_ligand.sdf structures/8K62/8k62_ligand.pdb structures/8K62/8k62_ligand.cif structures/8K62/8k62_complex.pdb structures/8K62/8k62_complex.cif 8K6D classic SARS-CoV-2 3CLpro SARS-CoV-2 Na M49K/S301P WU-04 "[""J7R""]" 2 Kd Kd = = 209 ± 46.4 nM 209.0 [] unit_conversion 6.679853713888946 success True direct_binding Isothermal titration calorimetry of purified 3CLpro M49K/S301P and WU-04. 3 Fig. 1c reports the WU-04 binding affinity for M49K/S301P as Kd = 209 ± 46.4 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8K6D\8K6D_metadata.json point structures/8K6D/8k6d_protein.pdb structures/8K6D/8k6d_pocket.pdb structures/8K6D/8k6d_ligand.sdf structures/8K6D/8k6d_ligand.pdb structures/8K6D/8k6d_ligand.cif structures/8K6D/8k6d_complex.pdb structures/8K6D/8k6d_complex.cif 8K71 classic factor-inhibiting hypoxia-inducible factor (FIH) Homo sapiens Na Na BNS "[""VIZ""]" 1 IC50 IC50 = = 0.30 ± 0.07 µM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition SPE-MS inhibition assay using recombinant human FIH, 0.15 µM FIH, 10.0 µM 2OG, and 5.0 µM HIF-1α C-TAD788–822. 4 Table 1 reports BNS FIH IC50 = 0.30 ± 0.07 µM; the table footnote specifies the SPE-MS FIH assay conditions. auto_single_measurement only accepted activity measurement [1] 1 structures\8K71\8K71_metadata.json point structures/8K71/8k71_protein.pdb structures/8K71/8k71_pocket.pdb structures/8K71/8k71_ligand.sdf structures/8K71/8k71_ligand.pdb structures/8K71/8k71_ligand.cif structures/8K71/8k71_complex.pdb structures/8K71/8k71_complex.cif 8K72 classic factor-inhibiting hypoxia-inducible factor (FIH) Na Na Na compound 20 "[""VJF""]" 1 IC50 IC50 = = 1.0 ± 0.1 µM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition SPE-MS inhibition assay using 0.15 µM FIH, 10.0 µM 2OG, and 5.0 µM HIF-1α C-TAD788–822. 10 Table 3 reports compound 20 FIH IC50 = 1.0 ± 0.1 µM. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\8K72\8K72_metadata.json point structures/8K72/8k72_protein.pdb structures/8K72/8k72_pocket.pdb structures/8K72/8k72_ligand.sdf structures/8K72/8k72_ligand.pdb structures/8K72/8k72_ligand.cif structures/8K72/8k72_complex.pdb structures/8K72/8k72_complex.cif 8K78 classic c-Met human kinase domain residues 1038-1346 with N-terminal His-SUMO tag followed by an Ulp1 protease cleavage site wild-type TPX-0022 "[""IYC""]" 1 IC50 IC50 = = 2.7 nM 2.7 [] unit_conversion 8.568636235841012 success True biochemical_inhibition ADP-Glo kinase inhibition assay using purified c-Met; Fig. 1B. 2 Fig. 1 caption states that TPX-0022 potency against c-Met was analysed using an in vitro kinase assay; panel B prints IC50 = 2.7 nM. The methods identify the expressed c-Met kinase domain as human wild-type. auto_single_measurement only accepted activity measurement [1] 1 structures\8K78\8K78_metadata.json point structures/8K78/8k78_protein.pdb structures/8K78/8k78_pocket.pdb structures/8K78/8k78_ligand.sdf structures/8K78/8k78_ligand.pdb structures/8K78/8k78_ligand.cif structures/8K78/8k78_complex.pdb structures/8K78/8k78_complex.cif 8K79 classic c-Src chicken kinase domain residues 251-533 with N-terminal 6xHis tag followed by a PreScission protease cleavage site Na TPX-0022 "[""IYC""]" 1 IC50 IC50 = = 3.7 nM 3.7 [] unit_conversion 8.431798275933005 success True biochemical_inhibition Kinase inhibition assay against c-Src; Fig. 3A. 5 Section 3.3 states that kinase assays gave an IC50 of 3.7 nM against c-Src, and Fig. 3A prints IC50 = 3.7 nM. The methods identify the expressed Src kinase domain as chicken Src. auto_single_measurement only accepted activity measurement [1] 1 structures\8K79\8K79_metadata.json point structures/8K79/8k79_protein.pdb structures/8K79/8k79_pocket.pdb structures/8K79/8k79_ligand.sdf structures/8K79/8k79_ligand.pdb structures/8K79/8k79_ligand.cif structures/8K79/8k79_complex.pdb structures/8K79/8k79_complex.cif 8K7P classic Staphylococcus aureus lipase (SAL) Staphylococcus aureus Na wild-type PSA (petroselinic acid) "[""4I1""]" 1 IC50 IC50 = = 3.4 μM 3400.0 [] unit_conversion 5.468521082957745 success True biochemical_inhibition SAL inhibition/activity assay using p-nitrophenyl butyrate hydrolysis monitored by absorbance at 405 nm; IC50 determined from inhibitor concentration series. 3 Figure 2 states that the IC50 of PSA versus SAL is 3.4 μM; the methods describe the SAL/pNPB biochemical activity assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8K7P\8K7P_metadata.json point structures/8K7P/8k7p_protein.pdb structures/8K7P/8k7p_pocket.pdb structures/8K7P/8k7p_ligand.sdf structures/8K7P/8k7p_ligand.pdb structures/8K7P/8k7p_ligand.cif structures/8K7P/8k7p_complex.pdb structures/8K7P/8k7p_complex.cif 8K8E extended human gamma-secretase human Na Na SB-250 "[""CHAIN:H""]" 1 IC50 IC50 = = 0.5 nM 0.5 [] unit_conversion 9.301029995663981 success True biochemical_inhibition Purified γ-secretase; linked transmembrane substrate-mimetic inhibitor SB-250, with 1 nM enzyme. 6 Linking the two peptidomimetic components yielded inhibitory potencies approaching stoichiometric levels (IC50 of 0.5 nM with 1 nM enzyme); SB-250 is identified as the linked substrate mimetic used for the cryo-EM structure. auto_single_measurement only accepted activity measurement [1] 1 structures\8K8E\8K8E_metadata.json point structures/8K8E/8k8e_protein.pdb structures/8K8E/8k8e_pocket.pdb structures/8K8E/8k8e_ligand.pdb structures/8K8E/8k8e_ligand.cif structures/8K8E/8k8e_complex.pdb structures/8K8E/8k8e_complex.cif 8K9W classic Plasmodium LysRS Na Na Na ADKI4 (compound 38) "[""JTR""]" 2 Kd Kd = = 62.8 nM 62.8 [] unit_conversion 7.202040356262804 success True direct_binding PfLysRS SPR direct-binding assay. 5 Supplementary Figure 3 reports compound 38 PfLysRS Kd 62.8 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8K9W\8K9W_metadata.json point structures/8K9W/8k9w_protein.pdb structures/8K9W/8k9w_pocket.pdb structures/8K9W/8k9w_ligand.sdf structures/8K9W/8k9w_ligand.pdb structures/8K9W/8k9w_ligand.cif structures/8K9W/8k9w_complex.pdb structures/8K9W/8k9w_complex.cif 8K9X classic Plasmodium LysRS Na Na Na ADKI5 (compound 36K3) "[""JUA""]" 2 Kd Kd = = 12.4 nM 12.4 [] unit_conversion 7.906578314837764 success True direct_binding PfLysRS direct-binding assay. 0 The supplement/review response reports compound 36K3 PfLysRS Kd 12.4 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8K9X\8K9X_metadata.json point structures/8K9X/8k9x_protein.pdb structures/8K9X/8k9x_pocket.pdb structures/8K9X/8k9x_ligand.sdf structures/8K9X/8k9x_ligand.pdb structures/8K9X/8k9x_ligand.cif structures/8K9X/8k9x_complex.pdb structures/8K9X/8k9x_complex.cif 8OGF extended Human carbonic anhydrase II human Na Na compound 31; 4-(((1-(3-((3aR,7R,7aS)-7-hydroxy-2,2-dimethyltetrahydro-[1,3]dioxolo[4,5-c]pyridin-5(4H)-yl)propyl)-1H-1,2,3-triazol-4-yl)methyl)amino)benzenesulfonamide "[""VMD""]" 1 Ki Ki = = 6384 nM 6384.0 [] unit_conversion 5.194907121657327 success True biochemical_inhibition Stopped Flow CO2 Hydrase assay; Table 1 inhibition data. 7 Table 1 reports compound 31, (I)-single tail: hCA II Ki = 6384 nM. Fig. 2 on page 8 explicitly identifies the hCA II/31 complex as PDB 8OGF. auto_single_measurement only accepted activity measurement [1] 1 structures\8OGF\8OGF_metadata.json point structures/8OGF/8ogf_ligand.sdf structures/8OGF/8ogf_ligand.cif structures/8OGF/8ogf_complex.cif 8OHQ extended heparanase human Na Na competitive inhibitor derived from siastatin B "[""VGO""]" 1 IC50 IC50 = = 27 ± 3 μM 27000.0 [] unit_conversion 4.568636235841013 success True biochemical_inhibition Competitive activity-based protein profiling assay in platelet lysate; Table 3. 6 Table 3 reports inhibitor 8 with HPSE IC50 = 27 ± 3 μM. Figure 4 identifies the HPSE complex with inhibitor 8. auto_single_measurement only accepted activity measurement [1] 1 structures\8OHQ\8OHQ_metadata.json point structures/8OHQ/8ohq_ligand.sdf structures/8OHQ/8ohq_ligand.cif structures/8OHQ/8ohq_complex.cif 8OHR extended heparanase human Na Na glucuronic acid configured 3-geminal diol iminosugar inhibitor "[""VP5""]" 1 IC50 IC50 = = 20 ± 80 μM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition Competitive activity-based protein profiling assay in platelet lysate; Table 3. 6 Table 3 reports inhibitor 9 with HPSE IC50 = 20 ± 80 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8OHR\8OHR_metadata.json point structures/8OHR/8ohr_ligand.sdf structures/8OHR/8ohr_ligand.cif structures/8OHR/8ohr_complex.cif 8OHT extended beta-glucuronidase Acidobacterium capsulatum Na Na competitive inhibitor derived from siastatin B "[""VON""]" 1 Ki Ki = = 5.8 ± 0.5 μM 5800.0 [] unit_conversion 5.236572006437063 success True biochemical_inhibition Enzyme inhibition constants for synthesized inhibitors; Table 1. 6 Table 1 reports inhibitor 8 with AcGH79 Ki = 5.8 ± 0.5 μM. Figure 4 identifies the AcGH79 complex with inhibitor 8. auto_single_measurement only accepted activity measurement [1] 1 structures\8OHT\8OHT_metadata.json point structures/8OHT/8oht_ligand.sdf structures/8OHT/8oht_ligand.cif structures/8OHT/8oht_complex.cif 8OHU extended beta-glucuronidase Acidobacterium capsulatum Na Na glucuronic acid configured isofagamine "[""SJ5""]" 1 Ki Ki = = 0.022 ± 0.003 μM 22.0 [] unit_conversion 7.657577319177793 success True biochemical_inhibition Enzyme inhibition constants for synthesized inhibitors; Table 1. 6 Table 1 reports inhibitor 11 with AcGH79 Ki = 0.022 ± 0.003 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8OHU\8OHU_metadata.json point structures/8OHU/8ohu_ligand.sdf structures/8OHU/8ohu_ligand.cif structures/8OHU/8ohu_complex.cif 8OHV extended beta-glucuronidase Acidobacterium capsulatum Na Na glucuronic acid configured 3-geminal diol iminosugar inhibitor "[""VP5""]" 1 Ki Ki = = 0.520 ± 0.030 μM 520.0 [] unit_conversion 6.2839966563652006 success True biochemical_inhibition Enzyme inhibition constants for synthesized inhibitors; Table 1. 6 Table 1 reports inhibitor 9 with AcGH79 Ki = 0.520 ± 0.030 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8OHV\8OHV_metadata.json point structures/8OHV/8ohv_ligand.sdf structures/8OHV/8ohv_ligand.cif structures/8OHV/8ohv_complex.cif 8OIA classic Trichomonas vaginalis riboside hydrolase Trichomonas vaginalis Na Na D-ribose "[""RIB""]" 1 Kd Kd = = 5.2 mM 5200000.0 [] unit_conversion 2.2839966563652006 success True direct_binding Affinity stated for the TvRH–D-ribose cocrystal/product complex. 4 “The latter cocrystals are affected by a strong pseudocentering ... incubating the enzyme with a high concentration of the aldopentose to overcome the low affinity (Kd = 5.2 mM).” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8OIA\8OIA_metadata.json point structures/8OIA/8oia_protein.pdb structures/8OIA/8oia_pocket.pdb structures/8OIA/8oia_ligand.sdf structures/8OIA/8oia_ligand.pdb structures/8OIA/8oia_ligand.cif structures/8OIA/8oia_complex.pdb structures/8OIA/8oia_complex.cif 8OIZ classic human CRBN-DDB1 human Na Na Pomalidomide (compound 3) "[""Y70""]" 1 IC50 IC50 = = 0.41 ± 0.1 µM 410.0 [] unit_conversion 6.3872161432802645 success True direct_binding Fluorescence-polarisation assay. 4 Pomalidomide (3) bound CRBN in the FP assay with IC50=0.41 µM ±0.1; page 13 maps compound 3 to PDB 8OIZ. auto_single_measurement only accepted activity measurement [1] 1 structures\8OIZ\8OIZ_metadata.json point structures/8OIZ/8oiz_protein.pdb structures/8OIZ/8oiz_pocket.pdb structures/8OIZ/8oiz_ligand.sdf structures/8OIZ/8oiz_ligand.pdb structures/8OIZ/8oiz_ligand.cif structures/8OIZ/8oiz_complex.pdb structures/8OIZ/8oiz_complex.cif 8OJH classic human CRBN-DDB1 human Na Na compound 4 "[""VP9""]" 1 IC50 IC50 = = 0.64 ± 0.39 µM 640.0 [] unit_conversion 6.1938200260161125 success True direct_binding Fluorescence-polarisation assay. 4 Compound 4 bound CRBN in the FP assay with IC50=0.64 µM ±0.39; page 13 maps compound 4 to PDB 8OJH. auto_single_measurement only accepted activity measurement [1] 1 structures\8OJH\8OJH_metadata.json point structures/8OJH/8ojh_protein.pdb structures/8OJH/8ojh_pocket.pdb structures/8OJH/8ojh_ligand.sdf structures/8OJH/8ojh_ligand.pdb structures/8OJH/8ojh_ligand.cif structures/8OJH/8ojh_complex.pdb structures/8OJH/8ojh_complex.cif 8OMD classic mKHK mouse Residues 2-298; N-terminal 6xHis tag and thrombin cleavage site Pro203Ser compound 4 "[""VTJ""]" 1 IC50 IC50 = = 7 nM 7.0 [] unit_conversion 8.154901959985743 success True biochemical_inhibition ADP-Glo kinase inhibition assay; mKHK assayed with D-fructose and ATP. 3 Table 1 reports compound 4 IC50 values: 399 nM hKHK-C, 8 nM hKHK-A, and 7 nM mKHK. The kinase-inhibition assay is described on page 4. auto_single_measurement only accepted activity measurement [1] 1 structures\8OMD\8OMD_metadata.json point structures/8OMD/8omd_protein.pdb structures/8OMD/8omd_pocket.pdb structures/8OMD/8omd_ligand.sdf structures/8OMD/8omd_ligand.pdb structures/8OMD/8omd_ligand.cif structures/8OMD/8omd_complex.pdb structures/8OMD/8omd_complex.cif 8OME classic hKHK-A human Residues 1-298; tag-free Na compound 4 "[""VTJ""]" 1 IC50 IC50 = = 8 nM 8.0 [] unit_conversion 8.096910013008056 success True biochemical_inhibition ADP-Glo kinase inhibition assay; hKHK-A assayed with D-fructose and ATP. 3 Table 1 reports compound 4 IC50 values: 399 nM hKHK-C, 8 nM hKHK-A, and 7 nM mKHK. The kinase-inhibition assay is described on page 4. auto_single_measurement only accepted activity measurement [1] 1 structures\8OME\8OME_metadata.json point structures/8OME/8ome_protein.pdb structures/8OME/8ome_pocket.pdb structures/8OME/8ome_ligand.sdf structures/8OME/8ome_ligand.pdb structures/8OME/8ome_ligand.cif structures/8OME/8ome_complex.pdb structures/8OME/8ome_complex.cif 8OMF classic hKHK-C human Residues 5-298; N-terminal 6xHis tag and thrombin cleavage site Na compound 4 "[""VTJ""]" 1 IC50 IC50 = = 399 nM 399.0 [] unit_conversion 6.399027104313252 success True biochemical_inhibition ADP-Glo kinase inhibition assay; hKHK-C assayed with D-fructose and ATP. 3 Table 1 reports compound 4 IC50 values: 399 nM hKHK-C, 8 nM hKHK-A, and 7 nM mKHK. The kinase-inhibition assay is described on page 4. auto_single_measurement only accepted activity measurement [1] 1 structures\8OMF\8OMF_metadata.json point structures/8OMF/8omf_protein.pdb structures/8OMF/8omf_pocket.pdb structures/8OMF/8omf_ligand.sdf structures/8OMF/8omf_ligand.pdb structures/8OMF/8omf_ligand.cif structures/8OMF/8omf_complex.pdb structures/8OMF/8omf_complex.cif 8OMJ classic hKHK-C Na Na Na compound 28 "[""VTM""]" 1 IC50 IC50 = = 2.3 nM 2.3 [] unit_conversion 8.638272163982407 success True biochemical_inhibition hKHK-C enzymatic inhibition assay (Table 1). 5 Table 1 reports compound 28 with hKHK-C IC50 = 2.3 nM. The text on the same page identifies the X-ray co-crystal structure of compound 28 with KHK as PDB 8OMJ. auto_single_measurement only accepted activity measurement [1] 1 structures\8OMJ\8OMJ_metadata.json point structures/8OMJ/8omj_protein.pdb structures/8OMJ/8omj_pocket.pdb structures/8OMJ/8omj_ligand.sdf structures/8OMJ/8omj_ligand.pdb structures/8OMJ/8omj_ligand.cif structures/8OMJ/8omj_complex.pdb structures/8OMJ/8omj_complex.cif 8OO1 classic UraA Escherichia coli UraA(G320P)-Sy45 complex G320P uracil "[""URA""]" 1 Kd Kd = = 144 ± 18 nM 144.0 [] unit_conversion 6.84163750790475 success True direct_binding Scintillation proximity uracil-binding assay; UraA(G320P) measured in the presence of Sy45. 5 Fig. 4D explicitly reports K_D = 144 ± 18 nM for UraA(G320P)-Sy45; the caption identifies the assay as a scintillation proximity uracil-binding assay and says fitted curves yield dissociation constants. auto_single_measurement only accepted activity measurement [1] 1 structures\8OO1\8OO1_metadata.json point structures/8OO1/8oo1_protein.pdb structures/8OO1/8oo1_pocket.pdb structures/8OO1/8oo1_ligand.sdf structures/8OO1/8oo1_ligand.pdb structures/8OO1/8oo1_ligand.cif structures/8OO1/8oo1_complex.pdb structures/8OO1/8oo1_complex.cif 8OR1 classic PD-L1 dimer human Na Na A56 "[""VYC""]" 2 Kd Kd < < 1 µM 1000.0 [] unit_conversion 6.0 success True direct_binding 1H NMR titration of PD-L1 with A56. 10 The 1H NMR titration section states that the A56/PD-L1 complex demonstrates strong binding with Kd < 1 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8OR1\8OR1_metadata.json point structures/8OR1/8or1_protein.pdb structures/8OR1/8or1_pocket.pdb structures/8OR1/8or1_ligand.sdf structures/8OR1/8or1_ligand.pdb structures/8OR1/8or1_ligand.cif structures/8OR1/8or1_complex.pdb structures/8OR1/8or1_complex.cif 8ORC classic Mus musculus acetylcholinesterase (mAChE) Mus musculus Na wild-type AL237 "[""VY8""]" 1 IC50 IC50 = = 217 μM 217000.0 [] unit_conversion 3.663540266151471 success True biochemical_inhibition Ellman enzymatic inhibition assay; Figure 6 reports mAChE/hAChE values as 217/120 μM for AL237. 7 Figure 6 lists AL237 IC50 (μM): AgAChE1 7.1; mAChE/hAChE 217/120. The paper states that the mAChE•AL237 crystal structure was determined in this work (PDB 8ORC). auto_single_measurement only accepted activity measurement [1] 1 structures\8ORC\8ORC_metadata.json point structures/8ORC/8orc_protein.pdb structures/8ORC/8orc_pocket.pdb structures/8ORC/8orc_ligand.sdf structures/8ORC/8orc_ligand.pdb structures/8ORC/8orc_ligand.cif structures/8ORC/8orc_complex.pdb structures/8ORC/8orc_complex.cif 8OTL classic InhA Mycobacterium tuberculosis cleaved InhA Na compound 21 (VZE), 5-(((4-(2-hydroxyphenoxy)benzyl)(octyl)amino)methyl)-2-phenoxyphenol "[""VZE""]" 1 IC50 IC50 = = 0.70 ± 0.07 µM 700.0 [] unit_conversion 6.154901959985743 success True biochemical_inhibition InhA inhibition initial-velocity assay at 25 °C; NADH 250 µM, dodecenoyl coenzyme A 50 µM, inhibitor 50 µM screening conditions, 30 mM PIPES, 150 mM NaCl, pH 6.8. Table reports compound 21 as 100% inhibition (91% at 5 µM) and IC50. 8 Table 1 reports compound 21 (EG1-57) with IC50 0.70 ± 0.07 µM; the text identifies compound 21 as the best InhA inhibitor, and the crystal structure section maps compound 21 to InhA/NAD+ PDB 8OTL. auto_single_measurement only accepted activity measurement [1] 1 structures\8OTL\8OTL_metadata.json point structures/8OTL/8otl_protein.pdb structures/8OTL/8otl_pocket.pdb structures/8OTL/8otl_ligand.sdf structures/8OTL/8otl_ligand.pdb structures/8OTL/8otl_ligand.cif structures/8OTL/8otl_complex.pdb structures/8OTL/8otl_complex.cif 8OTP extended human carbonic anhydrase II human Na Na 39a; 1-cyclopropyl-6-fluoro-4-oxo-7-(4-(4-sulfamoylbenzoyl)piperazin-1-yl)-1,4-dihydroquinoline-3-carboxylic acid "[""VZW""]" 1 Ki Ki = = 61.5 nM 61.5 [] unit_conversion 7.211124884224583 success True biochemical_inhibition Stopped-flow CO2 hydration inhibition assay. 8 Table 1 reports compound 39a Ki = 61.5 nM against hCA II. Figure 4 (page 10) identifies PDB 8OTP as hCA II in complex with compound 39a. auto_single_measurement only accepted activity measurement [1] 1 structures\8OTP\8OTP_metadata.json point structures/8OTP/8otp_ligand.sdf structures/8OTP/8otp_ligand.cif structures/8OTP/8otp_complex.cif 8OTV classic NUDT14 human NUDT14 residues 1-222; N-terminal 6x histidine tag followed by a TEV protease cleavage site Na compound 9 (ibrutinib derivative) "[""W0O""]" 2 Kd Kd ~ ~ 400 nM 400.0 [] unit_conversion 6.3979400086720375 success True direct_binding Purified-protein surface plasmon resonance (SPR). 7 Figure 4A caption states that compound 9 has an SPR KD of approximately 400 nM for NUDT14. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8OTV\8OTV_metadata.json point structures/8OTV/8otv_protein.pdb structures/8OTV/8otv_pocket.pdb structures/8OTV/8otv_ligand.sdf structures/8OTV/8otv_ligand.pdb structures/8OTV/8otv_ligand.cif structures/8OTV/8otv_complex.pdb structures/8OTV/8otv_complex.cif 8OUB extended human carbonic anhydrase II human Na Na 7c; 1-cyclopropyl-6-fluoro-4-oxo-7-(4-((4-sulfamoylbenzyl)carbamoyl)piperazin-1-yl)-1,4-dihydroquinoline-3-carboxylic acid "[""W1O""]" 1 Ki Ki = = 68.3 nM 68.3 [] unit_conversion 7.165579296318468 success True biochemical_inhibition Stopped-flow CO2 hydration inhibition assay. 8 Table 1 reports compound 7c Ki = 68.3 nM against hCA II. Figure 5 (page 11) identifies PDB 8OUB as hCA II in complex with compound 7c. auto_single_measurement only accepted activity measurement [1] 1 structures\8OUB\8OUB_metadata.json point structures/8OUB/8oub_ligand.sdf structures/8OUB/8oub_ligand.cif structures/8OUB/8oub_complex.cif 8OUU classic c-MET Na Na D1228V compound 29 "[""W49""]" 1 IC50 IC50 = = 0.068 µM 68.0 [] unit_conversion 7.167491087293763 success True biochemical_inhibition ADP-Glo activity assay; WT/D1228V values are printed in that order. 7 Table 3 lists compound 29 ADP-Glo IC50 as 0.031/0.068 µM (WT/D1228V). Page 24 maps 8OUU to compound 29. auto_single_measurement only accepted activity measurement [1] 1 structures\8OUU\8OUU_metadata.json point structures/8OUU/8ouu_protein.pdb structures/8OUU/8ouu_pocket.pdb structures/8OUU/8ouu_ligand.sdf structures/8OUU/8ouu_ligand.pdb structures/8OUU/8ouu_ligand.cif structures/8OUU/8ouu_complex.pdb structures/8OUU/8ouu_complex.cif 8OUV classic c-MET Na Na D1228V compound 15 "[""W3R""]" 1 Kd Kd = = 0.090 µM 90.0 [] unit_conversion 7.045757490560675 success True direct_binding SPR assay; WT/D1228V values are printed in that order. 3 Table 1 lists compound 15 SPR Kd as 0.24/0.090 µM (WT/D1228V). auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8OUV\8OUV_metadata.json point structures/8OUV/8ouv_protein.pdb structures/8OUV/8ouv_pocket.pdb structures/8OUV/8ouv_ligand.sdf structures/8OUV/8ouv_ligand.pdb structures/8OUV/8ouv_ligand.cif structures/8OUV/8ouv_complex.pdb structures/8OUV/8ouv_complex.cif 8OV6 classic BRD4; DCAF16; DDB1; DDA1 Na BRD4 tandem bromodomain construct, residues 43-459; DCAF16 lacking the proline-rich region (residues 276-380); DDB1 DeltaBPB, residues 396-705; full-length DDA1 DDB1 DeltaBPB deletion IBG1; U79 "[""U79""]" 1 IC50 IC50 = = 12.8 nM 12.8 [] unit_conversion 7.892790030352131 success True direct_binding alphaLISA displacement assay; IBG1 binding to BRD4 tandem in the presence of DCAF16–DDB1(ΔBPB)–DDA1. 3 “enhanced affinity of IBG1 to BRD4Tandem in the presence of DCAF16 (IC50 = 12.8 nM)” auto_single_measurement only accepted activity measurement [1] 1 structures\8OV6\8OV6_metadata.json point structures/8OV6/8ov6_protein.pdb structures/8OV6/8ov6_pocket.pdb structures/8OV6/8ov6_ligand.sdf structures/8OV6/8ov6_ligand.pdb structures/8OV6/8ov6_ligand.cif structures/8OV6/8ov6_complex.pdb structures/8OV6/8ov6_complex.cif 8OV7 classic c-MET Na Na D1228V compound 10 "[""W3W""]" 1 Kd Kd = = 0.15 µM 150.0 [] unit_conversion 6.823908740944319 success True direct_binding SPR assay; WT/D1228V values are printed in that order; table footnote states n=1. 3 Table 1 lists compound 10 SPR Kd as 0.52/0.15 µM (WT/D1228V). Page 24 maps 8OV7 to compound 10. auto_single_measurement only accepted activity measurement [1] 1 structures\8OV7\8OV7_metadata.json point structures/8OV7/8ov7_protein.pdb structures/8OV7/8ov7_pocket.pdb structures/8OV7/8ov7_ligand.sdf structures/8OV7/8ov7_ligand.pdb structures/8OV7/8ov7_ligand.cif structures/8OV7/8ov7_complex.pdb structures/8OV7/8ov7_complex.cif 8OVZ classic c-MET Na Na D1228V compound 16 "[""W3N""]" 1 Kd Kd = = 0.51 µM 510.0 [] unit_conversion 6.292429823902063 success True direct_binding SPR assay; WT/D1228V values are printed in that order; table footnote states n=1. 3 Table 1 lists compound 16 SPR Kd as 0.46/0.51 µM (WT/D1228V). Page 24 maps 8OVZ to compound 16. auto_single_measurement only accepted activity measurement [1] 1 structures\8OVZ\8OVZ_metadata.json point structures/8OVZ/8ovz_protein.pdb structures/8OVZ/8ovz_pocket.pdb structures/8OVZ/8ovz_ligand.sdf structures/8OVZ/8ovz_ligand.pdb structures/8OVZ/8ovz_ligand.cif structures/8OVZ/8ovz_complex.pdb structures/8OVZ/8ovz_complex.cif 8OW3 classic c-MET Na Na wild-type compound 2 "[""W40""]" 1 Kd Kd = = 2.5 µM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding SPR assay; WT/D1228V values are printed in that order. 3 Table 1 lists compound 2 SPR Kd as 2.5/2.1 µM (WT/D1228V). Page 24 maps 8OW3 to compound 2, wild-type c-MET. auto_single_measurement only accepted activity measurement [1] 1 structures\8OW3\8OW3_metadata.json point structures/8OW3/8ow3_protein.pdb structures/8OW3/8ow3_pocket.pdb structures/8OW3/8ow3_ligand.sdf structures/8OW3/8ow3_ligand.pdb structures/8OW3/8ow3_ligand.cif structures/8OW3/8ow3_complex.pdb structures/8OW3/8ow3_complex.cif 8OW7 classic sugar kinase K1058 Tannerella forsythia His6-tagged recombinant protein expressed in Escherichia coli Na N-acetylmuramic acid (MurNAc) "[""AMU""]" 1 Ki Ki = = 20 ± 23 mM 20000000.0 [] unit_conversion 1.6989700043360187 success True biochemical_inhibition Coupled enzyme assay with ATP; substrate-inhibition model (K1058*). 8 Table 2 reports K1058* Ki = 20 ± 23 mM for MurNAc; the asterisk denotes the substrate-inhibited model. auto_single_measurement only accepted activity measurement [1] 1 structures\8OW7\8OW7_metadata.json point structures/8OW7/8ow7_protein.pdb structures/8OW7/8ow7_pocket.pdb structures/8OW7/8ow7_ligand.sdf structures/8OW7/8ow7_ligand.pdb structures/8OW7/8ow7_ligand.cif structures/8OW7/8ow7_complex.pdb structures/8OW7/8ow7_complex.cif 8OW9 classic MurNAc kinase MurK Tannerella forsythia His6-tagged recombinant protein expressed in Escherichia coli Na N-acetylmuramic acid (MurNAc) "[""AMU""]" 1 Ki Ki = = 5.6 ± 2.3 mM 5600000.0 [] unit_conversion 2.2518119729937993 success True biochemical_inhibition Coupled enzyme assay with ATP; substrate-inhibition model (MurK*). 8 Table 2 reports MurK* Ki = 5.6 ± 2.3 mM for MurNAc; the asterisk denotes the substrate-inhibited model. auto_single_measurement only accepted activity measurement [1] 1 structures\8OW9\8OW9_metadata.json point structures/8OW9/8ow9_protein.pdb structures/8OW9/8ow9_pocket.pdb structures/8OW9/8ow9_ligand.sdf structures/8OW9/8ow9_ligand.pdb structures/8OW9/8ow9_ligand.cif structures/8OW9/8ow9_complex.pdb structures/8OW9/8ow9_complex.cif 8OWG classic c-MET Na Na D1228V compound 2 "[""W40""]" 1 Kd Kd = = 2.1 µM 2100.0 [] unit_conversion 5.6777807052660805 success True direct_binding SPR assay; WT/D1228V values are printed in that order. 3 Table 1 lists compound 2 SPR Kd as 2.5/2.1 µM (WT/D1228V). Page 24 maps 8OWG to compound 2. auto_single_measurement only accepted activity measurement [1] 1 structures\8OWG\8OWG_metadata.json point structures/8OWG/8owg_protein.pdb structures/8OWG/8owg_pocket.pdb structures/8OWG/8owg_ligand.sdf structures/8OWG/8owg_ligand.pdb structures/8OWG/8owg_ligand.cif structures/8OWG/8owg_complex.pdb structures/8OWG/8owg_complex.cif 8OWO classic SMYD3 Na full length recombinant SMYD3 Na FL01507 "[""9W9""]" 1 Kd Kd = = 17.9 µM 17900.0 [] unit_conversion 4.747146969020107 success True direct_binding Initial multiplexed GCI kinetic screening against apo SMYD3. 4 Table 1 lists FL01507 under “SMYD3 apo” with K_D = 17.9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8OWO\8OWO_metadata.json point structures/8OWO/8owo_protein.pdb structures/8OWO/8owo_pocket.pdb structures/8OWO/8owo_ligand.sdf structures/8OWO/8owo_ligand.pdb structures/8OWO/8owo_ligand.cif structures/8OWO/8owo_complex.pdb structures/8OWO/8owo_complex.cif 8OXU classic Hsp90 yeast Hsp90 C-terminal domain, residues 438-677, expressed as a GST-tagged fusion Na LA1011 "[""W5R""]" 1 Kd Kd = = 13.1 ± 1.7 μM 13100.0 [] unit_conversion 4.882728704344236 success True direct_binding Isothermal titration calorimetry of LA1011 binding to free 30 μM yeast Hsp90. 9 “LA1011 … bind[s] to Hsp90 with a Kd of 13.1 μM (Figure 3D)”; Figure 3D prints “Kd = 13.1 ± 1.7 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8OXU\8OXU_metadata.json point structures/8OXU/8oxu_protein.pdb structures/8OXU/8oxu_pocket.pdb structures/8OXU/8oxu_ligand.sdf structures/8OXU/8oxu_ligand.pdb structures/8OXU/8oxu_ligand.cif structures/8OXU/8oxu_complex.pdb structures/8OXU/8oxu_complex.cif 8OYG classic ASBT_NM Neisseria meningitidis GFP-tagged ASBT_NM expressed from modified pWaldo GFPd with a 3C protease-cleavable tag Na pantoate "[""PAF""]" 1 Kd Kd = = 127 ± 7 µM 127000.0 [] unit_conversion 3.8961962790440428 success True direct_binding Isothermal titration calorimetry of purified ASBTNM with pantoate; one-set-of-sites model. 28 Figure 2 reports pantoate binding to ASBTNM by isothermal calorimetry, with KD = 127 ± 7 µM. The Results text identifies this as the pantoate-bound ASBTNM structure, and the data-availability statement maps ASBTNM(Pan) to PDB 8OYG. auto_single_measurement only accepted activity measurement [1] 1 structures\8OYG\8OYG_metadata.json point structures/8OYG/8oyg_protein.pdb structures/8OYG/8oyg_pocket.pdb structures/8OYG/8oyg_ligand.sdf structures/8OYG/8oyg_ligand.pdb structures/8OYG/8oyg_ligand.cif structures/8OYG/8oyg_complex.pdb structures/8OYG/8oyg_complex.cif 8OYH extended furin (PCSK3) Na Na Na Guanidinomethyl-Phac-Can-Tle-Can-6-(aminomethyl)-3-amino-isoindol (inhibitor 17) "[""CHAIN:B""]" 1 Ki Ki = = 7.08 ± 0.44 pM 0.00708 [] unit_conversion 11.14996674231023 success True biochemical_inhibition Enzyme kinetic measurement with soluble human furin and Ac-Arg-Arg-Tle-Arg-Arg-AMC substrate. 4 Table 1 lists inhibitor 17 with Ki = 7.08 ± 0.44 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\8OYH\8OYH_metadata.json point structures/8OYH/8oyh_protein.pdb structures/8OYH/8oyh_pocket.pdb structures/8OYH/8oyh_ligand.pdb structures/8OYH/8oyh_ligand.cif structures/8OYH/8oyh_complex.pdb structures/8OYH/8oyh_complex.cif 8P01 classic human STING human wild-type human STING ectodomain, residues 149-379 wild type (WT) BI 7446; CDN 13 "[""W78""]" 1 Kd Kd = = 1.5 nM 1.5 [] unit_conversion 8.823908740944319 success True direct_binding Surface plasmon resonance (SPR) with biotinylated wt-hSTING (149–379); Table 5 reports hSTING Kd. 7 Table 5 prints “SPR with hSTING Kd [nM]” = 1.5 for compound 13 (BI 7446). The SPR construct is stated as wt-hSTING avi-149–379 on page 11, matching the requested structure construct. auto_single_measurement only accepted activity measurement [1] 1 structures\8P01\8P01_metadata.json point structures/8P01/8p01_protein.pdb structures/8P01/8p01_pocket.pdb structures/8P01/8p01_ligand.sdf structures/8P01/8p01_ligand.pdb structures/8P01/8p01_ligand.cif structures/8P01/8p01_complex.pdb structures/8P01/8p01_complex.cif 8P04 classic CLK1 human residues H148-I484 wild-type Leucettinib-92 (compound 32) "[""WAK""]" 1 IC50 IC50 = = 0.0091 μM 9.1 [] unit_conversion 8.040958607678906 success True biochemical_inhibition Radiometric dose–response kinase assay using purified recombinant human kinases. 4 Table 2, row 32, reports CLK1 IC50 = 0.0091 μM for compound 32; the table footnote states values are from dose–response curves using purified recombinant human kinases. auto_single_measurement only accepted activity measurement [1] 1 structures\8P04\8P04_metadata.json point structures/8P04/8p04_protein.pdb structures/8P04/8p04_pocket.pdb structures/8P04/8p04_ligand.sdf structures/8P04/8p04_ligand.pdb structures/8P04/8p04_ligand.cif structures/8P04/8p04_complex.pdb structures/8P04/8p04_complex.cif 8P08 classic human CLK1 human Recombinant CLK1 residues H148-I484 wild-type Leucettinib-21 (compound 4) "[""WAZ""]" 3 Kd Kd = = 0.388 nM 0.388 [] unit_conversion 9.411168274405792 success True direct_binding Enzymologic binding-kinetics/residence-time determination for CLK1. 11 Table 8 reports CLK1 Kd = 0.388 nM for Leucettinib-21; adjacent text identifies enzyme kinetics studies with Leucettinib-21. auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\8P08\8P08_metadata.json point structures/8P08/8p08_protein.pdb structures/8P08/8p08_pocket.pdb structures/8P08/8p08_ligand.sdf structures/8P08/8p08_ligand.pdb structures/8P08/8p08_ligand.cif structures/8P08/8p08_complex.pdb structures/8P08/8p08_complex.cif 8P0E classic Rubella virus p150 macro domain Rubella virus p150 residues 805-983 Na ADP-ribose "[""APR""]" 1 Kd Kd = = 58.1 ± 5.4 µM 58100.0 [] unit_conversion 4.235823867609669 success True direct_binding Isothermal titration calorimetry using 100 µM RuV macrodomain and 2 mM ADP-ribose at 25 °C. 10 ITC showed that RuV macrodomain binds ADP-ribose with a dissociation constant (KD) of 58.1 ± 5.4 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8P0E\8P0E_metadata.json point structures/8P0E/8p0e_protein.pdb structures/8P0E/8p0e_pocket.pdb structures/8P0E/8p0e_ligand.sdf structures/8P0E/8p0e_ligand.pdb structures/8P0E/8p0e_ligand.cif structures/8P0E/8p0e_complex.pdb structures/8P0E/8p0e_complex.cif 8P1Q classic USP28 human USP28cat (Deltatip); UCID tip-region deletion construct, residues 149-458-SGSG-529-707 Na FT206 "[""WFT""]" 1 IC50 IC50 = = 0.15 ± 0.06 µM 150.0 [] unit_conversion 6.823908740944319 success True biochemical_inhibition Ub-Rhodamine110 dose-response biochemical inhibition assay; Figure 5B table reports the USP28Δtip WT value. 9 Figure 5B prints an IC50 of 0.15 ± 0.06 µM for FT206 against WT USP28Δtip. Table 1 maps PDB 8P1Q to USP28cat Δtip bound to FT206. auto_single_measurement only accepted activity measurement [1] 1 structures\8P1Q\8P1Q_metadata.json point structures/8P1Q/8p1q_protein.pdb structures/8P1Q/8p1q_pocket.pdb structures/8P1Q/8p1q_ligand.sdf structures/8P1Q/8p1q_ligand.pdb structures/8P1Q/8p1q_ligand.cif structures/8P1Q/8p1q_complex.pdb structures/8P1Q/8p1q_complex.cif 8P23 classic anaerobic ribonucleotide reductase (PcNrdD) Prevotella copri Na Na ATP; CTP "[""CTP""]" 1 Kd Kd = = 11 ± 2.4 mM 11000000.0 [] unit_conversion 1.9586073148417746 success True direct_binding MST binding of CTP to ATP-loaded PcNrdD. 9 Figure 5 caption reports fitted KDs of 2.8 ± 0.5 mM and 11 ± 2.4 mM for GTP and CTP, respectively, in the presence of ATP. auto_single_measurement only accepted activity measurement [1] 1 structures\8P23\8P23_metadata.json point structures/8P23/8p23_protein.pdb structures/8P23/8p23_pocket.pdb structures/8P23/8p23_ligand.sdf structures/8P23/8p23_ligand.pdb structures/8P23/8p23_ligand.cif structures/8P23/8p23_complex.pdb structures/8P23/8p23_complex.cif 8P3C classic Burkholderia pseudomallei macrophage infectivity potentiator (BpMIP) Burkholderia pseudomallei Full length BpMIP Na NJS227 "[""WRX""]" 2 Kd Kd = = 19 ± 19 nM 19.0 [] unit_conversion 7.721246399047171 success True direct_binding Fluorescence-polarization tracer-displacement binding assay; Table 1 K_D,inhibitor. 3 Table 1 reports B. pseudomallei MIP K_D,inhibitor for NJS227 as 19 ± 19 nM. The paper maps the BpMIP–NJS227 crystal structure to PDB 8P3C. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8P3C\8P3C_metadata.json point structures/8P3C/8p3c_protein.pdb structures/8P3C/8p3c_pocket.pdb structures/8P3C/8p3c_ligand.sdf structures/8P3C/8p3c_ligand.pdb structures/8P3C/8p3c_ligand.cif structures/8P3C/8p3c_complex.pdb structures/8P3C/8p3c_complex.cif 8P3D classic Trypanosoma cruzi macrophage infectivity potentiator (TcMIP) Trypanosoma cruzi Full length TcMIP Na NJS224 "[""WS5""]" 2 Kd Kd = = 432 ± 125 nM 432.0 [] unit_conversion 6.364516253185088 success True direct_binding Fluorescence-polarization tracer-displacement binding assay; Table 1 K_D,inhibitor. 3 Table 1 reports T. cruzi MIP K_D,inhibitor for NJS224 as 432 ± 125 nM. The paper maps the TcMIP–NJS224 crystal structure to PDB 8P3D. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8P3D\8P3D_metadata.json point structures/8P3D/8p3d_protein.pdb structures/8P3D/8p3d_pocket.pdb structures/8P3D/8p3d_ligand.sdf structures/8P3D/8p3d_ligand.pdb structures/8P3D/8p3d_ligand.cif structures/8P3D/8p3d_complex.pdb structures/8P3D/8p3d_complex.cif 8P42 classic Trypanosoma cruzi macrophage infectivity potentiator (TcMIP) Trypanosoma cruzi Full length TcMIP Na NJS227 "[""WRX""]" 2 Kd Kd = = 467 ± 177 nM 467.0 [] unit_conversion 6.330683119433887 success True direct_binding Fluorescence-polarization tracer-displacement binding assay; Table 1 K_D,inhibitor. 3 Table 1 reports T. cruzi MIP K_D,inhibitor for NJS227 as 467 ± 177 nM. The paper maps the TcMIP–NJS227 crystal structure to PDB 8P42. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8P42\8P42_metadata.json point structures/8P42/8p42_protein.pdb structures/8P42/8p42_pocket.pdb structures/8P42/8p42_ligand.sdf structures/8P42/8p42_ligand.pdb structures/8P42/8p42_ligand.cif structures/8P42/8p42_complex.pdb structures/8P42/8p42_complex.cif 8P56 extended SARS-CoV-2 main protease (Mpro/3CLpro) SARS-CoV-2 ORF1ab polyprotein residues 3264-3569 Na X77 "[""X77""]" 1 IC50 IC50 = = 1.7 µM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition FRET biochemical assay with dual-labeled protease substrate; X77 is identified as the R enantiomer. 5 “The racemate showed an IC50 of 3.7 μM, while that of X77 is 1.7 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8P56\8P56_metadata.json point structures/8P56/8p56_protein.pdb structures/8P56/8p56_pocket.pdb structures/8P56/8p56_ligand.pdb structures/8P56/8p56_ligand.cif structures/8P56/8p56_complex.pdb structures/8P56/8p56_complex.cif 8P57 extended SARS-CoV-2 main protease (Mpro/3CLpro) SARS-CoV-2 ORF1ab polyprotein residues 3264-3569 Na X77 "[""X77""]" 1 IC50 IC50 = = 1.7 µM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition FRET biochemical assay with dual-labeled protease substrate; X77 is identified as the R enantiomer. 5 “The racemate showed an IC50 of 3.7 μM, while that of X77 is 1.7 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8P57\8P57_metadata.json point structures/8P57/8p57_protein.pdb structures/8P57/8p57_pocket.pdb structures/8P57/8p57_ligand.pdb structures/8P57/8p57_ligand.cif structures/8P57/8p57_complex.pdb structures/8P57/8p57_complex.cif 8P58 extended SARS-CoV-2 main protease (Mpro/3CLpro) SARS-CoV-2 ORF1ab polyprotein residues 3264-3569 Na X77 enantiomer R "[""X77""]" 1 IC50 IC50 = = 1.7 µM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition FRET biochemical assay with dual-labeled protease substrate. 5 “The racemate showed an IC50 of 3.7 μM, while that of X77 is 1.7 μM.” The text identifies X77 as the R enantiomer. auto_single_measurement only accepted activity measurement [1] 1 structures\8P58\8P58_metadata.json point structures/8P58/8p58_protein.pdb structures/8P58/8p58_pocket.pdb structures/8P58/8p58_ligand.pdb structures/8P58/8p58_ligand.cif structures/8P58/8p58_complex.pdb structures/8P58/8p58_complex.cif 8P5A extended SARS-CoV-2 main protease (Mpro/3CLpro) SARS-CoV-2 ORF1ab polyprotein residues 3264-3569 Na X77 enantiomer R "[""X77""]" 1 IC50 IC50 = = 1.7 µM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition FRET biochemical assay with dual-labeled protease substrate. 5 “The racemate showed an IC50 of 3.7 μM, while that of X77 is 1.7 μM.” The text identifies X77 as the R enantiomer. auto_single_measurement only accepted activity measurement [1] 1 structures\8P5A\8P5A_metadata.json point structures/8P5A/8p5a_protein.pdb structures/8P5A/8p5a_pocket.pdb structures/8P5A/8p5a_ligand.pdb structures/8P5A/8p5a_ligand.cif structures/8P5A/8p5a_complex.pdb structures/8P5A/8p5a_complex.cif 8P81 classic Cdk12/Cyclin K human Cdk12 kinase domain residues 714-1063 and Cyclin K cyclin box domain residues 1-267; final modeled residues Cdk12 716-1032 and Cyclin K 20-260 Na SR-4835 "[""RMF""]" 7 Kd Kd = = 93.9 nM 93.9 [] unit_conversion 7.027334407733889 success True direct_binding SPR, fully active T-loop-phosphorylated Cdk12*/CycK. 8 Figure 6A reports KD = 93.9 nM for Cdk12*/CycK with SR-4835. auto_metric_priority unique highest-priority metric family: Kd [7] 7 structures\8P81\8P81_metadata.json point structures/8P81/8p81_protein.pdb structures/8P81/8p81_pocket.pdb structures/8P81/8p81_ligand.sdf structures/8P81/8p81_ligand.pdb structures/8P81/8p81_ligand.cif structures/8P81/8p81_complex.pdb structures/8P81/8p81_complex.cif 8P87 extended SARS-CoV-2 main protease (Mpro/3CLpro) SARS-CoV-2 ORF1ab polyprotein residues 3264-3569 Na X77 "[""X77""]" 1 IC50 IC50 = = 1.7 µM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition FRET biochemical assay with dual-labeled protease substrate; X77 is identified as the R enantiomer. 5 “The racemate showed an IC50 of 3.7 μM, while that of X77 is 1.7 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8P87\8P87_metadata.json point structures/8P87/8p87_protein.pdb structures/8P87/8p87_pocket.pdb structures/8P87/8p87_ligand.pdb structures/8P87/8p87_ligand.cif structures/8P87/8p87_complex.pdb structures/8P87/8p87_complex.cif 8P8P classic Histidine Triad Nucleotide-Binding Protein 1 (HINT1) human Na Na compound 10 (5'-O-[(3-Indolyl)-1-Ethyl]Carbamoyl Ethenoadenosine) "[""X7I""]" 1 Ki Ki = = 0.132 ± 0.064 μM 132.0 [] unit_conversion 6.8794260687941495 success True biochemical_inhibition Continuous fluorescence HINT1 hydrolysis inhibition assay. 3 Table 1, “Determination of the Ki Values for Compounds 8–10,” reports compound 10 Ki = 0.132 ± 0.064 μM; the text identifies this as the continuous fluorescence HINT1 inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8P8P\8P8P_metadata.json point structures/8P8P/8p8p_protein.pdb structures/8P8P/8p8p_pocket.pdb structures/8P8P/8p8p_ligand.sdf structures/8P8P/8p8p_ligand.pdb structures/8P8P/8p8p_ligand.cif structures/8P8P/8p8p_complex.pdb structures/8P8P/8p8p_complex.cif 8P9I classic BRD4 human BRD4 BD1 residues N44-E168, N-terminal His6-tag with TEV cleavage site Na NB462 "[""X8T""]" 1 Kd Kd = = 145 nM 145.0 [] unit_conversion 6.838631997765026 success True direct_binding Isothermal titration calorimetry (ITC) measurement of NB462 binding to BRD4 BD1. 7 “ITC measurements showed that NB462 binds to BD1 with a Kd of 145 nM (Figure 2C).” auto_single_measurement only accepted activity measurement [1] 1 structures\8P9I\8P9I_metadata.json point structures/8P9I/8p9i_protein.pdb structures/8P9I/8p9i_pocket.pdb structures/8P9I/8p9i_ligand.sdf structures/8P9I/8p9i_ligand.pdb structures/8P9I/8p9i_ligand.cif structures/8P9I/8p9i_complex.pdb structures/8P9I/8p9i_complex.cif 8P9J classic BRD4 human BRD4 BD1 residues N44-E168, N-terminal His6-tag with TEV cleavage site Na NB500 "[""X8O""]" 1 Kd Kd = = 46 nM 46.0 [] unit_conversion 7.337242168318426 success True direct_binding Isothermal titration calorimetry (ITC) measurement of NB500 binding to BRD4 BD1. 7 Figure 2C visibly labels “NB500: Kd = 46 nM”; the figure caption identifies these as representative ITC data for NB500 binding to BRD4 BD1. auto_single_measurement only accepted activity measurement [1] 1 structures\8P9J\8P9J_metadata.json point structures/8P9J/8p9j_protein.pdb structures/8P9J/8p9j_pocket.pdb structures/8P9J/8p9j_ligand.sdf structures/8P9J/8p9j_ligand.pdb structures/8P9J/8p9j_ligand.cif structures/8P9J/8p9j_complex.pdb structures/8P9J/8p9j_complex.cif 8P9O extended Chaetomium thermophilum PCNA Chaetomium thermophilum Na Na Ct PolD3 PIP peptide, residues 437-451, sequence GKGGQGSIMSWFAKK "[""CHAIN:P""]" 1 Kd Kd = = 43.2 ± 3.9 µM 43200.0 [] unit_conversion 4.364516253185088 success True direct_binding Isothermal titration calorimetry at 25°C, performed in duplicate; 1 peptide:1 PCNA protomer stoichiometry. 4 “The mean dissociation constant (K_D) from two experiments was determined to be 43.2 μM ± 3.9 μM at 25°C.” auto_single_measurement only accepted activity measurement [1] 1 structures\8P9O\8P9O_metadata.json point structures/8P9O/8p9o_protein.pdb structures/8P9O/8p9o_pocket.pdb structures/8P9O/8p9o_ligand.pdb structures/8P9O/8p9o_ligand.cif structures/8P9O/8p9o_complex.pdb structures/8P9O/8p9o_complex.cif 8PA6 classic Histidine Triad Nucleotide-Binding Protein 1 (HINT1) human Na Na compound 8 (5'-O-[(3-Indolyl)-1-Ethyl]Carbamoyl 2-aminoethenoadenosine) "[""XKB""]" 1 Ki Ki = = 1.14 ± 0.07 μM 1140.0 [] unit_conversion 5.943095148663527 success True biochemical_inhibition Continuous fluorescence HINT1 hydrolysis inhibition assay. 3 Table 1, “Determination of the Ki Values for Compounds 8–10,” reports compound 8 Ki = 1.14 ± 0.07 μM; the text identifies this as the continuous fluorescence HINT1 inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8PA6\8PA6_metadata.json point structures/8PA6/8pa6_protein.pdb structures/8PA6/8pa6_pocket.pdb structures/8PA6/8pa6_ligand.sdf structures/8PA6/8pa6_ligand.pdb structures/8PA6/8pa6_ligand.cif structures/8PA6/8pa6_complex.pdb structures/8PA6/8pa6_complex.cif 8PA9 classic Histidine Triad Nucleotide-Binding Protein 1 (HINT1) human Na Na compound 9 (5'-O-[(3-Indolyl)-1-Ethyl]Carbamoyl N2-methyl-2-aminoethenoadenosine) "[""XKF""]" 1 Ki Ki = = 6.31 ± 0.09 μM 6310.0 [] unit_conversion 5.199970640755866 success True biochemical_inhibition Continuous fluorescence HINT1 hydrolysis inhibition assay. 3 Table 1, “Determination of the Ki Values for Compounds 8–10,” reports compound 9 Ki = 6.31 ± 0.09 μM; the text identifies this as the continuous fluorescence HINT1 inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8PA9\8PA9_metadata.json point structures/8PA9/8pa9_protein.pdb structures/8PA9/8pa9_pocket.pdb structures/8PA9/8pa9_ligand.sdf structures/8PA9/8pa9_ligand.pdb structures/8PA9/8pa9_ligand.cif structures/8PA9/8pa9_complex.pdb structures/8PA9/8pa9_complex.cif 8PAF classic Histidine Triad Nucleotide-Binding Protein 1 (HINT1) human Na Na compound 13 (5'-O-[N-(3-Indolepropionic acid)sulfamoyl] 2-aminoethenoadenosine) "[""XKK""]" 1 Ki Ki = = 1.43 ± 0.08 μM 1430.0 [] unit_conversion 5.844663962534938 success True biochemical_inhibition Continuous fluorescence HINT1 hydrolysis inhibition assay. 4 Table 2, “Determination of the Ki Values for Compounds 13 and 14,” reports compound 13 Ki = 1.43 ± 0.08 μM; the preceding text states inhibition was evaluated using the continuous fluorescence assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8PAF\8PAF_metadata.json point structures/8PAF/8paf_protein.pdb structures/8PAF/8paf_pocket.pdb structures/8PAF/8paf_ligand.sdf structures/8PAF/8paf_ligand.pdb structures/8PAF/8paf_ligand.cif structures/8PAF/8paf_complex.pdb structures/8PAF/8paf_complex.cif 8PAI classic Histidine Triad Nucleotide-Binding Protein 1 (HINT1) human Na Na compound 14 (5'-O-[N-(3-Indolepropionic acid)sulfamoyl] N2-methyl-2-aminoethenoadenosine) "[""XKO""]" 1 Ki Ki = = 0.730 ± 0.090 μM 730.0 [] unit_conversion 6.136677139879544 success True biochemical_inhibition Continuous fluorescence HINT1 hydrolysis inhibition assay. 4 Table 2, “Determination of the Ki Values for Compounds 13 and 14,” reports compound 14 Ki = 0.730 ± 0.090 μM; the preceding text states inhibition was evaluated using the continuous fluorescence assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8PAI\8PAI_metadata.json point structures/8PAI/8pai_protein.pdb structures/8PAI/8pai_pocket.pdb structures/8PAI/8pai_ligand.sdf structures/8PAI/8pai_ligand.pdb structures/8PAI/8pai_ligand.cif structures/8PAI/8pai_complex.pdb structures/8PAI/8pai_complex.cif 8PBO classic Peroxisome proliferator-activated receptor gamma (PPARgamma) Homo sapiens PPARgamma L204-Y477 fused to MGSS-His6-SG-TEV Na Compound 1 "[""Y5I""]" 1 Kd Kd = = 0.8 ± 0.1 μM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Isothermal titration calorimetry (ITC) measuring Compound 1 binding to the PPARγ ligand-binding domain. 6 “Compound 1 was characterized for its affinity to the ligand binding domain of PPARγ by isothermal titration calorimetry (ITC), yielding a measured dissociation constant of K_D = 0.8 ± 0.1 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8PBO\8PBO_metadata.json point structures/8PBO/8pbo_protein.pdb structures/8PBO/8pbo_pocket.pdb structures/8PBO/8pbo_ligand.sdf structures/8PBO/8pbo_ligand.pdb structures/8PBO/8pbo_ligand.cif structures/8PBO/8pbo_complex.pdb structures/8PBO/8pbo_complex.cif 8PC2 classic FKBP51 Na FKBP51 FK1 domain and pVHL:EloB:EloC Na SelDeg51 "[""XZW""]" 1 Kd Kd = = 0.78 ± 0.07 nM 0.78 [] unit_conversion 9.10790539730952 success True direct_binding Competitive HTRF assay using an FKBP-HTRF tracer in the presence of excess (5 μM) VCB; ternary FKBP51FK1–SelDeg51–VCB condition. 3 Table 1 lists SelDeg51 K_D(PROTAC:VCB) = 0.78 ± 0.07 nM; the table states this is binding to FKBP51FK1 in the presence of an excess of VCB. auto_single_measurement only accepted activity measurement [1] 1 structures\8PC2\8PC2_metadata.json point structures/8PC2/8pc2_protein.pdb structures/8PC2/8pc2_pocket.pdb structures/8PC2/8pc2_ligand.sdf structures/8PC2/8pc2_ligand.pdb structures/8PC2/8pc2_ligand.cif structures/8PC2/8pc2_complex.pdb structures/8PC2/8pc2_complex.cif 8PD1 classic Pseudomonas aeruginosa FabF Pseudomonas aeruginosa FabF C164A mutant C164A 132; N-isopropyl-1H-imidazole-4-carboxamide "[""YHU""]" 1 Kd Kd = = 480 ± 120 µM 480000.0 [] unit_conversion 3.3187587626244124 success True direct_binding Bio-layer interferometry (BLI); Table 4 reports the KD as an average of two experiments for compound 132. 13 Table 4 lists compound 132 with KD 480 ± 120 µM and PDB ID 8PD1; the table states values were determined using PaFabF C164A. auto_single_measurement only accepted activity measurement [1] 1 structures\8PD1\8PD1_metadata.json point structures/8PD1/8pd1_protein.pdb structures/8PD1/8pd1_pocket.pdb structures/8PD1/8pd1_ligand.sdf structures/8PD1/8pd1_ligand.pdb structures/8PD1/8pd1_ligand.cif structures/8PD1/8pd1_complex.pdb structures/8PD1/8pd1_complex.cif 8PD6 classic TRIM58 Na TRIM58(251-466)C277S,C278S C277S,C278S TRIM-473 "[""YCB""]" 1 Kd Kd = = 24 μM 24000.0 [] unit_conversion 4.619788758288394 success True direct_binding SPR binding experiment using TRIM58(251–466)C277S,C278S-Avi and TRIM-473; equilibrium fit shown. 4 Figure 2D states that SPR measured the interaction of TRIM58(251–466)C277S,C278S-Avi with TRIM-473 and reports Kd = 24 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8PD6\8PD6_metadata.json point structures/8PD6/8pd6_protein.pdb structures/8PD6/8pd6_pocket.pdb structures/8PD6/8pd6_ligand.sdf structures/8PD6/8pd6_ligand.pdb structures/8PD6/8pd6_ligand.cif structures/8PD6/8pd6_complex.pdb structures/8PD6/8pd6_complex.cif 8PE0 classic PilF-GSPII-B domain Thermus thermophilus PilF159-302 K167L c-di-GMP "[""C2E""]" 1 Kd Kd = = 2 ± 0.3 nM 2.0 [] unit_conversion 8.698970004336019 success True direct_binding ITC measurement of PilF159-302 K167L binding c-di-GMP. 10 The ITC measurement with PilF159-302 K167L yields a KD value of 2 ± 0.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8PE0\8PE0_metadata.json point structures/8PE0/8pe0_protein.pdb structures/8PE0/8pe0_pocket.pdb structures/8PE0/8pe0_ligand.sdf structures/8PE0/8pe0_ligand.pdb structures/8PE0/8pe0_ligand.cif structures/8PE0/8pe0_complex.pdb structures/8PE0/8pe0_complex.cif 8PFA classic PilF-GSPII-B domain Thermus thermophilus PilF159-302 K167R c-di-GMP "[""C2E""]" 1 Kd Kd = = 150 ± 7 nM 150.0 [] unit_conversion 6.823908740944319 success True direct_binding ITC measurement of PilF159-302 K167R binding c-di-GMP. 9 ITC measurements with PilF159-302 K167R revealed a KD value of 150 ± 7 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8PFA\8PFA_metadata.json point structures/8PFA/8pfa_protein.pdb structures/8PFA/8pfa_pocket.pdb structures/8PFA/8pfa_ligand.sdf structures/8PFA/8pfa_ligand.pdb structures/8PFA/8pfa_ligand.cif structures/8PFA/8pfa_complex.pdb structures/8PFA/8pfa_complex.cif 8PFZ classic Pseudomonas aeruginosa FabF Pseudomonas aeruginosa FabF C164A mutant C164A 136; (S)-2-(1H-pyrazole-3-carboxamido)butanoic acid "[""YQI""]" 1 Kd Kd = = 840 ± 140 µM 840000.0 [] unit_conversion 3.075720713938118 success True direct_binding Bio-layer interferometry (BLI); Table 4 reports the KD as an average of three experiments for compound 136. 13 Table 4 lists compound 136 with KD 840 ± 140 µM and PDB ID 8PFZ; the table states values were determined using PaFabF C164A. auto_single_measurement only accepted activity measurement [1] 1 structures\8PFZ\8PFZ_metadata.json point structures/8PFZ/8pfz_protein.pdb structures/8PFZ/8pfz_pocket.pdb structures/8PFZ/8pfz_ligand.sdf structures/8PFZ/8pfz_ligand.pdb structures/8PFZ/8pfz_ligand.cif structures/8PFZ/8pfz_complex.pdb structures/8PFZ/8pfz_complex.cif 8PH4 classic SARS-CoV-2 main protease (Mpro, nsp5) SARS-CoV-2 Na wild-type (wt) 35b "[""YQN""]" 1 Kd Kd = = 82.6 ± 5.5 µM 82600.0 [] unit_conversion 4.083019952679618 success True direct_binding Kd determination from combined NMR chemical-shift perturbations for the first binding site of 35b. 7 Figure 5 caption: “KD determination derived from combined CSPs for the first (left) ... binding sites of 35b”; panel f prints “KD = 82.6 ± 5.5 µM”. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\8PH4\8PH4_metadata.json point structures/8PH4/8ph4_protein.pdb structures/8PH4/8ph4_pocket.pdb structures/8PH4/8ph4_ligand.sdf structures/8PH4/8ph4_ligand.pdb structures/8PH4/8ph4_ligand.cif structures/8PH4/8ph4_complex.pdb structures/8PH4/8ph4_complex.cif 8PHI classic Prefusion-stabilized RSV F Variant DS-Cav1 Na Soluble trimeric RSV F ectodomain in prefusion conformation, stabilized by DS-Cav1 design Na Lonafarnib "[""336""]" 1 Kd Kd = = 180 ± 10 µM 180000.0 [] unit_conversion 3.7447274948966935 success True direct_binding Surface plasmon resonance using immobilized recombinant RSV subtype A prefusion F protein; lonafarnib concentration series 1.56–100 µM. 5 Fig. 4F prints lonafarnib binding kinetics and “K_D: 180 +/- 10 µM”; the caption identifies surface plasmon resonance with immobilized RSV subtype A prefusion F protein. Methods describe recombinant RSV F stabilized by the DS-Cav1 design. auto_single_measurement only accepted activity measurement [1] 1 structures\8PHI\8PHI_metadata.json point structures/8PHI/8phi_protein.pdb structures/8PHI/8phi_pocket.pdb structures/8PHI/8phi_ligand.sdf structures/8PHI/8phi_ligand.pdb structures/8PHI/8phi_ligand.cif structures/8PHI/8phi_complex.pdb structures/8PHI/8phi_complex.cif 8PI0 classic KRAS Na Na G12V fragment 15; 5-(1H-indol-2-l)piperazin-2-one "[""YVW""]" 1 Kd Kd = = 3.04 mM 3040000.0 [] unit_conversion 2.517126416391246 success True direct_binding Ligand-titrated [15N,1H]-HSQC chemical-shift-perturbation affinity determination; GMP-PNP-bound KRAS context. 4 Table 1 lists fragment 15 with K_D 3.04 mM and PDB code 8PI0. auto_single_measurement only accepted activity measurement [1] 1 structures\8PI0\8PI0_metadata.json point structures/8PI0/8pi0_protein.pdb structures/8PI0/8pi0_pocket.pdb structures/8PI0/8pi0_ligand.sdf structures/8PI0/8pi0_ligand.pdb structures/8PI0/8pi0_ligand.cif structures/8PI0/8pi0_complex.pdb structures/8PI0/8pi0_complex.cif 8PJ0 classic FabF (beta-ketoacyl-ACP synthase 2) Pseudomonas aeruginosa Na C164A compound 1 (EOS102727; N-(1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro-1H-pyrazol-4-yl)-3-methylbutanamide) "[""ZHX""]" 1 Kd Kd = = 35 ± 1 µM 35000.0 [] unit_conversion 4.455931955649724 success True direct_binding BLI steady-state binding; average of three experiments using repurchased material. 9 Table 3 reports PaFabF C164A K_D for compound 1 as 35 ± 1 µM; Fig. 6 maps fragment hit 1 to PDB 8PJ0. auto_single_measurement only accepted activity measurement [1] 1 structures\8PJ0\8PJ0_metadata.json point structures/8PJ0/8pj0_protein.pdb structures/8PJ0/8pj0_pocket.pdb structures/8PJ0/8pj0_ligand.sdf structures/8PJ0/8pj0_ligand.pdb structures/8PJ0/8pj0_ligand.cif structures/8PJ0/8pj0_complex.pdb structures/8PJ0/8pj0_complex.cif 8PK5 extended INTS13-INTS14 complex with ZNF609 Homo sapiens INTS13-INTS14-ZNF609 residues 25-41 (sIBM) Na Na "[""CHAIN:B""]" 1 Kd Kd >= >= 0.57 µM 570.0 [] unit_conversion 6.2441251443275085 success True direct_binding Fluorescence-polarization affinity measurement of GFP-tagged IBM peptides with INTS13-14. 5 Figure 2O prints Kd for ZNF609 as ≥0.57 µM; the Figure 2 legend identifies fluorescence-polarization measurements for GFP-tagged IBMs and INTS13-14. auto_single_measurement only accepted activity measurement [1] 1 structures\8PK5\8PK5_metadata.json point structures/8PK5/8pk5_protein.pdb structures/8PK5/8pk5_pocket.pdb structures/8PK5/8pk5_ligand.pdb structures/8PK5/8pk5_ligand.cif structures/8PK5/8pk5_complex.pdb structures/8PK5/8pk5_complex.cif 8PKU extended KEAP1 Na Kelch domain of KEAP1 Na ortho-dimethylbenzene linked cyclic peptide 3 (ortho-WRCDEETGEC) "[""CHAIN:P""]" 1 Kd Kd = = 48 ± 10 nM 48.0 [] unit_conversion 7.318758762624412 success True direct_binding Bio-layer interferometry (BLI); experimentally measured binding affinity for CP3 to recombinant Keap1; mean/standard error from three independent trials. 7 Table 1 reports CP3 Kd = 48 ± 10 nM; the table states Kd values were measured by biolayer interferometry. The text identifies CP3 as the ortho-dimethylbenzene-linked cyclic peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\8PKU\8PKU_metadata.json point structures/8PKU/8pku_protein.pdb structures/8PKU/8pku_pocket.pdb structures/8PKU/8pku_ligand.pdb structures/8PKU/8pku_ligand.cif structures/8PKU/8pku_complex.pdb structures/8PKU/8pku_complex.cif 8PKV extended KEAP1 Na Kelch domain of KEAP1 Na ortho-dimethylbenzene linked cyclic peptide 4 (ortho-WRCDPETGEC) "[""CHAIN:P""]" 1 Kd Kd = = 15 ± 1 nM 15.0 [] unit_conversion 7.823908740944319 success True direct_binding Bio-layer interferometry (BLI); experimentally measured binding affinity for CP4 to recombinant Keap1; mean/standard error from three independent trials. 7 Table 1 reports CP4 Kd = 15 ± 1 nM; the table states Kd values were measured by biolayer interferometry. auto_single_measurement only accepted activity measurement [1] 1 structures\8PKV\8PKV_metadata.json point structures/8PKV/8pkv_protein.pdb structures/8PKV/8pkv_pocket.pdb structures/8PKV/8pkv_ligand.pdb structures/8PKV/8pkv_ligand.cif structures/8PKV/8pkv_complex.pdb structures/8PKV/8pkv_complex.cif 8PKW extended KEAP1 Na Kelch domain of KEAP1 Na ortho-dimethylbenzene linked cyclic peptide 5 (ortho-WRCDPETaEC) "[""CHAIN:P""]" 1 Kd Kd = = 8.4 ± 0.6 nM 8.4 [] unit_conversion 8.075720713938118 success True direct_binding Bio-layer interferometry (BLI); experimentally measured binding affinity for CP5 to recombinant Keap1; mean/standard error from three independent trials. 7 Table 1 reports CP5 Kd = 8.4 ± 0.6 nM; the table states Kd values were measured by biolayer interferometry. auto_single_measurement only accepted activity measurement [1] 1 structures\8PKW\8PKW_metadata.json point structures/8PKW/8pkw_protein.pdb structures/8PKW/8pkw_pocket.pdb structures/8PKW/8pkw_ligand.pdb structures/8PKW/8pkw_ligand.cif structures/8PKW/8pkw_complex.pdb structures/8PKW/8pkw_complex.cif 8PKX extended KEAP1 Na Kelch domain of KEAP1 Na ortho-dimethylbenzene linked cyclic peptide 11 (ortho-WRCNPETaEC) "[""CHAIN:P""]" 1 Kd Kd = = 4.7 ± 1.7 nM 4.7 [] unit_conversion 8.327902142064282 success True direct_binding Bio-layer interferometry (BLI); experimentally measured binding affinity for CP11 to recombinant Keap1; mean/standard error from three independent trials. 7 Table 1 reports CP11 Kd = 4.7 ± 1.7 nM; the table states Kd values were measured by biolayer interferometry. auto_single_measurement only accepted activity measurement [1] 1 structures\8PKX\8PKX_metadata.json point structures/8PKX/8pkx_protein.pdb structures/8PKX/8pkx_pocket.pdb structures/8PKX/8pkx_ligand.pdb structures/8PKX/8pkx_ligand.cif structures/8PKX/8pkx_complex.pdb structures/8PKX/8pkx_complex.cif 8PM6 classic human BSEP human BSEP in nanodiscs Na GBM (glibenclamide) "[""GBM""]" 1 IC50 IC50 ~ ~ 10 μM 10000.0 [] unit_conversion 5.0 success True biochemical_inhibition [3H]-taurocholate transport by proteoliposome-reconstituted BSEP; GBM reduced uptake dose-dependently. 3 “The 3H-TC uptake by proteoliposome-reconstituted BSEP was also reduced by adding GBM in a dose-dependent manner, with an inhibition constant IC50 of ~10 μM.” auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\8PM6\8PM6_metadata.json point structures/8PM6/8pm6_protein.pdb structures/8PM6/8pm6_pocket.pdb structures/8PM6/8pm6_ligand.sdf structures/8PM6/8pm6_ligand.pdb structures/8PM6/8pm6_ligand.cif structures/8PM6/8pm6_complex.pdb structures/8PM6/8pm6_complex.cif 8PM8 classic transthyretin (TTR) Na Na V30M Tolcapone "[""TCW""]" 1 Kd Kd = = 440 nM 440.0 [] unit_conversion 6.356547323513812 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 thermodynamic parameters for Tolcapone interaction with V30M-TTR. 4 Table 2 reports a Tolcapone Kd of 440 nM for V30M-TTR. Page 8 assigns PDB 8PM8 to Tolcapone:V30M. auto_single_measurement only accepted activity measurement [1] 1 structures\8PM8\8PM8_metadata.json point structures/8PM8/8pm8_protein.pdb structures/8PM8/8pm8_pocket.pdb structures/8PM8/8pm8_ligand.sdf structures/8PM8/8pm8_ligand.pdb structures/8PM8/8pm8_ligand.cif structures/8PM8/8pm8_complex.pdb structures/8PM8/8pm8_complex.cif 8PM9 classic transthyretin (TTR) human Na wild type (WT) PITB (Pharmacokinetically Improved TTR Binder) "[""ZP2""]" 1 Kd Kd = = 16 nM 16.0 [] unit_conversion 7.795880017344075 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 thermodynamic parameters for PITB interaction with WT-TTR. 4 Table 2 reports a PITB Kd of 16 nM for WT-TTR. Page 8 assigns PDB 8PM9 to PITB:WT. auto_single_measurement only accepted activity measurement [1] 1 structures\8PM9\8PM9_metadata.json point structures/8PM9/8pm9_protein.pdb structures/8PM9/8pm9_pocket.pdb structures/8PM9/8pm9_ligand.sdf structures/8PM9/8pm9_ligand.pdb structures/8PM9/8pm9_ligand.cif structures/8PM9/8pm9_complex.pdb structures/8PM9/8pm9_complex.cif 8PMA classic transthyretin (TTR) human Na V30M PITB (Pharmacokinetically Improved TTR Binder) "[""ZP2""]" 1 Kd Kd = = 36 nM 36.0 [] unit_conversion 7.443697499232712 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 thermodynamic parameters for PITB interaction with V30M-TTR. 4 Table 2 reports a PITB Kd of 36 nM for V30M-TTR. Page 8 assigns PDB 8PMA to PITB:V30M. auto_single_measurement only accepted activity measurement [1] 1 structures\8PMA\8PMA_metadata.json point structures/8PMA/8pma_protein.pdb structures/8PMA/8pma_pocket.pdb structures/8PMA/8pma_ligand.sdf structures/8PMA/8pma_ligand.pdb structures/8PMA/8pma_ligand.cif structures/8PMA/8pma_complex.pdb structures/8PMA/8pma_complex.cif 8PMO classic transthyretin (TTR) human Na V122I PITB (Pharmacokinetically Improved TTR Binder) "[""ZP2""]" 1 Kd Kd = = 14 nM 14.0 [] unit_conversion 7.853871964321762 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 thermodynamic parameters for PITB interaction with V122I-TTR. 4 Table 2 reports a PITB Kd of 14 nM for V122I-TTR. Page 8 assigns PDB 8PMO to PITB:V122I. auto_single_measurement only accepted activity measurement [1] 1 structures\8PMO\8PMO_metadata.json point structures/8PMO/8pmo_protein.pdb structures/8PMO/8pmo_pocket.pdb structures/8PMO/8pmo_ligand.sdf structures/8PMO/8pmo_ligand.pdb structures/8PMO/8pmo_ligand.cif structures/8PMO/8pmo_complex.pdb structures/8PMO/8pmo_complex.cif 8POI classic SPF30 (SMNDC1) Na SMNDC1 residues 65-128 Na Compound 13; 4-(pyridin-2-yl)thiazol-2-amine "[""ZTI""]" 1 IC50 IC50 = = 0.53 µM 530.0 [] unit_conversion 6.275724130399211 success True biochemical_inhibition AlphaScreen titration of the SMNDC1 Tudor domain against an sDMA peptide. 8 Fig. 5 prints compound 13 with SMNDC1 IC50 0.53 µM; the text identifies compound 13 as the monobasic phosphate salt used for SMNDC1 Tudor-domain NMR titrations. auto_single_measurement only accepted activity measurement [1] 1 structures\8POI\8POI_metadata.json point structures/8POI/8poi_protein.pdb structures/8POI/8poi_pocket.pdb structures/8POI/8poi_ligand.sdf structures/8POI/8poi_ligand.pdb structures/8POI/8poi_ligand.cif structures/8POI/8poi_complex.pdb structures/8POI/8poi_complex.cif 8PPX classic Influenza A PA endonuclease Influenza A virus PA-Nter comprising the first 196 amino acids from A/California/07/2009 (H1N1), with residues 51-72 replaced by a GGS linker Residues 51-72 replaced by a GGS linker compound 36; 5-hydroxy-2-(4,5,7-trihydroxynaphthalen-2-yl)pyrimidin-4(3H)-one "[""85W""]" 1 IC50 IC50 = = 1.7 ± 0.3 µM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition AlphaScreen binding/inhibition assay of influenza endonuclease using recombinant PA-Nter. 6 Table 2 reports compound 36 IC50 ± SD of 1.7 ± 0.3 µM (AlphaScreen). The text identifies the PA-Nter–36 crystal structure as PDB 8PPX; the experimental section defines the recombinant PA-Nter construct. auto_single_measurement only accepted activity measurement [1] 1 structures\8PPX\8PPX_metadata.json point structures/8PPX/8ppx_protein.pdb structures/8PPX/8ppx_pocket.pdb structures/8PPX/8ppx_ligand.sdf structures/8PPX/8ppx_ligand.pdb structures/8PPX/8ppx_ligand.cif structures/8PPX/8ppx_complex.pdb structures/8PPX/8ppx_complex.cif 8PQR classic Nucleoside 2'-deoxyribosyltransferase (CtNDT) Chroococcidiopsis thermalis PCC 7203 Na WT DAD_Immucillin-H (DADMe-immucillin-H; DADMeH) "[""DIH""]" 1 Kd Kd = = 9 ± 5 nM 9.0 [] unit_conversion 8.045757490560675 success True direct_binding Isothermal titration calorimetry of wild-type CtNDT with DADMeH. 8 The paper reports for DADMeH: K_D = 9 ± 5 nM; Figure 4 states that wild-type CtNDT was present in the cell during ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8PQR\8PQR_metadata.json point structures/8PQR/8pqr_protein.pdb structures/8PQR/8pqr_pocket.pdb structures/8PQR/8pqr_ligand.sdf structures/8PQR/8pqr_ligand.pdb structures/8PQR/8pqr_ligand.cif structures/8PQR/8pqr_complex.pdb structures/8PQR/8pqr_complex.cif 8PUP classic Influenza A virus polymerase acidic subunit (PA) Influenza A virus, strain A/California/07/2009 (H1N1) PA N-terminal domain, residues 1-196, with flexible-loop residues 51-72 replaced by a GGS linker Residues 51-72 replaced by a GGS linker Compound 10a, N-(4-hydroxybenzyl)-3,4,6-trihydroxy-5-oxo-1-phenyl-5H-benzocycloheptene-8-carboxamide "[""H2I""]" 1 IC50 IC50 = = 1.5 ± 0.2 µM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition AlphaScreen inhibition assay of the GST-PA-Nter/L-742.001-biotin interaction; Table 1 reports the biochemical IC50 for compound 10a. 4 Table 1 lists compound 10a with IC50 = 1.5 ± 0.2 µM. The text identifies these as AlphaScreen biochemical assay values against influenza A endonuclease. auto_single_measurement only accepted activity measurement [1] 1 structures\8PUP\8PUP_metadata.json point structures/8PUP/8pup_protein.pdb structures/8PUP/8pup_pocket.pdb structures/8PUP/8pup_ligand.sdf structures/8PUP/8pup_ligand.pdb structures/8PUP/8pup_ligand.cif structures/8PUP/8pup_complex.pdb structures/8PUP/8pup_complex.cif 8PWC classic MDM2 Na Na Na Brigimadlin (BI 907828) "[""G7I""]" 1 IC50 IC50 = = 2 nmol/L 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition AlphaScreen assay of MDM2-p53 protein-protein interaction. 5 Figure 1 explicitly prints: “IC50 (MDM2–p53) = 2 nmol/L” for Brigimadlin (1). auto_single_measurement only accepted activity measurement [1] 1 structures\8PWC\8PWC_metadata.json point structures/8PWC/8pwc_protein.pdb structures/8PWC/8pwc_pocket.pdb structures/8PWC/8pwc_ligand.sdf structures/8PWC/8pwc_ligand.pdb structures/8PWC/8pwc_ligand.cif structures/8PWC/8pwc_complex.pdb structures/8PWC/8pwc_complex.cif 8PWO classic Hepatitis B core protein (HBc) Hepatitis B virus, genotype D, strain ayw Recombinant HBc capsid-like particles (CLPs), major capsid type T=4 wild-type Geraniol (2) "[""64Z""]" 1 Kd Kd = = 94 ± 7.9 µM 94000.0 [] unit_conversion 4.026872146400302 success True direct_binding Isothermal titration calorimetry (ITC) of geraniol with purified HBc capsids. 5 “geraniol displayed a slightly enhanced micromolar affinity (K_D = 94 ± 7.9 µM)” auto_single_measurement only accepted activity measurement [1] 1 structures\8PWO\8PWO_metadata.json point structures/8PWO/8pwo_protein.pdb structures/8PWO/8pwo_pocket.pdb structures/8PWO/8pwo_ligand.sdf structures/8PWO/8pwo_ligand.pdb structures/8PWO/8pwo_ligand.cif structures/8PWO/8pwo_complex.pdb structures/8PWO/8pwo_complex.cif 8PX3 extended Hepatitis B core protein (HBc) Hepatitis B virus, genotype D, strain ayw Recombinant HBc capsid-like particles (CLPs), major capsid type T=4 wild-type P1dC (P1-dimer, 7) "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 0.42 ± 0.04 µM 420.0 [] unit_conversion 6.376750709602099 success True direct_binding ITC of HBc with peptide dimers; Figure 3 identifies compound 7 as P1dC. 6 Figure 3C reports “(7) K_D=0.42±0.04 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8PX3\8PX3_metadata.json point structures/8PX3/8px3_protein.pdb structures/8PX3/8px3_pocket.pdb structures/8PX3/8px3_ligand.pdb structures/8PX3/8px3_ligand.cif structures/8PX3/8px3_complex.pdb structures/8PX3/8px3_complex.cif 8PX6 extended Hepatitis B core protein (HBc) Hepatitis B virus, genotype D, strain ayw Recombinant HBc capsid-like particles (CLPs), major capsid type T=4 wild-type SLLGRM-dimer (4) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 4.9 ± 0.7 µM 4900.0 [] unit_conversion 5.309803919971486 success True direct_binding ITC of HBc with peptide dimers; Figure 3 identifies compound 4 as the SLLGRM dimer. 6 Figure 3C reports “(4) K_D=4.9±0.7 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8PX6\8PX6_metadata.json point structures/8PX6/8px6_protein.pdb structures/8PX6/8px6_pocket.pdb structures/8PX6/8px6_ligand.pdb structures/8PX6/8px6_ligand.cif structures/8PX6/8px6_complex.pdb structures/8PX6/8px6_complex.cif 8PXA extended BRD4 human BRD4 BD1 Na compound 31 (GSK023; (S)-5-(1-((1-(1-isopropylpiperidine-4-carbonyl)piperidin-3-yl)methyl)-1H-benzo[d]imidazol-2-yl)-1,3-dimethylpyridin-2(1H)-one) "[""I0Z""]" 2 pKd Kd = = 8.1 unitless 7.943282347242821 [] p_metric_transform 8.1 success True direct_binding BROMOscan recombinant-protein binding assay. 12 Table 3 reports BRD4 BD1 BROMOscan pKd of 8.1 for compound 31. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8PXA\8PXA_metadata.json point structures/8PXA/8pxa_ligand.sdf structures/8PXA/8pxa_ligand.cif structures/8PXA/8pxa_complex.cif 8PXX extended PRPF40A Na WW12, PRPF40A residues 141-236 Na SF1_WWbs peptide (SF1 residues 575-590; PPLPGAPPPPPPPP) "[""CHAIN:B""]" 1 Kd Kd = = 1.40 ± 0.16 µM 1400.0 [] unit_conversion 5.853871964321762 success True direct_binding ITC titration of PRPF40A WW12 with SF1_WWbs peptide; fitted stoichiometry N = 1.00 ± 0.03. 4 Fig. 2 identifies the highest-affinity peptide as SF1_WWbs and reports its ITC fit: Kd = 1.40 ± 0.16 µM, N = 1.00 ± 0.03. auto_single_measurement only accepted activity measurement [1] 1 structures\8PXX\8PXX_metadata.json point structures/8PXX/8pxx_protein.pdb structures/8PXX/8pxx_pocket.pdb structures/8PXX/8pxx_ligand.pdb structures/8PXX/8pxx_ligand.cif structures/8PXX/8pxx_complex.pdb structures/8PXX/8pxx_complex.cif 8PY0 classic Oscillibacter ruminantium chemoreceptor Oscillibacter ruminantium sensor domain (ligand-binding domain, LBD) Na formate "[""FMT""]" 1 Kd Kd = = 63 ± 0.4 μM 63000.0 [] unit_conversion 4.200659450546418 success True direct_binding Isothermal titration calorimetry of 50 μM R6 with 5 mM Na formate. 6 Table 1 reports R6 (Oscillibacter ruminantium) K_D = 63 ± 0.4 μM; Fig. 4B shows ITC titration of R6 with Na formate. auto_single_measurement only accepted activity measurement [1] 1 structures\8PY0\8PY0_metadata.json point structures/8PY0/8py0_protein.pdb structures/8PY0/8py0_pocket.pdb structures/8PY0/8py0_ligand.sdf structures/8PY0/8py0_ligand.pdb structures/8PY0/8py0_ligand.cif structures/8PY0/8py0_complex.pdb structures/8PY0/8py0_complex.cif 8PY1 classic Asticcacaulis benevestitus chemoreceptor Asticcacaulis benevestitus sensor domain (ligand-binding domain, LBD) Na formate "[""FMT""]" 1 Kd Kd = = 5.6 ± 0.3 μM 5600.0 [] unit_conversion 5.251811972993799 success True direct_binding Isothermal titration calorimetry of 30 μM R3 with 1 mM Na formate. 6 Table 1 reports R3 (Asticcacaulis benevestitus) K_D = 5.6 ± 0.3 μM; Fig. 4A shows ITC titration of R3 with Na formate. auto_single_measurement only accepted activity measurement [1] 1 structures\8PY1\8PY1_metadata.json point structures/8PY1/8py1_protein.pdb structures/8PY1/8py1_pocket.pdb structures/8PY1/8py1_ligand.sdf structures/8PY1/8py1_ligand.pdb structures/8PY1/8py1_ligand.cif structures/8PY1/8py1_complex.pdb structures/8PY1/8py1_complex.cif 8Q05 extended Chlorella sorokiniana Rubisco Chlorella sorokiniana CsRubisco holoenzyme with CsLinker alpha3-alpha4 fragment, residues 142-272 Na CsLinker alpha3-alpha4 fragment "[""CHAIN:Z""]" 1 Kd Kd = = 1.21 µM 1210.0 [] unit_conversion 5.917214629683549 success True direct_binding Surface plasmon resonance using immobilized CsRubisco and CsLinker α3–α4 fragment as prey; reported 95% CI 1.10–1.33 µM. 3 “SPR experiments in which CsRubisco was immobilized as bait, and the α3–α4 fragments were used as prey ... K_D of the α3–α4 fragment for CsRubisco (1.21 µM, CI95: 1.10–1.33 µM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8Q05\8Q05_metadata.json point structures/8Q05/8q05_protein.pdb structures/8Q05/8q05_pocket.pdb structures/8Q05/8q05_ligand.pdb structures/8Q05/8q05_ligand.cif structures/8Q05/8q05_complex.pdb structures/8Q05/8q05_complex.cif 8Q0T classic Pks13 (polyketide synthase 13) Mycobacterium tuberculosis Pks13 thioesterase domain Na Compound 50 "[""IJJ""]" 1 IC50 IC50 = = 0.3 μM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition In vitro Pks13 TE-domain enzyme inhibition assay. 10 Table 1 reports compound 50 Pks13 IC50 = 0.3 μM; its footnote defines this as M. tuberculosis Pks13 TE-domain 50% inhibitory concentration. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q0T\8Q0T_metadata.json point structures/8Q0T/8q0t_protein.pdb structures/8Q0T/8q0t_pocket.pdb structures/8Q0T/8q0t_ligand.sdf structures/8Q0T/8q0t_ligand.pdb structures/8Q0T/8q0t_ligand.cif structures/8Q0T/8q0t_complex.pdb structures/8Q0T/8q0t_complex.cif 8Q0U classic Pks13 (polyketide synthase 13) Mycobacterium tuberculosis Pks13 thioesterase domain Na Compound 33 "[""IKG""]" 1 IC50 IC50 = = 0.4 μM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition In vitro Pks13 TE-domain enzyme inhibition assay. 14 Table 6 reports compound 33 Pks13 IC50 = 0.4 μM; table footnotes define the endpoint as M. tuberculosis Pks13 TE-domain 50% inhibitory concentration. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q0U\8Q0U_metadata.json point structures/8Q0U/8q0u_protein.pdb structures/8Q0U/8q0u_pocket.pdb structures/8Q0U/8q0u_ligand.sdf structures/8Q0U/8q0u_ligand.pdb structures/8Q0U/8q0u_ligand.cif structures/8Q0U/8q0u_complex.pdb structures/8Q0U/8q0u_complex.cif 8Q17 classic Pks13 (polyketide synthase 13) Mycobacterium tuberculosis Pks13 thioesterase domain Na Compound 14 "[""IL8""]" 1 IC50 IC50 = = 0.3 μM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition In vitro Pks13 TE-domain enzyme inhibition assay. 11 Table 2 reports compound 14 Pks13 IC50 = 0.3 μM; table footnotes define the endpoint as M. tuberculosis Pks13 TE-domain 50% inhibitory concentration. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q17\8Q17_metadata.json point structures/8Q17/8q17_protein.pdb structures/8Q17/8q17_pocket.pdb structures/8Q17/8q17_ligand.sdf structures/8Q17/8q17_ligand.pdb structures/8Q17/8q17_ligand.cif structures/8Q17/8q17_complex.pdb structures/8Q17/8q17_complex.cif 8Q1G extended LSD1-CoREST1 Na wild-type LSD1/Delta305CoREST1 wild-type LSD1 H3K4M-K14ac peptide "[""CHAIN:C""]" 1 IC50 IC50 = = 5.77 ± 1.18 µM 5770.0 [] unit_conversion 5.238824186844269 success True biochemical_inhibition LSD1 demethylase inhibition by peptide; 200 nM LC and 150 µM H3K4me2 peptide substrate. 7 Supplementary Figure 4a prints “H3K4M-K14ac: 5.77 ± 1.18 µM”; Supplementary Figure 2 identifies wild-type LSD1/Δ305CoREST1 with H3K4M-K14ac as PDB 8Q1G. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q1G\8Q1G_metadata.json point structures/8Q1G/8q1g_protein.pdb structures/8Q1G/8q1g_pocket.pdb structures/8Q1G/8q1g_ligand.pdb structures/8Q1G/8q1g_ligand.cif structures/8Q1G/8q1g_complex.pdb structures/8Q1G/8q1g_complex.cif 8Q1H extended LSD1-CoREST1 Na Y391K LSD1/Delta305CoREST1 Y391K LSD1 H3K4M peptide (Histone H3 N-terminal tail) "[""CHAIN:C""]" 1 IC50 IC50 = = 0.77 ± 0.09 µM 770.0 [] unit_conversion 6.113509274827518 success True biochemical_inhibition LSD1 demethylase inhibition by peptide; assay conditions stated to be the same as Supplementary Figure 4a. 7 Supplementary Figure 4b prints “H3K4M: 0.77 ± 0.09 µM”; Supplementary Figure 2 identifies Y391K LSD1/Δ305CoREST1 with H3K4M as PDB 8Q1H. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q1H\8Q1H_metadata.json point structures/8Q1H/8q1h_protein.pdb structures/8Q1H/8q1h_pocket.pdb structures/8Q1H/8q1h_ligand.pdb structures/8Q1H/8q1h_ligand.cif structures/8Q1H/8q1h_complex.pdb structures/8Q1H/8q1h_complex.cif 8Q1J extended LSD1-CoREST1 Na Y391K LSD1/Delta305CoREST1 Y391K LSD1 H3K4M-K14ac peptide "[""CHAIN:C""]" 1 IC50 IC50 = = 9.76 ± 1.87 µM 9760.0 [] unit_conversion 5.010550182333308 success True biochemical_inhibition LSD1 demethylase inhibition by peptide; assay conditions stated to be the same as Supplementary Figure 4a. 7 Supplementary Figure 4b prints “H3K4M-K14ac: 9.76 ± 1.87 µM”; Supplementary Figure 2 identifies Y391K LSD1/Δ305CoREST1 with H3K4M-K14ac as PDB 8Q1J. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q1J\8Q1J_metadata.json point structures/8Q1J/8q1j_protein.pdb structures/8Q1J/8q1j_pocket.pdb structures/8Q1J/8q1j_ligand.pdb structures/8Q1J/8q1j_ligand.cif structures/8Q1J/8q1j_complex.pdb structures/8Q1J/8q1j_complex.cif 8Q1Q extended Keap1 mouse Na Na P3-F "[""CHAIN:D""]" 1 Kd Kd = = 12 ± 1 nM 12.0 [] unit_conversion 7.920818753952375 success True direct_binding SPR; geometric mean ± sd. 3 Table 1 reports P3-F SPR Kd = 12 ± 1 nM; the text identifies P3-F as bound to the Keap1 Kelch domain. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q1Q\8Q1Q_metadata.json point structures/8Q1Q/8q1q_protein.pdb structures/8Q1Q/8q1q_pocket.pdb structures/8Q1Q/8q1q_ligand.pdb structures/8Q1Q/8q1q_ligand.cif structures/8Q1Q/8q1q_complex.pdb structures/8Q1Q/8q1q_complex.cif 8Q1R extended Keap1 mouse Na Na P8-F "[""CHAIN:E""]" 1 Kd Kd = = 100 ± 1.0 nM 100.0 [] unit_conversion 7.0 success True direct_binding SPR; geometric mean ± sd. 4 Table 2 reports P8-F SPR Kd = 100 ± 1.0 nM. The Figure 4 caption maps P8-F to PDB 8Q1R. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q1R\8Q1R_metadata.json point structures/8Q1R/8q1r_protein.pdb structures/8Q1R/8q1r_pocket.pdb structures/8Q1R/8q1r_ligand.pdb structures/8Q1R/8q1r_ligand.cif structures/8Q1R/8q1r_complex.pdb structures/8Q1R/8q1r_complex.cif 8Q1S extended 14-3-3 epsilon (YWHAE) human recombinant 14-3-3 epsilon Na GATAD1 phosphopeptide 95-LRNTKYKpSAPAAEKK-109 "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 3.4 ± 0.7 μM 3400.0 [] unit_conversion 5.468521082957745 success True direct_binding Isothermal titration calorimetry of recombinant human 14-3-3 epsilon with the GATAD1 phosphopeptide at 18 °C. 10 Fig. 5A prints “K_D = 3.4 ± 0.7 μM” for LRNTKYKpSAPAAEKK; the Fig. 5 caption identifies this as binding of the GATAD1 phosphopeptide to 14-3-3 epsilon. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q1S\8Q1S_metadata.json point structures/8Q1S/8q1s_protein.pdb structures/8Q1S/8q1s_pocket.pdb structures/8Q1S/8q1s_ligand.pdb structures/8Q1S/8q1s_ligand.cif structures/8Q1S/8q1s_complex.pdb structures/8Q1S/8q1s_complex.cif 8Q23 extended HsNMT1 human HsNMT1 residues 99-496, lacking the N-terminal unfolded domain; expressed from a pET28-derived construct with an N-terminal 10xHis-TEV tag, removed after cleavage Na Ac-D-ORN-SFSKPR (paper: ac[D-Orn]SFSKPR) "[""CHAIN:E"", ""CHAIN:I""]" 1 Kd Kd = = 50 nM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding Binding determination reported for the ac[D-Orn] derivative; the peptide is discussed as a potent inhibitor in the HsNMT1/Myr-CoA study. 7 “D-Orn derivatives were potent inhibitors, especially the ac version (K_D = 50 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8Q23\8Q23_metadata.json point structures/8Q23/8q23_protein.pdb structures/8Q23/8q23_pocket.pdb structures/8Q23/8q23_ligand.pdb structures/8Q23/8q23_ligand.cif structures/8Q23/8q23_complex.pdb structures/8Q23/8q23_complex.cif 8Q2Q classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 2b (YL_32) "[""IT6""]" 1 IC50 IC50 = = 37 µM 37000.0 [] unit_conversion 4.431798275933005 success True biochemical_inhibition HTRF biochemical inhibition assay 2 Figure 1C prints “2b – IC50 = 37 µM”. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q2Q\8Q2Q_metadata.json point structures/8Q2Q/8q2q_protein.pdb structures/8Q2Q/8q2q_pocket.pdb structures/8Q2Q/8q2q_ligand.sdf structures/8Q2Q/8q2q_ligand.pdb structures/8Q2Q/8q2q_ligand.cif structures/8Q2Q/8q2q_complex.pdb structures/8Q2Q/8q2q_complex.cif 8Q2R classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 3 (ZA_431) "[""ITJ""]" 2 Kd Kd = = 146 nM 146.0 [] unit_conversion 6.835647144215563 success True direct_binding Isothermal titration calorimetry (ITC) 3 Text states a submicromolar equilibrium dissociation constant (KD = 146 nM) was measured by ITC for compound 3. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8Q2R\8Q2R_metadata.json point structures/8Q2R/8q2r_protein.pdb structures/8Q2R/8q2r_pocket.pdb structures/8Q2R/8q2r_ligand.sdf structures/8Q2R/8q2r_ligand.pdb structures/8Q2R/8q2r_ligand.cif structures/8Q2R/8q2r_complex.pdb structures/8Q2R/8q2r_complex.cif 8Q2S classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 4 (ZA_232) "[""IU2""]" 1 IC50 IC50 > > 100 µM 100000.0 [] unit_conversion 4.0 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 1 3 Table 1 lists compound 4, PDB 8Q2S, IC50 >100 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q2S\8Q2S_metadata.json point structures/8Q2S/8q2s_protein.pdb structures/8Q2S/8q2s_pocket.pdb structures/8Q2S/8q2s_ligand.sdf structures/8Q2S/8q2s_ligand.pdb structures/8Q2S/8q2s_ligand.cif structures/8Q2S/8q2s_complex.pdb structures/8Q2S/8q2s_complex.cif 8Q2T classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 5 (ZA_236) "[""IUA""]" 1 IC50 IC50 = = 3 µM 3000.0 [] unit_conversion 5.522878745280337 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 1 3 Table 1 lists compound 5, PDB 8Q2T, IC50 3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q2T\8Q2T_metadata.json point structures/8Q2T/8q2t_protein.pdb structures/8Q2T/8q2t_pocket.pdb structures/8Q2T/8q2t_ligand.sdf structures/8Q2T/8q2t_ligand.pdb structures/8Q2T/8q2t_ligand.cif structures/8Q2T/8q2t_complex.pdb structures/8Q2T/8q2t_complex.cif 8Q2U classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 6 (ZA_308) "[""IUH""]" 1 IC50 IC50 = = 6 µM 6000.0 [] unit_conversion 5.221848749616356 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 1 3 Table 1 lists compound 6, PDB 8Q2U, IC50 6 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q2U\8Q2U_metadata.json point structures/8Q2U/8q2u_protein.pdb structures/8Q2U/8q2u_pocket.pdb structures/8Q2U/8q2u_ligand.sdf structures/8Q2U/8q2u_ligand.pdb structures/8Q2U/8q2u_ligand.cif structures/8Q2U/8q2u_complex.pdb structures/8Q2U/8q2u_complex.cif 8Q2V classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 7 (ZA_560) "[""IUQ""]" 1 IC50 IC50 = = 47 µM 47000.0 [] unit_conversion 4.327902142064283 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 1 3 Table 1 lists compound 7, PDB 8Q2V, IC50 47 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q2V\8Q2V_metadata.json point structures/8Q2V/8q2v_protein.pdb structures/8Q2V/8q2v_pocket.pdb structures/8Q2V/8q2v_ligand.sdf structures/8Q2V/8q2v_ligand.pdb structures/8Q2V/8q2v_ligand.cif structures/8Q2V/8q2v_complex.pdb structures/8Q2V/8q2v_complex.cif 8Q2W classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 8 (CS_01) "[""IUZ""]" 1 IC50 IC50 = = 8 µM 8000.0 [] unit_conversion 5.096910013008056 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 1 3 Table 1 lists compound 8, PDB 8Q2W, IC50 8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q2W\8Q2W_metadata.json point structures/8Q2W/8q2w_protein.pdb structures/8Q2W/8q2w_pocket.pdb structures/8Q2W/8q2w_ligand.sdf structures/8Q2W/8q2w_ligand.pdb structures/8Q2W/8q2w_ligand.cif structures/8Q2W/8q2w_complex.pdb structures/8Q2W/8q2w_complex.cif 8Q2X classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 10 (ZA_294) "[""IV6""]" 1 IC50 IC50 = = 11 µM 11000.0 [] unit_conversion 4.958607314841775 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 1 3 Table 1 lists compound 10, PDB 8Q2X, IC50 11 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q2X\8Q2X_metadata.json point structures/8Q2X/8q2x_protein.pdb structures/8Q2X/8q2x_pocket.pdb structures/8Q2X/8q2x_ligand.sdf structures/8Q2X/8q2x_ligand.pdb structures/8Q2X/8q2x_ligand.cif structures/8Q2X/8q2x_complex.pdb structures/8Q2X/8q2x_complex.cif 8Q2Y classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 11 (ZA_572) "[""IVI""]" 1 IC50 IC50 = = 9 µM 9000.0 [] unit_conversion 5.045757490560675 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 1 3 Table 1 lists compound 11, PDB 8Q2Y, IC50 9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q2Y\8Q2Y_metadata.json point structures/8Q2Y/8q2y_protein.pdb structures/8Q2Y/8q2y_pocket.pdb structures/8Q2Y/8q2y_ligand.sdf structures/8Q2Y/8q2y_ligand.pdb structures/8Q2Y/8q2y_ligand.cif structures/8Q2Y/8q2y_complex.pdb structures/8Q2Y/8q2y_complex.cif 8Q31 classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 12 (ZA_341) "[""IVR""]" 1 IC50 IC50 = = 9 µM 9000.0 [] unit_conversion 5.045757490560675 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 2 5 Table 2 lists compound 12, PDB 8Q31, IC50 9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q31\8Q31_metadata.json point structures/8Q31/8q31_protein.pdb structures/8Q31/8q31_pocket.pdb structures/8Q31/8q31_ligand.sdf structures/8Q31/8q31_ligand.pdb structures/8Q31/8q31_ligand.cif structures/8Q31/8q31_complex.pdb structures/8Q31/8q31_complex.cif 8Q32 classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 13 (ZA_364) "[""IW0""]" 1 IC50 IC50 = = 0.46 µM 460.0 [] unit_conversion 6.337242168318426 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 2 5 Table 2 lists compound 13, PDB 8Q32, IC50 0.46 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q32\8Q32_metadata.json point structures/8Q32/8q32_protein.pdb structures/8Q32/8q32_pocket.pdb structures/8Q32/8q32_ligand.sdf structures/8Q32/8q32_ligand.pdb structures/8Q32/8q32_ligand.cif structures/8Q32/8q32_complex.pdb structures/8Q32/8q32_complex.cif 8Q33 classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 15 (ZA_343) "[""IWV""]" 1 IC50 IC50 > > 100 µM 100000.0 [] unit_conversion 4.0 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 2 5 Table 2 lists compound 15, PDB 8Q33, IC50 >100 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q33\8Q33_metadata.json point structures/8Q33/8q33_protein.pdb structures/8Q33/8q33_pocket.pdb structures/8Q33/8q33_ligand.sdf structures/8Q33/8q33_ligand.pdb structures/8Q33/8q33_ligand.cif structures/8Q33/8q33_complex.pdb structures/8Q33/8q33_complex.cif 8Q35 classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 16 (ZA_354) "[""IWM""]" 1 IC50 IC50 = = 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 2 5 Table 2 lists compound 16, PDB 8Q35, IC50 2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q35\8Q35_metadata.json point structures/8Q35/8q35_protein.pdb structures/8Q35/8q35_pocket.pdb structures/8Q35/8q35_ligand.sdf structures/8Q35/8q35_ligand.pdb structures/8Q35/8q35_ligand.cif structures/8Q35/8q35_complex.pdb structures/8Q35/8q35_complex.cif 8Q37 classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 18 (ZA_312) "[""IWF""]" 1 IC50 IC50 = = 13 µM 13000.0 [] unit_conversion 4.886056647693163 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 2 5 Table 2 lists compound 18, PDB 8Q37, IC50 13 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q37\8Q37_metadata.json point structures/8Q37/8q37_protein.pdb structures/8Q37/8q37_pocket.pdb structures/8Q37/8q37_ligand.sdf structures/8Q37/8q37_ligand.pdb structures/8Q37/8q37_ligand.cif structures/8Q37/8q37_complex.pdb structures/8Q37/8q37_complex.cif 8Q38 extended YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 19 (ZA_347) "[""IZJ""]" 1 IC50 IC50 = = 1 µM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 2 5 Table 2 lists compound 19, PDB 8Q38, IC50 1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q38\8Q38_metadata.json point structures/8Q38/8q38_protein.pdb structures/8Q38/8q38_pocket.pdb structures/8Q38/8q38_ligand.pdb structures/8Q38/8q38_ligand.cif structures/8Q38/8q38_complex.pdb structures/8Q38/8q38_complex.cif 8Q39 classic YTHDC1 Na YTHDC1 residues 1285-1424 with an N-terminal hexahistidine tag and TEV cleavage site Na Compound 21 (ZA_515) "[""K1O""]" 1 IC50 IC50 = = 1 µM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition HTRF biochemical inhibition assay, Table 2 5 Table 2 lists compound 21, PDB 8Q39, IC50 1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q39\8Q39_metadata.json point structures/8Q39/8q39_protein.pdb structures/8Q39/8q39_pocket.pdb structures/8Q39/8q39_ligand.sdf structures/8Q39/8q39_ligand.pdb structures/8Q39/8q39_ligand.cif structures/8Q39/8q39_complex.pdb structures/8Q39/8q39_complex.cif 8Q3A classic YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 22 (ZA_393) "[""IYQ""]" 1 IC50 IC50 = = 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition Homogeneous time-resolved fluorescence (HTRF) assay using GST-YTHDC1. 5 Table 2 lists compound 22, IC50 = 2 µM, with PDB code 8Q3A; the table footnote defines IC50 as HTRF. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q3A\8Q3A_metadata.json point structures/8Q3A/8q3a_protein.pdb structures/8Q3A/8q3a_pocket.pdb structures/8Q3A/8q3a_ligand.sdf structures/8Q3A/8q3a_ligand.pdb structures/8Q3A/8q3a_ligand.cif structures/8Q3A/8q3a_complex.pdb structures/8Q3A/8q3a_complex.cif 8Q3G extended YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 23 (ZA_385) "[""J7L""]" 1 IC50 IC50 = = 1 µM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 5 Table 2 lists compound 23, IC50 = 1 µM, with PDB code 8Q3G; the table footnote defines IC50 as HTRF. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q3G\8Q3G_metadata.json point structures/8Q3G/8q3g_protein.pdb structures/8Q3G/8q3g_pocket.pdb structures/8Q3G/8q3g_ligand.pdb structures/8Q3G/8q3g_ligand.cif structures/8Q3G/8q3g_complex.pdb structures/8Q3G/8q3g_complex.cif 8Q4M classic YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 25 (ZA_349) "[""J9B""]" 1 IC50 IC50 = = 0.96 µM 960.0 [] unit_conversion 6.017728766960431 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 5 Table 2 lists compound 25, IC50 = 0.96 µM, with PDB code 8Q4M; the table footnote defines IC50 as HTRF. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q4M\8Q4M_metadata.json point structures/8Q4M/8q4m_protein.pdb structures/8Q4M/8q4m_pocket.pdb structures/8Q4M/8q4m_ligand.sdf structures/8Q4M/8q4m_ligand.pdb structures/8Q4M/8q4m_ligand.cif structures/8Q4M/8q4m_complex.pdb structures/8Q4M/8q4m_complex.cif 8Q4N extended YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 26 (ZA_513) "[""JIR""]" 1 IC50 IC50 = = 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 6 Table 2 (continued) lists compound 26, IC50 = 2 µM, with PDB code 8Q4N. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q4N\8Q4N_metadata.json point structures/8Q4N/8q4n_protein.pdb structures/8Q4N/8q4n_pocket.pdb structures/8Q4N/8q4n_ligand.pdb structures/8Q4N/8q4n_ligand.cif structures/8Q4N/8q4n_complex.pdb structures/8Q4N/8q4n_complex.cif 8Q4P classic YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 27 (ZA_309) "[""JII""]" 1 IC50 IC50 = = 4 µM 4000.0 [] unit_conversion 5.3979400086720375 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 6 Table 2 (continued) lists compound 27, IC50 = 4 µM, with PDB code 8Q4P. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q4P\8Q4P_metadata.json point structures/8Q4P/8q4p_protein.pdb structures/8Q4P/8q4p_pocket.pdb structures/8Q4P/8q4p_ligand.sdf structures/8Q4P/8q4p_ligand.pdb structures/8Q4P/8q4p_ligand.cif structures/8Q4P/8q4p_complex.pdb structures/8Q4P/8q4p_complex.cif 8Q4Q classic YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 29 (ZA_337) "[""JIB""]" 1 IC50 IC50 = = 0.87 µM 870.0 [] unit_conversion 6.060480747381382 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 6 Table 2 (continued) lists compound 29, IC50 = 0.87 µM, with PDB code 8Q4Q. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q4Q\8Q4Q_metadata.json point structures/8Q4Q/8q4q_protein.pdb structures/8Q4Q/8q4q_pocket.pdb structures/8Q4Q/8q4q_ligand.sdf structures/8Q4Q/8q4q_ligand.pdb structures/8Q4Q/8q4q_ligand.cif structures/8Q4Q/8q4q_complex.pdb structures/8Q4Q/8q4q_complex.cif 8Q4R classic YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 30 (ZA_326) "[""JHU""]" 1 IC50 IC50 = = 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 6 Table 2 (continued) lists compound 30, IC50 = 2 µM, with PDB code 8Q4R. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q4R\8Q4R_metadata.json point structures/8Q4R/8q4r_protein.pdb structures/8Q4R/8q4r_pocket.pdb structures/8Q4R/8q4r_ligand.sdf structures/8Q4R/8q4r_ligand.pdb structures/8Q4R/8q4r_ligand.cif structures/8Q4R/8q4r_complex.pdb structures/8Q4R/8q4r_complex.cif 8Q4T classic YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 31 (ZA_400) "[""JBD""]" 1 IC50 IC50 = = 0.45 µM 450.0 [] unit_conversion 6.346787486224656 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 6 Table 2 (continued) lists compound 31, IC50 = 0.45 µM, with PDB code 8Q4T. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q4T\8Q4T_metadata.json point structures/8Q4T/8q4t_protein.pdb structures/8Q4T/8q4t_pocket.pdb structures/8Q4T/8q4t_ligand.sdf structures/8Q4T/8q4t_ligand.pdb structures/8Q4T/8q4t_ligand.cif structures/8Q4T/8q4t_complex.pdb structures/8Q4T/8q4t_complex.cif 8Q4U classic YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 36 (ZA_540b) "[""JA0""]" 1 IC50 IC50 = = 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 8 Table 3 lists compound 36, IC50 = 2 µM, with PDB code 8Q4U. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q4U\8Q4U_metadata.json point structures/8Q4U/8q4u_protein.pdb structures/8Q4U/8q4u_pocket.pdb structures/8Q4U/8q4u_ligand.sdf structures/8Q4U/8q4u_ligand.pdb structures/8Q4U/8q4u_ligand.cif structures/8Q4U/8q4u_complex.pdb structures/8Q4U/8q4u_complex.cif 8Q4V classic YTHDC1 Na YTHDC1 YTH domain, residues 361-559; N-terminal hexahistidine tag and TEV cleavage site Na Compound 37 (ZA_356) "[""JO0""]" 1 IC50 IC50 = = 20 µM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition HTRF assay using GST-YTHDC1. 8 Table 3 lists compound 37, IC50 = 20 µM, with PDB code 8Q4V. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q4V\8Q4V_metadata.json point structures/8Q4V/8q4v_protein.pdb structures/8Q4V/8q4v_pocket.pdb structures/8Q4V/8q4v_ligand.sdf structures/8Q4V/8q4v_ligand.pdb structures/8Q4V/8q4v_ligand.cif structures/8Q4V/8q4v_complex.pdb structures/8Q4V/8q4v_complex.cif 8Q6L extended Carbonic Anhydrase I human Na Na compound 3; 3,4-dihydro-1H-benzo[c][1,2]oxaborinin-1-ol "[""KIX""]" 1 Ki Ki = = 3866 nM 3866.0 [] unit_conversion 5.412738150307465 success True biochemical_inhibition CO2 hydrase stopped-flow inhibition assay; Table 1 reports compound 3 against human hCA I. 3 Table 1 lists compound 3 with Ki = 3866 nM for hCA I; the table title specifies a CO2 hydrase stopped-flow assay against human isoforms. Figure 3 maps hCA I/compound 3 at pH 9 to PDB 8Q6L. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q6L\8Q6L_metadata.json point structures/8Q6L/8q6l_ligand.cif structures/8Q6L/8q6l_complex.cif 8Q71 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na GC-67 "[""KKO""]" 1 IC50 IC50 = = 0.21 ± 0.03 μM 210.0 [] unit_conversion 6.6777807052660805 success True biochemical_inhibition Standard fluorescence resonance energy transfer (FRET) assay measuring SARS-CoV-2 Mpro enzyme inhibition. 4 Table 1 reports GC-67 IC50 = 0.21 ± 0.03 μM; its footnote states that SARS-CoV-2 Mpro inhibitory activity was determined by a standard FRET assay. The adjacent text identifies GC-67 as the most promising Mpro inhibitor. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q71\8Q71_metadata.json point structures/8Q71/8q71_protein.pdb structures/8Q71/8q71_pocket.pdb structures/8Q71/8q71_ligand.sdf structures/8Q71/8q71_ligand.pdb structures/8Q71/8q71_ligand.cif structures/8Q71/8q71_complex.pdb structures/8Q71/8q71_complex.cif 8Q7G extended Carbonic Anhydrase I human Na Na compound 3; 3,4-dihydro-1H-benzo[c][1,2]oxaborinin-1-ol "[""KIX""]" 1 Ki Ki = = 3866 nM 3866.0 [] unit_conversion 5.412738150307465 success True biochemical_inhibition CO2 hydrase stopped-flow inhibition assay; Table 1 reports compound 3 against human hCA I. 3 Table 1 lists compound 3 with Ki = 3866 nM for hCA I; the table title specifies a CO2 hydrase stopped-flow assay against human isoforms. Figure 3 maps hCA I/compound 3 at pH 7 to PDB 8Q7G. auto_single_measurement only accepted activity measurement [1] 1 structures\8Q7G\8Q7G_metadata.json point structures/8Q7G/8q7g_ligand.cif structures/8Q7G/8q7g_complex.cif 8QA4 classic human 5,10-methylenetetrahydrofolate reductase (MTHFR) human full-length MTHFR_FL, residues 1-656 Na SAH "[""SAH""]" 1 Kd Kd range range 0.38–0.39 μM 380.0 390.0 [] range_unit_conversion success True direct_binding Isothermal titration calorimetry of 500 μM SAH injected into 30 μM as-purified full-length MTHFR_FL; reported affinity range for SAH. 6 Page 6 reports that ITC gave stronger affinity for SAH than SAM, with SAH Kd 0.38–0.39 μM; page 11 maps 8QA4 to the symmetric MTHFR + SAH dis-inhibited state. auto_single_measurement only accepted activity measurement [1] 1 structures\8QA4\8QA4_metadata.json interval structures/8QA4/8qa4_protein.pdb structures/8QA4/8qa4_pocket.pdb structures/8QA4/8qa4_ligand.sdf structures/8QA4/8qa4_ligand.pdb structures/8QA4/8qa4_ligand.cif structures/8QA4/8qa4_complex.pdb structures/8QA4/8qa4_complex.cif 8QA5 classic human 5,10-methylenetetrahydrofolate reductase (MTHFR) human full-length MTHFR_FL, residues 1-656 Na SAH "[""SAH""]" 1 Kd Kd range range 0.38–0.39 μM 380.0 390.0 [] range_unit_conversion success True direct_binding Isothermal titration calorimetry of 500 μM SAH injected into 30 μM as-purified full-length MTHFR_FL; reported affinity range for SAH. 6 Page 6 reports an SAH Kd of 0.38–0.39 μM by ITC; page 11 maps 8QA5 to the asymmetric MTHFR + SAH dis-inhibited state. auto_single_measurement only accepted activity measurement [1] 1 structures\8QA5\8QA5_metadata.json interval structures/8QA5/8qa5_protein.pdb structures/8QA5/8qa5_pocket.pdb structures/8QA5/8qa5_ligand.sdf structures/8QA5/8qa5_ligand.pdb structures/8QA5/8qa5_ligand.cif structures/8QA5/8qa5_complex.pdb structures/8QA5/8qa5_complex.cif 8QA6 classic human 5,10-methylenetetrahydrofolate reductase (MTHFR) human full-length MTHFR_FL, residues 1-656 Na SAM "[""SAM""]" 1 Kd Kd range range 0.86–0.99 μM 860.0 990.0 [] range_unit_conversion success True direct_binding Isothermal titration calorimetry of 500 μM SAM injected into 30 μM as-purified full-length MTHFR_FL; reported affinity range for SAM. 6 Page 6 reports a SAM Kd of 0.86–0.99 μM by ITC; page 11 maps 8QA6 to the MTHFR + SAM inhibited state. auto_single_measurement only accepted activity measurement [1] 1 structures\8QA6\8QA6_metadata.json interval structures/8QA6/8qa6_protein.pdb structures/8QA6/8qa6_pocket.pdb structures/8QA6/8qa6_ligand.sdf structures/8QA6/8qa6_ligand.pdb structures/8QA6/8qa6_ligand.cif structures/8QA6/8qa6_complex.pdb structures/8QA6/8qa6_complex.cif 8QB6 classic DispTs2 Terribacillus saccharophilus Mature dispersin polypeptide with a B. clausii secretion signal peptide and a polyhistidine tag Na 6-acetamido-6-deoxy-castanospermine (6-Ac-Cas; PDB ligand code GC2) "[""GC2""]" 1 Kd Kd = = 6 μM 6000.0 [] unit_conversion 5.221848749616356 success True direct_binding Isothermal titration calorimetry measurement of 6-Ac-Cas binding to DispTs2. 11 “6-Ac-Cas has micromolar affinity towards DispTs2 and DispSf, with a Kd of 6 and 15 μM, respectively.” Table 2 maps DispTs2 + 6-Ac-Cas to PDB 8qb6. auto_single_measurement only accepted activity measurement [1] 1 structures\8QB6\8QB6_metadata.json point structures/8QB6/8qb6_protein.pdb structures/8QB6/8qb6_pocket.pdb structures/8QB6/8qb6_ligand.sdf structures/8QB6/8qb6_ligand.pdb structures/8QB6/8qb6_ligand.cif structures/8QB6/8qb6_complex.pdb structures/8QB6/8qb6_complex.cif 8QCC classic IspE Escherichia coli Na Na compound (+/-)-1 "[""UKO""]" 1 IC50 IC50 = = 13.0 ± 2.9 µM 13000.0 [] unit_conversion 4.886056647693163 success True biochemical_inhibition Biochemical evaluation of compound (±)-1 against E. coli IspE; values are averages of duplicate measurements. 5 Figure 4 prints for compound (±)-1: EcIspE IC50 13.0 ± 2.9 µM. The text maps compound 1 to PDB 8QCC. auto_single_measurement only accepted activity measurement [1] 1 structures\8QCC\8QCC_metadata.json point structures/8QCC/8qcc_protein.pdb structures/8QCC/8qcc_pocket.pdb structures/8QCC/8qcc_ligand.sdf structures/8QCC/8qcc_ligand.pdb structures/8QCC/8qcc_ligand.cif structures/8QCC/8qcc_complex.pdb structures/8QCC/8qcc_complex.cif 8QCE classic DispLp Lactiplantibacillus paraplantarum Mature dispersin polypeptide with a B. clausii secretion signal peptide and a polyhistidine tag Na 6-acetamido-6-deoxy-castanospermine (6-Ac-Cas; PDB ligand code GC2) "[""GC2""]" 1 Kd Kd = = 1.12 mM 1120000.0 [] unit_conversion 2.950781977329818 success True direct_binding Isothermal titration calorimetry measurement of 6-Ac-Cas binding to DispLp. 11 “In marked contrast, the Kd of DispLp for 6-Ac-Cas was 1.12 mM.” Table 2 maps DispLp + 6-Ac-Cas to PDB 8qce. auto_single_measurement only accepted activity measurement [1] 1 structures\8QCE\8QCE_metadata.json point structures/8QCE/8qce_protein.pdb structures/8QCE/8qce_pocket.pdb structures/8QCE/8qce_ligand.sdf structures/8QCE/8qce_ligand.pdb structures/8QCE/8qce_ligand.cif structures/8QCE/8qce_complex.pdb structures/8QCE/8qce_complex.cif 8QCN classic IspE Escherichia coli Na Na compound 2 "[""QB9""]" 1 IC50 IC50 = = 36.5 ± 1.6 µM 36500.0 [] unit_conversion 4.437707135543525 success True biochemical_inhibition Biochemical evaluation of compound 2 against E. coli IspE; values are averages of duplicate measurements. 5 Figure 4 prints for compound 2: EcIspE IC50 36.5 ± 1.6 µM. The text maps compound 2 to PDB 8QCN. auto_single_measurement only accepted activity measurement [1] 1 structures\8QCN\8QCN_metadata.json point structures/8QCN/8qcn_protein.pdb structures/8QCN/8qcn_pocket.pdb structures/8QCN/8qcn_ligand.sdf structures/8QCN/8qcn_ligand.pdb structures/8QCN/8qcn_ligand.cif structures/8QCN/8qcn_complex.pdb structures/8QCN/8qcn_complex.cif 8QCO classic IspE Escherichia coli Na Na compound 3 "[""QBI""]" 1 IC50 IC50 = = 10.3 ± 0.7 µM 10300.0 [] unit_conversion 4.987162775294828 success True biochemical_inhibition Biochemical evaluation of compound 3 against E. coli IspE; values are averages of duplicate measurements. 5 Figure 4 prints for compound 3: EcIspE IC50 10.3 ± 0.7 µM. The text and Figure 6 map compound 3 to PDB 8QCO. auto_single_measurement only accepted activity measurement [1] 1 structures\8QCO\8QCO_metadata.json point structures/8QCO/8qco_protein.pdb structures/8QCO/8qco_pocket.pdb structures/8QCO/8qco_ligand.sdf structures/8QCO/8qco_ligand.pdb structures/8QCO/8qco_ligand.cif structures/8QCO/8qco_complex.pdb structures/8QCO/8qco_complex.cif 8QDG extended KMT9 Na Pet-Duet1-His-TEV-KMT9alpha-16-218-KMT9beta Na compound 1a "[""SDU""]" 1 Kd Kd = = 0.006 µM 6.0 [] unit_conversion 8.221848749616356 success True direct_binding Microscale thermophoresis (MST) determination of compound 1a binding to KMT9. 2 “Using Microscale Thermophoresis (MST), we determined a dissociation constant (Kd) of 0.006 µM for KMT9 binding of compound 1a”; Fig. 1b also labels compound 1a Kd = 0.006 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8QDG\8QDG_metadata.json point structures/8QDG/8qdg_protein.pdb structures/8QDG/8qdg_pocket.pdb structures/8QDG/8qdg_ligand.pdb structures/8QDG/8qdg_ligand.cif structures/8QDG/8qdg_complex.pdb structures/8QDG/8qdg_complex.cif 8QDK classic KRAS Na Na G12V fragment 1; N-(furan-2-ylmethyl)-1H-benzimidazol-2-amine "[""WZD""]" 1 Kd Kd = = 1.2 mM 1200000.0 [] unit_conversion 2.920818753952375 success True direct_binding Ligand-titrated [15N,1H]-HSQC chemical-shift-perturbation affinity determination; GMP-PNP-bound KRAS context. 4 Table 1 lists fragment 1 with K_D 1.2 mM and PDB code 8QDK. auto_single_measurement only accepted activity measurement [1] 1 structures\8QDK\8QDK_metadata.json point structures/8QDK/8qdk_protein.pdb structures/8QDK/8qdk_pocket.pdb structures/8QDK/8qdk_ligand.sdf structures/8QDK/8qdk_ligand.pdb structures/8QDK/8qdk_ligand.cif structures/8QDK/8qdk_complex.pdb structures/8QDK/8qdk_complex.cif 8QDN classic KRAS Na Na G12V fragment 2; 7-fluoro-N,N-dimethyl-1-benzofuran-2-carboxamide "[""R60""]" 1 Kd Kd = = 1.6 mM 1600000.0 [] unit_conversion 2.795880017344075 success True direct_binding Ligand-titrated [15N,1H]-HSQC chemical-shift-perturbation affinity determination; GMP-PNP-bound KRAS context. 4 Table 1 lists fragment 2 with K_D 1.6 mM and PDB code 8QDN. auto_single_measurement only accepted activity measurement [1] 1 structures\8QDN\8QDN_metadata.json point structures/8QDN/8qdn_protein.pdb structures/8QDN/8qdn_pocket.pdb structures/8QDN/8qdn_ligand.sdf structures/8QDN/8qdn_ligand.pdb structures/8QDN/8qdn_ligand.cif structures/8QDN/8qdn_complex.pdb structures/8QDN/8qdn_complex.cif 8QDP classic KRAS Na Na G12V fragment 3; N-[2-(5-fluoro-1H-indol-3-yl)ethyl]acetamide "[""HWH""]" 1 Kd Kd = = 1.8 mM 1800000.0 [] unit_conversion 2.7447274948966935 success True direct_binding Ligand-titrated [15N,1H]-HSQC chemical-shift-perturbation affinity determination; GMP-PNP-bound KRAS context. 4 Table 1 lists fragment 3 with K_D 1.8 mM and PDB code 8QDP. auto_single_measurement only accepted activity measurement [1] 1 structures\8QDP\8QDP_metadata.json point structures/8QDP/8qdp_protein.pdb structures/8QDP/8qdp_pocket.pdb structures/8QDP/8qdp_ligand.sdf structures/8QDP/8qdp_ligand.pdb structures/8QDP/8qdp_ligand.cif structures/8QDP/8qdp_complex.pdb structures/8QDP/8qdp_complex.cif 8QDS extended KRAS Na Na G12V fragment 4; N-(4-fluorophenyl)-2-(2-imino-1,3-thiazol-3-yl)acetamide "[""ZV2""]" 1 Kd Kd = = 10 mM 10000000.0 [] unit_conversion 2.0 success True direct_binding Ligand-titrated [15N,1H]-HSQC chemical-shift-perturbation affinity determination; GMP-PNP-bound KRAS context. 4 Table 1 lists fragment 4 with K_D 10 mM and PDB code 8QDS. auto_single_measurement only accepted activity measurement [1] 1 structures\8QDS\8QDS_metadata.json point structures/8QDS/8qds_protein.pdb structures/8QDS/8qds_pocket.pdb structures/8QDS/8qds_ligand.pdb structures/8QDS/8qds_ligand.cif structures/8QDS/8qds_complex.pdb structures/8QDS/8qds_complex.cif 8QDT classic KRAS Na Na G12V fragment 5; 2-fluoro-N-[(3-methyl-1H-pyrazol-4-yl)methyl]aniline "[""UXJ""]" 1 Kd Kd = = 5.2 mM 5200000.0 [] unit_conversion 2.2839966563652006 success True direct_binding Ligand-titrated [15N,1H]-HSQC chemical-shift-perturbation affinity determination; GMP-PNP-bound KRAS context. 4 Table 1 lists fragment 5 with K_D 5.2 mM and PDB code 8QDT. auto_single_measurement only accepted activity measurement [1] 1 structures\8QDT\8QDT_metadata.json point structures/8QDT/8qdt_protein.pdb structures/8QDT/8qdt_pocket.pdb structures/8QDT/8qdt_ligand.sdf structures/8QDT/8qdt_ligand.pdb structures/8QDT/8qdt_ligand.cif structures/8QDT/8qdt_complex.pdb structures/8QDT/8qdt_complex.cif 8QDV extended 14-3-3 zeta Na 14-3-3 zeta delta C, truncated after T234 Na bivalent acetylated Tau-pS214/pS324 peptide "[""CHAIN:C"", ""CHAIN:F""]" 1 Kd Kd = = 945.4 ± 70.2 nM 945.4 [] unit_conversion 6.024384402033105 success True direct_binding Fluorescence anisotropy measurement of pS2 Tau phosphopeptide binding to 14-3-3ζ. 5 Fig. 2e prints: “pS214/pS324 (K_D=945.4±70.2 nM)”. auto_single_measurement only accepted activity measurement [1] 1 structures\8QDV\8QDV_metadata.json point structures/8QDV/8qdv_protein.pdb structures/8QDV/8qdv_pocket.pdb structures/8QDV/8qdv_ligand.pdb structures/8QDV/8qdv_ligand.cif structures/8QDV/8qdv_complex.pdb structures/8QDV/8qdv_complex.cif 8QDW classic KRAS Na Na G12V fragment 9; N-methyl-1-(1-phenylpyrazol-4-yl)methanamine "[""W1Y""]" 1 Kd Kd = = 3.3 mM 3300000.0 [] unit_conversion 2.481486060122113 success True direct_binding Ligand-titrated [15N,1H]-HSQC chemical-shift-perturbation affinity determination; GMP-PNP-bound KRAS context. 4 Table 1 lists fragment 9 with K_D 3.3 mM and PDB code 8QDW. auto_single_measurement only accepted activity measurement [1] 1 structures\8QDW\8QDW_metadata.json point structures/8QDW/8qdw_protein.pdb structures/8QDW/8qdw_pocket.pdb structures/8QDW/8qdw_ligand.sdf structures/8QDW/8qdw_ligand.pdb structures/8QDW/8qdw_ligand.cif structures/8QDW/8qdw_complex.pdb structures/8QDW/8qdw_complex.cif 8QEJ classic KRAS Na Na G12V fragment 17; 5-(1H-indol-2-yl)pyrrolidin-2-one "[""UAO""]" 1 Kd Kd = = 4.6 mM 4600000.0 [] unit_conversion 2.3372421683184257 success True direct_binding Ligand-titrated [15N,1H]-HSQC chemical-shift-perturbation affinity determination; GMP-PNP-bound KRAS context. 4 Table 1 lists fragment 17 with K_D 4.6 mM and PDB code 8QEJ. auto_single_measurement only accepted activity measurement [1] 1 structures\8QEJ\8QEJ_metadata.json point structures/8QEJ/8qej_protein.pdb structures/8QEJ/8qej_pocket.pdb structures/8QEJ/8qej_ligand.sdf structures/8QEJ/8qej_ligand.pdb structures/8QEJ/8qej_ligand.cif structures/8QEJ/8qej_complex.pdb structures/8QEJ/8qej_complex.cif 8QER classic Pseudomonas aeruginosa FabF Pseudomonas aeruginosa FabF C164A C164A 138; 4-(1H-pyrazole-3-carboxamido)pentanoic acid "[""UGL""]" 1 Kd Kd = = 65 ± 3 µM 65000.0 [] unit_conversion 4.187086643357144 success True direct_binding Bio-layer interferometry (BLI); Table 4 reports the KD as an average of three experiments for compound 138. 13 Table 4 lists compound 138 with KD 65 ± 3 µM and PDB ID 8QER; the table states values were determined using PaFabF C164A. auto_single_measurement only accepted activity measurement [1] 1 structures\8QER\8QER_metadata.json point structures/8QER/8qer_protein.pdb structures/8QER/8qer_pocket.pdb structures/8QER/8qer_ligand.sdf structures/8QER/8qer_ligand.pdb structures/8QER/8qer_ligand.cif structures/8QER/8qer_complex.pdb structures/8QER/8qer_complex.cif 8QF7 extended Human Carbonic Anhydrase II human Na Na 25a; (3-((N-(4-sulfamoylbenzyl)phenylsulfonamido)methyl)phenyl)glycine "[""UIE""]" 1 Ki Ki = = 4.5 nM 4.5 [] unit_conversion 8.346787486224656 success True biochemical_inhibition Stopped-flow CO2-hydrase inhibition assay against human carbonic anhydrase II. 5 Table 1 reports Ki = 4.5 nM for compound 25a against hCA II. Figure 2 identifies 25a bound to hCA II as PDB 8QF7. auto_single_measurement only accepted activity measurement [1] 1 structures\8QF7\8QF7_metadata.json point structures/8QF7/8qf7_ligand.sdf structures/8QF7/8qf7_ligand.cif structures/8QF7/8qf7_complex.cif 8QF9 extended Human Carbonic Anhydrase II human Na Na 26a; (3-((N-(4-sulfamoylphenethyl)phenylsulfonamido)methyl)phenyl)glycine "[""UHO""]" 1 Ki Ki = = 9.4 nM 9.4 [] unit_conversion 8.0268721464003 success True biochemical_inhibition Stopped-flow CO2-hydrase inhibition assay against human carbonic anhydrase II. 5 Table 1 reports Ki = 9.4 nM for compound 26a against hCA II. Figure 2 identifies 26a bound to hCA II as PDB 8QF9. auto_single_measurement only accepted activity measurement [1] 1 structures\8QF9\8QF9_metadata.json point structures/8QF9/8qf9_ligand.sdf structures/8QF9/8qf9_ligand.cif structures/8QF9/8qf9_complex.cif 8QFK extended Human Carbonic Anhydrase II human Na Na 25f; (3-((N-(4-sulfamoylbenzyl)methylsulfonamido)methyl)phenyl)glycine "[""UII""]" 1 Ki Ki = = 8.5 nM 8.5 [] unit_conversion 8.070581074285707 success True biochemical_inhibition Stopped-flow CO2-hydrase inhibition assay against human carbonic anhydrase II. 5 Table 1 reports Ki = 8.5 nM for compound 25f against hCA II. Figure 2 identifies 25f bound to hCA II as PDB 8QFK. auto_single_measurement only accepted activity measurement [1] 1 structures\8QFK\8QFK_metadata.json point structures/8QFK/8qfk_ligand.sdf structures/8QFK/8qfk_ligand.cif structures/8QFK/8qfk_complex.cif 8QFX extended Human angiotensin-1-converting enzyme (ACE), N-domain Human Minimally glycosylated and truncated N-domain (N389, nACE) Na IPP (Ile-Pro-Pro) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 IC50 IC50 = = 1.42 ± 0.24 µM 1420.0 [] unit_conversion 5.847711655616944 success True biochemical_inhibition Fixed-time fluorometric ACE-inhibition assay using Z-Phe-His-Leu and recombinantly isolated nACE; IPP used in the trans configuration. 5 Table 2 reports nACE IC50 for IPP as 1.42 ± 0.24 µM; the text states these IC50 values were determined using recombinantly isolated nACE and that IPP was synthesised in the trans configuration. auto_single_measurement only accepted activity measurement [1] 1 structures\8QFX\8QFX_metadata.json point structures/8QFX/8qfx_protein.pdb structures/8QFX/8qfx_pocket.pdb structures/8QFX/8qfx_ligand.pdb structures/8QFX/8qfx_ligand.cif structures/8QFX/8qfx_complex.pdb structures/8QFX/8qfx_complex.cif 8QH8 classic Human Carbonic Anhydrase II Human Na Na Lasamide (LAS; 2,4-dichloro-5-sulfamoylbenzoic acid) "[""V8I""]" 1 Ki Ki = = 0.33 ± 0.02 nM 0.33 [] unit_conversion 9.481486060122112 success True biochemical_inhibition Stopped-flow CO2 hydration assay; mean ± SD of three independent experiments. 2 Table 1 reports LAS Ki for hCA II as 0.33 ± 0.02 nM; the paper maps the LAS–hCA II structure to PDB 8QH8. auto_single_measurement only accepted activity measurement [1] 1 structures\8QH8\8QH8_metadata.json point structures/8QH8/8qh8_protein.pdb structures/8QH8/8qh8_pocket.pdb structures/8QH8/8qh8_ligand.sdf structures/8QH8/8qh8_ligand.pdb structures/8QH8/8qh8_ligand.cif structures/8QH8/8qh8_complex.pdb structures/8QH8/8qh8_complex.cif 8QHG classic Human Carbonic Anhydrase IX mimic Human hCA IX-mimic H-tag protein N67Q; G132D (other active-site changes not individually specified) Lasamide (LAS; 2,4-dichloro-5-sulfamoylbenzoic acid) "[""V8I""]" 1 Ki Ki = = 1.59 ± 0.2 nM 1.59 [] unit_conversion 8.79860287567955 success True biochemical_inhibition Stopped-flow CO2 hydration assay; mean ± SD of three independent experiments. 3 Table 3 reports LAS Ki of 1.59 ± 0.2 nM for hCA IX-mimic H-tag. The paper identifies this LAS complex as PDB 8QHG and describes the IX-mimic mutations. auto_single_measurement only accepted activity measurement [1] 1 structures\8QHG\8QHG_metadata.json point structures/8QHG/8qhg_protein.pdb structures/8QHG/8qhg_pocket.pdb structures/8QHG/8qhg_ligand.sdf structures/8QHG/8qhg_ligand.pdb structures/8QHG/8qhg_ligand.cif structures/8QHG/8qhg_complex.pdb structures/8QHG/8qhg_complex.cif 8QHJ classic Human Carbonic Anhydrase XII mimic Human hCA XII-mimic N67K (other mimic changes not specified) Lasamide (LAS; 2,4-dichloro-5-sulfamoylbenzoic acid) "[""V8I""]" 1 Ki Ki = = 7.54 ± 0.72 nM 7.54 [] unit_conversion 8.122628654130226 success True biochemical_inhibition Stopped-flow CO2 hydration assay; mean ± SD of three independent experiments. 2 Table 1 reports LAS Ki for hCA XII as 7.54 ± 0.72 nM; the paper identifies the LAS-bound hCA XII-mimic as PDB 8QHJ and states the N67K mimic mutation. auto_single_measurement only accepted activity measurement [1] 1 structures\8QHJ\8QHJ_metadata.json point structures/8QHJ/8qhj_protein.pdb structures/8QHJ/8qhj_pocket.pdb structures/8QHJ/8qhj_ligand.sdf structures/8QHJ/8qhj_ligand.pdb structures/8QHJ/8qhj_ligand.cif structures/8QHJ/8qhj_complex.pdb structures/8QHJ/8qhj_complex.cif 8QHL extended Human angiotensin-1-converting enzyme (ACE), N-domain Human Minimally glycosylated and truncated N-domain (N389, nACE) Na VPP (Val-Pro-Pro) "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 2.65 ± 0.09 µM 2650.0 [] unit_conversion 5.576754126063192 success True biochemical_inhibition Fixed-time fluorometric ACE-inhibition assay using Z-Phe-His-Leu and recombinantly isolated nACE; VPP used in the trans configuration. 5 Table 2 reports nACE IC50 for VPP as 2.65 ± 0.09 µM; the text states these IC50 values were determined using recombinantly isolated nACE and that VPP was synthesised in the trans configuration. auto_single_measurement only accepted activity measurement [1] 1 structures\8QHL\8QHL_metadata.json point structures/8QHL/8qhl_protein.pdb structures/8QHL/8qhl_pocket.pdb structures/8QHL/8qhl_ligand.pdb structures/8QHL/8qhl_ligand.cif structures/8QHL/8qhl_complex.pdb structures/8QHL/8qhl_complex.cif 8QHO extended Carbonic Anhydrase II human Na Na compound 3; 3,4-dihydro-1H-benzo[c][1,2]oxaborinin-1-ol "[""KIX""]" 1 Ki Ki = = 1949 nM 1949.0 [] unit_conversion 5.710188160882378 success True biochemical_inhibition CO2 hydrase stopped-flow inhibition assay; Table 1 reports compound 3 against human hCA II. 3 Table 1 lists compound 3 with Ki = 1949 nM for hCA II; the table title specifies a CO2 hydrase stopped-flow assay against human isoforms. Figure 5 maps hCA II/compound 3 at pH 7 to PDB 8QHO. auto_single_measurement only accepted activity measurement [1] 1 structures\8QHO\8QHO_metadata.json point structures/8QHO/8qho_ligand.cif structures/8QHO/8qho_complex.cif 8QIY classic 4'-phosphopantetheine adenylyltransferase (PPAT) Mycobacterium abscessus Na Na compound 9 "[""VCC""]" 1 Kd Kd = = 464 ± 46 µM 464000.0 [] unit_conversion 3.3334820194451193 success True direct_binding Isothermal titration calorimetry (ITC) measurement of compound 9 binding to PPAT. 6 Table 1 reports reporter 9 Kd (ITC) = 464 ± 46 µM; the text and figure mapping identify 9 as the adenine-hotspot PPAT ligand and PDB 8QIY as compound 9. auto_single_measurement only accepted activity measurement [1] 1 structures\8QIY\8QIY_metadata.json point structures/8QIY/8qiy_protein.pdb structures/8QIY/8qiy_pocket.pdb structures/8QIY/8qiy_ligand.sdf structures/8QIY/8qiy_ligand.pdb structures/8QIY/8qiy_ligand.cif structures/8QIY/8qiy_complex.pdb structures/8QIY/8qiy_complex.cif 8QJ8 classic 4'-phosphopantetheine adenylyltransferase (PPAT) Mycobacterium abscessus Na Na compound 11 "[""VIW""]" 1 Kd Kd = = 3.4 ± 0.9 µM 3400.0 [] unit_conversion 5.468521082957745 success True direct_binding ITC measurement of compound 11 binding to PPAT. 8 Table 2, reporter 3 section, lists competitor 11 with Kd (ITC) = 3.4 ± 0.9 µM. auto_metric_priority unique highest-priority metric family: Kd [1] 5 structures\8QJ8\8QJ8_metadata.json point structures/8QJ8/8qj8_protein.pdb structures/8QJ8/8qj8_pocket.pdb structures/8QJ8/8qj8_ligand.sdf structures/8QJ8/8qj8_ligand.pdb structures/8QJ8/8qj8_ligand.cif structures/8QJ8/8qj8_complex.pdb structures/8QJ8/8qj8_complex.cif 8QJT classic BRM (SMARCA2) bromodomain Na Na Na compound 10 "[""VLC""]" 1 IC50 IC50 = = 2.7 nM 2.7 [] unit_conversion 8.568636235841012 success True direct_binding BRM bromodomain protein-fragment binding-affinity assay. 3 Table 1 reports compound 10 BRM IC50 = 2.7 nM; its footnote defines BRM binding affinity as using a bromodomain protein fragment. auto_single_measurement only accepted activity measurement [1] 1 structures\8QJT\8QJT_metadata.json point structures/8QJT/8qjt_protein.pdb structures/8QJT/8qjt_pocket.pdb structures/8QJT/8qjt_ligand.sdf structures/8QJT/8qjt_ligand.pdb structures/8QJT/8qjt_ligand.cif structures/8QJT/8qjt_complex.pdb structures/8QJT/8qjt_complex.cif 8QK9 classic LpxH E. coli Na Na JEDI-1444 "[""VQ9""]" 1 IC50 IC50 = = 2.6 nM 2.6 [] unit_conversion 8.585026652029182 success True biochemical_inhibition E. coli LpxH enzyme inhibition IC50 reported in Table 1. 4 Table 1 reports an E. coli LpxH enzyme-inhibition IC50 of 2.6 nM for JEDI-1444. auto_single_measurement only accepted activity measurement [1] 1 structures\8QK9\8QK9_metadata.json point structures/8QK9/8qk9_protein.pdb structures/8QK9/8qk9_pocket.pdb structures/8QK9/8qk9_ligand.sdf structures/8QK9/8qk9_ligand.pdb structures/8QK9/8qk9_ligand.cif structures/8QK9/8qk9_complex.pdb structures/8QK9/8qk9_complex.cif 8QKW extended Levansucrase beta (Lscβ) Pseudomonas syringae pv actinidiae Na Na TPIS (3), tetravalent pyrrolidine iminosugar "[""VXT""]" 3 Ki Ki = = 29 μM 29000.0 [] unit_conversion 4.5376020021010435 success True biochemical_inhibition Competitive inhibition of recombinant Lscβ sucrose hydrolysis; Ki determined by secondary plot from kinetic analyses. 6 The text states that TPIS (3) behaves as a competitive inhibitor of Lscβ and that a Ki value of 29 μM was calculated; Table 1 also lists Ki 29 μM. auto_metric_priority unique highest-priority metric family: Ki [3] 3 structures\8QKW\8QKW_metadata.json point structures/8QKW/8qkw_protein.pdb structures/8QKW/8qkw_pocket.pdb structures/8QKW/8qkw_ligand.pdb structures/8QKW/8qkw_ligand.cif structures/8QKW/8qkw_complex.pdb structures/8QKW/8qkw_complex.cif 8QKZ extended Carbonic Anhydrase II human Na Na compound 3; 3,4-dihydro-1H-benzo[c][1,2]oxaborinin-1-ol "[""KIX""]" 1 Ki Ki = = 1949 nM 1949.0 [] unit_conversion 5.710188160882378 success True biochemical_inhibition CO2 hydrase stopped-flow inhibition assay; Table 1 reports compound 3 against human hCA II. 3 Table 1 lists compound 3 with Ki = 1949 nM for hCA II; the table title specifies a CO2 hydrase stopped-flow assay against human isoforms. Figure 5 maps hCA II/compound 3 at pH 9 to PDB 8QKZ. auto_single_measurement only accepted activity measurement [1] 1 structures\8QKZ\8QKZ_metadata.json point structures/8QKZ/8qkz_ligand.cif structures/8QKZ/8qkz_complex.cif 8QLG extended AliD substrate-binding protein Streptococcus pneumoniae residues 28-652; lipobox segment removed Na Peptide 1 (FPPQSV) "[""CHAIN:C"", ""CHAIN:E""]" 1 Kd Kd = = 3,44 µM 3440.0 [] unit_conversion 5.46344155742847 success True direct_binding Microscale thermophoresis of fluorescently labelled heterologously expressed AliD with peptide 1 at 25 °C. 6 “The Kd for peptide 2 is 14.4 μM and peptide 1, the natural substrate of AliD, has a Kd of 3,44 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8QLG\8QLG_metadata.json point structures/8QLG/8qlg_protein.pdb structures/8QLG/8qlg_pocket.pdb structures/8QLG/8qlg_ligand.pdb structures/8QLG/8qlg_ligand.cif structures/8QLG/8qlg_complex.pdb structures/8QLG/8qlg_complex.cif 8QM5 classic eIF4E Na CloneID 2983 crystallographic construct with His6 tag, 15 residues derived from 4E-BP1 (GARIIYDRAFLMACR), Gly4 linker, TEV tag, and residues 36-217 of the eIF4E N127 variant Na compound 2 "[""W4U""]" 1 Kd Kd = = 7400 µM 7400000.0 [] unit_conversion 2.1307682802690238 success True direct_binding Direct binding to the crystallographic eIF4E variant. 0 The supplement maps 8QM5 to compound 2 and reports Kd 7400 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8QM5\8QM5_metadata.json point structures/8QM5/8qm5_protein.pdb structures/8QM5/8qm5_pocket.pdb structures/8QM5/8qm5_ligand.sdf structures/8QM5/8qm5_ligand.pdb structures/8QM5/8qm5_ligand.cif structures/8QM5/8qm5_complex.pdb structures/8QM5/8qm5_complex.cif 8QMU classic rabbit skeletal muscle glycogen phosphorylase b (rmGPb) rabbit Na Na (-)-epigallocatechin-3-gallate (EGCG) "[""KDH""]" 1 Ki Ki = = 49.8 ± 1.6 μM 49800.0 [] unit_conversion 4.302770657240282 success True biochemical_inhibition Current-work kinetic analysis of rmGPb inhibition by EGCG. 3 Table 1 reports EGCG Ki = 49.8 ± 1.6 μM for rmGPb. auto_single_measurement only accepted activity measurement [1] 1 structures\8QMU\8QMU_metadata.json point structures/8QMU/8qmu_protein.pdb structures/8QMU/8qmu_pocket.pdb structures/8QMU/8qmu_ligand.sdf structures/8QMU/8qmu_ligand.pdb structures/8QMU/8qmu_ligand.cif structures/8QMU/8qmu_complex.pdb structures/8QMU/8qmu_complex.cif 8QNH classic Cbl-b E3 ubiquitin ligase Na Truncated Cbl-b protein containing the TKB domain, linker helix region, and RING domain Na Ex23 (WO2020264398) "[""Z3N""]" 1 Kd Kd = = 0.003 μM 3.0 [] unit_conversion 8.522878745280337 success True direct_binding Internally synthesized and tested Cbl-b binding measurement. 3 “Ex23 was synthesized and tested internally to give an SPR Kd of 0.003 μM and a TR-FRET IC50 of 0.009 μM for Cbl-b.” auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8QNH\8QNH_metadata.json point structures/8QNH/8qnh_protein.pdb structures/8QNH/8qnh_pocket.pdb structures/8QNH/8qnh_ligand.sdf structures/8QNH/8qnh_ligand.pdb structures/8QNH/8qnh_ligand.cif structures/8QNH/8qnh_complex.pdb structures/8QNH/8qnh_complex.cif 8QNI classic Cbl-b E3 ubiquitin ligase Na Na Na compound 25 "[""W7R""]" 1 IC50 IC50 = = 0.015 μM 15.0 [] unit_conversion 7.823908740944319 success True direct_binding TR-FRET probe-displacement binding assay; average of at least three determinations. 5 Table 4 reports Cbl-b IC50 = 0.015 μM for compound 25; its footnote identifies the assay as TR-FRET probe displacement. auto_single_measurement only accepted activity measurement [1] 1 structures\8QNI\8QNI_metadata.json point structures/8QNI/8qni_protein.pdb structures/8QNI/8qni_pocket.pdb structures/8QNI/8qni_ligand.sdf structures/8QNI/8qni_ligand.pdb structures/8QNI/8qni_ligand.cif structures/8QNI/8qni_complex.pdb structures/8QNI/8qni_complex.cif 8QOB classic phosphoserine phosphatase (SerB) Brucella melitensis BmPSP, His-tag removed before crystallization Na AP3 (2-amino-3-phosphonopropionic acid) "[""WHT""]" 1 IC50 IC50 = = 3.61 mM 3610000.0 [] unit_conversion 2.4424927980943423 success True biochemical_inhibition Malachite green phosphatase assay at near-Km PS concentration (1 mM PS); AP3 inhibition curve, n=3. 10 “IC50 for AP3 was measured at 3.61 mM (Figure 10B)” and the Figure 10 caption gives 3.61 mM (95% confidence interval: 2.47–5.26 mM). auto_single_measurement only accepted activity measurement [1] 1 structures\8QOB\8QOB_metadata.json point structures/8QOB/8qob_protein.pdb structures/8QOB/8qob_pocket.pdb structures/8QOB/8qob_ligand.sdf structures/8QOB/8qob_ligand.pdb structures/8QOB/8qob_ligand.cif structures/8QOB/8qob_complex.pdb structures/8QOB/8qob_complex.cif 8QOW classic leukotriene A4 hydrolase (LTA4H) Na Na Na compound (S)-2 "[""WID""]" 2 IC50 IC50 = = 0.10 ± 0.07 nM 0.1 [] unit_conversion 10.0 success True biochemical_inhibition Biochemical LTA4H assay using a reduced enzyme concentration. 5 The text explicitly states that the accurate IC50 of (S)-2 in the biochemical LTA4H assay, assessed using a reduced enzyme concentration, was 0.10 ± 0.07 nM. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\8QOW\8QOW_metadata.json point structures/8QOW/8qow_protein.pdb structures/8QOW/8qow_pocket.pdb structures/8QOW/8qow_ligand.sdf structures/8QOW/8qow_ligand.pdb structures/8QOW/8qow_ligand.cif structures/8QOW/8qow_complex.pdb structures/8QOW/8qow_complex.cif 8QPN classic leukotriene A4 hydrolase (LTA4H) Na Na Na compound (S)-6 "[""WSL""]" 1 IC50 IC50 < < 3 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition LTA4H enzyme inhibition assay in screening mode using Arg-AMC as substrate (Table 1). 3 Table 1 reports compound (S)-6 LTA4H biochemical IC50 <3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8QPN\8QPN_metadata.json point structures/8QPN/8qpn_protein.pdb structures/8QPN/8qpn_pocket.pdb structures/8QPN/8qpn_ligand.sdf structures/8QPN/8qpn_ligand.pdb structures/8QPN/8qpn_ligand.cif structures/8QPN/8qpn_complex.pdb structures/8QPN/8qpn_complex.cif 8QQ4 classic leukotriene A4 hydrolase (LTA4H) Na Na Na compound (R)-6 "[""WEE""]" 1 IC50 IC50 < < 3 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition LTA4H enzyme inhibition assay in screening mode using Arg-AMC as substrate (Table 1). 3 Table 1 reports compound (R)-6 LTA4H biochemical IC50 <3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8QQ4\8QQ4_metadata.json point structures/8QQ4/8qq4_protein.pdb structures/8QQ4/8qq4_pocket.pdb structures/8QQ4/8qq4_ligand.sdf structures/8QQ4/8qq4_ligand.pdb structures/8QQ4/8qq4_ligand.cif structures/8QQ4/8qq4_complex.pdb structures/8QQ4/8qq4_complex.cif 8QQ9 extended Carbonic Anhydrase I human Na Na compound 11; 1-benzyl-3-(1-hydroxy-3,4-dihydro-1H-benzo[c][1,2]oxaborinin-7-yl)thiourea "[""WHK""]" 1 Ki Ki = = 613.6 nM 613.6 [] unit_conversion 6.2121146490590755 success True biochemical_inhibition CO2 hydrase stopped-flow inhibition assay; Table 1 reports compound 11 against human hCA I. 3 Table 1 lists compound 11 with Ki = 613.6 nM for hCA I; the table title specifies a CO2 hydrase stopped-flow assay against human isoforms. Figure 8 maps hCA I/inhibitor 11 to PDB 8QQ9. auto_single_measurement only accepted activity measurement [1] 1 structures\8QQ9\8QQ9_metadata.json point structures/8QQ9/8qq9_ligand.cif structures/8QQ9/8qq9_complex.cif 8QQA extended human carbonic anhydrase II human Na Na Bithionol "[""B1T""]" 1 Ki Ki = = 31.2 ± 2.0 μM 31200.0 [] unit_conversion 4.505845405981558 success True biochemical_inhibition Stopped-flow CO₂ hydration inhibition assay; Ki reported as mean ± SD of three independent experiments. 3 Table 1 reports Bithionol Ki = 31.2 ± 2.0 μM for hCA II. Figure 2 caption identifies the hCA II–bithionol complex as PDB 8QQA. auto_single_measurement only accepted activity measurement [1] 1 structures\8QQA\8QQA_metadata.json point structures/8QQA/8qqa_ligand.sdf structures/8QQA/8qqa_ligand.cif structures/8QQA/8qqa_complex.cif 8QQE extended DMC1 human Full-length human DMC1 with BRCA2 fragment T2398-H2417 Na BRCA2 PhePP peptide F2s6 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 3.4 ± 1.3 µM 3400.0 [] unit_conversion 5.468521082957745 success True direct_binding ITC, active untagged full-length human DMC1 with BRCA2 F2s6 peptide; 20°C. 7 ITC of active untagged full-length human DMC1 reported Kd = 3.4 ± 1.3 µM for F2s6. auto_single_measurement only accepted activity measurement [1] 1 structures\8QQE\8QQE_metadata.json point structures/8QQE/8qqe_protein.pdb structures/8QQE/8qqe_pocket.pdb structures/8QQE/8qqe_ligand.pdb structures/8QQE/8qqe_ligand.cif structures/8QQE/8qqe_complex.pdb structures/8QQE/8qqe_complex.cif 8QQI classic E. coli DNA gyrase Escherichia coli GyrA and GyrB expressed from pET28-GyrATS and pET28-GyrBTS; modeled residues 8-524 of GyrA and 405-804 of GyrB Na LEI-800 "[""LRL""]" 1 IC50 IC50 = = 35 (23–50) nM 35.0 [] unit_conversion 7.455931955649724 success True biochemical_inhibition DNA gyrase supercoiling-inhibition dose-response assay; n=3 gels; 95% CI printed. 7 Fig. 5c reports LEI-800 IC50 (95% CI) of 35 (23–50) nM for E. coli DNA gyrase supercoiling inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\8QQI\8QQI_metadata.json point structures/8QQI/8qqi_protein.pdb structures/8QQI/8qqi_pocket.pdb structures/8QQI/8qqi_ligand.sdf structures/8QQI/8qqi_ligand.pdb structures/8QQI/8qqi_ligand.cif structures/8QQI/8qqi_complex.pdb structures/8QQI/8qqi_complex.cif 8QRD classic OleP Na Recombinant OleP with an N-terminal hexahistidine tag followed by a thrombin cleavage site, expressed in E. coli BL21(DE3) Na testosterone (TES) "[""TES""]" 1 Kd Kd = = 41.6 ± 7.4 μM 41600.0 [] unit_conversion 4.380906669373258 success True direct_binding Spectrophotometric equilibrium binding by titration of purified OleP with TES at 298 K; apparent dissociation constant from a hyperbolic fit. 4 The paper reports apparent K_D values of 41.6 ± 7.4 μM for TES from equilibrium binding experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\8QRD\8QRD_metadata.json point structures/8QRD/8qrd_protein.pdb structures/8QRD/8qrd_pocket.pdb structures/8QRD/8qrd_ligand.sdf structures/8QRD/8qrd_ligand.pdb structures/8QRD/8qrd_ligand.cif structures/8QRD/8qrd_complex.pdb structures/8QRD/8qrd_complex.cif 8QS3 extended 14-3-3sigma Na Na Na compound 23 (1083848) "[""CHAIN:K"", ""CHAIN:Y""]" 1 Kd Kd = = 1.2 ± 0.0 nM 1.2 [] unit_conversion 8.920818753952375 success True direct_binding SPR of C-RAF 12-mer binding to 14-3-3σ covalently bound to compound 23. 7 Figure 5 reports Kd = 1.2 ± 0.0 nM for the C-RAF 12-mer peptide with 14-3-3σ covalently bound to molecular glue 23. auto_single_measurement only accepted activity measurement [1] 1 structures\8QS3\8QS3_metadata.json point structures/8QS3/8qs3_protein.pdb structures/8QS3/8qs3_pocket.pdb structures/8QS3/8qs3_ligand.pdb structures/8QS3/8qs3_ligand.cif structures/8QS3/8qs3_complex.pdb structures/8QS3/8qs3_complex.cif 8QSE extended 14-3-3sigma Na Na Na compound 23 (1083848) "[""CHAIN:H"", ""CHAIN:S""]" 1 Kd Kd = = 6.3 ± 0.5 nM 6.3 [] unit_conversion 8.200659450546418 success True direct_binding SPR of B-RAF 12-mer binding to 14-3-3σ covalently bound to compound 23. 7 Figure 5 reports Kd = 6.3 ± 0.5 nM for the B-RAF 12-mer peptide with 14-3-3σ covalently bound to molecular glue 23. auto_single_measurement only accepted activity measurement [1] 1 structures\8QSE\8QSE_metadata.json point structures/8QSE/8qse_protein.pdb structures/8QSE/8qse_pocket.pdb structures/8QSE/8qse_ligand.pdb structures/8QSE/8qse_ligand.cif structures/8QSE/8qse_complex.pdb structures/8QSE/8qse_complex.cif 8QTC extended Arabidopsis thaliana 14-3-3 isoform omega Arabidopsis thaliana 14-3-3 omega residues 1-259 Na pBZR1(169-175) "[""CHAIN:C""]" 1 Kd Kd = = 0.88±0.4 μM 880.0 [] unit_conversion 6.055517327849831 success True direct_binding Isothermal titration calorimetry (Fig. 2C) of full-length 14-3-3 omega with the minimal phosphorylated BZR1(169-175) motif. 5 Fig. 2C reports 14-3-3 omega binding pBZR1(169-175) with K_D 0.88±0.4 μM; Table 2 maps 8QTC to 14-3-3 omega(1-259)-pBZR1. auto_single_measurement only accepted activity measurement [1] 1 structures\8QTC\8QTC_metadata.json point structures/8QTC/8qtc_protein.pdb structures/8QTC/8qtc_pocket.pdb structures/8QTC/8qtc_ligand.pdb structures/8QTC/8qtc_ligand.cif structures/8QTC/8qtc_complex.pdb structures/8QTC/8qtc_complex.cif 8QTH classic Cbl-b Na Na Na compound 8 "[""WX0""]" 1 IC50 IC50 = = 190 nM 190.0 [] unit_conversion 6.721246399047171 success True direct_binding TR-FRET competitive ligand binding assay; Table 1. 3 Table 1 lists compound 8 Cbl-b IC50 = 190 nM; text identifies this as the TR-FRET competitive ligand binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8QTH\8QTH_metadata.json point structures/8QTH/8qth_protein.pdb structures/8QTH/8qth_pocket.pdb structures/8QTH/8qth_ligand.sdf structures/8QTH/8qth_ligand.pdb structures/8QTH/8qth_ligand.cif structures/8QTH/8qth_complex.pdb structures/8QTH/8qth_complex.cif 8QU2 extended NF-YB/C heterodimer Na NF-YB/C heterodimer Na 5D^N; 16-mer NF-YA-derived peptide stabilized with C8-hydrocarbon linker "[""CHAIN:A""]" 1 Kd Kd = = 0.8 ± 0.1 µM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Fluorescence-polarization direct binding of N-terminal FITC-labelled peptide to NF-YB/C; Figure 2 reports the mean of triplicates. 4 Figure 2C/D lists peptide 5D^N with K_D = 0.8 ± 0.1 µM; the caption identifies this as direct binding of the indicated stapled peptides to NF-YB/C by FP assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8QU2\8QU2_metadata.json point structures/8QU2/8qu2_protein.pdb structures/8QU2/8qu2_pocket.pdb structures/8QU2/8qu2_ligand.pdb structures/8QU2/8qu2_ligand.cif structures/8QU2/8qu2_complex.pdb structures/8QU2/8qu2_complex.cif 8QU3 extended NF-YB/C heterodimer Na NF-YB/C heterodimer Na 7D^N; 13-mer NF-YA-derived peptide stabilized with C8-hydrocarbon linker "[""CHAIN:A""]" 1 Kd Kd = = 4.1 ± 0.5 µM 4100.0 [] unit_conversion 5.3872161432802645 success True direct_binding Fluorescence-polarization direct binding of N-terminal FITC-labelled peptide to NF-YB/C; Figure 2 reports the mean of triplicates. 4 Figure 2C/D lists peptide 7D^N with K_D = 4.1 ± 0.5 µM; the caption identifies this as direct binding of the indicated stapled peptides to NF-YB/C by FP assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8QU3\8QU3_metadata.json point structures/8QU3/8qu3_protein.pdb structures/8QU3/8qu3_pocket.pdb structures/8QU3/8qu3_ligand.pdb structures/8QU3/8qu3_ligand.cif structures/8QU3/8qu3_complex.pdb structures/8QU3/8qu3_complex.cif 8QU4 extended NF-YB/C heterodimer Na NF-YB/C heterodimer Na 7D^N; 13-mer NF-YA-derived peptide stabilized with C8-hydrocarbon linker "[""CHAIN:A""]" 1 Kd Kd = = 4.1 ± 0.5 µM 4100.0 [] unit_conversion 5.3872161432802645 success True direct_binding Fluorescence-polarization direct binding of N-terminal FITC-labelled peptide to NF-YB/C; Figure 2 reports the mean of triplicates. 4 Figure 2C/D lists peptide 7D^N with K_D = 4.1 ± 0.5 µM; the caption identifies this as direct binding of the indicated stapled peptides to NF-YB/C by FP assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8QU4\8QU4_metadata.json point structures/8QU4/8qu4_protein.pdb structures/8QU4/8qu4_pocket.pdb structures/8QU4/8qu4_ligand.pdb structures/8QU4/8qu4_ligand.cif structures/8QU4/8qu4_complex.pdb structures/8QU4/8qu4_complex.cif 8QUB classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 9 "[""WVZ""]" 1 pKi Ki = = 3.7 199526.2314968879 [] p_metric_transform 3.7 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QUB to compound 9 and reports pKi 3.7. auto_single_measurement only accepted activity measurement [1] 1 structures\8QUB\8QUB_metadata.json point structures/8QUB/8qub_protein.pdb structures/8QUB/8qub_pocket.pdb structures/8QUB/8qub_ligand.sdf structures/8QUB/8qub_ligand.pdb structures/8QUB/8qub_ligand.cif structures/8QUB/8qub_complex.pdb structures/8QUB/8qub_complex.cif 8QUH classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 10 "[""AJ2""]" 1 pKi Ki = = 3.3 501187.2336272725 [] p_metric_transform 3.3 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QUH to compound 10 and reports pKi 3.3. auto_single_measurement only accepted activity measurement [1] 1 structures\8QUH\8QUH_metadata.json point structures/8QUH/8quh_protein.pdb structures/8QUH/8quh_pocket.pdb structures/8QUH/8quh_ligand.sdf structures/8QUH/8quh_ligand.pdb structures/8QUH/8quh_ligand.cif structures/8QUH/8quh_complex.pdb structures/8QUH/8quh_complex.cif 8QUJ classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 12 "[""WWR""]" 1 pKi Ki = = 3.5 316227.7660168379 [] p_metric_transform 3.5 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QUJ to compound 12 and reports pKi 3.5. auto_single_measurement only accepted activity measurement [1] 1 structures\8QUJ\8QUJ_metadata.json point structures/8QUJ/8quj_protein.pdb structures/8QUJ/8quj_pocket.pdb structures/8QUJ/8quj_ligand.sdf structures/8QUJ/8quj_ligand.pdb structures/8QUJ/8quj_ligand.cif structures/8QUJ/8quj_complex.pdb structures/8QUJ/8quj_complex.cif 8QUK classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 13 "[""WVU""]" 1 pKi Ki = = 3.4 398107.1705534969 [] p_metric_transform 3.4000000000000004 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QUK to compound 13 and reports pKi 3.4. auto_single_measurement only accepted activity measurement [1] 1 structures\8QUK\8QUK_metadata.json point structures/8QUK/8quk_protein.pdb structures/8QUK/8quk_pocket.pdb structures/8QUK/8quk_ligand.sdf structures/8QUK/8quk_ligand.pdb structures/8QUK/8quk_ligand.cif structures/8QUK/8quk_complex.pdb structures/8QUK/8quk_complex.cif 8QUL classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 14 "[""3IP""]" 1 pKi Ki = = 3.4 398107.1705534969 [] p_metric_transform 3.4000000000000004 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QUL to compound 14 and reports pKi 3.4. auto_single_measurement only accepted activity measurement [1] 1 structures\8QUL\8QUL_metadata.json point structures/8QUL/8qul_protein.pdb structures/8QUL/8qul_pocket.pdb structures/8QUL/8qul_ligand.sdf structures/8QUL/8qul_ligand.pdb structures/8QUL/8qul_ligand.cif structures/8QUL/8qul_complex.pdb structures/8QUL/8qul_complex.cif 8QUW classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 27 "[""WZR""]" 1 pKi Ki = = 4.7 19952.62314968879 [] p_metric_transform 4.7 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QUW to compound 27 and reports pKi 4.7. auto_single_measurement only accepted activity measurement [1] 1 structures\8QUW\8QUW_metadata.json point structures/8QUW/8quw_protein.pdb structures/8QUW/8quw_pocket.pdb structures/8QUW/8quw_ligand.sdf structures/8QUW/8quw_ligand.pdb structures/8QUW/8quw_ligand.cif structures/8QUW/8quw_complex.pdb structures/8QUW/8quw_complex.cif 8QUX classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 28 "[""S0I""]" 1 pKi Ki = = 4.6 25118.864315095823 [] p_metric_transform 4.6 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QUX to compound 28 and reports pKi 4.6. auto_single_measurement only accepted activity measurement [1] 1 structures\8QUX\8QUX_metadata.json point structures/8QUX/8qux_protein.pdb structures/8QUX/8qux_pocket.pdb structures/8QUX/8qux_ligand.sdf structures/8QUX/8qux_ligand.pdb structures/8QUX/8qux_ligand.cif structures/8QUX/8qux_complex.pdb structures/8QUX/8qux_complex.cif 8QUY classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 29 "[""X0L""]" 1 pKi Ki = = 4.6 25118.864315095823 [] p_metric_transform 4.6 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QUY to compound 29 and reports pKi 4.6. auto_single_measurement only accepted activity measurement [1] 1 structures\8QUY\8QUY_metadata.json point structures/8QUY/8quy_protein.pdb structures/8QUY/8quy_pocket.pdb structures/8QUY/8quy_ligand.sdf structures/8QUY/8quy_ligand.pdb structures/8QUY/8quy_ligand.cif structures/8QUY/8quy_complex.pdb structures/8QUY/8quy_complex.cif 8QV1 classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 30 "[""X0H""]" 1 pKi Ki = = 4.7 19952.62314968879 [] p_metric_transform 4.7 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QV1 to compound 30 and reports pKi 4.7. auto_single_measurement only accepted activity measurement [1] 1 structures\8QV1\8QV1_metadata.json point structures/8QV1/8qv1_protein.pdb structures/8QV1/8qv1_pocket.pdb structures/8QV1/8qv1_ligand.sdf structures/8QV1/8qv1_ligand.pdb structures/8QV1/8qv1_ligand.cif structures/8QV1/8qv1_complex.pdb structures/8QV1/8qv1_complex.cif 8QV4 classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 31 "[""WZX""]" 1 pKi Ki = = 5.0 10000.0 [] p_metric_transform 5.0 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QV4 to compound 31 and reports pKi 5.0. auto_single_measurement only accepted activity measurement [1] 1 structures\8QV4\8QV4_metadata.json point structures/8QV4/8qv4_protein.pdb structures/8QV4/8qv4_pocket.pdb structures/8QV4/8qv4_ligand.sdf structures/8QV4/8qv4_ligand.pdb structures/8QV4/8qv4_ligand.cif structures/8QV4/8qv4_complex.pdb structures/8QV4/8qv4_complex.cif 8QV9 classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 33 "[""WZL""]" 1 pKi Ki = = 5.3 5011.872336272725 [] p_metric_transform 5.3 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QV9 to compound 33 and reports pKi 5.3. auto_single_measurement only accepted activity measurement [1] 1 structures\8QV9\8QV9_metadata.json point structures/8QV9/8qv9_protein.pdb structures/8QV9/8qv9_pocket.pdb structures/8QV9/8qv9_ligand.sdf structures/8QV9/8qv9_ligand.pdb structures/8QV9/8qv9_ligand.cif structures/8QV9/8qv9_complex.pdb structures/8QV9/8qv9_complex.cif 8QVA classic HIV-1 capsid protein (CA) HIV-1 Hexameric HIV-1 CA A14C; E45C; W184A; M185A compound 37 "[""WZ9""]" 1 pKi Ki = = 5.3 5011.872336272725 [] p_metric_transform 5.3 success True biochemical_inhibition Biochemical inhibition assay. 0 The supplement maps 8QVA to compound 37 and reports pKi 5.3. auto_single_measurement only accepted activity measurement [1] 1 structures\8QVA\8QVA_metadata.json point structures/8QVA/8qva_protein.pdb structures/8QVA/8qva_pocket.pdb structures/8QVA/8qva_ligand.sdf structures/8QVA/8qva_ligand.pdb structures/8QVA/8qva_ligand.cif structures/8QVA/8qva_complex.pdb structures/8QVA/8qva_complex.cif 8QXW extended mouse importin alpha 2 (mIMPalpha2) mouse mIMPalpha2DeltaIBB; complexed with UL44 residues 410-433 Na UL44_410-433 "[""CHAIN:B""]" 1 Kd Kd = = 0.75 ± 0.04 µM 750.0 [] unit_conversion 6.1249387366083 success True direct_binding FITC-labelled UL44_410-433 peptide fluorescence-polarization binding assay with recombinant mIMPα2ΔIBB. 6 Fig. 3B reports Kd = 0.75 ± 0.04 µM for UL44_410-433 binding mIMPα2; the figure legend identifies purified recombinant IMPαΔIBBs and FITC-labelled peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\8QXW\8QXW_metadata.json point structures/8QXW/8qxw_protein.pdb structures/8QXW/8qxw_pocket.pdb structures/8QXW/8qxw_ligand.pdb structures/8QXW/8qxw_ligand.cif structures/8QXW/8qxw_complex.pdb structures/8QXW/8qxw_complex.cif 8QXX extended mouse importin alpha 2 (mIMPalpha2) mouse mIMPalpha2DeltaIBB; complexed with phosphorylated UL44 residues 410-433 Na UL44_410-433_pT (T427-phosphorylated) "[""CHAIN:B""]" 1 Kd Kd = = 10.71 ± 1.05 µM 10710.0 [] unit_conversion 4.970210529168145 success True direct_binding FITC-labelled T427-phosphorylated UL44_410-433 peptide fluorescence-polarization binding assay with recombinant mIMPα2ΔIBB. 6 Fig. 3B reports Kd = 10.71 ± 1.05 µM for UL44_410-433_pT binding mIMPα2; the figure legend identifies purified recombinant IMPαΔIBBs and FITC-labelled peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\8QXX\8QXX_metadata.json point structures/8QXX/8qxx_protein.pdb structures/8QXX/8qxx_pocket.pdb structures/8QXX/8qxx_ligand.pdb structures/8QXX/8qxx_ligand.cif structures/8QXX/8qxx_complex.pdb structures/8QXX/8qxx_complex.cif 8QYI classic OleP Na Recombinant OleP with an N-terminal hexahistidine tag followed by a thrombin cleavage site, expressed in E. coli BL21(DE3) Na lithocholic acid (LCA) "[""4OA""]" 1 Kd Kd = = 16.3 ± 0.5 μM 16300.0 [] unit_conversion 4.787812395596042 success True direct_binding Spectrophotometric equilibrium binding by titration of purified OleP with LCA at 298 K; apparent dissociation constant from a hyperbolic fit. 4 The paper reports apparent K_D values of 16.3 ± 0.5 μM for LCA from equilibrium binding experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\8QYI\8QYI_metadata.json point structures/8QYI/8qyi_protein.pdb structures/8QYI/8qyi_pocket.pdb structures/8QYI/8qyi_ligand.sdf structures/8QYI/8qyi_ligand.pdb structures/8QYI/8qyi_ligand.cif structures/8QYI/8qyi_complex.pdb structures/8QYI/8qyi_complex.cif 8QZD classic human soluble epoxide hydrolase (sEH), sEH-H Homo sapiens C-terminal hydrolase domain; residues 228-547 in the Figure 3 caption, while the co-crystallization methods state residues 222-555 Na Epoxykinin (compound 11) "[""XDZ""]" 1 IC50 IC50 = = 6.7 ± 3.2 nM 6.7 [] unit_conversion 8.173925197299173 success True biochemical_inhibition Inhibition of hydrolase activity of purified sEH (sEH-H). 6 “Epoxykinin inhibited the hydrolase activity of purified sEH (sEH-H) very potently with an IC50 value of 6.7 ± 3.2 nM (Figure 3B).” auto_single_measurement only accepted activity measurement [1] 1 structures\8QZD\8QZD_metadata.json point structures/8QZD/8qzd_protein.pdb structures/8QZD/8qzd_pocket.pdb structures/8QZD/8qzd_ligand.sdf structures/8QZD/8qzd_ligand.pdb structures/8QZD/8qzd_ligand.cif structures/8QZD/8qzd_complex.pdb structures/8QZD/8qzd_complex.cif 8R0I classic FabF (beta-ketoacyl-ACP synthase 2) Pseudomonas aeruginosa Na C164A compound 2 (3-amino-N-(1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro-1H-pyrazol-4-yl)benzamide) "[""XG7""]" 1 Kd Kd = = 19 ± 3 µM 19000.0 [] unit_conversion 4.721246399047171 success True direct_binding BLI steady-state binding; average of three experiments using repurchased material. 9 Table 3 reports PaFabF C164A K_D for compound 2 as 19 ± 3 µM; Fig. 7 maps compound 2 to PDB 8R0I. auto_single_measurement only accepted activity measurement [1] 1 structures\8R0I\8R0I_metadata.json point structures/8R0I/8r0i_protein.pdb structures/8R0I/8r0i_pocket.pdb structures/8R0I/8r0i_ligand.sdf structures/8R0I/8r0i_ligand.pdb structures/8R0I/8r0i_ligand.cif structures/8R0I/8r0i_complex.pdb structures/8R0I/8r0i_complex.cif 8R11 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 7 "[""XI0""]" 1 IC50 IC50 = = 2.1 µM 2100.0 [] unit_conversion 5.6777807052660805 success True biochemical_inhibition Mpro FRET assay with DTT. 7 Fig. 5 identifies compound 7 with “Mpro_FRET_DTT_IC50: 2.1 µM”; the text identifies its crystal structure as PDB 8r11. auto_single_measurement only accepted activity measurement [1] 1 structures\8R11\8R11_metadata.json point structures/8R11/8r11_protein.pdb structures/8R11/8r11_pocket.pdb structures/8R11/8r11_ligand.sdf structures/8R11/8r11_ligand.pdb structures/8R11/8r11_ligand.cif structures/8R11/8r11_complex.pdb structures/8R11/8r11_complex.cif 8R12 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 8 "[""XH9""]" 1 IC50 IC50 = = 24.2 µM 24200.0 [] unit_conversion 4.616184634019569 success True biochemical_inhibition Mpro FRET assay with DTT. 7 Fig. 5 identifies compound 8 with “Mpro_FRET_DTT_IC50: 24.2 µM”; the text identifies its crystal structure as PDB 8r12. auto_single_measurement only accepted activity measurement [1] 1 structures\8R12\8R12_metadata.json point structures/8R12/8r12_protein.pdb structures/8R12/8r12_pocket.pdb structures/8R12/8r12_ligand.sdf structures/8R12/8r12_ligand.pdb structures/8R12/8r12_ligand.cif structures/8R12/8r12_complex.pdb structures/8R12/8r12_complex.cif 8R14 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 11 "[""XHW""]" 1 IC50 IC50 = = 1.3 µM 1300.0 [] unit_conversion 5.886056647693163 success True biochemical_inhibition Mpro FRET assay with DTT. 8 The text states compound 11 has an Mpro FRET IC50 of 1.3 µM; Fig. 9 identifies its crystal structure as PDB 8r14. auto_single_measurement only accepted activity measurement [1] 1 structures\8R14\8R14_metadata.json point structures/8R14/8r14_protein.pdb structures/8R14/8r14_pocket.pdb structures/8R14/8r14_ligand.sdf structures/8R14/8r14_ligand.pdb structures/8R14/8r14_ligand.cif structures/8R14/8r14_complex.pdb structures/8R14/8r14_complex.cif 8R16 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 12 "[""XJ9""]" 1 IC50 IC50 = = 2.3 µM 2300.0 [] unit_conversion 5.638272163982407 success True biochemical_inhibition Mpro FRET assay with DTT. 8 The text states the tetrahydroisoquinoline series (compound 12) reached 2.3 µM; Fig. 10 identifies its crystal structure as PDB 8r16. auto_single_measurement only accepted activity measurement [1] 1 structures\8R16\8R16_metadata.json point structures/8R16/8r16_protein.pdb structures/8R16/8r16_pocket.pdb structures/8R16/8r16_ligand.sdf structures/8R16/8r16_ligand.pdb structures/8R16/8r16_ligand.cif structures/8R16/8r16_complex.pdb structures/8R16/8r16_complex.cif 8R1V classic FabF (beta-ketoacyl-ACP synthase 2) Pseudomonas aeruginosa Na C164A compound 3 (N-(1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro-1H-pyrazol-4-yl)-2-(4-methoxyphenoxy)acetamide) "[""XJR""]" 1 Kd Kd = = 23 ± 2 µM 23000.0 [] unit_conversion 4.638272163982407 success True direct_binding BLI steady-state binding; average of three experiments using repurchased material. 9 Table 3 reports PaFabF C164A K_D for compound 3 as 23 ± 2 µM; Fig. 7 maps compound 3 to PDB 8R1V. auto_single_measurement only accepted activity measurement [1] 1 structures\8R1V\8R1V_metadata.json point structures/8R1V/8r1v_protein.pdb structures/8R1V/8r1v_pocket.pdb structures/8R1V/8r1v_ligand.sdf structures/8R1V/8r1v_ligand.pdb structures/8R1V/8r1v_ligand.cif structures/8R1V/8r1v_complex.pdb structures/8R1V/8r1v_complex.cif 8R2G extended DMC1 Homo sapiens DMC1 ΔN, amino acids 83-340; BRCA2 Ex14-Tr peptide, amino acids 2401-2414 Na BRCA2 Ex14-Tr peptide "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L"", ""CHAIN:M"", ""CHAIN:N"", ""CHAIN:O""]" 1 Kd Kd = = 35.67 μM 35670.0 [] unit_conversion 4.447696890661646 success True direct_binding Microscale thermophoresis (MST); Ex14-Tr was the truncated peptide used for crystallographic studies. 3 Figure 2a reports Kd 35.67 μM for DMC1 ΔN binding BRCA2 Ex14-Tr; the text states this affinity was retained for the truncated Ex14-Tr peptide used in crystallographic studies. auto_single_measurement only accepted activity measurement [1] 1 structures\8R2G\8R2G_metadata.json point structures/8R2G/8r2g_protein.pdb structures/8R2G/8r2g_pocket.pdb structures/8R2G/8r2g_ligand.pdb structures/8R2G/8r2g_ligand.cif structures/8R2G/8r2g_complex.pdb structures/8R2G/8r2g_complex.cif 8R34 classic ScPho90 Saccharomyces cerevisiae ScPho90 with a thrombin-cleavable C-terminal His10 tag Na phosphate "[""PO4""]" 1 Kd Kd = = 1.9 ± 0.4 mM 1900000.0 [] unit_conversion 2.721246399047171 success True direct_binding Microscale thermophoresis measurement of phosphate binding affinity of purified ScPho90; samples contained 100 mM NaCl. 7 “Phosphate binding affinity of purified ScPho90 (C) was determined by microscale thermophoresis resulting in a Kd value of 1.9 ± 0.4 mM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8R34\8R34_metadata.json point structures/8R34/8r34_protein.pdb structures/8R34/8r34_pocket.pdb structures/8R34/8r34_ligand.sdf structures/8R34/8r34_ligand.pdb structures/8R34/8r34_ligand.cif structures/8R34/8r34_complex.pdb structures/8R34/8r34_complex.cif 8R3B classic Pent Na 5c2n-N33K designed 5-bladed beta-propeller; 47-residue monomer excluding Met1 Asn33Lys (N33K) sulfonato-calix[8]arene (sclx8) "[""EVB""]" 1 Kd Kd < < 3 µM 3000.0 [] unit_conversion 5.522878745280337 success True direct_binding Titration of 15N-Lys-labeled Pent with sclx8 by NMR; slow exchange on the NMR time scale. 5 “Titration of the sample with sclx8 yielded clear-cut evidence of a slow-exchange process on the NMR time scale… These data suggest that the dissociation constant is Kd < 3 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8R3B\8R3B_metadata.json point structures/8R3B/8r3b_protein.pdb structures/8R3B/8r3b_pocket.pdb structures/8R3B/8r3b_ligand.sdf structures/8R3B/8r3b_ligand.pdb structures/8R3B/8r3b_ligand.cif structures/8R3B/8r3b_complex.pdb structures/8R3B/8r3b_complex.cif 8R3C classic Pent Na 5c2n-N33K designed 5-bladed beta-propeller; 47-residue monomer excluding Met1 Asn33Lys (N33K) sulfonato-calix[8]arene (sclx8) "[""EVB""]" 1 Kd Kd < < 3 µM 3000.0 [] unit_conversion 5.522878745280337 success True direct_binding Titration of 15N-Lys-labeled Pent with sclx8 by NMR; slow exchange on the NMR time scale. 5 “Titration of the sample with sclx8 yielded clear-cut evidence of a slow-exchange process on the NMR time scale… These data suggest that the dissociation constant is Kd < 3 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8R3C\8R3C_metadata.json point structures/8R3C/8r3c_protein.pdb structures/8R3C/8r3c_pocket.pdb structures/8R3C/8r3c_ligand.sdf structures/8R3C/8r3c_ligand.pdb structures/8R3C/8r3c_ligand.cif structures/8R3C/8r3c_complex.pdb structures/8R3C/8r3c_complex.cif 8R41 classic CHI3L1 (chitinase-3-like protein 1) human residues 1-383, untagged Na compound 1 "[""XUF""]" 1 Kd Kd = = 35 μM 35000.0 [] unit_conversion 4.455931955649724 success True direct_binding MST direct-binding measurement. 3 Figure 2 prints for compound 1: “CHI3L1 K_D 35 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\8R41\8R41_metadata.json point structures/8R41/8r41_protein.pdb structures/8R41/8r41_pocket.pdb structures/8R41/8r41_ligand.sdf structures/8R41/8r41_ligand.pdb structures/8R41/8r41_ligand.cif structures/8R41/8r41_complex.pdb structures/8R41/8r41_complex.cif 8R42 classic CHI3L1 (chitinase-3-like protein 1) human residues 1-383, untagged Na compound 2 "[""XUC""]" 1 Kd Kd = = 18 μM 18000.0 [] unit_conversion 4.7447274948966935 success True direct_binding MST direct-binding measurement. 3 Figure 2 prints for compound 2: “CHI3L1 K_D 18 μM”. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8R42\8R42_metadata.json point structures/8R42/8r42_protein.pdb structures/8R42/8r42_pocket.pdb structures/8R42/8r42_ligand.sdf structures/8R42/8r42_ligand.pdb structures/8R42/8r42_ligand.cif structures/8R42/8r42_complex.pdb structures/8R42/8r42_complex.cif 8R49 extended plastidial phosphorylase Pho1 (stPho1) Solanum tuberosum stPho1DeltaL78, lacking residues 447-510 Na beta-cyclodextrin (beta-CD) "[""BRANCHED_ENTITY:2""]" 1 Ki Ki = = 31.1 ± 1.0 µM 31100.0 [] unit_conversion 4.507239610973162 success True biochemical_inhibition Kinetic inhibition measurement reported in Table 2; values were measured in the presence of 1 mM AMP. 4 Table 2 reports Ki for β-cyclodextrin of 31.1 ± 1.0 µM for stPho1ΔL78; its footnote states that values were measured in the presence of 1 mM AMP. Table 1 maps the β-CD complex to PDB 8R49. auto_single_measurement only accepted activity measurement [1] 1 structures\8R49\8R49_metadata.json point structures/8R49/8r49_protein.pdb structures/8R49/8r49_pocket.pdb structures/8R49/8r49_ligand.pdb structures/8R49/8r49_ligand.cif structures/8R49/8r49_complex.pdb structures/8R49/8r49_complex.cif 8R4G classic plastidial phosphorylase Pho1 (stPho1) Solanum tuberosum stPho1DeltaL78, lacking residues 447-510 Na alpha-D-glucose (alpha-D-Glc) "[""GLC""]" 1 Ki Ki = = 38.4 ± 1.5 mM 38400000.0 [] unit_conversion 1.4156687756324695 success True biochemical_inhibition Kinetic inhibition measurement reported in Table 2; values were measured in the presence of 1 mM AMP. 4 Table 2 reports Ki for α-D-glucose of 38.4 ± 1.5 mM for stPho1ΔL78; its footnote states that values were measured in the presence of 1 mM AMP. Table 1 maps the α-D-Glc complex to PDB 8R4G. auto_single_measurement only accepted activity measurement [1] 1 structures\8R4G\8R4G_metadata.json point structures/8R4G/8r4g_protein.pdb structures/8R4G/8r4g_pocket.pdb structures/8R4G/8r4g_ligand.sdf structures/8R4G/8r4g_ligand.pdb structures/8R4G/8r4g_ligand.cif structures/8R4G/8r4g_complex.pdb structures/8R4G/8r4g_complex.cif 8R4J classic plastidial phosphorylase Pho1 (stPho1) Solanum tuberosum stPho1DeltaL78, lacking residues 447-510 Na caffeine "[""CFF""]" 1 Ki Ki = = 1.4 ± 0.1 mM 1400000.0 [] unit_conversion 2.853871964321762 success True biochemical_inhibition Kinetic inhibition measurement reported in Table 2; values were measured in the presence of 1 mM AMP. 4 Table 2 reports Ki for caffeine of 1.4 ± 0.1 mM for stPho1ΔL78; its footnote states that values were measured in the presence of 1 mM AMP. Table 1 maps the caffeine complex to PDB 8R4J. auto_single_measurement only accepted activity measurement [1] 1 structures\8R4J\8R4J_metadata.json point structures/8R4J/8r4j_protein.pdb structures/8R4J/8r4j_pocket.pdb structures/8R4J/8r4j_ligand.sdf structures/8R4J/8r4j_ligand.pdb structures/8R4J/8r4j_ligand.cif structures/8R4J/8r4j_complex.pdb structures/8R4J/8r4j_complex.cif 8R52 classic rabbit skeletal muscle glycogen phosphorylase b (rmGPb) rabbit Na Na epigallocatechin (EGC) "[""EGT""]" 1 Ki Ki = = 285.5 ± 14.1 μM 285500.0 [] unit_conversion 3.544393887418133 success True biochemical_inhibition Current-work kinetic analysis of rmGPb inhibition by EGC. 3 Table 1 reports EGC Ki = 285.5 ± 14.1 μM for rmGPb. auto_single_measurement only accepted activity measurement [1] 1 structures\8R52\8R52_metadata.json point structures/8R52/8r52_protein.pdb structures/8R52/8r52_pocket.pdb structures/8R52/8r52_ligand.sdf structures/8R52/8r52_ligand.pdb structures/8R52/8r52_ligand.cif structures/8R52/8r52_complex.pdb structures/8R52/8r52_complex.cif 8R5C classic human TRIM7 human TRIM7 PRYSPRY domain, residues 338-511, expressed as an N-terminal His6-GST fusion with the tag cleaved Na compound 39; (2-(1-oxoisoindolin-2-yl)-3-phenylpropanoyl)-L-glutamine "[""Y3C""]" 1 Kd Kd = = 26.3 ± 0.1 µM 26300.0 [] unit_conversion 4.580044251510242 success True direct_binding Surface plasmon resonance dose-response analysis; pure stereoisomer 88; n = 3. 3 Figure 3 reports “(88) KD = 26.3 ± 0.1 µM” from SPR dose-response curves. Figure 2 identifies the compound 39 crystal ligand as having S-configuration. auto_single_measurement only accepted activity measurement [1] 1 structures\8R5C\8R5C_metadata.json point structures/8R5C/8r5c_protein.pdb structures/8R5C/8r5c_pocket.pdb structures/8R5C/8r5c_ligand.sdf structures/8R5C/8r5c_ligand.pdb structures/8R5C/8r5c_ligand.cif structures/8R5C/8r5c_complex.pdb structures/8R5C/8r5c_complex.cif 8R5K classic FKBP51 human Na Na Antascomicine B (paper: Antascomicin B) "[""Y6Z""]" 1 Kd Kd = = 6.7 ± 0.4 nM 6.7 [] unit_conversion 8.173925197299173 success True direct_binding Competitive fluorescence-polarization assay with purified human FKBPs; FKBP51 FK1 value in Table 1. 2 Table 1 states that Antascomicin B binds purified human FKBPs in a competitive fluorescence polarization assay and reports Kd values; the FKBP51FK1 entry is 6.7 ± 0.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8R5K\8R5K_metadata.json point structures/8R5K/8r5k_protein.pdb structures/8R5K/8r5k_pocket.pdb structures/8R5K/8r5k_ligand.sdf structures/8R5K/8r5k_ligand.pdb structures/8R5K/8r5k_ligand.cif structures/8R5K/8r5k_complex.pdb structures/8R5K/8r5k_complex.cif 8R5N classic DTX1 Homo sapiens DTX1 tandem WWE construct, residues 21-189 Na ATP "[""ATP""]" 1 Kd Kd = = 659 ± 294 µM 659000.0 [] unit_conversion 3.1811145854059903 success True direct_binding Protein-observed 15N-HSQC NMR titration of DTX1 with ATP; Table 1. 5 Table 1 reports ATP Kd 659 ± 294 µM for DTX1; the text identifies NMR-based Kd determinations for DTX1. auto_single_measurement only accepted activity measurement [1] 1 structures\8R5N\8R5N_metadata.json point structures/8R5N/8r5n_protein.pdb structures/8R5N/8r5n_pocket.pdb structures/8R5N/8r5n_ligand.sdf structures/8R5N/8r5n_ligand.pdb structures/8R5N/8r5n_ligand.cif structures/8R5N/8r5n_complex.pdb structures/8R5N/8r5n_complex.cif 8R74 classic galectin-1 human Na wild-type compound 5f (hydroxythiazole 5f) "[""YBC""]" 1 Kd Kd = = 0.337 ± 0.037 μM 337.0 [] unit_conversion 6.4723700991286615 success True direct_binding Competitive fluorescence-polarization determination of thiogalactoside affinity; Table 2 identifies 5f and reports human galectin-1 Kd. 4 Table 2 lists compound 5f with human galectin-1 Kd = 0.337 ± 0.037 μM. The paper maps the galectin-1:5f crystal structure to PDB 8R74. auto_single_measurement only accepted activity measurement [1] 1 structures\8R74\8R74_metadata.json point structures/8R74/8r74_protein.pdb structures/8R74/8r74_pocket.pdb structures/8R74/8r74_ligand.sdf structures/8R74/8r74_ligand.pdb structures/8R74/8r74_ligand.cif structures/8R74/8r74_complex.pdb structures/8R74/8r74_complex.cif 8R7O classic HUWE1 Homo sapiens HUWE1 WWE domain construct, residues 1611-1700 Na 2'F-ATP (2) "[""YGC""]" 1 Kd Kd = = 15 ± 2 µM 15000.0 [] unit_conversion 4.823908740944319 success True direct_binding Protein-observed 15N-HSQC NMR titration of HUWE1 WWE with 2′F-ATP (2); Table 1. 5 Table 1 reports a 2′F-ATP (2) Kd of 15 ± 2 µM for HUWE1; the text describes NMR-based Kd determinations. auto_single_measurement only accepted activity measurement [1] 1 structures\8R7O\8R7O_metadata.json point structures/8R7O/8r7o_protein.pdb structures/8R7O/8r7o_pocket.pdb structures/8R7O/8r7o_ligand.sdf structures/8R7O/8r7o_ligand.pdb structures/8R7O/8r7o_ligand.cif structures/8R7O/8r7o_complex.pdb structures/8R7O/8r7o_complex.cif 8R7S extended Cyclophilin TgCyp23 Toxoplasma gondii Na Na NIM811 (N-methyl-4-isoleucine cyclosporin) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 43 ± 10 nM 43.0 [] unit_conversion 7.366531544420414 success True direct_binding Isothermal titration calorimetry (ITC). 8 Table 1 reports TgCyp23 + NIM811 Kd = 43 ± 10 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8R7S\8R7S_metadata.json point structures/8R7S/8r7s_protein.pdb structures/8R7S/8r7s_pocket.pdb structures/8R7S/8r7s_ligand.pdb structures/8R7S/8r7s_ligand.cif structures/8R7S/8r7s_complex.pdb structures/8R7S/8r7s_complex.cif 8R7T extended Cyclophilin TgCyp23 Toxoplasma gondii Na Na Alisporivir (Debio 025) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 15 ± 3 nM 15.0 [] unit_conversion 7.823908740944319 success True direct_binding Isothermal titration calorimetry (ITC). 8 Table 1 reports TgCyp23 + Alisporivir Kd = 15 ± 3 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8R7T\8R7T_metadata.json point structures/8R7T/8r7t_protein.pdb structures/8R7T/8r7t_pocket.pdb structures/8R7T/8r7t_ligand.pdb structures/8R7T/8r7t_ligand.cif structures/8R7T/8r7t_complex.pdb structures/8R7T/8r7t_complex.cif 8R7U extended Cyclophilin TgCyp23 Toxoplasma gondii Na Na dihydro Cyclosporin A (dhCsA) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 200 ± 92 nM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Isothermal titration calorimetry (ITC). 8 Table 1 reports TgCyp23 + dhCsA Kd = 200 ± 92 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8R7U\8R7U_metadata.json point structures/8R7U/8r7u_protein.pdb structures/8R7U/8r7u_pocket.pdb structures/8R7U/8r7u_ligand.pdb structures/8R7U/8r7u_ligand.cif structures/8R7U/8r7u_complex.pdb structures/8R7U/8r7u_complex.cif 8R8U extended Human PADI4 human Na Na PADI4_3 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 2.7 ± 0.5 nM 2.7 [] unit_conversion 8.568636235841012 success True direct_binding Surface plasmon resonance; 10 mM CaCl2. 3 Table 1 reports PADI4_3 K_D = 2.7 ± 0.5 nM against Bio-hPADI4 wt at 10 mM CaCl2. auto_qualifier_priority unique best qualifier within highest-priority metric family [1, 4] 4 structures\8R8U\8R8U_metadata.json point structures/8R8U/8r8u_protein.pdb structures/8R8U/8r8u_pocket.pdb structures/8R8U/8r8u_ligand.pdb structures/8R8U/8r8u_ligand.cif structures/8R8U/8r8u_complex.pdb structures/8R8U/8r8u_complex.cif 8RD0 classic HUWE1 Homo sapiens HUWE1 WWE domain construct, residues 1611-1700 Na compound 3; N-(carboxymethyl)-phthalimide "[""51X""]" 1 Kd Kd = = 1763 µM 1763000.0 [] unit_conversion 2.7537476877006783 success True direct_binding 15N-HSQC NMR titration following fragment screening. 9 The text states that HSQC titrations yielded a Kd of 1763 µM for compound (3). auto_single_measurement only accepted activity measurement [1] 1 structures\8RD0\8RD0_metadata.json point structures/8RD0/8rd0_protein.pdb structures/8RD0/8rd0_pocket.pdb structures/8RD0/8rd0_ligand.sdf structures/8RD0/8rd0_ligand.pdb structures/8RD0/8rd0_ligand.cif structures/8RD0/8rd0_complex.pdb structures/8RD0/8rd0_complex.cif 8RD1 classic HUWE1 Homo sapiens HUWE1 WWE domain construct, residues 1611-1700 Na compound 4; 4-carboxy derivative of N-(carboxymethyl)-phthalimide "[""YP2""]" 1 Kd Kd = = 202 µM 202000.0 [] unit_conversion 3.6946486305533766 success True direct_binding 15N-HSQC NMR titration following fragment screening. 9 The text states that the stronger-affinity compound (4) had a Kd of 202 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8RD1\8RD1_metadata.json point structures/8RD1/8rd1_protein.pdb structures/8RD1/8rd1_pocket.pdb structures/8RD1/8rd1_ligand.sdf structures/8RD1/8rd1_ligand.pdb structures/8RD1/8rd1_ligand.cif structures/8RD1/8rd1_complex.pdb structures/8RD1/8rd1_complex.cif 8RD7 classic HUWE1 Homo sapiens HUWE1 WWE domain construct, residues 1611-1700 Na ADP-ribose (ADPr) "[""AR6""]" 1 Kd Kd = = 31 ± 6 µM 31000.0 [] unit_conversion 4.508638306165727 success True direct_binding Protein-observed 15N-HSQC NMR titration of HUWE1 WWE with ADP-ribose; Table 1. 5 Table 1 reports ADPr Kd 31 ± 6 µM for HUWE1; the text describes NMR-based Kd determinations. auto_single_measurement only accepted activity measurement [1] 1 structures\8RD7\8RD7_metadata.json point structures/8RD7/8rd7_protein.pdb structures/8RD7/8rd7_pocket.pdb structures/8RD7/8rd7_ligand.sdf structures/8RD7/8rd7_ligand.pdb structures/8RD7/8rd7_ligand.cif structures/8RD7/8rd7_complex.pdb structures/8RD7/8rd7_complex.cif 8RDZ classic ADP-ribose pyrophosphatase NUDT5 human NUDT5 residues 1-208; N-terminal 6x histidine tag followed by a TEV protease cleavage site Na ibrutinib (compound 1) "[""A1H14""]" 2 Kd Kd ~ ~ 200 nM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Purified-protein surface plasmon resonance (SPR). 2 Figure 1C caption states that SPR binding of compound 1 to NUDT5 gave KD ≈ 200 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8RDZ\8RDZ_metadata.json point structures/8RDZ/8rdz_protein.pdb structures/8RDZ/8rdz_pocket.pdb structures/8RDZ/8rdz_ligand.sdf structures/8RDZ/8rdz_ligand.pdb structures/8RDZ/8rdz_ligand.cif structures/8RDZ/8rdz_complex.pdb structures/8RDZ/8rdz_complex.cif 8RFA classic Arginase 2 Na Na Na compound 9 "[""A1HZ9""]" 1 IC50 IC50 = = 81 nM 81.0 [] unit_conversion 7.0915149811213505 success True biochemical_inhibition Table 1 enzyme inhibitory potency, Arg2 IC50. 3 Table 1 reports an Arg2 IC50 of 81 nM for compound 9; Figure 3 caption maps compound 9 to PDB 8RFA in Arg2. auto_single_measurement only accepted activity measurement [1] 1 structures\8RFA\8RFA_metadata.json point structures/8RFA/8rfa_protein.pdb structures/8RFA/8rfa_pocket.pdb structures/8RFA/8rfa_ligand.sdf structures/8RFA/8rfa_ligand.pdb structures/8RFA/8rfa_ligand.cif structures/8RFA/8rfa_complex.pdb structures/8RFA/8rfa_complex.cif 8RGF classic Arginase 2 Na Na Na compound 10 "[""A1H0A""]" 1 IC50 IC50 = = 15 nM 15.0 [] unit_conversion 7.823908740944319 success True biochemical_inhibition Table 1 enzyme inhibitory potency, Arg2 IC50. 3 Table 1 reports an Arg2 IC50 of 15 nM for compound 10; page 4 Figure 4 caption maps compound 10 to PDB 8RGF in Arg2. auto_single_measurement only accepted activity measurement [1] 1 structures\8RGF\8RGF_metadata.json point structures/8RGF/8rgf_protein.pdb structures/8RGF/8rgf_pocket.pdb structures/8RGF/8rgf_ligand.sdf structures/8RGF/8rgf_ligand.pdb structures/8RGF/8rgf_ligand.cif structures/8RGF/8rgf_complex.pdb structures/8RGF/8rgf_complex.cif 8RHJ extended Yeast 20S proteasome yeast 20S core particle (CP) Na compound 5, macrocyclic oxindole epoxyketone "[""POLYMER_ENTITY:15""]" 1 IC50 IC50 = = 0.19 ± 0.02 μM 190.0 [] unit_conversion 6.721246399047171 success True biochemical_inhibition Fluorometric kinetic enzyme inhibition assay. 4 Table 1 reports compound 5 ChT-L IC50 = 0.19 ± 0.02 μM; the adjacent text maps macrocyclic oxindole epoxyketone 5 to PDB 8RHJ bound to yeast CP. auto_single_measurement only accepted activity measurement [1] 1 structures\8RHJ\8RHJ_metadata.json point structures/8RHJ/8rhj_protein.pdb structures/8RHJ/8rhj_pocket.pdb structures/8RHJ/8rhj_ligand.pdb structures/8RHJ/8rhj_ligand.cif structures/8RHJ/8rhj_complex.pdb structures/8RHJ/8rhj_complex.cif 8RHT classic Trypanosoma brucei dihydrofolate reductase (TbDHFR) Trypanosoma brucei Isolated TbDHFR domain covering the N-terminal region and extending to residue 241 Na 1g (P25) "[""A1H0S""]" 1 Ki Ki = = 1.09 µM 1090.0 [] unit_conversion 5.962573502059376 success True biochemical_inhibition Enzymatic screening; inhibition constant against TbDHFR. 5 Table 2 reports TbDHFR Ki = 1.09 µM for compound 1g. auto_single_measurement only accepted activity measurement [1] 1 structures\8RHT\8RHT_metadata.json point structures/8RHT/8rht_protein.pdb structures/8RHT/8rht_pocket.pdb structures/8RHT/8rht_ligand.sdf structures/8RHT/8rht_ligand.pdb structures/8RHT/8rht_ligand.cif structures/8RHT/8rht_complex.pdb structures/8RHT/8rht_complex.cif 8RHU classic Trypanosoma brucei pteridine reductase 1 (TbPTR1) Trypanosoma brucei Whole-enzyme TbPTR1 tetramer Na 1g (P25) "[""A1H0S""]" 1 Ki Ki = = 7.89 µM 7890.0 [] unit_conversion 5.10292299679058 success True biochemical_inhibition Enzymatic screening; inhibition constant against TbPTR1. 5 Table 2 reports TbPTR1 Ki = 7.89 µM for compound 1g. auto_single_measurement only accepted activity measurement [1] 1 structures\8RHU\8RHU_metadata.json point structures/8RHU/8rhu_protein.pdb structures/8RHU/8rhu_pocket.pdb structures/8RHU/8rhu_ligand.sdf structures/8RHU/8rhu_ligand.pdb structures/8RHU/8rhu_ligand.cif structures/8RHU/8rhu_complex.pdb structures/8RHU/8rhu_complex.cif 8RHV classic Trypanosoma brucei pteridine reductase 1 (TbPTR1) Trypanosoma brucei Whole-enzyme TbPTR1 tetramer Na 1f (P30) "[""A1H0U""]" 1 Ki Ki = = 5.73 µM 5730.0 [] unit_conversion 5.24184537803261 success True biochemical_inhibition Enzymatic screening; inhibition constant against TbPTR1. 5 Table 2 reports TbPTR1 Ki = 5.73 µM for compound 1f. auto_single_measurement only accepted activity measurement [1] 1 structures\8RHV\8RHV_metadata.json point structures/8RHV/8rhv_protein.pdb structures/8RHV/8rhv_pocket.pdb structures/8RHV/8rhv_ligand.sdf structures/8RHV/8rhv_ligand.pdb structures/8RHV/8rhv_ligand.cif structures/8RHV/8rhv_complex.pdb structures/8RHV/8rhv_complex.cif 8RHW extended Trypanosoma brucei pteridine reductase 1 (TbPTR1) Trypanosoma brucei Whole-enzyme TbPTR1 tetramer Na 2f (P31) "[""A1H0W""]" 1 Ki Ki = = 9.15 µM 9150.0 [] unit_conversion 5.0385789059335515 success True biochemical_inhibition Enzymatic screening; inhibition constant against TbPTR1. 5 Table 2 reports TbPTR1 Ki = 9.15 µM for compound 2f. auto_single_measurement only accepted activity measurement [1] 1 structures\8RHW\8RHW_metadata.json point structures/8RHW/8rhw_protein.pdb structures/8RHW/8rhw_pocket.pdb structures/8RHW/8rhw_ligand.pdb structures/8RHW/8rhw_ligand.cif structures/8RHW/8rhw_complex.pdb structures/8RHW/8rhw_complex.cif 8RHX extended Trypanosoma brucei pteridine reductase 1 (TbPTR1) Trypanosoma brucei Whole-enzyme TbPTR1 tetramer Na 2d (P32) "[""A1H0T""]" 1 Ki Ki = = 4.94 µM 4940.0 [] unit_conversion 5.306273051076353 success True biochemical_inhibition Enzymatic screening; inhibition constant against TbPTR1. 5 Table 2 reports TbPTR1 Ki = 4.94 µM for compound 2d. auto_single_measurement only accepted activity measurement [1] 1 structures\8RHX\8RHX_metadata.json point structures/8RHX/8rhx_protein.pdb structures/8RHX/8rhx_pocket.pdb structures/8RHX/8rhx_ligand.pdb structures/8RHX/8rhx_ligand.cif structures/8RHX/8rhx_complex.pdb structures/8RHX/8rhx_complex.cif 8RHY extended Trypanosoma brucei pteridine reductase 1 (TbPTR1) Trypanosoma brucei Whole-enzyme TbPTR1 tetramer Na 2c (P34) "[""A1H0V""]" 1 Ki Ki = = 3.23 µM 3230.0 [] unit_conversion 5.490797477668897 success True biochemical_inhibition Enzymatic screening; inhibition constant against TbPTR1. 5 Table 2 reports TbPTR1 Ki = 3.23 µM for compound 2c. auto_single_measurement only accepted activity measurement [1] 1 structures\8RHY\8RHY_metadata.json point structures/8RHY/8rhy_protein.pdb structures/8RHY/8rhy_pocket.pdb structures/8RHY/8rhy_ligand.pdb structures/8RHY/8rhy_ligand.cif structures/8RHY/8rhy_complex.pdb structures/8RHY/8rhy_complex.cif 8RI1 classic BmrA Bacillus subtilis BmrA E504A mutant with N-terminal 6xHis tag E504A ATP-Mg2+ "[""ATP""]" 1 Kd Kd = = 154.0 ± 49.0 µM 154000.0 [] unit_conversion 3.8124792791635373 success True direct_binding Intrinsic-fluorescence ATP-Mg2+ binding assay; apo E504A BmrA showed Michaelian binding. 2 “Probing ATP-Mg2+ binding (Fig. 1A) indeed reveals a michaelian type binding (hyperbolic-type curve, Kd-app = 154.0 µM ± 49.0).” auto_single_measurement only accepted activity measurement [1] 1 structures\8RI1\8RI1_metadata.json point structures/8RI1/8ri1_protein.pdb structures/8RI1/8ri1_pocket.pdb structures/8RI1/8ri1_ligand.sdf structures/8RI1/8ri1_ligand.pdb structures/8RI1/8ri1_ligand.cif structures/8RI1/8ri1_complex.pdb structures/8RI1/8ri1_complex.cif 8RI2 classic NLRP3 human NACHT domain, residues 161-679 Na NP3-562 "[""A1H02""]" 1 IC50 IC50 = = 0.26 μM 260.0 [] unit_conversion 6.585026652029182 success True direct_binding Fluorescence-polarization binding assay using recombinant NLRP3 NACHT protein and a BODIPY-labeled sulfonylurea tracer (NP3-301); NP3-562 was reported to bind the same NACHT-domain ligand-binding site. 6 “NP3−562 had an IC50 of 0.26 μM in the FP binding assay”; the same page identifies the co-crystal structure as PDB 8RI2. auto_single_measurement only accepted activity measurement [1] 1 structures\8RI2\8RI2_metadata.json point structures/8RI2/8ri2_protein.pdb structures/8RI2/8ri2_pocket.pdb structures/8RI2/8ri2_ligand.sdf structures/8RI2/8ri2_ligand.pdb structures/8RI2/8ri2_ligand.cif structures/8RI2/8ri2_complex.pdb structures/8RI2/8ri2_complex.cif 8RIM classic arginase 2 (hArg2) human Na Na compound 20 "[""A1H04""]" 1 IC50 IC50 = = 0.081 ± 0.02 µM 81.0 [] unit_conversion 7.0915149811213505 success True biochemical_inhibition Biochemical Arg2 inhibition assay; Table 1 reports geometric mean ± standard deviation. 4 Table 1 reports compound 20: Arg2 IC50 0.081 ± 0.02 µM. Figure 3 maps compound 20 to the hArg2 structure printed as PDB 8RFA; the supplied sibling mapping uniquely corrects this to requested 8RIM. auto_single_measurement only accepted activity measurement [1] 1 structures\8RIM\8RIM_metadata.json point structures/8RIM/8rim_protein.pdb structures/8RIM/8rim_pocket.pdb structures/8RIM/8rim_ligand.sdf structures/8RIM/8rim_ligand.pdb structures/8RIM/8rim_ligand.cif structures/8RIM/8rim_complex.pdb structures/8RIM/8rim_complex.cif 8RIY extended NUDT5 human NUDT5 residues 1-208; N-terminal 6x histidine tag followed by a TEV protease cleavage site Na compound 9 (ibrutinib derivative) "[""W0O""]" 2 Kd Kd ~ ~ 250 nM 250.0 [] unit_conversion 6.6020599913279625 success True direct_binding Purified-protein surface plasmon resonance (SPR). 6 Figure 3A caption states that compound 9 has an SPR KD of approximately 250 nM for NUDT5. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8RIY\8RIY_metadata.json point structures/8RIY/8riy_ligand.sdf structures/8RIY/8riy_ligand.cif structures/8RIY/8riy_complex.cif 8RKS extended VPS29-VPS35 Na VPS35 residues 476-780 in complex with VPS29; bound FAM21 R21 peptide residues 1328-1341 Na FAM21 R21 peptide (1328SNIFDDPLNAFGGQ1341) "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L""]" 1 Kd Kd = = 17 µM 17000.0 [] unit_conversion 4.769551078621726 success True direct_binding ITC binding isotherm; R21 tested against individual retromer subunits/truncated subcomplexes. 4 Figure 2c reports Kd 17 µM for R21 binding to VPS29–VPS35C. auto_single_measurement only accepted activity measurement [1] 1 structures\8RKS\8RKS_metadata.json point structures/8RKS/8rks_protein.pdb structures/8RKS/8rks_pocket.pdb structures/8RKS/8rks_ligand.pdb structures/8RKS/8rks_ligand.cif structures/8RKS/8rks_complex.pdb structures/8RKS/8rks_complex.cif 8RLO extended Human Carbonic Anhydrase I human Na Na veralipride "[""A1H1P""]" 1 Ki Ki = = 2723 nM 2723.0 [] unit_conversion 5.564952358660035 success True biochemical_inhibition Stopped-flow CO2 hydration assay; recombinant human CA isoforms; Table 1. 2 Table 1 reports Ki = 2723 nM for veralipride against hCA I. Figure 2 maps the hCA I–veralipride structure to PDB 8RLO. auto_single_measurement only accepted activity measurement [1] 1 structures\8RLO\8RLO_metadata.json point structures/8RLO/8rlo_ligand.sdf structures/8RLO/8rlo_ligand.cif structures/8RLO/8rlo_complex.cif 8RLP extended Human Carbonic Anhydrase II human engineered human CA II protein Na veralipride "[""A1H11""]" 1 Ki Ki = = 405.7 nM 405.7 [] unit_conversion 6.391794992295674 success True biochemical_inhibition Stopped-flow CO2 hydration assay; engineered recombinant human CA II protein; Table 1. 2 Table 1 reports Ki = 405.7 nM for veralipride against hCA II. Figure 2 maps the hCA II–veralipride structure to PDB 8RLP. auto_single_measurement only accepted activity measurement [1] 1 structures\8RLP\8RLP_metadata.json point structures/8RLP/8rlp_ligand.sdf structures/8RLP/8rlp_ligand.cif structures/8RLP/8rlp_complex.cif 8RMT classic Galectin-3 human Na Na compound 12 "[""A1H1W""]" 1 IC50 IC50 = = 12 nM 12.0 [] unit_conversion 7.920818753952375 success True biochemical_inhibition Asialofetuin (ASF) competitive binding assay; Table 2 reports hGal-3 IC50. 3 Table 2 lists compound 12 with hGal-3 IC50 12 [1.77] nM; the text identifies the assay as an ASF competitive binding assay. Figure 5 maps compound 12 to PDB 8RMT. auto_single_measurement only accepted activity measurement [1] 1 structures\8RMT\8RMT_metadata.json point structures/8RMT/8rmt_protein.pdb structures/8RMT/8rmt_pocket.pdb structures/8RMT/8rmt_ligand.sdf structures/8RMT/8rmt_ligand.pdb structures/8RMT/8rmt_ligand.cif structures/8RMT/8rmt_complex.pdb structures/8RMT/8rmt_complex.cif 8RMU classic Galectin-3 human Na Na compound 10 "[""A1H1Y""]" 1 IC50 IC50 = = 28 nM 28.0 [] unit_conversion 7.552841968657781 success True biochemical_inhibition Asialofetuin (ASF) competitive binding assay; Table 2 reports hGal-3 IC50. 3 Table 2 lists compound 10 with hGal-3 IC50 28 [1.70] nM; the text identifies the assay as an ASF competitive binding assay. Figure 5 maps compound 10 to PDB 8RMU. auto_single_measurement only accepted activity measurement [1] 1 structures\8RMU\8RMU_metadata.json point structures/8RMU/8rmu_protein.pdb structures/8RMU/8rmu_pocket.pdb structures/8RMU/8rmu_ligand.sdf structures/8RMU/8rmu_ligand.pdb structures/8RMU/8rmu_ligand.cif structures/8RMU/8rmu_complex.pdb structures/8RMU/8rmu_complex.cif 8RMV classic Galectin-3 human Na Na compound 8 "[""A1H1X""]" 1 IC50 IC50 = = 52 nM 52.0 [] unit_conversion 7.2839966563652006 success True biochemical_inhibition Asialofetuin (ASF) competitive binding assay; Table 2 reports hGal-3 IC50. 3 Table 2 lists compound 8 with hGal-3 IC50 52 [1.28] nM; the text identifies the assay as an ASF competitive binding assay. Figure 5 maps compound 8 to PDB 8RMV. auto_single_measurement only accepted activity measurement [1] 1 structures\8RMV\8RMV_metadata.json point structures/8RMV/8rmv_protein.pdb structures/8RMV/8rmv_pocket.pdb structures/8RMV/8rmv_ligand.sdf structures/8RMV/8rmv_ligand.pdb structures/8RMV/8rmv_ligand.cif structures/8RMV/8rmv_complex.pdb structures/8RMV/8rmv_complex.cif 8ROU classic Human Carbonic Anhydrase II human Na Na 5b (1-carbamimidamido-N-[(4 sulfamoylphenyl)methyl]methanimidamide) "[""A1H15""]" 1 Ki Ki = = 369.5 nM 369.5 [] unit_conversion 6.432385557269155 success True biochemical_inhibition CO2-hydrase stopped-flow inhibition assay; Table 1 reports mean Ki values. 2 Table 1 prints Ki = 369.5 nM for 5b against hCA II; the table caption identifies a CO2-hydrase stopped-flow assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8ROU\8ROU_metadata.json point structures/8ROU/8rou_protein.pdb structures/8ROU/8rou_pocket.pdb structures/8ROU/8rou_ligand.sdf structures/8ROU/8rou_ligand.pdb structures/8ROU/8rou_ligand.cif structures/8ROU/8rou_complex.pdb structures/8ROU/8rou_complex.cif 8ROX extended DDB1-DDA1-DCAF15 E3 ubiquitin ligase human Codon-optimized human DCAF15 residues 1-600 with N-terminal His-ZZ-Tev tag, coexpressed with DDB1 residues 1-395-GNGNSG-706-1140 and DDA1 residues 1-102; tag cleaved for the purified complex Na furan 12 (compound 12) "[""A1H17""]" 1 IC50 IC50 = = 0.221 µM 221.0 [] unit_conversion 6.655607726314889 success True direct_binding Purified-protein DCAF15 TR-FRET ligand-displacement binding assay. 5 Table 2 lists compound 12 with DCAF15 IC50 = 0.221 µM; the table footnote defines the affinity data and IC50 assay context. auto_single_measurement only accepted activity measurement [1] 1 structures\8ROX\8ROX_metadata.json point structures/8ROX/8rox_protein.pdb structures/8ROX/8rox_pocket.pdb structures/8ROX/8rox_ligand.pdb structures/8ROX/8rox_ligand.cif structures/8ROX/8rox_complex.pdb structures/8ROX/8rox_complex.cif 8ROY extended DDB1-DDA1-DCAF15 E3 ubiquitin ligase human Codon-optimized human DCAF15 residues 1-600 with N-terminal His-ZZ-Tev tag, coexpressed with DDB1 residues 1-395-GNGNSG-706-1140 and DDA1 residues 1-102; tag cleaved for the purified complex Na furan 24 (compound 24) "[""A1H18""]" 1 IC50 IC50 = = 0.053 µM 53.0 [] unit_conversion 7.275724130399211 success True direct_binding Purified-protein DCAF15 TR-FRET ligand-displacement binding assay. 5 Table 3 lists compound 24 with DCAF15 IC50 = 0.053 µM; adjacent text identifies it as elaborated piperazine 24. auto_single_measurement only accepted activity measurement [1] 1 structures\8ROY\8ROY_metadata.json point structures/8ROY/8roy_protein.pdb structures/8ROY/8roy_pocket.pdb structures/8ROY/8roy_ligand.pdb structures/8ROY/8roy_ligand.cif structures/8ROY/8roy_complex.pdb structures/8ROY/8roy_complex.cif 8RQ0 extended Escherichia coli 50S subunit Escherichia coli Na Na Api88 "[""POLYMER_ENTITY:32""]" 1 Kd Kd = = 0.58 ± 0.05 µmol/L 580.0 [] unit_conversion 6.236572006437063 success True direct_binding Fluorescence-polarization assay with cf-labeled Api88 and purified 50S subunits. 3 Fig. 1e table reports Api88 Kd of 0.58 ± 0.05 µmol/L for the 50S subunit. auto_single_measurement only accepted activity measurement [1] 1 structures\8RQ0\8RQ0_metadata.json point structures/8RQ0/8rq0_protein.pdb structures/8RQ0/8rq0_pocket.pdb structures/8RQ0/8rq0_ligand.pdb structures/8RQ0/8rq0_ligand.cif structures/8RQ0/8rq0_complex.pdb structures/8RQ0/8rq0_complex.cif 8RQ9 classic CRBN-midi; BRD4(BD2) human CRBNmidi, residues 41-187 and 249-426 joined by a GSG linker, plus BRD4BD2 residues 333-460 C78I; I92V; K116N; Q134E; R283W; C287N; V293S; G302D; L342R; C343E; T359I; L423I CFT-1297 "[""A1H2F""]" 1 Kd Kd = = 0.68 μM 680.0 [] unit_conversion 6.167491087293763 success True direct_binding SPR ternary-complex assay with CFT-1297 pre-incubated with BRD4BD2. 8 A 3-fold enhanced affinity for the PROTAC:BRD4BD2 binding to CRBNmidi was reported, with ternary K_D = 0.68 μM versus binary K_D = 2.1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8RQ9\8RQ9_metadata.json point structures/8RQ9/8rq9_protein.pdb structures/8RQ9/8rq9_pocket.pdb structures/8RQ9/8rq9_ligand.sdf structures/8RQ9/8rq9_ligand.pdb structures/8RQ9/8rq9_ligand.cif structures/8RQ9/8rq9_complex.pdb structures/8RQ9/8rq9_complex.cif 8RQA classic CRBN-midi human CRBNmidi, residues 41-187 and 249-426 joined by a GSG linker C78I; I92V; K116N; Q134E; R283W; C287N; V293S; G302D; L342R; C343E; T359I; L423I lenalidomide "[""LVY""]" 1 Kd Kd = = 2.9 μM 2900.0 [] unit_conversion 5.537602002101044 success True direct_binding Isothermal titration calorimetry of lenalidomide titrated into CRBNmidi. 6 ITC titration of lenalidomide into CRBNmidi yielded K_D of 2.9 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8RQA\8RQA_metadata.json point structures/8RQA/8rqa_protein.pdb structures/8RQA/8rqa_pocket.pdb structures/8RQA/8rqa_ligand.sdf structures/8RQA/8rqa_ligand.pdb structures/8RQA/8rqa_ligand.cif structures/8RQA/8rqa_complex.pdb structures/8RQA/8rqa_complex.cif 8RU3 extended beta-catenin Na armadillo repeat domain, residues 134-665 Na a12-LW "[""CHAIN:P""]" 1 Kd Kd = = 0.06±0.01 µM 60.0 [] unit_conversion 7.221848749616356 success True direct_binding Direct fluorescence-polarization assay with FITC-labelled a11-LW-derived peptides and β-catenin. 3 Figure 2c reports a12-LW affinity (Kd) of 0.06±0.01 µM; the caption identifies the measurement as a direct FP assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8RU3\8RU3_metadata.json point structures/8RU3/8ru3_protein.pdb structures/8RU3/8ru3_pocket.pdb structures/8RU3/8ru3_ligand.pdb structures/8RU3/8ru3_ligand.cif structures/8RU3/8ru3_complex.pdb structures/8RU3/8ru3_complex.cif 8RU4 extended Human Catenin Beta-1 human armadillo repeat domain, residues 145-665 Na st3 "[""CHAIN:C""]" 1 Kd Kd = = 23±4 nM 23.0 [] unit_conversion 7.638272163982407 success True direct_binding Direct fluorescence-polarization assay with FITC-labelled a11-LW-derived peptides and β-catenin. 3 Figure 2c reports stitched peptide st3 affinity (Kd) of 23±4 nM; the caption identifies the measurement as a direct FP assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8RU4\8RU4_metadata.json point structures/8RU4/8ru4_protein.pdb structures/8RU4/8ru4_pocket.pdb structures/8RU4/8ru4_ligand.pdb structures/8RU4/8ru4_ligand.cif structures/8RU4/8ru4_complex.pdb structures/8RU4/8ru4_complex.cif 8RV4 classic SARS-CoV-2 nsp16-nsp10 SARS-CoV-2 nsp16-nsp10 complex Na inhibitor 2; compound 2 "[""A1H3C""]" 1 IC50 IC50 = = 9 ± 0.4 nM 9.0 [] unit_conversion 8.045757490560675 success True biochemical_inhibition Purified recombinant nsp16-nsp10 methyltransferase activity assay measuring SAM-to-SAH conversion in the presence of RNA substrate. 3 Figure 2 assigns PDB ID 8RV4 to compound 2 and prints IC50 = 9 ± 0.4 nM; its caption states IC50 values were determined using the authors' assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8RV4\8RV4_metadata.json point structures/8RV4/8rv4_protein.pdb structures/8RV4/8rv4_pocket.pdb structures/8RV4/8rv4_ligand.sdf structures/8RV4/8rv4_ligand.pdb structures/8RV4/8rv4_ligand.cif structures/8RV4/8rv4_complex.pdb structures/8RV4/8rv4_complex.cif 8RV7 classic SARS-CoV-2 nsp16-nsp10 SARS-CoV-2 nsp16-nsp10 complex Na Na "[""A1H3E""]" 1 IC50 IC50 = = 4.6 ± 0.2 nM 4.6 [] unit_conversion 8.337242168318426 success True biochemical_inhibition Purified recombinant nsp16-nsp10 methyltransferase activity assay measuring SAM-to-SAH conversion in the presence of RNA substrate. 3 Figure 2 assigns PDB ID 8RV7 to compound 7 and prints IC50 = 4.6 ± 0.2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8RV7\8RV7_metadata.json point structures/8RV7/8rv7_protein.pdb structures/8RV7/8rv7_pocket.pdb structures/8RV7/8rv7_ligand.sdf structures/8RV7/8rv7_ligand.pdb structures/8RV7/8rv7_ligand.cif structures/8RV7/8rv7_complex.pdb structures/8RV7/8rv7_complex.cif 8RVA classic SARS-CoV-2 nsp16-nsp10 SARS-CoV-2 nsp16-nsp10 complex Na Na "[""A1H3D""]" 1 IC50 IC50 = = 4 ± 0.5 nM 4.0 [] unit_conversion 8.397940008672037 success True biochemical_inhibition Purified recombinant nsp16-nsp10 methyltransferase activity assay measuring SAM-to-SAH conversion in the presence of RNA substrate. 3 Figure 2 assigns PDB ID 8RVA to compound 10 and prints IC50 = 4 ± 0.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8RVA\8RVA_metadata.json point structures/8RVA/8rva_protein.pdb structures/8RVA/8rva_pocket.pdb structures/8RVA/8rva_ligand.sdf structures/8RVA/8rva_ligand.pdb structures/8RVA/8rva_ligand.cif structures/8RVA/8rva_complex.pdb structures/8RVA/8rva_complex.cif 8RVF extended human monoacylglycerol lipase (hMAGL) human Na Na compound 5 "[""A1H35""]" 2 Kd Kd = = 6.65 nM 6.65 [] unit_conversion 8.177178354696895 success True direct_binding Cell-free fluorescence-polarization dose-response titration of reversible probe 5 with purified hMAGL. 9 Figure 3A labels probe 5 with Kd = 6.65 nM; its caption states this is a fluorescence-polarization dose-response titration of reversible probe 5 (20 nM) with purified hMAGL. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8RVF\8RVF_metadata.json point structures/8RVF/8rvf_protein.pdb structures/8RVF/8rvf_pocket.pdb structures/8RVF/8rvf_ligand.pdb structures/8RVF/8rvf_ligand.cif structures/8RVF/8rvf_complex.pdb structures/8RVF/8rvf_complex.cif 8RX7 extended LTA4 hydrolase (LTA4H) Na Na Na compound 2 "[""A1H3S""]" 1 IC50 IC50 = = 88 ± 23 nM 88.0 [] unit_conversion 7.055517327849831 success True biochemical_inhibition LTA4H enzyme-inhibition assay in screening mode using Arg-AMC substrate; Table 1 biochemical value. 3 Table 1 reports compound 2: LTA4H (biochemical) IC50 = 88 ± 23 nM. The table footnote identifies the screening-mode LTA4H enzyme-inhibition assay using Arg-AMC substrate. auto_single_measurement only accepted activity measurement [1] 1 structures\8RX7\8RX7_metadata.json point structures/8RX7/8rx7_protein.pdb structures/8RX7/8rx7_pocket.pdb structures/8RX7/8rx7_ligand.pdb structures/8RX7/8rx7_ligand.cif structures/8RX7/8rx7_complex.pdb structures/8RX7/8rx7_complex.cif 8RX9 extended LTA4 hydrolase (LTA4H) Na Na Na compound 3 "[""A1H3U""]" 1 IC50 IC50 = = 3 ± 3 nM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition LTA4H enzyme-inhibition screening assay using Arg-AMC substrate; Table 2 biochemical value. 5 Table 2 reports compound 3: LTA4H (biochemical) IC50 = 3 ± 3 nM. The table footnote identifies an LTA4H enzyme-inhibition assay using Arg-AMC substrate. auto_single_measurement only accepted activity measurement [1] 1 structures\8RX9\8RX9_metadata.json point structures/8RX9/8rx9_protein.pdb structures/8RX9/8rx9_pocket.pdb structures/8RX9/8rx9_ligand.pdb structures/8RX9/8rx9_ligand.cif structures/8RX9/8rx9_complex.pdb structures/8RX9/8rx9_complex.cif 8RXR classic VPS34 human VPS34DeltaC2, residues S282-H879 Na SB02024 "[""A1H4E""]" 1 IC50 IC50 = = 5 nM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition Purified VPS34 enzyme biochemical activity assay; Figure 1 legend states VPS34 enzyme was incubated with SB02024, with n=12 independent experiments. 8 Fig. 1D visibly prints “Biochemical assay IC50 = 5 nM.” The figure legend identifies this as a VPS34 enzyme assay with SB02024. Methods describe the VPS34ΔC2 construct as human VPS34 residues S282-H879, and page 5 maps the VPS34ΔC2/SB02024 complex to PDB 8RXR. auto_single_measurement only accepted activity measurement [1] 1 structures\8RXR\8RXR_metadata.json point structures/8RXR/8rxr_protein.pdb structures/8RXR/8rxr_pocket.pdb structures/8RXR/8rxr_ligand.sdf structures/8RXR/8rxr_ligand.pdb structures/8RXR/8rxr_ligand.cif structures/8RXR/8rxr_complex.pdb structures/8RXR/8rxr_complex.cif 8RYK extended human IL-1beta human Na Na compound 11 "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 14 µM 14000.0 [] unit_conversion 4.853871964321762 success True biochemical_inhibition TR-FRET-based IL-1β:IL-1R1 inhibition assay; compound 11 is the macrocyclic peptide in PDB 8RYK. 8 “Compound 11 showed a relatively weak IC50 of 14 μM in the TR-FRET-based IL-1β:IL-1R1 assay (Table 1 and Figure S5B).” auto_single_measurement only accepted activity measurement [1] 1 structures\8RYK\8RYK_metadata.json point structures/8RYK/8ryk_protein.pdb structures/8RYK/8ryk_pocket.pdb structures/8RYK/8ryk_ligand.pdb structures/8RYK/8ryk_ligand.cif structures/8RYK/8ryk_complex.pdb structures/8RYK/8ryk_complex.cif 8RZD classic SARS-CoV-2 nsp16-nsp10 SARS-CoV-2 nsp16-nsp10 complex Na Na "[""A1H4C""]" 1 IC50 IC50 = = 1.4 ± 0.1 nM 1.4 [] unit_conversion 8.853871964321762 success True biochemical_inhibition Purified recombinant nsp16-nsp10 methyltransferase activity assay measuring SAM-to-SAH conversion in the presence of RNA substrate. 3 Figure 2 assigns PDB ID 8RZD to compound 4 and prints IC50 = 1.4 ± 0.1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8RZD\8RZD_metadata.json point structures/8RZD/8rzd_protein.pdb structures/8RZD/8rzd_pocket.pdb structures/8RZD/8rzd_ligand.sdf structures/8RZD/8rzd_ligand.pdb structures/8RZD/8rzd_ligand.cif structures/8RZD/8rzd_complex.pdb structures/8RZD/8rzd_complex.cif 8RZJ classic ZgGH129 Zobellia galactanivorans Na Na ADG-IF (3,6-anhydro-D-galacto-isofagomine) "[""A1H36""]" 1 Ki Ki = = 1.50 ± 0.06 µM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition Inhibition assay of ZgGH129 with ADG-IF. 3 “ADG-IF 8 was a potent inhibitor of ZgGH129 with a Ki value of 1.50 ± 0.06 µM”; page 7 maps ADG-IF to PDB 8RZJ. auto_single_measurement only accepted activity measurement [1] 1 structures\8RZJ\8RZJ_metadata.json point structures/8RZJ/8rzj_protein.pdb structures/8RZJ/8rzj_pocket.pdb structures/8RZJ/8rzj_ligand.sdf structures/8RZJ/8rzj_ligand.pdb structures/8RZJ/8rzj_ligand.cif structures/8RZJ/8rzj_complex.pdb structures/8RZJ/8rzj_complex.cif 8RZW classic SHP2 Na full-length SHP2 Na compound 1 "[""A1H4N""]" 1 Kd Kd > > 5.0 mM 5000000.0 [] unit_conversion 2.3010299956639813 success True direct_binding ITC using full-length SHP2 (residues 1–528). 3 Table 1 reports compound 1, PTP/WPD-loop: SHP2 ITC K_D >5.0 mM; footnote specifies full-length SHP2 residues 1–528. auto_single_measurement only accepted activity measurement [1] 1 structures\8RZW\8RZW_metadata.json point structures/8RZW/8rzw_protein.pdb structures/8RZW/8rzw_pocket.pdb structures/8RZW/8rzw_ligand.sdf structures/8RZW/8rzw_ligand.pdb structures/8RZW/8rzw_ligand.cif structures/8RZW/8rzw_complex.pdb structures/8RZW/8rzw_complex.cif 8S01 classic SHP2 Na full-length SHP2 Na compound 3 "[""A1H4J""]" 1 Kd Kd = = 1.0 mM 1000000.0 [] unit_conversion 3.0 success True direct_binding ITC using full-length SHP2 (residues 1–528). 3 Table 1 reports compound 3 at the Tunnel Site with SHP2 ITC K_D 1.0 mM; footnote specifies full-length SHP2 residues 1–528. auto_single_measurement only accepted activity measurement [1] 1 structures\8S01\8S01_metadata.json point structures/8S01/8s01_protein.pdb structures/8S01/8s01_pocket.pdb structures/8S01/8s01_ligand.sdf structures/8S01/8s01_ligand.pdb structures/8S01/8s01_ligand.cif structures/8S01/8s01_complex.pdb structures/8S01/8s01_complex.cif 8S38 classic glutamate dehydrogenase 2 (MtGDH2) Medicago truncatula Na Na citrate (CIT) "[""CIT""]" 1 IC50 IC50 = = 3.128 ± 0.21 mM 3128000.0 [] unit_conversion 2.50473325561219 success True biochemical_inhibition In vitro inhibition of the oxidative deamination reaction (Glu → 2OG). 9 Table 4 reports MtGDH2 IC50 for CIT as 3.128 ± 0.21 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8S38\8S38_metadata.json point structures/8S38/8s38_protein.pdb structures/8S38/8s38_pocket.pdb structures/8S38/8s38_ligand.sdf structures/8S38/8s38_ligand.pdb structures/8S38/8s38_ligand.cif structures/8S38/8s38_complex.pdb structures/8S38/8s38_complex.cif 8S39 classic glutamate dehydrogenase 2 (MtGDH2) Medicago truncatula Na Na isophthalic acid (IPA) "[""8G0""]" 1 IC50 IC50 = = 0.509 ± 0.02 mM 509000.0 [] unit_conversion 3.2932822176632417 success True biochemical_inhibition In vitro inhibition of the oxidative deamination reaction (Glu → 2OG). 9 Table 4 reports MtGDH2 IC50 for IPA as 0.509 ± 0.02 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8S39\8S39_metadata.json point structures/8S39/8s39_protein.pdb structures/8S39/8s39_pocket.pdb structures/8S39/8s39_ligand.sdf structures/8S39/8s39_ligand.pdb structures/8S39/8s39_ligand.cif structures/8S39/8s39_complex.pdb structures/8S39/8s39_complex.cif 8S3A classic glutamate dehydrogenase 2 (MtGDH2) Medicago truncatula Na Na 2,6-pyridinedicarboxylic acid (PYR) "[""PDC""]" 1 IC50 IC50 = = 2.148 ± 0.16 mM 2148000.0 [] unit_conversion 2.6679657229724816 success True biochemical_inhibition In vitro inhibition of the oxidative deamination reaction (Glu → 2OG). 9 Table 4 reports MtGDH2 IC50 for PYR as 2.148 ± 0.16 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8S3A\8S3A_metadata.json point structures/8S3A/8s3a_protein.pdb structures/8S3A/8s3a_pocket.pdb structures/8S3A/8s3a_ligand.sdf structures/8S3A/8s3a_ligand.pdb structures/8S3A/8s3a_ligand.cif structures/8S3A/8s3a_complex.pdb structures/8S3A/8s3a_complex.cif 8S3B extended glutamate dehydrogenase 2 (MtGDH2) Medicago truncatula Na Na 3-(1H-tetrazol-5-yl)benzoic acid (TBA) "[""A1H40""]" 1 IC50 IC50 = = 0.648 ± 0.04 mM 648000.0 [] unit_conversion 3.1884249941294067 success True biochemical_inhibition In vitro inhibition of the oxidative deamination reaction (Glu → 2OG). 9 Table 4 reports MtGDH2 IC50 for TBA as 0.648 ± 0.04 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8S3B\8S3B_metadata.json point structures/8S3B/8s3b_protein.pdb structures/8S3B/8s3b_pocket.pdb structures/8S3B/8s3b_ligand.pdb structures/8S3B/8s3b_ligand.cif structures/8S3B/8s3b_complex.pdb structures/8S3B/8s3b_complex.cif 8S3R classic human PI3Kdelta human Na Na compound 7 "[""A1H48""]" 1 pKi Ki = = 9.2 ± 0.06 unitless 0.6309573444801942 [] p_metric_transform 9.2 success True biochemical_inhibition Cell-free ADP-Glo recombinant PI3K enzymatic inhibition assay; Table 1 reports pKi for compound 7. 4 Table 1 reports compound 7: PI3Kδ pKi 9.2 ± 0.06. The paper identifies the X-ray structure of compound 7 with PI3Kδ as PDB 8S3R (Figure 4). auto_single_measurement only accepted activity measurement [1] 1 structures\8S3R\8S3R_metadata.json point structures/8S3R/8s3r_protein.pdb structures/8S3R/8s3r_pocket.pdb structures/8S3R/8s3r_ligand.sdf structures/8S3R/8s3r_ligand.pdb structures/8S3R/8s3r_ligand.cif structures/8S3R/8s3r_complex.pdb structures/8S3R/8s3r_complex.cif 8S3X extended LIM Domain Kinase 2 (LIMK2) Na LIMK2 kinase domain, residues 330-632 Na compound 52 "[""A1H41""]" 1 Ki Ki = = 5 nM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition LanthaScreen™ Eu Kinase Binding Assay; Table 2 reports the LIMK2 value for compound 52. 7 Table 2, compound 52: Ki (nM) LIMK2 = 5. The text states that Ki values were measured using the LanthaScreen™ Eu Kinase Binding Assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8S3X\8S3X_metadata.json point structures/8S3X/8s3x_protein.pdb structures/8S3X/8s3x_pocket.pdb structures/8S3X/8s3x_ligand.pdb structures/8S3X/8s3x_ligand.cif structures/8S3X/8s3x_complex.pdb structures/8S3X/8s3x_complex.cif 8S4J classic VcGluP (VC0430), glutamate-specific TAXI TRAP substrate-binding protein Vibrio cholerae Mature VcGluP residues 29-328 Na L-glutamate "[""GLU""]" 1 Kd Kd = = 0.065 ± 0.031 µM 65.0 [] unit_conversion 7.187086643357144 success True direct_binding Intrinsic tryptophan-fluorescence ligand titration fitted to a one-site-specific binding model. 5 Fitting L-glutamate titrations gave a dissociation constant of 0.065 ± 0.031 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8S4J\8S4J_metadata.json point structures/8S4J/8s4j_protein.pdb structures/8S4J/8s4j_pocket.pdb structures/8S4J/8s4j_ligand.sdf structures/8S4J/8s4j_ligand.pdb structures/8S4J/8s4j_ligand.cif structures/8S4J/8s4j_complex.pdb structures/8S4J/8s4j_complex.cif 8S4M classic CYP125A1 (Rv3545c) Mycobacterium tuberculosis N-terminally truncated CYP125A1 residues 18-433, pET21a construct with TEV-cleavable Twin-Strep/hexa-histidine tag; tag-free protein used for crystallography Na 5g "[""A1H47""]" 1 Kd Kd = = 3.8 ± 0.18 µM 3800.0 [] unit_conversion 5.42021640338319 success True direct_binding Optical titration; Table 1 binding value for compound 5g. 5 Table 1 reports compound 5g K_D = 3.8 ± 0.18 µM for CYP125. auto_single_measurement only accepted activity measurement [1] 1 structures\8S4M\8S4M_metadata.json point structures/8S4M/8s4m_protein.pdb structures/8S4M/8s4m_pocket.pdb structures/8S4M/8s4m_ligand.sdf structures/8S4M/8s4m_ligand.pdb structures/8S4M/8s4m_ligand.cif structures/8S4M/8s4m_complex.pdb structures/8S4M/8s4m_complex.cif 8S4V classic TNKS2 (tankyrase 2) human residues 952-1161 Na EXQ-1i (compound 52; R-diol) "[""A1H43""]" 1 pIC50 IC50 = = 7.06 ± 0.11 unitless 87.09635899560814 [] p_metric_transform 7.06 success True biochemical_inhibition Biochemical TNKS2 activity assay; Table 2 reports pIC50 ± SEM (n = 3). 6 Table 2 lists EXQ-1i (52), R = tBu, TNKS2 pIC50 = 7.06 ± 0.11 (n = 3), with PDB id 8S4V. auto_single_measurement only accepted activity measurement [1] 1 structures\8S4V\8S4V_metadata.json point structures/8S4V/8s4v_protein.pdb structures/8S4V/8s4v_pocket.pdb structures/8S4V/8s4v_ligand.sdf structures/8S4V/8s4v_ligand.pdb structures/8S4V/8s4v_ligand.cif structures/8S4V/8s4v_complex.pdb structures/8S4V/8s4v_complex.cif 8S4W classic TNKS2 (tankyrase 2) human residues 952-1161 Na EXQ-1g (compound 51; S-diol) "[""A1H44""]" 1 pIC50 IC50 = = 7.08 ± 0.07 unitless 83.17637711026708 [] p_metric_transform 7.08 success True biochemical_inhibition Biochemical TNKS2 activity assay; Table 2 reports pIC50 ± SEM (n = 3). 6 Table 2 lists EXQ-1g (51), R = tBu, TNKS2 pIC50 = 7.08 ± 0.07 (n = 3), with PDB id 8S4W. auto_single_measurement only accepted activity measurement [1] 1 structures\8S4W\8S4W_metadata.json point structures/8S4W/8s4w_protein.pdb structures/8S4W/8s4w_pocket.pdb structures/8S4W/8s4w_ligand.sdf structures/8S4W/8s4w_ligand.pdb structures/8S4W/8s4w_ligand.cif structures/8S4W/8s4w_complex.pdb structures/8S4W/8s4w_complex.cif 8S4X classic TNKS2 (tankyrase 2) human residues 952-1161 Na EXQ-2d (compound 40) "[""A1H42""]" 1 pIC50 IC50 = = 7.86 ± 0.03 unitless 13.803842646028839 [] p_metric_transform 7.86 success True biochemical_inhibition Biochemical TNKS2 activity assay; Table 2 reports pIC50 ± SEM (n = 3). 6 Table 2 lists EXQ-2d (40), R = tBu, TNKS2 pIC50 = 7.86 ± 0.03 (n = 3), with PDB id 8S4X. auto_single_measurement only accepted activity measurement [1] 1 structures\8S4X\8S4X_metadata.json point structures/8S4X/8s4x_protein.pdb structures/8S4X/8s4x_pocket.pdb structures/8S4X/8s4x_ligand.sdf structures/8S4X/8s4x_ligand.pdb structures/8S4X/8s4x_ligand.cif structures/8S4X/8s4x_complex.pdb structures/8S4X/8s4x_complex.cif 8S53 classic CYP142A1 (Rv3518c) Mycobacterium tuberculosis CYP142A1 residues 1-398 N-His6-tagged pET15b construct Na 1a "[""3QO""]" 1 Kd Kd = = 180 ± 6.6 µM 180000.0 [] unit_conversion 3.7447274948966935 success True direct_binding Optical titration of fragment 1a binding CYP142. 2 Figure 1D prints K_D = 180 ± 6.6 µM for fragment 1a binding CYP142. auto_single_measurement only accepted activity measurement [1] 1 structures\8S53\8S53_metadata.json point structures/8S53/8s53_protein.pdb structures/8S53/8s53_pocket.pdb structures/8S53/8s53_ligand.sdf structures/8S53/8s53_ligand.pdb structures/8S53/8s53_ligand.cif structures/8S53/8s53_complex.pdb structures/8S53/8s53_complex.cif 8S60 classic TNKS2 (tankyrase 2) human residues 952-1161 Na EXQ-2e (compound 41) "[""A1H5B""]" 1 pIC50 IC50 = = 7.27 ± 0.02 unitless 53.70317963702533 [] p_metric_transform 7.27 success True biochemical_inhibition Biochemical TNKS2 activity assay; Table 2 reports pIC50 ± SEM (n = 5). 6 Table 2 lists EXQ-2e (41), R = CF3, TNKS2 pIC50 = 7.27 ± 0.02 (n = 5), with PDB id 8S60. auto_single_measurement only accepted activity measurement [1] 1 structures\8S60\8S60_metadata.json point structures/8S60/8s60_protein.pdb structures/8S60/8s60_pocket.pdb structures/8S60/8s60_ligand.sdf structures/8S60/8s60_ligand.pdb structures/8S60/8s60_ligand.cif structures/8S60/8s60_complex.pdb structures/8S60/8s60_complex.cif 8S65 classic 1-deoxy-D-xylulose 5-phosphate reductoisomerase (TgDXR) Toxoplasma gondii His10-tagged truncated TgDXR, amino acids 182-632 Na fosmidomycin (compound 1) "[""FOM""]" 2 Ki Ki = = 0.31 µM 310.0 [] unit_conversion 6.508638306165727 success True biochemical_inhibition In vitro TgDXR enzymatic inhibition assay; Ki values were calculated from the inhibition data. 11 Table 1 reports Ki = 0.31 µM for compound 1 against TgDXR. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8S65\8S65_metadata.json point structures/8S65/8s65_protein.pdb structures/8S65/8s65_pocket.pdb structures/8S65/8s65_ligand.sdf structures/8S65/8s65_ligand.pdb structures/8S65/8s65_ligand.cif structures/8S65/8s65_complex.pdb structures/8S65/8s65_complex.cif 8S6U extended Pab1 Ustilago maydis MLLE domain of Pab1, residues 567-636, with an N-terminal hexahistidine tag (H-Pab1-M) Na PAM2 of Upa1 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 15 µM 15000.0 [] unit_conversion 4.823908740944319 success True direct_binding Isothermal titration calorimetry with purified H-Pab1-M (Pab1 residues 567–636) and PAM2-Upa1 peptide (residues 128–144). 6 The paper reports ITC using purified H-Pab1-M and states K_D = 15 µM for the PAM2^Upa1 peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\8S6U\8S6U_metadata.json point structures/8S6U/8s6u_protein.pdb structures/8S6U/8s6u_pocket.pdb structures/8S6U/8s6u_ligand.pdb structures/8S6U/8s6u_ligand.cif structures/8S6U/8s6u_complex.pdb structures/8S6U/8s6u_complex.cif 8S70 classic Pseudomonas aeruginosa RecA Pseudomonas aeruginosa Full-length RecA, residues 1-328 Na ATPgammaS (ATPgS) "[""AGS""]" 1 Kd Kd = = 1.95 ± 0.24 µM 1950.0 [] unit_conversion 5.709965388637482 success True direct_binding Fluorescence-polarization assay using 10 nM FAM-32mer ssDNA and 1 µM RecA while ATPγS concentration was varied. 9 Figure 4B visibly reports K_D^App = 1.95 ± 0.24 µM for ATPγS versus RecA_Pa/ssDNA; the methods identify this as the ATPγS affinity experiment. auto_single_measurement only accepted activity measurement [1] 1 structures\8S70\8S70_metadata.json point structures/8S70/8s70_protein.pdb structures/8S70/8s70_pocket.pdb structures/8S70/8s70_ligand.sdf structures/8S70/8s70_ligand.pdb structures/8S70/8s70_ligand.cif structures/8S70/8s70_complex.pdb structures/8S70/8s70_complex.cif 8S85 classic JAK1 human Na Na compound 10 "[""A1H5R""]" 1 IC50 IC50 = = 24 nM 24.0 [] unit_conversion 7.619788758288394 success True biochemical_inhibition JAK1 biochemical inhibition assay; Fig. 3 reports the hit-optimization result for compound 10. 3 Fig. 3 explicitly prints for compound 10: “JAK1 IC50 = 24 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8S85\8S85_metadata.json point structures/8S85/8s85_protein.pdb structures/8S85/8s85_pocket.pdb structures/8S85/8s85_ligand.sdf structures/8S85/8s85_ligand.pdb structures/8S85/8s85_ligand.cif structures/8S85/8s85_complex.pdb structures/8S85/8s85_complex.cif 8S96 classic RNase A Na Na Na adenosine 5'-heptaphosphate (p7A) "[""ZSF""]" 1 Ki Ki = = 2.6 ± 0.4 μM 2600.0 [] unit_conversion 5.585026652029182 success True biochemical_inhibition RNase A inhibition assay; Table 1 reports inhibition constants for 5'-nucleoside oligophosphates. 3 Table 1 lists p7A with Ki = 2.6 ± 0.4 μM (this work). auto_single_measurement only accepted activity measurement [1] 1 structures\8S96\8S96_metadata.json point structures/8S96/8s96_protein.pdb structures/8S96/8s96_pocket.pdb structures/8S96/8s96_ligand.sdf structures/8S96/8s96_ligand.pdb structures/8S96/8s96_ligand.cif structures/8S96/8s96_complex.pdb structures/8S96/8s96_complex.cif 8S98 classic TYK2 Na Na Na compound 8 "[""ZRU""]" 1 Kd Kd = = 0.039 nM 0.039 [] unit_conversion 10.4089353929735 success True direct_binding TYK2-JH2 binding assay; Table 2 experimental TYK2-JH2 Kd (footnote c: assay run n = 1). 4 Figure 5 identifies compound 8 bound to the TYK2 JH2 domain (PDB: 8S98); Table 2 prints its TYK2-JH2 Kd as 0.039 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8S98\8S98_metadata.json point structures/8S98/8s98_protein.pdb structures/8S98/8s98_pocket.pdb structures/8S98/8s98_ligand.sdf structures/8S98/8s98_ligand.pdb structures/8S98/8s98_ligand.cif structures/8S98/8s98_complex.pdb structures/8S98/8s98_complex.cif 8S99 classic TYK2 Na Na Na compound 11 "[""ZS3""]" 1 Kd Kd = = 0.068 nM 0.068 [] unit_conversion 10.167491087293763 success True direct_binding TYK2-JH2 binding assay; Table 3 experimental TYK2-JH2 Kd (footnote c: assay run n = 1). 5 Table 3 prints compound 11 TYK2-JH2 Kd as 0.068 nM; Figure 7 identifies compound 11 bound to TYK2 JH2 (PDB: 8S99). auto_single_measurement only accepted activity measurement [1] 1 structures\8S99\8S99_metadata.json point structures/8S99/8s99_protein.pdb structures/8S99/8s99_pocket.pdb structures/8S99/8s99_ligand.sdf structures/8S99/8s99_ligand.pdb structures/8S99/8s99_ligand.cif structures/8S99/8s99_complex.pdb structures/8S99/8s99_complex.cif 8S9A classic TYK2 Na Na Na TAK-279 (compound 30; formerly NDI-034858) "[""ZSB""]" 1 Kd Kd = = 0.0038 nM 0.0038 [] unit_conversion 11.42021640338319 success True direct_binding TYK2-JH2 binding assay; Table 5 experimental TYK2-JH2 Kd (footnote d: average of n ≥ 2 assay runs). 9 Table 5 prints compound 30 TYK2-JH2 Kd as 0.0038 nM. The paper identifies compound 30 as TAK-279 (formerly NDI-034858), and Figure 10 identifies its TYK2-JH2 structure as PDB 8S9A. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\8S9A\8S9A_metadata.json point structures/8S9A/8s9a_protein.pdb structures/8S9A/8s9a_pocket.pdb structures/8S9A/8s9a_ligand.sdf structures/8S9A/8s9a_ligand.pdb structures/8S9A/8s9a_ligand.cif structures/8S9A/8s9a_complex.pdb structures/8S9A/8s9a_complex.cif 8S9Q classic HIV-1 integrase catalytic core domain HIV-1 catalytic core domain (CCD); F185H solubilizing background F185H (solubilizing background; paper-defined WT CCD) PIR (PDB/internal code STP03-0404) "[""WBV""]" 1 Kd Kd = = 24.4 ± 2.8 nM 24.4 [] unit_conversion 7.61261017366127 success True direct_binding SPR direct binding of pirmitegravir (PIR) to the paper-defined WT HIV-1 integrase CCD background. 33 Figure 3 reports PIR binding to WT CCD with Kd 24.4 ± 2.8 nM; the corrected Data Availability mapping assigns PIR-WT CCD to 8S9Q. auto_single_measurement only accepted activity measurement [1] 1 structures\8S9Q\8S9Q_metadata.json point structures/8S9Q/8s9q_protein.pdb structures/8S9Q/8s9q_pocket.pdb structures/8S9Q/8s9q_ligand.sdf structures/8S9Q/8s9q_ligand.pdb structures/8S9Q/8s9q_ligand.cif structures/8S9Q/8s9q_complex.pdb structures/8S9Q/8s9q_complex.cif 8SC8 classic PI3KG Na S144-A1102 Na MTX-531 "[""D0D""]" 1 IC50 IC50 = = 8.3 nM 8.3 [] unit_conversion 8.080921907623926 success True biochemical_inhibition Purified PI3K-family biochemical kinase assay; Table 1. 3 Table 1 reports the MTX-531 IC50 against PI3Kγ as 8.3 nM; Figure 1 maps MTX-531-bound PI3Kγ to PDB 8SC8. auto_single_measurement only accepted activity measurement [1] 1 structures\8SC8\8SC8_metadata.json point structures/8SC8/8sc8_protein.pdb structures/8SC8/8sc8_pocket.pdb structures/8SC8/8sc8_ligand.sdf structures/8SC8/8sc8_ligand.pdb structures/8SC8/8sc8_ligand.cif structures/8SC8/8sc8_complex.pdb structures/8SC8/8sc8_complex.cif 8SC9 classic PPARG Na L232-Y505 Na MTX-531 "[""D0D""]" 1 IC50 IC50 = = 2.5 µM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding Time-resolved resonance energy transfer (TR-FRET) competitive binding assay for PPARγ. 9 The text reports that TR-FRET competitive binding assays showed MTX-531 to be a weak PPARγ agonist with IC50 = 2.5 µM; Figure 7 maps MTX-531-bound PPARγ to PDB 8SC9. auto_single_measurement only accepted activity measurement [1] 1 structures\8SC9\8SC9_metadata.json point structures/8SC9/8sc9_protein.pdb structures/8SC9/8sc9_pocket.pdb structures/8SC9/8sc9_ligand.sdf structures/8SC9/8sc9_ligand.pdb structures/8SC9/8sc9_ligand.cif structures/8SC9/8sc9_complex.pdb structures/8SC9/8sc9_complex.cif 8SD2 classic Influenza virus hemagglutinin (HA) Influenza A virus Na Na compound 4 "[""FIE""]" 1 IC50 IC50 = = 0.22 ± 0.01 µM 220.0 [] unit_conversion 6.657577319177793 success True biochemical_inhibition Biochemical fluorescence-polarization HA inhibition assay; manually resynthesized and purified compound. 3 Fig. 2A prints “Compound 4 IC50 = 0.22 ± 0.01 µM (Biochemical)”; its caption specifies a biochemical FP assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8SD2\8SD2_metadata.json point structures/8SD2/8sd2_protein.pdb structures/8SD2/8sd2_pocket.pdb structures/8SD2/8sd2_ligand.sdf structures/8SD2/8sd2_ligand.pdb structures/8SD2/8sd2_ligand.cif structures/8SD2/8sd2_complex.pdb structures/8SD2/8sd2_complex.cif 8SD4 classic Influenza virus hemagglutinin (HA) Influenza A virus Na Na compound 7 "[""ZW4""]" 1 Kd Kd = = 41 nM 41.0 [] unit_conversion 7.3872161432802645 success True direct_binding Surface plasmon resonance, steady-state affinity analysis against H1/PR8 HA. 6 Fig. 4C left panel prints “KD = 41 nM”; the caption identifies the left panel as H1/PR8 and states that affinity was measured by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\8SD4\8SD4_metadata.json point structures/8SD4/8sd4_protein.pdb structures/8SD4/8sd4_pocket.pdb structures/8SD4/8sd4_ligand.sdf structures/8SD4/8sd4_ligand.pdb structures/8SD4/8sd4_ligand.cif structures/8SD4/8sd4_complex.pdb structures/8SD4/8sd4_complex.cif 8SDM extended HTRA1 serine protease human HTRA1 protease domain, residues D161-K379 S328A CKP 3B3 "[""CHAIN:I"", ""CHAIN:X"", ""CHAIN:Y""]" 1 Kd Kd = = 34 nM 34.0 [] unit_conversion 7.468521082957745 success True direct_binding Surface plasmon resonance binding measurement for parent 3B3 to HTRA1PD(SA). 2 “The binding affinities measured by surface plasmon resonance (SPR) (KD range 0.7–7.0 nM and KD of 34 nM for the parent 3B3)…” auto_single_measurement only accepted activity measurement [1] 1 structures\8SDM\8SDM_metadata.json point structures/8SDM/8sdm_protein.pdb structures/8SDM/8sdm_pocket.pdb structures/8SDM/8sdm_ligand.pdb structures/8SDM/8sdm_ligand.cif structures/8SDM/8sdm_complex.pdb structures/8SDM/8sdm_complex.cif 8SDO extended ATAD2 Homo sapiens ATAD2 bromodomain-containing protein, residues 966-1112 Histone H4 S1C (Ser1Cys) H4S1CK5ac (residues 1-15) "[""CHAIN:B""]" 1 Kd Kd = = 12.9 ± 2.5 µM 12900.0 [] unit_conversion 4.889410289700751 success True direct_binding ITC measurement of ATAD2 BRD binding to H4S1CK5ac peptide. 32 Table 2 lists H4S1CK5ac (1-15): KD for ATAD2 = 12.9 ± 2.5 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8SDO\8SDO_metadata.json point structures/8SDO/8sdo_protein.pdb structures/8SDO/8sdo_pocket.pdb structures/8SDO/8sdo_ligand.pdb structures/8SDO/8sdo_ligand.cif structures/8SDO/8sdo_complex.pdb structures/8SDO/8sdo_complex.cif 8SDQ extended ATAD2 Homo sapiens ATAD2 bromodomain-containing protein, residues 966-1112 Na H4S1phK5ac (residues 1-15) "[""CHAIN:B""]" 1 Kd Kd = = 439.0 ± 22.0 µM 439000.0 [] unit_conversion 3.3575354797578782 success True direct_binding ITC measurement of ATAD2 BRD binding to H4S1phK5ac peptide. 31 Table 1 lists H4S1phK5ac (1-15): KD for ATAD2 = 439.0 ± 22.0 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8SDQ\8SDQ_metadata.json point structures/8SDQ/8sdq_protein.pdb structures/8SDQ/8sdq_pocket.pdb structures/8SDQ/8sdq_ligand.pdb structures/8SDQ/8sdq_ligand.cif structures/8SDQ/8sdq_complex.pdb structures/8SDQ/8sdq_complex.cif 8SDX extended ATAD2B Homo sapiens ATAD2B bromodomain-containing protein, residues 953-1085 Histone H4 S1C (Ser1Cys) H4S1CK5ac (residues 1-15) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 19.4 ± 2.9 µM 19400.0 [] unit_conversion 4.7121982700697735 success True direct_binding ITC measurement of ATAD2B BRD binding to H4S1CK5ac peptide. 32 Table 2 lists H4S1CK5ac (1-15): KD for ATAD2B = 19.4 ± 2.9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8SDX\8SDX_metadata.json point structures/8SDX/8sdx_protein.pdb structures/8SDX/8sdx_pocket.pdb structures/8SDX/8sdx_ligand.pdb structures/8SDX/8sdx_ligand.cif structures/8SDX/8sdx_complex.pdb structures/8SDX/8sdx_complex.cif 8SG2 extended Pin1; PKC betaII C-terminal tail Homo sapiens Full-length Pin1, residues 1-163, in complex with pV5betaII Na pV5betaII (phosphorylated PKC betaII C-terminal V5 peptide) "[""CHAIN:B""]" 1 Kd Kd = = 1.5 µM 1500.0 [] unit_conversion 5.823908740944319 success True direct_binding NMR lineshape analysis of the full-length Pin1–pV5βII interaction; the paper identifies this as the high-affinity bivalent complex. 8 “NMR lineshape analysis was applied to obtain the Kd value of 1.5 µM” for Pin1–pV5βII interactions; the same passage describes the bivalent interaction of both Pin1 domains with the PKC C-terminus. auto_single_measurement only accepted activity measurement [1] 1 structures\8SG2\8SG2_metadata.json point structures/8SG2/8sg2_protein.pdb structures/8SG2/8sg2_pocket.pdb structures/8SG2/8sg2_ligand.pdb structures/8SG2/8sg2_ligand.cif structures/8SG2/8sg2_complex.pdb structures/8SG2/8sg2_complex.cif 8SGH extended Karyopherin-beta2 (Kapbeta2) Na Karyopherin-beta2-HNRNPH2(103-225) complex Na HNRNPH2 PY-NLS "[""CHAIN:B""]" 1 Kd Kd = = 50 [24, 87] nM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding Isothermal titration calorimetry of Kapβ2 with MBP-HNRNPH2(103–225); the paper states this fragment binds Kapβ2 with Kd 50 nM. The deposited Kapβ2-HNRNPH2(103–225) cryo-EM structure is PDB 8SGH. 4 Table 1 reports Kapβ2 with MBP-HNRNPH2(103–225): K_D 50 [24, 87] nM. Page 3 states HNRNPH2(103–225) binds Kapβ2 tightly with a dissociation constant of 50 nM measured by ITC; page 13 maps Kapβ2-HNRNPH2(103–225) to PDB 8SGH. auto_single_measurement only accepted activity measurement [1] 1 structures\8SGH\8SGH_metadata.json point structures/8SGH/8sgh_protein.pdb structures/8SGH/8sgh_pocket.pdb structures/8SGH/8sgh_ligand.pdb structures/8SGH/8sgh_ligand.cif structures/8SGH/8sgh_complex.pdb structures/8SGH/8sgh_complex.cif 8SHC classic Pendrin (ssPendrin) Sus scrofa Na Na niflumic acid (NFA) "[""NFL""]" 1 IC50 IC50 = = 15.5 ± 1.5 µM 15500.0 [] unit_conversion 4.809668301829708 success True biochemical_inhibition Inhibition of ssPendrin-mediated bicarbonate transport in reconstituted proteoliposomes; 100 µM NFA abolished HCO3− transport and the concentration giving 50% inhibition was determined. 3 “NFA, at a concentration of 100 µM abolished the transport of HCO3− and I− … and we determined the concentration at which NFA inhibited ssPendrin-mediated HCO3− transport by 50% (IC50) to be 15.5 ± 1.5 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8SHC\8SHC_metadata.json point structures/8SHC/8shc_protein.pdb structures/8SHC/8shc_pocket.pdb structures/8SHC/8shc_ligand.sdf structures/8SHC/8shc_ligand.pdb structures/8SHC/8shc_ligand.cif structures/8SHC/8shc_complex.pdb structures/8SHC/8shc_complex.cif 8SHW extended 38B7 Fab human (IgE mAb); peptide source species not stated 38B7 antigen-binding fragment (Fab) bound to a hydroxylated DPYSPS peptide Na hydroxy-proline-containing DPYSPS peptide (38B7_PepOH) "[""CHAIN:B"", ""CHAIN:Q""]" 1 Kd Kd = = 2.00 × 10−8 M 20.0 [] unit_conversion 7.698970004336019 success True direct_binding CartERRA LSA surface-plasmon-resonance kinetic analysis of 38B7 binding to peptide epitopes; Table I reports mean KD for 38B7pep_OH. 8 Table I lists, for ligand 38B7pep_OH with 38B7, Mean KD (M) = 2.00 × 10−8. auto_single_measurement only accepted activity measurement [1] 1 structures\8SHW\8SHW_metadata.json point structures/8SHW/8shw_protein.pdb structures/8SHW/8shw_pocket.pdb structures/8SHW/8shw_ligand.pdb structures/8SHW/8shw_ligand.cif structures/8SHW/8shw_complex.pdb structures/8SHW/8shw_complex.cif 8SKN classic Dynamin-1-like protein (DRP1) human GTPase-BSE fusion Na compound 3 "[""6I9""]" 1 IC50 IC50 = = 0.050 µM 50.0 [] unit_conversion 7.301029995663981 success True biochemical_inhibition AlphaLISA DRP1:MiD49 PPI assay; data obtained in triplicates. 3 Table 2 reports DRP1:MiD49 IC50 = 0.050 µM for compound 3; the table footnote states that data were obtained from AlphaLISA in triplicates. The text identifies compound 3 as the DRP1–compound 3 cocrystal used to resolve the structure. auto_single_measurement only accepted activity measurement [1] 1 structures\8SKN\8SKN_metadata.json point structures/8SKN/8skn_protein.pdb structures/8SKN/8skn_pocket.pdb structures/8SKN/8skn_ligand.sdf structures/8SKN/8skn_ligand.pdb structures/8SKN/8skn_ligand.cif structures/8SKN/8skn_complex.pdb structures/8SKN/8skn_complex.cif 8SKO classic New Delhi metallo-beta-lactamase-4 (NDM-4) Klebsiella pneumonia pET-15B (+)-TEV-NDM-4, DeltaN1-42 M154L L-captopril; (2S)-1-(3-mercapto-2-methylpropionyl)-L-proline "[""X8Z""]" 1 Ki Ki = = 210 µM 210000.0 [] unit_conversion 3.6777807052660805 success True biochemical_inhibition Direct competition with nitrocefin; Table 2 NDM-4 result. 7 Table 2 reports L-captopril against NDM-4: Ki 210 µM. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\8SKO\8SKO_metadata.json point structures/8SKO/8sko_protein.pdb structures/8SKO/8sko_pocket.pdb structures/8SKO/8sko_ligand.sdf structures/8SKO/8sko_ligand.pdb structures/8SKO/8sko_ligand.cif structures/8SKO/8sko_complex.pdb structures/8SKO/8sko_complex.cif 8SKP classic New Delhi metallo-beta-lactamase-4 (NDM-4) Klebsiella pneumonia pET-15B (+)-TEV-NDM-4, DeltaN1-42 M154L Compound 1; 1-hydroxypyridine-2(1H)-thione-6-carboxylic acid "[""WAF""]" 1 Ki Ki = = 0.12 µM 120.0 [] unit_conversion 6.920818753952375 success True biochemical_inhibition Direct competition with nitrocefin; Table 2 NDM-4 result. 7 Table 2 reports Compound 1 against NDM-4: Ki 0.12 µM. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\8SKP\8SKP_metadata.json point structures/8SKP/8skp_protein.pdb structures/8SKP/8skp_pocket.pdb structures/8SKP/8skp_ligand.sdf structures/8SKP/8skp_ligand.pdb structures/8SKP/8skp_ligand.cif structures/8SKP/8skp_complex.pdb structures/8SKP/8skp_complex.cif 8SLO classic Plasmodium falciparum M1 aminopeptidase (PfA-M1) Plasmodium falciparum Na Na MIPS2673 "[""BYW""]" 1 Ki Ki = = 211 ± 11 nM 211.0 [] unit_conversion 6.675717544702307 success True biochemical_inhibition Inhibition constant against purified, recombinant PfA-M1; fluorescence aminopeptidase activity assay. 5 “The binding affinities (Ki) of MIPS2673 towards purified, recombinant PfA-M1 show the compound to be a potent inhibitor (Ki = 211 ± 11 nM).” Figure 1B identifies the PfA-M1-bound structure as MIPS2673; the Methods describe aminopeptidase inhibition assays. auto_single_measurement only accepted activity measurement [1] 1 structures\8SLO\8SLO_metadata.json point structures/8SLO/8slo_protein.pdb structures/8SLO/8slo_pocket.pdb structures/8SLO/8slo_ligand.sdf structures/8SLO/8slo_ligand.pdb structures/8SLO/8slo_ligand.cif structures/8SLO/8slo_complex.pdb structures/8SLO/8slo_complex.cif 8SM5 extended BHRF1 Epstein-Barr virus BHRF1 residues 2-156 in complex with BID residues 81-98 Na BID BH3D peptide (BID BH3 peptide) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 0.3 ± 0.1 μM 300.0 [] unit_conversion 6.522878745280337 success True direct_binding Isothermal titration calorimetry of BID BH3D binding to BHRF1 at 10 °C (Table 3). 6 Table 3, “Thermodynamics of Binding of the BID BH3D to BHRF1 and Bcl-XL,” reports for BHRF1: Kd 0.3 ± 0.1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8SM5\8SM5_metadata.json point structures/8SM5/8sm5_protein.pdb structures/8SM5/8sm5_pocket.pdb structures/8SM5/8sm5_ligand.pdb structures/8SM5/8sm5_ligand.cif structures/8SM5/8sm5_complex.pdb structures/8SM5/8sm5_complex.cif 8SPN classic macrophage migration inhibitory factor (MIF) human pET-11b plasmid encoding MIF Na T-614 (iguratimod) "[""7TN""]" 1 Ki Ki = = 16 μM 16000.0 [] unit_conversion 4.795880017344075 success True biochemical_inhibition MIF keto-enol tautomerase inhibition using 4-HPP substrate; kinetic analysis. 4 “T614 binds MIF as a non-competitive inhibitor with a Ki value of 16 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8SPN\8SPN_metadata.json point structures/8SPN/8spn_protein.pdb structures/8SPN/8spn_pocket.pdb structures/8SPN/8spn_ligand.sdf structures/8SPN/8spn_ligand.pdb structures/8SPN/8spn_ligand.cif structures/8SPN/8spn_complex.pdb structures/8SPN/8spn_complex.cif 8SRV extended O-acetyl-L-serine sulfhydrylase A (CysK) Staphylococcus aureus NCTC 8325 Na Na CymR 10 (EDLDGYMFYI) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 25 ± 5 nM 25.0 [] unit_conversion 7.6020599913279625 success True direct_binding Surface plasmon resonance, steady-state 1:1 binding analysis of CymR 10 to immobilized SaCysK. 5 The text reports CymR 10 binding affinity as 25 ± 5 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8SRV\8SRV_metadata.json point structures/8SRV/8srv_protein.pdb structures/8SRV/8srv_pocket.pdb structures/8SRV/8srv_ligand.pdb structures/8SRV/8srv_ligand.cif structures/8SRV/8srv_complex.pdb structures/8SRV/8srv_complex.cif 8SRW extended O-acetyl-L-serine sulfhydrylase A (CysK) Staphylococcus aureus NCTC 8325 Na Na CymR 5-8b (YM(Nal)YI) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 Kd Kd = = 18 ± 2 nM 18.0 [] unit_conversion 7.7447274948966935 success True direct_binding Surface plasmon resonance binding analysis of the modified CymR 5-8b peptide and SaCysK. 8 The text reports CymR 5-8b binding affinity of 18 ± 2 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8SRW\8SRW_metadata.json point structures/8SRW/8srw_protein.pdb structures/8SRW/8srw_pocket.pdb structures/8SRW/8srw_ligand.pdb structures/8SRW/8srw_ligand.cif structures/8SRW/8srw_complex.pdb structures/8SRW/8srw_complex.cif 8SSH classic MtrR Neisseria gonorrhoeae Na Na Ethinyl Estradiol "[""3WF""]" 1 Kd Kd = = 0.94 ± 0.6 µM 940.0 [] unit_conversion 6.026872146400301 success True direct_binding Isothermal titration calorimetry (ITC) of purified MtrR with ethinyl estradiol. 3 ITC studies found that ethinyl estradiol binds MtrR with a Kd of 0.94 ± 0.6 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8SSH\8SSH_metadata.json point structures/8SSH/8ssh_protein.pdb structures/8SSH/8ssh_pocket.pdb structures/8SSH/8ssh_ligand.sdf structures/8SSH/8ssh_ligand.pdb structures/8SSH/8ssh_ligand.cif structures/8SSH/8ssh_complex.pdb structures/8SSH/8ssh_complex.cif 8SSN classic Abl kinase (Abl) Na Abl64-510, TEV-cleavable, N-terminal MBP-His6-tagged Na SKI; asciminib "[""SKI""]" 1 Kd Kd = = 1.34 ± 0.72 nM 1.34 [] unit_conversion 8.872895201635192 success True direct_binding FRET measurement of SKI binding to Abl64-510 prebound with asciminib; the Fig. 3D panel is labeled “Abl64-510-asciminib + SKI.” 5 Fig. 3D prints Kd = 1.34 ± 0.72 nM for “Abl64-510-asciminib + SKI.” auto_single_measurement only accepted activity measurement [1] 1 structures\8SSN\8SSN_metadata.json point structures/8SSN/8ssn_protein.pdb structures/8SSN/8ssn_pocket.pdb structures/8SSN/8ssn_ligand.sdf structures/8SSN/8ssn_ligand.pdb structures/8SSN/8ssn_ligand.cif structures/8SSN/8ssn_complex.pdb structures/8SSN/8ssn_complex.cif 8SSV classic Grp94 canine Grp94NDelta41, residues 69-337 with charged linker residues 287-327 replaced by 4 glycines Charged linker residues 287-327 replaced with 4 glycines (Grp94NDelta41) PU-H71 "[""H71""]" 1 Kd Kd = = 0.049 ± 0.004 µM 49.0 [] unit_conversion 7.309803919971486 success True direct_binding ITC titration of Grp94NΔ41 with PU-H71. 33 Table 1 reports Grp94NΔ41–PU-H71 Kd of 0.049 ± 0.004 µM; Table 2 maps Grp94N:PU-H71 to PDB 8SSV. auto_single_measurement only accepted activity measurement [1] 1 structures\8SSV\8SSV_metadata.json point structures/8SSV/8ssv_protein.pdb structures/8SSV/8ssv_pocket.pdb structures/8SSV/8ssv_ligand.sdf structures/8SSV/8ssv_ligand.pdb structures/8SSV/8ssv_ligand.cif structures/8SSV/8ssv_complex.pdb structures/8SSV/8ssv_complex.cif 8STS classic HIV-1 reverse transcriptase HIV-1 V106A/Y181C RT52A Y181C; V106A JLJ636; Compound 2b "[""7N1""]" 1 IC50 IC50 = = 100 ± 20 nM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition PicoGreen-based biochemical RT inhibition assay using recombinant V106A/Y181C RT52A; values reported from three replicates. 3 Figure 2b reports Compound 2b IC50 = 100 ± 20 nM against Y181C,V106A (N119); the Figure 2 caption defines IC50 as concentration required to inhibit half of enzyme activity. The biochemical assay is described as using recombinant double-mutant protein. auto_single_measurement only accepted activity measurement [1] 1 structures\8STS\8STS_metadata.json point structures/8STS/8sts_protein.pdb structures/8STS/8sts_pocket.pdb structures/8STS/8sts_ligand.sdf structures/8STS/8sts_ligand.pdb structures/8STS/8sts_ligand.cif structures/8STS/8sts_complex.pdb structures/8STS/8sts_complex.cif 8STT classic HIV-1 reverse transcriptase HIV-1 V106A/Y181C RT52A Y181C; V106A JLJ555; Compound 1a "[""29T""]" 1 IC50 IC50 = = 900 ± 150 nM 900.0 [] unit_conversion 6.045757490560675 success True biochemical_inhibition PicoGreen-based biochemical RT inhibition assay using recombinant V106A/Y181C RT52A; values reported from three replicates. 3 Figure 2b reports Compound 1a IC50 = 900 ± 150 nM against Y181C,V106A (N119); the Figure 2 caption defines IC50 as concentration required to inhibit half of enzyme activity. The biochemical assay is described as using recombinant double-mutant protein. auto_single_measurement only accepted activity measurement [1] 1 structures\8STT\8STT_metadata.json point structures/8STT/8stt_protein.pdb structures/8STT/8stt_pocket.pdb structures/8STT/8stt_ligand.sdf structures/8STT/8stt_ligand.pdb structures/8STT/8stt_ligand.cif structures/8STT/8stt_complex.pdb structures/8STT/8stt_complex.cif 8STU classic HIV-1 reverse transcriptase HIV-1 V106A/Y181C RT52A Y181C; V106A JLJ578; Compound 1b "[""H9Y""]" 1 IC50 IC50 = = 370 ± 50 nM 370.0 [] unit_conversion 6.431798275933005 success True biochemical_inhibition PicoGreen-based biochemical RT inhibition assay using recombinant V106A/Y181C RT52A; values reported from three replicates. 3 Figure 2b reports Compound 1b IC50 = 370 ± 50 nM against Y181C,V106A (N119); the Figure 2 caption defines IC50 as concentration required to inhibit half of enzyme activity. The biochemical assay is described as using recombinant double-mutant protein. auto_single_measurement only accepted activity measurement [1] 1 structures\8STU\8STU_metadata.json point structures/8STU/8stu_protein.pdb structures/8STU/8stu_pocket.pdb structures/8STU/8stu_ligand.sdf structures/8STU/8stu_ligand.pdb structures/8STU/8stu_ligand.cif structures/8STU/8stu_complex.pdb structures/8STU/8stu_complex.cif 8STV classic HIV-1 reverse transcriptase HIV-1 V106A/Y181C RT52A Y181C; V106A JLJ600; Compound 2a "[""3LQ""]" 1 IC50 IC50 = = 100 ± 30 nM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition PicoGreen-based biochemical RT inhibition assay using recombinant V106A/Y181C RT52A; values reported from three replicates. 3 Figure 2b reports Compound 2a IC50 = 100 ± 30 nM against Y181C,V106A (N119); the Figure 2 caption defines IC50 as concentration required to inhibit half of enzyme activity. The biochemical assay is described as using recombinant double-mutant protein. auto_single_measurement only accepted activity measurement [1] 1 structures\8STV\8STV_metadata.json point structures/8STV/8stv_protein.pdb structures/8STV/8stv_pocket.pdb structures/8STV/8stv_ligand.sdf structures/8STV/8stv_ligand.pdb structures/8STV/8stv_ligand.cif structures/8STV/8stv_complex.pdb structures/8STV/8stv_complex.cif 8SV0 extended Importin alpha 2 (IMPalpha2) mouse IMPalpha2DeltaIBB, residues 72-498 Na PsSiAdV pVII-NLS, residues 120-128, sequence PGGFKRRRL "[""CHAIN:C"", ""CHAIN:E""]" 1 Kd Kd = = 277.8 nM 277.8 [] unit_conversion 6.556267758598404 success True direct_binding Fluorescence polarization assay of FITC-tagged PsSiAdV pVII-NLS with serially diluted IMPs; direct binary peptide–IMPα2ΔIBB binding, performed in triplicate. 6 Figure 2 reports IMPα2 Kd 277.8 nM for PsSiAdV pVII-NLS; the methods specify fluorescence-polarization measurement of Kd, and the structure text identifies the IMPα2ΔIBB–pVII-NLS complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8SV0\8SV0_metadata.json point structures/8SV0/8sv0_protein.pdb structures/8SV0/8sv0_pocket.pdb structures/8SV0/8sv0_ligand.pdb structures/8SV0/8sv0_ligand.cif structures/8SV0/8sv0_complex.pdb structures/8SV0/8sv0_complex.cif 8SW6 extended Protein phosphatase 1 alpha catalytic subunit (PP1alpha) Na PP1alpha residues 7-330 in complex with PhosTAP_PP1_v3 (PhosTAP_PP1) PhosTAP peptide: PNUTS RVxF KTVTW to KNVHW; Thr five residues after the PhiPhi xF motif changed to Ala; CSRN P1 linker shortened PhosTAP_PP1_v3 (PP1-specific phosphatase targeting peptide, PhosTAP, version 3) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 4.0 ± 0.6 nM 4.0 [] unit_conversion 8.397940008672037 success True direct_binding Purified-protein ITC, 25 °C; Table 1, n=4. 4 Table 1 reports PhosTAP_PP1:PP1α7-330 with K_D 4.0 ± 0.6 nM. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\8SW6\8SW6_metadata.json point structures/8SW6/8sw6_protein.pdb structures/8SW6/8sw6_pocket.pdb structures/8SW6/8sw6_ligand.pdb structures/8SW6/8sw6_ligand.cif structures/8SW6/8sw6_complex.pdb structures/8SW6/8sw6_complex.cif 8SWQ classic purine nucleoside phosphorylase (PNP) Kluyveromyces lactis Na Na DADMe-IMMUCILLIN H (DIH) "[""DIH""]" 1 Ki Ki = = 155 pM 0.155 [] unit_conversion 9.809668301829708 success True biochemical_inhibition Steady-state kinetic inhibition assay. 4 DADMe-ImmH shows the strongest inhibition of K. lactis PNP (Ki = 155 pM). auto_single_measurement only accepted activity measurement [1] 1 structures\8SWQ\8SWQ_metadata.json point structures/8SWQ/8swq_protein.pdb structures/8SWQ/8swq_pocket.pdb structures/8SWQ/8swq_ligand.sdf structures/8SWQ/8swq_ligand.pdb structures/8SWQ/8swq_ligand.cif structures/8SWQ/8swq_complex.pdb structures/8SWQ/8swq_complex.cif 8SWS classic purine nucleoside phosphorylase (PNP) Kluyveromyces lactis Na S42E-H98R DADMe-IMMUCILLIN G (DIG) "[""IM5""]" 1 Kd Kd = = 3.7 ± 0.2 μM 3700.0 [] unit_conversion 5.431798275933005 success True direct_binding ITC, single-isotherm binding. 7 The S42E-H98R double variant changed to a single isotherm binding of 3.7 ± 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8SWS\8SWS_metadata.json point structures/8SWS/8sws_protein.pdb structures/8SWS/8sws_pocket.pdb structures/8SWS/8sws_ligand.sdf structures/8SWS/8sws_ligand.pdb structures/8SWS/8sws_ligand.cif structures/8SWS/8sws_complex.pdb structures/8SWS/8sws_complex.cif 8SX4 classic eIF4E Na eIF4E residues 27-217 Na Compound 7n "[""WXL""]" 1 IC50 IC50 = = 5.6 ± 0.2 μM 5600.0 [] unit_conversion 5.251811972993799 success True biochemical_inhibition Fluorescence-polarization competitive inhibition assay using fluorescein-labeled m7GTP and purified eIF4E. 4 Table 1 reports compound 7n IC50 = 5.6 ± 0.2 μM; the accompanying text states that unprotected phosphonic acids 7a–7n were tested for competitive inhibition of eIF4E by FP with fluorescein-labeled m7GTP. Figure 5 and the accession entry identify 7n-bound eIF4E as PDB 8SX4. auto_single_measurement only accepted activity measurement [1] 1 structures\8SX4\8SX4_metadata.json point structures/8SX4/8sx4_protein.pdb structures/8SX4/8sx4_pocket.pdb structures/8SX4/8sx4_ligand.sdf structures/8SX4/8sx4_ligand.pdb structures/8SX4/8sx4_ligand.cif structures/8SX4/8sx4_complex.pdb structures/8SX4/8sx4_complex.cif 8SXR classic SARS-CoV-2 Mpro SARS-CoV-2 Na Na C5a "[""WZK""]" 2 Kd Kd = = 0.17 ± 0.1 µM 170.0 [] unit_conversion 6.769551078621726 success True direct_binding Microscale thermophoresis inhibitory Kd measurement. 9 Figure 2 panel J reports Kd = 0.17 ± 0.1 µM for C5a. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8SXR\8SXR_metadata.json point structures/8SXR/8sxr_protein.pdb structures/8SXR/8sxr_pocket.pdb structures/8SXR/8sxr_ligand.sdf structures/8SXR/8sxr_ligand.pdb structures/8SXR/8sxr_ligand.cif structures/8SXR/8sxr_complex.pdb structures/8SXR/8sxr_complex.cif 8SY5 classic E. coli RNA polymerase Escherichia coli Na Na dS; BTP "[""X0F""]" 1 Kd Kd = = 5.7 ± 0.9 µM 5700.0 [] unit_conversion 5.2441251443275085 success True direct_binding Single-turnover nucleotide-incorporation kinetic assay; printed as apparent dissociation constant (Kd,app) for dS:BTP. 3 Table 1 reports dS:BTP Kd,app = 5.7 ± 0.9 µM; the text defines Kd,app as the apparent equilibrium constant for dissociation of NTPs from the RNAP elongation complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8SY5\8SY5_metadata.json point structures/8SY5/8sy5_protein.pdb structures/8SY5/8sy5_pocket.pdb structures/8SY5/8sy5_ligand.sdf structures/8SY5/8sy5_ligand.pdb structures/8SY5/8sy5_ligand.cif structures/8SY5/8sy5_complex.pdb structures/8SY5/8sy5_complex.cif 8SY6 classic E. coli RNA polymerase Escherichia coli Na Na dB; UTP "[""UTP""]" 1 Kd Kd = = 12 ± 1 µM 12000.0 [] unit_conversion 4.920818753952375 success True direct_binding Single-turnover nucleotide-incorporation kinetic assay; printed as apparent dissociation constant (Kd,app) for dB:UTP. 3 Table 1 reports dB:UTP Kd,app = 12 ± 1 µM; the text defines Kd,app as the apparent equilibrium constant for dissociation of NTPs from the RNAP elongation complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8SY6\8SY6_metadata.json point structures/8SY6/8sy6_protein.pdb structures/8SY6/8sy6_pocket.pdb structures/8SY6/8sy6_ligand.sdf structures/8SY6/8sy6_ligand.pdb structures/8SY6/8sy6_ligand.cif structures/8SY6/8sy6_complex.pdb structures/8SY6/8sy6_complex.cif 8SY7 classic E. coli RNA polymerase Escherichia coli Na Na dB; STP "[""X0O""]" 1 Kd Kd = = 15 ± 2 µM 15000.0 [] unit_conversion 4.823908740944319 success True direct_binding Single-turnover nucleotide-incorporation kinetic assay; printed as apparent dissociation constant (Kd,app) for dB:STP. 3 Table 1 reports dB:STP Kd,app = 15 ± 2 µM; the text defines Kd,app as the apparent equilibrium constant for dissociation of NTPs from the RNAP elongation complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8SY7\8SY7_metadata.json point structures/8SY7/8sy7_protein.pdb structures/8SY7/8sy7_pocket.pdb structures/8SY7/8sy7_ligand.sdf structures/8SY7/8sy7_ligand.pdb structures/8SY7/8sy7_ligand.cif structures/8SY7/8sy7_complex.pdb structures/8SY7/8sy7_complex.cif 8SZ3 classic human beta 1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) human Na Na compound 7j "[""X18""]" 1 IC50 IC50 = = 0.10 (±0.06) μM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition In vitro enzymatic potency (Table 2). 3 Table 2 prints B3GNT2 IC50 = 0.10 (±0.06) μM for compound 7j; Figure 3 identifies the 7j B3GNT2 cocrystal as PDB 8SZ3. auto_single_measurement only accepted activity measurement [1] 1 structures\8SZ3\8SZ3_metadata.json point structures/8SZ3/8sz3_protein.pdb structures/8SZ3/8sz3_pocket.pdb structures/8SZ3/8sz3_ligand.sdf structures/8SZ3/8sz3_ligand.pdb structures/8SZ3/8sz3_ligand.cif structures/8SZ3/8sz3_complex.pdb structures/8SZ3/8sz3_complex.cif 8SZM classic Escherichia coli ClpP protease Escherichia coli Recombinant ClpP expressed from modified pETSUMO with a removable N-terminal 2x(His6)-SUMO tag; purified untagged Na ACP6-12 "[""X3O""]" 1 Kd Kd = = 0.27 ± 0.04 μM 270.0 [] unit_conversion 6.568636235841012 success True direct_binding Apparent dissociation constant (Kd,app) determined by titrating ACP6-12 at different EcClpP concentrations and linearly fitting EC50 values. 7 Figure 5 reports Kd,app = 0.27 ± 0.04 μM for ACP6-12 binding to EcClpP. auto_single_measurement only accepted activity measurement [1] 1 structures\8SZM\8SZM_metadata.json point structures/8SZM/8szm_protein.pdb structures/8SZM/8szm_pocket.pdb structures/8SZM/8szm_ligand.sdf structures/8SZM/8szm_ligand.pdb structures/8SZM/8szm_ligand.cif structures/8SZM/8szm_complex.pdb structures/8SZM/8szm_complex.cif 8SZN classic Neisseria meningitidis ClpP protease Neisseria meningitidis Recombinant ClpP expressed from modified pETSUMO with a removable N-terminal 2x(His6)-SUMO tag; purified untagged Na ACP6-12 "[""X3O""]" 1 Kd Kd = = 0.69 ± 0.09 μM 690.0 [] unit_conversion 6.161150909262744 success True direct_binding Apparent dissociation constant (Kd,app) determined by titrating ACP6-12 at different NmClpP concentrations and linearly fitting EC50 values. 7 Figure 5 reports Kd,app = 0.69 ± 0.09 μM for ACP6-12 binding to NmClpP. auto_single_measurement only accepted activity measurement [1] 1 structures\8SZN\8SZN_metadata.json point structures/8SZN/8szn_protein.pdb structures/8SZN/8szn_pocket.pdb structures/8SZN/8szn_ligand.sdf structures/8SZN/8szn_ligand.pdb structures/8SZN/8szn_ligand.cif structures/8SZN/8szn_complex.pdb structures/8SZN/8szn_complex.cif 8T0P extended Cse4, Ame1, Okp1 Saccharomyces cerevisiae (budding yeast) Okp1 residues 125-275 and Ame1 residues 124-231 heterodimer bound to Cse4 residues 28-60 peptide Na Na "[""CHAIN:C""]" 1 Kd Kd ~ ~ 750 nM 750.0 [] unit_conversion 6.1249387366083 success True direct_binding Fluorescence-polarization measurement of Cse4 affinity for the truncated crystallographic Okp1-Ame1 complex. 3 The paper states that the dissociation constant for Cse4 binding to the truncated Okp1-Ame1 complex used for crystallography was ~750 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8T0P\8T0P_metadata.json point structures/8T0P/8t0p_protein.pdb structures/8T0P/8t0p_pocket.pdb structures/8T0P/8t0p_ligand.pdb structures/8T0P/8t0p_ligand.cif structures/8T0P/8t0p_complex.pdb structures/8T0P/8t0p_complex.cif 8T2C extended O-acetyl-L-serine sulfhydrylase A (CysK) Staphylococcus aureus NCTC 8325 Na Na CymR 5 (YMFYI) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 34 ± 7 nM 34.0 [] unit_conversion 7.468521082957745 success True direct_binding Surface plasmon resonance binding analysis of the CymR 5 pentapeptide and SaCysK. 7 SPR determined a binding affinity of 34 ± 7 nM for CymR 5. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8T2C\8T2C_metadata.json point structures/8T2C/8t2c_protein.pdb structures/8T2C/8t2c_pocket.pdb structures/8T2C/8t2c_ligand.pdb structures/8T2C/8t2c_ligand.cif structures/8T2C/8t2c_complex.pdb structures/8T2C/8t2c_complex.cif 8T2H classic DYRK1A Na Na Na DYR530 "[""XIR""]" 1 Kd Kd = = 0.91 nM 0.91 [] unit_conversion 9.040958607678906 success True direct_binding Active-site-directed competition binding assay; Figure 1B reports the DYRK1A affinity for DYR530. 2 Figure 1B visibly prints “DYR530 DYRK1A Kd: 0.91 nM”. auto_single_measurement only accepted activity measurement [1] 1 structures\8T2H\8T2H_metadata.json point structures/8T2H/8t2h_protein.pdb structures/8T2H/8t2h_pocket.pdb structures/8T2H/8t2h_ligand.sdf structures/8T2H/8t2h_ligand.pdb structures/8T2H/8t2h_ligand.cif structures/8T2H/8t2h_complex.pdb structures/8T2H/8t2h_complex.cif 8T2N extended GABARAP human (GABARAP); Rift Valley fever virus (NSs3 ligand) Human GABARAP residues 1-117 in complex with an NSs3 peptide containing RVFV NSs residues 234-255 Na NSs3 LIR peptide (WIPV core, residues 238-241; NSs3 residues 234-255) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 16000 ± 3.0 nM 16000.0 [] unit_conversion 4.795880017344075 success True direct_binding ITC with purified NSs3 peptide and GABARAP. 6 Table 2 reports NSs3 binding to GABARAP at 16000 ± 3.0 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8T2N\8T2N_metadata.json point structures/8T2N/8t2n_protein.pdb structures/8T2N/8t2n_pocket.pdb structures/8T2N/8t2n_ligand.pdb structures/8T2N/8t2n_ligand.cif structures/8T2N/8t2n_complex.pdb structures/8T2N/8t2n_complex.cif 8T32 extended GABARAP human GABARAP residues 1-117, acetylated at K48, complexed with TP53INP2LIR peptide residues 31-43 K48 acetylation TP53INP2/DOR LIR peptide (residues 31-43) "[""CHAIN:B""]" 1 Kd Kd = = 0.23 ± 0.08 µM 230.0 [] unit_conversion 6.638272163982407 success True direct_binding ITC, 20 mM phosphate pH 6.5, 150 mM NaCl; purified GABARAP[K48Ac] and TP53INP2LIR peptide. 4 Table 1 reports GABARAP[K48Ac] K_D = 0.23 ± 0.08 µM for TP53INP2LIR. auto_single_measurement only accepted activity measurement [1] 1 structures\8T32\8T32_metadata.json point structures/8T32/8t32_protein.pdb structures/8T32/8t32_pocket.pdb structures/8T32/8t32_ligand.pdb structures/8T32/8t32_ligand.cif structures/8T32/8t32_complex.pdb structures/8T32/8t32_complex.cif 8T33 extended GABARAP human GABARAP residues 1-117, acetylated at K46, complexed with TP53INP2LIR peptide residues 31-43 K46 acetylation TP53INP2/DOR LIR peptide (residues 31-43) "[""CHAIN:B""]" 1 Kd Kd = = 0.047 ± 0.003 µM 47.0 [] unit_conversion 7.327902142064282 success True direct_binding ITC, 20 mM phosphate pH 6.5, 150 mM NaCl; purified GABARAP[K46Ac] and TP53INP2LIR peptide. 4 Table 1 reports GABARAP[K46Ac] K_D = 0.047 ± 0.003 µM for TP53INP2LIR. auto_single_measurement only accepted activity measurement [1] 1 structures\8T33\8T33_metadata.json point structures/8T33/8t33_protein.pdb structures/8T33/8t33_pocket.pdb structures/8T33/8t33_ligand.pdb structures/8T33/8t33_ligand.cif structures/8T33/8t33_complex.pdb structures/8T33/8t33_complex.cif 8T4R extended RAG2 PHD finger Na Na Na H3K4tBuNle peptide "[""CHAIN:D""]" 1 Kd Kd = = 57 ± 6 μM 57000.0 [] unit_conversion 4.2441251443275085 success True direct_binding ITC at 25 °C, pH 7.4, 50 mM sodium phosphate, 150 mM NaCl, and 2 mM TCEP. 16 Table 1 reports RAG2 PHD binding to H3K4tBuNle with K_D = 57 ± 6 μM; the table states affinities were determined by ITC. Figure 3 identifies the RAG2 PHD–H3K4tBuNle structure as PDB 8T4R. auto_single_measurement only accepted activity measurement [1] 1 structures\8T4R\8T4R_metadata.json point structures/8T4R/8t4r_protein.pdb structures/8T4R/8t4r_pocket.pdb structures/8T4R/8t4r_ligand.pdb structures/8T4R/8t4r_ligand.cif structures/8T4R/8t4r_complex.pdb structures/8T4R/8t4r_complex.cif 8T5A classic HIV-1 integrase catalytic core domain HIV-1 catalytic core domain (CCD); F185H solubilizing background F185H; Y99H; A128T PIR (PDB/internal code STP03-0404) "[""WBV""]" 1 Kd Kd = = 77 ± 5.5 nM 77.0 [] unit_conversion 7.113509274827518 success True direct_binding SPR direct binding of pirmitegravir (PIR) to HIV-1 integrase CCD Y99H/A128T on the F185H solubilizing background. 33 Figure 3 reports PIR binding to CCD Y99H/A128T with Kd 77 ± 5.5 nM; the corrected Data Availability mapping assigns this complex to 8T5A. auto_single_measurement only accepted activity measurement [1] 1 structures\8T5A\8T5A_metadata.json point structures/8T5A/8t5a_protein.pdb structures/8T5A/8t5a_pocket.pdb structures/8T5A/8t5a_ligand.sdf structures/8T5A/8t5a_ligand.pdb structures/8T5A/8t5a_ligand.cif structures/8T5A/8t5a_complex.pdb structures/8T5A/8t5a_complex.cif 8T5E extended Bim binder Na Na Na Bim BH3 peptide "[""CHAIN:B""]" 1 Kd Kd < < 500 pM 0.5 [] unit_conversion 9.301029995663981 success True direct_binding Fluorescence-polarization measurements (n=4) of the de novo RFdiffusion Bim binder. 6 Fig. 3c labels the Bim result “Kd < 500 pM”; its caption states that FP measurements (n=4) indicate a subnanomolar binding affinity. auto_single_measurement only accepted activity measurement [1] 1 structures\8T5E\8T5E_metadata.json point structures/8T5E/8t5e_protein.pdb structures/8T5E/8t5e_pocket.pdb structures/8T5E/8t5e_ligand.pdb structures/8T5E/8t5e_ligand.cif structures/8T5E/8t5e_complex.pdb structures/8T5E/8t5e_complex.cif 8T5G classic SOS2 Na SOS2SB Na compound 12 "[""THA""]" 1 Kd Kd = = 550 µM 550000.0 [] unit_conversion 3.259637310505756 success True direct_binding SPR; SOS2 SPR K_D reported in Table 1. 4 Table 1 reports compound 12: SOS2 SPR K_D 550 µM; PDB code 8T5G. auto_single_measurement only accepted activity measurement [1] 1 structures\8T5G\8T5G_metadata.json point structures/8T5G/8t5g_protein.pdb structures/8T5G/8t5g_pocket.pdb structures/8T5G/8t5g_ligand.sdf structures/8T5G/8t5g_ligand.pdb structures/8T5G/8t5g_ligand.cif structures/8T5G/8t5g_complex.pdb structures/8T5G/8t5g_complex.cif 8T5R classic SOS2 Na SOS2SB Na compound 13 "[""6LH""]" 1 Kd Kd ~ ~ 2,000 µM 2000000.0 [] unit_conversion 2.6989700043360187 success True direct_binding SPR; SOS2 SPR K_D reported in Table 1. 4 Table 1 reports compound 13: SOS2 SPR K_D ~2,000 µM; PDB code 8T5R. auto_single_measurement only accepted activity measurement [1] 1 structures\8T5R\8T5R_metadata.json point structures/8T5R/8t5r_protein.pdb structures/8T5R/8t5r_pocket.pdb structures/8T5R/8t5r_ligand.sdf structures/8T5R/8t5r_ligand.pdb structures/8T5R/8t5r_ligand.cif structures/8T5R/8t5r_complex.pdb structures/8T5R/8t5r_complex.cif 8T5W classic Influenza PA-N endonuclease Na Na I38T Baloxavir (BXA) "[""E4Z""]" 1 Kd Kd = = 9.3 ± 4.2 μM 9300.0 [] unit_conversion 5.031517051446064 success True direct_binding Spectral-shift (SpS) binding assay; Table 1. 4 Table 1 reports BXA Kd = 9.3 ± 4.2 μM for I38T PA_N. auto_single_measurement only accepted activity measurement [1] 1 structures\8T5W\8T5W_metadata.json point structures/8T5W/8t5w_protein.pdb structures/8T5W/8t5w_pocket.pdb structures/8T5W/8t5w_ligand.sdf structures/8T5W/8t5w_ligand.pdb structures/8T5W/8t5w_ligand.cif structures/8T5W/8t5w_complex.pdb structures/8T5W/8t5w_complex.cif 8T6D extended SHP2 Na Na Na GDC-1971 (RLY-1971; compound 1) "[""YR2""]" 2 IC50 IC50 = = 0.17 µM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition Biochemical SHP2 dephosphorylation assay. 3 Table 1 reports E76K SHP2 IC50 0.17 µM for 1 (GDC-1971/RLY-1971). auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\8T6D\8T6D_metadata.json point structures/8T6D/8t6d_protein.pdb structures/8T6D/8t6d_pocket.pdb structures/8T6D/8t6d_ligand.pdb structures/8T6D/8t6d_ligand.cif structures/8T6D/8t6d_complex.pdb structures/8T6D/8t6d_complex.cif 8T6F classic human myeloid cell leukemia 1 (MCL1) human MBP-MCL1 fusion; MCL1 residues 173-321 Na BRD-810 inhibitor (BRD810 in PDB title) "[""YI7""]" 1 Kd Kd = = 0.3 nM 0.3 [] unit_conversion 9.522878745280337 success True direct_binding SPR binding assay using MCL1 protein (residues 173–321). 3 Table 1 reports SPR (nM, Kd) for BRD-810 as 0.3 nM; the text identifies BRD-810 as binding the MCL1 BH3 groove, and the paper maps the BRD-810–MBP–MCL1 structure to PDB 8T6F. auto_single_measurement only accepted activity measurement [1] 1 structures\8T6F\8T6F_metadata.json point structures/8T6F/8t6f_protein.pdb structures/8T6F/8t6f_pocket.pdb structures/8T6F/8t6f_ligand.sdf structures/8T6F/8t6f_ligand.pdb structures/8T6F/8t6f_ligand.cif structures/8T6F/8t6f_complex.pdb structures/8T6F/8t6f_complex.cif 8T6Z classic Influenza PA-N endonuclease Na Na I38T compound 23; 6-(4-(1H-tetrazol-5-yl)-2-(trifluoromethyl)phenyl)-3-hydroxy-4-oxo-1,4-dihydropyridine-2-carboxylic acid "[""IJM""]" 1 Kd Kd = = 384 ± 19.4 μM 384000.0 [] unit_conversion 3.4156687756324695 success True direct_binding Spectral-shift (SpS) binding assay; Table 1. 4 Table 1 reports compound 23 Kd = 384 ± 19.4 μM for I38T PA_N. auto_single_measurement only accepted activity measurement [1] 1 structures\8T6Z\8T6Z_metadata.json point structures/8T6Z/8t6z_protein.pdb structures/8T6Z/8t6z_pocket.pdb structures/8T6Z/8t6z_ligand.sdf structures/8T6Z/8t6z_ligand.pdb structures/8T6Z/8t6z_ligand.cif structures/8T6Z/8t6z_complex.pdb structures/8T6Z/8t6z_complex.cif 8T7Q classic SHP2 Na Na Na Compound 4 "[""ZH5""]" 1 IC50 IC50 = = 0.038 µM 38.0 [] unit_conversion 7.42021640338319 success True biochemical_inhibition SHP2 biochemical assay; Table 3 compound 4 (X = CH, R = H). 7 Table 3 reports biochemical IC50 0.038 µM for compound 4; Figure 6 maps compound 4 to PDB 8T7Q. auto_single_measurement only accepted activity measurement [1] 1 structures\8T7Q\8T7Q_metadata.json point structures/8T7Q/8t7q_protein.pdb structures/8T7Q/8t7q_pocket.pdb structures/8T7Q/8t7q_ligand.sdf structures/8T7Q/8t7q_ligand.pdb structures/8T7Q/8t7q_ligand.cif structures/8T7Q/8t7q_complex.pdb structures/8T7Q/8t7q_complex.cif 8T81 classic Influenza PA-N endonuclease Na Na E23K compound 23; 6-(4-(1H-tetrazol-5-yl)-2-(trifluoromethyl)phenyl)-3-hydroxy-4-oxo-1,4-dihydropyridine-2-carboxylic acid "[""IJM""]" 1 Kd Kd = = 328 ± 26.6 μM 328000.0 [] unit_conversion 3.484126156288321 success True direct_binding Spectral-shift (SpS) binding assay; Table 1. 4 Table 1 reports compound 23 Kd = 328 ± 26.6 μM for E23K PA_N. auto_single_measurement only accepted activity measurement [1] 1 structures\8T81\8T81_metadata.json point structures/8T81/8t81_protein.pdb structures/8T81/8t81_pocket.pdb structures/8T81/8t81_ligand.sdf structures/8T81/8t81_ligand.pdb structures/8T81/8t81_ligand.cif structures/8T81/8t81_complex.pdb structures/8T81/8t81_complex.cif 8T8Q classic SHP2 Na Na Na Compound 3 "[""ZJX""]" 1 IC50 IC50 = = 0.12 µM 120.0 [] unit_conversion 6.920818753952375 success True biochemical_inhibition SHP2 biochemical assay; Table 3 compound 3 (X = F). 7 Table 3 reports biochemical IC50 0.12 µM for compound 3; Figure 6 maps compound 3 to PDB 8T8Q. auto_single_measurement only accepted activity measurement [1] 1 structures\8T8Q\8T8Q_metadata.json point structures/8T8Q/8t8q_protein.pdb structures/8T8Q/8t8q_pocket.pdb structures/8T8Q/8t8q_ligand.sdf structures/8T8Q/8t8q_ligand.pdb structures/8T8Q/8t8q_ligand.cif structures/8T8Q/8t8q_complex.pdb structures/8T8Q/8t8q_complex.cif 8T94 classic Influenza PA-N endonuclease Na Na WT (wild type) compound 23; 6-(4-(1H-tetrazol-5-yl)-2-(trifluoromethyl)phenyl)-3-hydroxy-4-oxo-1,4-dihydropyridine-2-carboxylic acid "[""IJM""]" 1 Kd Kd = = 277 ± 30.6 μM 277000.0 [] unit_conversion 3.557520230935552 success True direct_binding Spectral-shift (SpS) binding assay; Table 1. 4 Table 1 reports compound 23 Kd = 277 ± 30.6 μM for WT PA_N. auto_single_measurement only accepted activity measurement [1] 1 structures\8T94\8T94_metadata.json point structures/8T94/8t94_protein.pdb structures/8T94/8t94_pocket.pdb structures/8T94/8t94_ligand.sdf structures/8T94/8t94_ligand.pdb structures/8T94/8t94_ligand.cif structures/8T94/8t94_complex.pdb structures/8T94/8t94_complex.cif 8T9V classic Ricin toxin A subunit (RTA) Na RTA residues 1-267; expressed with an N-terminal deca-histidine/SUMO tag that was removed before complexation Na RU-NT-59 "[""ZJT""]" 1 Ki Ki = = 4 ± 0.3 µM 4000.0 [] unit_conversion 5.3979400086720375 success True direct_binding Fluorescence-polarization competition assay measuring displacement of BODIPY-TMR-X-labelled P11 from RTA. 6 Table 2 reports Ki = 4 ± 0.3 µM for RU-NT-59; footnote states Ki values were measured by fluorescence polarization. auto_metric_priority unique highest-priority metric family: Ki [1] 3 structures\8T9V\8T9V_metadata.json point structures/8T9V/8t9v_protein.pdb structures/8T9V/8t9v_pocket.pdb structures/8T9V/8t9v_ligand.sdf structures/8T9V/8t9v_ligand.pdb structures/8T9V/8t9v_ligand.cif structures/8T9V/8t9v_complex.pdb structures/8T9V/8t9v_complex.cif 8TAB classic Ricin toxin A subunit (RTA) Na RTA residues 1-267; expressed with an N-terminal deca-histidine/SUMO tag that was removed before complexation Na PD00589 "[""U4T""]" 1 Ki Ki = = 8 ± 0.3 µM 8000.0 [] unit_conversion 5.096910013008056 success True direct_binding Fluorescence-polarization competition assay measuring displacement of BODIPY-TMR-X-labelled P11 from RTA. 6 Table 2 reports Ki = 8 ± 0.3 µM for PD00589; footnote states Ki values were measured by fluorescence polarization. auto_metric_priority unique highest-priority metric family: Ki [1] 3 structures\8TAB\8TAB_metadata.json point structures/8TAB/8tab_protein.pdb structures/8TAB/8tab_pocket.pdb structures/8TAB/8tab_ligand.sdf structures/8TAB/8tab_ligand.pdb structures/8TAB/8tab_ligand.cif structures/8TAB/8tab_complex.pdb structures/8TAB/8tab_complex.cif 8TAD classic Ricin toxin A subunit (RTA) Na RTA residues 1-267; expressed with an N-terminal deca-histidine/SUMO tag that was removed before complexation Na RU-NT-206 "[""ZXJ""]" 1 Ki Ki = = 1 ± 0.3 µM 1000.0 [] unit_conversion 6.0 success True direct_binding Fluorescence-polarization competition assay measuring displacement of BODIPY-TMR-X-labelled P11 from RTA. 6 Table 2 reports Ki = 1 ± 0.3 µM for RU-NT-206; footnote states Ki values were measured by fluorescence polarization. auto_metric_priority unique highest-priority metric family: Ki [1] 3 structures\8TAD\8TAD_metadata.json point structures/8TAD/8tad_protein.pdb structures/8TAD/8tad_pocket.pdb structures/8TAD/8tad_ligand.sdf structures/8TAD/8tad_ligand.pdb structures/8TAD/8tad_ligand.cif structures/8TAD/8tad_complex.pdb structures/8TAD/8tad_complex.cif 8TAW classic CYP199A4 Rhodopseudomonas palustris HaA2 Na T252E 4-(pyridin-2-yl)benzoic acid (4-pyridin-2-ylbenzoate) "[""PQS""]" 1 Kd Kd = = 0.10 ± 0.1 μM 100.0 [] unit_conversion 7.0 success True direct_binding Native mass spectrometry binding-affinity measurement; the paper states that 4-(pyridin-2-yl)benzoic acid bound T252E more tightly than WT. 6 “4-pyridin-2-ylbenzoic acid was found to bind more tightly to the T252E mutant than to WT CYP199A4 (0.10 ± 0.1 vs. 1.0 ± 0.1 μM)” and the preceding text identifies native mass spectrometry as the binding-affinity method. auto_single_measurement only accepted activity measurement [1] 1 structures\8TAW\8TAW_metadata.json point structures/8TAW/8taw_protein.pdb structures/8TAW/8taw_pocket.pdb structures/8TAW/8taw_ligand.sdf structures/8TAW/8taw_ligand.pdb structures/8TAW/8taw_ligand.cif structures/8TAW/8taw_complex.pdb structures/8TAW/8taw_complex.cif 8TB5 classic TYK2 Na Na Na Compound 7 "[""ZOQ""]" 1 IC50 IC50 = = 0.48 μM 480.0 [] unit_conversion 6.318758762624412 success True direct_binding TR-FRET binding assay. 4 “compound 7 … binding to the TYK2 JH2 domain (IC50 = 0.48 μM, TR-FRET binding assay)” and its crystal structure is identified as PDB 8TB5. auto_single_measurement only accepted activity measurement [1] 1 structures\8TB5\8TB5_metadata.json point structures/8TB5/8tb5_protein.pdb structures/8TB5/8tb5_pocket.pdb structures/8TB5/8tb5_ligand.sdf structures/8TB5/8tb5_ligand.pdb structures/8TB5/8tb5_ligand.cif structures/8TB5/8tb5_complex.pdb structures/8TB5/8tb5_complex.cif 8TB6 classic TYK2 Na Na Na Compound 14 "[""ZOI""]" 1 IC50 IC50 = = 0.005 μM 5.0 [] unit_conversion 8.301029995663981 success True direct_binding TYK2 JH2 binding assay; Table 1 reports TYK2 JH2 binding IC50 values. 3 Table 1 lists compound 14 with a TYK2 JH2 binding IC50 of 0.005 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TB6\8TB6_metadata.json point structures/8TB6/8tb6_protein.pdb structures/8TB6/8tb6_pocket.pdb structures/8TB6/8tb6_ligand.sdf structures/8TB6/8tb6_ligand.pdb structures/8TB6/8tb6_ligand.cif structures/8TB6/8tb6_complex.pdb structures/8TB6/8tb6_complex.cif 8TBF classic KRAS; CypA Na Na WT RMC-7977 "[""ZNI""]" 1 Kd Kd = = 116 nM 116.0 [] unit_conversion 6.935542010773082 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding KRAS WT. 23 Extended Data Table 2 reports KRAS WT Kd2 = 116 nM (95% CI 128–104; n=8). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBF\8TBF_metadata.json point structures/8TBF/8tbf_protein.pdb structures/8TBF/8tbf_pocket.pdb structures/8TBF/8tbf_ligand.sdf structures/8TBF/8tbf_ligand.pdb structures/8TBF/8tbf_ligand.cif structures/8TBF/8tbf_complex.pdb structures/8TBF/8tbf_complex.cif 8TBG classic HRAS; CypA Na Na WT RMC-7977 "[""ZNI""]" 1 Kd Kd = = 94.7 nM 94.7 [] unit_conversion 7.023650020996726 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding HRAS WT. 24 Extended Data Table 3 reports HRAS WT Kd2 = 94.7 nM (95% CI 106–84.3; n=3). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBG\8TBG_metadata.json point structures/8TBG/8tbg_protein.pdb structures/8TBG/8tbg_pocket.pdb structures/8TBG/8tbg_ligand.sdf structures/8TBG/8tbg_ligand.pdb structures/8TBG/8tbg_ligand.cif structures/8TBG/8tbg_complex.pdb structures/8TBG/8tbg_complex.cif 8TBH classic KRAS; CypA Na Na G12R RMC-7977 "[""ZNI""]" 1 Kd Kd = = 271 nM 271.0 [] unit_conversion 6.567030709125595 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding KRAS G12R. 23 Extended Data Table 2 reports KRAS G12R Kd2 = 271 nM (95% CI 308–237; n=3). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBH\8TBH_metadata.json point structures/8TBH/8tbh_protein.pdb structures/8TBH/8tbh_pocket.pdb structures/8TBH/8tbh_ligand.sdf structures/8TBH/8tbh_ligand.pdb structures/8TBH/8tbh_ligand.cif structures/8TBH/8tbh_complex.pdb structures/8TBH/8tbh_complex.cif 8TBI classic NRAS; CypA Na Na WT RMC-7977 "[""ZNI""]" 1 Kd Kd = = 101 nM 101.0 [] unit_conversion 6.995678626217357 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding NRAS WT. 24 Extended Data Table 3 reports NRAS WT Kd2 = 101 nM (95% CI 115–87.7; n=3). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBI\8TBI_metadata.json point structures/8TBI/8tbi_protein.pdb structures/8TBI/8tbi_pocket.pdb structures/8TBI/8tbi_ligand.sdf structures/8TBI/8tbi_ligand.pdb structures/8TBI/8tbi_ligand.cif structures/8TBI/8tbi_complex.pdb structures/8TBI/8tbi_complex.cif 8TBJ classic KRAS; CypA Na Na G12A RMC-7977 "[""ZNI""]" 1 Kd Kd = = 342 nM 342.0 [] unit_conversion 6.465973893943865 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding KRAS G12A. 23 Extended Data Table 2 reports KRAS G12A Kd2 = 342 nM (95% CI 415–282; n=3). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBJ\8TBJ_metadata.json point structures/8TBJ/8tbj_protein.pdb structures/8TBJ/8tbj_pocket.pdb structures/8TBJ/8tbj_ligand.sdf structures/8TBJ/8tbj_ligand.pdb structures/8TBJ/8tbj_ligand.cif structures/8TBJ/8tbj_complex.pdb structures/8TBJ/8tbj_complex.cif 8TBK classic KRAS; CypA Na Na G12C RMC-7977 "[""ZNI""]" 1 Kd Kd = = 40.3 nM 40.3 [] unit_conversion 7.394694953858891 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding KRAS G12C. 23 Extended Data Table 2 reports KRAS G12C Kd2 = 40.3 nM (95% CI 43.9–36.9; n=3). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBK\8TBK_metadata.json point structures/8TBK/8tbk_protein.pdb structures/8TBK/8tbk_pocket.pdb structures/8TBK/8tbk_ligand.sdf structures/8TBK/8tbk_ligand.pdb structures/8TBK/8tbk_ligand.cif structures/8TBK/8tbk_complex.pdb structures/8TBK/8tbk_complex.cif 8TBL classic KRAS; CypA Na Na G12D RMC-7977 "[""ZNI""]" 1 Kd Kd = = 317 nM 317.0 [] unit_conversion 6.498940737782249 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding KRAS G12D. 23 Extended Data Table 2 reports KRAS G12D Kd2 = 317 nM (95% CI 358–280; n=3). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBL\8TBL_metadata.json point structures/8TBL/8tbl_protein.pdb structures/8TBL/8tbl_pocket.pdb structures/8TBL/8tbl_ligand.sdf structures/8TBL/8tbl_ligand.pdb structures/8TBL/8tbl_ligand.cif structures/8TBL/8tbl_complex.pdb structures/8TBL/8tbl_complex.cif 8TBM classic KRAS; CypA Na Na G12V RMC-7977 "[""ZNI""]" 1 Kd Kd = = 84.8 nM 84.8 [] unit_conversion 7.071604147743287 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding KRAS G12V. 23 Extended Data Table 2 reports KRAS G12V Kd2 = 84.8 nM (95% CI 74–98; n=6). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBM\8TBM_metadata.json point structures/8TBM/8tbm_protein.pdb structures/8TBM/8tbm_pocket.pdb structures/8TBM/8tbm_ligand.sdf structures/8TBM/8tbm_ligand.pdb structures/8TBM/8tbm_ligand.cif structures/8TBM/8tbm_complex.pdb structures/8TBM/8tbm_complex.cif 8TBN classic KRAS; CypA Na Na G12S RMC-7977 "[""ZNI""]" 1 Kd Kd = = 128 nM 128.0 [] unit_conversion 6.892790030352131 success True direct_binding Steady-state SPR Kd2 for compound-bound CypA binding KRAS G12S. 23 Extended Data Table 2 reports KRAS G12S Kd2 = 128 nM (95% CI 114–143; n=3). auto_single_measurement only accepted activity measurement [1] 1 structures\8TBN\8TBN_metadata.json point structures/8TBN/8tbn_protein.pdb structures/8TBN/8tbn_pocket.pdb structures/8TBN/8tbn_ligand.sdf structures/8TBN/8tbn_ligand.pdb structures/8TBN/8tbn_ligand.cif structures/8TBN/8tbn_complex.pdb structures/8TBN/8tbn_complex.cif 8TCE classic Lipoprotein(a) Kringle IV domain 8 (Lp(a) KIV8) Homo sapiens (human) Recombinant apo(a) KIV8 domain, residues 1377-1470, based on GenBank NP_005568.2 Na LY3353871 (LSN3353871) "[""HWF""]" 1 Kd Kd = = 756 nM 756.0 [] unit_conversion 6.121478204498794 success True direct_binding Isothermal titration calorimetry (ITC) with purified recombinant apo(a) KIV8. 2 LSN3353871 binds apo(a) KIV8 with Kd 756 nM, determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8TCE\8TCE_metadata.json point structures/8TCE/8tce_protein.pdb structures/8TCE/8tce_pocket.pdb structures/8TCE/8tce_ligand.sdf structures/8TCE/8tce_ligand.pdb structures/8TCE/8tce_ligand.cif structures/8TCE/8tce_complex.pdb structures/8TCE/8tce_complex.cif 8TCU classic PYCR1 Na PYCR1 residues 1-294, C-terminus truncated by 25 residues, with an N-terminal His tag and TEV cleavage site; His tag not removed Na compound 2 (2-chloro-5-(2-oxoimidazolidin-1-yl)benzoic acid) "[""ZR3""]" 1 IC50 IC50 = = 1.1 ± 0.2 mM 1100000.0 [] unit_conversion 2.9586073148417746 success True biochemical_inhibition Purified PYCR1 enzyme activity concentration-response assay; 50 μM NADH and 200 μM L-P5C. 30 Table 2 reports compound 2 IC50 = 1.1 ± 0.2 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TCU\8TCU_metadata.json point structures/8TCU/8tcu_protein.pdb structures/8TCU/8tcu_pocket.pdb structures/8TCU/8tcu_ligand.sdf structures/8TCU/8tcu_ligand.pdb structures/8TCU/8tcu_ligand.cif structures/8TCU/8tcu_complex.pdb structures/8TCU/8tcu_complex.cif 8TCV extended PYCR1 Na PYCR1 residues 1-294, C-terminus truncated by 25 residues, with an N-terminal His tag and TEV cleavage site; His tag not removed Na compound 14 (4-bromobenzene-1,3-dicarboxylic acid) "[""ZR0""]" 1 IC50 IC50 > > 10 mM 10000000.0 [] unit_conversion 2.0 success True biochemical_inhibition Purified PYCR1 enzyme activity concentration-response assay; 50 μM NADH and 200 μM L-P5C. 30 Table 2 reports compound 14 IC50 >10 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TCV\8TCV_metadata.json point structures/8TCV/8tcv_protein.pdb structures/8TCV/8tcv_pocket.pdb structures/8TCV/8tcv_ligand.pdb structures/8TCV/8tcv_ligand.cif structures/8TCV/8tcv_complex.pdb structures/8TCV/8tcv_complex.cif 8TCW classic PYCR1 Na PYCR1 residues 1-294, C-terminus truncated by 25 residues, with an N-terminal His tag and TEV cleavage site; His tag not removed Na compound 19 (2-methyl-3-(2-oxoimidazolidin-1-yl)benzoic acid) "[""ZR6""]" 1 IC50 IC50 > > 10 mM 10000000.0 [] unit_conversion 2.0 success True biochemical_inhibition Purified PYCR1 enzyme activity concentration-response assay; 50 μM NADH and 200 μM L-P5C. 30 Table 2 reports compound 19 IC50 >10 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TCW\8TCW_metadata.json point structures/8TCW/8tcw_protein.pdb structures/8TCW/8tcw_pocket.pdb structures/8TCW/8tcw_ligand.sdf structures/8TCW/8tcw_ligand.pdb structures/8TCW/8tcw_ligand.cif structures/8TCW/8tcw_complex.pdb structures/8TCW/8tcw_complex.cif 8TCX classic PYCR1 Na PYCR1 residues 1-294, C-terminus truncated by 25 residues, with an N-terminal His tag and TEV cleavage site; His tag not removed Na compound 20 (2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-carboxylic acid) "[""ZR9""]" 1 IC50 IC50 = = 0.3 ± 0.01 mM 300000.0 [] unit_conversion 3.5228787452803374 success True biochemical_inhibition Purified PYCR1 enzyme activity concentration-response assay; 50 μM NADH and 200 μM L-P5C. 30 Table 2 reports compound 20 IC50 = 0.3 ± 0.01 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TCX\8TCX_metadata.json point structures/8TCX/8tcx_protein.pdb structures/8TCX/8tcx_pocket.pdb structures/8TCX/8tcx_ligand.sdf structures/8TCX/8tcx_ligand.pdb structures/8TCX/8tcx_ligand.cif structures/8TCX/8tcx_complex.pdb structures/8TCX/8tcx_complex.cif 8TCY classic PYCR1 Na PYCR1 residues 1-294, C-terminus truncated by 25 residues, with an N-terminal His tag and TEV cleavage site; His tag not removed Na compound 22 (7-fluoro-2-oxo-1,2,3,4-tetrahydroquinoline-6-carboxylic acid) "[""ZRE""]" 1 IC50 IC50 > > 1 mM 1000000.0 [] unit_conversion 3.0 success True biochemical_inhibition Purified PYCR1 enzyme activity concentration-response assay; 50 μM NADH and 200 μM L-P5C. 30 Table 2 reports compound 22 IC50 >1 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TCY\8TCY_metadata.json point structures/8TCY/8tcy_protein.pdb structures/8TCY/8tcy_pocket.pdb structures/8TCY/8tcy_ligand.sdf structures/8TCY/8tcy_ligand.pdb structures/8TCY/8tcy_ligand.cif structures/8TCY/8tcy_complex.pdb structures/8TCY/8tcy_complex.cif 8TCZ classic PYCR1 Na PYCR1 residues 1-294, C-terminus truncated by 25 residues, with an N-terminal His tag and TEV cleavage site; His tag not removed Na compound 32 (2-(pyridin-2-yl)cyclopropane-1-carboxylic acid) "[""ZRI""]" 1 IC50 IC50 > > 10 mM 10000000.0 [] unit_conversion 2.0 success True biochemical_inhibition Purified PYCR1 enzyme activity concentration-response assay; 50 μM NADH and 200 μM L-P5C. 30 Table 2 reports compound 32 IC50 >10 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TCZ\8TCZ_metadata.json point structures/8TCZ/8tcz_protein.pdb structures/8TCZ/8tcz_pocket.pdb structures/8TCZ/8tcz_ligand.sdf structures/8TCZ/8tcz_ligand.pdb structures/8TCZ/8tcz_ligand.cif structures/8TCZ/8tcz_complex.pdb structures/8TCZ/8tcz_complex.cif 8TD0 classic PYCR1 Na PYCR1 residues 1-294, C-terminus truncated by 25 residues, with an N-terminal His tag and TEV cleavage site; His tag not removed Na compound 33 (5-oxo-7a-phenyl-hexahydropyrrolo[2,1-b][1,3]thiazole-3-carboxylic acid) "[""ZS5""]" 1 IC50 IC50 = = 0.029 ± 0.003 mM 29000.0 [] unit_conversion 4.5376020021010435 success True biochemical_inhibition Purified PYCR1 enzyme activity concentration-response assay; 50 μM NADH and 200 μM L-P5C. 30 Table 2 reports compound 33 IC50 = 0.029 ± 0.003 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TD0\8TD0_metadata.json point structures/8TD0/8td0_protein.pdb structures/8TD0/8td0_pocket.pdb structures/8TD0/8td0_ligand.sdf structures/8TD0/8td0_ligand.pdb structures/8TD0/8td0_ligand.cif structures/8TD0/8td0_complex.pdb structures/8TD0/8td0_complex.cif 8TD1 classic PYCR1 Na PYCR1 residues 1-294, C-terminus truncated by 25 residues, with an N-terminal His tag and TEV cleavage site; His tag not removed Na compound 36 (3-(6-Oxa-9-azaspiro(4.5)decane-9-carbonyl)benzoic acid) "[""ZRZ""]" 1 IC50 IC50 = = 5.4 ± 0.4 mM 5400000.0 [] unit_conversion 2.267606240177032 success True biochemical_inhibition Purified PYCR1 enzyme activity concentration-response assay; 50 μM NADH and 200 μM L-P5C. 30 Table 2 reports compound 36 IC50 = 5.4 ± 0.4 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TD1\8TD1_metadata.json point structures/8TD1/8td1_protein.pdb structures/8TD1/8td1_pocket.pdb structures/8TD1/8td1_ligand.sdf structures/8TD1/8td1_ligand.pdb structures/8TD1/8td1_ligand.cif structures/8TD1/8td1_complex.pdb structures/8TD1/8td1_complex.cif 8TD2 classic Delta1-pyrroline-5-carboxylate reductase isoform 1 (PYCR1) Na Recombinant PYCR1 with a truncated C-terminus, residues 1-294 Na compound 7 (cyclobutane-1,1-dicarboxylic acid) "[""ZPS""]" 1 Ki Ki = = 4.5 ± 0.7 mM 4500000.0 [] unit_conversion 2.346787486224656 success True biochemical_inhibition Competitive inhibition kinetics with L-P5C variable and NADH fixed at 175 μM. 10 Table 1 reports compound 7 Ki = 4.5 ± 0.7 mM; the text states these values were globally fit to a competitive inhibition model. auto_single_measurement only accepted activity measurement [1] 1 structures\8TD2\8TD2_metadata.json point structures/8TD2/8td2_protein.pdb structures/8TD2/8td2_pocket.pdb structures/8TD2/8td2_ligand.sdf structures/8TD2/8td2_ligand.pdb structures/8TD2/8td2_ligand.cif structures/8TD2/8td2_complex.pdb structures/8TD2/8td2_complex.cif 8TD4 classic Delta1-pyrroline-5-carboxylate reductase isoform 1 (PYCR1) Na Recombinant PYCR1 with a truncated C-terminus, residues 1-294 Na compound 22 (1,3-dithiolane-2-carboxylic acid) "[""UJD""]" 1 Ki Ki = = 0.04 ± 0.01 mM 40000.0 [] unit_conversion 4.3979400086720375 success True biochemical_inhibition Competitive inhibition kinetics with L-P5C variable and NADH fixed at 175 μM. 10 Table 1 reports compound 22 Ki = 0.04 ± 0.01 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TD4\8TD4_metadata.json point structures/8TD4/8td4_protein.pdb structures/8TD4/8td4_pocket.pdb structures/8TD4/8td4_ligand.sdf structures/8TD4/8td4_ligand.pdb structures/8TD4/8td4_ligand.cif structures/8TD4/8td4_complex.pdb structures/8TD4/8td4_complex.cif 8TD6 classic Delta1-pyrroline-5-carboxylate reductase isoform 1 (PYCR1) Na Recombinant PYCR1 with a truncated C-terminus, residues 1-294 Na compound 27 (2-(methylthio)acetic acid) "[""MTG""]" 1 Ki Ki = = 2.5 ± 0.5 mM 2500000.0 [] unit_conversion 2.6020599913279625 success True biochemical_inhibition Competitive inhibition kinetics with L-P5C variable and NADH fixed at 175 μM. 10 Table 1 reports compound 27 Ki = 2.5 ± 0.5 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TD6\8TD6_metadata.json point structures/8TD6/8td6_protein.pdb structures/8TD6/8td6_pocket.pdb structures/8TD6/8td6_ligand.sdf structures/8TD6/8td6_ligand.pdb structures/8TD6/8td6_ligand.cif structures/8TD6/8td6_complex.pdb structures/8TD6/8td6_complex.cif 8TD8 classic Delta1-pyrroline-5-carboxylate reductase isoform 1 (PYCR1) Na Recombinant PYCR1 with a truncated C-terminus, residues 1-294 Na compound 39 (2S-hydroxy-3,3-dimethylbutyric acid) "[""G8I""]" 1 Ki Ki = = 0.8 ± 0.1 mM 800000.0 [] unit_conversion 3.0969100130080562 success True biochemical_inhibition Competitive inhibition kinetics with L-P5C variable and NADH fixed at 175 μM. 10 Table 1 reports compound 39 Ki = 0.8 ± 0.1 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TD8\8TD8_metadata.json point structures/8TD8/8td8_protein.pdb structures/8TD8/8td8_pocket.pdb structures/8TD8/8td8_ligand.sdf structures/8TD8/8td8_ligand.pdb structures/8TD8/8td8_ligand.cif structures/8TD8/8td8_complex.pdb structures/8TD8/8td8_complex.cif 8TD9 classic Delta1-pyrroline-5-carboxylate reductase isoform 1 (PYCR1) Na Recombinant PYCR1 with a truncated C-terminus, residues 1-294 Na compound 41 (L-pipecolic acid) "[""YCP""]" 1 Ki Ki = = 1.7 ± 0.3 mM 1700000.0 [] unit_conversion 2.769551078621726 success True biochemical_inhibition Competitive inhibition kinetics with L-P5C variable and NADH fixed at 175 μM. 10 Table 1 reports compound 41 Ki = 1.7 ± 0.3 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TD9\8TD9_metadata.json point structures/8TD9/8td9_protein.pdb structures/8TD9/8td9_pocket.pdb structures/8TD9/8td9_ligand.sdf structures/8TD9/8td9_ligand.pdb structures/8TD9/8td9_ligand.cif structures/8TD9/8td9_complex.pdb structures/8TD9/8td9_complex.cif 8TDC classic Delta1-pyrroline-5-carboxylate reductase isoform 1 (PYCR1) Na Recombinant PYCR1 with a truncated C-terminus, residues 1-294 Na compound 66 (1,3-dithiane-2-carboxylic acid) "[""GIW""]" 1 Ki Ki = = 0.9 ± 0.2 mM 900000.0 [] unit_conversion 3.045757490560675 success True biochemical_inhibition Competitive inhibition kinetics with L-P5C variable and NADH fixed at 175 μM. 10 Table 1 reports compound 66 Ki = 0.9 ± 0.2 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TDC\8TDC_metadata.json point structures/8TDC/8tdc_protein.pdb structures/8TDC/8tdc_pocket.pdb structures/8TDC/8tdc_ligand.sdf structures/8TDC/8tdc_ligand.pdb structures/8TDC/8tdc_ligand.cif structures/8TDC/8tdc_complex.pdb structures/8TDC/8tdc_complex.cif 8TDD classic Delta1-pyrroline-5-carboxylate reductase isoform 1 (PYCR1) Na Recombinant PYCR1 with a truncated C-terminus, residues 1-294 Na compound 70 (2-(furan-2-yl)acetic acid) "[""SJU""]" 1 IC50 IC50 = = 39 ± 8 μM 39000.0 [] unit_conversion 4.4089353929735005 success True biochemical_inhibition Concentration–response enzyme-inhibition assay; its kinetic pattern did not fit the standard inhibition models. 10 The text reports that the concentration–response behavior of compound 70 yields an IC50 of 39 ± 8 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TDD\8TDD_metadata.json point structures/8TDD/8tdd_protein.pdb structures/8TDD/8tdd_pocket.pdb structures/8TDD/8tdd_ligand.sdf structures/8TDD/8tdd_ligand.pdb structures/8TDD/8tdd_ligand.cif structures/8TDD/8tdd_complex.pdb structures/8TDD/8tdd_complex.cif 8TE9 classic OalseP (IseP) Oleidesulfovibrio alaskensis IseP without the native signal peptide; expressed with an N-terminal His6-HRV 3C tag and tag-cleaved before crystallization Na isethionate "[""8X3""]" 1 Kd Kd = = 0.95 (68% CI: 0.6–1.4) µM 950.0 [] unit_conversion 6.022276394711152 success True direct_binding Isothermal titration calorimetry (ITC) of recombinant OalseP with isethionate. 7 Table 1 reports “KD isethionate (68% CI) µM 0.95 (0.6–1.4)”; the text identifies this as ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8TE9\8TE9_metadata.json point structures/8TE9/8te9_protein.pdb structures/8TE9/8te9_pocket.pdb structures/8TE9/8te9_ligand.sdf structures/8TE9/8te9_ligand.pdb structures/8TE9/8te9_ligand.cif structures/8TE9/8te9_complex.pdb structures/8TE9/8te9_complex.cif 8TF0 classic Grp94 canine Grp94NDelta41, residues 69-337 with charged linker residues 287-327 replaced by 4 glycines Charged linker residues 287-327 replaced with 4 glycines (Grp94NDelta41) PU-H36 "[""ZUY""]" 1 Kd Kd = = 2.6 ± 0.05 µM 2600.0 [] unit_conversion 5.585026652029182 success True direct_binding ITC titration of Grp94NΔ41 with PU-H36. 33 Table 1 reports Grp94NΔ41–PU-H36 Kd of 2.6 ± 0.05 µM; Table 2 maps Grp94N:PU-H36 to PDB 8TF0. auto_single_measurement only accepted activity measurement [1] 1 structures\8TF0\8TF0_metadata.json point structures/8TF0/8tf0_protein.pdb structures/8TF0/8tf0_pocket.pdb structures/8TF0/8tf0_ligand.sdf structures/8TF0/8tf0_ligand.pdb structures/8TF0/8tf0_ligand.cif structures/8TF0/8tf0_complex.pdb structures/8TF0/8tf0_complex.cif 8TGF extended LGG-1 C. elegans LGG-1 with CeEPG5 LIR1 peptide, residues 505-515 (STWEILADDDD) Na CeEPG5 LIR1 peptide (STWEILADDDD) "[""CHAIN:B""]" 1 Kd Kd = = 1.46 μM 1460.0 [] unit_conversion 5.835647144215563 success True direct_binding Isothermal titration calorimetry of CeEPG5 LIR1 peptide into LGG-1. 9 Figure 4E labels the CeEPG5 LIR1 peptide STWEILADDDD and reports “Kd 1.46 μM, LGG-1 + CeEPG5 LIR1”; the caption identifies this as ITC analysis. auto_single_measurement only accepted activity measurement [1] 1 structures\8TGF\8TGF_metadata.json point structures/8TGF/8tgf_protein.pdb structures/8TGF/8tgf_pocket.pdb structures/8TGF/8tgf_ligand.pdb structures/8TGF/8tgf_ligand.cif structures/8TGF/8tgf_complex.pdb structures/8TGF/8tgf_complex.cif 8TH1 extended G3BP1 human G3BP1 NTF2-like domain D3L in the SARS-CoV-2 nucleocapsid peptide SARS-CoV-2 N-D3L peptide (residues 1-25) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 1.10 ± 0.06 μM 1100.0 [] unit_conversion 5.958607314841775 success True direct_binding Surface plasmon resonance with purified GST-NTF2L and N1-25 D3L peptide. 6 Figure 2E lists N1-25 D3L binding to GST-NTF2L with KD = 1.10 ± 0.06 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TH1\8TH1_metadata.json point structures/8TH1/8th1_protein.pdb structures/8TH1/8th1_pocket.pdb structures/8TH1/8th1_ligand.pdb structures/8TH1/8th1_ligand.cif structures/8TH1/8th1_complex.pdb structures/8TH1/8th1_complex.cif 8TH5 extended G3BP1 human G3BP1 NTF2-like domain P13L in the SARS-CoV-2 nucleocapsid peptide SARS-CoV-2 N-P13L peptide (residues 1-25) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 2.60 ± 0.20 μM 2600.0 [] unit_conversion 5.585026652029182 success True direct_binding Surface plasmon resonance with purified GST-NTF2L and N1-25 P13L peptide. 6 Figure 2E lists N1-25 P13L binding to GST-NTF2L with KD = 2.60 ± 0.20 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TH5\8TH5_metadata.json point structures/8TH5/8th5_protein.pdb structures/8TH5/8th5_pocket.pdb structures/8TH5/8th5_ligand.pdb structures/8TH5/8th5_ligand.cif structures/8TH5/8th5_complex.pdb structures/8TH5/8th5_complex.cif 8TH6 extended G3BP1 human G3BP1 NTF2-like domain Na USP10 peptide (residues 2-25) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 0.11 ± 0.00 μM 110.0 [] unit_conversion 6.958607314841775 success True direct_binding Surface plasmon resonance with purified GST-NTF2L and USP10(2-25) peptide. 8 Figure 3C lists USP10(2-25) binding to GST-NTF2L with KD = 0.11 ± 0.00 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TH6\8TH6_metadata.json point structures/8TH6/8th6_protein.pdb structures/8TH6/8th6_pocket.pdb structures/8TH6/8th6_ligand.pdb structures/8TH6/8th6_ligand.cif structures/8TH6/8th6_complex.pdb structures/8TH6/8th6_complex.cif 8TIC classic human beta 1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) human Na Na compound 1 "[""FKX""]" 1 IC50 IC50 = = 9.1 (±2.5) μM 9100.0 [] unit_conversion 5.040958607678906 success True biochemical_inhibition In vitro enzymatic potency from uHTS (Table 1). 2 Table 1 prints B3GNT2 IC50 = 9.1 (±2.5) μM for hit compound 1; Figure 2 identifies compound 1 in complex with B3GNT2 as PDB 8TIC. auto_single_measurement only accepted activity measurement [1] 1 structures\8TIC\8TIC_metadata.json point structures/8TIC/8tic_protein.pdb structures/8TIC/8tic_pocket.pdb structures/8TIC/8tic_ligand.sdf structures/8TIC/8tic_ligand.pdb structures/8TIC/8tic_ligand.cif structures/8TIC/8tic_complex.pdb structures/8TIC/8tic_complex.cif 8TJC classic human beta 1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) human Na Na compound 8a "[""HI8""]" 1 IC50 IC50 = = 0.60 (±0.04) μM 600.0 [] unit_conversion 6.221848749616356 success True biochemical_inhibition In vitro enzymatic potency (Table 3). 5 Table 3 prints B3GNT2 IC50 = 0.60 (±0.04) μM for compound 8a. The accession list on page 19, together with the sibling mappings, supports 8TJC as the 8a cocrystal despite the Figure 4 caption transposition. auto_single_measurement only accepted activity measurement [1] 1 structures\8TJC\8TJC_metadata.json point structures/8TJC/8tjc_protein.pdb structures/8TJC/8tjc_pocket.pdb structures/8TJC/8tjc_ligand.sdf structures/8TJC/8tjc_ligand.pdb structures/8TJC/8tjc_ligand.cif structures/8TJC/8tjc_complex.pdb structures/8TJC/8tjc_complex.cif 8TK9 extended ZIG-4 Caenorhabditis elegans Secreted ZIG-4 and INS-6 co-expressed using baculovirus; both C-terminally hexahistidine-tagged Na INS-6 "[""CHAIN:B""]" 1 Kd Kd = = 55.7 pM 0.055700000000000006 [] unit_conversion 10.254144804826272 success True direct_binding SPR sensorgram kinetic fit for INS-6 binding to immobilized ZIG-4. 53 Figure S4E explicitly reports for “INS-6 on ZIG-4”: K_D = 55.7 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TK9\8TK9_metadata.json point structures/8TK9/8tk9_protein.pdb structures/8TK9/8tk9_pocket.pdb structures/8TK9/8tk9_ligand.pdb structures/8TK9/8tk9_ligand.cif structures/8TK9/8tk9_complex.pdb structures/8TK9/8tk9_complex.cif 8TKT extended ZIG-4 Caenorhabditis elegans Secreted ZIG-4 and INS-6 co-expressed using baculovirus; both C-terminally hexahistidine-tagged Na INS-6 "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 55.7 pM 0.055700000000000006 [] unit_conversion 10.254144804826272 success True direct_binding SPR sensorgram kinetic fit for INS-6 binding to immobilized ZIG-4. 53 Figure S4E explicitly reports for “INS-6 on ZIG-4”: K_D = 55.7 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TKT\8TKT_metadata.json point structures/8TKT/8tkt_protein.pdb structures/8TKT/8tkt_pocket.pdb structures/8TKT/8tkt_ligand.pdb structures/8TKT/8tkt_ligand.cif structures/8TKT/8tkt_complex.pdb structures/8TKT/8tkt_complex.cif 8TKU extended ZIG-4 Caenorhabditis elegans Secreted ZIG-4 and INS-6 co-expressed using baculovirus; both C-terminally hexahistidine-tagged Na INS-6 "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H""]" 1 Kd Kd = = 55.7 pM 0.055700000000000006 [] unit_conversion 10.254144804826272 success True direct_binding SPR sensorgram kinetic fit for INS-6 binding to immobilized ZIG-4. 53 Figure S4E explicitly reports for “INS-6 on ZIG-4”: K_D = 55.7 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TKU\8TKU_metadata.json point structures/8TKU/8tku_protein.pdb structures/8TKU/8tku_pocket.pdb structures/8TKU/8tku_ligand.pdb structures/8TKU/8tku_ligand.cif structures/8TKU/8tku_complex.pdb structures/8TKU/8tku_complex.cif 8TMT classic KPC-44 carbapenemase Klebsiella pneumoniae KPC-44 Delta4, lacking the last four amino acids 15-amino-acid duplication Ala262-Glu276 vaborbactam "[""4D6""]" 1 IC50 IC50 = = 0.22 ± 0.000092 µM 220.0 [] unit_conversion 6.657577319177793 success True biochemical_inhibition Purified KPC-44 inhibition of nitrocefin hydrolysis by vaborbactam; Table 3. 5 Table 3 reports the vaborbactam IC50 for KPC-44 as 0.22 ± 0.000092 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TMT\8TMT_metadata.json point structures/8TMT/8tmt_protein.pdb structures/8TMT/8tmt_pocket.pdb structures/8TMT/8tmt_ligand.sdf structures/8TMT/8tmt_ligand.pdb structures/8TMT/8tmt_ligand.cif structures/8TMT/8tmt_complex.pdb structures/8TMT/8tmt_complex.cif 8TN6 extended PiB' Na Na Na rucaparib "[""RPB""]" 1 Kd Kd = = 0.37 nM 0.37 [] unit_conversion 9.431798275933005 success True direct_binding Fluorescently monitored titration of PiB' into rucaparib; nonlinear least-squares single-site binding fit. 6 A nonlinear least-squares fit returned a Kd of 0.37 nM for PiB' with rucaparib. auto_qualifier_priority unique best qualifier within highest-priority metric family [1] 2 structures\8TN6\8TN6_metadata.json point structures/8TN6/8tn6_protein.pdb structures/8TN6/8tn6_pocket.pdb structures/8TN6/8tn6_ligand.pdb structures/8TN6/8tn6_ligand.cif structures/8TN6/8tn6_complex.pdb structures/8TN6/8tn6_complex.cif 8TNB classic PiB' Na Na Na mefuparib "[""IQM""]" 1 Kd Kd = = 350 nM 350.0 [] unit_conversion 6.455931955649724 success True direct_binding Ultraviolet-visible absorption titration of PiB' with mefuparib. 6 Ultraviolet-visible absorption titrations reported Kd = 350 nM for PiB' with mefuparib. auto_single_measurement only accepted activity measurement [1] 1 structures\8TNB\8TNB_metadata.json point structures/8TNB/8tnb_protein.pdb structures/8TNB/8tnb_pocket.pdb structures/8TNB/8tnb_ligand.sdf structures/8TNB/8tnb_ligand.pdb structures/8TNB/8tnb_ligand.cif structures/8TNB/8tnb_complex.pdb structures/8TNB/8tnb_complex.cif 8TNC extended PiB' Na Na Na niraparib "[""3JD""]" 1 Kd Kd = = 550 nM 550.0 [] unit_conversion 6.259637310505756 success True direct_binding Ultraviolet-visible absorption titration of PiB' with niraparib. 6 Ultraviolet-visible absorption titrations reported Kd = 550 nM for PiB' with niraparib. auto_single_measurement only accepted activity measurement [1] 1 structures\8TNC\8TNC_metadata.json point structures/8TNC/8tnc_protein.pdb structures/8TNC/8tnc_pocket.pdb structures/8TNC/8tnc_ligand.pdb structures/8TNC/8tnc_ligand.cif structures/8TNC/8tnc_complex.pdb structures/8TNC/8tnc_complex.cif 8TND extended PiB' Na Na Na veliparib "[""78P""]" 1 Kd Kd = = 24 mM 24000000.0 [] unit_conversion 1.6197887582883936 success True direct_binding Ultraviolet-visible absorption titration of PiB' with veliparib. 6 Ultraviolet-visible absorption titrations reported Kd = 24 mM for PiB' with veliparib. auto_single_measurement only accepted activity measurement [1] 1 structures\8TND\8TND_metadata.json point structures/8TND/8tnd_protein.pdb structures/8TND/8tnd_pocket.pdb structures/8TND/8tnd_ligand.pdb structures/8TND/8tnd_ligand.cif structures/8TND/8tnd_complex.pdb structures/8TND/8tnd_complex.cif 8TOQ extended human angiotensin-converting enzyme 2 (hACE2) human Na Na peptide 1 "[""CHAIN:E""]" 1 Kd Kd = = 0.040 ± 0.005 nM 0.04 [] unit_conversion 10.397940008672037 success True direct_binding Surface plasmon resonance (SPR) binding to immobilized hACE2. 3 Figure 3B reports peptide 1 binding to immobilized hACE2 by SPR: K_D = 0.040 ± 0.005 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TOQ\8TOQ_metadata.json point structures/8TOQ/8toq_protein.pdb structures/8TOQ/8toq_pocket.pdb structures/8TOQ/8toq_ligand.pdb structures/8TOQ/8toq_ligand.cif structures/8TOQ/8toq_complex.pdb structures/8TOQ/8toq_complex.cif 8TOR extended human angiotensin-converting enzyme 2 (hACE2) human Na Na peptide 2 "[""CHAIN:E""]" 1 Kd Kd = = 0.040 ± 0.003 nM 0.04 [] unit_conversion 10.397940008672037 success True direct_binding Surface plasmon resonance (SPR) binding to immobilized hACE2. 3 Figure 3B reports peptide 2 binding to immobilized hACE2 by SPR: K_D = 0.040 ± 0.003 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TOR\8TOR_metadata.json point structures/8TOR/8tor_protein.pdb structures/8TOR/8tor_pocket.pdb structures/8TOR/8tor_ligand.pdb structures/8TOR/8tor_ligand.cif structures/8TOR/8tor_complex.pdb structures/8TOR/8tor_complex.cif 8TOS extended human angiotensin-converting enzyme 2 (hACE2) human Na Na peptide 6 "[""CHAIN:E""]" 1 Kd Kd = = 3.3 ± 0.9 nM 3.3 [] unit_conversion 8.481486060122112 success True direct_binding Surface plasmon resonance (SPR) binding to immobilized hACE2. 3 Figure 3B reports peptide 6 binding to immobilized hACE2 by SPR: K_D = 3.3 ± 0.9 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TOS\8TOS_metadata.json point structures/8TOS/8tos_protein.pdb structures/8TOS/8tos_pocket.pdb structures/8TOS/8tos_ligand.pdb structures/8TOS/8tos_ligand.cif structures/8TOS/8tos_complex.pdb structures/8TOS/8tos_complex.cif 8TOT extended human angiotensin-converting enzyme 2 (hACE2) human Na Na peptide 2 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.040 ± 0.003 nM 0.04 [] unit_conversion 10.397940008672037 success True direct_binding Surface plasmon resonance (SPR) binding to immobilized hACE2. 3 Figure 3B reports peptide 2 binding to immobilized hACE2 by SPR: K_D = 0.040 ± 0.003 nM. The paper identifies two further ACE2–cyclic peptide 2 crystal complexes and lists 8TOT among deposited peptide–hACE2 structures. auto_single_measurement only accepted activity measurement [1] 1 structures\8TOT\8TOT_metadata.json point structures/8TOT/8tot_protein.pdb structures/8TOT/8tot_pocket.pdb structures/8TOT/8tot_ligand.pdb structures/8TOT/8tot_ligand.cif structures/8TOT/8tot_complex.pdb structures/8TOT/8tot_complex.cif 8TOU extended human angiotensin-converting enzyme 2 (hACE2) human Na Na peptide 2 "[""CHAIN:B""]" 1 Kd Kd = = 0.040 ± 0.003 nM 0.04 [] unit_conversion 10.397940008672037 success True direct_binding Surface plasmon resonance (SPR) binding to immobilized hACE2. 3 Figure 3B reports peptide 2 binding to immobilized hACE2 by SPR: K_D = 0.040 ± 0.003 nM. The paper identifies two further ACE2–cyclic peptide 2 crystal complexes and lists 8TOU among deposited peptide–hACE2 structures. auto_single_measurement only accepted activity measurement [1] 1 structures\8TOU\8TOU_metadata.json point structures/8TOU/8tou_protein.pdb structures/8TOU/8tou_pocket.pdb structures/8TOU/8tou_ligand.pdb structures/8TOU/8tou_ligand.cif structures/8TOU/8tou_complex.pdb structures/8TOU/8tou_complex.cif 8TPV classic human hypoxanthine-guanine phosphoribosyltransferase (HGPRT) human Na Na compound 5: [2S,4R]-4-Guanin-9-yl-2-(2-phosphonoethoxymethyl)-1-N-(3-phosphonopropionyl)pyrrolidine "[""JEI""]" 1 Ki Ki = = 0.003 ± 0.005 µM 3.0 [] unit_conversion 8.522878745280337 success True biochemical_inhibition Continuous spectrophotometric inhibition assay; assay buffer contained MgCl2. 4 Table 1 reports human HGPRT compound 5 Ki = 0.003 ± 0.005 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TPV\8TPV_metadata.json point structures/8TPV/8tpv_protein.pdb structures/8TPV/8tpv_pocket.pdb structures/8TPV/8tpv_ligand.sdf structures/8TPV/8tpv_ligand.pdb structures/8TPV/8tpv_ligand.cif structures/8TPV/8tpv_complex.pdb structures/8TPV/8tpv_complex.cif 8TPY classic human hypoxanthine-guanine phosphoribosyltransferase (HGPRT) human Na Na compound 1: [2S,4R]-4-Guanin-9-yl-2-hydroxymethyl-1-N-(3-phosphonopropionyl)pyrrolidine "[""JG6""]" 1 Ki Ki = = 0.09 ± 0.2 µM 90.0 [] unit_conversion 7.045757490560675 success True biochemical_inhibition Continuous spectrophotometric inhibition assay; assay buffer contained MgCl2. 4 Table 1 reports human HGPRT compound 1 Ki = 0.09 ± 0.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TPY\8TPY_metadata.json point structures/8TPY/8tpy_protein.pdb structures/8TPY/8tpy_pocket.pdb structures/8TPY/8tpy_ligand.sdf structures/8TPY/8tpy_ligand.pdb structures/8TPY/8tpy_ligand.cif structures/8TPY/8tpy_complex.pdb structures/8TPY/8tpy_complex.cif 8TQF classic Serine hydroxymethyltransferase 8 (SHMT8) Glycine max (soybean) Soybean SHMT8 from cultivar Essex; expressed in E. coli Na PLP-glycine; diglutamylated 5-formyltetrahydrofolate (diGlu-FTFH) "[""S8R""]" 1 Kd Kd = = 20 ± 3 µM 20000.0 [] unit_conversion 4.698970004336019 success True direct_binding Classical spectroscopic folate-binding assay with SHMT8 from cultivar Essex; glycine held at 5 mM. diGlu-FTFH binding data were fit to a substrate-inhibition equation. 7 Table 3 reports SHMT8 + Gly with diGlu-FTFH: Kd = 20 ± 3 µM. The table footnote specifies that polyGlu-FTFH dissociation constants were fit to the substrate-inhibition equation. auto_single_measurement only accepted activity measurement [1] 1 structures\8TQF\8TQF_metadata.json point structures/8TQF/8tqf_protein.pdb structures/8TQF/8tqf_pocket.pdb structures/8TQF/8tqf_ligand.sdf structures/8TQF/8tqf_ligand.pdb structures/8TQF/8tqf_ligand.cif structures/8TQF/8tqf_complex.pdb structures/8TQF/8tqf_complex.cif 8TQG classic Mtb Pks13 (Rv3800c) thioesterase domain Mycobacterium tuberculosis Pks13-TE domain, residues 1451-1733 of Rv3800c, expressed with an N-terminal TEV-cleavable His tag; His tag cleaved for crystallization Na X20419 "[""JR0""]" 1 IC50 IC50 = = 0.48 μM 480.0 [] unit_conversion 6.318758762624412 success True biochemical_inhibition Pks13-TE enzyme inhibition reported in the series 2 SAR figure. 6 Figure 4B lists X20419: IC50 = 0.48 μM; the caption states enzyme and Mtb inhibition are listed. auto_single_measurement only accepted activity measurement [1] 1 structures\8TQG\8TQG_metadata.json point structures/8TQG/8tqg_protein.pdb structures/8TQG/8tqg_pocket.pdb structures/8TQG/8tqg_ligand.sdf structures/8TQG/8tqg_ligand.pdb structures/8TQG/8tqg_ligand.cif structures/8TQG/8tqg_complex.pdb structures/8TQG/8tqg_complex.cif 8TR4 classic Mtb Pks13 (Rv3800c) thioesterase domain Mycobacterium tuberculosis Pks13-TE domain, residues 1451-1733 of Rv3800c, expressed with an N-terminal TEV-cleavable His tag; His tag cleaved for crystallization Na X20404 "[""K6C""]" 1 IC50 IC50 = = 0.4 μM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition Pks13-TE enzyme inhibition reported in the series 1 SAR figure. 6 Figure 4A lists X20404: IC50 = 0.4 μM; the caption states enzyme and Mtb inhibition are listed. auto_single_measurement only accepted activity measurement [1] 1 structures\8TR4\8TR4_metadata.json point structures/8TR4/8tr4_protein.pdb structures/8TR4/8tr4_pocket.pdb structures/8TR4/8tr4_ligand.sdf structures/8TR4/8tr4_ligand.pdb structures/8TR4/8tr4_ligand.cif structures/8TR4/8tr4_complex.pdb structures/8TR4/8tr4_complex.cif 8TRJ classic P2X7 receptor rat full-length wild-type rP2X7 receptor wild-type BzATP "[""KD9""]" 1 Kd Kd = = 7.4 ± 2.7 nM 7.4 [] unit_conversion 8.130768280269024 success True direct_binding Biolayer interferometry (BLI) measurement of BzATP binding to biotinylated rP2X7 immobilized on streptavidin biosensors; equilibrium dissociation constant determined from association/dissociation kinetic analysis. 3 Fig. 2D caption reports the equilibrium dissociation constant of BzATP to rP2X7 as K_D = 7.4 ± 2.7 nM; the BLI method is described on page 11. auto_single_measurement only accepted activity measurement [1] 1 structures\8TRJ\8TRJ_metadata.json point structures/8TRJ/8trj_protein.pdb structures/8TRJ/8trj_pocket.pdb structures/8TRJ/8trj_ligand.sdf structures/8TRJ/8trj_ligand.pdb structures/8TRJ/8trj_ligand.cif structures/8TRJ/8trj_complex.pdb structures/8TRJ/8trj_complex.cif 8TRY classic Mtb Pks13 (Rv3800c) thioesterase domain Mycobacterium tuberculosis Pks13-TE domain, residues 1451-1733 of Rv3800c, expressed with an N-terminal TEV-cleavable His tag; His tag cleaved for crystallization Na X20348 "[""QU0""]" 1 IC50 IC50 = = 0.9 μM 900.0 [] unit_conversion 6.045757490560675 success True direct_binding TAMRA activity-probe competitive binding assay. 7 The text states that X20348 showed an IC50 value of 0.9 μM in the TAMRA-based binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8TRY\8TRY_metadata.json point structures/8TRY/8try_protein.pdb structures/8TRY/8try_pocket.pdb structures/8TRY/8try_ligand.sdf structures/8TRY/8try_ligand.pdb structures/8TRY/8try_ligand.cif structures/8TRY/8try_complex.pdb structures/8TRY/8try_complex.cif 8TS4 classic Trypanosoma brucei hypoxanthine-guanine phosphoribosyltransferase 1 (TbrHGPRT1) Trypanosoma brucei Na Na compound 4: [2S,4S]-4-Guanin-9-yl-2-(2-phosphonoethoxymethyl)-1-N-(3-phosphonopropionyl)pyrrolidine "[""KFF""]" 1 Ki Ki = = 0.07 ± 0.02 µM 70.0 [] unit_conversion 7.154901959985743 success True biochemical_inhibition Continuous spectrophotometric inhibition assay; assay buffer contained MgCl2. 4 Table 1 reports TbrHGPRT1 compound 4 Ki = 0.07 ± 0.02 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TS4\8TS4_metadata.json point structures/8TS4/8ts4_protein.pdb structures/8TS4/8ts4_pocket.pdb structures/8TS4/8ts4_ligand.sdf structures/8TS4/8ts4_ligand.pdb structures/8TS4/8ts4_ligand.cif structures/8TS4/8ts4_complex.pdb structures/8TS4/8ts4_complex.cif 8TTR classic CA IX mimic Na CA IX protein mimic Na Na "[""LGO""]" 1 Ki Ki = = 24.3 nM 24.3 [] unit_conversion 7.614393726401688 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay against human carbonic anhydrase IX. 4 Table 1 reports SH7f Ki = 24.3 nM for hCA IX. The paper identifies SH7f as the co-crystallized ligand in CA IX mimic structure PDB 8TTR (pages 5 and 14). auto_single_measurement only accepted activity measurement [1] 1 structures\8TTR\8TTR_metadata.json point structures/8TTR/8ttr_protein.pdb structures/8TTR/8ttr_pocket.pdb structures/8TTR/8ttr_ligand.sdf structures/8TTR/8ttr_ligand.pdb structures/8TTR/8ttr_ligand.cif structures/8TTR/8ttr_complex.pdb structures/8TTR/8ttr_complex.cif 8TTU extended SNX27 Na SNX27 FERM complexed with Fam21A repeat 19 (1261-1274) Na Fam21A repeat 19 (1261-1274) "[""CHAIN:B""]" 1 Kd Kd ~ ~ 7 μM 7000.0 [] unit_conversion 5.154901959985743 success True direct_binding ITC binding of individual Fam21A repeat 19 peptide to SNX27 FERM; the text reports repeat 19 at approximately 7 μM. 6 “both FAM21R19 and FAM21R20 peptides bind to SNX27 with a Kd of ~7 μM and ~20 μM respectively” auto_single_measurement only accepted activity measurement [1] 1 structures\8TTU\8TTU_metadata.json point structures/8TTU/8ttu_protein.pdb structures/8TTU/8ttu_pocket.pdb structures/8TTU/8ttu_ligand.pdb structures/8TTU/8ttu_ligand.cif structures/8TTU/8ttu_complex.pdb structures/8TTU/8ttu_complex.cif 8TTV extended SNX27 Na SNX27 FERM complexed with Fam21A repeat 20 (1289-1302) Na Fam21A repeat 20 (1289-1302) "[""CHAIN:B""]" 1 Kd Kd ~ ~ 20 μM 20000.0 [] unit_conversion 4.698970004336019 success True direct_binding ITC binding of individual Fam21A repeat 20 peptide to SNX27 FERM; the text reports repeat 20 at approximately 20 μM. 6 “both FAM21R19 and FAM21R20 peptides bind to SNX27 with a Kd of ~7 μM and ~20 μM respectively” auto_single_measurement only accepted activity measurement [1] 1 structures\8TTV\8TTV_metadata.json point structures/8TTV/8ttv_protein.pdb structures/8TTV/8ttv_pocket.pdb structures/8TTV/8ttv_ligand.pdb structures/8TTV/8ttv_ligand.cif structures/8TTV/8ttv_complex.pdb structures/8TTV/8ttv_complex.cif 8TU3 classic Bruton's tyrosine kinase (BTK) human kinase domain of human BTK Na covalent inhibitor compound 10 "[""UEO""]" 2 Kd Kd = = 0.6 nM 0.6 [] unit_conversion 9.221848749616356 success True direct_binding BTK Kd measurement in the kinase selectivity assessment (Table 5). 9 Table 5 lists BTK Kd = 0.6 nM for compound 10; the text identifies the table's Kd measurements as the selectivity assessment of covalent BTK inhibitors. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8TU3\8TU3_metadata.json point structures/8TU3/8tu3_protein.pdb structures/8TU3/8tu3_pocket.pdb structures/8TU3/8tu3_ligand.sdf structures/8TU3/8tu3_ligand.pdb structures/8TU3/8tu3_ligand.cif structures/8TU3/8tu3_complex.pdb structures/8TU3/8tu3_complex.cif 8TUA classic PIP3-dependent Rac exchanger 1 (P-Rex1) human full-length human P-Rex1 Na inositol 1,3,4,5-tetrakisphosphate (IP4) "[""4IP""]" 1 IC50 IC50 = = 1.4 µM 1400.0 [] unit_conversion 5.853871964321762 success True biochemical_inhibition In vitro GEF activity assay on soluble Cdc42 in the presence of liposomes containing PIP3; IP4 inhibited PIP3-mediated activation of full-length P-Rex1. 2 “Using an in vitro GEF activity assay on soluble Cdc42 in the presence of liposomes, we observed that IP4 inhibits PIP3-mediated activation of P-Rex1 with an IC50 value of 1.4 µM.” Figure 1 caption reports the same IC50 and a confidence interval of 0.81–2.3. auto_single_measurement only accepted activity measurement [1] 1 structures\8TUA\8TUA_metadata.json point structures/8TUA/8tua_protein.pdb structures/8TUA/8tua_pocket.pdb structures/8TUA/8tua_ligand.sdf structures/8TUA/8tua_ligand.pdb structures/8TUA/8tua_ligand.cif structures/8TUA/8tua_complex.pdb structures/8TUA/8tua_complex.cif 8TUC classic CaMKK2 Na CaMKK2 kinase domain Na CC-8977; compound 3 "[""O7I""]" 1 IC50 IC50 = = 7.0 nM 7.0 [] unit_conversion 8.154901959985743 success True direct_binding CaMKK2 binding determined by TR-FRET. 3 Table 1 reports compound 3/CC-8977 with CaMKK2 binding IC50 = 7.0 nM; the table footnote states CaMKK1 and CaMKK2 binding were determined by TR-FRET. Figure 4 identifies PDB 8TUC as the cocrystal structure of 3/CC-8977 bound in the CaMKK2 ATP pocket. auto_single_measurement only accepted activity measurement [1] 1 structures\8TUC\8TUC_metadata.json point structures/8TUC/8tuc_protein.pdb structures/8TUC/8tuc_pocket.pdb structures/8TUC/8tuc_ligand.sdf structures/8TUC/8tuc_ligand.pdb structures/8TUC/8tuc_ligand.cif structures/8TUC/8tuc_complex.pdb structures/8TUC/8tuc_complex.cif 8TVM classic IRAK4 Na Na Na compound 24 "[""VDC""]" 1 IC50 IC50 = = 0.1 nM 0.1 [] unit_conversion 10.0 success True biochemical_inhibition IRAK4 IC50 reported in Table 3; the paper describes compound 24 as having picomolar IRAK4 biochemical potency. 3 Table 3 reports IRAK4 IC50 = 0.1 nM for compound 24. Figure 6 identifies compound 24 as one of the two cocrystallized ligands with PDB codes 8TVN and 8TVM; the supplied structure title specifically assigns compound 24 to 8TVM. auto_single_measurement only accepted activity measurement [1] 1 structures\8TVM\8TVM_metadata.json point structures/8TVM/8tvm_protein.pdb structures/8TVM/8tvm_pocket.pdb structures/8TVM/8tvm_ligand.sdf structures/8TVM/8tvm_ligand.pdb structures/8TVM/8tvm_ligand.cif structures/8TVM/8tvm_complex.pdb structures/8TVM/8tvm_complex.cif 8TYP classic Human complement component C1s Homo sapiens eC1s-2SP expressed and secreted from HEK293T cells; modeled residues 358-434, 438-495, 500-598, and 609-683 Na A1; 6-(4-phenylpiperazin-1-yl)pyridine-3-carboximidamide "[""SQT""]" 1 Kd Kd = = 9.8 ± 1.1 µM 9800.0 [] unit_conversion 5.008773924307505 success True direct_binding Surface plasmon resonance; apparent Kd for A1 binding to recombinant human C1s-2SP/eC1s-2SP. 13 “The Ki parameters for A1 inhibition of the human C1s-2SP fragment corresponded well to its apparent Kd of 9.8 ± 1.1 µM, as determined by SPR.” auto_single_measurement only accepted activity measurement [1] 1 structures\8TYP\8TYP_metadata.json point structures/8TYP/8typ_protein.pdb structures/8TYP/8typ_pocket.pdb structures/8TYP/8typ_ligand.sdf structures/8TYP/8typ_ligand.pdb structures/8TYP/8typ_ligand.cif structures/8TYP/8typ_complex.pdb structures/8TYP/8typ_complex.cif 8TZI classic Human equilibrative nucleoside transporter 1 (hENT1) Human Thermostabilized hENT1cryst variant with three mutations and a disordered-loop truncation; 11 transmembrane helices Na JH-ENT-01 "[""U00""]" 1 Ki Ki = = 92.7 ± 12.6 nM 92.7 [] unit_conversion 7.032920265855503 success True direct_binding Cold-competition scintillation proximity assay using purified thermostabilized hENT1cryst; n = 6 technical replicates across biological duplicates. 3 Figure 1c reports “JH-ENT-01 Ki = 92.7 ± 12.6 nM”; the caption identifies this as a cold-competition scintillation proximity assay using purified hENT1cryst. auto_single_measurement only accepted activity measurement [1] 1 structures\8TZI\8TZI_metadata.json point structures/8TZI/8tzi_protein.pdb structures/8TZI/8tzi_pocket.pdb structures/8TZI/8tzi_ligand.sdf structures/8TZI/8tzi_ligand.pdb structures/8TZI/8tzi_ligand.cif structures/8TZI/8tzi_complex.pdb structures/8TZI/8tzi_complex.cif 8U0H classic PTPN2 Na Na Na Cmpd-2 "[""UB0""]" 1 Kd Kd = = 85 nM 85.0 [] unit_conversion 7.070581074285707 success True direct_binding Biolayer interferometry of biotinylated PTPN2 with Cmpd-2. 2 “Cmpd-1 and Cmpd-2 bind PTPN2 with K_D values of 52 nM and 85 nM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8U0H\8U0H_metadata.json point structures/8U0H/8u0h_protein.pdb structures/8U0H/8u0h_pocket.pdb structures/8U0H/8u0h_ligand.sdf structures/8U0H/8u0h_ligand.pdb structures/8U0H/8u0h_ligand.cif structures/8U0H/8u0h_complex.pdb structures/8U0H/8u0h_complex.cif 8U15 classic SALL4 human SALL4 ZF1-2 residues 379-432 Na CC-220 "[""8W7""]" 1 Kd Kd = = 166±27 μM 166000.0 [] unit_conversion 3.779891911959945 success True direct_binding SPR affinity; SALL4 ZF1-2(379–432) binding to immobilized DDB1:CRBN complexed with 5 μM CC-220; N=4. 2 Table 1 reports ZF1-2(379–432) with CRBN:CC-220: K_D 166±27 μM (N=4). Page 3 assigns the CC-220 ZF1-2(379–432) structure to PDB 8U15. auto_single_measurement only accepted activity measurement [1] 1 structures\8U15\8U15_metadata.json point structures/8U15/8u15_protein.pdb structures/8U15/8u15_pocket.pdb structures/8U15/8u15_ligand.sdf structures/8U15/8u15_ligand.pdb structures/8U15/8u15_ligand.cif structures/8U15/8u15_complex.pdb structures/8U15/8u15_complex.cif 8U16 classic SALL4 human SALL4 ZF1-2 residues 379-432 Na Pomalidomide (POM) "[""Y70""]" 1 Kd Kd = = 2.9±0.4 μM 2900.0 [] unit_conversion 5.537602002101044 success True direct_binding SPR affinity; SALL4 ZF1-2(379–432) binding to immobilized DDB1:CRBN complexed with 5 μM pomalidomide; N=12. 2 Table 1 reports ZF1-2(379–432) with CRBN:POM: K_D 2.9±0.4 μM (N=12). Page 3 assigns the POM ZF1-2(379–432) structure to PDB 8U16. auto_single_measurement only accepted activity measurement [1] 1 structures\8U16\8U16_metadata.json point structures/8U16/8u16_protein.pdb structures/8U16/8u16_pocket.pdb structures/8U16/8u16_ligand.sdf structures/8U16/8u16_ligand.pdb structures/8U16/8u16_ligand.cif structures/8U16/8u16_complex.pdb structures/8U16/8u16_complex.cif 8U17 classic SALL4 human SALL4 ZF1-2 residues 370-454 Na Pomalidomide (POM) "[""Y70""]" 1 Kd Kd = = 0.06±0.01 μM 60.0 [] unit_conversion 7.221848749616356 success True direct_binding SPR affinity; SALL4 ZF1-2(370–454) binding to immobilized DDB1:CRBN complexed with 5 μM pomalidomide. 2 Table 1 reports ZF1-2(370–454) with CRBN:POM: K_D 0.06±0.01 μM. Page 3 assigns the POM ZF1-2(370–454) structure to PDB 8U17. auto_single_measurement only accepted activity measurement [1] 1 structures\8U17\8U17_metadata.json point structures/8U17/8u17_protein.pdb structures/8U17/8u17_pocket.pdb structures/8U17/8u17_ligand.sdf structures/8U17/8u17_ligand.pdb structures/8U17/8u17_ligand.cif structures/8U17/8u17_complex.pdb structures/8U17/8u17_complex.cif 8U19 classic SyoA (CYP255) Amycolatopsis thermoflava N1165 Na Na syringol "[""3DM""]" 1 Kd Kd = = 16 ± 1 µM 16000.0 [] unit_conversion 4.795880017344075 success True direct_binding SyoA–syringol binding affinity determined by UV-Vis spectral titration; data fitted to a hyperbolic binding equation. 5 Binding analysis reported that syringol binds SyoA with K_D = 16 ± 1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U19\8U19_metadata.json point structures/8U19/8u19_protein.pdb structures/8U19/8u19_pocket.pdb structures/8U19/8u19_ligand.sdf structures/8U19/8u19_ligand.pdb structures/8U19/8u19_ligand.cif structures/8U19/8u19_complex.pdb structures/8U19/8u19_complex.cif 8U1I classic SyoA (CYP255) Amycolatopsis thermoflava N1165 Na Na 4-methylsyringol "[""UB9""]" 1 Kd Kd = = 7.2 ± 0.2 µM 7200.0 [] unit_conversion 5.142667503568731 success True direct_binding SyoA–4-methylsyringol binding affinity determined by UV-Vis spectral titration; data fitted to a hyperbolic binding equation. 5 Binding analysis reported that 4-methylsyringol binds SyoA with K_D = 7.2 ± 0.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U1I\8U1I_metadata.json point structures/8U1I/8u1i_protein.pdb structures/8U1I/8u1i_pocket.pdb structures/8U1I/8u1i_ligand.sdf structures/8U1I/8u1i_ligand.pdb structures/8U1I/8u1i_ligand.cif structures/8U1I/8u1i_complex.pdb structures/8U1I/8u1i_complex.cif 8U2D classic Bruton's tyrosine kinase Na Na Na N-[(2R)-1-[(3R)-3-(methylcarbamoyl)-1H,2H,3H,4H,9H-pyrido[3,4-b]indol-2-yl]-3-(3-methylphenyl)-1-oxopropan-2-yl]-1H-indazole-5-carboxamide "[""UQX""]" 1 Kd Kd = = 11 nM 11.0 [] unit_conversion 7.958607314841775 success True direct_binding Internal DNA-encoded library (DEL) screen; assay format otherwise not stated. 3 BTK binder E is stated to have been identified from an internal DEL screen with “Kd = 11 nM”; Figure 1 maps binder E to PDB 8U2D. auto_single_measurement only accepted activity measurement [1] 1 structures\8U2D\8U2D_metadata.json point structures/8U2D/8u2d_protein.pdb structures/8U2D/8u2d_pocket.pdb structures/8U2D/8u2d_ligand.sdf structures/8U2D/8u2d_ligand.pdb structures/8U2D/8u2d_ligand.cif structures/8U2D/8u2d_complex.pdb structures/8U2D/8u2d_complex.cif 8U2M extended P450Blt Micromonospora sp. MW-13 Na Na Biarylitide; MRYLH "[""CHAIN:D""]" 1 Kd Kd = = 2.1 µM 2100.0 [] unit_conversion 5.6777807052660805 success True direct_binding UV–visible substrate-binding assay; Table 2 reports binding of P450Blt to MRYLH–OH. 4 Table 2 lists P450Blt: Kd 2.1 µM. The text identifies the MRYLH-bound crystal structure as PDB 8U2M. auto_single_measurement only accepted activity measurement [1] 1 structures\8U2M\8U2M_metadata.json point structures/8U2M/8u2m_protein.pdb structures/8U2M/8u2m_pocket.pdb structures/8U2M/8u2m_ligand.pdb structures/8U2M/8u2m_ligand.cif structures/8U2M/8u2m_complex.pdb structures/8U2M/8u2m_complex.cif 8U36 extended Importin alpha 2 (IMPalpha2) mouse Truncated mouse IMPalpha2 lacking the autoinhibitory IMPbeta1-binding (IBB) domain Na FrAdV1 Pre-pVII NLSd peptide (PPRKRRRVA) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 49 ± 2 nM 49.0 [] unit_conversion 7.309803919971486 success True direct_binding Fluorescence-polarization assay using FITC-labelled synthetic FrAdV1 Pre-pVII NLSd peptide and purified mIMPα2ΔIBB. 8 Figure 3B reports NLSd Kd = 49 ± 2 nM for mIMPα2ΔIBB; Figure 3A shows the direct peptide-binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8U36\8U36_metadata.json point structures/8U36/8u36_protein.pdb structures/8U36/8u36_pocket.pdb structures/8U36/8u36_ligand.pdb structures/8U36/8u36_ligand.cif structures/8U36/8u36_complex.pdb structures/8U36/8u36_complex.cif 8U5M classic Sts-1 HP domain human Na Na rebamipide "[""VJX""]" 3 Ki Ki = = 2 μM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition Competitive-inhibition kinetics of purified Sts-1HP using increasing rebamipide concentrations. 4 “...suggesting that it is a competitive inhibitor with a Ki of 2 μM.” auto_metric_priority unique highest-priority metric family: Ki [3] 4 structures\8U5M\8U5M_metadata.json point structures/8U5M/8u5m_protein.pdb structures/8U5M/8u5m_pocket.pdb structures/8U5M/8u5m_ligand.sdf structures/8U5M/8u5m_ligand.pdb structures/8U5M/8u5m_ligand.cif structures/8U5M/8u5m_complex.pdb structures/8U5M/8u5m_complex.cif 8U6A classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ729 "[""VQK""]" 1 IC50 IC50 = = 0.060 ± 0.011 μM 60.0 [] unit_conversion 7.221848749616356 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT; mean ± SD. 10 Table 1 lists compound 1e IC50 = 0.060 ± 0.011 μM; the surrounding text identifies biochemical inhibition of WT HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6A\8U6A_metadata.json point structures/8U6A/8u6a_protein.pdb structures/8U6A/8u6a_pocket.pdb structures/8U6A/8u6a_ligand.sdf structures/8U6A/8u6a_ligand.pdb structures/8U6A/8u6a_ligand.cif structures/8U6A/8u6a_complex.pdb structures/8U6A/8u6a_complex.cif 8U6B classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ731; N-(4-chloro-3-(3-chloro-5-cyanophenoxy)phenethyl)acrylamide "[""VTN""]" 1 IC50 IC50 = = 0.4 ± 0.1 μM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT; mean ± SD. 12 Table 2 lists compound 2b IC50 = 0.4 ± 0.1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6B\8U6B_metadata.json point structures/8U6B/8u6b_protein.pdb structures/8U6B/8u6b_pocket.pdb structures/8U6B/8u6b_ligand.sdf structures/8U6B/8u6b_ligand.pdb structures/8U6B/8u6b_ligand.cif structures/8U6B/8u6b_complex.pdb structures/8U6B/8u6b_complex.cif 8U6C classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ732; 2-chloro-N-(4-chloro-3-(3-chloro-5-cyanophenoxy)phenethyl)acetamide "[""VWU""]" 1 IC50 IC50 = = 0.75 ± 0.35 μM 750.0 [] unit_conversion 6.1249387366083 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT; mean ± SD. 12 Table 2 lists compound 2c IC50 = 0.75 ± 0.35 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6C\8U6C_metadata.json point structures/8U6C/8u6c_protein.pdb structures/8U6C/8u6c_pocket.pdb structures/8U6C/8u6c_ligand.sdf structures/8U6C/8u6c_ligand.pdb structures/8U6C/8u6c_ligand.cif structures/8U6C/8u6c_complex.pdb structures/8U6C/8u6c_complex.cif 8U6D classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ736; N-(2-(4-chloro-3-(3-chloro-5-cyanophenoxy)phenoxy)ethyl)-N-methylacrylamide "[""VTS""]" 1 IC50 IC50 = = 0.75 ± 0.45 μM 750.0 [] unit_conversion 6.1249387366083 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT; mean ± SD. 12 Table 2 lists compound 2i IC50 = 0.75 ± 0.45 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6D\8U6D_metadata.json point structures/8U6D/8u6d_protein.pdb structures/8U6D/8u6d_pocket.pdb structures/8U6D/8u6d_ligand.sdf structures/8U6D/8u6d_ligand.pdb structures/8U6D/8u6d_ligand.cif structures/8U6D/8u6d_complex.pdb structures/8U6D/8u6d_complex.cif 8U6E classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ738; N-(4-chloro-3-(3-chloro-5-cyanophenoxy)phenethyl)-N-methylacrylamide "[""VTV""]" 1 IC50 IC50 = = 0.5 μM 500.0 [] unit_conversion 6.301029995663981 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT. 12 Table 2 lists compound 2d IC50 = 0.5 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6E\8U6E_metadata.json point structures/8U6E/8u6e_protein.pdb structures/8U6E/8u6e_pocket.pdb structures/8U6E/8u6e_ligand.sdf structures/8U6E/8u6e_ligand.pdb structures/8U6E/8u6e_ligand.cif structures/8U6E/8u6e_complex.pdb structures/8U6E/8u6e_complex.cif 8U6F classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ742; N-(2-(5-chloro-2-(3-chloro-5-cyanophenoxy)phenoxy)ethyl)-N-methylacrylamide "[""VU8""]" 1 IC50 IC50 = = 0.06 μM 60.0 [] unit_conversion 7.221848749616356 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT. 10 Table 1 lists compound 1i IC50 = 0.06 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6F\8U6F_metadata.json point structures/8U6F/8u6f_protein.pdb structures/8U6F/8u6f_pocket.pdb structures/8U6F/8u6f_ligand.sdf structures/8U6F/8u6f_ligand.pdb structures/8U6F/8u6f_ligand.cif structures/8U6F/8u6f_complex.pdb structures/8U6F/8u6f_complex.cif 8U6K classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ747; N-(2-(2-((6-cyanonaphthalen-1-yl)oxy)phenoxy)ethyl)-N-methylacrylamide "[""VRF""]" 1 IC50 IC50 < < 0.01 μM 10.0 [] unit_conversion 8.0 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT. 10 Table 1 lists compound 1l IC50 < 0.01 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6K\8U6K_metadata.json point structures/8U6K/8u6k_protein.pdb structures/8U6K/8u6k_pocket.pdb structures/8U6K/8u6k_ligand.sdf structures/8U6K/8u6k_ligand.pdb structures/8U6K/8u6k_ligand.cif structures/8U6K/8u6k_complex.pdb structures/8U6K/8u6k_complex.cif 8U6L classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ748; N-(2-(5-chloro-2-((6-cyanonaphthalen-1-yl)oxy)phenoxy)ethyl)-N-methylacrylamide "[""VRQ""]" 1 IC50 IC50 = = 0.025 ± 0.01 μM 25.0 [] unit_conversion 7.6020599913279625 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT; mean ± SD. 10 Table 1 lists compound 1k IC50 = 0.025 ± 0.01 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6L\8U6L_metadata.json point structures/8U6L/8u6l_protein.pdb structures/8U6L/8u6l_pocket.pdb structures/8U6L/8u6l_ligand.sdf structures/8U6L/8u6l_ligand.pdb structures/8U6L/8u6l_ligand.cif structures/8U6L/8u6l_complex.pdb structures/8U6L/8u6l_complex.cif 8U6N classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ752; 3-(2-((6-cyanonaphthalen-1-yl)oxy)phenoxy)-N,N-dimethylpropanamide "[""VWK""]" 1 IC50 IC50 = = 0.02 ± 0.01 μM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT; mean ± SD. 13 Table 3 lists compound 3a IC50 = 0.02 ± 0.01 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6N\8U6N_metadata.json point structures/8U6N/8u6n_protein.pdb structures/8U6N/8u6n_pocket.pdb structures/8U6N/8u6n_ligand.sdf structures/8U6N/8u6n_ligand.pdb structures/8U6N/8u6n_ligand.cif structures/8U6N/8u6n_complex.pdb structures/8U6N/8u6n_complex.cif 8U6O classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 RT52A wild-type (WT) JLJ753; 5-(2-(3-oxo-3-(pyrrolidin-1-yl)propoxy)phenoxy)-2-naphthonitrile "[""VWB""]" 1 IC50 IC50 = = 0.02 ± 0.01 μM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition PicoGreen biochemical inhibition assay against WT HIV-1 RT; mean ± SD. 13 Table 3 lists compound 3b IC50 = 0.02 ± 0.01 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6O\8U6O_metadata.json point structures/8U6O/8u6o_protein.pdb structures/8U6O/8u6o_pocket.pdb structures/8U6O/8u6o_ligand.sdf structures/8U6O/8u6o_ligand.pdb structures/8U6O/8u6o_ligand.cif structures/8U6O/8u6o_complex.pdb structures/8U6O/8u6o_complex.cif 8U6P classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 (HIV-1) recombinant RT52A enzyme wild-type compound 3c (JLJ754) "[""VOI""]" 1 IC50 IC50 = = 0.02 ± 0.01 µM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition PicoGreen biochemical assay of purified WT HIV-1 RT catalytic activity; Table 3 reports compound 3c. 13 Table 3 lists compound 3c with IC50 = 0.02 ± 0.01 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6P\8U6P_metadata.json point structures/8U6P/8u6p_protein.pdb structures/8U6P/8u6p_pocket.pdb structures/8U6P/8u6p_ligand.sdf structures/8U6P/8u6p_ligand.pdb structures/8U6P/8u6p_ligand.cif structures/8U6P/8u6p_complex.pdb structures/8U6P/8u6p_complex.cif 8U6Q classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 (HIV-1) recombinant RT52A enzyme wild-type compound 3d (JLJ755) "[""VOU""]" 1 IC50 IC50 = = 0.02 ± 0.01 µM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition PicoGreen biochemical assay of purified WT HIV-1 RT catalytic activity; Table 3 reports compound 3d. 13 Table 3 lists compound 3d with IC50 = 0.02 ± 0.01 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6Q\8U6Q_metadata.json point structures/8U6Q/8u6q_protein.pdb structures/8U6Q/8u6q_pocket.pdb structures/8U6Q/8u6q_ligand.sdf structures/8U6Q/8u6q_ligand.pdb structures/8U6Q/8u6q_ligand.cif structures/8U6Q/8u6q_complex.pdb structures/8U6Q/8u6q_complex.cif 8U6R classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 (HIV-1) recombinant RT52A enzyme wild-type compound 3e (JLJ756) "[""VP2""]" 1 IC50 IC50 = = 1.3 ± 1 µM 1300.0 [] unit_conversion 5.886056647693163 success True biochemical_inhibition PicoGreen biochemical assay of purified WT HIV-1 RT catalytic activity; Table 3 reports compound 3e. 13 Table 3 lists compound 3e with IC50 = 1.3 ± 1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6R\8U6R_metadata.json point structures/8U6R/8u6r_protein.pdb structures/8U6R/8u6r_pocket.pdb structures/8U6R/8u6r_ligand.sdf structures/8U6R/8u6r_ligand.pdb structures/8U6R/8u6r_ligand.cif structures/8U6R/8u6r_complex.pdb structures/8U6R/8u6r_complex.cif 8U6S classic HIV-1 reverse transcriptase Human immunodeficiency virus type 1 (HIV-1) recombinant RT52A enzyme wild-type compound 3f (JLJ757) "[""VPB""]" 1 IC50 IC50 = = 0.06 ± 0.01 µM 60.0 [] unit_conversion 7.221848749616356 success True biochemical_inhibition PicoGreen biochemical assay of purified WT HIV-1 RT catalytic activity; Table 3 reports compound 3f. 13 Table 3 lists compound 3f with IC50 = 0.06 ± 0.01 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U6S\8U6S_metadata.json point structures/8U6S/8u6s_protein.pdb structures/8U6S/8u6s_pocket.pdb structures/8U6S/8u6s_ligand.sdf structures/8U6S/8u6s_ligand.pdb structures/8U6S/8u6s_ligand.cif structures/8U6S/8u6s_complex.pdb structures/8U6S/8u6s_complex.cif 8U77 extended Taf14 Saccharomyces cerevisiae Taf14_ET residues 168-243 in complex with a synthetic Yng1_EBM peptide Na Na "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H""]" 1 Kd Kd = = 0.6 ± 0.2 μM 600.0 [] unit_conversion 6.221848749616356 success True direct_binding Tryptophan fluorescence binding curve for Taf14_ET with synthetic Yng1_EBM peptide; 1:1 stoichiometry. 2 Fig. 1g reports Taf14_ET + Yng1_EBM, Kd = 0.6 ± 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8U77\8U77_metadata.json point structures/8U77/8u77_protein.pdb structures/8U77/8u77_pocket.pdb structures/8U77/8u77_ligand.pdb structures/8U77/8u77_ligand.cif structures/8U77/8u77_complex.pdb structures/8U77/8u77_complex.cif 8U7E classic Sts-1 HP domain human Na Na compound 11, para-ethyl derivative of rebamipide "[""VXE""]" 1 IC50 IC50 = = 8 μM 8000.0 [] unit_conversion 5.096910013008056 success True biochemical_inhibition Initial SAR-library IC50 summary against Sts-1HP. 26 Figure 3 labels “11: R = CH2CH3: 8 μM”; its caption states that IC50 values are against Sts-1HP. auto_single_measurement only accepted activity measurement [1] 1 structures\8U7E\8U7E_metadata.json point structures/8U7E/8u7e_protein.pdb structures/8U7E/8u7e_pocket.pdb structures/8U7E/8u7e_ligand.sdf structures/8U7E/8u7e_ligand.pdb structures/8U7E/8u7e_ligand.cif structures/8U7E/8u7e_complex.pdb structures/8U7E/8u7e_complex.cif 8U7W classic SHP2 Na Na Na compound 7 "[""W8I""]" 1 IC50 IC50 = = 47 nM 47.0 [] unit_conversion 7.327902142064282 success True biochemical_inhibition SHP2 enzymatic inhibition assay; Table 1. 2 Figure 4 identifies PDB 8U7W as SHP2 with compound 7; Table 1 reports SHP2 IC50 = 47 nM for compound 7. auto_single_measurement only accepted activity measurement [1] 1 structures\8U7W\8U7W_metadata.json point structures/8U7W/8u7w_protein.pdb structures/8U7W/8u7w_pocket.pdb structures/8U7W/8u7w_ligand.sdf structures/8U7W/8u7w_ligand.pdb structures/8U7W/8u7w_ligand.cif structures/8U7W/8u7w_complex.pdb structures/8U7W/8u7w_complex.cif 8U7X classic SHP2 Na Na Na compound 24 "[""WAB""]" 1 IC50 IC50 = = 72 nM 72.0 [] unit_conversion 7.142667503568731 success True biochemical_inhibition SHP2 enzymatic inhibition assay; Table 3. 4 Figure 6 identifies PDB 8U7X as SHP2 with compound 24; Table 3 reports SHP2 IC50 = 72 nM for compound 24. auto_single_measurement only accepted activity measurement [1] 1 structures\8U7X\8U7X_metadata.json point structures/8U7X/8u7x_protein.pdb structures/8U7X/8u7x_pocket.pdb structures/8U7X/8u7x_ligand.sdf structures/8U7X/8u7x_ligand.pdb structures/8U7X/8u7x_ligand.cif structures/8U7X/8u7x_complex.pdb structures/8U7X/8u7x_complex.cif 8U8J classic phosphorylated ERK2 human His6-2P-ERK2 Na ERK1/2 inhibitor #16 "[""WAL""]" 1 Ki Ki = = 0.03 nM 0.03 [] unit_conversion 10.522878745280337 success True biochemical_inhibition Aggregate kinase assay measuring phosphorylation of fluorescent Omnia peptide substrate; Figure 4 states Ki estimates were measured using kinase assays. 9 Figure 4A visibly prints “Inhibitor #16 Ki = 0.03 nM”; its caption states these Ki estimates were measured using kinase assays for phosphorylation of Omnia peptide substrate. auto_single_measurement only accepted activity measurement [1] 1 structures\8U8J\8U8J_metadata.json point structures/8U8J/8u8j_protein.pdb structures/8U8J/8u8j_pocket.pdb structures/8U8J/8u8j_ligand.sdf structures/8U8J/8u8j_ligand.pdb structures/8U8J/8u8j_ligand.cif structures/8U8J/8u8j_complex.pdb structures/8U8J/8u8j_complex.cif 8U8K classic phosphorylated ERK2 human His6-2P-ERK2 Na ERK1/2 inhibitor #8 "[""W8U""]" 1 Ki Ki = = 0.05 nM 0.05 [] unit_conversion 10.301029995663981 success True biochemical_inhibition Aggregate kinase assay measuring phosphorylation of fluorescent Omnia peptide substrate; Figure 4 states Ki estimates were measured using kinase assays. 9 Figure 4A visibly prints “Inhibitor #8 Ki = 0.05 nM”; its caption states these Ki estimates were measured using kinase assays for phosphorylation of Omnia peptide substrate. auto_single_measurement only accepted activity measurement [1] 1 structures\8U8K\8U8K_metadata.json point structures/8U8K/8u8k_protein.pdb structures/8U8K/8u8k_pocket.pdb structures/8U8K/8u8k_ligand.sdf structures/8U8K/8u8k_ligand.pdb structures/8U8K/8u8k_ligand.cif structures/8U8K/8u8k_complex.pdb structures/8U8K/8u8k_complex.cif 8UC9 classic SOS2 Na SOS2SB Na compound 9 "[""QBC""]" 1 Kd Kd = = 330 µM 330000.0 [] unit_conversion 3.481486060122113 success True direct_binding SPR; SOS2 SPR K_D reported in Table 1. 4 Table 1 reports compound 9: SOS2 SPR K_D 330 µM; PDB code 8UC9. auto_single_measurement only accepted activity measurement [1] 1 structures\8UC9\8UC9_metadata.json point structures/8UC9/8uc9_protein.pdb structures/8UC9/8uc9_pocket.pdb structures/8UC9/8uc9_ligand.sdf structures/8UC9/8uc9_ligand.pdb structures/8UC9/8uc9_ligand.cif structures/8UC9/8uc9_complex.pdb structures/8UC9/8uc9_complex.cif 8UDP classic SARS-CoV-2 3CL protease SARS-CoV-2 Na Na 14 "[""WBO""]" 1 IC50 IC50 = = 0.01 µM 10.0 [] unit_conversion 8.0 success True biochemical_inhibition Purified 3CL protease fluorogenic-substrate biochemical assay. 8 Fig. 6 prints compound 14 IC50 = 0.01 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8UDP\8UDP_metadata.json point structures/8UDP/8udp_protein.pdb structures/8UDP/8udp_pocket.pdb structures/8UDP/8udp_ligand.sdf structures/8UDP/8udp_ligand.pdb structures/8UDP/8udp_ligand.cif structures/8UDP/8udp_complex.pdb structures/8UDP/8udp_complex.cif 8UDY classic SARS-CoV-2 3CL protease SARS-CoV-2 Na Na 25 "[""WD6""]" 1 IC50 IC50 = = 0.1 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition Purified 3CL protease fluorogenic-substrate biochemical assay. 10 Fig. 8 prints compound 25 IC50 = 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8UDY\8UDY_metadata.json point structures/8UDY/8udy_protein.pdb structures/8UDY/8udy_pocket.pdb structures/8UDY/8udy_ligand.sdf structures/8UDY/8udy_ligand.pdb structures/8UDY/8udy_ligand.cif structures/8UDY/8udy_complex.pdb structures/8UDY/8udy_complex.cif 8UFW classic hCA IX-mimic Na hCA IX-mimic Na Na "[""WJN""]" 1 Ki Ki = = 6.2 nM 6.2 [] unit_conversion 8.207608310501746 success True biochemical_inhibition In vitro CA inhibition; reported for the transmembrane, tumor-associated CA IX isoform. 3 “FC-531 displayed high inhibition potencies for the transmembrane and tumor-associated isoforms CA IX and CA XII (i.e. KIs = 6.2 nM and 2.3 nM, respectively; Table S1).” Fig. 1 assigns FC-531 bound to hCA IX-mimic to PDB 8UFW. auto_single_measurement only accepted activity measurement [1] 1 structures\8UFW\8UFW_metadata.json point structures/8UFW/8ufw_protein.pdb structures/8UFW/8ufw_pocket.pdb structures/8UFW/8ufw_ligand.sdf structures/8UFW/8ufw_ligand.pdb structures/8UFW/8ufw_ligand.cif structures/8UFW/8ufw_complex.pdb structures/8UFW/8ufw_complex.cif 8UFX classic hCA II Na Na Na Na "[""WJN""]" 1 Ki Ki = = 9.7 nM 9.7 [] unit_conversion 8.013228265733755 success True biochemical_inhibition In vitro CA inhibition; hCA II is described as a physiologically relevant isoform. 3 “FC-531 showed remarkable efficacy in inhibiting the hCA II isoform (KI = 9.7 nM).” Fig. 1 assigns FC-531 bound to hCA II to PDB 8UFX. auto_single_measurement only accepted activity measurement [1] 1 structures\8UFX\8UFX_metadata.json point structures/8UFX/8ufx_protein.pdb structures/8UFX/8ufx_pocket.pdb structures/8UFX/8ufx_ligand.sdf structures/8UFX/8ufx_ligand.pdb structures/8UFX/8ufx_ligand.cif structures/8UFX/8ufx_complex.pdb structures/8UFX/8ufx_complex.cif 8UG1 classic hKHK-C human Na Na compound 13 "[""WNH""]" 1 IC50 IC50 = = 134 ± 114 nM 134.0 [] unit_conversion 6.872895201635192 success True biochemical_inhibition Human KHK-C enzyme activity assay; Table 1 in vitro activity. 7 Table 1 reports compound 13 hKHK-C IC50 = 134 ± 114 nM. The paper states that hKHK-C–compound 13 coordinates were deposited as 8UG1. auto_single_measurement only accepted activity measurement [1] 1 structures\8UG1\8UG1_metadata.json point structures/8UG1/8ug1_protein.pdb structures/8UG1/8ug1_pocket.pdb structures/8UG1/8ug1_ligand.sdf structures/8UG1/8ug1_ligand.pdb structures/8UG1/8ug1_ligand.cif structures/8UG1/8ug1_complex.pdb structures/8UG1/8ug1_complex.cif 8UG3 classic hKHK-C human Na Na compound 23 "[""WRE""]" 1 IC50 IC50 = = 20 ± 8 nM 20.0 [] unit_conversion 7.698970004336019 success True biochemical_inhibition Human KHK-C enzyme activity assay; Table 1 in vitro activity. 7 Table 1 reports compound 23 hKHK-C IC50 = 20 ± 8 nM. The paper states that hKHK-C–compound 23 coordinates were deposited as 8UG3. auto_single_measurement only accepted activity measurement [1] 1 structures\8UG3\8UG3_metadata.json point structures/8UG3/8ug3_protein.pdb structures/8UG3/8ug3_pocket.pdb structures/8UG3/8ug3_ligand.sdf structures/8UG3/8ug3_ligand.pdb structures/8UG3/8ug3_ligand.cif structures/8UG3/8ug3_complex.pdb structures/8UG3/8ug3_complex.cif 8UGU classic BRD2 human (Homo sapiens) Na wild-type 4IND "[""59E""]" 1 Kd Kd = = 61±67 nM 61.0 [] unit_conversion 7.214670164989233 success True direct_binding SPR binding measurement in Table 1. 3 Table 1 reports 4IND K_D = 61±67 nM for BRD2-BD2, determined by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\8UGU\8UGU_metadata.json point structures/8UGU/8ugu_protein.pdb structures/8UGU/8ugu_pocket.pdb structures/8UGU/8ugu_ligand.sdf structures/8UGU/8ugu_ligand.pdb structures/8UGU/8ugu_ligand.cif structures/8UGU/8ugu_complex.pdb structures/8UGU/8ugu_complex.cif 8UGV classic BRD2 human (Homo sapiens) Na wild-type 6IND "[""WNX""]" 1 Kd Kd = = 93±67 nM 93.0 [] unit_conversion 7.031517051446065 success True direct_binding SPR binding measurement in Table 1. 3 Table 1 reports 6IND K_D = 93±67 nM for BRD2-BD2, determined by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\8UGV\8UGV_metadata.json point structures/8UGV/8ugv_protein.pdb structures/8UGV/8ugv_pocket.pdb structures/8UGV/8ugv_ligand.sdf structures/8UGV/8ugv_ligand.pdb structures/8UGV/8ugv_ligand.cif structures/8UGV/8ugv_complex.pdb structures/8UGV/8ugv_complex.cif 8UH0 classic SOS2 Na SOS2SB Na compound 10 "[""WRN""]" 1 Kd Kd = = 730 µM 730000.0 [] unit_conversion 3.136677139879544 success True direct_binding SPR; SOS2 SPR K_D reported in Table 1. 4 Table 1 reports compound 10: SOS2 SPR K_D 730 µM; PDB code 8UH0. auto_single_measurement only accepted activity measurement [1] 1 structures\8UH0\8UH0_metadata.json point structures/8UH0/8uh0_protein.pdb structures/8UH0/8uh0_pocket.pdb structures/8UH0/8uh0_ligand.sdf structures/8UH0/8uh0_ligand.pdb structures/8UH0/8uh0_ligand.cif structures/8UH0/8uh0_complex.pdb structures/8UH0/8uh0_complex.cif 8UIQ classic 6-hydroxynicotinic acid 3-monooxygenase (NicC) Pseudomonas putida H47Q NicC variant H47Q 2-mercaptopyridine (2-MP) "[""PYS""]" 1 Kd Kd = = 2.0 ± 1.8 mM 2000000.0 [] unit_conversion 2.6989700043360187 success True direct_binding Equilibrium titration of H47Q NicC (30 μM) with 2-MP; binding was monitored by the flavin absorbance change at 450 nm and fit to a hyperbolic binding equation. 20 Figure 2B states that equilibrium titrations of the H47Q NicC variant with 2-MP estimate a Kd for E·2-MP of 2.0 ± 1.8 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\8UIQ\8UIQ_metadata.json point structures/8UIQ/8uiq_protein.pdb structures/8UIQ/8uiq_pocket.pdb structures/8UIQ/8uiq_ligand.sdf structures/8UIQ/8uiq_ligand.pdb structures/8UIQ/8uiq_ligand.cif structures/8UIQ/8uiq_complex.pdb structures/8UIQ/8uiq_complex.cif 8UJY classic human WD repeat-containing protein 5 (WDR5) human WDR5 residues 22-334 expressed with an N-terminal 6xHis-SUMO tag; the tag was cleaved during dialysis Na compound 8 "[""VV3""]" 1 Ki Ki = = 0.023 ± 0.001 nM 0.023 [] unit_conversion 10.638272163982407 success True direct_binding TR-FRET binding assay 4 Table 1 reports compound 8 TR-FRET Ki (WDR5) = 0.023 ± 0.001 nM. The table footnote states TR-FRET Ki values represent four independent replicate determinations ± standard deviation. auto_single_measurement only accepted activity measurement [1] 1 structures\8UJY\8UJY_metadata.json point structures/8UJY/8ujy_protein.pdb structures/8UJY/8ujy_pocket.pdb structures/8UJY/8ujy_ligand.sdf structures/8UJY/8ujy_ligand.pdb structures/8UJY/8ujy_ligand.cif structures/8UJY/8ujy_complex.pdb structures/8UJY/8ujy_complex.cif 8UK5 extended ATAD2B Homo sapiens ATAD2B bromodomain-containing protein, residues 953-1085 Na H4S1phK5ac (residues 1-15) "[""CHAIN:B""]" 1 Kd Kd = = 84.2 ± 13.1 µM 84200.0 [] unit_conversion 4.0746879085003505 success True direct_binding ITC measurement of ATAD2B BRD binding to H4S1phK5ac peptide. 31 Table 1 lists H4S1phK5ac (1-15): KD for ATAD2B = 84.2 ± 13.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8UK5\8UK5_metadata.json point structures/8UK5/8uk5_protein.pdb structures/8UK5/8uk5_pocket.pdb structures/8UK5/8uk5_ligand.pdb structures/8UK5/8uk5_ligand.cif structures/8UK5/8uk5_complex.pdb structures/8UK5/8uk5_complex.cif 8UKO extended cAMP-dependent protein kinase A catalytic subunit alpha (PKAc alpha) mouse PKAc alpha residues 16-351 (pET28HMT-PKAc alpha16-351) with N-terminal 6xHis-MBP-TEV expression tag Na CaV1.2 Ser1981 peptide (RGFLRSASLGRRASFHL) "[""CHAIN:C""]" 1 Kd Kd = = 34 ± 4 µM 34000.0 [] unit_conversion 4.468521082957745 success True direct_binding ITC titration of CaV1.2 Ser1981 peptide into PKAc in the presence of AMP-PNP and Mg2+. 4 Table 3 reports CaV1.2 S1981 peptide Kd = 34 ± 4 µM; the text states binding was detected when the Ser1981 peptide was titrated into PKAc. auto_single_measurement only accepted activity measurement [1] 1 structures\8UKO\8UKO_metadata.json point structures/8UKO/8uko_protein.pdb structures/8UKO/8uko_pocket.pdb structures/8UKO/8uko_ligand.pdb structures/8UKO/8uko_ligand.cif structures/8UKO/8uko_complex.pdb structures/8UKO/8uko_complex.cif 8UKP extended cAMP-dependent protein kinase A catalytic subunit alpha (PKAc alpha) mouse PKAc alpha residues 16-351 (pET28HMT-PKAc alpha16-351) with N-terminal 6xHis-MBP-TEV expression tag Na CaV1.2 Ser1981 peptide (RGFLRSASLGRRASFHL) "[""CHAIN:C""]" 1 Kd Kd = = 34 ± 4 µM 34000.0 [] unit_conversion 4.468521082957745 success True direct_binding ITC titration of CaV1.2 Ser1981 peptide into PKAc in the presence of AMP-PNP and Mg2+. 4 Table 3 reports CaV1.2 S1981 peptide Kd = 34 ± 4 µM; the text states binding was detected when the Ser1981 peptide was titrated into PKAc. auto_single_measurement only accepted activity measurement [1] 1 structures\8UKP\8UKP_metadata.json point structures/8UKP/8ukp_protein.pdb structures/8UKP/8ukp_pocket.pdb structures/8UKP/8ukp_ligand.pdb structures/8UKP/8ukp_ligand.cif structures/8UKP/8ukp_complex.pdb structures/8UKP/8ukp_complex.cif 8UMG classic chromodomains of human CHD1 human tandem chromodomains of CHD1 Na UNC10142 "[""X31""]" 2 Kd Kd = = 4.3 ± 0.4 μM 4300.0 [] unit_conversion 5.366531544420413 success True direct_binding Isothermal titration calorimetry (ITC) confirmation of UNC10142 binding to CHD1 tandem chromodomains. 8 Using ITC as an orthogonal assay, the authors confirmed UNC10142 binding to the tandem chromodomains of CHD1 (Kd = 4.3 ± 0.4 μM; Figure 3B). auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8UMG\8UMG_metadata.json point structures/8UMG/8umg_protein.pdb structures/8UMG/8umg_pocket.pdb structures/8UMG/8umg_ligand.sdf structures/8UMG/8umg_ligand.pdb structures/8UMG/8umg_ligand.cif structures/8UMG/8umg_complex.pdb structures/8UMG/8umg_complex.cif 8UN3 classic KRAS Na Na G13D Cpd5 "[""XOI""]" 1 IC50 IC50 = = 0.63 μM 630.0 [] unit_conversion 6.200659450546418 success True biochemical_inhibition Paired recombinant KRAS G13D and WT KRAS TR-FRET assays monitoring inhibition of GDP exchange; biochemical IC50. 2 “An evaluation of 5 in paired KRAS G13D and WT KRAS TR-FRET assays using recombinant proteins to monitor inhibition of GDP exchange revealed a biochemical IC50 of 0.63 μM for KRAS G13D.” auto_single_measurement only accepted activity measurement [1] 1 structures\8UN3\8UN3_metadata.json point structures/8UN3/8un3_protein.pdb structures/8UN3/8un3_pocket.pdb structures/8UN3/8un3_ligand.sdf structures/8UN3/8un3_ligand.pdb structures/8UN3/8un3_ligand.cif structures/8UN3/8un3_complex.pdb structures/8UN3/8un3_complex.cif 8UN4 classic KRAS Na Na G13D Cpd36 "[""XV3""]" 1 IC50 IC50 = = 0.52 nM 0.52 [] unit_conversion 9.2839966563652 success True biochemical_inhibition KRAS G13D GDP HTRF biochemical IC50; selectivity over WT reported as 9.2×. 4 Table 3 reports for compound 36: “KRAS G13D GDP IC50/nM (Selectivity over WT)” = “0.52 (9.2x)”; the footnote defines this as KRAS G13D GDP HTRF IC50. auto_single_measurement only accepted activity measurement [1] 1 structures\8UN4\8UN4_metadata.json point structures/8UN4/8un4_protein.pdb structures/8UN4/8un4_pocket.pdb structures/8UN4/8un4_ligand.sdf structures/8UN4/8un4_ligand.pdb structures/8UN4/8un4_ligand.cif structures/8UN4/8un4_complex.pdb structures/8UN4/8un4_complex.cif 8UN5 classic KRAS Na Na G13D Cpd38 "[""XQ6""]" 1 IC50 IC50 = = 0.69 nM 0.69 [] unit_conversion 9.161150909262744 success True biochemical_inhibition KRAS G13D GDP HTRF biochemical IC50; selectivity over WT reported as 11×. 4 Table 3 reports for compound 38: “KRAS G13D GDP IC50/nM (Selectivity over WT)” = “0.69 (11x)”; the footnote defines this as KRAS G13D GDP HTRF IC50. auto_single_measurement only accepted activity measurement [1] 1 structures\8UN5\8UN5_metadata.json point structures/8UN5/8un5_protein.pdb structures/8UN5/8un5_pocket.pdb structures/8UN5/8un5_ligand.sdf structures/8UN5/8un5_ligand.pdb structures/8UN5/8un5_ligand.cif structures/8UN5/8un5_complex.pdb structures/8UN5/8un5_complex.cif 8UO8 classic synaptic vesicle protein 2B Na Na Na padsevonil "[""X3U""]" 2 Kd Kd = = 31 ± 3 nM 31.0 [] unit_conversion 7.508638306165727 success True direct_binding SV2B 3H-PSL direct-binding experiment; mean ± SEM, two independent experiments, n=48. 7 Supplementary Table 4 reports “SV2B 3H-PSL Kd” as “31 ± 3 nM” (Fig. 4c). auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8UO8\8UO8_metadata.json point structures/8UO8/8uo8_protein.pdb structures/8UO8/8uo8_pocket.pdb structures/8UO8/8uo8_ligand.sdf structures/8UO8/8uo8_ligand.pdb structures/8UO8/8uo8_ligand.cif structures/8UO8/8uo8_complex.pdb structures/8UO8/8uo8_complex.cif 8UPZ classic Sinorhizobium meliloti proline utilization A (SmPutA) Sinorhizobium meliloti Minimal PutA proline dehydrogenase domain (design #2), SmPutADeltaalpha2; residues 26-83 and 190-522 connected by an SSGS linker alpha2 deletion 1a; (Prop-2-ynylthio)acetic acid "[""X79""]" 1 Ki Ki = = 1.03 ± 0.09 mM 1030000.0 [] unit_conversion 2.987162775294828 success True biochemical_inhibition Competitive inhibition of SmPutAΔα2 with L-proline as variable substrate. 9 Competitive inhibition constant (Ki) of 1.03 ± 0.09 mM for 1a. auto_single_measurement only accepted activity measurement [1] 1 structures\8UPZ\8UPZ_metadata.json point structures/8UPZ/8upz_protein.pdb structures/8UPZ/8upz_pocket.pdb structures/8UPZ/8upz_ligand.sdf structures/8UPZ/8upz_ligand.pdb structures/8UPZ/8upz_ligand.cif structures/8UPZ/8upz_complex.pdb structures/8UPZ/8upz_complex.cif 8UQ0 classic Sinorhizobium meliloti proline utilization A (SmPutA) Sinorhizobium meliloti Minimal PutA proline dehydrogenase domain (design #2), SmPutADeltaalpha2; residues 26-83 and 190-522 connected by an SSGS linker alpha2 deletion 1b; 2-(Cyanomethylthio)acetic acid "[""X7K""]" 1 Ki Ki = = 7.0 ± 0.6 mM 7000000.0 [] unit_conversion 2.154901959985743 success True biochemical_inhibition Competitive inhibition of SmPutAΔα2 with L-proline as variable substrate. 9 Competitive inhibition constant (Ki) of 7.0 ± 0.6 mM for 1b. auto_single_measurement only accepted activity measurement [1] 1 structures\8UQ0\8UQ0_metadata.json point structures/8UQ0/8uq0_protein.pdb structures/8UQ0/8uq0_pocket.pdb structures/8UQ0/8uq0_ligand.sdf structures/8UQ0/8uq0_ligand.pdb structures/8UQ0/8uq0_ligand.cif structures/8UQ0/8uq0_complex.pdb structures/8UQ0/8uq0_complex.cif 8UQ1 classic Sinorhizobium meliloti proline utilization A (SmPutA) Sinorhizobium meliloti Minimal PutA proline dehydrogenase domain (design #2), SmPutADeltaalpha2; residues 26-83 and 190-522 connected by an SSGS linker alpha2 deletion 2a; (Allylthio)acetic acid "[""X7Q""]" 1 Ki Ki = = 8 ± 1 mM 8000000.0 [] unit_conversion 2.0969100130080562 success True biochemical_inhibition Competitive inhibition of SmPutAΔα2 with L-proline as variable substrate. 9 Competitive inhibition constant (Ki) of 8 ± 1 mM for 2a. auto_single_measurement only accepted activity measurement [1] 1 structures\8UQ1\8UQ1_metadata.json point structures/8UQ1/8uq1_protein.pdb structures/8UQ1/8uq1_pocket.pdb structures/8UQ1/8uq1_ligand.sdf structures/8UQ1/8uq1_ligand.pdb structures/8UQ1/8uq1_ligand.cif structures/8UQ1/8uq1_complex.pdb structures/8UQ1/8uq1_complex.cif 8UQH classic PRMT4 Na PRMT4 catalytic core, residues 140-480 Na YD1130 (YD-1130) "[""X9L""]" 2 Kd Kd = = 188 ± 41.7 nM 188.0 [] unit_conversion 6.7258421507363195 success True direct_binding Isothermal titration calorimetry of YD1130 binding purified PRMT4 catalytic core (residues 140–480); duplicate experiment. 10 Figure 9c caption states representative ITC data of YD1130 bound to PRMT4 (140–480 aa), and the figure prints Kd = 188 ± 41.7 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8UQH\8UQH_metadata.json point structures/8UQH/8uqh_protein.pdb structures/8UQH/8uqh_pocket.pdb structures/8UQH/8uqh_ligand.sdf structures/8UQH/8uqh_ligand.pdb structures/8UQH/8uqh_ligand.cif structures/8UQH/8uqh_complex.pdb structures/8UQH/8uqh_complex.cif 8UQY classic PTE-R18 (round 18 arylesterase variant of phosphotriesterase) Pseudomonas diminuta PTE-R18 H254R; D233E; F306I; I274S; T172I; S269T; M138I; T199I; L272M; A80V; S111R; A204G; L130V; L271F; A49V; K77E; L140M; I313F Eu(III) "[""EU3""]" 1 Kd Kd = = 11 μM 11000.0 [] unit_conversion 4.958607314841775 success True direct_binding Isothermal titration calorimetry of apo PTE-R18 with EuCl3; fitted using the A + B ↔ AB model (N = 1). 8 ITC using apo PTE-R18 with EuCl3 gave a Kd of 11 μM (95% confidence interval 7.2–17.2 μM) for Eu(III). auto_single_measurement only accepted activity measurement [1] 1 structures\8UQY\8UQY_metadata.json point structures/8UQY/8uqy_protein.pdb structures/8UQY/8uqy_pocket.pdb structures/8UQY/8uqy_ligand.sdf structures/8UQY/8uqy_ligand.pdb structures/8UQY/8uqy_ligand.cif structures/8UQY/8uqy_complex.pdb structures/8UQY/8uqy_complex.cif 8UQZ classic PTE-R18 (round 18 arylesterase variant of phosphotriesterase) Pseudomonas diminuta PTE-R18 H254R; D233E; F306I; I274S; T172I; S269T; M138I; T199I; L272M; A80V; S111R; A204G; L130V; L271F; A49V; K77E; L140M; I313F Gd(III) "[""GD3""]" 1 Kd Kd = = 20 μM 20000.0 [] unit_conversion 4.698970004336019 success True direct_binding Isothermal titration calorimetry of apo PTE-R18 with GdCl3; fitted using the A + B ↔ AB model (N = 1). 8 ITC using apo PTE-R18 with GdCl3 gave a Kd of 20 μM (95% confidence interval 14.2–26.8 μM) for Gd(III). auto_single_measurement only accepted activity measurement [1] 1 structures\8UQZ\8UQZ_metadata.json point structures/8UQZ/8uqz_protein.pdb structures/8UQZ/8uqz_pocket.pdb structures/8UQZ/8uqz_ligand.sdf structures/8UQZ/8uqz_ligand.pdb structures/8UQZ/8uqz_ligand.cif structures/8UQZ/8uqz_complex.pdb structures/8UQZ/8uqz_complex.cif 8URT classic yeast cholinephosphotransferase 1 (yCPT1) Saccharomyces cerevisiae Full-length yCPT1 with C-terminal Protein C tag and poly-His tag Na chelerythrine "[""CTI""]" 1 IC50 IC50 = = 0.443 µM 443.0 [] unit_conversion 6.3535962737769305 success True biochemical_inhibition Chelerythrine titration against purified yCPT1; inhibition assessed by CMP released from CDP-choline in the enzyme assay. 6 “Titration of chelerythrine with yCPT1 showed an IC50 of 0.443 µM for this inhibitor.” auto_single_measurement only accepted activity measurement [1] 1 structures\8URT\8URT_metadata.json point structures/8URT/8urt_protein.pdb structures/8URT/8urt_pocket.pdb structures/8URT/8urt_ligand.sdf structures/8URT/8urt_ligand.pdb structures/8URT/8urt_ligand.cif structures/8URT/8urt_complex.pdb structures/8URT/8urt_complex.cif 8USS classic IL17A Na Na Na Compound 7 "[""XCW""]" 1 IC50 IC50 = = 4.0 µM 4000.0 [] unit_conversion 5.3979400086720375 success True biochemical_inhibition IL17A-IL17RA-Fc AlphaLISA biochemical interaction assay (AL IC50); Table 2 reports Compound 7. 5 Table 2, “Series 1 In Vitro Data”, reports Compound 7 with AL IC50 = 4.0 µM. The table footnote defines AL as the IL17A-IL17RA-Fc AlphaLISA biochemical interaction assay. PDB 8USS is explicitly deposited for IL17A complexed to Compound 7 on PDF page 36. auto_single_measurement only accepted activity measurement [1] 1 structures\8USS\8USS_metadata.json point structures/8USS/8uss_protein.pdb structures/8USS/8uss_pocket.pdb structures/8USS/8uss_ligand.sdf structures/8USS/8uss_ligand.pdb structures/8USS/8uss_ligand.cif structures/8USS/8uss_complex.pdb structures/8USS/8uss_complex.cif 8UUF classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun11941 "[""XWO""]" 2 Ki Ki = = 34.3 ± 3.0 nM 34.3 [] unit_conversion 7.464705879957229 success True biochemical_inhibition FRET enzymatic assay using Dabcyl-FTLRGG/APTKV-E(Edans) substrate. 12 Fig. 2 reports Jun11941: Ki = 34.3 ± 3.0 nM; its caption defines the FRET enzymatic assay. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8UUF\8UUF_metadata.json point structures/8UUF/8uuf_protein.pdb structures/8UUF/8uuf_pocket.pdb structures/8UUF/8uuf_ligand.sdf structures/8UUF/8uuf_ligand.pdb structures/8UUF/8uuf_ligand.cif structures/8UUF/8uuf_complex.pdb structures/8UUF/8uuf_complex.cif 8UUG classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun12303 "[""XXW""]" 2 Ki Ki = = 88.2 ± 6.0 nM 88.2 [] unit_conversion 7.054531414868181 success True biochemical_inhibition FRET enzymatic assay using Dabcyl-FTLRGG/APTKV-E(Edans) substrate. 12 Fig. 2 reports Jun12303: Ki = 88.2 ± 6.0 nM; its caption defines the FRET enzymatic assay. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8UUG\8UUG_metadata.json point structures/8UUG/8uug_protein.pdb structures/8UUG/8uug_pocket.pdb structures/8UUG/8uug_ligand.sdf structures/8UUG/8uug_ligand.pdb structures/8UUG/8uug_ligand.cif structures/8UUG/8uug_complex.pdb structures/8UUG/8uug_complex.cif 8UUH classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun12199 "[""XYI""]" 2 Ki Ki = = 47.6 ± 3.0 nM 47.6 [] unit_conversion 7.3223930472795065 success True biochemical_inhibition FRET enzymatic assay using Dabcyl-FTLRGG/APTKV-E(Edans) substrate. 12 Fig. 2 reports Jun12199: Ki = 47.6 ± 3.0 nM; its caption defines the FRET enzymatic assay. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8UUH\8UUH_metadata.json point structures/8UUH/8uuh_protein.pdb structures/8UUH/8uuh_pocket.pdb structures/8UUH/8uuh_ligand.sdf structures/8UUH/8uuh_ligand.pdb structures/8UUH/8uuh_ligand.cif structures/8UUH/8uuh_complex.pdb structures/8UUH/8uuh_complex.cif 8UUI extended Interleukin-23 (IL23) heterodimer human Human p19 (6x His-tagged) and p40 IL23 chains Na peptide 23-446 "[""CHAIN:D""]" 2 Kd Kd = = 794 nM 794.0 [] unit_conversion 6.100179497572904 success True direct_binding SPR kinetic dissociation constant for peptide binding to IL23. 3 Table 1 lists peptide 23-446 with an SPR kinetic KD of 794 nM; the table title identifies these as SPR binding affinities of experimental peptides to IL23. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8UUI\8UUI_metadata.json point structures/8UUI/8uui_protein.pdb structures/8UUI/8uui_pocket.pdb structures/8UUI/8uui_ligand.pdb structures/8UUI/8uui_ligand.cif structures/8UUI/8uui_complex.pdb structures/8UUI/8uui_complex.cif 8UUU classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun12162 "[""XYR""]" 2 Ki Ki = = 33.6 ± 3.0 nM 33.6 [] unit_conversion 7.4736607226101555 success True biochemical_inhibition FRET enzymatic assay using Dabcyl-FTLRGG/APTKV-E(Edans) substrate. 12 Fig. 2 reports Jun12162: Ki = 33.6 ± 3.0 nM; its caption defines the FRET enzymatic assay. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8UUU\8UUU_metadata.json point structures/8UUU/8uuu_protein.pdb structures/8UUU/8uuu_pocket.pdb structures/8UUU/8uuu_ligand.sdf structures/8UUU/8uuu_ligand.pdb structures/8UUU/8uuu_ligand.cif structures/8UUU/8uuu_complex.pdb structures/8UUU/8uuu_complex.cif 8UUV classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun12197 "[""Y2I""]" 2 Ki Ki = = 33.2 ± 3.0 nM 33.2 [] unit_conversion 7.478861916295964 success True biochemical_inhibition FRET enzymatic assay using Dabcyl-FTLRGG/APTKV-E(Edans) substrate. 12 Fig. 2 reports Jun12197: Ki = 33.2 ± 3.0 nM; its caption defines the FRET enzymatic assay. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8UUV\8UUV_metadata.json point structures/8UUV/8uuv_protein.pdb structures/8UUV/8uuv_pocket.pdb structures/8UUV/8uuv_ligand.sdf structures/8UUV/8uuv_ligand.pdb structures/8UUV/8uuv_ligand.cif structures/8UUV/8uuv_complex.pdb structures/8UUV/8uuv_complex.cif 8UUW classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun12145 "[""Y2N""]" 2 Ki Ki = = 35.2 ± 2.0 nM 35.2 [] unit_conversion 7.453457336521869 success True biochemical_inhibition FRET enzymatic assay using Dabcyl-FTLRGG/APTKV-E(Edans) substrate. 12 Fig. 2 reports Jun12145: Ki = 35.2 ± 2.0 nM; its caption defines the FRET enzymatic assay. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8UUW\8UUW_metadata.json point structures/8UUW/8uuw_protein.pdb structures/8UUW/8uuw_pocket.pdb structures/8UUW/8uuw_ligand.sdf structures/8UUW/8uuw_ligand.pdb structures/8UUW/8uuw_ligand.cif structures/8UUW/8uuw_complex.pdb structures/8UUW/8uuw_complex.cif 8UUY classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun12129 "[""Y2R""]" 2 Ki Ki = = 75.5 ± 2.0 nM 75.5 [] unit_conversion 7.1220530483708115 success True biochemical_inhibition FRET enzymatic assay using Dabcyl-FTLRGG/APTKV-E(Edans) substrate. 12 Fig. 2 reports Jun12129: Ki = 75.5 ± 2.0 nM; its caption defines the FRET enzymatic assay. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8UUY\8UUY_metadata.json point structures/8UUY/8uuy_protein.pdb structures/8UUY/8uuy_pocket.pdb structures/8UUY/8uuy_ligand.sdf structures/8UUY/8uuy_ligand.pdb structures/8UUY/8uuy_ligand.cif structures/8UUY/8uuy_complex.pdb structures/8UUY/8uuy_complex.cif 8UV0 classic CDK2 Na Na Na compound 17 "[""XKU""]" 1 IC50 IC50 = = 0.29 nM 0.29 [] unit_conversion 9.537602002101044 success True biochemical_inhibition Mean IC50 measured in the presence of 1 mM ATP; biochemical CDK2/Cyclin E1 inhibition assay. 4 Table 2 reports compound 17 with CDK2/Cyclin E1 IC50 = 0.29 nM. The table footnote states that mean IC50 values were measured in the presence of 1 mM ATP. auto_single_measurement only accepted activity measurement [1] 1 structures\8UV0\8UV0_metadata.json point structures/8UV0/8uv0_protein.pdb structures/8UV0/8uv0_pocket.pdb structures/8UV0/8uv0_ligand.sdf structures/8UV0/8uv0_ligand.pdb structures/8UV0/8uv0_ligand.cif structures/8UV0/8uv0_complex.pdb structures/8UV0/8uv0_complex.cif 8UV2 classic human p97/VCP ATPase human full-length p97 ATPase WT NSC799462 "[""XKM""]" 1 IC50 IC50 = = 15 nM 15.0 [] unit_conversion 7.823908740944319 success True biochemical_inhibition Purified p97 ATPase activity inhibition; the paper states NSC799462 has an IC50 of 15 nM. 4 “NSC799462 exhibits a lower IC50 of 15 nM … indicating a stronger inhibitory potency.” auto_single_measurement only accepted activity measurement [1] 1 structures\8UV2\8UV2_metadata.json point structures/8UV2/8uv2_protein.pdb structures/8UV2/8uv2_pocket.pdb structures/8UV2/8uv2_ligand.sdf structures/8UV2/8uv2_ligand.pdb structures/8UV2/8uv2_ligand.cif structures/8UV2/8uv2_complex.pdb structures/8UV2/8uv2_complex.cif 8UWP classic SETDB1 Na SETDB1-TTD Na MR46747 "[""XRU""]" 1 Kd Kd = = 4 μM 4000.0 [] unit_conversion 5.3979400086720375 success True direct_binding SPR dose-response/steady-state affinity fit (1:1 binding model) of MR46747, the (S)-enantiomer of MR43625, to SETDB1-TTD. 10 Figure 6 identifies PDB ID 8UWP as SETDB1-TTD in complex with MR46747 and reports K_D = 4 μM for MR46747 by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\8UWP\8UWP_metadata.json point structures/8UWP/8uwp_protein.pdb structures/8UWP/8uwp_pocket.pdb structures/8UWP/8uwp_ligand.sdf structures/8UWP/8uwp_ligand.pdb structures/8UWP/8uwp_ligand.cif structures/8UWP/8uwp_complex.pdb structures/8UWP/8uwp_complex.cif 8UX2 classic mono-ADP-ribosyltransferase CteC Chromobacterium violaceum SeMet-CteC36-276 Na NAD+ "[""NAD""]" 1 Kd Kd = = 123 μM 123000.0 [] unit_conversion 3.910094888560602 success True direct_binding Isothermal titration calorimetry of NAD+ binding to CteC36-276; reported equilibrium dissociation constant. 4 “The equilibrium dissociation constants (Kd) of CteC36–276 to Ub and NAD+ were very similar, 119 μM ... and 123 μM ...” auto_single_measurement only accepted activity measurement [1] 1 structures\8UX2\8UX2_metadata.json point structures/8UX2/8ux2_protein.pdb structures/8UX2/8ux2_pocket.pdb structures/8UX2/8ux2_ligand.sdf structures/8UX2/8ux2_ligand.pdb structures/8UX2/8ux2_ligand.cif structures/8UX2/8ux2_complex.pdb structures/8UX2/8ux2_complex.cif 8UXS classic KLHDC2 ubiquitin ligase human Kelch repeat domain of KLHDC2, residues 22-362, expressed with an N-terminal His-tag factor TS (TSF) and TEV-cleavage site Na C29 "[""XU8""]" 1 IC50 IC50 = = 2.9 µM 2900.0 [] unit_conversion 5.537602002101044 success True biochemical_inhibition AlphaLISA competition assay: C29 competed with a biotinylated 12-aa SelK C-end degron peptide for GST-KLHDC2 binding; IC50 from nonlinear dose-response fitting. 5 Fig. 2c table reports C29 IC50 2.9 µM (95% CI [2.6–3.2]); the caption identifies this as AlphaLISA competition-assay IC50 data. Page 12 maps PDB 8UXS to the KLHDC2-C29 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8UXS\8UXS_metadata.json point structures/8UXS/8uxs_protein.pdb structures/8UXS/8uxs_pocket.pdb structures/8UXS/8uxs_ligand.sdf structures/8UXS/8uxs_ligand.pdb structures/8UXS/8uxs_ligand.cif structures/8UXS/8uxs_complex.pdb structures/8UXS/8uxs_complex.cif 8V10 extended dwarf Ndc80 complex (Ndc80c^dwarf) Saccharomyces cerevisiae Ndc80c^dwarf with Saccharomyces cerevisiae Mps1 residues 137-171 appended to the N-terminus of Nuf2 Na Saccharomyces cerevisiae Mps1 peptide, residues 137-171 "[""CHAIN:B""]" 1 Kd Kd = = 0.28 ± 0.03 μM 280.0 [] unit_conversion 6.552841968657781 success True direct_binding Fluorescence-polarization direct titration of Bodipy-FL Mps1(137–171) peptide with Ndc80c^dwarf. 23 Figure 3A visibly prints “Mps1 Kd = 0.28 ± 0.03 μM”; its caption identifies the fluorescent ligand as Mps1(137–171) and the titrated target as Ndc80c^dwarf. auto_single_measurement only accepted activity measurement [1] 1 structures\8V10\8V10_metadata.json point structures/8V10/8v10_protein.pdb structures/8V10/8v10_pocket.pdb structures/8V10/8v10_ligand.pdb structures/8V10/8v10_ligand.cif structures/8V10/8v10_complex.pdb structures/8V10/8v10_complex.cif 8V11 extended dwarf Ndc80 complex (Ndc80c^dwarf) Saccharomyces cerevisiae Ndc80c^dwarf with Saccharomyces cerevisiae Ipl1 residues 26-39 and 45-59 appended to the N-terminus of Nuf2 Na Saccharomyces cerevisiae Ipl1 peptide, residues 26-39 and 45-59 "[""CHAIN:B"", ""CHAIN:F""]" 1 Kd Kd = = 18.8 ± 1.6 μM 18800.0 [] unit_conversion 4.72584215073632 success True direct_binding Fluorescence-polarization direct titration of Bodipy-FL Ipl1(26–39;45–59) peptide with Ndc80c^dwarf. 23 Figure 3A visibly prints “Ipl1 Kd = 18.8 ± 1.6 μM”; the Figure 3 caption identifies the fluorescent ligand as Ipl1(26–39;45–59) and the target as Ndc80c^dwarf. auto_single_measurement only accepted activity measurement [1] 1 structures\8V11\8V11_metadata.json point structures/8V11/8v11_protein.pdb structures/8V11/8v11_pocket.pdb structures/8V11/8v11_ligand.pdb structures/8V11/8v11_ligand.cif structures/8V11/8v11_complex.pdb structures/8V11/8v11_complex.cif 8V17 classic HIV-1 capsid protein (CA) Na disulfide-linked hexamer Na IC-1k "[""Y4X""]" 1 Kd Kd = = 24.6 ± 0.6 nM 24.6 [] unit_conversion 7.609064892896621 success True direct_binding SPR binding assay, disulfide-stabilized hexameric HIV-1 CA NL4.3 protein. 8 Table 4 reports IC-1k K_D of 24.6 ± 0.6 nM for CA hexamer; Figure 4 identifies the hexamer as disulfide-stabilized. Figure 5 maps IC-1k bound to the HIV-1 CA disulfide-linked hexamer to PDB 8V17. auto_single_measurement only accepted activity measurement [1] 1 structures\8V17\8V17_metadata.json point structures/8V17/8v17_protein.pdb structures/8V17/8v17_pocket.pdb structures/8V17/8v17_ligand.sdf structures/8V17/8v17_ligand.pdb structures/8V17/8v17_ligand.cif structures/8V17/8v17_complex.pdb structures/8V17/8v17_complex.cif 8V1L classic human G3BP1 human NTF2L domain of G3BP1 Na G3Ia (FAZ-3532) "[""Y9M""]" 1 Kd Kd = = 0.54 µM 540.0 [] unit_conversion 6.267606240177031 success True direct_binding SPR binding to sensor-bound, biotinylated AVI-tagged G3BP1 NTF2L domain. 3 Figure 1E prints SPR Kd = 0.54 µM for FAZ-3532 (G3Ia); the figure caption identifies sensor-immobilized human G3BP1. auto_single_measurement only accepted activity measurement [1] 1 structures\8V1L\8V1L_metadata.json point structures/8V1L/8v1l_protein.pdb structures/8V1L/8v1l_pocket.pdb structures/8V1L/8v1l_ligand.sdf structures/8V1L/8v1l_ligand.pdb structures/8V1L/8v1l_ligand.cif structures/8V1L/8v1l_complex.pdb structures/8V1L/8v1l_complex.cif 8V1O classic IRAK4 Na kinase domain Na compound 4 "[""Y9T""]" 1 Kd Kd = = 0.32 nM 0.32 [] unit_conversion 9.494850021680094 success True direct_binding IRAK4 dissociation constant (Kd); described as a high-affinity IRAK4 ligand. 2 Compound 4 showed very potent affinity to IRAK4, with dissociation constant Kd = 0.32 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V1O\8V1O_metadata.json point structures/8V1O/8v1o_protein.pdb structures/8V1O/8v1o_pocket.pdb structures/8V1O/8v1o_ligand.sdf structures/8V1O/8v1o_ligand.pdb structures/8V1O/8v1o_ligand.cif structures/8V1O/8v1o_complex.pdb structures/8V1O/8v1o_complex.cif 8V2F classic IRAK4 Na kinase domain Na compound 9 "[""YJU""]" 1 Kd Kd = = 0.37 nM 0.37 [] unit_conversion 9.431798275933005 success True direct_binding IRAK4 dissociation constant (Kd), compared with compound 4. 4 Compound 9 retained similar affinity to compound 4 and is reported with Kd = 0.37 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V2F\8V2F_metadata.json point structures/8V2F/8v2f_protein.pdb structures/8V2F/8v2f_pocket.pdb structures/8V2F/8v2f_ligand.sdf structures/8V2F/8v2f_ligand.pdb structures/8V2F/8v2f_ligand.cif structures/8V2F/8v2f_complex.pdb structures/8V2F/8v2f_complex.cif 8V2L classic IRAK4 Na kinase domain Na compound 8 "[""YK0""]" 1 Kd Kd = = 3.5 nM 3.5 [] unit_conversion 8.455931955649724 success True direct_binding IRAK4 dissociation constant (Kd), compared with compound 4. 4 Compound 8 demonstrated a significant loss in affinity toward IRAK4, with Kd = 3.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V2L\8V2L_metadata.json point structures/8V2L/8v2l_protein.pdb structures/8V2L/8v2l_pocket.pdb structures/8V2L/8v2l_ligand.sdf structures/8V2L/8v2l_ligand.pdb structures/8V2L/8v2l_ligand.cif structures/8V2L/8v2l_complex.pdb structures/8V2L/8v2l_complex.cif 8V5C classic IpaD (invasion plasmid antigen D) Shigella flexneri IpaD residues 122-321; N-terminal delta1-121 truncation WT (wild-type) deoxycholate (DOC) "[""DXC""]" 1 Kd Kd = = 6.2 ± 1.1 µM 6200.0 [] unit_conversion 5.207608310501746 success True direct_binding Direct-binding assay with IpaD Delta1-121 WT; apparent Kd. 3 Supplementary Table S1 reports apparent Kd 6.2 ± 1.1 µM for IpaD Delta1-121 WT. auto_single_measurement only accepted activity measurement [1] 1 structures\8V5C\8V5C_metadata.json point structures/8V5C/8v5c_protein.pdb structures/8V5C/8v5c_pocket.pdb structures/8V5C/8v5c_ligand.sdf structures/8V5C/8v5c_ligand.pdb structures/8V5C/8v5c_ligand.cif structures/8V5C/8v5c_complex.pdb structures/8V5C/8v5c_complex.cif 8V5E classic IpaD (invasion plasmid antigen D) Shigella flexneri IpaD residues 122-321; N-terminal delta1-121 truncation Q148 deletion (delta Q148) deoxycholate (DOC) "[""DXC""]" 1 Kd Kd = = 5.0 ± 1.8 µM 5000.0 [] unit_conversion 5.301029995663981 success True direct_binding Direct-binding assay with IpaD Delta1-121 DeltaQ148; apparent Kd. 3 Supplementary Table S1 reports apparent Kd 5.0 ± 1.8 µM for IpaD Delta1-121 DeltaQ148. auto_single_measurement only accepted activity measurement [1] 1 structures\8V5E\8V5E_metadata.json point structures/8V5E/8v5e_protein.pdb structures/8V5E/8v5e_pocket.pdb structures/8V5E/8v5e_ligand.sdf structures/8V5E/8v5e_ligand.pdb structures/8V5E/8v5e_ligand.cif structures/8V5E/8v5e_complex.pdb structures/8V5E/8v5e_complex.cif 8V5G classic Acetyl-CoA synthetase (CnAcs1) Cryptococcus neoformans H99 Trimer with Subunit A His11-Val676, Subunit B His11-Gly654, and Subunit C Arg39-Ile539; Subunit C lacks the C-terminal domain Na Compound 14; ethylsulfamide AMP inhibitor "[""YDO""]" 1 IC50 IC50 = = 83.7 mM 83700000.0 [] unit_conversion 1.07727454200674 success True biochemical_inhibition Inhibition of CnAcs1; compounds evaluated for inhibitory activity against CaAcs2 and CnAcs1. 3 “compound 14 showed significantly weaker potency compared to the reference compounds, with IC₅₀ values of 13.6 mM for CaAcs2 and 83.7 mM for CnAcs1.” auto_single_measurement only accepted activity measurement [1] 1 structures\8V5G\8V5G_metadata.json point structures/8V5G/8v5g_protein.pdb structures/8V5G/8v5g_pocket.pdb structures/8V5G/8v5g_ligand.sdf structures/8V5G/8v5g_ligand.pdb structures/8V5G/8v5g_ligand.cif structures/8V5G/8v5g_complex.pdb structures/8V5G/8v5g_complex.cif 8V5H classic MASTL Na Na Na compound 2 "[""A1AAE""]" 1 Ki Ki = = 0.37 nM 0.37 [] unit_conversion 9.431798275933005 success True biochemical_inhibition MASTL Ki reported in Table 2. 2 Table 2 lists compound 2 with MASTL Ki = 0.37 nM; Figure 1 identifies the co-crystal structure of compound 2 in MASTL as PDB 8V5H. auto_single_measurement only accepted activity measurement [1] 1 structures\8V5H\8V5H_metadata.json point structures/8V5H/8v5h_protein.pdb structures/8V5H/8v5h_pocket.pdb structures/8V5H/8v5h_ligand.sdf structures/8V5H/8v5h_ligand.pdb structures/8V5H/8v5h_ligand.cif structures/8V5H/8v5h_complex.pdb structures/8V5H/8v5h_complex.cif 8V66 classic Nanorana parkeri saxiphilin (NpSxph) Nanorana parkeri NpSxph carrying a C-terminal 3C protease cleavage site, GFP, and His10 tags in series; tags were cleaved before crystallization Na GTX5 "[""YGZ""]" 1 Kd Kd = = 1.8 ± 0.8 nM 1.8 [] unit_conversion 8.744727494896694 success True direct_binding ITC; Table 1 NpSxph:toxin thermodynamic binding parameters. 5 Table 1 reports Kd = 1.8 ± 0.8 nM for NpSxph binding GTX5. auto_single_measurement only accepted activity measurement [1] 1 structures\8V66\8V66_metadata.json point structures/8V66/8v66_protein.pdb structures/8V66/8v66_pocket.pdb structures/8V66/8v66_ligand.sdf structures/8V66/8v66_ligand.pdb structures/8V66/8v66_ligand.cif structures/8V66/8v66_complex.pdb structures/8V66/8v66_complex.cif 8V68 classic Nanorana parkeri saxiphilin (NpSxph) Nanorana parkeri NpSxph carrying a C-terminal 3C protease cleavage site, GFP, and His10 tags in series; tags were cleaved before crystallization Na dcSTX "[""YGF""]" 1 Kd Kd = = 11.3 ± 4.0 nM 11.3 [] unit_conversion 7.94692155651658 success True direct_binding ITC; Table 1 NpSxph:toxin thermodynamic binding parameters. 5 Table 1 reports Kd = 11.3 ± 4.0 nM for NpSxph binding dcSTX. auto_single_measurement only accepted activity measurement [1] 1 structures\8V68\8V68_metadata.json point structures/8V68/8v68_protein.pdb structures/8V68/8v68_pocket.pdb structures/8V68/8v68_ligand.sdf structures/8V68/8v68_ligand.pdb structures/8V68/8v68_ligand.cif structures/8V68/8v68_complex.pdb structures/8V68/8v68_complex.cif 8V6W classic human inositol phosphate multikinase human core catalytic domain Na compound 1 "[""YHE""]" 2 Kd Kd = = 11 nM 11.0 [] unit_conversion 7.958607314841775 success True direct_binding Isothermal titration calorimetry of compound 1 with IPMK 2 Figure 1C reports Kd = 11 nM for compound 1 binding to IPMK. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8V6W\8V6W_metadata.json point structures/8V6W/8v6w_protein.pdb structures/8V6W/8v6w_pocket.pdb structures/8V6W/8v6w_ligand.sdf structures/8V6W/8v6w_ligand.pdb structures/8V6W/8v6w_ligand.cif structures/8V6W/8v6w_complex.pdb structures/8V6W/8v6w_complex.cif 8V6X classic human inositol phosphate multikinase human core catalytic domain Na compound 2 "[""YHH""]" 1 IC50 IC50 = = 8.1 ± 2.1 nM 8.1 [] unit_conversion 8.09151498112135 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 4 Figure 3A reports compound 2 IPMK IC50 = 8.1 ± 2.1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V6X\8V6X_metadata.json point structures/8V6X/8v6x_protein.pdb structures/8V6X/8v6x_pocket.pdb structures/8V6X/8v6x_ligand.sdf structures/8V6X/8v6x_ligand.pdb structures/8V6X/8v6x_ligand.cif structures/8V6X/8v6x_complex.pdb structures/8V6X/8v6x_complex.cif 8V6Y classic human inositol phosphate multikinase human core catalytic domain Na compound 3 "[""YHN""]" 1 IC50 IC50 = = 29 ± 5 nM 29.0 [] unit_conversion 7.537602002101044 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 4 Figure 3A reports compound 3 IPMK IC50 = 29 ± 5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V6Y\8V6Y_metadata.json point structures/8V6Y/8v6y_protein.pdb structures/8V6Y/8v6y_pocket.pdb structures/8V6Y/8v6y_ligand.sdf structures/8V6Y/8v6y_ligand.pdb structures/8V6Y/8v6y_ligand.cif structures/8V6Y/8v6y_complex.pdb structures/8V6Y/8v6y_complex.cif 8V6Z classic human inositol phosphate multikinase human core catalytic domain Na compound 4 "[""YHS""]" 1 IC50 IC50 = = 1.9 ± 0.2 nM 1.9 [] unit_conversion 8.721246399047171 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 4 Figure 3A reports compound 4 IPMK IC50 = 1.9 ± 0.2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V6Z\8V6Z_metadata.json point structures/8V6Z/8v6z_protein.pdb structures/8V6Z/8v6z_pocket.pdb structures/8V6Z/8v6z_ligand.sdf structures/8V6Z/8v6z_ligand.pdb structures/8V6Z/8v6z_ligand.cif structures/8V6Z/8v6z_complex.pdb structures/8V6Z/8v6z_complex.cif 8V70 classic human inositol phosphate multikinase human core catalytic domain Na compound 6 "[""YHW""]" 1 IC50 IC50 = = 3.8 ± 0.4 nM 3.8 [] unit_conversion 8.42021640338319 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 6 Figure 4B reports compound 6 IPMK IC50 = 3.8 ± 0.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V70\8V70_metadata.json point structures/8V70/8v70_protein.pdb structures/8V70/8v70_pocket.pdb structures/8V70/8v70_ligand.sdf structures/8V70/8v70_ligand.pdb structures/8V70/8v70_ligand.cif structures/8V70/8v70_complex.pdb structures/8V70/8v70_complex.cif 8V71 classic human inositol phosphate multikinase human core catalytic domain Na compound 7 "[""YI8""]" 1 IC50 IC50 = = 2.5 ± 0.3 nM 2.5 [] unit_conversion 8.602059991327963 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 6 Figure 4B reports compound 7 IPMK IC50 = 2.5 ± 0.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V71\8V71_metadata.json point structures/8V71/8v71_protein.pdb structures/8V71/8v71_pocket.pdb structures/8V71/8v71_ligand.sdf structures/8V71/8v71_ligand.pdb structures/8V71/8v71_ligand.cif structures/8V71/8v71_complex.pdb structures/8V71/8v71_complex.cif 8V72 classic human inositol phosphate multikinase human core catalytic domain Na compound 8 "[""YIB""]" 1 IC50 IC50 = = 3.3 ± 0.4 nM 3.3 [] unit_conversion 8.481486060122112 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 6 Figure 4B reports compound 8 IPMK IC50 = 3.3 ± 0.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V72\8V72_metadata.json point structures/8V72/8v72_protein.pdb structures/8V72/8v72_pocket.pdb structures/8V72/8v72_ligand.sdf structures/8V72/8v72_ligand.pdb structures/8V72/8v72_ligand.cif structures/8V72/8v72_complex.pdb structures/8V72/8v72_complex.cif 8V73 classic human inositol phosphate multikinase human core catalytic domain Na compound 9 "[""YIG""]" 1 IC50 IC50 = = 11 ± 2 nM 11.0 [] unit_conversion 7.958607314841775 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 5 Table 1 reports compound 9 IPMK IC50 = 11 ± 2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V73\8V73_metadata.json point structures/8V73/8v73_protein.pdb structures/8V73/8v73_pocket.pdb structures/8V73/8v73_ligand.sdf structures/8V73/8v73_ligand.pdb structures/8V73/8v73_ligand.cif structures/8V73/8v73_complex.pdb structures/8V73/8v73_complex.cif 8V74 classic human inositol phosphate multikinase human core catalytic domain Na compound 10 "[""YJQ""]" 1 IC50 IC50 = = 3.5 ± 0.4 nM 3.5 [] unit_conversion 8.455931955649724 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 5 Table 1 reports compound 10 IPMK IC50 = 3.5 ± 0.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V74\8V74_metadata.json point structures/8V74/8v74_protein.pdb structures/8V74/8v74_pocket.pdb structures/8V74/8v74_ligand.sdf structures/8V74/8v74_ligand.pdb structures/8V74/8v74_ligand.cif structures/8V74/8v74_complex.pdb structures/8V74/8v74_complex.cif 8V75 classic human inositol phosphate multikinase human core catalytic domain Na compound 11 "[""YIK""]" 1 IC50 IC50 = = 1.0 ± 0.2 nM 1.0 [] unit_conversion 9.0 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 7 Figure 5B reports compound 11 IPMK IC50 = 1.0 ± 0.2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V75\8V75_metadata.json point structures/8V75/8v75_protein.pdb structures/8V75/8v75_pocket.pdb structures/8V75/8v75_ligand.sdf structures/8V75/8v75_ligand.pdb structures/8V75/8v75_ligand.cif structures/8V75/8v75_complex.pdb structures/8V75/8v75_complex.cif 8V76 classic human inositol phosphate multikinase human core catalytic domain Na compound 15 "[""YIU""]" 1 IC50 IC50 = = 1.1 ± 0.2 nM 1.1 [] unit_conversion 8.958607314841775 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 8 Figure 6B reports compound 15 IPMK IC50 = 1.1 ± 0.2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V76\8V76_metadata.json point structures/8V76/8v76_protein.pdb structures/8V76/8v76_pocket.pdb structures/8V76/8v76_ligand.sdf structures/8V76/8v76_ligand.pdb structures/8V76/8v76_ligand.cif structures/8V76/8v76_complex.pdb structures/8V76/8v76_complex.cif 8V77 classic human inositol phosphate multikinase human core catalytic domain Na compound 12 "[""YJ3""]" 1 IC50 IC50 = = 3.4 ± 0.5 nM 3.4 [] unit_conversion 8.468521082957745 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 8 Figure 6B reports compound 12 IPMK IC50 = 3.4 ± 0.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V77\8V77_metadata.json point structures/8V77/8v77_protein.pdb structures/8V77/8v77_pocket.pdb structures/8V77/8v77_ligand.sdf structures/8V77/8v77_ligand.pdb structures/8V77/8v77_ligand.cif structures/8V77/8v77_complex.pdb structures/8V77/8v77_complex.cif 8V78 classic human inositol phosphate multikinase human core catalytic domain Na compound 13 "[""YJB""]" 1 IC50 IC50 = = 9.5 ± 2.1 nM 9.5 [] unit_conversion 8.022276394711152 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 8 Figure 6B reports compound 13 IPMK IC50 = 9.5 ± 2.1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V78\8V78_metadata.json point structures/8V78/8v78_protein.pdb structures/8V78/8v78_pocket.pdb structures/8V78/8v78_ligand.sdf structures/8V78/8v78_ligand.pdb structures/8V78/8v78_ligand.cif structures/8V78/8v78_complex.pdb structures/8V78/8v78_complex.cif 8V79 classic human inositol phosphate multikinase human core catalytic domain Na compound 14 "[""YJH""]" 1 IC50 IC50 = = 2.8 ± 0.6 nM 2.8 [] unit_conversion 8.55284196865778 success True biochemical_inhibition 33P-radiolabeled HPLC IPMK kinase assay 7 Figure 5B reports compound 14 IPMK IC50 = 2.8 ± 0.6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8V79\8V79_metadata.json point structures/8V79/8v79_protein.pdb structures/8V79/8v79_pocket.pdb structures/8V79/8v79_ligand.sdf structures/8V79/8v79_ligand.pdb structures/8V79/8v79_ligand.cif structures/8V79/8v79_complex.pdb structures/8V79/8v79_complex.cif 8V8E classic SARS-CoV-2 main protease SARS-CoV-2 Catalytic domain residues 1-199 with 6His-tag Na Ensitrelvir (ESV) "[""7YY""]" 1 Kd Kd = = 4.6 ± 1.1 µM 4600.0 [] unit_conversion 5.337242168318426 success True direct_binding Isothermal titration calorimetry (ITC) of noncovalent ESV binding to monomeric MPro1-199-6H; 28 °C. 13 “noncovalent ESV also binds to monomeric MPro1-199-6H with a Kd of 4.6 ± 1.1 µM” auto_single_measurement only accepted activity measurement [1] 1 structures\8V8E\8V8E_metadata.json point structures/8V8E/8v8e_protein.pdb structures/8V8E/8v8e_pocket.pdb structures/8V8E/8v8e_ligand.sdf structures/8V8E/8v8e_ligand.pdb structures/8V8E/8v8e_ligand.cif structures/8V8E/8v8e_complex.pdb structures/8V8E/8v8e_complex.cif 8V8Z extended Lipoprotein(a) Kringle IV domain 8 (Lp(a) KIV8) Homo sapiens (human) Recombinant apo(a) KIV8 domain, residues 1377-1470, based on GenBank NP_005568.2 Na LY3473329 "[""A1AAK""]" 1 Kd Kd = = 22 nM 22.0 [] unit_conversion 7.657577319177793 success True direct_binding ITC with purified recombinant apo(a) KIV8. 15 Extended Data Table 1 reports KIV8 Kd 22 nM for LY3473329. auto_single_measurement only accepted activity measurement [1] 1 structures\8V8Z\8V8Z_metadata.json point structures/8V8Z/8v8z_protein.pdb structures/8V8Z/8v8z_pocket.pdb structures/8V8Z/8v8z_ligand.pdb structures/8V8Z/8v8z_ligand.cif structures/8V8Z/8v8z_complex.pdb structures/8V8Z/8v8z_complex.cif 8V9W classic JGFN4 nanobody (VHH) Na JGFN4 with C-terminal 6xHis tag WT (wild type) fentanyl "[""7V7""]" 2 Kd Kd = = 1.10E-03 ± 8.91E-05 M 1100000.0 [] unit_conversion 2.9586073148417746 success True direct_binding Differential scanning fluorimetry with free fentanyl; Table 2. 5 Table 2 reports WT DSF KD of 1.10E-03 ± 8.91E-05 M. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8V9W\8V9W_metadata.json point structures/8V9W/8v9w_protein.pdb structures/8V9W/8v9w_pocket.pdb structures/8V9W/8v9w_ligand.sdf structures/8V9W/8v9w_ligand.pdb structures/8V9W/8v9w_ligand.cif structures/8V9W/8v9w_complex.pdb structures/8V9W/8v9w_complex.cif 8V9X classic JGFN4 nanobody (VHH) Na JGFN4 with C-terminal 6xHis tag WT (wild type) fentanyl "[""7V7""]" 2 Kd Kd = = 1.10E-03 ± 8.91E-05 M 1100000.0 [] unit_conversion 2.9586073148417746 success True direct_binding Differential scanning fluorimetry with free fentanyl; Table 2. 5 Table 2 reports WT DSF KD of 1.10E-03 ± 8.91E-05 M. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8V9X\8V9X_metadata.json point structures/8V9X/8v9x_protein.pdb structures/8V9X/8v9x_pocket.pdb structures/8V9X/8v9x_ligand.sdf structures/8V9X/8v9x_ligand.pdb structures/8V9X/8v9x_ligand.cif structures/8V9X/8v9x_complex.pdb structures/8V9X/8v9x_complex.cif 8VA0 classic JGFN4 nanobody (VHH) Na JGFN4 N76D with C-terminal 6xHis tag N76D fentanyl "[""7V7""]" 2 Kd Kd = = 8.65E-05 ± 1.03E-06 M 86500.0 [] unit_conversion 4.062983892535186 success True direct_binding Differential scanning fluorimetry with free fentanyl; Table 2. 5 Table 2 reports N76D DSF KD of 8.65E-05 ± 1.03E-06 M. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8VA0\8VA0_metadata.json point structures/8VA0/8va0_protein.pdb structures/8VA0/8va0_pocket.pdb structures/8VA0/8va0_ligand.sdf structures/8VA0/8va0_ligand.pdb structures/8VA0/8va0_ligand.cif structures/8VA0/8va0_complex.pdb structures/8VA0/8va0_complex.cif 8VAU classic human CD38 human recombinant CD38 extracellular domain Na nicotinamide riboside (NR); covalently attached ribose "[""NNR""]" 1 IC50 IC50 = = 46.14 ± 14.26 μM 46140.0 [] unit_conversion 4.335922409814925 success True biochemical_inhibition NGD+-based fluorescence inactivation assay of recombinant CD38 extracellular domain with varied NR concentrations. 4 Figure 3A explicitly reports IC50 = 46.14 ± 14.26 μM for covalent inhibition of human CD38 by NR. auto_single_measurement only accepted activity measurement [1] 1 structures\8VAU\8VAU_metadata.json point structures/8VAU/8vau_protein.pdb structures/8VAU/8vau_pocket.pdb structures/8VAU/8vau_ligand.sdf structures/8VAU/8vau_ligand.pdb structures/8VAU/8vau_ligand.cif structures/8VAU/8vau_complex.pdb structures/8VAU/8vau_complex.cif 8VB1 classic HIV-1 protease HIV-1, IIIB strain Recombinant HIV-1 protease, expressed and purified Na GS-9770 "[""A1AAD""]" 1 Ki Ki = = 0.16 nM 0.16 [] unit_conversion 9.795880017344075 success True biochemical_inhibition Fluorogenic biochemical enzyme-inhibition assay using purified recombinant HIV-1 protease; apparent inhibitory constant (Ki(app)). 4 “GS-9770 demonstrated an apparent inhibitory constant (Ki(app)) value of 0.16 nM against HIV-1 PR.” auto_single_measurement only accepted activity measurement [1] 1 structures\8VB1\8VB1_metadata.json point structures/8VB1/8vb1_protein.pdb structures/8VB1/8vb1_pocket.pdb structures/8VB1/8vb1_ligand.sdf structures/8VB1/8vb1_ligand.pdb structures/8VB1/8vb1_ligand.cif structures/8VB1/8vb1_complex.pdb structures/8VB1/8vb1_complex.cif 8VB7 classic HIV-1 reverse transcriptase Na Na Na dATP "[""DTP""]" 1 Kd Kd = = 0.8±0.1 µM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Transient pre-steady-state kinetic analysis of dATP nucleotide addition; Kd was fitted from dNTP-concentration dependence. Figure 6e reports the WT value. 8 Fig. 6e table: WT Kd = 0.8±0.1 µM; caption identifies transient kinetic analysis of nucleotide addition by wild-type HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\8VB7\8VB7_metadata.json point structures/8VB7/8vb7_protein.pdb structures/8VB7/8vb7_pocket.pdb structures/8VB7/8vb7_ligand.sdf structures/8VB7/8vb7_ligand.pdb structures/8VB7/8vb7_ligand.cif structures/8VB7/8vb7_complex.pdb structures/8VB7/8vb7_complex.cif 8VB8 classic HIV-1 reverse transcriptase Na Na Na dATP "[""DTP""]" 1 Kd Kd = = 0.8±0.1 µM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Transient pre-steady-state kinetic analysis of dATP nucleotide addition; Kd was fitted from dNTP-concentration dependence. Figure 6e reports the WT value. 8 Fig. 6e table: WT Kd = 0.8±0.1 µM; caption identifies transient kinetic analysis of nucleotide addition by wild-type HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\8VB8\8VB8_metadata.json point structures/8VB8/8vb8_protein.pdb structures/8VB8/8vb8_pocket.pdb structures/8VB8/8vb8_ligand.sdf structures/8VB8/8vb8_ligand.pdb structures/8VB8/8vb8_ligand.cif structures/8VB8/8vb8_complex.pdb structures/8VB8/8vb8_complex.cif 8VB9 classic HIV-1 reverse transcriptase Na Na Na dATP "[""DTP""]" 1 Kd Kd = = 0.8±0.1 µM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Transient pre-steady-state kinetic analysis of dATP nucleotide addition; Kd was fitted from dNTP-concentration dependence. Figure 6e reports the WT value. 8 Fig. 6e table: WT Kd = 0.8±0.1 µM; caption identifies transient kinetic analysis of nucleotide addition by wild-type HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\8VB9\8VB9_metadata.json point structures/8VB9/8vb9_protein.pdb structures/8VB9/8vb9_pocket.pdb structures/8VB9/8vb9_ligand.sdf structures/8VB9/8vb9_ligand.pdb structures/8VB9/8vb9_ligand.cif structures/8VB9/8vb9_complex.pdb structures/8VB9/8vb9_complex.cif 8VBC classic HIV-1 reverse transcriptase Na Na Na dATP (conformers dATP-g and dATP-i) "[""DTP""]" 1 Kd Kd = = 0.8±0.1 µM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Transient pre-steady-state kinetic analysis of dATP nucleotide addition; Kd was fitted from dNTP-concentration dependence. Figure 6e reports the WT value. 8 Fig. 6e table: WT Kd = 0.8±0.1 µM; caption identifies transient kinetic analysis of nucleotide addition by wild-type HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\8VBC\8VBC_metadata.json point structures/8VBC/8vbc_protein.pdb structures/8VBC/8vbc_pocket.pdb structures/8VBC/8vbc_ligand.sdf structures/8VBC/8vbc_ligand.pdb structures/8VBC/8vbc_ligand.cif structures/8VBC/8vbc_complex.pdb structures/8VBC/8vbc_complex.cif 8VBD classic HIV-1 reverse transcriptase Na Na Na dATP (conformers dATP-g and dATP-i) "[""DTP""]" 1 Kd Kd = = 0.8±0.1 µM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Transient pre-steady-state kinetic analysis of dATP nucleotide addition; Kd was fitted from dNTP-concentration dependence. Figure 6e reports the WT value. 8 Fig. 6e table: WT Kd = 0.8±0.1 µM; caption identifies transient kinetic analysis of nucleotide addition by wild-type HIV-1 RT. auto_single_measurement only accepted activity measurement [1] 1 structures\8VBD\8VBD_metadata.json point structures/8VBD/8vbd_protein.pdb structures/8VBD/8vbd_pocket.pdb structures/8VBD/8vbd_ligand.sdf structures/8VBD/8vbd_ligand.pdb structures/8VBD/8vbd_ligand.cif structures/8VBD/8vbd_complex.pdb structures/8VBD/8vbd_complex.cif 8VEO classic PRMT5:MEP50 Na Na Na MTA "[""MTA""]" 1 Ki Ki = = 0.25 µM 250.0 [] unit_conversion 6.6020599913279625 success True biochemical_inhibition Radioactive biochemical FlashPlate methyltransferase assay using 3H-SAM and biotinylated histone H4 peptide; printed as measured Ki of MTA. 7 “the measured Ki of MTA is 0.25 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8VEO\8VEO_metadata.json point structures/8VEO/8veo_protein.pdb structures/8VEO/8veo_pocket.pdb structures/8VEO/8veo_ligand.sdf structures/8VEO/8veo_ligand.pdb structures/8VEO/8veo_ligand.cif structures/8VEO/8veo_complex.pdb structures/8VEO/8veo_complex.cif 8VET classic PRMT5:MEP50 Na Na Na oxamide compound 1 "[""A1AAS""]" 1 IC50 IC50 = = 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True biochemical_inhibition PRMT5 biochemical peptide-displacement assay with MTA and the unmethylated Me0 peptide. 3 Table 1 reports compound 1R, +MTA (Me0 peptide), PRMT5 biochemical IC50 = 2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8VET\8VET_metadata.json point structures/8VET/8vet_protein.pdb structures/8VET/8vet_pocket.pdb structures/8VET/8vet_ligand.sdf structures/8VET/8vet_ligand.pdb structures/8VET/8vet_ligand.cif structures/8VET/8vet_complex.pdb structures/8VET/8vet_complex.cif 8VEY classic PRMT5:MEP50 Na Na Na TNG908 "[""A1AAV""]" 1 Kd Kd = = 0.3 ± 0.1 nM 0.3 [] unit_conversion 9.522878745280337 success True direct_binding Double-titration fluorescence-anisotropy direct binding to the PRMT5:MTA complex. 9 Table 8 reports double-titration Kd = 0.3 ± 0.1 nM for PRMT5:MTA. auto_metric_priority unique highest-priority metric family: Kd [1] 5 structures\8VEY\8VEY_metadata.json point structures/8VEY/8vey_protein.pdb structures/8VEY/8vey_pocket.pdb structures/8VEY/8vey_ligand.sdf structures/8VEY/8vey_ligand.pdb structures/8VEY/8vey_ligand.cif structures/8VEY/8vey_complex.pdb structures/8VEY/8vey_complex.cif 8VG5 classic D-dopachrome tautomerase (D-DT) Na Na V113N 4-CPPC (4-(3-carboxyphenyl)-2,5-pyridinedicarboxylic acid) "[""7L9""]" 1 Ki Ki = = 58.1 ± 3.4 μM 58100.0 [] unit_conversion 4.235823867609669 success True biochemical_inhibition Current inhibition study of V113N D-DT with 4-CPPC. 7 The inhibition constants are 37.7 ± 5.6 μM for WT D-DT and 58.1 ± 3.4 μM for V113N in the presence of 4-CPPC; V113N–4-CPPC is assigned to PDB 8VG5 in the Figure 4 caption. auto_single_measurement only accepted activity measurement [1] 1 structures\8VG5\8VG5_metadata.json point structures/8VG5/8vg5_protein.pdb structures/8VG5/8vg5_pocket.pdb structures/8VG5/8vg5_ligand.sdf structures/8VG5/8vg5_ligand.pdb structures/8VG5/8vg5_ligand.cif structures/8VG5/8vg5_complex.pdb structures/8VG5/8vg5_complex.cif 8VG8 classic D-dopachrome tautomerase (D-DT) Na Na T115A 4-CPPC (4-(3-carboxyphenyl)-2,5-pyridinedicarboxylic acid) "[""7L9""]" 1 Ki Ki = = 36.4 ± 3.3 μM 36400.0 [] unit_conversion 4.438898616350944 success True biochemical_inhibition Current inhibition assay for T115A D-DT with 4-CPPC. 5 In the presence of 4-CPPC, the corresponding Ki values of WT D-DT and T115A were 37.7 ± 5.6 μM and 36.4 ± 3.3 μM, respectively; T115A–4-CPPC is assigned to PDB 8VG8 in the Figure 2 caption. auto_single_measurement only accepted activity measurement [1] 1 structures\8VG8\8VG8_metadata.json point structures/8VG8/8vg8_protein.pdb structures/8VG8/8vg8_pocket.pdb structures/8VG8/8vg8_ligand.sdf structures/8VG8/8vg8_ligand.pdb structures/8VG8/8vg8_ligand.cif structures/8VG8/8vg8_complex.pdb structures/8VG8/8vg8_complex.cif 8VGC extended ExbD Escherichia coli ExbD periplasmic domain, residues 59-141 Na D-box peptide, TonB residues 43-54, sequence QPISVTMVTPAD "[""CHAIN:P""]" 1 Kd Kd = = 19 ± 1 µM 19000.0 [] unit_conversion 4.721246399047171 success True direct_binding Isothermal titration calorimetry of synthetic D-box peptide binding to purified ExbD periplasmic domain. 2 Figure 1 caption reports ITC binding of the D-box peptide to purified ExbD59-141 with estimated Kd = 19 ± 1 µM; methods identify the peptide as TonB residues 43-54 (QPISVTMVTPAD). auto_single_measurement only accepted activity measurement [1] 1 structures\8VGC\8VGC_metadata.json point structures/8VGC/8vgc_protein.pdb structures/8VGC/8vgc_pocket.pdb structures/8VGC/8vgc_ligand.pdb structures/8VGC/8vgc_ligand.cif structures/8VGC/8vgc_complex.pdb structures/8VGC/8vgc_complex.cif 8VGD extended ExbD Escherichia coli ExbD periplasmic domain, residues 59-141 Na D-box peptide, TonB residues 43-54, sequence QPISVTMVTPAD "[""CHAIN:P""]" 1 Kd Kd = = 19 ± 1 µM 19000.0 [] unit_conversion 4.721246399047171 success True direct_binding Isothermal titration calorimetry of synthetic D-box peptide binding to purified ExbD periplasmic domain. 2 Figure 1 caption reports ITC binding of the D-box peptide to purified ExbD59-141 with estimated Kd = 19 ± 1 µM; methods identify the peptide as TonB residues 43-54 (QPISVTMVTPAD). auto_single_measurement only accepted activity measurement [1] 1 structures\8VGD\8VGD_metadata.json point structures/8VGD/8vgd_protein.pdb structures/8VGD/8vgd_pocket.pdb structures/8VGD/8vgd_ligand.pdb structures/8VGD/8vgd_ligand.cif structures/8VGD/8vgd_complex.pdb structures/8VGD/8vgd_complex.cif 8VHL classic DHODH human Na Na compound 17 "[""A1AA2""]" 1 IC50 IC50 = = 4.1 nM 4.1 [] unit_conversion 8.387216143280265 success True biochemical_inhibition hDHODH enzymatic assay (Table 2) 4 Table 2 reports compound 17 with hDHODH enzymatic assay IC50 of 4.1 nM; Figure 3 maps compound 17 bound to DHODH to PDB entry 8VHL. auto_single_measurement only accepted activity measurement [1] 1 structures\8VHL\8VHL_metadata.json point structures/8VHL/8vhl_protein.pdb structures/8VHL/8vhl_pocket.pdb structures/8VHL/8vhl_ligand.sdf structures/8VHL/8vhl_ligand.pdb structures/8VHL/8vhl_ligand.cif structures/8VHL/8vhl_complex.pdb structures/8VHL/8vhl_complex.cif 8VHM classic DHODH human Na Na fragment 2 "[""A1AA1""]" 1 Kd Kd = = 130 μM 130000.0 [] unit_conversion 3.886056647693163 success True direct_binding surface plasmon resonance (SPR) 2 The paper reports compound 2 as a weak binder with KD = 130 μM by SPR; Figure 2 maps crystal structure of 2 bound to DHODH to PDB entry 8VHM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8VHM\8VHM_metadata.json point structures/8VHM/8vhm_protein.pdb structures/8VHM/8vhm_pocket.pdb structures/8VHM/8vhm_ligand.sdf structures/8VHM/8vhm_ligand.pdb structures/8VHM/8vhm_ligand.cif structures/8VHM/8vhm_complex.pdb structures/8VHM/8vhm_complex.cif 8VHN classic E. coli class Ia ribonucleotide reductase alpha subunit (alpha2) Escherichia coli Na wild-type (WT) ATP (2 molecules) "[""ATP""]" 1 Kd Kd = = 158 ± 37 µM 158000.0 [] unit_conversion 3.801342913045578 success True direct_binding Ultrafiltration equilibrium ATP-binding assay at 25 °C; total ATP binding to α2, fitted with a one-state binding model. 7 “Using this approximation, the Kd for ATP binding at 25 °C was estimated to be 158 ± 37 μM with the maximum number of binding sites being 6.8 ± 0.6 per α2.” auto_single_measurement only accepted activity measurement [1] 1 structures\8VHN\8VHN_metadata.json point structures/8VHN/8vhn_protein.pdb structures/8VHN/8vhn_pocket.pdb structures/8VHN/8vhn_ligand.sdf structures/8VHN/8vhn_ligand.pdb structures/8VHN/8vhn_ligand.cif structures/8VHN/8vhn_complex.pdb structures/8VHN/8vhn_complex.cif 8VIE classic TMEM175 human Na Na 2-PPA "[""A1AB0""]" 1 IC50 IC50 ~ ~ 31 µM 31000.0 [] unit_conversion 4.508638306165727 success True biochemical_inhibition In vitro proteoliposome K+ flux assay. 3 The text states that 2-PPA was the most potent tested compound, with an IC50 of ~31 µM, in the in vitro proteoliposome K+ flux assay for TMEM175. auto_single_measurement only accepted activity measurement [1] 1 structures\8VIE\8VIE_metadata.json point structures/8VIE/8vie_protein.pdb structures/8VIE/8vie_pocket.pdb structures/8VIE/8vie_ligand.sdf structures/8VIE/8vie_ligand.pdb structures/8VIE/8vie_ligand.cif structures/8VIE/8vie_complex.pdb structures/8VIE/8vie_complex.cif 8VJP extended hMcl-1 Na hMcl-1(172-323) Na 155H1 "[""CHAIN:B""]" 1 IC50 IC50 = = 18 ± 3 nM 18.0 [] unit_conversion 7.7447274948966935 success True biochemical_inhibition DELFIA displacement assay measuring 155H1-mediated displacement of a biotinylated BH3 peptide from hMcl-1(172–323). 4 Table 2 reports compound 11 (155H1) with IC50 = 18 ± 3 nM against hMcl-1(172–323); its footnote specifies a DELFIA displacement assay. The text identifies 155H1 as a stapled covalent hMcl-1-targeting peptide, and page 11 maps the hMcl-1(172–323)-155H1 structure to PDB 8VJP. auto_single_measurement only accepted activity measurement [1] 1 structures\8VJP\8VJP_metadata.json point structures/8VJP/8vjp_protein.pdb structures/8VJP/8vjp_pocket.pdb structures/8VJP/8vjp_ligand.pdb structures/8VJP/8vjp_ligand.cif structures/8VJP/8vjp_complex.pdb structures/8VJP/8vjp_complex.cif 8VKA extended Plasmodium vivax glycylpeptide N-tetradecanoyltransferase (N-myristoyltransferase, NMT) Plasmodium vivax PvNMT residues 27-410 Na inhibitor 9c "[""A1AB7""]" 1 IC50 IC50 = = 230 nM 230.0 [] unit_conversion 6.638272163982407 success True biochemical_inhibition Purified-enzyme NMT activity assay measuring free CoA; PvNMT concentration 25 nM, with MyrCoA and PfARF peptide substrate. 5 Table 1 reports PvNMT IC50 = 230 nM for compound 9c. The paper maps PDB 8VKA to 9c. auto_single_measurement only accepted activity measurement [1] 1 structures\8VKA\8VKA_metadata.json point structures/8VKA/8vka_protein.pdb structures/8VKA/8vka_pocket.pdb structures/8VKA/8vka_ligand.pdb structures/8VKA/8vka_ligand.cif structures/8VKA/8vka_complex.pdb structures/8VKA/8vka_complex.cif 8VKB extended Plasmodium vivax glycylpeptide N-tetradecanoyltransferase (N-myristoyltransferase, NMT) Plasmodium vivax PvNMT residues 27-410 Na inhibitor 10b "[""A1AB8""]" 1 IC50 IC50 = = 91 nM 91.0 [] unit_conversion 7.040958607678906 success True biochemical_inhibition Purified-enzyme NMT activity assay measuring free CoA; PvNMT concentration 25 nM, with MyrCoA and PfARF peptide substrate. 6 Table 2 reports PvNMT IC50 = 91 nM for compound 10b. The paper maps PDB 8VKB to 10b. auto_single_measurement only accepted activity measurement [1] 1 structures\8VKB\8VKB_metadata.json point structures/8VKB/8vkb_protein.pdb structures/8VKB/8vkb_pocket.pdb structures/8VKB/8vkb_ligand.pdb structures/8VKB/8vkb_ligand.cif structures/8VKB/8vkb_complex.pdb structures/8VKB/8vkb_complex.cif 8VKF classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na wild-type 4-propionylbenzoic acid "[""LVK""]" 1 Kd Kd = = 9.1 ± 0.4 μM 9100.0 [] unit_conversion 5.040958607678906 success True direct_binding UV–vis absorbance spectroscopy; dissociation-constant determination for substrate binding. 4 “4-propionylbenzoic acid bound more tightly (Kd; 9.1 μM)”; Table 1 prints Kd 9.1 ± 0.4 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8VKF\8VKF_metadata.json point structures/8VKF/8vkf_protein.pdb structures/8VKF/8vkf_pocket.pdb structures/8VKF/8vkf_ligand.sdf structures/8VKF/8vkf_ligand.pdb structures/8VKF/8vkf_ligand.cif structures/8VKF/8vkf_complex.pdb structures/8VKF/8vkf_complex.cif 8VL0 classic CYP199A4 Rhodopseudomonas palustris strain HaA2 Na wild-type 4-(2-oxopropyl)benzoic acid "[""LVC""]" 1 Kd Kd = = 80 ± 3 μM 80000.0 [] unit_conversion 4.096910013008056 success True direct_binding UV–vis absorbance spectroscopy; dissociation-constant determination for substrate binding. 4 “4-(2-oxopropyl)benzoic acid (Kd; 80 μM)”; Table 1 prints Kd 80 ± 3 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8VL0\8VL0_metadata.json point structures/8VL0/8vl0_protein.pdb structures/8VL0/8vl0_pocket.pdb structures/8VL0/8vl0_ligand.sdf structures/8VL0/8vl0_ligand.pdb structures/8VL0/8vl0_ligand.cif structures/8VL0/8vl0_complex.pdb structures/8VL0/8vl0_complex.cif 8VL8 classic Salmonella enterica Typhimurium Tsr Salmonella enterica Typhimurium Soluble periplasmic Tsr ligand-binding domain, residues 32-187, with an N-terminal TEV cleavage tag (MENLYFQ) Na L-serine (L-Ser) "[""SER""]" 1 Kd Kd ~ ~ 5 µM 5000.0 [] unit_conversion 5.301029995663981 success True direct_binding Isothermal titration calorimetry (ITC) of purified recombinant SeTsr LBD with L-serine; experiments at pH 7.5 and 25°C. 15 “L-serine produces a robust exothermic binding curve, exhibiting a K_D of approximately 5 µM (Figure 7K).” Figure 7 identifies panels K–M as ITC analyses of SeTsr LBD with L-serine, norepinephrine, or DHMA. auto_single_measurement only accepted activity measurement [1] 1 structures\8VL8\8VL8_metadata.json point structures/8VL8/8vl8_protein.pdb structures/8VL8/8vl8_pocket.pdb structures/8VL8/8vl8_ligand.sdf structures/8VL8/8vl8_ligand.pdb structures/8VL8/8vl8_ligand.cif structures/8VL8/8vl8_complex.pdb structures/8VL8/8vl8_complex.cif 8VLD extended ASH1L human ASH1L_PHD, aa 2579-2629 Na histone H3K4me2 peptide "[""CHAIN:P"", ""CHAIN:T""]" 1 Kd Kd = = 1.0 ± 0.4 µM 1000.0 [] unit_conversion 6.0 success True direct_binding MST direct binding measurement; ASH1L_PHD binding to H3K4me2 peptide. 5 The binding-affinities table reports WT ASH1L_PHD–H3K4me2 Kd = 1.0 ± 0.4 µM; the text identifies 1–2 µM binding to di- and trimethylated peptides by tryptophan fluorescence and MST. auto_single_measurement only accepted activity measurement [1] 1 structures\8VLD\8VLD_metadata.json point structures/8VLD/8vld_protein.pdb structures/8VLD/8vld_pocket.pdb structures/8VLD/8vld_ligand.pdb structures/8VLD/8vld_ligand.cif structures/8VLD/8vld_complex.pdb structures/8VLD/8vld_complex.cif 8VOK classic CYP199A4 Rhodopseudomonas palustris HaA2 Na wild-type 4-hydroxybenzoic acid "[""PHB""]" 1 Kd Kd = = 458 ± 38 μM 458000.0 [] unit_conversion 3.3391345219961304 success True direct_binding UV–vis titration/difference-spectrum binding assay. 3 Table 1 lists 4-hydroxybenzoic acid with Kd 458 ± 38 μM; Figure 4 identifies the CYP199A4–4-hydroxybenzoic acid crystal structure as PDB 8VOK. auto_single_measurement only accepted activity measurement [1] 1 structures\8VOK\8VOK_metadata.json point structures/8VOK/8vok_protein.pdb structures/8VOK/8vok_pocket.pdb structures/8VOK/8vok_ligand.sdf structures/8VOK/8vok_ligand.pdb structures/8VOK/8vok_ligand.cif structures/8VOK/8vok_complex.pdb structures/8VOK/8vok_complex.cif 8VOT classic CYP199A4 Rhodopseudomonas palustris HaA2 Na wild-type 4-(hydroxymethyl)benzoic acid "[""E5X""]" 1 Kd Kd = = 85 ± 2 μM 85000.0 [] unit_conversion 4.070581074285707 success True direct_binding UV–vis titration/difference-spectrum binding assay. 3 Table 1 lists 4-(hydroxymethyl)benzoic acid with Kd 85 ± 2 μM; Figure 5 identifies the CYP199A4–4-(hydroxymethyl)benzoic acid crystal structure as PDB 8VOT. auto_single_measurement only accepted activity measurement [1] 1 structures\8VOT\8VOT_metadata.json point structures/8VOT/8vot_protein.pdb structures/8VOT/8vot_pocket.pdb structures/8VOT/8vot_ligand.sdf structures/8VOT/8vot_ligand.pdb structures/8VOT/8vot_ligand.cif structures/8VOT/8vot_complex.pdb structures/8VOT/8vot_complex.cif 8VP4 extended JF1cpCasp2 (circularly permuted caspase-2) Na Reengineered circularly permuted caspase-2, JF1cpCasp2 Engineered L5-loop mutant with cpCasp2 L5 residues deleted and replaced by a GG linker AcVDVAD-CHO "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 47.96 nM 47.96 [] unit_conversion 7.319120825573189 success True biochemical_inhibition Fluorometric enzyme inhibition assay; Table 3, JF1cpCasp2 row. 7 Table 3 reports an IC50 of 47.96 nM (SEM 3.14; N = 3) for AcVDVAD-CHO against JF1cpCasp2. The text identifies 8VP4 as JF1cpCasp2 bound to AcVDVAD-CHO. auto_single_measurement only accepted activity measurement [1] 1 structures\8VP4\8VP4_metadata.json point structures/8VP4/8vp4_protein.pdb structures/8VP4/8vp4_pocket.pdb structures/8VP4/8vp4_ligand.pdb structures/8VP4/8vp4_ligand.cif structures/8VP4/8vp4_complex.pdb structures/8VP4/8vp4_complex.cif 8VQL classic Influenza virus hemagglutinin (HA) Influenza A virus Na Na compound 6'(S) (6S prime) "[""A1ADD""]" 1 Kd Kd = = 51 nM 51.0 [] unit_conversion 7.292429823902063 success True direct_binding Surface plasmon resonance binding affinity for H1/PR8 HA. 4 Table 1 lists compound 6′(S) with KD of 51 nM; its footnote states that H1/PR8 binding affinity was assessed by surface plasmon resonance. auto_single_measurement only accepted activity measurement [1] 1 structures\8VQL\8VQL_metadata.json point structures/8VQL/8vql_protein.pdb structures/8VQL/8vql_pocket.pdb structures/8VQL/8vql_ligand.sdf structures/8VQL/8vql_ligand.pdb structures/8VQL/8vql_ligand.cif structures/8VQL/8vql_complex.pdb structures/8VQL/8vql_complex.cif 8VQM classic Influenza virus hemagglutinin (HA) Influenza A virus Na Na compound 6'(R) (6R prime) "[""A1ADU""]" 1 Kd Kd = = 55 nM 55.0 [] unit_conversion 7.259637310505756 success True direct_binding Surface plasmon resonance binding affinity for H1/PR8 HA. 4 Table 1 lists compound 6′(R) with KD of 55 nM; its footnote states that H1/PR8 binding affinity was assessed by surface plasmon resonance. auto_single_measurement only accepted activity measurement [1] 1 structures\8VQM\8VQM_metadata.json point structures/8VQM/8vqm_protein.pdb structures/8VQM/8vqm_pocket.pdb structures/8VQM/8vqm_ligand.sdf structures/8VQM/8vqm_ligand.pdb structures/8VQM/8vqm_ligand.cif structures/8VQM/8vqm_complex.pdb structures/8VQM/8vqm_complex.cif 8VQN classic Influenza virus hemagglutinin (HA) Influenza A virus Na Na compound 6R "[""A1ADV""]" 2 Kd Kd = = 210 nM 210.0 [] unit_conversion 6.6777807052660805 success True direct_binding Surface plasmon resonance binding affinity for H1/PR8 HA. 4 Table 1 lists compound 6(R) with KD of 210 nM; its footnote states that H1/PR8 binding affinity was assessed by surface plasmon resonance. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8VQN\8VQN_metadata.json point structures/8VQN/8vqn_protein.pdb structures/8VQN/8vqn_pocket.pdb structures/8VQN/8vqn_ligand.sdf structures/8VQN/8vqn_ligand.pdb structures/8VQN/8vqn_ligand.cif structures/8VQN/8vqn_complex.pdb structures/8VQN/8vqn_complex.cif 8VQQ classic Influenza virus hemagglutinin (HA) Influenza A virus Na Na compound 6S "[""A1ADC""]" 1 Kd Kd = = 220 nM 220.0 [] unit_conversion 6.657577319177793 success True direct_binding Surface plasmon resonance binding affinity for H1/PR8 HA. 4 Table 1 lists compound 6(S) with KD of 220 nM; its footnote states that H1/PR8 binding affinity was assessed by surface plasmon resonance. auto_single_measurement only accepted activity measurement [1] 1 structures\8VQQ\8VQQ_metadata.json point structures/8VQQ/8vqq_protein.pdb structures/8VQQ/8vqq_pocket.pdb structures/8VQQ/8vqq_ligand.sdf structures/8VQQ/8vqq_ligand.pdb structures/8VQQ/8vqq_ligand.cif structures/8VQQ/8vqq_complex.pdb structures/8VQQ/8vqq_complex.cif 8VTQ extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na PPN3 "[""A1ADX""]" 1 IC50 IC50 = = 1.65±0.28 μM 1650.0 [] unit_conversion 5.782516055786093 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports PPN3 IC50 = 1.65±0.28 μM and PDB 8VTQ. auto_single_measurement only accepted activity measurement [1] 1 structures\8VTQ\8VTQ_metadata.json point structures/8VTQ/8vtq_protein.pdb structures/8VTQ/8vtq_pocket.pdb structures/8VTQ/8vtq_ligand.pdb structures/8VTQ/8vtq_ligand.cif structures/8VTQ/8vtq_complex.pdb structures/8VTQ/8vtq_complex.cif 8VUG extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na PPN1 "[""A1AD1""]" 1 IC50 IC50 = = 1.01±0.06 μM 1010.0 [] unit_conversion 5.995678626217357 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports PPN1 IC50 = 1.01±0.06 μM and PDB 8VUG. auto_single_measurement only accepted activity measurement [1] 1 structures\8VUG\8VUG_metadata.json point structures/8VUG/8vug_protein.pdb structures/8VUG/8vug_pocket.pdb structures/8VUG/8vug_ligand.pdb structures/8VUG/8vug_ligand.cif structures/8VUG/8vug_complex.pdb structures/8VUG/8vug_complex.cif 8VW4 classic Cbl-b Na TKB Na compound 26 "[""A1AEG""]" 2 Kd Kd = = 0.078 μM 78.0 [] unit_conversion 7.107905397309519 success True direct_binding SPR binding affinity to Cbl-b protein. 6 Table 4 reports compound 26: SPR Kd = 0.078 μM; footnote identifies this as binding affinity to Cbl-b protein. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8VW4\8VW4_metadata.json point structures/8VW4/8vw4_protein.pdb structures/8VW4/8vw4_pocket.pdb structures/8VW4/8vw4_ligand.sdf structures/8VW4/8vw4_ligand.pdb structures/8VW4/8vw4_ligand.cif structures/8VW4/8vw4_complex.pdb structures/8VW4/8vw4_complex.cif 8VW5 classic Cbl-b Na TKB Na compound 2 "[""A1AD4""]" 2 Kd Kd = = 0.28 μM 280.0 [] unit_conversion 6.552841968657781 success True direct_binding SPR binding to Cbl-b. 2 Figure 2 reports for compound 2: SPR Kd (μM) = 0.28. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8VW5\8VW5_metadata.json point structures/8VW5/8vw5_protein.pdb structures/8VW5/8vw5_pocket.pdb structures/8VW5/8vw5_ligand.sdf structures/8VW5/8vw5_ligand.pdb structures/8VW5/8vw5_ligand.cif structures/8VW5/8vw5_complex.pdb structures/8VW5/8vw5_complex.cif 8VWN classic Vibrio cholerae NFeoB Vibrio cholerae Vibrio cholerae NFeoB(His)6 NTPase domain WT GDP "[""GDP""]" 1 Kd Kd = = 3.18 ± 0.23 μM 3180.0 [] unit_conversion 5.497572880015568 success True direct_binding Isothermal titration calorimetry of WT VcNFeoB(His)6 with GDP; single binding site (N ≈ 1). 7 Figure 7 states: “The GDP Kd for both WT (3.18 μM ± 0.23 μM) ...” and identifies the WT GDP-bound structure as PDB ID 8VWN. auto_single_measurement only accepted activity measurement [1] 1 structures\8VWN\8VWN_metadata.json point structures/8VWN/8vwn_protein.pdb structures/8VWN/8vwn_pocket.pdb structures/8VWN/8vwn_ligand.sdf structures/8VWN/8vwn_ligand.pdb structures/8VWN/8vwn_ligand.cif structures/8VWN/8vwn_complex.pdb structures/8VWN/8vwn_complex.cif 8VX0 classic Cytochrome P450 2C9*14 human CYP2C9 residues 1-23 replaced by MAKKT; C-terminal Val substituted to Ile; C-terminal 4xHis tag Arg125His (CYP2C9*14); C-terminal Val->Ile construct substitution Losartan "[""LSN""]" 1 Kd Kd = = 12.4 ± 0.4 μM 12400.0 [] unit_conversion 4.906578314837765 success True direct_binding Isothermal titration calorimetry (triplicate) of CYP2C9*14 with losartan. 17 Figure 5 prints “CYP2C9*14 + Losartan, K_D = 12.4 ± 0.4 μM”; the caption identifies these as ITC binding isotherms performed in triplicate. auto_single_measurement only accepted activity measurement [1] 1 structures\8VX0\8VX0_metadata.json point structures/8VX0/8vx0_protein.pdb structures/8VX0/8vx0_pocket.pdb structures/8VX0/8vx0_ligand.sdf structures/8VX0/8vx0_ligand.pdb structures/8VX0/8vx0_ligand.cif structures/8VX0/8vx0_complex.pdb structures/8VX0/8vx0_complex.cif 8VXD extended Casein kinase I isoform delta (CK1d) Na Na Na inhibitor 7 "[""A1AD7""]" 1 IC50 IC50 = = 2.9 ± 0.9 nM 2.9 [] unit_conversion 8.537602002101044 success True biochemical_inhibition Enzymatic ADP-Glo assay with 20 μM ATP. 2 Table 1 reports CK1δ IC50 of 2.9 ± 0.9 nM for compound 7; its footnote specifies an ADP-Glo enzymatic assay with 20 μM ATP. auto_single_measurement only accepted activity measurement [1] 1 structures\8VXD\8VXD_metadata.json point structures/8VXD/8vxd_protein.pdb structures/8VXD/8vxd_pocket.pdb structures/8VXD/8vxd_ligand.pdb structures/8VXD/8vxd_ligand.cif structures/8VXD/8vxd_complex.pdb structures/8VXD/8vxd_complex.cif 8VXE extended p38 alpha (Mitogen-activated protein kinase 14) Na Na Na inhibitor 6 "[""A1AD9""]" 1 IC50 IC50 = = 0.14 μM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition In vitro p38α inhibition; assay format not stated. 2 The text states that compound 6 inhibited p38α and p38β with IC50 values of 0.14 and 0.25 μM, respectively; Table 1 shows the same ordered pair. auto_single_measurement only accepted activity measurement [1] 1 structures\8VXE\8VXE_metadata.json point structures/8VXE/8vxe_protein.pdb structures/8VXE/8vxe_pocket.pdb structures/8VXE/8vxe_ligand.pdb structures/8VXE/8vxe_ligand.cif structures/8VXE/8vxe_complex.pdb structures/8VXE/8vxe_complex.cif 8VXI classic CYP125MRCA Na Na Na sitosterol "[""A1LXL""]" 1 Kd Kd = = 1.48 ± 0.03 µM 1480.0 [] unit_conversion 5.8297382846050425 success True direct_binding Purified CYP125MRCA substrate titration monitored by UV-Vis difference spectroscopy; values fitted to the Hill binding model (n = 3.74). 6 Table 1 reports the CYP125MRCA dissociation constant for sitosterol as 1.48 ± 0.03 µM. The supplied structure title explicitly identifies 8VXI as sitosterol-bound CYP125MRCA. auto_single_measurement only accepted activity measurement [1] 1 structures\8VXI\8VXI_metadata.json point structures/8VXI/8vxi_protein.pdb structures/8VXI/8vxi_pocket.pdb structures/8VXI/8vxi_ligand.sdf structures/8VXI/8vxi_ligand.pdb structures/8VXI/8vxi_ligand.cif structures/8VXI/8vxi_complex.pdb structures/8VXI/8vxi_complex.cif 8VZ7 classic Human Cytochrome P450 2C9*27 human CYP2C9 residues 1-23 replaced by MAKKT; C-terminal Val substituted to Ile; C-terminal 4xHis tag Arg150Leu (R150L; CYP2C9*27); C-terminal Val->Ile construct substitution Losartan "[""LSN""]" 1 Kd Kd = = 28.5 ± 0.9 μM 28500.0 [] unit_conversion 4.54515513999149 success True direct_binding Isothermal titration calorimetry (triplicate) of CYP2C9*27 with losartan. 17 Figure 5 prints “CYP2C9*27 + Losartan, K_D = 28.5 ± 0.9 μM”; the caption identifies these as ITC binding isotherms performed in triplicate. auto_single_measurement only accepted activity measurement [1] 1 structures\8VZ7\8VZ7_metadata.json point structures/8VZ7/8vz7_protein.pdb structures/8VZ7/8vz7_pocket.pdb structures/8VZ7/8vz7_ligand.sdf structures/8VZ7/8vz7_ligand.pdb structures/8VZ7/8vz7_ligand.cif structures/8VZ7/8vz7_complex.pdb structures/8VZ7/8vz7_complex.cif 8VZV extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na LM10 "[""A1AER""]" 1 IC50 IC50 = = 0.30±0.06 μM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports LM10 IC50 = 0.30±0.06 μM and PDB 8VZV. auto_single_measurement only accepted activity measurement [1] 1 structures\8VZV\8VZV_metadata.json point structures/8VZV/8vzv_ligand.cif structures/8VZV/8vzv_complex.cif 8W0R classic emopamil binding protein (EBP) Homo sapiens (human) human EBP residues T2-N230 with an N-terminal Strep tag Na compound 1 "[""A1AEU""]" 1 Ki Ki = = 11 nM 11.0 [] unit_conversion 7.958607314841775 success True direct_binding Human EBP competitive radioligand-binding validation; the paper reports compound 1 as a potent human EBP binder. 2 “Further validation revealed that 1 is a potent EBP binder (EBP_human Ki = 11 nM)” auto_single_measurement only accepted activity measurement [1] 1 structures\8W0R\8W0R_metadata.json point structures/8W0R/8w0r_protein.pdb structures/8W0R/8w0r_pocket.pdb structures/8W0R/8w0r_ligand.sdf structures/8W0R/8w0r_ligand.pdb structures/8W0R/8w0r_ligand.cif structures/8W0R/8w0r_complex.pdb structures/8W0R/8w0r_complex.cif 8W10 classic Plasmodium vivax PMX Plasmodium vivax Na Na MK-7602 "[""ZRN""]" 2 Kd Kd > > 1 × 10^-11 M 0.01 [] unit_conversion 11.0 success True direct_binding Surface plasmon resonance binding experiment with PvPMX. 9 Fig. 2C table reports for PvPMX: KD (M) >1 × 10^-11; the caption identifies representative SPR sensorgrams of MK-7602 with P. vivax PMX. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8W10\8W10_metadata.json point structures/8W10/8w10_protein.pdb structures/8W10/8w10_pocket.pdb structures/8W10/8w10_ligand.sdf structures/8W10/8w10_ligand.pdb structures/8W10/8w10_ligand.cif structures/8W10/8w10_complex.pdb structures/8W10/8w10_complex.cif 8W1H extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na PYN3 "[""A1AEY""]" 1 IC50 IC50 = = 0.69±0.08 μM 690.0 [] unit_conversion 6.161150909262744 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports PYN3 IC50 = 0.69±0.08 μM and PDB 8W1H. auto_single_measurement only accepted activity measurement [1] 1 structures\8W1H\8W1H_metadata.json point structures/8W1H/8w1h_protein.pdb structures/8W1H/8w1h_pocket.pdb structures/8W1H/8w1h_ligand.pdb structures/8W1H/8w1h_ligand.cif structures/8W1H/8w1h_complex.pdb structures/8W1H/8w1h_complex.cif 8W1U extended SARS-CoV-2 Main protease (Mpro) SARS-CoV-2 Mpro construct with N-terminal 6xHis tag and Mpro recognition sequence, plus C-terminal 6xHis tag after an HRV 3C cleavage site; authentic termini produced after processing Na Compound 5 (NZ-804) "[""A1AFE""]" 1 IC50 IC50 = = 0.0089 μM 8.9 [] unit_conversion 8.050609993355087 success True biochemical_inhibition Purified recombinant Mpro biochemical inhibition assay for the optimized lead NZ-804 (Compound 5). 4 “Compound 5, NZ-804 exhibited yet another increase in potency (IC50 = 0.0089 μM, EC50 = 0.014 μM).” auto_single_measurement only accepted activity measurement [1] 1 structures\8W1U\8W1U_metadata.json point structures/8W1U/8w1u_protein.pdb structures/8W1U/8w1u_pocket.pdb structures/8W1U/8w1u_ligand.pdb structures/8W1U/8w1u_ligand.cif structures/8W1U/8w1u_complex.pdb structures/8W1U/8w1u_complex.cif 8W1V classic beta2 adrenergic receptor (beta2AR) Na beta2AR-T4L bound with nanobody Nb60 Na bitopic ligand 4 "[""A1AE2""]" 2 pKd Kd = = 9.37 ± 0.04 unitless 0.42657951880159345 [] p_metric_transform 9.37 success True direct_binding Membrane-based kinetic competition assay with 3H-DHA; pKd determined from koff/kon. 5 Table 4 reports ligand 4 pKd = 9.37 ± 0.04; the text identifies ligand 4 as the crystallized β2AR bitopic ligand. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8W1V\8W1V_metadata.json point structures/8W1V/8w1v_protein.pdb structures/8W1V/8w1v_pocket.pdb structures/8W1V/8w1v_ligand.sdf structures/8W1V/8w1v_ligand.pdb structures/8W1V/8w1v_ligand.cif structures/8W1V/8w1v_complex.pdb structures/8W1V/8w1v_complex.cif 8W23 classic human tankyrase 2 (TNKS2) human SAM-PARP filament Na TDI-2804 (TDI-012804 in the paper) "[""A1AE4""]" 1 IC50 IC50 = = 3.46 nM 3.46 [] unit_conversion 8.460923901207224 success True biochemical_inhibition In vitro PARylation enzymatic-activity assay; Figure 2c labels the TNKS2 curve for TDI-012804. 4 Figure 2c explicitly reports TDI-012804: TNKS2 (3.46 nM). auto_single_measurement only accepted activity measurement [1] 1 structures\8W23\8W23_metadata.json point structures/8W23/8w23_protein.pdb structures/8W23/8w23_pocket.pdb structures/8W23/8w23_ligand.sdf structures/8W23/8w23_ligand.pdb structures/8W23/8w23_ligand.cif structures/8W23/8w23_complex.pdb structures/8W23/8w23_complex.cif 8W25 classic human tankyrase 2 (TNKS2) human SAM-PARP filament Na TDI-2804 (TDI-012804 in the paper) "[""A1AE4""]" 1 IC50 IC50 = = 3.46 nM 3.46 [] unit_conversion 8.460923901207224 success True biochemical_inhibition In vitro PARylation enzymatic-activity assay; Figure 2c labels the TNKS2 curve for TDI-012804. 4 Figure 2c explicitly reports TDI-012804: TNKS2 (3.46 nM). auto_single_measurement only accepted activity measurement [1] 1 structures\8W25\8W25_metadata.json point structures/8W25/8w25_protein.pdb structures/8W25/8w25_pocket.pdb structures/8W25/8w25_ligand.sdf structures/8W25/8w25_ligand.pdb structures/8W25/8w25_ligand.cif structures/8W25/8w25_complex.pdb structures/8W25/8w25_complex.cif 8W27 classic human tankyrase 2 (TNKS2) human SAM-PARP filament Na XAV (XAV939 in the paper) "[""XAV""]" 1 IC50 IC50 = = 1.13 nM 1.13 [] unit_conversion 8.94692155651658 success True biochemical_inhibition In vitro PARylation enzymatic-activity assay; Figure 2c labels the TNKS2 curve for XAV939. 4 Figure 2c explicitly reports XAV939: TNKS2 (1.13 nM). auto_single_measurement only accepted activity measurement [1] 1 structures\8W27\8W27_metadata.json point structures/8W27/8w27_protein.pdb structures/8W27/8w27_pocket.pdb structures/8W27/8w27_ligand.sdf structures/8W27/8w27_ligand.pdb structures/8W27/8w27_ligand.cif structures/8W27/8w27_complex.pdb structures/8W27/8w27_complex.cif 8W28 classic human tankyrase 2 (TNKS2) human SAM-PARP filament Na XAV (XAV939 in the paper) "[""XAV""]" 1 IC50 IC50 = = 1.13 nM 1.13 [] unit_conversion 8.94692155651658 success True biochemical_inhibition In vitro PARylation enzymatic-activity assay; Figure 2c labels the TNKS2 curve for XAV939. 4 Figure 2c explicitly reports XAV939: TNKS2 (1.13 nM). auto_single_measurement only accepted activity measurement [1] 1 structures\8W28\8W28_metadata.json point structures/8W28/8w28_protein.pdb structures/8W28/8w28_pocket.pdb structures/8W28/8w28_ligand.sdf structures/8W28/8w28_ligand.pdb structures/8W28/8w28_ligand.cif structures/8W28/8w28_complex.pdb structures/8W28/8w28_complex.cif 8W2F classic Plasmodium falciparum 20S proteasome Plasmodium falciparum P. falciparum 3D7 proteasome with a C-terminal 8His-tagged beta7 subunit (Pf3D7_beta7_8His) Na SW584 "[""A1AE6""]" 1 IC50 IC50 = = 0.0058 ± 0.0024 μM 5.8 [] unit_conversion 8.236572006437063 success True biochemical_inhibition Purified Pf20S β5 chymotrypsin-like activity assay; no WLW-vs. 57 Table 3 reports SW584 Pf20Sβ5 IC50 = 0.0058 ± 0.0024 μM (n=4); the table note specifies [WLW-vs] = 0.5 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8W2F\8W2F_metadata.json point structures/8W2F/8w2f_protein.pdb structures/8W2F/8w2f_pocket.pdb structures/8W2F/8w2f_ligand.sdf structures/8W2F/8w2f_ligand.pdb structures/8W2F/8w2f_ligand.cif structures/8W2F/8w2f_complex.pdb structures/8W2F/8w2f_complex.cif 8W2K extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na PAN3F "[""A1AE7""]" 1 IC50 IC50 = = 0.70±0.03 μM 700.0 [] unit_conversion 6.154901959985743 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports PAN3F IC50 = 0.70±0.03 μM and PDB 8W2K. auto_single_measurement only accepted activity measurement [1] 1 structures\8W2K\8W2K_metadata.json point structures/8W2K/8w2k_protein.pdb structures/8W2K/8w2k_pocket.pdb structures/8W2K/8w2k_ligand.pdb structures/8W2K/8w2k_ligand.cif structures/8W2K/8w2k_complex.pdb structures/8W2K/8w2k_complex.cif 8W39 classic SmcR Vibrio vulnificus Full-length His-tagged SmcR Wild-type PTSP "[""A1AFF""]" 1 Kd Kd ~ ~ 1 µM 1000.0 [] unit_conversion 6.0 success True direct_binding Isothermal titration calorimetry of purified wild-type SmcR titrated into PTSP; the paper reports an approximate Kd. 5 “the wild-type SmcR-PTSP interaction had a Kd of approximately 1 µM” determined by isothermal titration calorimetry. auto_single_measurement only accepted activity measurement [1] 1 structures\8W39\8W39_metadata.json point structures/8W39/8w39_protein.pdb structures/8W39/8w39_pocket.pdb structures/8W39/8w39_ligand.sdf structures/8W39/8w39_ligand.pdb structures/8W39/8w39_ligand.cif structures/8W39/8w39_complex.pdb structures/8W39/8w39_complex.cif 8W3W classic IRAK4 human Na Na compound 4 "[""A1AFO""]" 1 IC50 IC50 = = 7.6 nM 7.6 [] unit_conversion 8.119186407719209 success True biochemical_inhibition IRAK4 enzyme potency measured in a DELFIA assay using activated full-length IRAK4 protein with 600 μM ATP (the ATP Km for IRAK4), assessing phosphorylation of a peptide substrate. 2 Table 2 reports compound 4 IRAK4 IC50 = 7.6 nM. Table 1 footnote defines the IRAK4 enzyme DELFIA assay conditions. Figure 2 identifies compound 4 in complex with human IRAK4, and the Accessions section maps compound 4 to PDB 8W3W. auto_single_measurement only accepted activity measurement [1] 1 structures\8W3W\8W3W_metadata.json point structures/8W3W/8w3w_protein.pdb structures/8W3W/8w3w_pocket.pdb structures/8W3W/8w3w_ligand.sdf structures/8W3W/8w3w_ligand.pdb structures/8W3W/8w3w_ligand.cif structures/8W3W/8w3w_complex.pdb structures/8W3W/8w3w_complex.cif 8W3X classic IRAK4 human Na Na compound 6 "[""A1AFH""]" 1 IC50 IC50 = = 23.9 nM 23.9 [] unit_conversion 7.621602099051862 success True biochemical_inhibition IRAK4 enzyme potency measured in a DELFIA assay using activated full-length IRAK4 protein with 600 μM ATP (the ATP Km for IRAK4), assessing phosphorylation of a peptide substrate. 2 Table 2 reports compound 6 IRAK4 IC50 = 23.9 nM. Table 1 footnote defines the IRAK4 enzyme DELFIA assay conditions. Figure 3 identifies compound 6 in complex with human IRAK4, and the Accessions section maps compound 6 to PDB 8W3X. auto_single_measurement only accepted activity measurement [1] 1 structures\8W3X\8W3X_metadata.json point structures/8W3X/8w3x_protein.pdb structures/8W3X/8w3x_pocket.pdb structures/8W3X/8w3x_ligand.sdf structures/8W3X/8w3x_ligand.pdb structures/8W3X/8w3x_ligand.cif structures/8W3X/8w3x_complex.pdb structures/8W3X/8w3x_complex.cif 8W4B classic sigma-1 receptor (xlo1R) Xenopus laevis Na Na progesterone "[""STR""]" 1 Kd Kd = = 0.94 ± 0.22 μM 940.0 [] unit_conversion 6.026872146400301 success True direct_binding Microscale thermophoresis (MST) binding assay; mean ± SD, N = 3 biologically independent experiments. 5 “Kd = 0.94 ± 0.22 μM for the wild-type receptor”. auto_single_measurement only accepted activity measurement [1] 1 structures\8W4B\8W4B_metadata.json point structures/8W4B/8w4b_protein.pdb structures/8W4B/8w4b_pocket.pdb structures/8W4B/8w4b_ligand.sdf structures/8W4B/8w4b_ligand.pdb structures/8W4B/8w4b_ligand.cif structures/8W4B/8w4b_complex.pdb structures/8W4B/8w4b_complex.cif 8W4C classic sigma-1 receptor (xlo1R) Xenopus laevis Na Na progesterone "[""STR""]" 1 Kd Kd = = 0.94 ± 0.22 μM 940.0 [] unit_conversion 6.026872146400301 success True direct_binding Microscale thermophoresis (MST) binding assay; mean ± SD, N = 3 biologically independent experiments. 5 “Kd = 0.94 ± 0.22 μM for the wild-type receptor”. auto_single_measurement only accepted activity measurement [1] 1 structures\8W4C\8W4C_metadata.json point structures/8W4C/8w4c_protein.pdb structures/8W4C/8w4c_pocket.pdb structures/8W4C/8w4c_ligand.sdf structures/8W4C/8w4c_ligand.pdb structures/8W4C/8w4c_ligand.cif structures/8W4C/8w4c_complex.pdb structures/8W4C/8w4c_complex.cif 8W5C classic FGFR4 Na kinase domain WT (wild-type) 8K (paper compound 8k) "[""VZO""]" 1 IC50 IC50 = = 34.0 nM 34.0 [] unit_conversion 7.468521082957745 success True biochemical_inhibition FGFR4 biochemical kinase inhibition assay (150 μM ATP). 6 Table 1 reports FGFR4 IC50 = 34.0 nM for compound 8k; Figure 3 and the text identify the wild-type FGFR4 cocrystal of 8k as PDB 8W5C. auto_single_measurement only accepted activity measurement [1] 1 structures\8W5C\8W5C_metadata.json point structures/8W5C/8w5c_protein.pdb structures/8W5C/8w5c_pocket.pdb structures/8W5C/8w5c_ligand.sdf structures/8W5C/8w5c_ligand.pdb structures/8W5C/8w5c_ligand.cif structures/8W5C/8w5c_complex.pdb structures/8W5C/8w5c_complex.cif 8W5Z extended tick tyrosylprotein sulfotransferase (TPST) Na engineered soluble TPST, residues 36-393, with an N-terminal His6-tag Na PAP; F51Y54-peptide "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 40.8 ± 4.9 µM 40800.0 [] unit_conversion 4.38933983691012 success True direct_binding Fluorescence-polarization binding measurement of tick TPST to F51Y54-peptide in the presence of PAP. 3 Figure 1F lists Kd values from fluorescence-polarization measurements; F51Y54-peptide is reported as 40.8 ± 4.9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8W5Z\8W5Z_metadata.json point structures/8W5Z/8w5z_protein.pdb structures/8W5Z/8w5z_pocket.pdb structures/8W5Z/8w5z_ligand.pdb structures/8W5Z/8w5z_ligand.cif structures/8W5Z/8w5z_complex.pdb structures/8W5Z/8w5z_complex.cif 8W7D classic EcPPAT (Escherichia coli PurF) Escherichia coli Na Na FR901483 (compound 1) "[""7TG""]" 1 Ki Ki = = 60.1 ± 0.4 nM 60.1 [] unit_conversion 7.221125527997261 success True biochemical_inhibition In vitro PPAT activity inhibition assay; kinetic parameters and inhibition constant reported for wild-type PurF in Table 1. 2 Table 1, “Kinetic Parameters and Inhibition Constant of the Wild-Type and Mutant PurF,” reports wild-type PurF Ki = 60.1 ± 0.4 nM. The paper identifies compound 1 as (−)-FR901483 and states that E. coli PurF was used for the PurF–1 crystal structure deposited as PDB 8W7D. auto_single_measurement only accepted activity measurement [1] 1 structures\8W7D\8W7D_metadata.json point structures/8W7D/8w7d_protein.pdb structures/8W7D/8w7d_pocket.pdb structures/8W7D/8w7d_ligand.sdf structures/8W7D/8w7d_ligand.pdb structures/8W7D/8w7d_ligand.cif structures/8W7D/8w7d_complex.pdb structures/8W7D/8w7d_complex.cif 8W8J classic Pseudomonas aeruginosa prolyl-tRNA synthetase (PaProRS) Pseudomonas aeruginosa Na Na PAA-19 "[""W1Q""]" 1 IC50 IC50 = = 18.5 ± 1.6 nM 18.5 [] unit_conversion 7.732828271596986 success True biochemical_inhibition Pre-transfer editing assay (PTEA) against PaProRS. 6 Table 1 reports PAA-19 IC50 = 18.5 ± 1.6 nM against PaProRS; the methods identify PTEA as the enzyme-inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8W8J\8W8J_metadata.json point structures/8W8J/8w8j_protein.pdb structures/8W8J/8w8j_pocket.pdb structures/8W8J/8w8j_ligand.sdf structures/8W8J/8w8j_ligand.pdb structures/8W8J/8w8j_ligand.cif structures/8W8J/8w8j_complex.pdb structures/8W8J/8w8j_complex.cif 8W8L classic Pseudomonas aeruginosa prolyl-tRNA synthetase (PaProRS) Pseudomonas aeruginosa Na Na PAA-38 "[""W20""]" 2 Kd Kd = = 0.399 ± 0.074 nM 0.399 [] unit_conversion 9.399027104313252 success True direct_binding ITC-derived direct binding affinity of PAA-38 to PaProRS; a competitive ITC experiment was used because the affinity approached the direct-titration limit. 8 The text states that ITC measured PAA-38 binding to PaProRS and calculated the real affinity as Kd = 0.399 ± 0.074 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8W8L\8W8L_metadata.json point structures/8W8L/8w8l_protein.pdb structures/8W8L/8w8l_pocket.pdb structures/8W8L/8w8l_ligand.sdf structures/8W8L/8w8l_ligand.pdb structures/8W8L/8w8l_ligand.cif structures/8W8L/8w8l_complex.pdb structures/8W8L/8w8l_complex.cif 8W9I classic Pseudomonas aeruginosa prolyl-tRNA synthetase (PaProRS) Pseudomonas aeruginosa Na Na PAA-5 "[""W2H""]" 2 Kd Kd = = 21.9 ± 6.6 nM 21.9 [] unit_conversion 7.6595558851598815 success True direct_binding Isothermal titration calorimetry (ITC) of PAA-5 binding to PaProRS. 3 Figure 3D labels PAA-5 to PaProRS with Kd = 21.9 ± 6.6 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8W9I\8W9I_metadata.json point structures/8W9I/8w9i_protein.pdb structures/8W9I/8w9i_pocket.pdb structures/8W9I/8w9i_ligand.sdf structures/8W9I/8w9i_ligand.pdb structures/8W9I/8w9i_ligand.cif structures/8W9I/8w9i_complex.pdb structures/8W9I/8w9i_complex.cif 8WCH classic SAR11_0655 Candidatus Pelagibacter ubique HTCC1062 Signal sequence removed; N-terminal His6 and thrombin tags Na L-pyroglutamate "[""PCA""]" 1 Kd Kd < < 5 nM 5.0 [] unit_conversion 8.301029995663981 success True direct_binding ITC-confirmed high-affinity SAR11_0655–L-pyroglutamate interaction. 5 Fig. 3 lists “Pyroglutamate SAR11_0655” and the figure legend states that SBPs with Kd <5 nM are highlighted; the plotted SAR11_0655 value is <5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WCH\8WCH_metadata.json point structures/8WCH/8wch_protein.pdb structures/8WCH/8wch_pocket.pdb structures/8WCH/8wch_ligand.sdf structures/8WCH/8wch_ligand.pdb structures/8WCH/8wch_ligand.cif structures/8WCH/8wch_complex.pdb structures/8WCH/8wch_complex.cif 8WDN classic PDE4D Na PDE4D catalytic domain, residues T86-S413, GenBank NM_001197221.1 Na 7b-1 "[""W8E""]" 1 IC50 IC50 = = 0.17 ± 0.02 μM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition PDE enzymatic scintillation proximity assay; PDE4D catalytic domain, n ≥ 3 independent experiments. 4 Table 2 reports 7b-1 (2S,3R) PDE4D IC50 = 0.17 ± 0.02 μM. The enzymatic SPA method is described on page 12; PDB 8WDN is mapped to PDE4D–7b-1 on page 7. auto_single_measurement only accepted activity measurement [1] 1 structures\8WDN\8WDN_metadata.json point structures/8WDN/8wdn_protein.pdb structures/8WDN/8wdn_pocket.pdb structures/8WDN/8wdn_ligand.sdf structures/8WDN/8wdn_ligand.pdb structures/8WDN/8wdn_ligand.cif structures/8WDN/8wdn_complex.pdb structures/8WDN/8wdn_complex.cif 8WGS classic V30M-TTR Na Na V30M compound 4 "[""WGH""]" 2 Kd Kd = = 120 ± 30 nM 120.0 [] unit_conversion 6.920818753952375 success True direct_binding Isothermal titration calorimetry (ITC) measurement of V30M-TTR with compound 4. 6 Table 3 reports the dissociation constant of compound 4 determined by ITC as Kd = 120 ± 30 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8WGS\8WGS_metadata.json point structures/8WGS/8wgs_protein.pdb structures/8WGS/8wgs_pocket.pdb structures/8WGS/8wgs_ligand.sdf structures/8WGS/8wgs_ligand.pdb structures/8WGS/8wgs_ligand.cif structures/8WGS/8wgs_complex.pdb structures/8WGS/8wgs_complex.cif 8WGT classic V30M-TTR Na Na V30M compound 7 "[""WGJ""]" 2 Kd Kd = = 53 ± 16 nM 53.0 [] unit_conversion 7.275724130399211 success True direct_binding Isothermal titration calorimetry (ITC) measurement of V30M-TTR with compound 7. 6 Table 3 reports the dissociation constant of compound 7 determined by ITC as Kd = 53 ± 16 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8WGT\8WGT_metadata.json point structures/8WGT/8wgt_protein.pdb structures/8WGT/8wgt_pocket.pdb structures/8WGT/8wgt_ligand.sdf structures/8WGT/8wgt_ligand.pdb structures/8WGT/8wgt_ligand.cif structures/8WGT/8wgt_complex.pdb structures/8WGT/8wgt_complex.cif 8WIJ classic threonyl-tRNA synthetase (ThrRS) Escherichia coli catalytic domain, residues 242-642 L489M Obafluorin (OB) "[""X5V""]" 1 IC50 IC50 = = 215 nM 215.0 [] unit_conversion 6.667561540084394 success True biochemical_inhibition ATP hydrolysis inhibition assay; Fig. 2b plots OB inhibition of EcThrRS_L489M. 3 “OB had a strong inhibitory effect on EcThrRS_L489M, with an IC50 value of 215 nM (Fig. 2b).” auto_single_measurement only accepted activity measurement [1] 1 structures\8WIJ\8WIJ_metadata.json point structures/8WIJ/8wij_protein.pdb structures/8WIJ/8wij_pocket.pdb structures/8WIJ/8wij_ligand.sdf structures/8WIJ/8wij_ligand.pdb structures/8WIJ/8wij_ligand.cif structures/8WIJ/8wij_complex.pdb structures/8WIJ/8wij_complex.cif 8WIS extended hemagglutinin from Asiatic toad influenza-like virus (tHA) Asiatic toad (Bufo gargarizans) soluble recombinant HA ectodomain Na LSTc; 6'SLNLN "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 35.7 μM 35700.0 [] unit_conversion 4.447331783887806 success True direct_binding SPR assay of recombinant soluble tHA binding the α2–6 sialylated glycan receptor analog. 4 “tHA binds to both α2–3 and α2–6 SA receptors, with affinities of 35.3 nM and 35.7 μM, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\8WIS\8WIS_metadata.json point structures/8WIS/8wis_protein.pdb structures/8WIS/8wis_pocket.pdb structures/8WIS/8wis_ligand.pdb structures/8WIS/8wis_ligand.cif structures/8WIS/8wis_complex.pdb structures/8WIS/8wis_complex.cif 8WJY classic PKMYT1 (MYT1) Na Na Na compound 4 "[""W9X""]" 1 IC50 IC50 = = 4.2 nM 4.2 [] unit_conversion 8.3767507096021 success True direct_binding MYT1 HTRF binding assay. 5 Table 1 reports compound 4: MYT1 IC50 = 4.2 nM; its footnote states MYT1 binding affinity was tested in the HTRF assay. Figure 4 identifies compound 4 bound to MYT1 (PDB 8WJY). auto_single_measurement only accepted activity measurement [1] 1 structures\8WJY\8WJY_metadata.json point structures/8WJY/8wjy_protein.pdb structures/8WJY/8wjy_pocket.pdb structures/8WJY/8wjy_ligand.sdf structures/8WJY/8wjy_ligand.pdb structures/8WJY/8wjy_ligand.cif structures/8WJY/8wjy_complex.pdb structures/8WJY/8wjy_complex.cif 8WLK classic VMAT2 human Na WT tetrabenazine (TBZ) "[""EBZ""]" 1 Kd Kd = = 60.0 ± 30.2 nM 60.0 [] unit_conversion 7.221848749616356 success True direct_binding MST binding assay; Fig. 3f table, mean ± SEM, n=3–4 independent experiments. 4 Fig. 3f reports VMAT2_WT Kd = 60.0 ± 30.2 nM for TBZ. auto_single_measurement only accepted activity measurement [1] 1 structures\8WLK\8WLK_metadata.json point structures/8WLK/8wlk_protein.pdb structures/8WLK/8wlk_pocket.pdb structures/8WLK/8wlk_ligand.sdf structures/8WLK/8wlk_ligand.pdb structures/8WLK/8wlk_ligand.cif structures/8WLK/8wlk_complex.pdb structures/8WLK/8wlk_complex.cif 8WLL classic VMAT2 human Na Y422C reserpine (RES) "[""YHR""]" 1 Kd Kd = = 196.8 ± 109.6 nM 196.8 [] unit_conversion 6.705974905904677 success True direct_binding MST binding assay; Fig. 4a table, mean ± SEM, n=3–4 independent experiments. 6 Fig. 4a reports VMAT2 Y422C Kd = 196.8 ± 109.6 nM for RES. auto_single_measurement only accepted activity measurement [1] 1 structures\8WLL\8WLL_metadata.json point structures/8WLL/8wll_protein.pdb structures/8WLL/8wll_pocket.pdb structures/8WLL/8wll_ligand.sdf structures/8WLL/8wll_ligand.pdb structures/8WLL/8wll_ligand.cif structures/8WLL/8wll_complex.pdb structures/8WLL/8wll_complex.cif 8WLM classic VMAT2 human Na WT serotonin (5-HT) "[""SRO""]" 1 Kd Kd = = 3.30 ± 1.01 µM 3300.0 [] unit_conversion 5.481486060122112 success True direct_binding MST binding assay; Fig. 2b, mean ± SEM, n=3–4 independent experiments. 3 Fig. 2b reports WT Kd = 3.30 ± 1.01 µM for 5-HT. auto_single_measurement only accepted activity measurement [1] 1 structures\8WLM\8WLM_metadata.json point structures/8WLM/8wlm_protein.pdb structures/8WLM/8wlm_pocket.pdb structures/8WLM/8wlm_ligand.sdf structures/8WLM/8wlm_ligand.pdb structures/8WLM/8wlm_ligand.cif structures/8WLM/8wlm_complex.pdb structures/8WLM/8wlm_complex.cif 8WMS extended human DPPA3; human UHRF1 PHD domain human human DPPA3 residues 81-118 peptide; human UHRF1 PHD finger residues 299-366 Na Na "[""CHAIN:B""]" 1 Kd Kd = = 0.868 μM 868.0 [] unit_conversion 6.0614802748235075 success True direct_binding Isothermal titration calorimetry of hDPPA3(81–118) binding to hUHRF1 PHD; the crystallographic complex contains these same constructs. 3 Fig. 1c reports WT hDPPA3 K_D = 0.868 μM for hPHD; text identifies hDPPA3 residues 81–118 and hPHD residues 299–366. auto_single_measurement only accepted activity measurement [1] 1 structures\8WMS\8WMS_metadata.json point structures/8WMS/8wms_protein.pdb structures/8WMS/8wms_pocket.pdb structures/8WMS/8wms_ligand.pdb structures/8WMS/8wms_ligand.cif structures/8WMS/8wms_complex.pdb structures/8WMS/8wms_complex.cif 8WNG classic H. pylori isoleucyl-tRNA synthetase (HpIleRS) Helicobacter pylori HpIleRS expressed as an N-terminal His6-SUMO fusion; tag removed by Ulp1 before further purification Na Ile "[""ILE""]" 1 Kd Kd = = 13.9 ± 0.6 μM 13900.0 [] unit_conversion 4.856985199745905 success True direct_binding Isothermal titration calorimetry (ITC), 25 °C; purified HpIleRS binding Ile. Table 2 reports the WT protein value. 8 Table 2: WT HpIleRS with Ile, Kd 13.9 ± 0.6 μM. The text states that ITC measurements indicate HpIleRS binds Ile with this dissociation constant. auto_single_measurement only accepted activity measurement [1] 1 structures\8WNG\8WNG_metadata.json point structures/8WNG/8wng_protein.pdb structures/8WNG/8wng_pocket.pdb structures/8WNG/8wng_ligand.sdf structures/8WNG/8wng_ligand.pdb structures/8WNG/8wng_ligand.cif structures/8WNG/8wng_complex.pdb structures/8WNG/8wng_complex.cif 8WOM classic Arabidopsis ABCB19 Arabidopsis thaliana Na wild-type brassinolide "[""BLD""]" 1 Kd Kd = = 1.13 ± 0.54 µM 1130.0 [] unit_conversion 5.94692155651658 success True direct_binding Isothermal titration calorimetry (ITC) of purified wild-type ABCB19 reconstituted into amphipols with brassinolide. 5 “a binding between brassinolide and ABCB19 was detected using isothermal titration calorimetry (ITC) with a dissociation constant (Kd) of 1.13 ± 0.54 µM” auto_single_measurement only accepted activity measurement [1] 1 structures\8WOM\8WOM_metadata.json point structures/8WOM/8wom_protein.pdb structures/8WOM/8wom_pocket.pdb structures/8WOM/8wom_ligand.sdf structures/8WOM/8wom_ligand.pdb structures/8WOM/8wom_ligand.cif structures/8WOM/8wom_complex.pdb structures/8WOM/8wom_complex.cif 8WQA extended CUL2-RBX1-ELOB-ELOC-FEM1B Na Na Na CCDC89 C-degron "[""CHAIN:K"", ""CHAIN:L""]" 1 Kd Kd = = 2.2 ± 0.1 µM 2200.0 [] unit_conversion 5.657577319177793 success True direct_binding ITC; FEM1B-EB-EC ternary complex binding to CCDC89 SUMO-fusion C-degron. 6 Fig. 4b prints CCDC89 K_D = 2.2 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WQA\8WQA_metadata.json point structures/8WQA/8wqa_protein.pdb structures/8WQA/8wqa_pocket.pdb structures/8WQA/8wqa_ligand.pdb structures/8WQA/8wqa_ligand.cif structures/8WQA/8wqa_complex.pdb structures/8WQA/8wqa_complex.cif 8WQB extended CUL2-RBX1-ELOB-ELOC-FEM1B Na Na Na CCDC89 C-degron "[""CHAIN:K""]" 1 Kd Kd = = 2.2 ± 0.1 µM 2200.0 [] unit_conversion 5.657577319177793 success True direct_binding ITC; FEM1B-EB-EC ternary complex binding to CCDC89 SUMO-fusion C-degron. 6 Fig. 4b prints CCDC89 K_D = 2.2 ± 0.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WQB\8WQB_metadata.json point structures/8WQB/8wqb_protein.pdb structures/8WQB/8wqb_pocket.pdb structures/8WQB/8wqb_ligand.pdb structures/8WQB/8wqb_ligand.cif structures/8WQB/8wqb_complex.pdb structures/8WQB/8wqb_complex.cif 8WQE extended CUL2-RBX1-ELOB-ELOC-FEM1B Na Na Na CUX1 C-degron "[""POLYMER_ENTITY:6""]" 1 Kd Kd = = 2.8 ± 0.3 µM 2800.0 [] unit_conversion 5.552841968657781 success True direct_binding ITC; FEM1B-EB-EC ternary complex binding to CUX1 SUMO-fusion C-degron. 6 Fig. 4b prints CUX1 K_D = 2.8 ± 0.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WQE\8WQE_metadata.json point structures/8WQE/8wqe_protein.pdb structures/8WQE/8wqe_pocket.pdb structures/8WQE/8wqe_ligand.pdb structures/8WQE/8wqe_ligand.cif structures/8WQE/8wqe_complex.pdb structures/8WQE/8wqe_complex.cif 8WQF extended CUL2-RBX1-ELOB-ELOC-FEM1B Na Na Na CUX1 C-degron "[""CHAIN:K""]" 1 Kd Kd = = 2.8 ± 0.3 µM 2800.0 [] unit_conversion 5.552841968657781 success True direct_binding ITC; FEM1B-EB-EC ternary complex binding to CUX1 SUMO-fusion C-degron. 6 Fig. 4b prints CUX1 K_D = 2.8 ± 0.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WQF\8WQF_metadata.json point structures/8WQF/8wqf_protein.pdb structures/8WQF/8wqf_pocket.pdb structures/8WQF/8wqf_ligand.pdb structures/8WQF/8wqf_ligand.cif structures/8WQF/8wqf_complex.pdb structures/8WQF/8wqf_complex.cif 8WQI extended FEM1B Na Na Na CUX1 C-degron "[""CHAIN:G""]" 1 Kd Kd = = 2.8 ± 0.3 µM 2800.0 [] unit_conversion 5.552841968657781 success True direct_binding ITC; FEM1B-EB-EC ternary complex binding to CUX1 SUMO-fusion C-degron. 6 Fig. 4b prints CUX1 K_D = 2.8 ± 0.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WQI\8WQI_metadata.json point structures/8WQI/8wqi_protein.pdb structures/8WQI/8wqi_pocket.pdb structures/8WQI/8wqi_ligand.pdb structures/8WQI/8wqi_ligand.cif structures/8WQI/8wqi_complex.pdb structures/8WQI/8wqi_complex.cif 8WQM classic AtHPPD (4-hydroxyphenylpyruvate dioxygenase) Arabidopsis thaliana Codon-optimized AtHPPD in an N-terminal hexa-his-tagged vector with an HRV 3C protease cleavage site Na atovaquone "[""AOQ""]" 1 Ki Ki = = 44.63 ± 1.27 µM 44630.0 [] unit_conversion 4.3503731131594705 success True biochemical_inhibition Spectrophotometric AtHPPD inhibition assay monitoring maleylacetoacetate production; experiments performed in triplicate. 2 “Its inhibitory effect against AtHPPD was determined, with a Ki value of 44.63 ± 1.27 µM (Fig. 1C and S1B).” auto_single_measurement only accepted activity measurement [1] 1 structures\8WQM\8WQM_metadata.json point structures/8WQM/8wqm_protein.pdb structures/8WQM/8wqm_pocket.pdb structures/8WQM/8wqm_ligand.sdf structures/8WQM/8wqm_ligand.pdb structures/8WQM/8wqm_ligand.cif structures/8WQM/8wqm_complex.pdb structures/8WQM/8wqm_complex.cif 8WR2 classic Human pyridoxal kinase (PDXK) human hPDXK expressed from pET28a with an N-terminal His6 tag and thrombin cleavage site; His6 tag cleaved during purification Na Luteolin "[""LU2""]" 2 Kd Kd = = 6.61 ± 2.64 μM 6610.0 [] unit_conversion 5.17979854051436 success True direct_binding Surface plasmon resonance measurement of luteolin binding to PDXK. 3 “a surface plasmon resonance assay was employed to assess the binding affinity of luteolin for PDXK as a KD value of 6.61 ± 2.64 μM (Fig. 2C).” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8WR2\8WR2_metadata.json point structures/8WR2/8wr2_protein.pdb structures/8WR2/8wr2_pocket.pdb structures/8WR2/8wr2_ligand.sdf structures/8WR2/8wr2_ligand.pdb structures/8WR2/8wr2_ligand.cif structures/8WR2/8wr2_complex.pdb structures/8WR2/8wr2_complex.cif 8WS4 classic CYP199A4 Rhodopseudomonas palustris Na F182A 4-methoxybenzoic acid (4-MBA) "[""ANN""]" 1 Kd Kd = = 0.65 µM 650.0 [] unit_conversion 6.187086643357144 success True direct_binding UV-visible spectral titration of the F182A mutant toward substrate 1 (4-MBA). 6 Fig. 5 lists substrate 1 with Kd 0.65 µM; its caption identifies these as dissociation constants to the F182A mutant. Substrate 1 is 4-methoxybenzoic acid. auto_single_measurement only accepted activity measurement [1] 1 structures\8WS4\8WS4_metadata.json point structures/8WS4/8ws4_protein.pdb structures/8WS4/8ws4_pocket.pdb structures/8WS4/8ws4_ligand.sdf structures/8WS4/8ws4_ligand.pdb structures/8WS4/8ws4_ligand.cif structures/8WS4/8ws4_complex.pdb structures/8WS4/8ws4_complex.cif 8WTE extended 4TCR2 T-cell receptor and HLA-A*11:01 Mus musculus (4TCR2 T-cell receptor); Homo sapiens (HLA-A*11:01) Soluble 4TCR2; TCR alpha residues 1-198 and beta residues 1-240; engineered interchain disulfide C alpha Cys159-C beta Cys170 wild-type 4TCR2 KRAS-G12V peptide VVGAVGVGK "[""CHAIN:G"", ""CHAIN:J""]" 1 Kd Kd = = 30.8 µM 30800.0 [] unit_conversion 4.511449283499556 success True direct_binding Surface plasmon resonance; soluble 4TCR2 flowed over immobilized KRAS-G12V–HLA-A*11:01. 6 Fig. 4c reports 4TCR2 binding KRAS-G12V–HLA-A*11:01 with K_D = 30.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WTE\8WTE_metadata.json point structures/8WTE/8wte_protein.pdb structures/8WTE/8wte_pocket.pdb structures/8WTE/8wte_ligand.pdb structures/8WTE/8wte_ligand.cif structures/8WTE/8wte_complex.pdb structures/8WTE/8wte_complex.cif 8WUE classic sigma-1 receptor (xlo1R) Xenopus laevis Na Na dehydroepiandrosterone sulfate (DHEAS) "[""ZWY""]" 1 Kd Kd = = 18.0 ± 2.5 μM 18000.0 [] unit_conversion 4.7447274948966935 success True direct_binding Microscale thermophoresis (MST) binding assay; mean ± SD, N = 3 biologically independent experiments. 8 “wild-type xlo1R (Kd = 18.0 ± 2.5 μM; Fig. 4f and Supplementary Table 3)”. auto_single_measurement only accepted activity measurement [1] 1 structures\8WUE\8WUE_metadata.json point structures/8WUE/8wue_protein.pdb structures/8WUE/8wue_pocket.pdb structures/8WUE/8wue_ligand.sdf structures/8WUE/8wue_ligand.pdb structures/8WUE/8wue_ligand.cif structures/8WUE/8wue_complex.pdb structures/8WUE/8wue_complex.cif 8WUL extended Affinity-enhanced 4TCR2-MH T-cell receptor and HLA-A*11:01 Mus musculus (4TCR2 T-cell receptor); Homo sapiens (HLA-A*11:01) Soluble 4TCR2-MH; TCR alpha residues 1-198 and beta residues 1-240; engineered interchain disulfide C alpha Cys159-C beta Cys170 beta K51M; beta E100H KRAS-G12V peptide VVGAVGVGK "[""CHAIN:K"", ""CHAIN:N"", ""CHAIN:Q"", ""CHAIN:T""]" 1 Kd Kd = = 1.95 µM 1950.0 [] unit_conversion 5.709965388637482 success True direct_binding Surface plasmon resonance; 4TCR2-MH flowed over immobilized KRAS-G12V–HLA-A*11:01. 6 Fig. 4d reports 4TCR2-MH binding KRAS-G12V–HLA-A*11:01 with K_D = 1.95 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WUL\8WUL_metadata.json point structures/8WUL/8wul_protein.pdb structures/8WUL/8wul_pocket.pdb structures/8WUL/8wul_ligand.pdb structures/8WUL/8wul_ligand.cif structures/8WUL/8wul_complex.pdb structures/8WUL/8wul_complex.cif 8WUY classic TR3/Nur77 ligand-binding domain Homo sapiens LBD residues 361-598 with a C-terminal His-tag Na A8 (3,4,5-trihydroxy-N-methyl-N-octylbenzamide) "[""XBF""]" 1 Kd Kd = = 3.71 μM 3710.0 [] unit_conversion 5.430626090384954 success True direct_binding ITC isothermal titration of compound A8 with purified Nur77 LBD; one-site binding model. 3 “ITC isothermal titration calorimetry experiments showed that compound A8 could directly interact with LBD with a binding constant (KD) of 3.71 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8WUY\8WUY_metadata.json point structures/8WUY/8wuy_protein.pdb structures/8WUY/8wuy_pocket.pdb structures/8WUY/8wuy_ligand.sdf structures/8WUY/8wuy_ligand.pdb structures/8WUY/8wuy_ligand.cif structures/8WUY/8wuy_complex.pdb structures/8WUY/8wuy_complex.cif 8WUZ classic human caseinolytic peptidase P (hClP) human hClP residues 57-277 without mitochondrial localization sequence Na ZYZ-17 "[""XFU""]" 1 Kd Kd = = 15 nM 15.0 [] unit_conversion 7.823908740944319 success True direct_binding Microscale thermophoresis (MST) binding assay using recombinant hClpP. 5 “ZYZ-17 showed a Kd value of 15 nM (Fig. 3A), indicating its potent binding to recombinant hClpP.” auto_single_measurement only accepted activity measurement [1] 1 structures\8WUZ\8WUZ_metadata.json point structures/8WUZ/8wuz_protein.pdb structures/8WUZ/8wuz_pocket.pdb structures/8WUZ/8wuz_ligand.sdf structures/8WUZ/8wuz_ligand.pdb structures/8WUZ/8wuz_ligand.cif structures/8WUZ/8wuz_complex.pdb structures/8WUZ/8wuz_complex.cif 8WWB classic sigma-1 receptor (xlo1R) Xenopus laevis Na Na dehydroepiandrosterone sulfate (DHEAS) "[""ZWY""]" 1 Kd Kd = = 18.0 ± 2.5 μM 18000.0 [] unit_conversion 4.7447274948966935 success True direct_binding Microscale thermophoresis (MST) binding assay; mean ± SD, N = 3 biologically independent experiments. 8 “wild-type xlo1R (Kd = 18.0 ± 2.5 μM; Fig. 4f and Supplementary Table 3)”. auto_single_measurement only accepted activity measurement [1] 1 structures\8WWB\8WWB_metadata.json point structures/8WWB/8wwb_protein.pdb structures/8WWB/8wwb_pocket.pdb structures/8WWB/8wwb_ligand.sdf structures/8WWB/8wwb_ligand.pdb structures/8WWB/8wwb_ligand.cif structures/8WWB/8wwb_complex.pdb structures/8WWB/8wwb_complex.cif 8WX7 classic SHP2 human Human SHP2 isoform 1, residues 1-525; expressed with a TEV-cleavable His tag and purified after His-tag removal Na JAB-3186 (compound 22) "[""XD8""]" 2 Kd Kd = = 0.53 nM 0.53 [] unit_conversion 9.275724130399212 success True direct_binding Surface plasmon resonance (SPR) binding assay; compound 22. 5 Compound 22 exhibited comparable SHP2 IC50 (3.1 nM) and SPR Kd (0.53 nM). auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8WX7\8WX7_metadata.json point structures/8WX7/8wx7_protein.pdb structures/8WX7/8wx7_pocket.pdb structures/8WX7/8wx7_ligand.sdf structures/8WX7/8wx7_ligand.pdb structures/8WX7/8wx7_ligand.cif structures/8WX7/8wx7_complex.pdb structures/8WX7/8wx7_complex.cif 8WXQ extended WDR5 Na WDR5 seven tandem WD-40 repeats, residues 24-334 Na MBD3C40-51 peptide "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.13 ± 0.02 μM 130.0 [] unit_conversion 6.886056647693163 success True direct_binding ITC in 200 mM NaCl solution; WDR5 with MBD3C40-51 peptide. 5 Table 2 reports WDR5–MBD3C Kd = 0.13 ± 0.02 μM; Fig. 2D reports the same value. auto_single_measurement only accepted activity measurement [1] 1 structures\8WXQ\8WXQ_metadata.json point structures/8WXQ/8wxq_protein.pdb structures/8WXQ/8wxq_pocket.pdb structures/8WXQ/8wxq_ligand.pdb structures/8WXQ/8wxq_ligand.cif structures/8WXQ/8wxq_complex.pdb structures/8WXQ/8wxq_complex.cif 8WXR extended WDR5 Na WDR5 seven tandem WD-40 repeats, residues 24-334 MBD3C peptide F47A MBD3C40-51 (F47A) peptide "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.65 ± 0.03 μM 650.0 [] unit_conversion 6.187086643357144 success True direct_binding ITC in 200 mM NaCl solution; WDR5 with MBD3C40-51 F47A peptide. 5 Table 2 and Fig. 2D report WDR5–MBD3C F47A Kd = 0.65 ± 0.03 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8WXR\8WXR_metadata.json point structures/8WXR/8wxr_protein.pdb structures/8WXR/8wxr_pocket.pdb structures/8WXR/8wxr_ligand.pdb structures/8WXR/8wxr_ligand.cif structures/8WXR/8wxr_complex.pdb structures/8WXR/8wxr_complex.cif 8WXY classic BRD4 human Na Na compound 23 "[""XGN""]" 1 IC50 IC50 = = 7492 ± 1076 nM 7492.0 [] unit_conversion 5.1254022312968 success True biochemical_inhibition TR-FRET inhibitory activity assay; Table 2. 4 Table 2 reports compound 23: BRD4 BD1 IC50 = 7492 ± 1076 nM; footnote states activities were determined by TR-FRET. auto_single_measurement only accepted activity measurement [1] 1 structures\8WXY\8WXY_metadata.json point structures/8WXY/8wxy_protein.pdb structures/8WXY/8wxy_pocket.pdb structures/8WXY/8wxy_ligand.sdf structures/8WXY/8wxy_ligand.pdb structures/8WXY/8wxy_ligand.cif structures/8WXY/8wxy_complex.pdb structures/8WXY/8wxy_complex.cif 8WXZ classic Falcilysin Plasmodium falciparum Mature falcilysin residues 59-1193; N-terminal 58 residues excluded E132Q Hemoglobin beta chain peptide (VVYPWTQRFFESFGD) "[""ACY""]" 1 Kd Kd = = 499 nM 499.0 [] unit_conversion 6.30189945437661 success True direct_binding Binding of E132Q falcilysin to the hemoglobin β-peptide; value reported in comparison with peptide-binding-defective mutants. 4 “the E132Q single FLN mutant ... binds ... to the β-peptide with a Kd of 499 nM” auto_single_measurement only accepted activity measurement [1] 1 structures\8WXZ\8WXZ_metadata.json point structures/8WXZ/8wxz_protein.pdb structures/8WXZ/8wxz_pocket.pdb structures/8WXZ/8wxz_ligand.sdf structures/8WXZ/8wxz_ligand.pdb structures/8WXZ/8wxz_ligand.cif structures/8WXZ/8wxz_complex.pdb structures/8WXZ/8wxz_complex.cif 8WY3 classic BRD4 human Na Na compound 21 "[""XHE""]" 1 IC50 IC50 = = 4014 ± 613 nM 4014.0 [] unit_conversion 5.396422631848534 success True biochemical_inhibition TR-FRET inhibitory activity assay; Table 2. 4 Table 2 reports compound 21: BRD4 BD1 IC50 = 4014 ± 613 nM; footnote states activities were determined by TR-FRET. auto_single_measurement only accepted activity measurement [1] 1 structures\8WY3\8WY3_metadata.json point structures/8WY3/8wy3_protein.pdb structures/8WY3/8wy3_pocket.pdb structures/8WY3/8wy3_ligand.sdf structures/8WY3/8wy3_ligand.pdb structures/8WY3/8wy3_ligand.cif structures/8WY3/8wy3_complex.pdb structures/8WY3/8wy3_complex.cif 8WY7 classic BRD4 human Na Na compound 22 "[""XHN""]" 1 IC50 IC50 = = 4937 ± 2569 nM 4937.0 [] unit_conversion 5.306536872780469 success True biochemical_inhibition TR-FRET inhibitory activity assay; Table 2. 4 Table 2 reports compound 22: BRD4 BD1 IC50 = 4937 ± 2569 nM; footnote states activities were determined by TR-FRET. auto_single_measurement only accepted activity measurement [1] 1 structures\8WY7\8WY7_metadata.json point structures/8WY7/8wy7_protein.pdb structures/8WY7/8wy7_pocket.pdb structures/8WY7/8wy7_ligand.sdf structures/8WY7/8wy7_ligand.pdb structures/8WY7/8wy7_ligand.cif structures/8WY7/8wy7_complex.pdb structures/8WY7/8wy7_complex.cif 8X3S extended WDR5 human WDR5 residues 22-334 in complex with PTENalpha-NTE residues 1-173 Na PTENalpha-NTE residues 1-173 "[""CHAIN:B""]" 1 Kd Kd = = 17 ± 2 μM 17000.0 [] unit_conversion 4.769551078621726 success True direct_binding ITC measurement of recombinant PTENα-NTE1–173 binding WDR5 residues 22–334. 2 ITC data state that recombinant PTENα-NTE1–173 binds WDR5 residues 22–334 with Kd 17 ± 2 μM; Fig. 1 reports the same determination. auto_single_measurement only accepted activity measurement [1] 1 structures\8X3S\8X3S_metadata.json point structures/8X3S/8x3s_protein.pdb structures/8X3S/8x3s_pocket.pdb structures/8X3S/8x3s_ligand.pdb structures/8X3S/8x3s_ligand.cif structures/8X3S/8x3s_complex.pdb structures/8X3S/8x3s_complex.cif 8X44 classic PhDIMT1 (DIMT1) Pyrococcus horikoshii Full-length PhDIMT1 (873 bp), 6xHis-tagged pET-28a(+) construct wild-type 5'-methylthioadenosine (MTA) "[""MTA""]" 1 Kd Kd = = 5.30 ± 1.51 µM 5300.0 [] unit_conversion 5.275724130399211 success True direct_binding ITC measurement of wild-type PhDIMT1 binding MTA. 5 The text explicitly reports MTA binding: “K_D: 5.30 ± 1.51 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8X44\8X44_metadata.json point structures/8X44/8x44_protein.pdb structures/8X44/8x44_pocket.pdb structures/8X44/8x44_ligand.sdf structures/8X44/8x44_ligand.pdb structures/8X44/8x44_ligand.cif structures/8X44/8x44_complex.pdb structures/8X44/8x44_complex.cif 8X45 classic PhDIMT1 (DIMT1) Pyrococcus horikoshii Full-length PhDIMT1 (873 bp), 6xHis-tagged pET-28a(+) construct wild-type 5'-methylthioadenosine (MTA) "[""MTA""]" 1 Kd Kd = = 5.30 ± 1.51 µM 5300.0 [] unit_conversion 5.275724130399211 success True direct_binding ITC measurement of wild-type PhDIMT1 binding MTA. 5 The text explicitly reports MTA binding: “K_D: 5.30 ± 1.51 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8X45\8X45_metadata.json point structures/8X45/8x45_protein.pdb structures/8X45/8x45_pocket.pdb structures/8X45/8x45_ligand.sdf structures/8X45/8x45_ligand.pdb structures/8X45/8x45_ligand.cif structures/8X45/8x45_complex.pdb structures/8X45/8x45_complex.cif 8X46 classic PhDIMT1 (DIMT1) Pyrococcus horikoshii Full-length PhDIMT1 (873 bp), 6xHis-tagged pET-28a(+) construct wild-type adenosylornithine (SFG; sinefungin) "[""SFG""]" 1 Kd Kd = = 7.14 ± 1.75 µM 7140.0 [] unit_conversion 5.146301788223825 success True direct_binding ITC measurement of wild-type PhDIMT1 binding SFG. 4 Figure 1F visibly prints “K_D = 7.14 ± 1.75 µM” for SFG. auto_single_measurement only accepted activity measurement [1] 1 structures\8X46\8X46_metadata.json point structures/8X46/8x46_protein.pdb structures/8X46/8x46_pocket.pdb structures/8X46/8x46_ligand.sdf structures/8X46/8x46_ligand.pdb structures/8X46/8x46_ligand.cif structures/8X46/8x46_complex.pdb structures/8X46/8x46_complex.cif 8X47 classic PhDIMT1 (DIMT1) Pyrococcus horikoshii Full-length PhDIMT1 (873 bp), 6xHis-tagged pET-28a(+) construct wild-type S-adenosyl-L-homocysteine (SAH) "[""SAH""]" 1 Kd Kd = = 1.67 ± 0.40 µM 1670.0 [] unit_conversion 5.777283528852417 success True direct_binding ITC measurement of wild-type PhDIMT1 binding SAH. 4 Figure 1E visibly prints “K_D = 1.67 ± 0.40 µM” for SAH. auto_single_measurement only accepted activity measurement [1] 1 structures\8X47\8X47_metadata.json point structures/8X47/8x47_protein.pdb structures/8X47/8x47_pocket.pdb structures/8X47/8x47_ligand.sdf structures/8X47/8x47_ligand.pdb structures/8X47/8x47_ligand.cif structures/8X47/8x47_complex.pdb structures/8X47/8x47_complex.cif 8X7B classic alpha-synuclein human N-terminally acetylated alpha-synuclein E46K ThT "[""TFX""]" 1 Kd Kd = = 40.5 µM 40500.0 [] unit_conversion 4.392544976785332 success True direct_binding SPR binding assay using immobilized sonicated α-syn PFFs. 4 Figure 2B prints K_D = 40.5 µM for ThT binding to E46K α-syn fibrils; Methods identifies SPR affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8X7B\8X7B_metadata.json point structures/8X7B/8x7b_protein.pdb structures/8X7B/8x7b_pocket.pdb structures/8X7B/8x7b_ligand.sdf structures/8X7B/8x7b_ligand.pdb structures/8X7B/8x7b_ligand.cif structures/8X7B/8x7b_complex.pdb structures/8X7B/8x7b_complex.cif 8X7L classic alpha-synuclein human N-terminally acetylated alpha-synuclein E46K EB "[""IZ8""]" 1 Kd Kd = = 1.99 µM 1990.0 [] unit_conversion 5.701146923590294 success True direct_binding SPR binding assay using immobilized sonicated α-syn PFFs. 4 Figure 2B prints K_D = 1.99 µM for EB binding to E46K α-syn fibrils; Methods identifies SPR affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8X7L\8X7L_metadata.json point structures/8X7L/8x7l_protein.pdb structures/8X7L/8x7l_pocket.pdb structures/8X7L/8x7l_ligand.sdf structures/8X7L/8x7l_ligand.pdb structures/8X7L/8x7l_ligand.cif structures/8X7L/8x7l_complex.pdb structures/8X7L/8x7l_complex.cif 8X7M classic alpha-synuclein human N-terminally acetylated alpha-synuclein E46K CR "[""CGO""]" 1 Kd Kd = = 1.23 µM 1230.0 [] unit_conversion 5.910094888560602 success True direct_binding SPR binding assay using immobilized sonicated α-syn PFFs. 4 Figure 2B prints K_D = 1.23 µM for CR binding to E46K α-syn fibrils; Methods identifies SPR affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8X7M\8X7M_metadata.json point structures/8X7M/8x7m_protein.pdb structures/8X7M/8x7m_pocket.pdb structures/8X7M/8x7m_ligand.sdf structures/8X7M/8x7m_ligand.pdb structures/8X7M/8x7m_ligand.cif structures/8X7M/8x7m_complex.pdb structures/8X7M/8x7m_complex.cif 8X7O classic alpha-synuclein human N-terminally acetylated alpha-synuclein E46K PiB "[""IZV""]" 1 Kd Kd = = 13.1 µM 13100.0 [] unit_conversion 4.882728704344236 success True direct_binding SPR binding assay using immobilized sonicated α-syn PFFs. 4 Figure 2B prints K_D = 13.1 µM for PiB binding to E46K α-syn fibrils; Methods identifies SPR affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8X7O\8X7O_metadata.json point structures/8X7O/8x7o_protein.pdb structures/8X7O/8x7o_pocket.pdb structures/8X7O/8x7o_ligand.sdf structures/8X7O/8x7o_ligand.pdb structures/8X7O/8x7o_ligand.cif structures/8X7O/8x7o_complex.pdb structures/8X7O/8x7o_complex.cif 8X7P classic alpha-synuclein human N-terminally acetylated alpha-synuclein E46K CCA "[""V79""]" 1 Kd Kd = = 5.77 µM 5770.0 [] unit_conversion 5.238824186844269 success True direct_binding SPR binding assay using immobilized sonicated α-syn PFFs. 4 Figure 2B prints K_D = 5.77 µM for CCA binding to E46K α-syn fibrils; Methods identifies SPR affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8X7P\8X7P_metadata.json point structures/8X7P/8x7p_protein.pdb structures/8X7P/8x7p_pocket.pdb structures/8X7P/8x7p_ligand.sdf structures/8X7P/8x7p_ligand.pdb structures/8X7P/8x7p_ligand.cif structures/8X7P/8x7p_complex.pdb structures/8X7P/8x7p_complex.cif 8X7Q classic alpha-synuclein human N-terminally acetylated alpha-synuclein E46K pFTAA "[""3LS""]" 1 Kd Kd = = 0.736 µM 736.0 [] unit_conversion 6.133122185662501 success True direct_binding SPR binding assay using immobilized sonicated α-syn PFFs. 4 Figure 2B prints K_D = 0.736 µM for pFTAA binding to E46K α-syn fibrils; Methods identifies SPR affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8X7Q\8X7Q_metadata.json point structures/8X7Q/8x7q_protein.pdb structures/8X7Q/8x7q_pocket.pdb structures/8X7Q/8x7q_ligand.sdf structures/8X7Q/8x7q_ligand.pdb structures/8X7Q/8x7q_ligand.cif structures/8X7Q/8x7q_complex.pdb structures/8X7Q/8x7q_complex.cif 8X7R classic alpha-synuclein human N-terminally acetylated alpha-synuclein E46K C05-03 "[""Y9W""]" 1 Kd Kd = = 3.78 µM 3780.0 [] unit_conversion 5.422508200162774 success True direct_binding SPR binding assay using immobilized sonicated α-syn PFFs. 4 Figure 2B prints K_D = 3.78 µM for C05-03 binding to E46K α-syn fibrils; Methods identifies SPR affinity measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\8X7R\8X7R_metadata.json point structures/8X7R/8x7r_protein.pdb structures/8X7R/8x7r_pocket.pdb structures/8X7R/8x7r_ligand.sdf structures/8X7R/8x7r_ligand.pdb structures/8X7R/8x7r_ligand.cif structures/8X7R/8x7r_complex.pdb structures/8X7R/8x7r_complex.cif 8X8I classic AbBioC methyltransferase Acinetobacter baumannii Tag-free AbBioC obtained after removal of the N-terminal SUMO tag Na S-adenosyl-L-methionine (SAM) "[""SAM""]" 1 Kd Kd = = 2.57 ± 0.75 µM 2570.0 [] unit_conversion 5.590066876668706 success True direct_binding Isothermal titration calorimetry of AbBioC binding SAM. 9 Fig. 4G reports ITC binding of AbBioC to SAM with Kd = 2.57 ± 0.75 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8X8I\8X8I_metadata.json point structures/8X8I/8x8i_protein.pdb structures/8X8I/8x8i_pocket.pdb structures/8X8I/8x8i_ligand.sdf structures/8X8I/8x8i_ligand.pdb structures/8X8I/8x8i_ligand.cif structures/8X8I/8x8i_complex.pdb structures/8X8I/8x8i_complex.cif 8X8J classic AbBioC methyltransferase Acinetobacter baumannii Tag-free AbBioC obtained after removal of the N-terminal SUMO tag Na sinefungin (SIN) "[""SFG""]" 1 Kd Kd = = 0.808 ± 0.135 µM 808.0 [] unit_conversion 6.092588639225414 success True direct_binding Isothermal titration calorimetry of AbBioC binding sinefungin. 10 Fig. 5D reports ITC binding of AbBioC to SIN with Kd = 0.808 ± 0.135 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8X8J\8X8J_metadata.json point structures/8X8J/8x8j_protein.pdb structures/8X8J/8x8j_pocket.pdb structures/8X8J/8x8j_ligand.sdf structures/8X8J/8x8j_ligand.pdb structures/8X8J/8x8j_ligand.cif structures/8X8J/8x8j_complex.pdb structures/8X8J/8x8j_complex.cif 8X8K extended STBD1 Na STBD1(260-358) CBM20-containing fragment Na maltotetraose "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 358.20±37.60 µM 358200.0 [] unit_conversion 3.445874418486987 success True direct_binding Fluorescence-polarization assay measuring STBD1(260-358) binding to linear maltotetraose. 2 Fig. 1F prints: “maltotetraose, Kd=358.20±37.60 µM.” The caption identifies these as FP-based binding-affinity measurements of STBD1(260-358) with oligosaccharides. auto_single_measurement only accepted activity measurement [1] 1 structures\8X8K\8X8K_metadata.json point structures/8X8K/8x8k_protein.pdb structures/8X8K/8x8k_pocket.pdb structures/8X8K/8x8k_ligand.pdb structures/8X8K/8x8k_ligand.cif structures/8X8K/8x8k_complex.pdb structures/8X8K/8x8k_complex.cif 8X9F classic ChCODH2 Carboxydothermus hydrogenoformans Na R57G/N59L EV (ethyl viologen) "[""S8I""]" 1 Kd Kd = = 144 µM 144000.0 [] unit_conversion 3.8416375079047507 success True direct_binding Isothermal titration calorimetry under CO-saturated conditions; purified R57G/N59L protein was titrated with EVox. 4 “The dissociation constant (Kd) values were 449 µM for WT and 144 µM for R57G/N59L.” The ITC method specifies EVox as the injected ligand. auto_single_measurement only accepted activity measurement [1] 1 structures\8X9F\8X9F_metadata.json point structures/8X9F/8x9f_protein.pdb structures/8X9F/8x9f_pocket.pdb structures/8X9F/8x9f_ligand.sdf structures/8X9F/8x9f_ligand.pdb structures/8X9F/8x9f_ligand.cif structures/8X9F/8x9f_complex.pdb structures/8X9F/8x9f_complex.cif 8XF7 classic FtsB Streptococcus pyogenes FtsB lacking the first 27 amino acids, expressed with an N-terminal His6-SUMO tag Na Ferrioxamine E (FOE) "[""6L0""]" 1 Kd Kd = = 2.9 ± 1.0 nM 2.9 [] unit_conversion 8.537602002101044 success True direct_binding ITC; 50 mM acetate pH 5.5; Table 1. 6 Table 1 reports FOE with Fe: K_D = 2.9 ± 1.0 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8XF7\8XF7_metadata.json point structures/8XF7/8xf7_protein.pdb structures/8XF7/8xf7_pocket.pdb structures/8XF7/8xf7_ligand.sdf structures/8XF7/8xf7_ligand.pdb structures/8XF7/8xf7_ligand.cif structures/8XF7/8xf7_complex.pdb structures/8XF7/8xf7_complex.cif 8XF8 extended FtsB Streptococcus pyogenes FtsB lacking the first 27 amino acids, expressed with an N-terminal His6-SUMO tag Na Ferrioxamine B (FOB) "[""0UE""]" 1 Kd Kd = = 8.5 ± 2.2 nM 8.5 [] unit_conversion 8.070581074285707 success True direct_binding ITC; 50 mM acetate pH 5.5; Table 1. 6 Table 1 reports FOB with Fe: K_D = 8.5 ± 2.2 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8XF8\8XF8_metadata.json point structures/8XF8/8xf8_protein.pdb structures/8XF8/8xf8_pocket.pdb structures/8XF8/8xf8_ligand.pdb structures/8XF8/8xf8_ligand.cif structures/8XF8/8xf8_complex.pdb structures/8XF8/8xf8_complex.cif 8XFV extended human Golgi resident glutaminyl cyclase human Na Na compound 36; (Z)-3-((1H-benzo[d]imidazol-5-yl)methylene)-4-(piperidin-4-yloxy)indolin-2-one "[""A1D46""]" 1 IC50 IC50 = = 1.40 μM 1400.0 [] unit_conversion 5.853871964321762 success True biochemical_inhibition Coupled sQC/gQC–PGP-1 enzymatic inhibition assay; gQC IC50 reported for compound 36. 8 Table 4 reports compound 36: gQC IC50 = 1.40 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8XFV\8XFV_metadata.json point structures/8XFV/8xfv_protein.pdb structures/8XFV/8xfv_pocket.pdb structures/8XFV/8xfv_ligand.pdb structures/8XFV/8xfv_ligand.cif structures/8XFV/8xfv_complex.pdb structures/8XFV/8xfv_complex.cif 8XGA extended human Golgi resident glutaminyl cyclase human Na Na compound 32; (Z)-3-((1H-benzo[d]imidazol-5-yl)methylene)-4-((tetrahydro-2H-pyran-4-yl)oxy)indolin-2-one "[""A1D47""]" 1 IC50 IC50 = = 0.57 μM 570.0 [] unit_conversion 6.2441251443275085 success True biochemical_inhibition Coupled sQC/gQC–PGP-1 enzymatic inhibition assay; gQC IC50 reported for compound 32. 8 Table 4 reports compound 32: gQC IC50 = 0.57 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8XGA\8XGA_metadata.json point structures/8XGA/8xga_protein.pdb structures/8XGA/8xga_pocket.pdb structures/8XGA/8xga_ligand.pdb structures/8XGA/8xga_ligand.cif structures/8XGA/8xga_complex.pdb structures/8XGA/8xga_complex.cif 8XGB classic human secretory glutaminyl cyclase human Na Na PQ912; (S)-1-(1H-benzo[d]imidazol-5-yl)-5-(4-propoxyphenyl)imidazolidin-2-one "[""A1D49""]" 1 IC50 IC50 = = 0.036 μM 36.0 [] unit_conversion 7.443697499232712 success True biochemical_inhibition Coupled sQC/gQC–PGP-1 enzymatic inhibition assay; sQC IC50 reported for PQ912. 10 Table 5 reports PQ912: sQC IC50 = 0.036 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8XGB\8XGB_metadata.json point structures/8XGB/8xgb_protein.pdb structures/8XGB/8xgb_pocket.pdb structures/8XGB/8xgb_ligand.sdf structures/8XGB/8xgb_ligand.pdb structures/8XGB/8xgb_ligand.cif structures/8XGB/8xgb_complex.pdb structures/8XGB/8xgb_complex.cif 8XGK classic Keap1 Na Na Na compound 34 "[""A1LVB""]" 1 Kd Kd = = 0.0059 μM 5.8999999999999995 [] unit_conversion 8.229147988357855 success True direct_binding SPR direct-binding assay 9 Table 6 reports SPR Kd = 0.0059 μM for compound 34; Figure 8 identifies compound 34 in the Keap1 Kelch domain as PDB 8XGK. auto_single_measurement only accepted activity measurement [1] 1 structures\8XGK\8XGK_metadata.json point structures/8XGK/8xgk_protein.pdb structures/8XGK/8xgk_pocket.pdb structures/8XGK/8xgk_ligand.sdf structures/8XGK/8xgk_ligand.pdb structures/8XGK/8xgk_ligand.cif structures/8XGK/8xgk_complex.pdb structures/8XGK/8xgk_complex.cif 8XGT extended human secretory glutaminyl cyclase human Na Na compound 2; (Z)-3-((1H-benzo[d]imidazol-5-yl)methylene)-4-hydroxyindolin-2-one "[""A1D48""]" 1 IC50 IC50 = = 4.04 μM 4040.0 [] unit_conversion 5.393618634889394 success True biochemical_inhibition Coupled sQC/gQC–PGP-1 enzymatic inhibition assay; sQC IC50 reported for compound 2. 5 Table 1 reports compound 2: sQC IC50 = 4.04 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8XGT\8XGT_metadata.json point structures/8XGT/8xgt_protein.pdb structures/8XGT/8xgt_pocket.pdb structures/8XGT/8xgt_ligand.pdb structures/8XGT/8xgt_ligand.cif structures/8XGT/8xgt_complex.pdb structures/8XGT/8xgt_complex.cif 8XGV classic Keap1 Na Na Na compound 22 "[""A1LVC""]" 1 Kd Kd = = 0.0029 μM 2.9 [] unit_conversion 8.537602002101044 success True direct_binding SPR direct-binding assay 6 Table 3 reports SPR Kd = 0.0029 μM for compound 22; Figure 5 identifies compound 22 in the Keap1 Kelch domain as PDB 8XGV. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8XGV\8XGV_metadata.json point structures/8XGV/8xgv_protein.pdb structures/8XGV/8xgv_pocket.pdb structures/8XGV/8xgv_ligand.sdf structures/8XGV/8xgv_ligand.pdb structures/8XGV/8xgv_ligand.cif structures/8XGV/8xgv_complex.pdb structures/8XGV/8xgv_complex.cif 8XGY extended human secretory glutaminyl cyclase human Na Na compound 40; (R,Z)-3-((1H-benzo[d]imidazol-5-yl)methylene)-4-((1-acetylpyrrolidin-3-yl)oxy)indolin-2-one "[""A1D5C""]" 1 IC50 IC50 = = 0.41 μM 410.0 [] unit_conversion 6.3872161432802645 success True biochemical_inhibition Coupled sQC/gQC–PGP-1 enzymatic inhibition assay; sQC IC50 reported for compound 40. 10 Table 5 reports compound 40: sQC IC50 = 0.41 μM. The paper explicitly identifies the structure as sQC:40 (PDB 8XGY). auto_single_measurement only accepted activity measurement [1] 1 structures\8XGY\8XGY_metadata.json point structures/8XGY/8xgy_protein.pdb structures/8XGY/8xgy_pocket.pdb structures/8XGY/8xgy_ligand.pdb structures/8XGY/8xgy_ligand.cif structures/8XGY/8xgy_complex.pdb structures/8XGY/8xgy_complex.cif 8XP4 classic Human lysyl-tRNA synthetase (KARS) human KARS70-580; C-terminal 6xHis expression tag Na N6-acetyl-L-lysine (AcK) "[""ALY""]" 1 Kd Kd = = 407 ± 291 µM 407000.0 [] unit_conversion 3.3904055907747797 success True direct_binding Microscale thermophoresis assay of purified recombinant KARS binding AcK; KARS70–580 was His-tag labelled. 4 “Microscale Thermophoresis (MST) assays revealed that the dissociation constant (Kd) of KARS binding to AcK (407 ± 291 μM)…” auto_single_measurement only accepted activity measurement [1] 1 structures\8XP4\8XP4_metadata.json point structures/8XP4/8xp4_protein.pdb structures/8XP4/8xp4_pocket.pdb structures/8XP4/8xp4_ligand.sdf structures/8XP4/8xp4_ligand.pdb structures/8XP4/8xp4_ligand.cif structures/8XP4/8xp4_complex.pdb structures/8XP4/8xp4_complex.cif 8XR5 classic PD-L1 human PD-L1 residues 18-134 with a C-terminal 6xHis tag Na X18 "[""A1LV3""]" 1 IC50 IC50 = = 1.3 ± 0.1 nM 1.3 [] unit_conversion 8.886056647693163 success True biochemical_inhibition PD-1/PD-L1 HTRF binding assay. 7 Table 3 reports X18 IC50 = 1.3 ± 0.1 nM; the footnote specifies a PD-1/PD-L1 HTRF binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8XR5\8XR5_metadata.json point structures/8XR5/8xr5_protein.pdb structures/8XR5/8xr5_pocket.pdb structures/8XR5/8xr5_ligand.sdf structures/8XR5/8xr5_ligand.pdb structures/8XR5/8xr5_ligand.cif structures/8XR5/8xr5_complex.pdb structures/8XR5/8xr5_complex.cif 8XV7 extended UHRF1 Homo sapiens TTD-PHD domain, residues 134-366, with deletion of residues 167-175 deletion of residues 167-175 hStella peptide (hSTE-1; residues 75-121) "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H""]" 1 Kd Kd = = 786.00 ± 187.36 nM 786.0 [] unit_conversion 6.104577453960593 success True direct_binding ITC determination of hSTE-1 binding to UHRF1 TTD-PHD. 8 Fig. 5g reports Kd = 786.00 ± 187.36 nM for hSTE-1 with TTD-PHD; the figure caption states these affinities were determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8XV7\8XV7_metadata.json point structures/8XV7/8xv7_protein.pdb structures/8XV7/8xv7_pocket.pdb structures/8XV7/8xv7_ligand.pdb structures/8XV7/8xv7_ligand.cif structures/8XV7/8xv7_complex.pdb structures/8XV7/8xv7_complex.cif 8XV8 extended UHRF1 Homo sapiens PHD domain, residues 298-367 Na hStella peptide (hSTE-1; residues 75-121) "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H""]" 1 Kd Kd = = 818.00 ± 42.58 nM 818.0 [] unit_conversion 6.087246696328677 success True direct_binding ITC determination of hSTE-1 binding to the UHRF1 PHD domain. 8 Fig. 5g reports Kd = 818.00 ± 42.58 nM for hSTE-1 with PHD; the figure caption states these affinities were determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8XV8\8XV8_metadata.json point structures/8XV8/8xv8_protein.pdb structures/8XV8/8xv8_pocket.pdb structures/8XV8/8xv8_ligand.pdb structures/8XV8/8xv8_ligand.cif structures/8XV8/8xv8_complex.pdb structures/8XV8/8xv8_complex.cif 8XWD classic alpha-synuclein fibril human full-length alpha-synuclein wild-type (WT) epigallocatechin gallate (EGCG) "[""KDH""]" 1 Kd Kd = = 2.88 × 10^-6 M 2880.0 [] unit_conversion 5.5406075122407685 success True direct_binding SPR association/dissociation measurement using sonicated alpha-synuclein preformed fibrils (PFFs) and EGCG. 6 Figure 3A visibly reports “K_D = 2.88 × 10^-6 M” for EGCG binding to alpha-syn PFFs; the main text identifies the corresponding EGCG–alpha-syn fibril cryo-EM structure. auto_single_measurement only accepted activity measurement [1] 1 structures\8XWD\8XWD_metadata.json point structures/8XWD/8xwd_protein.pdb structures/8XWD/8xwd_pocket.pdb structures/8XWD/8xwd_ligand.sdf structures/8XWD/8xwd_ligand.pdb structures/8XWD/8xwd_ligand.cif structures/8XWD/8xwd_complex.pdb structures/8XWD/8xwd_complex.cif 8Y0V classic HIF prolyl hydroxylase 2 (PHD2) Na Recombinant PHD2 residues 181-426; crystallized PHD2 residues P181-E407 Na ISM012-042 "[""A1D5X""]" 1 IC50 IC50 = = 2.5 nM 2.5 [] unit_conversion 8.602059991327963 success True biochemical_inhibition PHD2 hydroxylase assay; ISM012-042 inhibition relative to DMSO control. 2 “ISM012-042 inhibited PHD1 and PHD2 hydroxylase activity with IC50 values of 1.9 and 2.5 nM, respectively”; Fig. 1e labels the PHD2 hydroxylase assay IC50 as 2.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y0V\8Y0V_metadata.json point structures/8Y0V/8y0v_protein.pdb structures/8Y0V/8y0v_pocket.pdb structures/8Y0V/8y0v_ligand.sdf structures/8Y0V/8y0v_ligand.pdb structures/8Y0V/8y0v_ligand.cif structures/8Y0V/8y0v_complex.pdb structures/8Y0V/8y0v_complex.cif 8Y1U extended ASB7-Elongin B/C human ASB7 residues 11-318; Elongin B residues 1-104; Elongin C residues 17-112; bound to a 23-residue LZTS1 peptide Na LZTS1-degron peptide "[""CHAIN:B""]" 1 Kd Kd = = 0.8 μM 800.0 [] unit_conversion 6.096910013008056 success True direct_binding Isothermal titration calorimetry of purified ASB7-Elongin B/C with the synthesized LZTS1 degron peptide. 2 Figure 1f labels the LZTS1-degron interaction with ASB7-Elongin B/C as K_D = 0.8 μM; the adjacent text states that corresponding 23-residue peptides were tested by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y1U\8Y1U_metadata.json point structures/8Y1U/8y1u_protein.pdb structures/8Y1U/8y1u_pocket.pdb structures/8Y1U/8y1u_ligand.pdb structures/8Y1U/8y1u_ligand.cif structures/8Y1U/8y1u_complex.pdb structures/8Y1U/8y1u_complex.cif 8Y1Y extended MCL-1 Na Na Na BAK-BH3long "[""CHAIN:B""]" 1 Kd Kd = = 33.4 ± 5.0 nM 33.4 [] unit_conversion 7.476253533188435 success True direct_binding SPR; immobilized MCL-1 WT. 3 Table S2 reports K_D = 33.4 ± 5.0 nM for immobilized MCL-1 WT and BAK-BH3long; Table S1 maps MCL-1/BAK-BH3long to PDB 8Y1Y. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y1Y\8Y1Y_metadata.json point structures/8Y1Y/8y1y_protein.pdb structures/8Y1Y/8y1y_pocket.pdb structures/8Y1Y/8y1y_ligand.pdb structures/8Y1Y/8y1y_ligand.cif structures/8Y1Y/8y1y_complex.pdb structures/8Y1Y/8y1y_complex.cif 8Y20 classic MCL-1 Na MBP-MCL-1 Na A-1210477 "[""A1LXV""]" 1 Kd Kd = = 10.9 ± 2.2 nM 10.9 [] unit_conversion 7.962573502059376 success True direct_binding SPR; immobilized MCL-1 WT. 3 Table S3 reports K_D = 10.9 ± 2.2 nM for immobilized MCL-1 WT and A-1210477; Table S1 maps MBP-MCL-1/A-1210477 to PDB 8Y20. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y20\8Y20_metadata.json point structures/8Y20/8y20_protein.pdb structures/8Y20/8y20_pocket.pdb structures/8Y20/8y20_ligand.sdf structures/8Y20/8y20_ligand.pdb structures/8Y20/8y20_ligand.cif structures/8Y20/8y20_complex.pdb structures/8Y20/8y20_complex.cif 8Y42 classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na compound 51 "[""A1D51""]" 1 IC50 IC50 = = 20.7±1.2 nM 20.7 [] unit_conversion 7.684029654543082 success True biochemical_inhibition Purified SARS-CoV-2 3CLpro FRET inhibition assay. 8 Table 2 reports compound 51 IC50 = 20.7±1.2 nM; Figure 3 identifies compound 51 as PDB 8Y42. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y42\8Y42_metadata.json point structures/8Y42/8y42_protein.pdb structures/8Y42/8y42_pocket.pdb structures/8Y42/8y42_ligand.sdf structures/8Y42/8y42_ligand.pdb structures/8Y42/8y42_ligand.cif structures/8Y42/8y42_complex.pdb structures/8Y42/8y42_complex.cif 8Y44 classic SARS-CoV-2 3CL protease (3CLpro) SARS-CoV-2 Na Na compound 44 "[""A1D50""]" 1 IC50 IC50 = = 32.7±0.6 nM 32.7 [] unit_conversion 7.485452247339714 success True biochemical_inhibition Purified SARS-CoV-2 3CLpro FRET inhibition assay. 7 Table 2 reports compound 44 IC50 = 32.7±0.6 nM; Figure 3 identifies compound 44 as PDB 8Y44. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y44\8Y44_metadata.json point structures/8Y44/8y44_protein.pdb structures/8Y44/8y44_pocket.pdb structures/8Y44/8y44_ligand.sdf structures/8Y44/8y44_ligand.pdb structures/8Y44/8y44_ligand.cif structures/8Y44/8y44_complex.pdb structures/8Y44/8y44_complex.cif 8Y58 extended TRIM21 human PRYSPRY residues 287-465 with an N-terminal 6xHis tag D355A acepromazine (ACE) "[""PMZ""]" 1 Kd Kd = = 5.66 µM 5660.0 [] unit_conversion 5.247183568811728 success True direct_binding Isothermal titration calorimetry of ACE into purified TRIM21 D355A PRYSPRY. 12 Figure 6A prints Kd (µM) = 5.66 for ACE; the text identifies binding to TRIM21 D355A PRYSPRY. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y58\8Y58_metadata.json point structures/8Y58/8y58_protein.pdb structures/8Y58/8y58_pocket.pdb structures/8Y58/8y58_ligand.pdb structures/8Y58/8y58_ligand.cif structures/8Y58/8y58_complex.pdb structures/8Y58/8y58_complex.cif 8Y59 extended TRIM21 human PRYSPRY residues 287-465 with an N-terminal 6xHis tag D355A (S)-ACE-OH ((S)-hydroxyl-acepromazine) "[""A1D5Y""]" 1 Kd Kd = = 17.9 µM 17900.0 [] unit_conversion 4.747146969020107 success True direct_binding Isothermal titration calorimetry of (S)-ACE-OH into purified TRIM21 D355A PRYSPRY. 12 Figure 6A prints Kd (µM) = 17.9 for (S)-ACE-OH; the text identifies binding to TRIM21 D355A PRYSPRY. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y59\8Y59_metadata.json point structures/8Y59/8y59_protein.pdb structures/8Y59/8y59_pocket.pdb structures/8Y59/8y59_ligand.pdb structures/8Y59/8y59_ligand.cif structures/8Y59/8y59_complex.pdb structures/8Y59/8y59_complex.cif 8Y5B extended TRIM21 human PRYSPRY residues 287-465 with an N-terminal 6xHis tag D355A (R)-ACE-OH ((R)-hydroxyl-acepromazine) "[""A1D5Z""]" 1 Kd Kd = = 9.11 µM 9110.0 [] unit_conversion 5.040481623027002 success True direct_binding Isothermal titration calorimetry of (R)-ACE-OH into purified TRIM21 D355A PRYSPRY. 12 Figure 6A prints Kd (µM) = 9.11 for (R)-ACE-OH; the text identifies binding to TRIM21 D355A PRYSPRY. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y5B\8Y5B_metadata.json point structures/8Y5B/8y5b_protein.pdb structures/8Y5B/8y5b_pocket.pdb structures/8Y5B/8y5b_ligand.pdb structures/8Y5B/8y5b_ligand.cif structures/8Y5B/8y5b_complex.pdb structures/8Y5B/8y5b_complex.cif 8Y5V extended Norovirus GII.4 Sydney P domain Na Na Na 2'-FL "[""BRANCHED_ENTITY:2""]" 1 IC50 IC50 = = 7.5 mM 7500000.0 [] unit_conversion 2.1249387366083 success True biochemical_inhibition Direct ELISA measuring inhibition of GII.4 VLP binding to human A-type saliva (HBGA source). 1 Both 2′-FL powder and crushed tablets inhibited GII.4 VLP binding to A-type saliva, with IC50 values of 7.5 mM and 36 mM, respectively. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y5V\8Y5V_metadata.json point structures/8Y5V/8y5v_protein.pdb structures/8Y5V/8y5v_pocket.pdb structures/8Y5V/8y5v_ligand.pdb structures/8Y5V/8y5v_ligand.cif structures/8Y5V/8y5v_complex.pdb structures/8Y5V/8y5v_complex.cif 8Y65 classic human urate transporter GLUT9 human Na Na urate "[""URC""]" 1 Kd Kd = = 230.9 ± 17.1 μM 230900.0 [] unit_conversion 3.6365760670828235 success True direct_binding Microscale thermophoresis (MST) measurement with purified GLUT9 and urate. 4 Fig. 2f reports the GLUT9-UA binding affinity as 230.9 ± 17.1 μM by MST. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y65\8Y65_metadata.json point structures/8Y65/8y65_protein.pdb structures/8Y65/8y65_pocket.pdb structures/8Y65/8y65_ligand.sdf structures/8Y65/8y65_ligand.pdb structures/8Y65/8y65_ligand.cif structures/8Y65/8y65_complex.pdb structures/8Y65/8y65_complex.cif 8Y66 classic human urate transporter GLUT9 human Na Na apigenin "[""AGI""]" 1 Kd Kd = = 0.5 ± 0.1 μM 500.0 [] unit_conversion 6.301029995663981 success True direct_binding Microscale thermophoresis (MST) measurement with purified GLUT9 and apigenin. 6 Fig. 4e reports the GLUT9-API binding affinity as 0.5 ± 0.1 μM by MST. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y66\8Y66_metadata.json point structures/8Y66/8y66_protein.pdb structures/8Y66/8y66_pocket.pdb structures/8Y66/8y66_ligand.sdf structures/8Y66/8y66_ligand.pdb structures/8Y66/8y66_ligand.cif structures/8Y66/8y66_complex.pdb structures/8Y66/8y66_complex.cif 8Y7L classic Nur77 LBD Na Na Na NB1; N-(2'-(4-hydroxypiperidin-1-yl)-[4,4'-bipyridin]-2-yl)cinnamamide "[""A1D59""]" 1 Kd Kd = = 0.12 µmol/L 120.0 [] unit_conversion 6.920818753952375 success True direct_binding SPR analysis of NB1 binding to Nur77 LBD. 3 Figure 1G is labeled “NB1-Nur77 K_D = 0.12 µmol/L”; the caption states it is “SPR analysis of NB1 binding to Nur77LBD,” and Figure 1H identifies the NB1/Nur77LBD crystal structure as PDB ID 8Y7L. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y7L\8Y7L_metadata.json point structures/8Y7L/8y7l_protein.pdb structures/8Y7L/8y7l_pocket.pdb structures/8Y7L/8y7l_ligand.sdf structures/8Y7L/8y7l_ligand.pdb structures/8Y7L/8y7l_ligand.cif structures/8Y7L/8y7l_complex.pdb structures/8Y7L/8y7l_complex.cif 8Y9O classic AtKAI2 Arabidopsis thaliana AtKAI2 expressed from pET-48b(+) with an N-terminal Trx-His6 tag, removed by HRV3C protease before crystallization Na KK181N1 "[""IB0""]" 1 Kd Kd = = 27.7 ± 0.7 µM 27700.0 [] unit_conversion 4.557520230935552 success True direct_binding Isothermal titration calorimetry (ITC) of purified AtKAI2 with KK181N1; three independent experiments. 5 Fig. 2a reports: “AtKAI2 Kd = 27.7 ± 0.7 µM”; the caption states the value was calculated from three independent experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\8Y9O\8Y9O_metadata.json point structures/8Y9O/8y9o_protein.pdb structures/8Y9O/8y9o_pocket.pdb structures/8Y9O/8y9o_ligand.sdf structures/8Y9O/8y9o_ligand.pdb structures/8Y9O/8y9o_ligand.cif structures/8Y9O/8y9o_complex.pdb structures/8Y9O/8y9o_complex.cif 8YD2 classic MtbClpP1P2 complex M. tuberculosis Na Na bortezomib (BTZ) "[""BO2""]" 1 IC50 IC50 = = 43 µM 43000.0 [] unit_conversion 4.366531544420414 success True biochemical_inhibition PMK-AMC hydrolysis by purified MtbClpP1P2 complex; IC50 estimated from the inhibition portion of the BTZ dose-response. 3 Fig. 1b visibly prints IC50 = 43 µM for PMK-AMC hydrolysis by the MtbClpP1P2 complex; the text identifies this as BTZ inhibition at high concentration after low-concentration activation. auto_single_measurement only accepted activity measurement [1] 1 structures\8YD2\8YD2_metadata.json point structures/8YD2/8yd2_protein.pdb structures/8YD2/8yd2_pocket.pdb structures/8YD2/8yd2_ligand.sdf structures/8YD2/8yd2_ligand.pdb structures/8YD2/8yd2_ligand.cif structures/8YD2/8yd2_complex.pdb structures/8YD2/8yd2_complex.cif 8YDU extended SARS-CoV-2 spike protein SARS-CoV-2 Na Na CeSPIACE "[""CHAIN:A""]" 1 Kd Kd = = 219 ± 6 pM 0.219 [] unit_conversion 9.659555885159882 success True direct_binding SPR affinity measurement using tandem-linked CeSPIACE and immobilized mutant RBDs; Fig. 2D. 4 Fig. 2D lists BA.2 RBD binding K_D as 219 ± 6 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\8YDU\8YDU_metadata.json point structures/8YDU/8ydu_protein.pdb structures/8YDU/8ydu_pocket.pdb structures/8YDU/8ydu_ligand.pdb structures/8YDU/8ydu_ligand.cif structures/8YDU/8ydu_complex.pdb structures/8YDU/8ydu_complex.cif 8YDV extended SARS-CoV-2 spike protein SARS-CoV-2 Na Na CeSPIACE "[""CHAIN:A"", ""CHAIN:C""]" 1 Kd Kd = = 667 ± 13 pM 0.667 [] unit_conversion 9.175874166083451 success True direct_binding SPR affinity measurement using tandem-linked CeSPIACE and immobilized mutant RBDs; Fig. 2D. 4 Fig. 2D lists BA.5 RBD binding K_D as 667 ± 13 pM. auto_single_measurement only accepted activity measurement [1] 1 structures\8YDV\8YDV_metadata.json point structures/8YDV/8ydv_protein.pdb structures/8YDV/8ydv_pocket.pdb structures/8YDV/8ydv_ligand.pdb structures/8YDV/8ydv_ligand.cif structures/8YDV/8ydv_complex.pdb structures/8YDV/8ydv_complex.cif 8YE8 extended mouse BAHCC1 TTD domain mouse Bahcc1 residues 1904-2044 wild-type (WT) H4(14-25)K20me1 peptide "[""CHAIN:C""]" 1 Kd Kd = = 40.4 ± 2.7 µM 40400.0 [] unit_conversion 4.393618634889395 success True direct_binding Isothermal titration calorimetry (ITC) of murine Bahcc1 TTD with H4(14-25)K20me1 peptide. 4 Table 1 reports Bahcc1_TTD, WT binding to H4K20me1(14-25) with Kd 40.4 ± 2.7 µM; the paper identifies PDB 8YE8 as the Bahcc1 TTD:H4K20me1 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8YE8\8YE8_metadata.json point structures/8YE8/8ye8_protein.pdb structures/8YE8/8ye8_pocket.pdb structures/8YE8/8ye8_ligand.pdb structures/8YE8/8ye8_ligand.cif structures/8YE8/8ye8_complex.pdb structures/8YE8/8ye8_complex.cif 8YEV classic Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) Na Na Na coumestrol "[""CUE""]" 1 IC50 IC50 = = 2.3 µM 2300.0 [] unit_conversion 5.638272163982407 success True biochemical_inhibition Z'LYTE enzyme-based kinase inhibition assay; coumestrol inhibition of DYRK1A. 6 “An enzyme-based assay confirmed that coumestrol dose-dependently inhibited DYRK1A activity, with an IC50 of 2.3 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8YEV\8YEV_metadata.json point structures/8YEV/8yev_protein.pdb structures/8YEV/8yev_pocket.pdb structures/8YEV/8yev_ligand.sdf structures/8YEV/8yev_ligand.pdb structures/8YEV/8yev_ligand.cif structures/8YEV/8yev_complex.pdb structures/8YEV/8yev_complex.cif 8YFK extended FIP200 Homo sapiens FIP200 claw domain residues 1490-1594 Na TNIP1_FIR_pS123 "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 160.0 ± 15.8 µM 160000.0 [] unit_conversion 3.795880017344075 success True direct_binding Isothermal titration calorimetry (ITC) of FIP200 claw domain with TNIP1 FIR peptide pS123. 2 Figure 1A prints K_D = 160.0 ± 15.8 µM for pS123; the text states binding capacity was assessed by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8YFK\8YFK_metadata.json point structures/8YFK/8yfk_protein.pdb structures/8YFK/8yfk_pocket.pdb structures/8YFK/8yfk_ligand.pdb structures/8YFK/8yfk_ligand.cif structures/8YFK/8yfk_complex.pdb structures/8YFK/8yfk_complex.cif 8YFL extended FIP200 Homo sapiens FIP200 claw domain residues 1490-1594 Na TNIP1_FIR_pS122pS123 "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 195.0 ± 30.8 µM 195000.0 [] unit_conversion 3.7099653886374817 success True direct_binding Isothermal titration calorimetry (ITC) of FIP200 claw domain with doubly phosphorylated TNIP1 FIR peptide pS122pS123. 2 Figure 1A prints K_D = 195.0 ± 30.8 µM for pS122pS123; the text states binding capacity was assessed by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8YFL\8YFL_metadata.json point structures/8YFL/8yfl_protein.pdb structures/8YFL/8yfl_pocket.pdb structures/8YFL/8yfl_ligand.pdb structures/8YFL/8yfl_ligand.cif structures/8YFL/8yfl_complex.pdb structures/8YFL/8yfl_complex.cif 8YFM extended FIP200 Homo sapiens FIP200 claw domain residues 1490-1594 Na TNIP1_FIR_pS122 "[""CHAIN:B"", ""CHAIN:E""]" 1 Kd Kd = = 260.0 ± 82.3 µM 260000.0 [] unit_conversion 3.585026652029182 success True direct_binding Isothermal titration calorimetry (ITC) of FIP200 claw domain with TNIP1 FIR peptide pS122. 2 Figure 1A prints K_D = 260.0 ± 82.3 µM for pS122; the text states binding capacity was assessed by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\8YFM\8YFM_metadata.json point structures/8YFM/8yfm_protein.pdb structures/8YFM/8yfm_pocket.pdb structures/8YFM/8yfm_ligand.pdb structures/8YFM/8yfm_ligand.cif structures/8YFM/8yfm_complex.pdb structures/8YFM/8yfm_complex.cif 8YHQ classic cytochrome bc1 complex (complex III) Saccharomyces cerevisiae Na Na pyraclostrobin (PYR) "[""A1D6K""]" 1 Ki Ki = = 0.76 ± 0.02 nM 0.76 [] unit_conversion 9.119186407719209 success True biochemical_inhibition In vitro inhibition of yeast complex III; Figure 1B reports Ki for PYR. 2 Figure 1B lists yeast Ki values: MET, 0.92 ± 0.09 nM; PYR, 0.76 ± 0.02 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8YHQ\8YHQ_metadata.json point structures/8YHQ/8yhq_protein.pdb structures/8YHQ/8yhq_pocket.pdb structures/8YHQ/8yhq_ligand.sdf structures/8YHQ/8yhq_ligand.pdb structures/8YHQ/8yhq_ligand.cif structures/8YHQ/8yhq_complex.pdb structures/8YHQ/8yhq_complex.cif 8YIE extended GH13_30 alpha-glucosidase CmmB Arthrobacter globiformis Na Na acarbose "[""BRANCHED_ENTITY:2""]" 1 Ki Ki = = 2.37 ± 0.06 µM 2370.0 [] unit_conversion 5.625251653989896 success True biochemical_inhibition Competitive inhibition of purified CmmB-catalyzed pNPG hydrolysis; reaction rates were measured with 0, 2.5, and 5 µM acarbose. 5 The paper states that acarviosin and acarbose acted as competitive inhibitors and reports Ki values of 1.23 ± 0.05 and 2.37 ± 0.06 µM, respectively. Table 1 maps 8YIE to the acarbose complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8YIE\8YIE_metadata.json point structures/8YIE/8yie_protein.pdb structures/8YIE/8yie_pocket.pdb structures/8YIE/8yie_ligand.pdb structures/8YIE/8yie_ligand.cif structures/8YIE/8yie_complex.pdb structures/8YIE/8yie_complex.cif 8YIF classic GH13_30 alpha-glucosidase CmmB Arthrobacter globiformis Na Na acarviosin "[""A1L2I""]" 1 Ki Ki = = 1.23 ± 0.05 µM 1230.0 [] unit_conversion 5.910094888560602 success True biochemical_inhibition Competitive inhibition of purified CmmB-catalyzed pNPG hydrolysis; reaction rates were measured with 0, 0.313, and 1.25 µM acarviosin. 5 The paper states that acarviosin and acarbose acted as competitive inhibitors and reports Ki values of 1.23 ± 0.05 and 2.37 ± 0.06 µM, respectively. Table 1 maps 8YIF to the acarviosin complex. auto_single_measurement only accepted activity measurement [1] 1 structures\8YIF\8YIF_metadata.json point structures/8YIF/8yif_protein.pdb structures/8YIF/8yif_pocket.pdb structures/8YIF/8yif_ligand.sdf structures/8YIF/8yif_ligand.pdb structures/8YIF/8yif_ligand.cif structures/8YIF/8yif_complex.pdb structures/8YIF/8yif_complex.cif 8YIN classic cytochrome bc1 complex (complex III) Saccharomyces cerevisiae Na Na YF23694 "[""A1D6O""]" 2 Ki Ki = = 2.56 ± 0.25 nM 2.56 [] unit_conversion 8.59176003468815 success True biochemical_inhibition In vitro yeast complex III inhibition kinetics; Figure 6D reports Ki. 7 Figure 6D reports YF23694 Ki = 2.56 ± 0.25 nM for yeast complex III. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8YIN\8YIN_metadata.json point structures/8YIN/8yin_protein.pdb structures/8YIN/8yin_pocket.pdb structures/8YIN/8yin_ligand.sdf structures/8YIN/8yin_ligand.pdb structures/8YIN/8yin_ligand.cif structures/8YIN/8yin_complex.pdb structures/8YIN/8yin_complex.cif 8YJC classic Vibrio vulnificus MARTX cysteine protease domain Vibrio vulnificus Residues 3578-3796 C3727A InsP6 "[""IHP""]" 1 Kd Kd = = 1.4 ± 0.5 μM 1400.0 [] unit_conversion 5.853871964321762 success True direct_binding Isothermal titration calorimetry of pre-CPD C3727A (3570–3796) with InsP6. 9 “The binding affinity of InsP6 to the pre-CPD C3727A was 1.4 ± 0.5 μM measured by isothermal titration calorimetry (Fig 3D).” auto_single_measurement only accepted activity measurement [1] 1 structures\8YJC\8YJC_metadata.json point structures/8YJC/8yjc_protein.pdb structures/8YJC/8yjc_pocket.pdb structures/8YJC/8yjc_ligand.sdf structures/8YJC/8yjc_ligand.pdb structures/8YJC/8yjc_ligand.cif structures/8YJC/8yjc_complex.pdb structures/8YJC/8yjc_complex.cif 8YQ8 classic Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) Plasmodium falciparum PfDHFR-TS V1/S N51I+C59R+S108N+I164L FB8 "[""A1LZS""]" 1 Ki Ki = = 0.62 nM 0.62 [] unit_conversion 9.207608310501746 success True biochemical_inhibition DHFR inhibition assay; Table 1 Pf QM result. 3 Table 1 reports FB8 Ki of 0.62 nM against Pf QM; QM is defined as N51I + C59R + S108N + I164L. The paper maps FB8 to PDB 8YQ8. auto_single_measurement only accepted activity measurement [1] 1 structures\8YQ8\8YQ8_metadata.json point structures/8YQ8/8yq8_protein.pdb structures/8YQ8/8yq8_pocket.pdb structures/8YQ8/8yq8_ligand.sdf structures/8YQ8/8yq8_ligand.pdb structures/8YQ8/8yq8_ligand.cif structures/8YQ8/8yq8_complex.pdb structures/8YQ8/8yq8_complex.cif 8YQ9 classic Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) Plasmodium falciparum PfDHFR-TS V1/S N51I+C59R+S108N+I164L FB6 "[""A1LZT""]" 1 Ki Ki = = 0.24 nM 0.24 [] unit_conversion 9.619788758288394 success True biochemical_inhibition DHFR inhibition assay; Table 1 Pf QM result. 3 Table 1 reports FB6 Ki of 0.24 nM against Pf QM; QM is defined as N51I + C59R + S108N + I164L. The paper maps FB6 to PDB 8YQ9. auto_single_measurement only accepted activity measurement [1] 1 structures\8YQ9\8YQ9_metadata.json point structures/8YQ9/8yq9_protein.pdb structures/8YQ9/8yq9_pocket.pdb structures/8YQ9/8yq9_ligand.sdf structures/8YQ9/8yq9_ligand.pdb structures/8YQ9/8yq9_ligand.cif structures/8YQ9/8yq9_complex.pdb structures/8YQ9/8yq9_complex.cif 8YS6 classic 2-oxoglutarate:acceptor oxidoreductase (OOR; OorDABC) Helicobacter pylori OorDABC in pET-28b with an N-terminal hexahistidine tag Na Napabucasin (NPB) "[""A1D65""]" 1 Kd Kd = = 21.3 ± 8.41 nM 21.3 [] unit_conversion 7.671620396561262 success True direct_binding Microscale thermophoresis measurement of NPB binding to purified OOR. 6 Fig. 3b reports Kd = 21.3 ± 8.41 nM for NPB binding to OOR. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\8YS6\8YS6_metadata.json point structures/8YS6/8ys6_protein.pdb structures/8YS6/8ys6_pocket.pdb structures/8YS6/8ys6_ligand.sdf structures/8YS6/8ys6_ligand.pdb structures/8YS6/8ys6_ligand.cif structures/8YS6/8ys6_complex.pdb structures/8YS6/8ys6_complex.cif 8YTK classic Human cytoplasmic prolyl-tRNA synthetase (HsProRS) human Na Na PAA-5 "[""W2H""]" 1 IC50 IC50 = = 14.7 ± 2.0 nM 14.7 [] unit_conversion 7.8326826652518236 success True biochemical_inhibition Pre-transfer editing assay (PTEA) against HsProRS. 6 Table 1 reports PAA-5 IC50 = 14.7 ± 2.0 nM against HsProRS. auto_single_measurement only accepted activity measurement [1] 1 structures\8YTK\8YTK_metadata.json point structures/8YTK/8ytk_protein.pdb structures/8YTK/8ytk_pocket.pdb structures/8YTK/8ytk_ligand.sdf structures/8YTK/8ytk_ligand.pdb structures/8YTK/8ytk_ligand.cif structures/8YTK/8ytk_complex.pdb structures/8YTK/8ytk_complex.cif 8YWY classic SARS-CoV-2 main protease SARS-CoV-2 Na E166N Bofutrelvir "[""FHR""]" 1 IC50 IC50 > > 100 µM 100000.0 [] unit_conversion 4.0 success True biochemical_inhibition FRET-based protease inhibition assay. 2 Fig. 1a prints IC50>100 µM for the SARS-CoV-2 E166N protease; Table 1 maps PDB 8YWY to E166N-Bofutrelvir. auto_single_measurement only accepted activity measurement [1] 1 structures\8YWY\8YWY_metadata.json point structures/8YWY/8ywy_protein.pdb structures/8YWY/8ywy_pocket.pdb structures/8YWY/8ywy_ligand.sdf structures/8YWY/8ywy_ligand.pdb structures/8YWY/8ywy_ligand.cif structures/8YWY/8ywy_complex.pdb structures/8YWY/8ywy_complex.cif 8Z1S classic Na Na Na Na compound 4 "[""A1L0Q""]" 1 IC50 IC50 = = 67 ± 5 nM 67.0 [] unit_conversion 7.173925197299173 success True biochemical_inhibition mGal-3 IC50 assay; Figure 2 reports compound 4 (atropisomer 1). 3 Figure 2 explicitly reports for compound 4: mGal-3 IC50 (nM) = 67 ± 5; Figure 3 maps compound 4 to PDB ID 8Z1S bound with hGal-3. auto_single_measurement only accepted activity measurement [1] 1 structures\8Z1S\8Z1S_metadata.json point structures/8Z1S/8z1s_protein.pdb structures/8Z1S/8z1s_pocket.pdb structures/8Z1S/8z1s_ligand.sdf structures/8Z1S/8z1s_ligand.pdb structures/8Z1S/8z1s_ligand.cif structures/8Z1S/8z1s_complex.pdb structures/8Z1S/8z1s_complex.cif 8Z1T classic Na Na Na Na compound 5 "[""A1L0Q""]" 1 IC50 IC50 = = 7000 ± 2000 nM 7000.0 [] unit_conversion 5.154901959985743 success True biochemical_inhibition mGal-3 IC50 assay; Figure 2 reports compound 5 (atropisomer 2). 3 Figure 2 explicitly reports for compound 5: mGal-3 IC50 (nM) = 7000 ± 2000; Figure 3 maps compound 5 to PDB ID 8Z1T bound with hGal-3. auto_single_measurement only accepted activity measurement [1] 1 structures\8Z1T\8Z1T_metadata.json point structures/8Z1T/8z1t_protein.pdb structures/8Z1T/8z1t_pocket.pdb structures/8Z1T/8z1t_ligand.sdf structures/8Z1T/8z1t_ligand.pdb structures/8Z1T/8z1t_ligand.cif structures/8Z1T/8z1t_complex.pdb structures/8Z1T/8z1t_complex.cif 8Z25 classic Na Na Na Na compound 20 "[""A1L0R""]" 1 IC50 IC50 = = 57, 40 nM 47.7493455452533 [57.0, 40.0] replicate_geometric_mean 7.321032576499773 success True biochemical_inhibition mGal-3 IC50 assay; Table 3 reports the two duplicate determinations for compound 20. 5 Table 3 explicitly prints compound 20 mGal-3 IC50 values as 57, 40 nM; its footnote states that both IC50 values are provided for duplicate determinations. Figure 5 maps compound 20 to printed PDB ID 8Z2S bound with hGal-3; the supplied sibling mapping uniquely identifies this as requested 8Z25. auto_single_measurement only accepted activity measurement [1] 1 structures\8Z25\8Z25_metadata.json point structures/8Z25/8z25_protein.pdb structures/8Z25/8z25_pocket.pdb structures/8Z25/8z25_ligand.sdf structures/8Z25/8z25_ligand.pdb structures/8Z25/8z25_ligand.cif structures/8Z25/8z25_complex.pdb structures/8Z25/8z25_complex.cif 8Z30 classic HOIP Na Na Na tolfenamic acid "[""TLF""]" 1 Kd Kd = = 6 ± 1 μM 6000.0 [] unit_conversion 5.221848749616356 success True direct_binding Isothermal titration calorimetry (ITC), assuming a 1:1 binding mode. 3 Figure 3B prints “Tolfenamic acid vs HOIPPUB” and Kd (μM) 6 ± 1; the text states that its affinity was determined using ITC at 6 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Z30\8Z30_metadata.json point structures/8Z30/8z30_protein.pdb structures/8Z30/8z30_pocket.pdb structures/8Z30/8z30_ligand.sdf structures/8Z30/8z30_ligand.pdb structures/8Z30/8z30_ligand.cif structures/8Z30/8z30_complex.pdb structures/8Z30/8z30_complex.cif 8Z37 classic Human STING ligand-binding domain Human hSTING-LBD, residues 155-343 Na Honokiol "[""Y4T""]" 1 Kd Kd = = 12.9 ± 0.4 µM 12900.0 [] unit_conversion 4.889410289700751 success True direct_binding Bio-layer interferometry (BLI) binding of honokiol to purified hSTING-LBD. 6 Figure 3 reports: “hSTING-LBD versus honokiol K_D = 12.9 ± 0.4 μM”; the text states that honokiol binds purified hSTING-LBD as revealed by BLI assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8Z37\8Z37_metadata.json point structures/8Z37/8z37_protein.pdb structures/8Z37/8z37_pocket.pdb structures/8Z37/8z37_ligand.sdf structures/8Z37/8z37_ligand.pdb structures/8Z37/8z37_ligand.cif structures/8Z37/8z37_complex.pdb structures/8Z37/8z37_complex.cif 8Z3J classic Aha1 Na Aha1-CTD (Aha1 residues 204-338) Na Benzbromarone "[""R75""]" 1 Kd Kd = = 0.84 ± 0.35 μM 840.0 [] unit_conversion 6.075720713938118 success True direct_binding Isothermal titration calorimetry of Aha1-CTD with Benzbromarone. 3 Fig. 1 legend states that ITC determined the thermodynamic parameters for Benzbromarone binding to Aha1-CTD and reports Kd = 0.84 ± 0.35 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8Z3J\8Z3J_metadata.json point structures/8Z3J/8z3j_protein.pdb structures/8Z3J/8z3j_pocket.pdb structures/8Z3J/8z3j_ligand.sdf structures/8Z3J/8z3j_ligand.pdb structures/8Z3J/8z3j_ligand.cif structures/8Z3J/8z3j_complex.pdb structures/8Z3J/8z3j_complex.cif 8Z53 classic Dwarf14 (AtD14) Arabidopsis thaliana Na Na Zaxinone "[""A1L1M""]" 2 Kd Kd = = 1.788 µM 1788.0 [] unit_conversion 5.747632485540102 success True direct_binding Intrinsic tryptophan fluorescence binding assay with purified AtD14. 5 Fig. 3c prints “Kd: 1.788 µM” for Zax binding to AtD14; the caption states that apparent dissociation constants were derived by intrinsic protein fluorescence measurements. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\8Z53\8Z53_metadata.json point structures/8Z53/8z53_protein.pdb structures/8Z53/8z53_pocket.pdb structures/8Z53/8z53_ligand.sdf structures/8Z53/8z53_ligand.pdb structures/8Z53/8z53_ligand.cif structures/8Z53/8z53_complex.pdb structures/8Z53/8z53_complex.cif 8Z5L classic IMP-1 metallo-beta-lactamase Na Na Na compound 4b "[""A1LXO""]" 1 IC50 IC50 = = 4.81 µM 4810.0 [] unit_conversion 5.317854923626168 success True biochemical_inhibition In vitro UV absorbance photometry using cephalosporin C; IMP-1 inhibition assay. 6 Table 3 reports compound 4b IC50 = 4.81 µM for IMP-1. The paper states that the IMP-1–compound 4b crystal structure was deposited as PDB 8Z5L. auto_single_measurement only accepted activity measurement [1] 1 structures\8Z5L\8Z5L_metadata.json point structures/8Z5L/8z5l_protein.pdb structures/8Z5L/8z5l_pocket.pdb structures/8Z5L/8z5l_ligand.sdf structures/8Z5L/8z5l_ligand.pdb structures/8Z5L/8z5l_ligand.cif structures/8Z5L/8z5l_complex.pdb structures/8Z5L/8z5l_complex.cif 8ZE8 extended ASAP1 SH3 domain Mus musculus ASAP1; Homo sapiens Ankyrin-B ASAP1 SH3 domain residues 1083-1147 in complex with gAnkB peptide residues 1699-1710 Na gAnkB/Ankyrin-B peptide residues 1699-1710 "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 0.19 ± 0.02 μM 190.0 [] unit_conversion 6.721246399047171 success True direct_binding Isothermal titration calorimetry (ITC) using purified ASAP1-SH3 and the 12-residue gAnkB peptide. 3 Fig. 1D/F reports ASAP1 SH3 (1083–1147) binding gAnkB (1699–1710) with Kd 0.19 ± 0.02 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZE8\8ZE8_metadata.json point structures/8ZE8/8ze8_protein.pdb structures/8ZE8/8ze8_pocket.pdb structures/8ZE8/8ze8_ligand.pdb structures/8ZE8/8ze8_ligand.cif structures/8ZE8/8ze8_complex.pdb structures/8ZE8/8ze8_complex.cif 8ZEB extended BCL-XL Na Na Na cp-B6X-4 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 12 nM 12.0 [] unit_conversion 7.920818753952375 success True direct_binding Surface plasmon resonance (single-cycle kinetics). 6 Figure 3f reports the affinity of cp-B6X-4 toward BCL-XL, with K_D = 12 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZEB\8ZEB_metadata.json point structures/8ZEB/8zeb_protein.pdb structures/8ZEB/8zeb_pocket.pdb structures/8ZEB/8zeb_ligand.pdb structures/8ZEB/8zeb_ligand.cif structures/8ZEB/8zeb_complex.pdb structures/8ZEB/8zeb_complex.cif 8ZIF classic gamma-lyase CndF Na Na Na pyridoxal 5'-phosphate; L-homoserine; ethyl acetoacetate "[""EAC""]" 1 Kd Kd = = 0.4 mM 400000.0 [] unit_conversion 3.3979400086720375 success True direct_binding ITC: affinity between EAA and CndF with HSE bound; buffer contained PLP. 12 “To evaluate the affinity between EAA and CndF with HSE bound... resulting in a Kd of 0.4 mM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ZIF\8ZIF_metadata.json point structures/8ZIF/8zif_protein.pdb structures/8ZIF/8zif_pocket.pdb structures/8ZIF/8zif_ligand.sdf structures/8ZIF/8zif_ligand.pdb structures/8ZIF/8zif_ligand.cif structures/8ZIF/8zif_complex.pdb structures/8ZIF/8zif_complex.cif 8ZIL classic gamma-lyase CndF Na Na Na ethyl acetoacetate "[""EAC""]" 1 Kd Kd = = 3.2 mM 3200000.0 [] unit_conversion 2.4948500216800937 success True direct_binding ITC: affinity between EAA and CndF without HSE bound; buffer contained PLP. 12 “To evaluate the affinity between EAA and CndF without HSE bound... resulting in a Kd of 3.2 mM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ZIL\8ZIL_metadata.json point structures/8ZIL/8zil_protein.pdb structures/8ZIL/8zil_pocket.pdb structures/8ZIL/8zil_ligand.sdf structures/8ZIL/8zil_ligand.pdb structures/8ZIL/8zil_ligand.cif structures/8ZIL/8zil_complex.pdb structures/8ZIL/8zil_complex.cif 8ZKN classic MCT8 (thyroid hormone transporter) human MCT8 fused with a C-terminal FLAG tag wild-type (WT) silychristin "[""A1IET""]" 1 Kd Kd = = 30.5 ± 2 nM 30.5 [] unit_conversion 7.515700160653214 success True direct_binding Microscale thermophoresis (MST) binding assay of purified human MCT8 WT. 5 Fig. 4e reports Kd of silychristin for WT MCT8 as 30.5 ± 2 nM; the text identifies this as MST binding affinity. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZKN\8ZKN_metadata.json point structures/8ZKN/8zkn_protein.pdb structures/8ZKN/8zkn_pocket.pdb structures/8ZKN/8zkn_ligand.sdf structures/8ZKN/8zkn_ligand.pdb structures/8ZKN/8zkn_ligand.cif structures/8ZKN/8zkn_complex.pdb structures/8ZKN/8zkn_complex.cif 8ZL2 classic Drosophila INDY Drosophila melanogaster full-length INDY Na DIDS (4,4'-diisothiocyano-2,2'-disulfonic acid stilbene) "[""4DS""]" 1 IC50 IC50 = = 2.2 ± 2.5 μM 2200.0 [] unit_conversion 5.657577319177793 success True biochemical_inhibition [14C]-citrate transport by purified full-length INDY reconstituted into proteoliposomes; DIDS-mediated inhibition. 2 “INDY-mediated transport of citrate ... is almost completely inhibited in the presence of DIDS, with an IC50 value of 2.2 ± 2.5 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ZL2\8ZL2_metadata.json point structures/8ZL2/8zl2_protein.pdb structures/8ZL2/8zl2_pocket.pdb structures/8ZL2/8zl2_ligand.sdf structures/8ZL2/8zl2_ligand.pdb structures/8ZL2/8zl2_ligand.cif structures/8ZL2/8zl2_complex.pdb structures/8ZL2/8zl2_complex.cif 8ZL3 classic Drosophila INDY Drosophila melanogaster full-length INDY Na DIDS (4,4'-diisothiocyano-2,2'-disulfonic acid stilbene) "[""4DS""]" 1 IC50 IC50 = = 2.2 ± 2.5 μM 2200.0 [] unit_conversion 5.657577319177793 success True biochemical_inhibition [14C]-citrate transport by purified full-length INDY reconstituted into proteoliposomes; DIDS-mediated inhibition. 2 “INDY-mediated transport of citrate ... is almost completely inhibited in the presence of DIDS, with an IC50 value of 2.2 ± 2.5 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ZL3\8ZL3_metadata.json point structures/8ZL3/8zl3_protein.pdb structures/8ZL3/8zl3_pocket.pdb structures/8ZL3/8zl3_ligand.sdf structures/8ZL3/8zl3_ligand.pdb structures/8ZL3/8zl3_ligand.cif structures/8ZL3/8zl3_complex.pdb structures/8ZL3/8zl3_complex.cif 8ZLO classic alpha-synuclein human N-terminally acetylated alpha-synuclein E46K F0502B "[""1KI""]" 1 Kd Kd = = 4.18 µM 4180.0 [] unit_conversion 5.3788237182249645 success True direct_binding SPR binding assay comparing F0502B binding to WT polymorph 1a, E46K polymorph, and WT polymorph 5a. 8 Figure 5A prints K_D = 4.18 µM for F0502B binding to the E46K polymorph. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZLO\8ZLO_metadata.json point structures/8ZLO/8zlo_protein.pdb structures/8ZLO/8zlo_pocket.pdb structures/8ZLO/8zlo_ligand.sdf structures/8ZLO/8zlo_ligand.pdb structures/8ZLO/8zlo_ligand.cif structures/8ZLO/8zlo_complex.pdb structures/8ZLO/8zlo_complex.cif 8ZLW extended Drosophila melanogaster retinal degeneration C (RDGC) Drosophila melanogaster RDGC IQ motif (aa 1-25) with Ca2+-bound dCaM Na Ca2+ "[""CHAIN:R""]" 1 Kd Kd = = 0.25 ± 0.09 µM 250.0 [] unit_conversion 6.6020599913279625 success True direct_binding ITC assay of RDGC (aa 1–25) with Ca2+-CaM. 8 Fig. 4g reports Kd values for “RDGC (aa 1–25)/Ca2+-CaM”; WT is 0.25 ± 0.09 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZLW\8ZLW_metadata.json point structures/8ZLW/8zlw_protein.pdb structures/8ZLW/8zlw_pocket.pdb structures/8ZLW/8zlw_ligand.pdb structures/8ZLW/8zlw_ligand.cif structures/8ZLW/8zlw_complex.pdb structures/8ZLW/8zlw_complex.cif 8ZMF classic 5-HT2C receptor Homo sapiens Residues 51-391; N-terminal FLAG and TEV cleavage sequences; C-terminal GFP and 8xHis; ICL3 residues 243-300 replaced by BRIL Na compound 5 "[""A1L10""]" 1 Ki Ki = = 0.56 nM 0.56 [] unit_conversion 9.2518119729938 success True direct_binding Binding assay for human 5-HT2A and 5-HT2C receptors; Table 1 reports compound 5. 4 Table 1 lists compound 5 with h 5-HT2C Ki of 0.56 nM; its footnote states the values were determined by binding assay for human 5-HT2A and 5-HT2C receptors. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZMF\8ZMF_metadata.json point structures/8ZMF/8zmf_protein.pdb structures/8ZMF/8zmf_pocket.pdb structures/8ZMF/8zmf_ligand.sdf structures/8ZMF/8zmf_ligand.pdb structures/8ZMF/8zmf_ligand.cif structures/8ZMF/8zmf_complex.pdb structures/8ZMF/8zmf_complex.cif 8ZML extended TNIK Na Na Na compound 4 "[""A1D8H""]" 4 Kd Kd = = 4.3 nM 4.3 [] unit_conversion 8.366531544420413 success True direct_binding SPR assay. 7 “Profiling in the SPR assay showed the excellent affinity of compound 4 to the TNIK kinase domain (Kd of 4.3 nM).” auto_metric_priority unique highest-priority metric family: Kd [4] 4 structures\8ZML\8ZML_metadata.json point structures/8ZML/8zml_protein.pdb structures/8ZML/8zml_pocket.pdb structures/8ZML/8zml_ligand.pdb structures/8ZML/8zml_ligand.cif structures/8ZML/8zml_complex.pdb structures/8ZML/8zml_complex.cif 8ZMT classic cytochrome bc1 complex (complex III) Saccharomyces cerevisiae Na Na Metyltetraprole (MET) "[""A1D6P""]" 1 Ki Ki = = 0.92 ± 0.09 nM 0.92 [] unit_conversion 9.036212172654444 success True biochemical_inhibition In vitro inhibition of yeast complex III; Figure 1B reports Ki for MET. 2 Figure 1B lists yeast Ki values: MET, 0.92 ± 0.09 nM; PYR, 0.76 ± 0.02 nM. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\8ZMT\8ZMT_metadata.json point structures/8ZMT/8zmt_protein.pdb structures/8ZMT/8zmt_pocket.pdb structures/8ZMT/8zmt_ligand.sdf structures/8ZMT/8zmt_ligand.pdb structures/8ZMT/8zmt_ligand.cif structures/8ZMT/8zmt_complex.pdb structures/8ZMT/8zmt_complex.cif 8ZMY classic alpha-synuclein human Recombinant N-terminally acetylated alpha-synuclein wild-type F0502B "[""1KI""]" 1 Kd Kd = = 6.95 µM 6950.0 [] unit_conversion 5.158015195409886 success True direct_binding SPR binding assay comparing F0502B binding to WT polymorph 1a, E46K polymorph, and WT polymorph 5a. 8 Figure 5A prints K_D = 6.95 µM for F0502B binding to WT polymorph 5a. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZMY\8ZMY_metadata.json point structures/8ZMY/8zmy_protein.pdb structures/8ZMY/8zmy_pocket.pdb structures/8ZMY/8zmy_ligand.sdf structures/8ZMY/8zmy_ligand.pdb structures/8ZMY/8zmy_ligand.cif structures/8ZMY/8zmy_complex.pdb structures/8ZMY/8zmy_complex.cif 8ZMZ classic R-eLACCO2 Na R-eLACCO2 containing TTHA0766 and cpmApple domains Na L-lactate "[""2OP""]" 1 Kd Kd = = 460 µM 460000.0 [] unit_conversion 3.3372421683184257 success True direct_binding Purified-protein L-lactate dose-response curve; fluorescence titration fitted to determine apparent Kd; n=3 experimental triplicates. 3 Fig. 1e legend prints “R-eLACCO2 (Kd 460 µM)”; the caption identifies this as an L-lactate dose-response curve. Methods state purified-protein lactate titrations were fitted to determine apparent Kd (page 12). auto_single_measurement only accepted activity measurement [1] 1 structures\8ZMZ\8ZMZ_metadata.json point structures/8ZMZ/8zmz_protein.pdb structures/8ZMZ/8zmz_pocket.pdb structures/8ZMZ/8zmz_ligand.sdf structures/8ZMZ/8zmz_ligand.pdb structures/8ZMZ/8zmz_ligand.cif structures/8ZMZ/8zmz_complex.pdb structures/8ZMZ/8zmz_complex.cif 8ZOS classic cytochrome bc1 complex (complex III) Sus scrofa (porcine) Na Na pyraclostrobin (PYR) "[""A1D6K""]" 1 Ki Ki = = 10.45 ± 0.80 nM 10.45 [] unit_conversion 7.980883709552927 success True biochemical_inhibition In vitro inhibition of porcine complex III; Figure 1B reports Ki for PYR. 2 Figure 1B lists porcine Ki values: MET, 298.87 ± 23.04 nM; PYR, 10.45 ± 0.80 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZOS\8ZOS_metadata.json point structures/8ZOS/8zos_protein.pdb structures/8ZOS/8zos_pocket.pdb structures/8ZOS/8zos_ligand.sdf structures/8ZOS/8zos_ligand.pdb structures/8ZOS/8zos_ligand.cif structures/8ZOS/8zos_complex.pdb structures/8ZOS/8zos_complex.cif 8ZOW classic cytochrome bc1 complex (complex III) Sus scrofa (porcine) Na Na Metyltetraprole (MET) "[""A1D6P""]" 1 Ki Ki = = 298.87 ± 23.04 nM 298.87 [] unit_conversion 6.524517676423884 success True biochemical_inhibition In vitro inhibition of porcine complex III; Figure 1B reports Ki for MET. 2 Figure 1B lists porcine Ki values: MET, 298.87 ± 23.04 nM; PYR, 10.45 ± 0.80 nM. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\8ZOW\8ZOW_metadata.json point structures/8ZOW/8zow_protein.pdb structures/8ZOW/8zow_pocket.pdb structures/8ZOW/8zow_ligand.sdf structures/8ZOW/8zow_ligand.pdb structures/8ZOW/8zow_ligand.cif structures/8ZOW/8zow_complex.pdb structures/8ZOW/8zow_complex.cif 8ZP0 classic cytochrome bc1 complex (complex III) Sus scrofa (porcine) Na Na YF23694 "[""A1D6O""]" 2 Ki Ki = = 1457.7 ± 111.3 nM 1457.7 [] unit_conversion 5.836331846217331 success True biochemical_inhibition In vitro porcine complex III inhibition kinetics; Figure 6E reports Ki. 7 Figure 6E reports YF23694 Ki = 1457.7 ± 111.3 nM for porcine complex III. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\8ZP0\8ZP0_metadata.json point structures/8ZP0/8zp0_protein.pdb structures/8ZP0/8zp0_pocket.pdb structures/8ZP0/8zp0_ligand.sdf structures/8ZP0/8zp0_ligand.pdb structures/8ZP0/8zp0_ligand.cif structures/8ZP0/8zp0_complex.pdb structures/8ZP0/8zp0_complex.cif 8ZPU extended rabbit antibody C7 rabbit single-chain variable fragment (scFv) light-chain Cys80Ser phosphorylated Akt peptide (RPHFPQF[pS]YSAS) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 26.9 ± 14.2 nM 26.9 [] unit_conversion 7.570247719997592 success True direct_binding ITC; C7 WT interacting with phosphopeptide. 4 Table 1 reports C7 WT K_D = 26.9 ± 14.2 nM for phosphopeptides; ITC is stated as the binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZPU\8ZPU_metadata.json point structures/8ZPU/8zpu_protein.pdb structures/8ZPU/8zpu_pocket.pdb structures/8ZPU/8zpu_ligand.pdb structures/8ZPU/8zpu_ligand.cif structures/8ZPU/8zpu_complex.pdb structures/8ZPU/8zpu_complex.cif 8ZQ2 classic PDE4D Na Na Na 2-1 "[""A1D8O""]" 1 IC50 IC50 = = 61 ± 6 nmol/L 61.0 [] unit_conversion 7.214670164989233 success True biochemical_inhibition PDE4 inhibitory activity, second-round isoaurostatin optimization. 3 Table 2 reports compound 2-1 IC50 = 61 ± 6 nmol/L; the text states that ethyl substitution resulted in 2-1 with improved PDE4 inhibitory activity. Figure 3 assigns PDE4D–2-1 to PDB 8ZQ2. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZQ2\8ZQ2_metadata.json point structures/8ZQ2/8zq2_protein.pdb structures/8ZQ2/8zq2_pocket.pdb structures/8ZQ2/8zq2_ligand.sdf structures/8ZQ2/8zq2_ligand.pdb structures/8ZQ2/8zq2_ligand.cif structures/8ZQ2/8zq2_complex.pdb structures/8ZQ2/8zq2_complex.cif 8ZQU classic PDE4D Na Na Na 2-6 "[""A1D8P""]" 1 IC50 IC50 = = 35 ± 4 nmol/L 35.0 [] unit_conversion 7.455931955649724 success True biochemical_inhibition PDE4 inhibitory activity, second-round isoaurostatin optimization. 3 Table 2 reports compound 2-6 IC50 = 35 ± 4 nmol/L; the text identifies 2-6 as having the best PDE4 inhibitory activity. Figure 3 assigns PDE4D–2-6 to PDB 8ZQU. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZQU\8ZQU_metadata.json point structures/8ZQU/8zqu_protein.pdb structures/8ZQU/8zqu_pocket.pdb structures/8ZQU/8zqu_ligand.sdf structures/8ZQU/8zqu_ligand.pdb structures/8ZQU/8zqu_ligand.cif structures/8ZQU/8zqu_complex.pdb structures/8ZQU/8zqu_complex.cif 8ZR9 classic AbCapV Acinetobacter baumannii C-terminal His6-tagged AbCapV Na 3',3'-cGAMP "[""4BW""]" 1 Kd Kd = = 2.68 ± 0.24 nM 2.68 [] unit_conversion 8.57186520597121 success True direct_binding Surface plasmon resonance (SPR) direct-binding assay using purified AbCapV and 3',3'-cGAMP. 3 “Surface plasmon resonance (SPR) confirmed direct binding between purified AbCapV and 3’3’-cGAMP, with a Kd value of 2.68 ± 0.24 nM (Fig. 1d).” auto_single_measurement only accepted activity measurement [1] 1 structures\8ZR9\8ZR9_metadata.json point structures/8ZR9/8zr9_protein.pdb structures/8ZR9/8zr9_pocket.pdb structures/8ZR9/8zr9_ligand.sdf structures/8ZR9/8zr9_ligand.pdb structures/8ZR9/8zr9_ligand.cif structures/8ZR9/8zr9_complex.pdb structures/8ZR9/8zr9_complex.cif 8ZRL classic BmMDH2 Bacillus methanolicus MGA3 Na Na ADPR (ADP-ribose) "[""APR""]" 4 Kd Kd = = 303 nM 303.0 [] unit_conversion 6.518557371497695 success True direct_binding Isothermal titration calorimetry measurement of ADPR binding to purified BmMDH2 in the Mn2+-containing assay buffer; Figure 4D. 5 The text reports that ITC revealed ADPR binding to BmMDH2 with KD of 303 nM. auto_metric_priority unique highest-priority metric family: Kd [4] 4 structures\8ZRL\8ZRL_metadata.json point structures/8ZRL/8zrl_protein.pdb structures/8ZRL/8zrl_pocket.pdb structures/8ZRL/8zrl_ligand.sdf structures/8ZRL/8zrl_ligand.pdb structures/8ZRL/8zrl_ligand.cif structures/8ZRL/8zrl_complex.pdb structures/8ZRL/8zrl_complex.cif 8ZRV classic ECHS1 (short-chain enoyl-CoA hydratase 1) human ECHS1 residues 28-290; N-terminal 8xHis-SUMO-TEV expression tags removed during purification Na Hexanoyl-CoA "[""HXC""]" 1 Kd Kd = = 2.57 µM 2570.0 [] unit_conversion 5.590066876668706 success True direct_binding Surface plasmon resonance (SPR) binding assay with purified ECHS1 and hexanoyl-CoA. 3 “The SPR results revealed that ECHS1 exhibited slightly weaker binding affinities ... with KDs of 2.69, 2.57, and 2.64 µM observed for acetoacetyl-CoA, hexanoyl-CoA, and octanoyl-CoA, respectively.” Table 2 maps ECHS1–Hexanoyl-CoA to PDB 8ZRV. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZRV\8ZRV_metadata.json point structures/8ZRV/8zrv_protein.pdb structures/8ZRV/8zrv_pocket.pdb structures/8ZRV/8zrv_ligand.sdf structures/8ZRV/8zrv_ligand.pdb structures/8ZRV/8zrv_ligand.cif structures/8ZRV/8zrv_complex.pdb structures/8ZRV/8zrv_complex.cif 8ZRW classic ECHS1 (short-chain enoyl-CoA hydratase 1) human ECHS1 residues 28-290; N-terminal 8xHis-SUMO-TEV expression tags removed during purification Na Octanoyl-CoA "[""CO8""]" 1 Kd Kd = = 2.64 µM 2640.0 [] unit_conversion 5.578396073130168 success True direct_binding Surface plasmon resonance (SPR) binding assay with purified ECHS1 and octanoyl-CoA. 3 “The SPR results revealed that ECHS1 exhibited slightly weaker binding affinities ... with KDs of 2.69, 2.57, and 2.64 µM observed for acetoacetyl-CoA, hexanoyl-CoA, and octanoyl-CoA, respectively.” Table 2 maps ECHS1–Octanoyl-CoA to PDB 8ZRW. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZRW\8ZRW_metadata.json point structures/8ZRW/8zrw_protein.pdb structures/8ZRW/8zrw_pocket.pdb structures/8ZRW/8zrw_ligand.sdf structures/8ZRW/8zrw_ligand.pdb structures/8ZRW/8zrw_ligand.cif structures/8ZRW/8zrw_complex.pdb structures/8ZRW/8zrw_complex.cif 8ZRX classic ECHS1 (short-chain enoyl-CoA hydratase 1) human ECHS1 residues 28-290; N-terminal 8xHis-SUMO-TEV expression tags removed during purification Na Acetoacetyl-CoA "[""CAA""]" 1 Kd Kd = = 2.69 µM 2690.0 [] unit_conversion 5.570247719997592 success True direct_binding Surface plasmon resonance (SPR) binding assay with purified ECHS1 and acetoacetyl-CoA. 3 “The SPR results revealed that ECHS1 exhibited slightly weaker binding affinities ... with KDs of 2.69, 2.57, and 2.64 µM observed for acetoacetyl-CoA, hexanoyl-CoA, and octanoyl-CoA, respectively.” Table 2 maps ECHS1–Acetoacetyl-CoA to PDB 8ZRX. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZRX\8ZRX_metadata.json point structures/8ZRX/8zrx_protein.pdb structures/8ZRX/8zrx_pocket.pdb structures/8ZRX/8zrx_ligand.sdf structures/8ZRX/8zrx_ligand.pdb structures/8ZRX/8zrx_ligand.cif structures/8ZRX/8zrx_complex.pdb structures/8ZRX/8zrx_complex.cif 8ZRY classic ECHS1 (short-chain enoyl-CoA hydratase 1) human ECHS1 residues 28-290; N-terminal 8xHis-SUMO-TEV expression tags removed during purification Na Crotonoyl-CoA "[""A1D88""]" 1 Kd Kd = = 863 nM 863.0 [] unit_conversion 6.06398920428479 success True direct_binding Surface plasmon resonance (SPR) binding assay with purified ECHS1 and crotonyl-CoA. 2 “Using SPR assay to assess the binding affinity of ECHS1 for crotonyl-CoA ... we verified that ECHS1 exhibits a binding affinity of 863 nM for crotonyl-CoA (Fig. 2b).” Table 2 maps ECHS1–Crotonyl-CoA to PDB 8ZRY. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZRY\8ZRY_metadata.json point structures/8ZRY/8zry_protein.pdb structures/8ZRY/8zry_pocket.pdb structures/8ZRY/8zry_ligand.sdf structures/8ZRY/8zry_ligand.pdb structures/8ZRY/8zry_ligand.cif structures/8ZRY/8zry_complex.pdb structures/8ZRY/8zry_complex.cif 8ZTX classic PKMYT1 (Myt1) Human PKMYT1 residues 75-362; N-terminal His6-SUMO expression tag cleaved before crystallization Na compound 6b "[""A1D83""]" 1 IC50 IC50 = = 100.8 ± 50.3 nM 100.8 [] unit_conversion 6.996539467890494 success True biochemical_inhibition ADP-Glo kinase dose-response assay of PKMYT1 catalytic activity. 7 Figure 7A reports compound 6b IC50 = 100.8 ± 50.3 nM for PKMYT1; Figure 4 maps compound 6b to PDB 8ZTX. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZTX\8ZTX_metadata.json point structures/8ZTX/8ztx_protein.pdb structures/8ZTX/8ztx_pocket.pdb structures/8ZTX/8ztx_ligand.sdf structures/8ZTX/8ztx_ligand.pdb structures/8ZTX/8ztx_ligand.cif structures/8ZTX/8ztx_complex.pdb structures/8ZTX/8ztx_complex.cif 8ZUV classic Na Na Na Na compound 21 "[""A1L0R""]" 1 IC50 IC50 = = 3800, 4000 nM 3898.7177379235895 [3800.0, 4000.0] replicate_geometric_mean 5.409078206027614 success True biochemical_inhibition mGal-3 IC50 assay; Table 3 reports the two duplicate determinations for compound 21. 5 Table 3 explicitly prints compound 21 mGal-3 IC50 values as 3800, 4000 nM; its footnote states that both IC50 values are provided for duplicate determinations. Figure 5 maps compound 21 to PDB ID 8ZUV bound with hGal-3. auto_single_measurement only accepted activity measurement [1] 1 structures\8ZUV\8ZUV_metadata.json point structures/8ZUV/8zuv_protein.pdb structures/8ZUV/8zuv_pocket.pdb structures/8ZUV/8zuv_ligand.sdf structures/8ZUV/8zuv_ligand.pdb structures/8ZUV/8zuv_ligand.cif structures/8ZUV/8zuv_complex.pdb structures/8ZUV/8zuv_complex.cif 8ZVN classic AtKAI2 Arabidopsis thaliana Na Na (+)-6'-carba-dMGer "[""A1L2E""]" 1 IC50 IC50 = = 2.5 μM 2500.0 [] unit_conversion 5.6020599913279625 success True biochemical_inhibition Competitive inhibition of purified KAI2 hydrolytic activity using dYLG (0.5 μM) as substrate. 3 “The IC50 values of (+)-dMGer, (+)-6′-carba-dMGer, and (+)-1′-carba-dMGer were 0.16, 2.5, and 78 μM, respectively, when 0.5 μM dYLG was used as the substrate.” auto_single_measurement only accepted activity measurement [1] 1 structures\8ZVN\8ZVN_metadata.json point structures/8ZVN/8zvn_protein.pdb structures/8ZVN/8zvn_pocket.pdb structures/8ZVN/8zvn_ligand.sdf structures/8ZVN/8zvn_ligand.pdb structures/8ZVN/8zvn_ligand.cif structures/8ZVN/8zvn_complex.pdb structures/8ZVN/8zvn_complex.cif 9ASC classic Glycosyltransferase ArnC Salmonella enterica Na Na UDP "[""UDP""]" 1 Kd Kd = = 8.48±6.83 μM 8480.0 [] unit_conversion 5.071604147743287 success True direct_binding Microscale thermophoresis UDP titration with 1 mM MnCl2. 7 Figure 3 caption reports a Kd of 8.48±6.83 μM with 1 mM MnCl2. auto_single_measurement only accepted activity measurement [1] 1 structures\9ASC\9ASC_metadata.json point structures/9ASC/9asc_protein.pdb structures/9ASC/9asc_pocket.pdb structures/9ASC/9asc_ligand.sdf structures/9ASC/9asc_ligand.pdb structures/9ASC/9asc_ligand.cif structures/9ASC/9asc_complex.pdb structures/9ASC/9asc_complex.cif 9AT2 extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na PAN3 "[""A1AF5""]" 1 IC50 IC50 = = 1.26±0.01 μM 1260.0 [] unit_conversion 5.899629454882437 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports PAN3 IC50 = 1.26±0.01 μM and PDB 9AT2. auto_single_measurement only accepted activity measurement [1] 1 structures\9AT2\9AT2_metadata.json point structures/9AT2/9at2_protein.pdb structures/9AT2/9at2_pocket.pdb structures/9AT2/9at2_ligand.pdb structures/9AT2/9at2_ligand.cif structures/9AT2/9at2_complex.pdb structures/9AT2/9at2_complex.cif 9ATN extended MLL4 PHD2/3 fingers human MLL4 residues 227-324 linked to ASXL2 residues 650-670 by an SGPSSG linker Na ASXL2 residues 650-670 "[""CHAIN:B""]" 1 Kd Kd = = 0.7 ± 0.1 µM 700.0 [] unit_conversion 6.154901959985743 success True direct_binding Fluorescence spectroscopy binding-affinity determination of MLL4 PHD2/3 with ASXL2 650-670 peptide. 2 Fig. 1i table reports MLL4 with ASXL2 650-670: Kd 0.7 ± 0.1 µM; the legend identifies these as fluorescence-spectroscopy affinities. auto_single_measurement only accepted activity measurement [1] 1 structures\9ATN\9ATN_metadata.json point structures/9ATN/9atn_protein.pdb structures/9ATN/9atn_pocket.pdb structures/9ATN/9atn_ligand.pdb structures/9ATN/9atn_ligand.cif structures/9ATN/9atn_complex.pdb structures/9ATN/9atn_complex.cif 9AV4 classic 17B-HSD13 human Na Na compound 1 "[""A1AG4""]" 1 IC50 IC50 = = 200 (28–1400) nM 200.0 [] unit_conversion 6.698970004336019 success True biochemical_inhibition Inhibition of β-estradiol turnover by purified recombinant human 17B-HSD13; geometric mean of at least 3 replicates. 3 Table 1 reports compound 1 biochemical IC50 = 200 (28–1400) nM; Fig. 1 assigns compound 1 to PDB 9AV4. auto_single_measurement only accepted activity measurement [1] 1 structures\9AV4\9AV4_metadata.json point structures/9AV4/9av4_protein.pdb structures/9AV4/9av4_pocket.pdb structures/9AV4/9av4_ligand.sdf structures/9AV4/9av4_ligand.pdb structures/9AV4/9av4_ligand.cif structures/9AV4/9av4_complex.pdb structures/9AV4/9av4_complex.cif 9AV5 classic 17B-HSD13 human Na Na compound 3 "[""A1AG5""]" 1 IC50 IC50 = = 140 (120–180) nM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition Inhibition of β-estradiol turnover by purified recombinant human 17B-HSD13; geometric mean of at least 3 replicates. 3 Table 1 reports compound 3 biochemical IC50 = 140 (120–180) nM; Fig. 1 assigns compound 3 to PDB 9AV5. auto_single_measurement only accepted activity measurement [1] 1 structures\9AV5\9AV5_metadata.json point structures/9AV5/9av5_protein.pdb structures/9AV5/9av5_pocket.pdb structures/9AV5/9av5_ligand.sdf structures/9AV5/9av5_ligand.pdb structures/9AV5/9av5_ligand.cif structures/9AV5/9av5_complex.pdb structures/9AV5/9av5_complex.cif 9AV8 classic 17B-HSD13 human Na Na compound 4 "[""A1AG6""]" 1 IC50 IC50 = = 47 (21–108) nM 47.0 [] unit_conversion 7.327902142064282 success True biochemical_inhibition Inhibition of β-estradiol turnover by purified recombinant human 17B-HSD13; geometric mean of at least 3 replicates. 3 Table 1 reports compound 4 biochemical IC50 = 47 (21–108) nM; Fig. 1 assigns compound 4 to PDB 9AV8. auto_single_measurement only accepted activity measurement [1] 1 structures\9AV8\9AV8_metadata.json point structures/9AV8/9av8_protein.pdb structures/9AV8/9av8_pocket.pdb structures/9AV8/9av8_ligand.sdf structures/9AV8/9av8_ligand.pdb structures/9AV8/9av8_ligand.cif structures/9AV8/9av8_complex.pdb structures/9AV8/9av8_complex.cif 9AVH classic aryl-alcohol oxidase (BaAAO) Bjerkandera adusta Na Na 4-methoxybenzoic acid "[""ANN""]" 1 Kd Kd = = 1815 ± 197 µM 1815000.0 [] unit_conversion 2.741123370627869 success True direct_binding Stopped-flow direct-binding analysis of BaAAO with 4-methoxybenzoic acid; complex formation and dissociation were measured in 50 mM sodium phosphate, pH 6.0, at 12 °C. 9 Table 3 reports Kd(acid) = 1815 ± 197 µM for the BaAAO–4-methoxybenzoic acid complex; the text identifies these as final-product complex formation/dissociation measurements. auto_single_measurement only accepted activity measurement [1] 1 structures\9AVH\9AVH_metadata.json point structures/9AVH/9avh_protein.pdb structures/9AVH/9avh_pocket.pdb structures/9AVH/9avh_ligand.sdf structures/9AVH/9avh_ligand.pdb structures/9AVH/9avh_ligand.cif structures/9AVH/9avh_complex.pdb structures/9AVH/9avh_complex.cif 9AX6 classic KRAS4B; CypA human CypA; Na for KRAS4B His6-TEV-KRAS4B, residues 1-169, with CypA; CypA construct not stated KRAS4B G12D, C51S, C80L, C118S; CypA mutation not stated RMC-6236 "[""A1AHB""]" 1 Kd Kd = = 364 nmol/L 364.0 [] unit_conversion 6.438898616350944 success True direct_binding SPR affinity of the RMC-6236:CypA binary complex for KRAS G12D (Kd2), measuring formation of the crystallographic RMC-6236–CypA–KRAS relationship. 3 “the affinity of the RMC-6236:CypA binary complex for KRASG12V, KRASG12D, and KRASWT (K_D2), which were 131, 364, and 154 nmol/L, respectively.” The exact KRAS4B G12D/C51S/C80L/C118S construct is specified in the protein-production methods on page 16. auto_single_measurement only accepted activity measurement [1] 1 structures\9AX6\9AX6_metadata.json point structures/9AX6/9ax6_protein.pdb structures/9AX6/9ax6_pocket.pdb structures/9AX6/9ax6_ligand.sdf structures/9AX6/9ax6_ligand.pdb structures/9AX6/9ax6_ligand.cif structures/9AX6/9ax6_complex.pdb structures/9AX6/9ax6_complex.cif 9AXN classic HY11-6B2 mouse murine Fab Na fentanyl "[""7V7""]" 1 IC50 IC50 = = 26 nM 26.0 [] unit_conversion 7.585026652029182 success True direct_binding Competitive ELISA. 3 Figure 2E reports HY11-6B2 fentanyl IC50 of 26 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9AXN\9AXN_metadata.json point structures/9AXN/9axn_protein.pdb structures/9AXN/9axn_pocket.pdb structures/9AXN/9axn_ligand.sdf structures/9AXN/9axn_ligand.pdb structures/9AXN/9axn_ligand.cif structures/9AXN/9axn_complex.pdb structures/9AXN/9axn_complex.cif 9B17 extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na PAN1 "[""A1AH9""]" 1 IC50 IC50 = = 0.81±0.02 μM 810.0 [] unit_conversion 6.09151498112135 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports PAN1 IC50 = 0.81±0.02 μM and PDB 9B17. auto_single_measurement only accepted activity measurement [1] 1 structures\9B17\9B17_metadata.json point structures/9B17/9b17_protein.pdb structures/9B17/9b17_pocket.pdb structures/9B17/9b17_ligand.pdb structures/9B17/9b17_ligand.cif structures/9B17/9b17_complex.pdb structures/9B17/9b17_complex.cif 9B1Q extended human Tryptophan 2,3-dioxygenase (TDO) human Na Na PYN1 "[""A1AH8""]" 1 IC50 IC50 = = 1.16±0.04 μM 1160.0 [] unit_conversion 5.935542010773082 success True biochemical_inhibition Spectroscopy-based enzyme assay; 50 mM pH 7.4 Tris buffer, 100 μM L-Trp, 25 °C. 2 Table 1 reports PYN1 IC50 = 1.16±0.04 μM and PDB 9B1Q. auto_single_measurement only accepted activity measurement [1] 1 structures\9B1Q\9B1Q_metadata.json point structures/9B1Q/9b1q_protein.pdb structures/9B1Q/9b1q_pocket.pdb structures/9B1Q/9b1q_ligand.pdb structures/9B1Q/9b1q_ligand.cif structures/9B1Q/9b1q_complex.pdb structures/9B1Q/9b1q_complex.cif 9B1U classic PqqT Methylobacterium extorquens AM1 PqqT expressed with a His6 affinity tag; tag cleaved by TEV protease Na PQQ "[""PQQ""]" 1 Kd Kd = = 60 ± 40 nM 60.0 [] unit_conversion 7.221848749616356 success True direct_binding PQQ binding to WT-PqqT measured by isothermal titration calorimetry (ITC). 4 The paper states that the Kd for WT-PqqT binding PQQ measured by ITC was 60 ± 40 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9B1U\9B1U_metadata.json point structures/9B1U/9b1u_protein.pdb structures/9B1U/9b1u_pocket.pdb structures/9B1U/9b1u_ligand.sdf structures/9B1U/9b1u_ligand.pdb structures/9B1U/9b1u_ligand.cif structures/9B1U/9b1u_complex.pdb structures/9B1U/9b1u_complex.cif 9B2H classic HIV-1 wild-type protease Na Na wild-type GRL-072-17A; inhibitor 4l "[""A1AIH""]" 1 Ki Ki = = 0.044 nM 0.044 [] unit_conversion 10.356547323513812 success True biochemical_inhibition HIV-1 protease inhibitory activity; Table 3 states Ki values represent at least five data points. 38 Table 3, entry 12, reports inhibitor 4l with Ki = 0.044 nM. The table footnote identifies the measurement as HIV-1 protease inhibitory activity; page 7 maps inhibitor 4l to wild-type HIV-1 protease PDB 9B2H. auto_single_measurement only accepted activity measurement [1] 1 structures\9B2H\9B2H_metadata.json point structures/9B2H/9b2h_protein.pdb structures/9B2H/9b2h_pocket.pdb structures/9B2H/9b2h_ligand.sdf structures/9B2H/9b2h_ligand.pdb structures/9B2H/9b2h_ligand.cif structures/9B2H/9b2h_complex.pdb structures/9B2H/9b2h_complex.cif 9B4G extended human phosphatidylserine synthase 1 (PSS1) human human PSS1 cloned into pEG-BacMam with a C-terminal Flag tag WT (wild type) DS55980254 "[""A1AIT""]" 1 IC50 IC50 = = 1.65 μM 1650.0 [] unit_conversion 5.782516055786093 success True biochemical_inhibition In vitro recombinant PSS1 base-exchange activity assay; DS55980254 inhibition. 3 Figure 1 legend states: “The IC50 of DS to PSS1WT is 1.65 μM (the deviation range is 1.22–2.26 μM).” auto_single_measurement only accepted activity measurement [1] 1 structures\9B4G\9B4G_metadata.json point structures/9B4G/9b4g_protein.pdb structures/9B4G/9b4g_pocket.pdb structures/9B4G/9b4g_ligand.pdb structures/9B4G/9b4g_ligand.cif structures/9B4G/9b4g_complex.pdb structures/9B4G/9b4g_complex.cif 9B95 classic human P2X1 receptor Homo sapiens Full-length human P2X1 with a C-terminal 3C-cleavable muGFP-octa-histidine tag (P2X1-CT) WT (wild-type) NF449 "[""A1ALI""]" 1 Ki Ki = = 6.6 nM 6.6 [] unit_conversion 8.18045606445813 success True direct_binding Competition radioligand-binding assay using 50 nM [³H]-α,β-methylene ATP and increasing NF449 on HEK293 cells expressing WT-P2X1. 7 Fig. 5B explicitly labels the NF449 competition-binding curve “Ki = 6.6 nM”; its legend identifies the WT-P2X1 radioligand-binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9B95\9B95_metadata.json point structures/9B95/9b95_protein.pdb structures/9B95/9b95_pocket.pdb structures/9B95/9b95_ligand.sdf structures/9B95/9b95_ligand.pdb structures/9B95/9b95_ligand.cif structures/9B95/9b95_complex.pdb structures/9B95/9b95_complex.cif 9B9H extended DCAF1 and WDR5 Na N-terminal His-tagged DCAF1(1077-1390); N-His-tagged WDR5(24-334) Na OICR-40333 "[""A1AM2""]" 1 Kd Kd = = 18 ± 1.6 nM 18.0 [] unit_conversion 7.7447274948966935 success True direct_binding SPR assessment of ternary-complex formation: immobilized DCAF1, with WDR5 plus PROTAC 1. 6 Table 1 reports WDR5 + PROTAC 1 K_D = 18 ± 1.6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9B9H\9B9H_metadata.json point structures/9B9H/9b9h_protein.pdb structures/9B9H/9b9h_pocket.pdb structures/9B9H/9b9h_ligand.pdb structures/9B9H/9b9h_ligand.cif structures/9B9H/9b9h_complex.pdb structures/9B9H/9b9h_complex.cif 9B9L extended RPRD1B Na RPRD1B C-terminal interacting domain, residues 2-133 Na singly phosphorylated Thr4 CTD peptide (pThr4 CTD peptide) "[""CHAIN:C""]" 1 Kd Kd = = 5.3 ± 2 µM 5300.0 [] unit_conversion 5.275724130399211 success True direct_binding Fluorescence-anisotropy measurement using FITC-labeled pThr4 CTD peptide and RPRD1B CID. 8 Figure 4A reports the RPRD1B WT–pThr4 peptide Kd as 5.3 ± 2 µM; the caption identifies fluorescence-anisotropy measurements of RPRD1B CID with FITC-labeled pS2/pT4 CTD peptides. auto_single_measurement only accepted activity measurement [1] 1 structures\9B9L\9B9L_metadata.json point structures/9B9L/9b9l_protein.pdb structures/9B9L/9b9l_pocket.pdb structures/9B9L/9b9l_ligand.pdb structures/9B9L/9b9l_ligand.cif structures/9B9L/9b9l_complex.pdb structures/9B9L/9b9l_complex.cif 9B9T extended DCAF1 and WDR5 Na N-terminal His-tagged DCAF1(1077-1390); N-His-tagged WDR5(24-334) Na OICR-40407 "[""A1ANM""]" 1 Kd Kd = = 10 ± 0.5 nM 10.0 [] unit_conversion 8.0 success True direct_binding SPR assessment of ternary-complex formation: immobilized DCAF1, with WDR5 plus PROTAC 2. 6 Table 1 reports WDR5 + PROTAC 2 K_D = 10 ± 0.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9B9T\9B9T_metadata.json point structures/9B9T/9b9t_protein.pdb structures/9B9T/9b9t_pocket.pdb structures/9B9T/9b9t_ligand.pdb structures/9B9T/9b9t_ligand.cif structures/9B9T/9b9t_complex.pdb structures/9B9T/9b9t_complex.cif 9B9W extended DCAF1 and WDR5 Na N-terminal His-tagged DCAF1(1077-1390); N-His-tagged WDR5(24-334) Na OICR-40792 "[""A1ANN""]" 1 Kd Kd = = 13 ± 0.5 nM 13.0 [] unit_conversion 7.886056647693163 success True direct_binding SPR assessment of ternary-complex formation: immobilized DCAF1, with WDR5 plus PROTAC 3. 6 Table 1 reports WDR5 + PROTAC 3 K_D = 13 ± 0.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9B9W\9B9W_metadata.json point structures/9B9W/9b9w_protein.pdb structures/9B9W/9b9w_pocket.pdb structures/9B9W/9b9w_ligand.pdb structures/9B9W/9b9w_ligand.cif structures/9B9W/9b9w_complex.pdb structures/9B9W/9b9w_complex.cif 9BA3 classic Htc10 chemoreceptor ligand-binding domain Halomonas titanicae Native Htc10-LBD, residues 32-309 Na guanine "[""GUN""]" 1 Kd Kd = = 7 ± 0.6 µM 7000.0 [] unit_conversion 5.154901959985743 success True direct_binding Isothermal titration calorimetry (ITC) of native Htc10-LBD-YNDN with guanine. 4 Fig. 1A explicitly reports guanine binding by native Htc10-LBD-YNDN with Kd = 7 ± 0.6 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BA3\9BA3_metadata.json point structures/9BA3/9ba3_protein.pdb structures/9BA3/9ba3_pocket.pdb structures/9BA3/9ba3_ligand.sdf structures/9BA3/9ba3_ligand.pdb structures/9BA3/9ba3_ligand.cif structures/9BA3/9ba3_complex.pdb structures/9BA3/9ba3_complex.cif 9BA7 classic Vibrio cholerae NFeoB Vibrio cholerae Vibrio cholerae NFeoB(His)6 NTPase domain N150T GDP "[""GDP""]" 1 Kd Kd = = 3.60 ± 0.36 μM 3600.0 [] unit_conversion 5.443697499232712 success True direct_binding Isothermal titration calorimetry of N150T VcNFeoB(His)6 with GDP; single binding site (N ≈ 1). 7 Figure 7 states: “The GDP Kd for ... N150T VcNFeoB (3.60 μM ± 0.36 μM) ...” and identifies GDP-bound N150T VcNFeoB as PDB ID 9BA7. auto_single_measurement only accepted activity measurement [1] 1 structures\9BA7\9BA7_metadata.json point structures/9BA7/9ba7_protein.pdb structures/9BA7/9ba7_pocket.pdb structures/9BA7/9ba7_ligand.sdf structures/9BA7/9ba7_ligand.pdb structures/9BA7/9ba7_ligand.cif structures/9BA7/9ba7_complex.pdb structures/9BA7/9ba7_complex.cif 9BDS classic trp RNA binding attenuation protein (TRAP) Alkalihalobacillus halodurans (Aha) dTRAP WT-WT, linked tandem Aha TRAP protomers with a 10-residue (G4S)2 linker Na Trp "[""TRP""]" 1 Kd Kd = = 4.5 ± 1.4 µM 4500.0 [] unit_conversion 5.346787486224656 success True direct_binding CD at 228 nm, fitted with a two-state binding model; the methods define the fitted apparent dissociation constant as K_D. 5 Figure 3 caption reports dTRAP's apparent Trp-binding affinity as 4.5 ± 1.4 µM; page 10 defines the CD fitted parameter as K_D. Figure 6 maps holo dTRAP to PDB 9BDS. auto_single_measurement only accepted activity measurement [1] 1 structures\9BDS\9BDS_metadata.json point structures/9BDS/9bds_protein.pdb structures/9BDS/9bds_pocket.pdb structures/9BDS/9bds_ligand.sdf structures/9BDS/9bds_ligand.pdb structures/9BDS/9bds_ligand.cif structures/9BDS/9bds_complex.pdb structures/9BDS/9bds_complex.cif 9BG1 classic KRAS; CypA Na Na G12V Compound 3 "[""A1AOH""]" 1 Kd Kd = = 2697 nM 2697.0 [] unit_conversion 5.569119053547109 success True direct_binding SPR KRAS K_D2, i.e. CypA:Compound 3 binary complex binding active KRAS G12V. 4 Table 1 reports KRAS G12V K_D2 = 2697 nM for Compound 3. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\9BG1\9BG1_metadata.json point structures/9BG1/9bg1_protein.pdb structures/9BG1/9bg1_pocket.pdb structures/9BG1/9bg1_ligand.sdf structures/9BG1/9bg1_ligand.pdb structures/9BG1/9bg1_ligand.cif structures/9BG1/9bg1_complex.pdb structures/9BG1/9bg1_complex.cif 9BG2 classic KRAS; CypA Na Na G12V Compound 10 "[""A1AOJ""]" 1 IC50 IC50 = = 165 nM 165.0 [] unit_conversion 6.782516055786093 success True biochemical_inhibition KRAS–BRAF RBD disruption assay. 8 Table 3 reports KRAS G12V RAS–BRAF RBD disruption IC50 = 165 nM for Compound 10. auto_single_measurement only accepted activity measurement [1] 1 structures\9BG2\9BG2_metadata.json point structures/9BG2/9bg2_protein.pdb structures/9BG2/9bg2_pocket.pdb structures/9BG2/9bg2_ligand.sdf structures/9BG2/9bg2_ligand.pdb structures/9BG2/9bg2_ligand.cif structures/9BG2/9bg2_complex.pdb structures/9BG2/9bg2_complex.cif 9BG4 classic KRAS; CypA Na Na G12V Compound 2 "[""A1AOG""]" 1 Kd Kd = = 4933 nM 4933.0 [] unit_conversion 5.306888884537859 success True direct_binding SPR KRAS K_D2, i.e. CypA:Compound 2 binary complex binding active KRAS G12V. 4 Table 1 reports KRAS G12V K_D2 = 4933 nM for Compound 2. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9BG4\9BG4_metadata.json point structures/9BG4/9bg4_protein.pdb structures/9BG4/9bg4_pocket.pdb structures/9BG4/9bg4_ligand.sdf structures/9BG4/9bg4_ligand.pdb structures/9BG4/9bg4_ligand.cif structures/9BG4/9bg4_complex.pdb structures/9BG4/9bg4_complex.cif 9BG6 classic KRAS; CypA human Na G12V Daraxonrasib (RMC-6236) "[""A1AHB""]" 1 IC50 IC50 = = 48 nM 48.0 [] unit_conversion 7.318758762624412 success True biochemical_inhibition KRAS G12V GMPPNP-bound BRAF-RBD disruption assay, 3 h. 10 Table 4 reports KRAS G12V RAS–BRAF RBD disruption IC50 = 48 nM for Compound 13; Figure 9 identifies Compound 13 as daraxonrasib. auto_single_measurement only accepted activity measurement [1] 1 structures\9BG6\9BG6_metadata.json point structures/9BG6/9bg6_protein.pdb structures/9BG6/9bg6_pocket.pdb structures/9BG6/9bg6_ligand.sdf structures/9BG6/9bg6_ligand.pdb structures/9BG6/9bg6_ligand.cif structures/9BG6/9bg6_complex.pdb structures/9BG6/9bg6_complex.cif 9BG7 classic KRAS; CypA Na Na G12V Compound 6 "[""A1AOI""]" 1 IC50 IC50 = = 214 nM 214.0 [] unit_conversion 6.669586226650809 success True biochemical_inhibition KRAS–BRAF RBD disruption assay. 6 Table 2 reports KRAS G12V RAS–BRAF RBD disruption IC50 = 214 nM for Compound 6. auto_single_measurement only accepted activity measurement [1] 1 structures\9BG7\9BG7_metadata.json point structures/9BG7/9bg7_protein.pdb structures/9BG7/9bg7_pocket.pdb structures/9BG7/9bg7_ligand.sdf structures/9BG7/9bg7_ligand.pdb structures/9BG7/9bg7_ligand.cif structures/9BG7/9bg7_complex.pdb structures/9BG7/9bg7_complex.cif 9BG9 classic KRAS; CypA Na Na WT Daraxonrasib (RMC-6236) "[""A1AHB""]" 1 IC50 IC50 = = 92 nM 92.0 [] unit_conversion 7.036212172654444 success True biochemical_inhibition KRAS WT GMPPNP-bound BRAF-RBD disruption assay, 3 h. 10 Table 4 reports WT RAS–BRAF RBD disruption IC50 = 92 nM for Compound 13; Figure 9 identifies Compound 13 as daraxonrasib. auto_single_measurement only accepted activity measurement [1] 1 structures\9BG9\9BG9_metadata.json point structures/9BG9/9bg9_protein.pdb structures/9BG9/9bg9_pocket.pdb structures/9BG9/9bg9_ligand.sdf structures/9BG9/9bg9_ligand.pdb structures/9BG9/9bg9_ligand.cif structures/9BG9/9bg9_complex.pdb structures/9BG9/9bg9_complex.cif 9BHJ classic MerTK Na Na Na compound 2; 6-{1-[([1,1'-biphenyl]-4-yl)carbamoyl]azetidin-3-yl}-3-[(1-methyl-1H-pyrazol-4-yl)amino]pyrazine-2-carboxamide "[""A1APG""]" 1 IC50 IC50 = = 2.0 nM 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition MerTK HTRF biochemical kinase assay 3 The text identifies compound 2 as MerTK-biochemical-assay active with MerTK IC50 2.0 nM and states that its bound MerTK X-ray structure is PDB 9BHJ. auto_single_measurement only accepted activity measurement [1] 1 structures\9BHJ\9BHJ_metadata.json point structures/9BHJ/9bhj_protein.pdb structures/9BHJ/9bhj_pocket.pdb structures/9BHJ/9bhj_ligand.sdf structures/9BHJ/9bhj_ligand.pdb structures/9BHJ/9bhj_ligand.cif structures/9BHJ/9bhj_complex.pdb structures/9BHJ/9bhj_complex.cif 9BHK classic MerTK Na Na Na compound 32; 6-{1-[6-(3-hydroxy-3-methylbutoxy)-1,3-benzoxazol-2-yl]azetidin-3-yl}-3-[(1-methyl-1H-pyrazol-4-yl)amino]pyrazine-2-carboxamide "[""A1APH""]" 1 IC50 IC50 = = 1.3 nM 1.3 [] unit_conversion 8.886056647693163 success True biochemical_inhibition MerTK biochemical HTRF kinase assay 7 Table 8 prints Mer HTRF IC50 1.3 nM for compound 32, and Figure 5 maps MerTK-bound compound 32 to PDB 9BHK. auto_single_measurement only accepted activity measurement [1] 1 structures\9BHK\9BHK_metadata.json point structures/9BHK/9bhk_protein.pdb structures/9BHK/9bhk_pocket.pdb structures/9BHK/9bhk_ligand.sdf structures/9BHK/9bhk_ligand.pdb structures/9BHK/9bhk_ligand.cif structures/9BHK/9bhk_complex.pdb structures/9BHK/9bhk_complex.cif 9BI8 classic HPK1 Na Na Na GNE-6893 "[""A1APL""]" 1 Ki Ki < < 0.019 nM 0.019 [] unit_conversion 10.721246399047171 success True biochemical_inhibition HTRF enzymatic assay (n > 2). 6 Figure 7 reports HPK1 Ki <0.019 nM for GNE-6893; its caption identifies the assay as HTRF enzymatic. auto_single_measurement only accepted activity measurement [1] 1 structures\9BI8\9BI8_metadata.json point structures/9BI8/9bi8_protein.pdb structures/9BI8/9bi8_pocket.pdb structures/9BI8/9bi8_ligand.sdf structures/9BI8/9bi8_ligand.pdb structures/9BI8/9bi8_ligand.cif structures/9BI8/9bi8_complex.pdb structures/9BI8/9bi8_complex.cif 9BIK classic HPK1 Na Na Na compound 1; inhibitor 1 "[""A1APO""]" 1 Ki Ki = = 4.9 nM 4.9 [] unit_conversion 8.309803919971486 success True biochemical_inhibition HTRF enzymatic assay (n > 2). 2 Figure 1 reports HPK1 Ki 4.9 nM for compound 1; its caption identifies the assay as HTRF enzymatic. auto_single_measurement only accepted activity measurement [1] 1 structures\9BIK\9BIK_metadata.json point structures/9BIK/9bik_protein.pdb structures/9BIK/9bik_pocket.pdb structures/9BIK/9bik_ligand.sdf structures/9BIK/9bik_ligand.pdb structures/9BIK/9bik_ligand.cif structures/9BIK/9bik_complex.pdb structures/9BIK/9bik_complex.cif 9BIR classic PepT2 (SLC15A2) Rattus norvegicus C-terminal His-tagged GFP expression construct; GFP removed by TEV cleavage Na cefadroxil "[""A1APP""]" 1 IC50 IC50 = = 19 ± 3 µM 19000.0 [] unit_conversion 4.721246399047171 success True biochemical_inhibition Inhibition of radiolabeled di-alanine uptake by reconstituted rat PepT2 in proteoliposomes. 2 “While cefadroxil displayed an IC50 of 19 µM ± 3” in PepT2 proteoliposome uptake-inhibition experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\9BIR\9BIR_metadata.json point structures/9BIR/9bir_protein.pdb structures/9BIR/9bir_pocket.pdb structures/9BIR/9bir_ligand.sdf structures/9BIR/9bir_ligand.pdb structures/9BIR/9bir_ligand.cif structures/9BIR/9bir_complex.pdb structures/9BIR/9bir_complex.cif 9BIS classic PepT2 (SLC15A2) Rattus norvegicus C-terminal His-tagged GFP expression construct; GFP removed by TEV cleavage Na amoxicillin "[""AXL""]" 1 IC50 IC50 = = 270 ± 39 µM 270000.0 [] unit_conversion 3.568636235841013 success True biochemical_inhibition Inhibition of radiolabeled di-alanine uptake by reconstituted rat PepT2 in proteoliposomes. 2 “amoxicillin and cloxacillin displayed significantly weaker values of 270 µM ± 39 and 203 µM ± 21, respectively” in PepT2 proteoliposome uptake-inhibition experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\9BIS\9BIS_metadata.json point structures/9BIS/9bis_protein.pdb structures/9BIS/9bis_pocket.pdb structures/9BIS/9bis_ligand.sdf structures/9BIS/9bis_ligand.pdb structures/9BIS/9bis_ligand.cif structures/9BIS/9bis_complex.pdb structures/9BIS/9bis_complex.cif 9BIT classic PepT2 (SLC15A2) Rattus norvegicus C-terminal His-tagged GFP expression construct; GFP removed by TEV cleavage Na cloxacillin "[""CXN""]" 1 IC50 IC50 = = 203 ± 21 µM 203000.0 [] unit_conversion 3.6925039620867874 success True biochemical_inhibition Inhibition of radiolabeled di-alanine uptake by reconstituted rat PepT2 in proteoliposomes. 2 “amoxicillin and cloxacillin displayed significantly weaker values of 270 µM ± 39 and 203 µM ± 21, respectively” in PepT2 proteoliposome uptake-inhibition experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\9BIT\9BIT_metadata.json point structures/9BIT/9bit_protein.pdb structures/9BIT/9bit_pocket.pdb structures/9BIT/9bit_ligand.sdf structures/9BIT/9bit_ligand.pdb structures/9BIT/9bit_ligand.cif structures/9BIT/9bit_complex.pdb structures/9BIT/9bit_complex.cif 9BIU classic PepT2 (SLC15A2) Rattus norvegicus C-terminal His-tagged GFP expression construct; GFP removed by TEV cleavage Na cloxacillin "[""CXN""]" 1 IC50 IC50 = = 203 ± 21 µM 203000.0 [] unit_conversion 3.6925039620867874 success True biochemical_inhibition Inhibition of radiolabeled di-alanine uptake by reconstituted rat PepT2 in proteoliposomes. 2 “amoxicillin and cloxacillin displayed significantly weaker values of 270 µM ± 39 and 203 µM ± 21, respectively” in PepT2 proteoliposome uptake-inhibition experiments. auto_single_measurement only accepted activity measurement [1] 1 structures\9BIU\9BIU_metadata.json point structures/9BIU/9biu_protein.pdb structures/9BIU/9biu_pocket.pdb structures/9BIU/9biu_ligand.sdf structures/9BIU/9biu_ligand.pdb structures/9BIU/9biu_ligand.cif structures/9BIU/9biu_complex.pdb structures/9BIU/9biu_complex.cif 9BJ1 classic HPK1 Na Na Na Na "[""A1APR""]" 1 Ki Ki = = 0.013 nM 0.013 [] unit_conversion 10.886056647693163 success True biochemical_inhibition HTRF enzymatic assay (n > 2). 4 Figure 4 reports HPK1 Ki 0.013 nM for compound 4; its caption identifies the assay as HTRF enzymatic. auto_single_measurement only accepted activity measurement [1] 1 structures\9BJ1\9BJ1_metadata.json point structures/9BJ1/9bj1_protein.pdb structures/9BJ1/9bj1_pocket.pdb structures/9BJ1/9bj1_ligand.sdf structures/9BJ1/9bj1_ligand.pdb structures/9BJ1/9bj1_ligand.cif structures/9BJ1/9bj1_complex.pdb structures/9BJ1/9bj1_complex.cif 9BJA classic Clostridioides difficile toxin B (TcdB) cysteine protease domain Clostridioides difficile TcdB residues 543-799 with His6 tag Na IP6 (inositol hexakisphosphate) "[""IHP""]" 1 Kd Kd = = 1.36 (1.34, 1.38) µM 1360.0 [] unit_conversion 5.866461091629782 success True direct_binding Isothermal titration calorimetry of IP6 binding to tCPD in 10 mM Tris, 150 mM NaCl, 1 mM TCEP, pH 7.5; 10 °C. 5 Table 3 reports IP6 Kd (SD) of 1.36 (1.34, 1.38) µM; the Figure 4 caption identifies the measurements as ITC thermograms of tCPD bound to IP6, and the methods define tCPD as TcdB residues 543–799 with a His6 tag. auto_single_measurement only accepted activity measurement [1] 1 structures\9BJA\9BJA_metadata.json point structures/9BJA/9bja_protein.pdb structures/9BJA/9bja_pocket.pdb structures/9BJA/9bja_ligand.sdf structures/9BJA/9bja_ligand.pdb structures/9BJA/9bja_ligand.cif structures/9BJA/9bja_complex.pdb structures/9BJA/9bja_complex.cif 9BKM classic human dihydroorotate dehydrogenase (DHODH) human Na Na compound 10 "[""A1AQM""]" 1 IC50 IC50 = = 0.22 nM 0.22 [] unit_conversion 9.657577319177793 success True biochemical_inhibition Human DHODH enzyme light-absorbance biochemical assay using DCIP. 2 The paper states that compound 10 had human DHODH IC50 = 0.22 nM; Figure 4 identifies compound 10 bound to human DHODH as PDB 9BKM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BKM\9BKM_metadata.json point structures/9BKM/9bkm_protein.pdb structures/9BKM/9bkm_pocket.pdb structures/9BKM/9bkm_ligand.sdf structures/9BKM/9bkm_ligand.pdb structures/9BKM/9bkm_ligand.cif structures/9BKM/9bkm_complex.pdb structures/9BKM/9bkm_complex.cif 9BKN classic human dihydroorotate dehydrogenase (DHODH) human Na Na compound 16 "[""A1AQK""]" 2 Kd Kd = = 2.22 nM 2.22 [] unit_conversion 8.653647025549361 success True direct_binding Surface plasmon resonance with recombinant human DHODH immobilized on a sensor chip. 6 The paper reports SPR binding kinetics and affinity for compound 16 to recombinant human DHODH, with KD = 2.22 nM; Figure 6 identifies the compound-16 complex as PDB 9BKN. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9BKN\9BKN_metadata.json point structures/9BKN/9bkn_protein.pdb structures/9BKN/9bkn_pocket.pdb structures/9BKN/9bkn_ligand.sdf structures/9BKN/9bkn_ligand.pdb structures/9BKN/9bkn_ligand.cif structures/9BKN/9bkn_complex.pdb structures/9BKN/9bkn_complex.cif 9BKO classic human dihydroorotate dehydrogenase (DHODH) human Na Na compound 26 "[""A1AQL""]" 1 IC50 IC50 = = 0.26 nM 0.26 [] unit_conversion 9.585026652029182 success True biochemical_inhibition Human DHODH biochemical inhibition assay. 5 Table 3 reports DHODH IC50 = 0.26 nM for compound 26. auto_single_measurement only accepted activity measurement [1] 1 structures\9BKO\9BKO_metadata.json point structures/9BKO/9bko_protein.pdb structures/9BKO/9bko_pocket.pdb structures/9BKO/9bko_ligand.sdf structures/9BKO/9bko_ligand.pdb structures/9BKO/9bko_ligand.cif structures/9BKO/9bko_complex.pdb structures/9BKO/9bko_complex.cif 9BLG classic non-receptor protein tyrosine phosphatase SHP2 Na C-terminal His6-tagged full-length SHP2, amino acids 2-527 Na PF-07284892 (ARRY-558) "[""A1AQ1""]" 1 IC50 IC50 = = 21 (±5; n=20) nmol/L 21.0 [] unit_conversion 7.6777807052660805 success True biochemical_inhibition Cell-free biochemical activity assay; PF-07284892 inhibited SHP2. Methods describe recombinant C-terminal His6-tagged full-length SHP2 (amino acids 2–527). 2 “In cell-free systems, PF-07284892 inhibited SHP2 biochemical activity with an IC50 of 21 nmol/L (±5 nmol/L, n = 20).” auto_single_measurement only accepted activity measurement [1] 1 structures\9BLG\9BLG_metadata.json point structures/9BLG/9blg_protein.pdb structures/9BLG/9blg_pocket.pdb structures/9BLG/9blg_ligand.sdf structures/9BLG/9blg_ligand.pdb structures/9BLG/9blg_ligand.cif structures/9BLG/9blg_complex.pdb structures/9BLG/9blg_complex.cif 9BLH classic calcium/calmodulin-dependent protein kinase type II subunit delta (CaMKIIδ) human CaMKIIδ residues 11-309 Na ribociclib "[""6ZZ""]" 1 IC50 IC50 = = 153 nM 153.0 [] unit_conversion 6.815308569182401 success True biochemical_inhibition In vitro CaMKIIδ kinase activity assay using a peptide substrate. 4 Figure 2B explicitly prints “IC50: 153 nM” for ribociclib; the caption identifies it as an in vitro CaMKIIδ activity assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9BLH\9BLH_metadata.json point structures/9BLH/9blh_protein.pdb structures/9BLH/9blh_pocket.pdb structures/9BLH/9blh_ligand.sdf structures/9BLH/9blh_ligand.pdb structures/9BLH/9blh_ligand.cif structures/9BLH/9blh_complex.pdb structures/9BLH/9blh_complex.cif 9BO0 classic SARS-CoV-2 main protease SARS-CoV-2 Na T21I Mpro61 "[""XEK""]" 1 Ki Ki = = 55 (47–63) nM 55.0 [] unit_conversion 7.259637310505756 success True biochemical_inhibition FRET-based kinetic assay; Ki determined with the Morrison equation. 6 Figure 5D lists Mpro61 Ki for T21I as 55 (47–63) nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BO0\9BO0_metadata.json point structures/9BO0/9bo0_protein.pdb structures/9BO0/9bo0_pocket.pdb structures/9BO0/9bo0_ligand.sdf structures/9BO0/9bo0_ligand.pdb structures/9BO0/9bo0_ligand.cif structures/9BO0/9bo0_complex.pdb structures/9BO0/9bo0_complex.cif 9BO1 classic SARS-CoV-2 main protease SARS-CoV-2 Na T190I Mpro61 "[""XEK""]" 1 Ki Ki = = 79 (71–88) nM 79.0 [] unit_conversion 7.102372908709558 success True biochemical_inhibition FRET-based kinetic assay; Ki determined with the Morrison equation. 6 Figure 5D lists Mpro61 Ki for T190I as 79 (71–88) nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BO1\9BO1_metadata.json point structures/9BO1/9bo1_protein.pdb structures/9BO1/9bo1_pocket.pdb structures/9BO1/9bo1_ligand.sdf structures/9BO1/9bo1_ligand.pdb structures/9BO1/9bo1_ligand.cif structures/9BO1/9bo1_complex.pdb structures/9BO1/9bo1_complex.cif 9BO2 classic SARS-CoV-2 main protease SARS-CoV-2 Na A173V/L50F Mpro61 "[""XEK""]" 1 Ki Ki = = 92 (82–102) nM 92.0 [] unit_conversion 7.036212172654444 success True biochemical_inhibition FRET-based kinetic assay; Ki determined with the Morrison equation. 6 Figure 5D lists Mpro61 Ki for A173V/L50F as 92 (82–102) nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BO2\9BO2_metadata.json point structures/9BO2/9bo2_protein.pdb structures/9BO2/9bo2_pocket.pdb structures/9BO2/9bo2_ligand.sdf structures/9BO2/9bo2_ligand.pdb structures/9BO2/9bo2_ligand.cif structures/9BO2/9bo2_complex.pdb structures/9BO2/9bo2_complex.cif 9BO3 classic SARS-CoV-2 main protease SARS-CoV-2 Na E166V Mpro61 "[""XEK""]" 1 Ki Ki > > 1000 nM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition FRET-based kinetic assay; Ki determined with the Morrison equation. 6 Figure 5D lists Mpro61 Ki for E166V as >1000 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BO3\9BO3_metadata.json point structures/9BO3/9bo3_protein.pdb structures/9BO3/9bo3_pocket.pdb structures/9BO3/9bo3_ligand.sdf structures/9BO3/9bo3_ligand.pdb structures/9BO3/9bo3_ligand.cif structures/9BO3/9bo3_complex.pdb structures/9BO3/9bo3_complex.cif 9BOQ classic human p97/VCP ATPase human full-length p97 ATPase WT NSC799462 "[""XKM""]" 1 IC50 IC50 = = 15 nM 15.0 [] unit_conversion 7.823908740944319 success True biochemical_inhibition Purified p97 ATPase activity inhibition; the paper states NSC799462 has an IC50 of 15 nM. The assay does not state oligomeric state. 4 “NSC799462 exhibits a lower IC50 of 15 nM … indicating a stronger inhibitory potency.” auto_single_measurement only accepted activity measurement [1] 1 structures\9BOQ\9BOQ_metadata.json point structures/9BOQ/9boq_protein.pdb structures/9BOQ/9boq_pocket.pdb structures/9BOQ/9boq_ligand.sdf structures/9BOQ/9boq_ligand.pdb structures/9BOQ/9boq_ligand.cif structures/9BOQ/9boq_complex.pdb structures/9BOQ/9boq_complex.cif 9BP9 extended Human DNA polymerase theta helicase domain (Poltheta-hel) human Poltheta-hel residues 1-894; expressed as a His6-SUMO-PreScissionProtease fusion Na AB25583 "[""WCN""]" 1 IC50 IC50 = = 6 nM 6.0 [] unit_conversion 8.221848749616356 success True biochemical_inhibition ADP-Glo ATPase inhibition assay; recombinant Polθ-he incubated with ssDNA and 100 µM ATP for 60 min at room temperature. 2 “The IC50 of AB25583 against Polθ-hel was determined using the Promega ADP-Glo assay in triplicate” and “AB25583 exhibited 6 nM IC50.” auto_single_measurement only accepted activity measurement [1] 1 structures\9BP9\9BP9_metadata.json point structures/9BP9/9bp9_protein.pdb structures/9BP9/9bp9_pocket.pdb structures/9BP9/9bp9_ligand.pdb structures/9BP9/9bp9_ligand.cif structures/9BP9/9bp9_complex.pdb structures/9BP9/9bp9_complex.cif 9BPA extended Human DNA polymerase theta helicase domain (Poltheta-hel) human Poltheta-hel residues 1-894; expressed as a His6-SUMO-PreScissionProtease fusion Na AB25583 "[""WCN""]" 1 IC50 IC50 = = 6 nM 6.0 [] unit_conversion 8.221848749616356 success True biochemical_inhibition ADP-Glo ATPase inhibition assay; recombinant Polθ-he incubated with ssDNA and 100 µM ATP for 60 min at room temperature. 2 “The IC50 of AB25583 against Polθ-hel was determined using the Promega ADP-Glo assay in triplicate” and “AB25583 exhibited 6 nM IC50.” auto_single_measurement only accepted activity measurement [1] 1 structures\9BPA\9BPA_metadata.json point structures/9BPA/9bpa_protein.pdb structures/9BPA/9bpa_pocket.pdb structures/9BPA/9bpa_ligand.pdb structures/9BPA/9bpa_ligand.cif structures/9BPA/9bpa_complex.pdb structures/9BPA/9bpa_complex.cif 9BPC classic P2X3 receptor Canis lupus sp. P2X3 with deletion of five N-terminal residues and 33 C-terminal residues, expressed with a 12His-eGFP-GGS-(thrombin)-GGS-protein-GGS-(HRV3c)-Rho1E tag Na camlipixant "[""A1AQX""]" 1 Kd Kd = = 100 nM 100.0 [] unit_conversion 7.0 success True direct_binding Isothermal titration calorimetry (ITC) of purified P2X3 with camlipixant; no ATP bound. 4 “camlipixant binds to P2X3 with no ATP bound with a Kd of 100 nM using isothermal titration calorimetry (ITC)” auto_single_measurement only accepted activity measurement [1] 1 structures\9BPC\9BPC_metadata.json point structures/9BPC/9bpc_protein.pdb structures/9BPC/9bpc_pocket.pdb structures/9BPC/9bpc_ligand.sdf structures/9BPC/9bpc_ligand.pdb structures/9BPC/9bpc_ligand.cif structures/9BPC/9bpc_complex.pdb structures/9BPC/9bpc_complex.cif 9BQ9 classic Topoisomerase 2 Alpha Human TOP2A residues 29-424 Na obex 5c (compound 5c) "[""A1ASE""]" 1 IC50 IC50 = = 1.5 µM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition In vitro ATPase inhibition assay of recombinant human TOP2A by compound 5c. 3 Fig. 1e labels TOP2A IC50 1.5 µM; its caption identifies inhibition of ATPase activity of recombinant human TOP2A and TOP2B by compound 5c. auto_single_measurement only accepted activity measurement [1] 1 structures\9BQ9\9BQ9_metadata.json point structures/9BQ9/9bq9_protein.pdb structures/9BQ9/9bq9_pocket.pdb structures/9BQ9/9bq9_ligand.sdf structures/9BQ9/9bq9_ligand.pdb structures/9BQ9/9bq9_ligand.cif structures/9BQ9/9bq9_complex.pdb structures/9BQ9/9bq9_complex.cif 9BQC classic Topoisomerase 2 Beta Human TOP2B residues 45-438 Na obex 5c (compound 5c) "[""A1ASE""]" 1 IC50 IC50 = = 0.4 µM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition In vitro ATPase inhibition assay of recombinant human TOP2B by compound 5c. 3 Fig. 1e labels TOP2B IC50 0.4 µM; its caption identifies inhibition of ATPase activity of recombinant human TOP2A and TOP2B by compound 5c. auto_single_measurement only accepted activity measurement [1] 1 structures\9BQC\9BQC_metadata.json point structures/9BQC/9bqc_protein.pdb structures/9BQC/9bqc_pocket.pdb structures/9BQC/9bqc_ligand.sdf structures/9BQC/9bqc_ligand.pdb structures/9BQC/9bqc_ligand.cif structures/9BQC/9bqc_complex.pdb structures/9BQC/9bqc_complex.cif 9BQD classic Topoisomerase 2 Beta Human TOP2B residues 45-438 Na topobexin (compound 9) "[""A1ASC""]" 1 IC50 IC50 = = 0.35 µM 350.0 [] unit_conversion 6.455931955649724 success True biochemical_inhibition ATPase inhibition assay of TOP2B by topobexin. 4 The text states that high TOP2B selectivity was independently confirmed in an ATPase assay: TOP2B IC50 = 0.35 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BQD\9BQD_metadata.json point structures/9BQD/9bqd_protein.pdb structures/9BQD/9bqd_pocket.pdb structures/9BQD/9bqd_ligand.sdf structures/9BQD/9bqd_ligand.pdb structures/9BQD/9bqd_ligand.cif structures/9BQD/9bqd_complex.pdb structures/9BQD/9bqd_complex.cif 9BS5 extended BoSusB (BoGH97C_Sus) Bacteroides ovatus BoSusB expressed from a Lucigen pET-ite construct without a TEV cleavage site, retaining an N-terminal 6xHis tag Na acarbose "[""BRANCHED_ENTITY:2""]" 1 Ki Ki = = 69.3 ± 8.9 nM 69.3 [] unit_conversion 7.159266765388193 success True biochemical_inhibition Purified BoSusB GH97 enzyme kinetics using pNP-Glc; competitive-inhibition model. 8 Table 4 reports BoSusB inhibition constant as 69.3 ± 8.9 nM, with footnote c identifying the metric as Ki. Page 25 maps PDB 9BS5 to the BoSusB-acarbose structure. auto_single_measurement only accepted activity measurement [1] 1 structures\9BS5\9BS5_metadata.json point structures/9BS5/9bs5_protein.pdb structures/9BS5/9bs5_pocket.pdb structures/9BS5/9bs5_ligand.pdb structures/9BS5/9bs5_ligand.cif structures/9BS5/9bs5_complex.pdb structures/9BS5/9bs5_complex.cif 9BT3 extended Chorismate mutase (*MtbCM) Mycobacterium tuberculosis Na Na L2.1 "[""CHAIN:A"", ""CHAIN:B"", ""CHAIN:C"", ""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 2 Kd Kd = = 46 nM 46.0 [] unit_conversion 7.337242168318426 success True direct_binding Surface plasmon resonance binding to biotinylated *MtbCM; KD calculated from koff/kon for nonequilibrated sensorgrams. 4 Table 2 reports L2.1 KD (Req) = 46 nM for binding to biotinylated Mycobacterium tuberculosis chorismate mutase. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9BT3\9BT3_metadata.json point structures/9BT3/9bt3_protein.pdb structures/9BT3/9bt3_pocket.pdb structures/9BT3/9bt3_ligand.pdb structures/9BT3/9bt3_ligand.cif structures/9BT3/9bt3_complex.pdb structures/9BT3/9bt3_complex.cif 9BT6 extended Chorismate mutase (*MtbCM) Mycobacterium tuberculosis Na Na L2.1 "[""POLYMER_ENTITY:2""]" 2 Kd Kd = = 46 nM 46.0 [] unit_conversion 7.337242168318426 success True direct_binding Surface plasmon resonance binding to biotinylated *MtbCM; KD calculated from koff/kon for nonequilibrated sensorgrams. 4 Table 2 reports L2.1 KD (Req) = 46 nM for binding to biotinylated Mycobacterium tuberculosis chorismate mutase. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9BT6\9BT6_metadata.json point structures/9BT6/9bt6_protein.pdb structures/9BT6/9bt6_pocket.pdb structures/9BT6/9bt6_ligand.pdb structures/9BT6/9bt6_ligand.cif structures/9BT6/9bt6_complex.pdb structures/9BT6/9bt6_complex.cif 9BT7 extended Chorismate mutase (*MtbCM) Mycobacterium tuberculosis Na Na D1.3 "[""CHAIN:C"", ""CHAIN:D""]" 2 Kd Kd = = 0.15 µM 150.0 [] unit_conversion 6.823908740944319 success True direct_binding Surface plasmon resonance binding to biotinylated *MtbCM; KD obtained from a single-site hyperbolic fit after equilibrium. 4 Table 2 reports D1.3 KD (Req) = 0.15 µM for binding to biotinylated Mycobacterium tuberculosis chorismate mutase. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9BT7\9BT7_metadata.json point structures/9BT7/9bt7_protein.pdb structures/9BT7/9bt7_pocket.pdb structures/9BT7/9bt7_ligand.pdb structures/9BT7/9bt7_ligand.cif structures/9BT7/9bt7_complex.pdb structures/9BT7/9bt7_complex.cif 9BTA classic HCoV-HKU1 spike glycoprotein D1 Human coronavirus HKU1 Soluble secreted HKU1 D1 domain residues 14-296 with C-terminal 6-His and Avi tags WT 9O-acetyl GD3 sialoglycan (9OAc-GD3ap) "[""A1AR1""]" 1 Kd Kd = = 5.1 ± 0.3 µM 5100.0 [] unit_conversion 5.292429823902063 success True direct_binding Surface plasmon resonance; Figure 2 reports HKU1 D1 affinity for 9OAc-GD3ap. 3 Figure 2 lists 9OAc-GD3ap K_D = 5.1 ± 0.3 µM for HKU1 D1. auto_single_measurement only accepted activity measurement [1] 1 structures\9BTA\9BTA_metadata.json point structures/9BTA/9bta_protein.pdb structures/9BTA/9bta_pocket.pdb structures/9BTA/9bta_ligand.sdf structures/9BTA/9bta_ligand.pdb structures/9BTA/9bta_ligand.cif structures/9BTA/9bta_complex.pdb structures/9BTA/9bta_complex.cif 9BTB classic HCoV-HKU1 spike glycoprotein D1 Human coronavirus HKU1 Soluble secreted HKU1 D1 domain residues 14-296 with C-terminal 6-His and Avi tags WT 9O-acetyl GD3 sialoglycan (9OAc-GD3ap) "[""A1AR1""]" 1 Kd Kd = = 5.1 ± 0.3 µM 5100.0 [] unit_conversion 5.292429823902063 success True direct_binding Surface plasmon resonance; Figure 2 reports HKU1 D1 affinity for 9OAc-GD3ap. 3 Figure 2 lists 9OAc-GD3ap K_D = 5.1 ± 0.3 µM for HKU1 D1. auto_single_measurement only accepted activity measurement [1] 1 structures\9BTB\9BTB_metadata.json point structures/9BTB/9btb_protein.pdb structures/9BTB/9btb_pocket.pdb structures/9BTB/9btb_ligand.sdf structures/9BTB/9btb_ligand.pdb structures/9BTB/9btb_ligand.cif structures/9BTB/9btb_complex.pdb structures/9BTB/9btb_complex.cif 9BTC classic HCoV-HKU1 spike glycoprotein D1 Human coronavirus HKU1 Soluble secreted HKU1 D1 domain residues 14-296 with C-terminal 6-His and Avi tags WT 9O-acetyl GD3 sialoglycan (9OAc-GD3ap) "[""A1AR1""]" 1 Kd Kd = = 5.1 ± 0.3 µM 5100.0 [] unit_conversion 5.292429823902063 success True direct_binding Surface plasmon resonance; Figure 2 reports HKU1 D1 affinity for 9OAc-GD3ap. 3 Figure 2 lists 9OAc-GD3ap K_D = 5.1 ± 0.3 µM for HKU1 D1. auto_single_measurement only accepted activity measurement [1] 1 structures\9BTC\9BTC_metadata.json point structures/9BTC/9btc_protein.pdb structures/9BTC/9btc_pocket.pdb structures/9BTC/9btc_ligand.sdf structures/9BTC/9btc_ligand.pdb structures/9BTC/9btc_ligand.cif structures/9BTC/9btc_complex.pdb structures/9BTC/9btc_complex.cif 9BTN extended SHOC2 human SHOC2 80-582 Na cyclic peptide 4 "[""CHAIN:L""]" 1 Kd Kd = = 0.30 ± 0.19 (n=9) µM 300.0 [] unit_conversion 6.522878745280337 success True direct_binding SPR binding to SHOC2; Table 1 specifies the SHOC2 construct as amino acids 80–582. 6 Table 1 reports Peptide 4 SPR Kd on SHOC2 of 0.30 ± 0.19 µM (n=9). auto_single_measurement only accepted activity measurement [1] 1 structures\9BTN\9BTN_metadata.json point structures/9BTN/9btn_protein.pdb structures/9BTN/9btn_pocket.pdb structures/9BTN/9btn_ligand.pdb structures/9BTN/9btn_ligand.cif structures/9BTN/9btn_complex.pdb structures/9BTN/9btn_complex.cif 9BV5 classic cytochrome P450 3A4 (CYP3A4) human CYP3A4WT with N-terminal deletion of residues 3-23 and a C-terminal 4x His-tag wild-type (CYP3A4WT) SJ000362065 (SCM-01) "[""A1ASV""]" 1 IC50 IC50 = = 0.32 ± 0.03 μM 320.0 [] unit_conversion 6.494850021680094 success True biochemical_inhibition P450-Glo biochemical inhibition assay; concentration-dependent inhibition; triplicate experiments. 3 Fig. 2a reports CYP3A4 IC50 for SCM-01 as 0.32 ± 0.03 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BV5\9BV5_metadata.json point structures/9BV5/9bv5_protein.pdb structures/9BV5/9bv5_pocket.pdb structures/9BV5/9bv5_ligand.sdf structures/9BV5/9bv5_ligand.pdb structures/9BV5/9bv5_ligand.cif structures/9BV5/9bv5_complex.pdb structures/9BV5/9bv5_complex.cif 9BV6 classic cytochrome P450 3A4 (CYP3A4) human CYP3A4WT with N-terminal deletion of residues 3-23 and a C-terminal 4x His-tag wild-type (CYP3A4WT) SJ000388260 (SCM-02) "[""A1ASU""]" 1 IC50 IC50 = = 0.057 ± 0.002 μM 57.0 [] unit_conversion 7.2441251443275085 success True biochemical_inhibition P450-Glo biochemical inhibition assay; concentration-dependent inhibition; triplicate experiments. 3 Fig. 2b reports CYP3A4 IC50 for SCM-02 as 0.057 ± 0.002 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BV6\9BV6_metadata.json point structures/9BV6/9bv6_protein.pdb structures/9BV6/9bv6_pocket.pdb structures/9BV6/9bv6_ligand.sdf structures/9BV6/9bv6_ligand.pdb structures/9BV6/9bv6_ligand.cif structures/9BV6/9bv6_complex.pdb structures/9BV6/9bv6_complex.cif 9BV8 classic cytochrome P450 3A4 (CYP3A4) human CYP3A4WT with N-terminal deletion of residues 3-23 and a C-terminal 4x His-tag wild-type (CYP3A4WT) SJYHJ-114 (SCM-08) "[""A1ASS""]" 1 IC50 IC50 = = 0.43 ± 0.02 μM 430.0 [] unit_conversion 6.366531544420413 success True biochemical_inhibition P450-Glo biochemical inhibition assay; concentration-dependent inhibition; triplicate experiments. 5 Fig. 3b reports CYP3A4 IC50 for SCM-08 as 0.43 ± 0.02 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BV8\9BV8_metadata.json point structures/9BV8/9bv8_protein.pdb structures/9BV8/9bv8_pocket.pdb structures/9BV8/9bv8_ligand.sdf structures/9BV8/9bv8_ligand.pdb structures/9BV8/9bv8_ligand.cif structures/9BV8/9bv8_complex.pdb structures/9BV8/9bv8_complex.cif 9BV9 classic cytochrome P450 3A4 (CYP3A4) human CYP3A4WT with N-terminal deletion of residues 3-23 and a C-terminal 4x His-tag wild-type (CYP3A4WT) Z56791366 (SCM-18) "[""A1ASR""]" 1 IC50 IC50 = = 0.36 ± 0.01 μM 360.0 [] unit_conversion 6.443697499232712 success True biochemical_inhibition P450-Glo biochemical inhibition assay; concentration-dependent inhibition; triplicate experiments. 8 Fig. 5b reports CYP3A4 IC50 for SCM-18 as 0.36 ± 0.01 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BV9\9BV9_metadata.json point structures/9BV9/9bv9_protein.pdb structures/9BV9/9bv9_pocket.pdb structures/9BV9/9bv9_ligand.sdf structures/9BV9/9bv9_ligand.pdb structures/9BV9/9bv9_ligand.cif structures/9BV9/9bv9_complex.pdb structures/9BV9/9bv9_complex.cif 9BVA classic cytochrome P450 3A4 (CYP3A4) human CYP3A4WT with N-terminal deletion of residues 3-23 and a C-terminal 4x His-tag wild-type (CYP3A4WT) SJYHJ-106 (SCM-24) "[""A1ASQ""]" 1 IC50 IC50 = = 0.146 ± 0.006 μM 146.0 [] unit_conversion 6.835647144215563 success True biochemical_inhibition P450-Glo biochemical inhibition assay; concentration-dependent inhibition; triplicate experiments. 9 Fig. 6a reports CYP3A4 IC50 for SCM-24 as 0.146 ± 0.006 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BVA\9BVA_metadata.json point structures/9BVA/9bva_protein.pdb structures/9BVA/9bva_pocket.pdb structures/9BVA/9bva_ligand.sdf structures/9BVA/9bva_ligand.pdb structures/9BVA/9bva_ligand.cif structures/9BVA/9bva_complex.pdb structures/9BVA/9bva_complex.cif 9BVB classic cytochrome P450 3A4 (CYP3A4) human CYP3A4WT with N-terminal deletion of residues 3-23 and a C-terminal 4x His-tag wild-type (CYP3A4WT) SJYHJ-075 (SCM-25) "[""A1ASP""]" 1 IC50 IC50 = = 0.027 ± 0.004 μM 27.0 [] unit_conversion 7.568636235841012 success True biochemical_inhibition P450-Glo biochemical inhibition assay; concentration-dependent inhibition; triplicate experiments. 9 Fig. 6b reports CYP3A4 IC50 for SCM-25 as 0.027 ± 0.004 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BVB\9BVB_metadata.json point structures/9BVB/9bvb_protein.pdb structures/9BVB/9bvb_pocket.pdb structures/9BVB/9bvb_ligand.sdf structures/9BVB/9bvb_ligand.pdb structures/9BVB/9bvb_ligand.cif structures/9BVB/9bvb_complex.pdb structures/9BVB/9bvb_complex.cif 9BVC classic cytochrome P450 3A4 (CYP3A4) human CYP3A4WT with N-terminal deletion of residues 3-23 and a C-terminal 4x His-tag wild-type (CYP3A4WT) SJYHJ-110 (SCM-26) "[""A1ASO""]" 1 IC50 IC50 = = 0.067 ± 0.004 μM 67.0 [] unit_conversion 7.173925197299173 success True biochemical_inhibition P450-Glo biochemical inhibition assay; concentration-dependent inhibition; triplicate experiments. 9 Fig. 6c reports CYP3A4 IC50 for SCM-26 as 0.067 ± 0.004 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9BVC\9BVC_metadata.json point structures/9BVC/9bvc_protein.pdb structures/9BVC/9bvc_pocket.pdb structures/9BVC/9bvc_ligand.sdf structures/9BVC/9bvc_ligand.pdb structures/9BVC/9bvc_ligand.cif structures/9BVC/9bvc_complex.pdb structures/9BVC/9bvc_complex.cif 9BVE extended SOS2 Na SOS2 residues 562-1047, with an N-terminal GST tag and TEV cleavage site; GST tag cleaved before crystallization Na compound 9 "[""A1ASY""]" 1 Kd Kd = = 24 µM 24000.0 [] unit_conversion 4.619788758288394 success True direct_binding SPR direct-binding assay using immobilized SOS2 (construct residues 562–1047). 3 Table 1 reports compound 9 with SOS2 SPR K_D of 24 µM; Figure 2 maps compound 9 to PDB 9BVE. auto_single_measurement only accepted activity measurement [1] 1 structures\9BVE\9BVE_metadata.json point structures/9BVE/9bve_protein.pdb structures/9BVE/9bve_pocket.pdb structures/9BVE/9bve_ligand.pdb structures/9BVE/9bve_ligand.cif structures/9BVE/9bve_complex.pdb structures/9BVE/9bve_complex.cif 9BVF classic SOS2 Na SOS2 residues 562-1047, with an N-terminal GST tag and TEV cleavage site; GST tag cleaved before crystallization Na compound 6 "[""A1ASX""]" 1 Kd Kd = = 1.4 µM 1400.0 [] unit_conversion 5.853871964321762 success True direct_binding SPR direct-binding assay using immobilized SOS2 (construct residues 562–1047). 3 Table 1 reports compound 6 with SOS2 SPR K_D of 1.4 µM; Figure 2 maps compound 6 to PDB 9BVF. auto_single_measurement only accepted activity measurement [1] 1 structures\9BVF\9BVF_metadata.json point structures/9BVF/9bvf_protein.pdb structures/9BVF/9bvf_pocket.pdb structures/9BVF/9bvf_ligand.sdf structures/9BVF/9bvf_ligand.pdb structures/9BVF/9bvf_ligand.cif structures/9BVF/9bvf_complex.pdb structures/9BVF/9bvf_complex.cif 9BVI classic SOS2 Na SOS2 residues 562-1047, with an N-terminal GST tag and TEV cleavage site; GST tag cleaved before crystallization Na compound 2 "[""A1ASW""]" 1 Kd Kd = = 4.6 µM 4600.0 [] unit_conversion 5.337242168318426 success True direct_binding SPR direct-binding assay using immobilized SOS2 (construct residues 562–1047). 3 Table 1 reports compound 2 with SOS2 SPR K_D of 4.6 µM; Figure 2 maps compound 2 to PDB 9BVI. auto_single_measurement only accepted activity measurement [1] 1 structures\9BVI\9BVI_metadata.json point structures/9BVI/9bvi_protein.pdb structures/9BVI/9bvi_pocket.pdb structures/9BVI/9bvi_ligand.sdf structures/9BVI/9bvi_ligand.pdb structures/9BVI/9bvi_ligand.cif structures/9BVI/9bvi_complex.pdb structures/9BVI/9bvi_complex.cif 9C0Y classic Clathrin heavy chain Na GST-fused clathrin heavy chain terminal domain; GST tag cleaved before crystallization Na Pitstop 2c "[""A1ATR""]" 2 IC50 IC50 = = 1.8 µM 1800.0 [] unit_conversion 5.7447274948966935 success True biochemical_inhibition ELISA-based inhibition of the clathrin terminal-domain association with an amphiphysin clathrin-binding domain; table value for compound 76/Pitstop 2c. 6 Table 1, “IC50, cytotoxicity, and cellular activities of Pitstop 2 derivatives,” lists entry 17, compound 76, Pitstop 2c: IC50 [µM] ELISA = 1.8. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\9C0Y\9C0Y_metadata.json point structures/9C0Y/9c0y_protein.pdb structures/9C0Y/9c0y_pocket.pdb structures/9C0Y/9c0y_ligand.sdf structures/9C0Y/9c0y_ligand.pdb structures/9C0Y/9c0y_ligand.cif structures/9C0Y/9c0y_complex.pdb structures/9C0Y/9c0y_complex.cif 9C0Z classic Clathrin heavy chain Na GST-fused clathrin heavy chain terminal domain; GST tag cleaved before crystallization Na Pitstop 2d "[""A1ATQ""]" 2 IC50 IC50 = = 1.7 µM 1700.0 [] unit_conversion 5.769551078621726 success True biochemical_inhibition ELISA-based inhibition of the clathrin terminal-domain association with an amphiphysin clathrin-binding domain; table value for compound 65/Pitstop 2d. 6 Table 1, “IC50, cytotoxicity, and cellular activities of Pitstop 2 derivatives,” lists entry 16, compound 65, Pitstop 2d: IC50 [µM] ELISA = 1.7. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\9C0Z\9C0Z_metadata.json point structures/9C0Z/9c0z_protein.pdb structures/9C0Z/9c0z_pocket.pdb structures/9C0Z/9c0z_ligand.sdf structures/9C0Z/9c0z_ligand.pdb structures/9C0Z/9c0z_ligand.cif structures/9C0Z/9c0z_complex.pdb structures/9C0Z/9c0z_complex.cif 9C1R classic cMET Na Na D1228N compound 13 "[""A1ATS""]" 1 IC50 IC50 = = 6 nM 6.0 [] unit_conversion 8.221848749616356 success True biochemical_inhibition MET D1228N enzyme inhibition assay (Table 2; paired D1228N/exon Δ14 values reported as 6/6 nM). 4 Table 2 reports compound 13 with MET D1228N/exon Δ14 enzyme IC50 values of 6/6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9C1R\9C1R_metadata.json point structures/9C1R/9c1r_protein.pdb structures/9C1R/9c1r_pocket.pdb structures/9C1R/9c1r_ligand.sdf structures/9C1R/9c1r_ligand.pdb structures/9C1R/9c1r_ligand.cif structures/9C1R/9c1r_complex.pdb structures/9C1R/9c1r_complex.cif 9C1Z classic endothelial nitric oxide synthase human heme domain Na compound 8; 7-((3-(((4-(6-aminopyridin-2-yl)butyl)amino)methyl)phenoxy)methyl)quinolin-2-amine "[""V5D""]" 1 Ki Ki = = 1.96 µM 1960.0 [] unit_conversion 5.707743928643524 success True biochemical_inhibition Hemoglobin capture assay; Figure 3 reports heNOS inhibition for compound 8. 4 Figure 3C lists compound 8: heNOS (1.96 µM). The text states that Ki values for synthesized compounds were evaluated using the hemoglobin capture assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9C1Z\9C1Z_metadata.json point structures/9C1Z/9c1z_protein.pdb structures/9C1Z/9c1z_pocket.pdb structures/9C1Z/9c1z_ligand.sdf structures/9C1Z/9c1z_ligand.pdb structures/9C1Z/9c1z_ligand.cif structures/9C1Z/9c1z_complex.pdb structures/9C1Z/9c1z_complex.cif 9C4P classic acetohydroxyacid synthase (AtAHAS) Arabidopsis thaliana Na wild-type triasulfuron "[""A1AUE""]" 1 Ki Ki = = 0.192 ± 0.013 µM 192.0 [] unit_conversion 6.71669877129645 success True biochemical_inhibition Purified-enzyme inhibition assay; Ki measured for wild-type enzyme (Table 1). 3 Table 1 reports triasulfuron Ki = 0.192 ± 0.013 µM for wild-type AtAHAS; footnote states Ki values were measured for the wild-type enzyme. auto_single_measurement only accepted activity measurement [1] 1 structures\9C4P\9C4P_metadata.json point structures/9C4P/9c4p_protein.pdb structures/9C4P/9c4p_pocket.pdb structures/9C4P/9c4p_ligand.sdf structures/9C4P/9c4p_ligand.pdb structures/9C4P/9c4p_ligand.cif structures/9C4P/9c4p_complex.pdb structures/9C4P/9c4p_complex.cif 9C4Q classic acetohydroxyacid synthase (AtAHAS) Arabidopsis thaliana Na wild-type FMO "[""A1AUH""]" 1 Ki Ki = = 0.086 ± 0.013 µM 86.0 [] unit_conversion 7.0655015487564325 success True biochemical_inhibition Purified-enzyme inhibition assay; Ki measured for wild-type enzyme (Table 1). 3 Table 1 reports FMO Ki = 0.086 ± 0.013 µM for wild-type AtAHAS; footnote states Ki values were measured for the wild-type enzyme. auto_single_measurement only accepted activity measurement [1] 1 structures\9C4Q\9C4Q_metadata.json point structures/9C4Q/9c4q_protein.pdb structures/9C4Q/9c4q_pocket.pdb structures/9C4Q/9c4q_ligand.sdf structures/9C4Q/9c4q_ligand.pdb structures/9C4Q/9c4q_ligand.cif structures/9C4Q/9c4q_complex.pdb structures/9C4Q/9c4q_complex.cif 9C4R classic acetohydroxyacid synthase (AtAHAS) Arabidopsis thaliana Na wild-type CMO "[""A1AUL""]" 1 Ki Ki = = 1.448 ± 0.058 µM 1448.0 [] unit_conversion 5.839231438138872 success True biochemical_inhibition Purified-enzyme inhibition assay; Ki measured for wild-type enzyme (Table 1). 3 Table 1 reports CMO Ki = 1.448 ± 0.058 µM for wild-type AtAHAS; footnote states Ki values were measured for the wild-type enzyme. auto_single_measurement only accepted activity measurement [1] 1 structures\9C4R\9C4R_metadata.json point structures/9C4R/9c4r_protein.pdb structures/9C4R/9c4r_pocket.pdb structures/9C4R/9c4r_ligand.sdf structures/9C4R/9c4r_ligand.pdb structures/9C4R/9c4r_ligand.cif structures/9C4R/9c4r_complex.pdb structures/9C4R/9c4r_complex.cif 9C68 extended CRISPR-associated adenosine deaminase 1 (Cad1) unknown Bacteroidales bacterium Cad1-CARF-His6, residues 1-185 Na cA6 "[""CHAIN:C""]" 1 Kd Kd = = 30 nM 30.0 [] unit_conversion 7.522878745280337 success True direct_binding Isothermal titration calorimetry of purified Cad1-CARF-His6 with cA6. 4 The paper states that Cad1-CARF-His6 binds cA6 with a Kd of 30 nM. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\9C68\9C68_metadata.json point structures/9C68/9c68_protein.pdb structures/9C68/9c68_pocket.pdb structures/9C68/9c68_ligand.pdb structures/9C68/9c68_ligand.cif structures/9C68/9c68_complex.pdb structures/9C68/9c68_complex.cif 9C6R classic Blood cell-specific ChET alpha1/beta1-tubulin Gallus gallus (chicken) ChET-Cp-52 C8 ring Na Cryptophycin-52 (Cp-52) "[""YGY""]" 1 Kd Kd = = 65 ± 17 nM 65.0 [] unit_conversion 7.187086643357144 success True direct_binding Mass-photometry Cp-52 binding/assembly isotherm; apparent dissociation constant (Kd-app) for ChET, with C8/C9 ring formation. 9 “Kd-app-ChET = 65 ± 17 nM”; Table 2 reproduces the ChET Kd-app value. auto_single_measurement only accepted activity measurement [1] 1 structures\9C6R\9C6R_metadata.json point structures/9C6R/9c6r_protein.pdb structures/9C6R/9c6r_pocket.pdb structures/9C6R/9c6r_ligand.sdf structures/9C6R/9c6r_ligand.pdb structures/9C6R/9c6r_ligand.cif structures/9C6R/9c6r_complex.pdb structures/9C6R/9c6r_complex.cif 9C6S classic Blood cell-specific ChET alpha1/beta1-tubulin Gallus gallus (chicken) ChET-Cp-52 C9 ring Na Cryptophycin-52 (Cp-52) "[""YGY""]" 1 Kd Kd = = 65 ± 17 nM 65.0 [] unit_conversion 7.187086643357144 success True direct_binding Mass-photometry Cp-52 binding/assembly isotherm; apparent dissociation constant (Kd-app) for ChET, with C8/C9 ring formation. 9 “Kd-app-ChET = 65 ± 17 nM”; Table 2 reproduces the ChET Kd-app value. auto_single_measurement only accepted activity measurement [1] 1 structures\9C6S\9C6S_metadata.json point structures/9C6S/9c6s_protein.pdb structures/9C6S/9c6s_pocket.pdb structures/9C6S/9c6s_ligand.sdf structures/9C6S/9c6s_ligand.pdb structures/9C6S/9c6s_ligand.cif structures/9C6S/9c6s_complex.pdb structures/9C6S/9c6s_complex.cif 9C79 extended Human monoclonal antibody MAD21-101 human Antigen-binding fragment (Fab) used for X-ray crystallography Light-chain C-terminal crystal-packing shortening: T197-HQGLSSPV to T197-QGTTS-V pGluPADGNPDPNANPNVDPN-NH2 peptide corresponding to PfCSP pGlu96-Asn113 "[""CHAIN:D""]" 1 Kd Kd = = 3.8 nM 3.8 [] unit_conversion 8.42021640338319 success True direct_binding ITC of Fab with synthetic pGluPADGNPDPNANP-NH2 peptide; 25°C, triplicate determinations. 9 “The highly protective MAD21-101 produces the strongest binding with an equilibrium dissociation constant (Kd) of 3.8 nM.” The ITC peptide is specified in the methods as pGluPADGNPDPNANP-NH2 (page 26). auto_single_measurement only accepted activity measurement [1] 1 structures\9C79\9C79_metadata.json point structures/9C79/9c79_protein.pdb structures/9C79/9c79_pocket.pdb structures/9C79/9c79_ligand.pdb structures/9C79/9c79_ligand.cif structures/9C79/9c79_complex.pdb structures/9C79/9c79_complex.cif 9CA3 classic MarE Streptomyces sp. B9173 Full-length untagged MarE (residues 1-284) C280S (2S,3S)-beta-methyl-L-tryptophan (beta-Me-L-Trp) "[""78U""]" 1 Kd Kd = = 4.57 ± 0.20 µM 4570.0 [] unit_conversion 5.34008379993015 success True direct_binding ITC measurement of β-Me-L-Trp binding to heme-reconstituted MarE C280S in the presence of 0.1 mM sodium cyanide; one-site binding model, triplicate measurements. 8 Table 2 reports C280S K_D = 4.57 ± 0.20 µM; the Figure 8 caption states β-Me-L-Trp binding was measured by ITC. Experimental procedures specify heme-containing protein and 0.1 mM sodium cyanide. auto_single_measurement only accepted activity measurement [1] 1 structures\9CA3\9CA3_metadata.json point structures/9CA3/9ca3_protein.pdb structures/9CA3/9ca3_pocket.pdb structures/9CA3/9ca3_ligand.sdf structures/9CA3/9ca3_ligand.pdb structures/9CA3/9ca3_ligand.cif structures/9CA3/9ca3_complex.pdb structures/9CA3/9ca3_complex.cif 9CBF classic Danio rerio histone deacetylase 10 (HDAC10) Danio rerio Humanized Danio rerio HDAC10 construct A24E; D94A Inhibitor 1 (m-aminomethyl phenylthioketone) "[""A1AVR""]" 1 IC50 IC50 = = 0.29 ± 0.05 µM 290.0 [] unit_conversion 6.537602002101044 success True biochemical_inhibition Adapted peroxidase protocol with N-acetylputrescine; inhibitor was incubated with HDAC10 for 18 h to ensure complete deacetylation to the active thiol before IC50 measurement. 4 Table 2 prints HDAC10 IC50 for inhibitor 1 as 0.29 ± 0.05 µM; text identifies the assay as using humanized HDAC10 and states inhibitors were deacetylated before measurement. auto_single_measurement only accepted activity measurement [1] 1 structures\9CBF\9CBF_metadata.json point structures/9CBF/9cbf_protein.pdb structures/9CBF/9cbf_pocket.pdb structures/9CBF/9cbf_ligand.sdf structures/9CBF/9cbf_ligand.pdb structures/9CBF/9cbf_ligand.cif structures/9CBF/9cbf_complex.pdb structures/9CBF/9cbf_complex.cif 9CBG classic Danio rerio histone deacetylase 10 (HDAC10) Danio rerio Humanized Danio rerio HDAC10 construct A24E; D94A Inhibitor 2 (m-aminoethyl phenylthioketone) "[""A1AVN""]" 1 IC50 IC50 = = 0.26 ± 0.03 µM 260.0 [] unit_conversion 6.585026652029182 success True biochemical_inhibition Adapted peroxidase protocol with N-acetylputrescine; inhibitor was incubated with HDAC10 for 18 h to ensure complete deacetylation to the active thiol before IC50 measurement. 4 Table 2 prints HDAC10 IC50 for inhibitor 2 as 0.26 ± 0.03 µM; text identifies the assay as using humanized HDAC10 and states inhibitors were deacetylated before measurement. auto_single_measurement only accepted activity measurement [1] 1 structures\9CBG\9CBG_metadata.json point structures/9CBG/9cbg_protein.pdb structures/9CBG/9cbg_pocket.pdb structures/9CBG/9cbg_ligand.sdf structures/9CBG/9cbg_ligand.pdb structures/9CBG/9cbg_ligand.cif structures/9CBG/9cbg_complex.pdb structures/9CBG/9cbg_complex.cif 9CBH classic Danio rerio histone deacetylase 10 (HDAC10) Danio rerio Humanized Danio rerio HDAC10 construct A24E; D94A Inhibitor 4 (p-aminomethyl phenylthioketone) "[""A1AVM""]" 1 IC50 IC50 = = 0.04 ± 0.01 µM 40.0 [] unit_conversion 7.3979400086720375 success True biochemical_inhibition Adapted peroxidase protocol with N-acetylputrescine; inhibitor was incubated with HDAC10 for 18 h to ensure complete deacetylation to the active thiol before IC50 measurement. 4 Table 2 prints HDAC10 IC50 for inhibitor 4 as 0.04 ± 0.01 µM; text identifies the assay as using humanized HDAC10 and states inhibitors were deacetylated before measurement. auto_single_measurement only accepted activity measurement [1] 1 structures\9CBH\9CBH_metadata.json point structures/9CBH/9cbh_protein.pdb structures/9CBH/9cbh_pocket.pdb structures/9CBH/9cbh_ligand.sdf structures/9CBH/9cbh_ligand.pdb structures/9CBH/9cbh_ligand.cif structures/9CBH/9cbh_complex.pdb structures/9CBH/9cbh_complex.cif 9CBI classic Danio rerio histone deacetylase 10 (HDAC10) Danio rerio Humanized Danio rerio HDAC10 construct A24E; D94A Inhibitor 5 (p-aminoethyl phenylthioketone) "[""A1AVQ""]" 1 IC50 IC50 = = 0.07 ± 0.01 µM 70.0 [] unit_conversion 7.154901959985743 success True biochemical_inhibition Adapted peroxidase protocol with N-acetylputrescine; inhibitor was incubated with HDAC10 for 18 h to ensure complete deacetylation to the active thiol before IC50 measurement. 4 Table 2 prints HDAC10 IC50 for inhibitor 5 as 0.07 ± 0.01 µM; text identifies the assay as using humanized HDAC10 and states inhibitors were deacetylated before measurement. auto_single_measurement only accepted activity measurement [1] 1 structures\9CBI\9CBI_metadata.json point structures/9CBI/9cbi_protein.pdb structures/9CBI/9cbi_pocket.pdb structures/9CBI/9cbi_ligand.sdf structures/9CBI/9cbi_ligand.pdb structures/9CBI/9cbi_ligand.cif structures/9CBI/9cbi_complex.pdb structures/9CBI/9cbi_complex.cif 9CBJ classic Danio rerio histone deacetylase 10 (HDAC10) Danio rerio Humanized Danio rerio HDAC10 construct A24E; D94A Inhibitor 6 (p-aminopropyl phenylthioketone) "[""A1AVP""]" 1 IC50 IC50 = = 0.4 ± 0.1 µM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition Adapted peroxidase protocol with N-acetylputrescine; inhibitor was incubated with HDAC10 for 18 h to ensure complete deacetylation to the active thiol before IC50 measurement. 4 Table 2 prints HDAC10 IC50 for inhibitor 6 as 0.4 ± 0.1 µM; text identifies the assay as using humanized HDAC10 and states inhibitors were deacetylated before measurement. auto_single_measurement only accepted activity measurement [1] 1 structures\9CBJ\9CBJ_metadata.json point structures/9CBJ/9cbj_protein.pdb structures/9CBJ/9cbj_pocket.pdb structures/9CBJ/9cbj_ligand.sdf structures/9CBJ/9cbj_ligand.pdb structures/9CBJ/9cbj_ligand.cif structures/9CBJ/9cbj_complex.pdb structures/9CBJ/9cbj_complex.cif 9CBK classic Danio rerio histone deacetylase 6 (HDAC6) Danio rerio Na Na Inhibitor 4 (p-aminomethyl phenylthioketone) "[""A1AVM""]" 1 IC50 IC50 = = 0.32 ± 0.06 µM 320.0 [] unit_conversion 6.494850021680094 success True biochemical_inhibition Adapted peroxidase protocol with N-acetylputrescine; because of HDAC6 instability in 18 h incubations, inhibitor was pre-deacetylated in basic solution before IC50 measurement. 4 Table 2 prints HDAC6 IC50 for inhibitor 4 as 0.32 ± 0.06 µM. The accompanying text states that HDAC6 inhibitors were pre-deacetylated before IC50 measurement. auto_single_measurement only accepted activity measurement [1] 1 structures\9CBK\9CBK_metadata.json point structures/9CBK/9cbk_protein.pdb structures/9CBK/9cbk_pocket.pdb structures/9CBK/9cbk_ligand.sdf structures/9CBK/9cbk_ligand.pdb structures/9CBK/9cbk_ligand.cif structures/9CBK/9cbk_complex.pdb structures/9CBK/9cbk_complex.cif 9CC5 extended Amylin-22alpha-beta-L designed binder Na Na Na Amylin (human islet amyloid polypeptide; hIAPP) "[""CHAIN:B""]" 1 Kd Kd = = 100 nM 100.0 [] unit_conversion 7.0 success True direct_binding Biolayer interferometry (BLI) measurement of designed binder–amylin interaction. 3 Fig. 2d labels the amylin-22αβL design with “Kd = 100 nM”; the caption states that BLI measurements of designed binder–amylin interactions are shown below each design model. auto_single_measurement only accepted activity measurement [1] 1 structures\9CC5\9CC5_metadata.json point structures/9CC5/9cc5_protein.pdb structures/9CC5/9cc5_pocket.pdb structures/9CC5/9cc5_ligand.pdb structures/9CC5/9cc5_ligand.cif structures/9CC5/9cc5_complex.pdb structures/9CC5/9cc5_complex.cif 9CCE extended DYNA_1b7 Na Na Na dynorphin A (residues 1 to 17) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 7 nM 7.0 [] unit_conversion 8.154901959985743 success True direct_binding Bio-layer interferometry; DYNA_1b7–dynorphin A binding, with the co-crystal structure described for this 7-nM-Kd design. 7 “a co-crystal structure of a 7-nM-Kd dynorphin A binding design, DYNA_1b7, in complex with dynorphin A (residues 1 to 17)” auto_single_measurement only accepted activity measurement [1] 1 structures\9CCE\9CCE_metadata.json point structures/9CCE/9cce_protein.pdb structures/9CCE/9cce_pocket.pdb structures/9CCE/9cce_ligand.pdb structures/9CCE/9cce_ligand.cif structures/9CCE/9cce_complex.pdb structures/9CCE/9cce_complex.cif 9CCX classic Klebsiella pneumoniae LpxH Klebsiella pneumoniae Modified pET21b KpLpxH fusion with a C-terminal TEV protease site (ENLYFQGS) followed by a His10 tag Na JH-LPH-86 "[""A1AVZ""]" 1 IC50 IC50 = = 85 nM 85.0 [] unit_conversion 7.070581074285707 success True biochemical_inhibition LpxE-coupled LpxH activity assay; Table 1. 6 Table 1 reports JH-LPH-86 IC50 = 85 nM; table footnote states unparenthesized values were assayed against K. pneumoniae LpxH. auto_single_measurement only accepted activity measurement [1] 1 structures\9CCX\9CCX_metadata.json point structures/9CCX/9ccx_protein.pdb structures/9CCX/9ccx_pocket.pdb structures/9CCX/9ccx_ligand.sdf structures/9CCX/9ccx_ligand.pdb structures/9CCX/9ccx_ligand.cif structures/9CCX/9ccx_complex.pdb structures/9CCX/9ccx_complex.cif 9CCY classic Klebsiella pneumoniae LpxH Klebsiella pneumoniae Modified pET21b KpLpxH fusion with a C-terminal TEV protease site (ENLYFQGS) followed by a His10 tag Na JH-LPH-90 "[""A1AVY""]" 1 IC50 IC50 = = 112 nM 112.0 [] unit_conversion 6.950781977329818 success True biochemical_inhibition LpxE-coupled LpxH activity assay; Table 1. 6 Table 1 reports JH-LPH-90 IC50 = 112 nM; unparenthesized values were assayed against K. pneumoniae LpxH. auto_single_measurement only accepted activity measurement [1] 1 structures\9CCY\9CCY_metadata.json point structures/9CCY/9ccy_protein.pdb structures/9CCY/9ccy_pocket.pdb structures/9CCY/9ccy_ligand.sdf structures/9CCY/9ccy_ligand.pdb structures/9CCY/9ccy_ligand.cif structures/9CCY/9ccy_complex.pdb structures/9CCY/9ccy_complex.cif 9CCZ classic Klebsiella pneumoniae LpxH Klebsiella pneumoniae Modified pET21b KpLpxH fusion with a C-terminal TEV protease site (ENLYFQGS) followed by a His10 tag Na JH-LPH-92 "[""A1AV0""]" 1 IC50 IC50 = = 4.6 nM 4.6 [] unit_conversion 8.337242168318426 success True biochemical_inhibition LpxE-coupled LpxH activity assay; Table 1. 6 Table 1 reports JH-LPH-92 IC50 = 4.6 nM; unparenthesized values were assayed against K. pneumoniae LpxH. auto_single_measurement only accepted activity measurement [1] 1 structures\9CCZ\9CCZ_metadata.json point structures/9CCZ/9ccz_protein.pdb structures/9CCZ/9ccz_pocket.pdb structures/9CCZ/9ccz_ligand.sdf structures/9CCZ/9ccz_ligand.pdb structures/9CCZ/9ccz_ligand.cif structures/9CCZ/9ccz_complex.pdb structures/9CCZ/9ccz_complex.cif 9CD0 classic Klebsiella pneumoniae LpxH Klebsiella pneumoniae Modified pET21b KpLpxH fusion with a C-terminal TEV protease site (ENLYFQGS) followed by a His10 tag Na JH-LPH-106 "[""A1AVX""]" 2 Ki Ki = = 0.02 nM 0.02 [] unit_conversion 10.698970004336019 success True biochemical_inhibition Ki derived for competitive inhibition; Figure 3C KpLpxH bar. 7 Figure 3C reports a Ki value of 0.02 nM for JH-LPH-106 against KpLpxH. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9CD0\9CD0_metadata.json point structures/9CD0/9cd0_protein.pdb structures/9CD0/9cd0_pocket.pdb structures/9CD0/9cd0_ligand.sdf structures/9CD0/9cd0_ligand.pdb structures/9CD0/9cd0_ligand.cif structures/9CD0/9cd0_complex.pdb structures/9CD0/9cd0_complex.cif 9CD1 classic Klebsiella pneumoniae LpxH Klebsiella pneumoniae Modified pET21b KpLpxH fusion with a C-terminal TEV protease site (ENLYFQGS) followed by a His10 tag Na JH-LPH-107 "[""A1AVW""]" 2 Ki Ki = = 0.05 nM 0.05 [] unit_conversion 10.301029995663981 success True biochemical_inhibition Ki derived for competitive inhibition; Figure 3C KpLpxH bar. 7 Figure 3C reports a Ki value of 0.05 nM for JH-LPH-107 against KpLpxH. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9CD1\9CD1_metadata.json point structures/9CD1/9cd1_protein.pdb structures/9CD1/9cd1_pocket.pdb structures/9CD1/9cd1_ligand.sdf structures/9CD1/9cd1_ligand.pdb structures/9CD1/9cd1_ligand.cif structures/9CD1/9cd1_complex.pdb structures/9CD1/9cd1_complex.cif 9CD5 extended FGFR1 Na Na Na TYRA-300 (22) "[""A1AV2""]" 1 IC50 IC50 = = 108 nM 108.0 [] unit_conversion 6.96657624451305 success True biochemical_inhibition Functional kinase Mobility Shift Assay measuring phosphorylation of a peptide substrate; 100 μM ATP. 7 Table 5 reports enzymatic IC50 for compound 22 against FGFR1 as 108 nM; the text identifies compound 22 as TYRA-300. auto_single_measurement only accepted activity measurement [1] 1 structures\9CD5\9CD5_metadata.json point structures/9CD5/9cd5_protein.pdb structures/9CD5/9cd5_pocket.pdb structures/9CD5/9cd5_ligand.pdb structures/9CD5/9cd5_ligand.cif structures/9CD5/9cd5_complex.pdb structures/9CD5/9cd5_complex.cif 9CD7 extended FGFR3 Na Na Na TYRA-300 (22) "[""A1AV2""]" 1 IC50 IC50 = = 1.6 nM 1.6 [] unit_conversion 8.795880017344075 success True biochemical_inhibition Functional kinase Mobility Shift Assay measuring phosphorylation of a peptide substrate; ATP was set to the Km for each enzyme variant. 7 Table 5 reports an enzymatic IC50 of 1.6 nM for compound 22 against FGFR3 WT; compound 22 is identified as TYRA-300. auto_single_measurement only accepted activity measurement [1] 1 structures\9CD7\9CD7_metadata.json point structures/9CD7/9cd7_protein.pdb structures/9CD7/9cd7_pocket.pdb structures/9CD7/9cd7_ligand.pdb structures/9CD7/9cd7_ligand.cif structures/9CD7/9cd7_complex.pdb structures/9CD7/9cd7_complex.cif 9CDK classic SARS-CoV-2 Main Protease (Mpro) SARS-CoV-2 Na A173V Mpro61 "[""XEK""]" 1 Ki Ki = = 83 (69–100) nM 83.0 [] unit_conversion 7.080921907623926 success True biochemical_inhibition FRET-based biochemical kinetic inhibition assay; Ki determined using the Morrison equation. 6 Figure 5D lists Mpro61 Ki for A173V Mpro as 83 (69–100) nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9CDK\9CDK_metadata.json point structures/9CDK/9cdk_protein.pdb structures/9CDK/9cdk_pocket.pdb structures/9CDK/9cdk_ligand.sdf structures/9CDK/9cdk_ligand.pdb structures/9CDK/9cdk_ligand.cif structures/9CDK/9cdk_complex.pdb structures/9CDK/9cdk_complex.cif 9CDL classic SARS-CoV-2 Main Protease (Mpro) SARS-CoV-2 Na E166V/L50F Mpro61 "[""XEK""]" 1 Ki Ki > > 1000 nM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition FRET-based biochemical kinetic inhibition assay; Ki determined using the Morrison equation. 6 Figure 5D lists Mpro61 Ki for E166V/L50F Mpro as >1000 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9CDL\9CDL_metadata.json point structures/9CDL/9cdl_protein.pdb structures/9CDL/9cdl_pocket.pdb structures/9CDL/9cdl_ligand.sdf structures/9CDL/9cdl_ligand.pdb structures/9CDL/9cdl_ligand.cif structures/9CDL/9cdl_complex.pdb structures/9CDL/9cdl_complex.cif 9CDM classic SARS-CoV-2 Main Protease (Mpro) SARS-CoV-2 Na L50F Mpro61 "[""XEK""]" 1 Ki Ki = = 67 (60–75) nM 67.0 [] unit_conversion 7.173925197299173 success True biochemical_inhibition FRET-based biochemical kinetic inhibition assay; Ki determined using the Morrison equation. 6 Figure 5D lists Mpro61 Ki for L50F Mpro as 67 (60–75) nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9CDM\9CDM_metadata.json point structures/9CDM/9cdm_protein.pdb structures/9CDM/9cdm_pocket.pdb structures/9CDM/9cdm_ligand.sdf structures/9CDM/9cdm_ligand.pdb structures/9CDM/9cdm_ligand.cif structures/9CDM/9cdm_complex.pdb structures/9CDM/9cdm_complex.cif 9CDT extended MCL1 Na Na Na MCB_D2 "[""CHAIN:B""]" 1 Kd Kd = = 2.0 µM 2000.0 [] unit_conversion 5.698970004336019 success True direct_binding SPR nine-point single-cycle kinetics experiment. 4 Fig. 2b reports affinity determination of MCB_D2 using SPR and prints Kd 2.0 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9CDT\9CDT_metadata.json point structures/9CDT/9cdt_protein.pdb structures/9CDT/9cdt_pocket.pdb structures/9CDT/9cdt_ligand.pdb structures/9CDT/9cdt_ligand.cif structures/9CDT/9cdt_complex.pdb structures/9CDT/9cdt_complex.cif 9CDY classic dual leucine zipper kinase (DLK) human Na Na compound 51 "[""A1AZ8""]" 1 Ki Ki = = 1.9 nM 1.9 [] unit_conversion 8.721246399047171 success True biochemical_inhibition Pyrazolopyridinone SAR, experimentally determined DLK Ki (reported alongside FEP prediction). 12 Table 9 lists compound 51 with DLK Ki = 1.9 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9CDY\9CDY_metadata.json point structures/9CDY/9cdy_protein.pdb structures/9CDY/9cdy_pocket.pdb structures/9CDY/9cdy_ligand.sdf structures/9CDY/9cdy_ligand.pdb structures/9CDY/9cdy_ligand.cif structures/9CDY/9cdy_complex.pdb structures/9CDY/9cdy_complex.cif 9CDZ extended MDM2 Na Na Na RMG_14 "[""CHAIN:B"", ""CHAIN:D""]" 2 Kd Kd = = 3.0 µM 3000.0 [] unit_conversion 5.522878745280337 success True direct_binding Surface plasmon resonance single-cycle kinetics experiment for RMG_14 binding MDM2. 9 Figure 5d prints “KD: 3.0 µM” for RMG_14. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9CDZ\9CDZ_metadata.json point structures/9CDZ/9cdz_protein.pdb structures/9CDZ/9cdz_pocket.pdb structures/9CDZ/9cdz_ligand.pdb structures/9CDZ/9cdz_ligand.cif structures/9CDZ/9cdz_complex.pdb structures/9CDZ/9cdz_complex.cif 9CE8 classic Mycobacterium tuberculosis 20S proteasome core particle Mycobacterium tuberculosis Na Wild-type (WT) Ixazomib "[""6V8""]" 1 IC50 IC50 = = 1.1 µM 1100.0 [] unit_conversion 5.958607314841775 success True biochemical_inhibition Z-VLR-AMC peptidase-inhibition dose-response fitted to a modified Hill model. 3 Ixazomib inhibited 20SWT peptidase activity, yielding IC50 1.1 µM (95% C.I. 1.0–1.3). auto_single_measurement only accepted activity measurement [1] 1 structures\9CE8\9CE8_metadata.json point structures/9CE8/9ce8_protein.pdb structures/9CE8/9ce8_pocket.pdb structures/9CE8/9ce8_ligand.sdf structures/9CE8/9ce8_ligand.pdb structures/9CE8/9ce8_ligand.cif structures/9CE8/9ce8_complex.pdb structures/9CE8/9ce8_complex.cif 9CFP classic TarGH Staphylococcus aureus Na Na targocil-II "[""A1AV9""]" 1 Kd Kd = = 0.93 ± 0.25 µM 930.0 [] unit_conversion 6.031517051446064 success True direct_binding Microscale thermophoresis measurement of targocil-II binding to AMP-PNP-bound S. aureus TarGH. 6 Fig. 3c reports targocil-II binding to AMP-PNP-bound TarGH: Kd = 0.93 ± 0.25 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9CFP\9CFP_metadata.json point structures/9CFP/9cfp_protein.pdb structures/9CFP/9cfp_pocket.pdb structures/9CFP/9cfp_ligand.sdf structures/9CFP/9cfp_ligand.pdb structures/9CFP/9cfp_ligand.cif structures/9CFP/9cfp_complex.pdb structures/9CFP/9cfp_complex.cif 9CJQ classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Mpro quadruple mutant QM T21I; L50F; S144A; E166V Ensitrelvir "[""7YY""]" 1 IC50 IC50 = = 5.1 µM 5100.0 [] unit_conversion 5.292429823902063 success True biochemical_inhibition Inhibition assay against 1.0 µM Mpro; IC50 summarized from Fig. 2A-C, at least three replicates. 6 Table 3 reports QM (T21I/L50F/S144A/E166V) ensitrelvir IC50 = 5.1 µM (4.0 to 6.5 µM). auto_single_measurement only accepted activity measurement [1] 1 structures\9CJQ\9CJQ_metadata.json point structures/9CJQ/9cjq_protein.pdb structures/9CJQ/9cjq_pocket.pdb structures/9CJQ/9cjq_ligand.sdf structures/9CJQ/9cjq_ligand.pdb structures/9CJQ/9cjq_ligand.cif structures/9CJQ/9cjq_complex.pdb structures/9CJQ/9cjq_complex.cif 9CPF extended MCL-1:BAK BH3 complex human MBP-GS-MCL-1, MCL-1 residues 171-321, with V74A BAK BH3 peptide BAK BH3 V74A BAK BH3 V74A peptide (BAK_BH3_V74A; SSTMGQAGRQLAIIGDDINRRY) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 IC50 IC50 = = 195.4 ± 39.3 nM 195.4 [] unit_conversion 6.709075440617246 success True biochemical_inhibition Competitive fluorescence-polarization displacement of BID SAHB-FAM from MCL-1; batch 2. 32 Figure 4C reports BAK BH3 V74A IC50 = 195.4 ± 39.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9CPF\9CPF_metadata.json point structures/9CPF/9cpf_protein.pdb structures/9CPF/9cpf_pocket.pdb structures/9CPF/9cpf_ligand.pdb structures/9CPF/9cpf_ligand.cif structures/9CPF/9cpf_complex.pdb structures/9CPF/9cpf_complex.cif 9CPN extended MCL-1:BAK BH3 complex human MBP-GS-MCL-1, MCL-1 residues 171-321, with WT BAK BH3 peptide BAK BH3 WT BAK BH3 WT peptide (BAK_BH3_WT; SSTMGQVGRQLAIIGDDINRRY) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G"", ""CHAIN:H""]" 1 Kd Kd = = 20.5 ± 8.0 nM 20.5 [] unit_conversion 7.688246138944246 success True direct_binding Microscale thermophoresis direct binding of MCL-1 and BAK BH3 peptide. 5 The text states that direct MCL-1–BAK BH3 peptide binding measured by MST gave K_D = 20.5 ± 8.0 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\9CPN\9CPN_metadata.json point structures/9CPN/9cpn_protein.pdb structures/9CPN/9cpn_pocket.pdb structures/9CPN/9cpn_ligand.pdb structures/9CPN/9cpn_ligand.cif structures/9CPN/9cpn_complex.pdb structures/9CPN/9cpn_complex.cif 9CSC classic CtfAB Thermosipho melanesiensis Heterodimeric CtfAB with N-terminal 6xHis-tagged CtfA alpha subunit and untagged CtfB beta subunit WT (wild-type) acetate "[""ACT""]" 1 Ki Ki = = 2.47 × 10^4 ± 1.66 × 10^4 µm 24700000.000000004 [] unit_conversion 1.6073030467403342 success True biochemical_inhibition Forward ping-pong bi-bi kinetic fit; Ki,B for acetate. 6 Table 1 reports Ki,B = 2.47 × 10^4 ± 1.66 × 10^4 µm for T. melanesiensis CtfAB. auto_single_measurement only accepted activity measurement [1] 1 structures\9CSC\9CSC_metadata.json point structures/9CSC/9csc_protein.pdb structures/9CSC/9csc_pocket.pdb structures/9CSC/9csc_ligand.sdf structures/9CSC/9csc_ligand.pdb structures/9CSC/9csc_ligand.cif structures/9CSC/9csc_complex.pdb structures/9CSC/9csc_complex.cif 9CTI classic EcPKS2 Elysia chlorotica condensing region Na malonyl-CoA (MC) "[""MLC""]" 1 IC50 IC50 = = 10 µM 10000.0 [] unit_conversion 5.0 success True biochemical_inhibition Purified EcPKS2 inhibited by MC; reported with 250 µM MC in the inhibition experiment. 3 “EcPKS2 was rapidly inactivated, with a t1/2 of 1.4 min in the presence of 250 µM MC, with a 10 µM IC50.” auto_single_measurement only accepted activity measurement [1] 1 structures\9CTI\9CTI_metadata.json point structures/9CTI/9cti_protein.pdb structures/9CTI/9cti_pocket.pdb structures/9CTI/9cti_ligand.sdf structures/9CTI/9cti_ligand.pdb structures/9CTI/9cti_ligand.cif structures/9CTI/9cti_complex.pdb structures/9CTI/9cti_complex.cif 9CTL classic EcPKS2 Elysia chlorotica full-length Na malonyl-CoA (MC); Cys-loaded malonate (MalCys) "[""MLC""]" 1 IC50 IC50 = = 10 µM 10000.0 [] unit_conversion 5.0 success True biochemical_inhibition Purified EcPKS2 inhibited by MC; reported with 250 µM MC in the inhibition experiment. 3 “EcPKS2 was rapidly inactivated, with a t1/2 of 1.4 min in the presence of 250 µM MC, with a 10 µM IC50.” auto_single_measurement only accepted activity measurement [1] 1 structures\9CTL\9CTL_metadata.json point structures/9CTL/9ctl_protein.pdb structures/9CTL/9ctl_pocket.pdb structures/9CTL/9ctl_ligand.sdf structures/9CTL/9ctl_ligand.pdb structures/9CTL/9ctl_ligand.cif structures/9CTL/9ctl_complex.pdb structures/9CTL/9ctl_complex.cif 9CUN extended Ami1 Mycobacterium tuberculosis Ami1 residues 25-241; expressed as a SUMO fusion and cleaved Na compound 5 (tetrazole compound) "[""A1A0I""]" 1 Kd Kd = = 39 ± 6.1 μM 39000.0 [] unit_conversion 4.4089353929735005 success True direct_binding Differential scanning fluorimetry dose-response assay; Ami1 thermal-shift curves were measured across compound 5 concentrations, in triplicate. 4 “The calculated dissociation constant (Kd) for compound 1 was 6.69 ± 0.79 μM, and for compound 5, it was 39 ± 6.1 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9CUN\9CUN_metadata.json point structures/9CUN/9cun_protein.pdb structures/9CUN/9cun_pocket.pdb structures/9CUN/9cun_ligand.pdb structures/9CUN/9cun_ligand.cif structures/9CUN/9cun_complex.pdb structures/9CUN/9cun_complex.cif 9CY8 extended EphA4 Na EphA4-LBD Na compound 22 "[""CHAIN:B""]" 1 Kd Kd = = 137 ± 2 nM 137.0 [] unit_conversion 6.863279432843593 success True direct_binding Isothermal titration calorimetry measurement of compound 22 binding to EphA4-LBD. 4 Table 3 reports compound 22 (151G10) with Kd 137 ± 2 nM; the paper states dissociation constants were obtained by isothermal titration calorimetry. PDB 9CY8 is identified as the EphA4-LBD–compound 22 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9CY8\9CY8_metadata.json point structures/9CY8/9cy8_protein.pdb structures/9CY8/9cy8_pocket.pdb structures/9CY8/9cy8_ligand.pdb structures/9CY8/9cy8_ligand.cif structures/9CY8/9cy8_complex.pdb structures/9CY8/9cy8_complex.cif 9D0P extended PLK1 Na Na Na AZD1775 "[""8X7""]" 1 IC50 IC50 = = 76 nM 76.0 [] unit_conversion 7.119186407719209 success True biochemical_inhibition PLK1 ADP-Glo biochemical assay. 12 Table 4 reports “PLK1 ADP-Glo IC50 [nM]” of 76 for AZD1775; page 14 maps PDB 9D0P to PLK1 with AZD1775 bound. auto_single_measurement only accepted activity measurement [1] 1 structures\9D0P\9D0P_metadata.json point structures/9D0P/9d0p_protein.pdb structures/9D0P/9d0p_pocket.pdb structures/9D0P/9d0p_ligand.pdb structures/9D0P/9d0p_ligand.cif structures/9D0P/9d0p_complex.pdb structures/9D0P/9d0p_complex.cif 9D0Q extended Wee1 kinase human Na Na compound 11 "[""A1A1S""]" 1 IC50 IC50 = = 22 nM 22.0 [] unit_conversion 7.657577319177793 success True biochemical_inhibition Wee1 ADP-Glo biochemical assay using Wee1 kinase domain. 8 Table 2 reports “Wee1 ADP-Glo IC50 [nM]” of 22 for compound 11; page 11 maps PDB 9D0Q to compound 11. auto_single_measurement only accepted activity measurement [1] 1 structures\9D0Q\9D0Q_metadata.json point structures/9D0Q/9d0q_protein.pdb structures/9D0Q/9d0q_pocket.pdb structures/9D0Q/9d0q_ligand.pdb structures/9D0Q/9d0q_ligand.cif structures/9D0Q/9d0q_complex.pdb structures/9D0Q/9d0q_complex.cif 9D0R extended Wee1 kinase human Na Na compound 10 "[""A1A1T""]" 1 IC50 IC50 = = 0.7 nM 0.7 [] unit_conversion 9.154901959985743 success True biochemical_inhibition Wee1 ADP-Glo biochemical assay using Wee1 kinase domain. 7 Table 1 reports “Wee1 ADP-Glo IC50 [nM]” of 0.7 for compound 10; page 11 maps PDB 9D0R to compound 10. auto_single_measurement only accepted activity measurement [1] 1 structures\9D0R\9D0R_metadata.json point structures/9D0R/9d0r_protein.pdb structures/9D0R/9d0r_pocket.pdb structures/9D0R/9d0r_ligand.pdb structures/9D0R/9d0r_ligand.cif structures/9D0R/9d0r_complex.pdb structures/9D0R/9d0r_complex.cif 9D0S extended Wee1 kinase human Na Na compound 14 "[""A1A1R""]" 1 IC50 IC50 = = 1.0 nM 1.0 [] unit_conversion 9.0 success True biochemical_inhibition Wee1 ADP-Glo biochemical assay using Wee1 kinase domain. 9 Table 3 reports “Wee1 ADP-Glo IC50 [nM]” of 1.0 for compound 14; page 11 maps PDB 9D0S to compound 14. auto_single_measurement only accepted activity measurement [1] 1 structures\9D0S\9D0S_metadata.json point structures/9D0S/9d0s_protein.pdb structures/9D0S/9d0s_pocket.pdb structures/9D0S/9d0s_ligand.pdb structures/9D0S/9d0s_ligand.cif structures/9D0S/9d0s_complex.pdb structures/9D0S/9d0s_complex.cif 9D11 classic SMARCA2 Na Na Na compound 22 (SMI-1074) "[""A1A1O""]" 1 IC50 IC50 = = 66 nM 66.0 [] unit_conversion 7.180456064458131 success True direct_binding TR-FRET binding assay using recombinant human SMARCA2/4 bromodomain proteins 5 Table 2 reports compound 22 (SMI-1074) with SMARCA2 IC50 = 66 nM; its footnote states binding affinities were determined by TR-FRET using recombinant human SMARCA2/4 bromodomain proteins. Figure 4B identifies PDB 9D11 as the cocrystal structure of ligand 22 with SMARCA2. auto_single_measurement only accepted activity measurement [1] 1 structures\9D11\9D11_metadata.json point structures/9D11/9d11_protein.pdb structures/9D11/9d11_pocket.pdb structures/9D11/9d11_ligand.sdf structures/9D11/9d11_ligand.pdb structures/9D11/9d11_ligand.cif structures/9D11/9d11_complex.pdb structures/9D11/9d11_complex.cif 9D12 classic SMARCA2 Na Na Na compound 15 (SMI-6080) "[""A1A1P""]" 1 IC50 IC50 = = 43 nM 43.0 [] unit_conversion 7.366531544420414 success True direct_binding TR-FRET binding assay using recombinant human SMARCA2/4 bromodomain proteins 4 Table 1 reports compound 15 (SMI-6080) with SMARCA2 IC50 = 43 nM; its footnote states binding affinities were determined by TR-FRET using recombinant human SMARCA2/4 bromodomain proteins. Figure 4A identifies PDB 9D12 as the cocrystal structure of ligand 15 with SMARCA2. auto_single_measurement only accepted activity measurement [1] 1 structures\9D12\9D12_metadata.json point structures/9D12/9d12_protein.pdb structures/9D12/9d12_pocket.pdb structures/9D12/9d12_ligand.sdf structures/9D12/9d12_ligand.pdb structures/9D12/9d12_ligand.cif structures/9D12/9d12_complex.pdb structures/9D12/9d12_complex.cif 9D2U classic KPC-2 Na Na Na compound 14 "[""A1A18""]" 1 IC50 IC50 = = 1.6 ± 0.24 µM 1600.0 [] unit_conversion 5.795880017344075 success True biochemical_inhibition Purified-enzyme inhibition; Table 1. 2 Table 1 reports KPC-2 IC50 = 1.6 ± 0.24 µM for compound 14. auto_single_measurement only accepted activity measurement [1] 1 structures\9D2U\9D2U_metadata.json point structures/9D2U/9d2u_protein.pdb structures/9D2U/9d2u_pocket.pdb structures/9D2U/9d2u_ligand.sdf structures/9D2U/9d2u_ligand.pdb structures/9D2U/9d2u_ligand.cif structures/9D2U/9d2u_complex.pdb structures/9D2U/9d2u_complex.cif 9D40 classic human MASP-2 human catalytic region Na Analog 20; compound 20 "[""A1A1Z""]" 1 IC50 IC50 = = 0.0035 µM 3.5 [] unit_conversion 8.455931955649724 success True biochemical_inhibition Purified human MASP-2 inhibition assay; Table 1 reports inhibitor activity. The methods identify human MASP-2 protein comprising CCP1, CCP2, and serine-protease domains and a Z-Lys-SBzl/DTNB enzymatic assay. 4 Table 1, “MASP-2 Inhibitors derived from compound 2,” reports compound 20 MASP-2 IC50 = 0.0035 µM. Figure 4A identifies the human MASP-2 co-crystal of compound 20 as PDB ID 9D40. auto_single_measurement only accepted activity measurement [1] 1 structures\9D40\9D40_metadata.json point structures/9D40/9d40_protein.pdb structures/9D40/9d40_pocket.pdb structures/9D40/9d40_ligand.sdf structures/9D40/9d40_ligand.pdb structures/9D40/9d40_ligand.cif structures/9D40/9d40_complex.pdb structures/9D40/9d40_complex.cif 9D4V classic PAK1 Na Na Na compound 7 "[""A1A2P""]" 1 Ki Ki = = 31.1 nM 31.1 [] unit_conversion 7.507239610973162 success True biochemical_inhibition PAK1 Ki; mean of a minimum of two determinations performed in duplicate. 5 Table 1 reports compound 7 PAK1 Ki = 31.1 nM; Table 7 maps PAK1/compound 7 to PDB 9D4V. auto_single_measurement only accepted activity measurement [1] 1 structures\9D4V\9D4V_metadata.json point structures/9D4V/9d4v_protein.pdb structures/9D4V/9d4v_pocket.pdb structures/9D4V/9d4v_ligand.sdf structures/9D4V/9d4v_ligand.pdb structures/9D4V/9d4v_ligand.cif structures/9D4V/9d4v_complex.pdb structures/9D4V/9d4v_complex.cif 9D4W classic PAK1 Na Na Na compound 12 "[""A1A2Q""]" 1 Ki Ki = = 17.2 nM 17.2 [] unit_conversion 7.764471553092451 success True biochemical_inhibition PAK1 Ki; mean of a minimum of two determinations performed in duplicate. 5 Table 1 reports compound 12 PAK1 Ki = 17.2 nM; Table 7 maps PAK1/compound 12 to PDB 9D4W. auto_single_measurement only accepted activity measurement [1] 1 structures\9D4W\9D4W_metadata.json point structures/9D4W/9d4w_protein.pdb structures/9D4W/9d4w_pocket.pdb structures/9D4W/9d4w_ligand.sdf structures/9D4W/9d4w_ligand.pdb structures/9D4W/9d4w_ligand.cif structures/9D4W/9d4w_complex.pdb structures/9D4W/9d4w_complex.cif 9D4X classic PAK1 Na Na Na compound 16 "[""A1A2S""]" 1 Ki Ki = = 8.9 nM 8.9 [] unit_conversion 8.050609993355087 success True biochemical_inhibition PAK1 Ki; mean of a minimum of two determinations performed in duplicate. 6 Table 2 reports compound 16 PAK1 Ki = 8.9 nM; Table 7 maps PAK1/compound 16 to PDB 9D4X. auto_single_measurement only accepted activity measurement [1] 1 structures\9D4X\9D4X_metadata.json point structures/9D4X/9d4x_protein.pdb structures/9D4X/9d4x_pocket.pdb structures/9D4X/9d4x_ligand.sdf structures/9D4X/9d4x_ligand.pdb structures/9D4X/9d4x_ligand.cif structures/9D4X/9d4x_complex.pdb structures/9D4X/9d4x_complex.cif 9D4Y classic PAK1 Na Na Na compound 31 "[""A1A2S""]" 1 Ki Ki = = 40.7 nM 40.7 [] unit_conversion 7.39040559077478 success True biochemical_inhibition PAK1 Ki reported in Table 4. 11 Table 4 reports compound 31 PAK1 Ki = 40.7 nM; Table 7 maps PAK1/compound 31 to PDB 9D4Y. auto_single_measurement only accepted activity measurement [1] 1 structures\9D4Y\9D4Y_metadata.json point structures/9D4Y/9d4y_protein.pdb structures/9D4Y/9d4y_pocket.pdb structures/9D4Y/9d4y_ligand.sdf structures/9D4Y/9d4y_ligand.pdb structures/9D4Y/9d4y_ligand.cif structures/9D4Y/9d4y_complex.pdb structures/9D4Y/9d4y_complex.cif 9D50 classic PAK1 Na Na Na compound 24 "[""A1A2T""]" 1 Ki Ki = = 67.7 nM 67.7 [] unit_conversion 7.169411331314856 success True biochemical_inhibition PAK1 Ki reported in Table 4. 11 Table 4 reports compound 24 PAK1 Ki = 67.7 nM; Table 7 maps PAK1/compound 24 to PDB 9D50. auto_single_measurement only accepted activity measurement [1] 1 structures\9D50\9D50_metadata.json point structures/9D50/9d50_protein.pdb structures/9D50/9d50_pocket.pdb structures/9D50/9d50_ligand.sdf structures/9D50/9d50_ligand.pdb structures/9D50/9d50_ligand.cif structures/9D50/9d50_complex.pdb structures/9D50/9d50_complex.cif 9D51 classic PAK2 Na Na Na compound 12 "[""A1A2Q""]" 1 Ki Ki = = 30.4 nM 30.4 [] unit_conversion 7.517126416391246 success True biochemical_inhibition PAK2 Ki; mean of a minimum of two determinations performed in duplicate. 5 Table 1 reports compound 12 PAK2 Ki = 30.4 nM; Table 7 maps PAK2/compound 12 to PDB 9D51. auto_single_measurement only accepted activity measurement [1] 1 structures\9D51\9D51_metadata.json point structures/9D51/9d51_protein.pdb structures/9D51/9d51_pocket.pdb structures/9D51/9d51_ligand.sdf structures/9D51/9d51_ligand.pdb structures/9D51/9d51_ligand.cif structures/9D51/9d51_complex.pdb structures/9D51/9d51_complex.cif 9D52 classic PAK4 Na Na Na compound 18 "[""A1A2R""]" 1 Ki Ki = = 50.37 nM 50.37 [] unit_conversion 7.297828049142289 success True biochemical_inhibition PAK4 Ki stated in the discussion for compound 18. 7 The text states: “18 PAK1 Ki = 216.3 nM, PAK4 Ki = 50.37 nM”; Table 7 maps PAK4/compound 18 to PDB 9D52. auto_single_measurement only accepted activity measurement [1] 1 structures\9D52\9D52_metadata.json point structures/9D52/9d52_protein.pdb structures/9D52/9d52_pocket.pdb structures/9D52/9d52_ligand.sdf structures/9D52/9d52_ligand.pdb structures/9D52/9d52_ligand.cif structures/9D52/9d52_complex.pdb structures/9D52/9d52_complex.cif 9D54 classic KPC-2 Na Na Na compound 12 "[""A1A22""]" 1 IC50 IC50 = = 0.24 ± 0.016 µM 240.0 [] unit_conversion 6.619788758288394 success True biochemical_inhibition Purified-enzyme inhibition; Table 1. 2 Table 1 reports KPC-2 IC50 = 0.24 ± 0.016 µM for compound 12. auto_single_measurement only accepted activity measurement [1] 1 structures\9D54\9D54_metadata.json point structures/9D54/9d54_protein.pdb structures/9D54/9d54_pocket.pdb structures/9D54/9d54_ligand.sdf structures/9D54/9d54_ligand.pdb structures/9D54/9d54_ligand.cif structures/9D54/9d54_complex.pdb structures/9D54/9d54_complex.cif 9D5O extended BRD2 human (Homo sapiens) Na wild-type 3IND "[""A1A12""]" 1 Kd Kd = = 2300±67 nM 2300.0 [] unit_conversion 5.638272163982407 success True direct_binding SPR binding measurement in Table 1; the table labels the compound as 6g (IND3). 3 Table 1 reports 6g (IND3; 3IND) K_D = 2300±67 nM for BRD2-BD2, determined by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\9D5O\9D5O_metadata.json point structures/9D5O/9d5o_protein.pdb structures/9D5O/9d5o_pocket.pdb structures/9D5O/9d5o_ligand.pdb structures/9D5O/9d5o_ligand.cif structures/9D5O/9d5o_complex.pdb structures/9D5O/9d5o_complex.cif 9D5Q classic KPC-2 Na Na Na compound 21 "[""A1A13""]" 1 IC50 IC50 = = 1.96 ± 0.32 µM 1960.0 [] unit_conversion 5.707743928643524 success True biochemical_inhibition Purified-enzyme inhibition; Table 2. 4 Table 2 reports KPC-2 IC50 = 1.96 ± 0.32 µM for compound 21. auto_single_measurement only accepted activity measurement [1] 1 structures\9D5Q\9D5Q_metadata.json point structures/9D5Q/9d5q_protein.pdb structures/9D5Q/9d5q_pocket.pdb structures/9D5Q/9d5q_ligand.sdf structures/9D5Q/9d5q_ligand.pdb structures/9D5Q/9d5q_ligand.cif structures/9D5Q/9d5q_complex.pdb structures/9D5Q/9d5q_complex.cif 9D5R classic KPC-2 Na Na Na compound 22 "[""A1A14""]" 1 IC50 IC50 = = 0.18 ± 0.02 µM 180.0 [] unit_conversion 6.7447274948966935 success True biochemical_inhibition Purified-enzyme inhibition; Table 2. 4 Table 2 reports KPC-2 IC50 = 0.18 ± 0.02 µM for compound 22. auto_single_measurement only accepted activity measurement [1] 1 structures\9D5R\9D5R_metadata.json point structures/9D5R/9d5r_protein.pdb structures/9D5R/9d5r_pocket.pdb structures/9D5R/9d5r_ligand.sdf structures/9D5R/9d5r_ligand.pdb structures/9D5R/9d5r_ligand.cif structures/9D5R/9d5r_complex.pdb structures/9D5R/9d5r_complex.cif 9D6B classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-607 "[""A1A17""]" 1 IC50 IC50 = = 5.1 µM 5100.0 [] unit_conversion 5.292429823902063 success True direct_binding Confirmatory dose-response HTRF peptide-displacement binding assay. 14 Figure 9 lists AVI-607, PDB 9D6B, with IC50 5.1 µM; its caption identifies the confirmatory HTRF dose-response screen. auto_single_measurement only accepted activity measurement [1] 1 structures\9D6B\9D6B_metadata.json point structures/9D6B/9d6b_protein.pdb structures/9D6B/9d6b_pocket.pdb structures/9D6B/9d6b_ligand.sdf structures/9D6B/9d6b_ligand.pdb structures/9D6B/9d6b_ligand.cif structures/9D6B/9d6b_complex.pdb structures/9D6B/9d6b_complex.cif 9D6G classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-3716 "[""A1A2F""]" 1 IC50 IC50 = = 4.7 µM 4700.0 [] unit_conversion 5.327902142064282 success True direct_binding Confirmatory dose-response HTRF peptide-displacement binding assay. 14 Figure 9 lists AVI-3716, PDB 9D6G, with IC50 4.7 µM; its caption identifies the confirmatory HTRF dose-response screen. auto_single_measurement only accepted activity measurement [1] 1 structures\9D6G\9D6G_metadata.json point structures/9D6G/9d6g_protein.pdb structures/9D6G/9d6g_pocket.pdb structures/9D6G/9d6g_ligand.sdf structures/9D6G/9d6g_ligand.pdb structures/9D6G/9d6g_ligand.cif structures/9D6G/9d6g_complex.pdb structures/9D6G/9d6g_complex.cif 9D6H classic SARS-CoV-2 NSP3 macrodomain SARS-CoV-2 Na Na AVI-1504 "[""A1AJW""]" 1 IC50 IC50 = = 9.8 µM 9800.0 [] unit_conversion 5.008773924307505 success True direct_binding Confirmatory dose-response HTRF peptide-displacement binding assay. 11 Figure 7 lists AVI-1504, PDB 9D6H, with IC50 9.8 µM; its caption identifies the confirmatory HTRF dose-response screen. auto_single_measurement only accepted activity measurement [1] 1 structures\9D6H\9D6H_metadata.json point structures/9D6H/9d6h_protein.pdb structures/9D6H/9d6h_pocket.pdb structures/9D6H/9d6h_ligand.sdf structures/9D6H/9d6h_ligand.pdb structures/9D6H/9d6h_ligand.cif structures/9D6H/9d6h_complex.pdb structures/9D6H/9d6h_complex.cif 9D75 extended p38alpha MAP kinase human Na Na compound 95 (OSF346) "[""A1A2L""]" 1 IC50 IC50 = = 0.191 ± 0.021 μM 191.0 [] unit_conversion 6.718966632752272 success True biochemical_inhibition ADP-Glo assay using recombinant human p38α MAPK. 5 Table 1 reports compound 95 p38α MAPK IC50 = 0.191 ± 0.021 μM; the text identifies the human p38α MAPK crystal structure of compound 95 as PDB 9D75. auto_single_measurement only accepted activity measurement [1] 1 structures\9D75\9D75_metadata.json point structures/9D75/9d75_protein.pdb structures/9D75/9d75_pocket.pdb structures/9D75/9d75_ligand.pdb structures/9D75/9d75_ligand.cif structures/9D75/9d75_complex.pdb structures/9D75/9d75_complex.cif 9D7N extended p38alpha MAP kinase human Na Na compound 94 (OSF267) "[""A1A2O""]" 1 IC50 IC50 = = 0.371 ± 0.123 μM 371.0 [] unit_conversion 6.430626090384954 success True biochemical_inhibition ADP-Glo assay using recombinant human p38α MAPK. 5 Table 1 reports compound 94 p38α MAPK IC50 = 0.371 ± 0.123 μM; the text identifies the human p38α MAPK crystal structure of compound 94 as PDB 9D7N. auto_single_measurement only accepted activity measurement [1] 1 structures\9D7N\9D7N_metadata.json point structures/9D7N/9d7n_protein.pdb structures/9D7N/9d7n_pocket.pdb structures/9D7N/9d7n_ligand.pdb structures/9D7N/9d7n_ligand.cif structures/9D7N/9d7n_complex.pdb structures/9D7N/9d7n_complex.cif 9D8E classic ACVR1 (ALK2) Na Na Na CDD-2789 "[""A1A29""]" 1 Kd Kd = = 2.1 nM 2.1 [] unit_conversion 8.67778070526608 success True direct_binding LantaScreen kinase binding assay / SelectScreen profiling; ALK2 inhibitor binding. 5 Fig. 2 visibly labels CDD-2789 with Kd = 2.1 nM; the caption states these are Kd values, and the text identifies the assay as a LantaScreen kinase binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9D8E\9D8E_metadata.json point structures/9D8E/9d8e_protein.pdb structures/9D8E/9d8e_pocket.pdb structures/9D8E/9d8e_ligand.sdf structures/9D8E/9d8e_ligand.pdb structures/9D8E/9d8e_ligand.cif structures/9D8E/9d8e_complex.pdb structures/9D8E/9d8e_complex.cif 9D8F classic ACVR1 (ALK2) Na Na Na CDD-2281 "[""A1A3C""]" 1 Kd Kd = = 1.3 nM 1.3 [] unit_conversion 8.886056647693163 success True direct_binding LantaScreen kinase binding assay / SelectScreen profiling; ALK2 inhibitor binding. 5 Fig. 2 visibly labels CDD-2281 with Kd = 1.3 nM; the caption states these are Kd values, and the text identifies the assay as a LantaScreen kinase binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9D8F\9D8F_metadata.json point structures/9D8F/9d8f_protein.pdb structures/9D8F/9d8f_pocket.pdb structures/9D8F/9d8f_ligand.sdf structures/9D8F/9d8f_ligand.pdb structures/9D8F/9d8f_ligand.cif structures/9D8F/9d8f_complex.pdb structures/9D8F/9d8f_complex.cif 9D8T classic KPC-2 Na Na Na compound 16 "[""A1A20""]" 1 IC50 IC50 = = 3.22 ± 0.23 µM 3220.0 [] unit_conversion 5.492144128304169 success True biochemical_inhibition Purified-enzyme inhibition; Table 2. 4 Table 2 reports KPC-2 IC50 = 3.22 ± 0.23 µM for compound 16. auto_single_measurement only accepted activity measurement [1] 1 structures\9D8T\9D8T_metadata.json point structures/9D8T/9d8t_protein.pdb structures/9D8T/9d8t_pocket.pdb structures/9D8T/9d8t_ligand.sdf structures/9D8T/9d8t_ligand.pdb structures/9D8T/9d8t_ligand.cif structures/9D8T/9d8t_complex.pdb structures/9D8T/9d8t_complex.cif 9D8Z classic ACVR1 (ALK2) Na Na Na CDD-2282 "[""A1A3D""]" 1 Kd Kd = = 1.4 nM 1.4 [] unit_conversion 8.853871964321762 success True direct_binding LantaScreen kinase binding assay / SelectScreen profiling; ALK2 inhibitor binding. 5 Fig. 2 visibly labels CDD-2282 with Kd = 1.4 nM; the caption states these are Kd values, and the text identifies the assay as a LantaScreen kinase binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9D8Z\9D8Z_metadata.json point structures/9D8Z/9d8z_protein.pdb structures/9D8Z/9d8z_pocket.pdb structures/9D8Z/9d8z_ligand.sdf structures/9D8Z/9d8z_ligand.pdb structures/9D8Z/9d8z_ligand.cif structures/9D8Z/9d8z_complex.pdb structures/9D8Z/9d8z_complex.cif 9D9N classic NDM-1 Na Na Na compound 5 "[""A1A25""]" 1 IC50 IC50 = = 5.95 ± 1.9 µM 5950.0 [] unit_conversion 5.22548303427145 success True biochemical_inhibition Purified NDM-1 biochemical inhibition assay. 2 Table 1 reports compound 5 NDM-1 IC50 5.95 ± 1.9 µM; the PDB title and primary-citation mapping identify 9D9N as NDM-1 with compound 5. auto_single_measurement only accepted activity measurement [1] 1 structures\9D9N\9D9N_metadata.json point structures/9D9N/9d9n_protein.pdb structures/9D9N/9d9n_pocket.pdb structures/9D9N/9d9n_ligand.sdf structures/9D9N/9d9n_ligand.pdb structures/9D9N/9d9n_ligand.cif structures/9D9N/9d9n_complex.pdb structures/9D9N/9d9n_complex.cif 9DA0 classic Human norovirus GII.4 Houston protease Human norovirus Na R112A rupintrivir "[""AG7""]" 1 Ki Ki = = 564 ± 513 µM 564000.0 [] unit_conversion 3.248720896016658 success True biochemical_inhibition Time-dependent covalent inhibition/FRET protease assay; Table 1 labels this strain GII.4 HOV. 5 Table 1 reports GII.4 HOV R112A Ki = 564 ± 513 µM for rupintrivir. auto_single_measurement only accepted activity measurement [1] 1 structures\9DA0\9DA0_metadata.json point structures/9DA0/9da0_protein.pdb structures/9DA0/9da0_pocket.pdb structures/9DA0/9da0_ligand.sdf structures/9DA0/9da0_ligand.pdb structures/9DA0/9da0_ligand.cif structures/9DA0/9da0_complex.pdb structures/9DA0/9da0_complex.cif 9DA1 classic human DNPH1 Homo sapiens truncated DNPH1, residues 20-161 Na inhibitor 1a "[""A1BBB""]" 2 Ki Ki = = 0.60 μM 600.0 [] unit_conversion 6.221848749616356 success True biochemical_inhibition Competitive inhibition of hmdUMP hydrolysis. 2 Figure 1 labels 1a “Ki = 0.60 μM”; text states DNPH1 inhibition by 1a is competitive with hmdUMP. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9DA1\9DA1_metadata.json point structures/9DA1/9da1_protein.pdb structures/9DA1/9da1_pocket.pdb structures/9DA1/9da1_ligand.sdf structures/9DA1/9da1_ligand.pdb structures/9DA1/9da1_ligand.cif structures/9DA1/9da1_complex.pdb structures/9DA1/9da1_complex.cif 9DA2 classic human DNPH1 Homo sapiens truncated DNPH1, residues 20-161 Na inhibitor 1b "[""A1BBC""]" 3 Kd Kd = = 0.43 μM 430.0 [] unit_conversion 6.366531544420413 success True direct_binding Isothermal calorimetry titration. 2 “Isothermal calorimetry titration results in a similar KD value of 0.43 μM for compound 1b.” auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\9DA2\9DA2_metadata.json point structures/9DA2/9da2_protein.pdb structures/9DA2/9da2_pocket.pdb structures/9DA2/9da2_ligand.sdf structures/9DA2/9da2_ligand.pdb structures/9DA2/9da2_ligand.cif structures/9DA2/9da2_complex.pdb structures/9DA2/9da2_complex.cif 9DA3 classic human DNPH1 Homo sapiens truncated DNPH1, residues 20-161 Na inhibitor 2a "[""A1BBD""]" 1 Ki Ki = = 0.61 μM 610.0 [] unit_conversion 6.214670164989233 success True biochemical_inhibition Competitive inhibition of hmdUMP hydrolysis. 4 “Compound 2a with a Ki value of 0.61 μM …”; Figure 2 caption identifies competitive inhibition by TS1 mimic 2a. auto_single_measurement only accepted activity measurement [1] 1 structures\9DA3\9DA3_metadata.json point structures/9DA3/9da3_protein.pdb structures/9DA3/9da3_pocket.pdb structures/9DA3/9da3_ligand.sdf structures/9DA3/9da3_ligand.pdb structures/9DA3/9da3_ligand.cif structures/9DA3/9da3_complex.pdb structures/9DA3/9da3_complex.cif 9DA4 extended human DNPH1 Homo sapiens truncated DNPH1, residues 20-161 Na inhibitor 2b "[""A1BBE""]" 1 Ki Ki = = 2.85 μM 2850.0 [] unit_conversion 5.54515513999149 success True biochemical_inhibition Competitive inhibition of hmdUMP hydrolysis. 4 Figure 2A labels compound 2b “Ki = 2.85 μM”; the text states 2b binds with a Ki of 2.9 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9DA4\9DA4_metadata.json point structures/9DA4/9da4_protein.pdb structures/9DA4/9da4_pocket.pdb structures/9DA4/9da4_ligand.pdb structures/9DA4/9da4_ligand.cif structures/9DA4/9da4_complex.pdb structures/9DA4/9da4_complex.cif 9DA5 classic human DNPH1 Homo sapiens truncated DNPH1, residues 20-161 Na inhibitor 2c "[""A1BBF""]" 1 Ki Ki = = 3.67 μM 3670.0 [] unit_conversion 5.435333935747911 success True biochemical_inhibition Inhibition of hmdUMP hydrolysis. 3 Figure 2A labels compound 2c “Ki = 3.67 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9DA5\9DA5_metadata.json point structures/9DA5/9da5_protein.pdb structures/9DA5/9da5_pocket.pdb structures/9DA5/9da5_ligand.sdf structures/9DA5/9da5_ligand.pdb structures/9DA5/9da5_ligand.cif structures/9DA5/9da5_complex.pdb structures/9DA5/9da5_complex.cif 9DA6 classic human DNPH1 Homo sapiens truncated DNPH1, residues 20-161 Na inhibitor 3a "[""NRI""]" 2 Kd Kd = = 1.3 μM 1300.0 [] unit_conversion 5.886056647693163 success True direct_binding Isothermal calorimetry titration. 5 “Isothermal calorimetry titration results in a KD value of 1.3 μM for compound 3a.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9DA6\9DA6_metadata.json point structures/9DA6/9da6_protein.pdb structures/9DA6/9da6_pocket.pdb structures/9DA6/9da6_ligand.sdf structures/9DA6/9da6_ligand.pdb structures/9DA6/9da6_ligand.cif structures/9DA6/9da6_complex.pdb structures/9DA6/9da6_complex.cif 9DAG classic NDM-1 Na Na Na compound 13 "[""A1A3B""]" 2 Kd Kd = = 3.40 ± 0.51 µM 3400.0 [] unit_conversion 5.468521082957745 success True direct_binding Isothermal titration calorimetry in solution. 5 The ITC analysis reports measured Kd = 3.40 ± 0.51 µM for compound 13 binding to NDM-1. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9DAG\9DAG_metadata.json point structures/9DAG/9dag_protein.pdb structures/9DAG/9dag_pocket.pdb structures/9DAG/9dag_ligand.sdf structures/9DAG/9dag_ligand.pdb structures/9DAG/9dag_ligand.cif structures/9DAG/9dag_complex.pdb structures/9DAG/9dag_complex.cif 9DAL classic Human norovirus GII.3 protease Human norovirus Na R112A rupintrivir "[""AG7""]" 1 Ki Ki = = 94 ± 38 µM 94000.0 [] unit_conversion 4.026872146400302 success True biochemical_inhibition Time-dependent covalent inhibition/FRET protease assay; Table 1. 5 Table 1 reports GII.3 R112A Ki = 94 ± 38 µM for rupintrivir. auto_single_measurement only accepted activity measurement [1] 1 structures\9DAL\9DAL_metadata.json point structures/9DAL/9dal_protein.pdb structures/9DAL/9dal_pocket.pdb structures/9DAL/9dal_ligand.sdf structures/9DAL/9dal_ligand.pdb structures/9DAL/9dal_ligand.cif structures/9DAL/9dal_complex.pdb structures/9DAL/9dal_complex.cif 9DAR classic Escherichia coli dihydrofolate reductase (DHFR) Escherichia coli Na Na cycloguanil (CYC) "[""1CY""]" 1 IC50 IC50 = = 23 ± 16 µM 23000.0 [] unit_conversion 4.638272163982407 success True biochemical_inhibition Apparent IC50 from in vitro inhibition of purified bacterial DHFR. 30 Table 2 reports CYC: EcDHFR IC50 = 23 ± 16 µM; the text identifies EcDHFR•CYC as the paired crystallographic complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9DAR\9DAR_metadata.json point structures/9DAR/9dar_protein.pdb structures/9DAR/9dar_pocket.pdb structures/9DAR/9dar_ligand.sdf structures/9DAR/9dar_ligand.pdb structures/9DAR/9dar_ligand.cif structures/9DAR/9dar_complex.pdb structures/9DAR/9dar_complex.cif 9DB7 classic NDM-1 Na Na Na compound 22 "[""A1A14""]" 1 IC50 IC50 = = 3.55 ± 0.42 µM 3550.0 [] unit_conversion 5.449771646944906 success True biochemical_inhibition Purified-enzyme inhibition; Table 2. 4 Table 2 reports NDM-1 IC50 = 3.55 ± 0.42 µM for compound 22. auto_single_measurement only accepted activity measurement [1] 1 structures\9DB7\9DB7_metadata.json point structures/9DB7/9db7_protein.pdb structures/9DB7/9db7_pocket.pdb structures/9DB7/9db7_ligand.sdf structures/9DB7/9db7_ligand.pdb structures/9DB7/9db7_ligand.cif structures/9DB7/9db7_complex.pdb structures/9DB7/9db7_complex.cif 9DCY extended AS1 Na Designed allosteric facilitated dissociation switch AS1 Na CS221B effector peptide "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd ~ ~ 10 pM 0.01 [] unit_conversion 11.0 success True direct_binding Fluorescence-polarization affinity measurement of host protein with TAMRA-labelled effector peptide; AS1 was identified as the tightest-binding design. 3 “AS1, the design with the tightest effector binding (Kd,HE ~10 pM).” auto_single_measurement only accepted activity measurement [1] 1 structures\9DCY\9DCY_metadata.json point structures/9DCY/9dcy_protein.pdb structures/9DCY/9dcy_pocket.pdb structures/9DCY/9dcy_ligand.pdb structures/9DCY/9dcy_ligand.cif structures/9DCY/9dcy_complex.pdb structures/9DCY/9dcy_complex.cif 9DDG classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 4 "[""A1A3O""]" 1 IC50 IC50 = = 840 nM 840.0 [] unit_conversion 6.075720713938118 success True biochemical_inhibition Enzyme IC50, Table 1. 3 Table 1 lists compound 4 with SARS-CoV-2 Mpro enzyme IC50 of 840 nM; page 13 maps PDB 9DDG to compound 4. auto_single_measurement only accepted activity measurement [1] 1 structures\9DDG\9DDG_metadata.json point structures/9DDG/9ddg_protein.pdb structures/9DDG/9ddg_pocket.pdb structures/9DDG/9ddg_ligand.sdf structures/9DDG/9ddg_ligand.pdb structures/9DDG/9ddg_ligand.cif structures/9DDG/9ddg_complex.pdb structures/9DDG/9ddg_complex.cif 9DEQ classic integrin alphaIIb beta3 human full-length integrin alphaIIb beta3 in native lipids Na m-tirofiban (S-m-tirofiban; modified tirofiban) "[""A1A5G""]" 2 Kd Kd = = 23.0 nM 23.0 [] unit_conversion 7.638272163982407 success True biochemical_inhibition Kd for inhibitor binding to ADP-activated platelet αIIbβ3, derived from ODEs fitted to Alexa647-fibrinogen displacement data. 2 The derived Kd values for ADP-activated platelet αIIbβ3 include 23.0 nM for m-tirofiban. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9DEQ\9DEQ_metadata.json point structures/9DEQ/9deq_protein.pdb structures/9DEQ/9deq_pocket.pdb structures/9DEQ/9deq_ligand.sdf structures/9DEQ/9deq_ligand.pdb structures/9DEQ/9deq_ligand.cif structures/9DEQ/9deq_complex.pdb structures/9DEQ/9deq_complex.cif 9DER classic integrin alphaIIb beta3 human full-length integrin alphaIIb beta3 in native lipids Na tirofiban "[""AGG""]" 2 Kd Kd = = 1.44 nM 1.44 [] unit_conversion 8.84163750790475 success True biochemical_inhibition Kd for inhibitor binding to ADP-activated platelet αIIbβ3, derived from ODEs fitted to Alexa647-fibrinogen displacement data. 2 The derived Kd values for ADP-activated platelet αIIbβ3 include 1.44 nM for tirofiban. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9DER\9DER_metadata.json point structures/9DER/9der_protein.pdb structures/9DER/9der_pocket.pdb structures/9DER/9der_ligand.sdf structures/9DER/9der_ligand.pdb structures/9DER/9der_ligand.cif structures/9DER/9der_complex.pdb structures/9DER/9der_complex.cif 9DEW classic NDM-1 Na Na Na compound 2 "[""A1A4D""]" 1 IC50 IC50 = = 11.8 ± 0.66 µM 11800.0 [] unit_conversion 4.928117992693875 success True biochemical_inhibition Purified-enzyme inhibition; Table 1. 2 Table 1 reports NDM-1 IC50 = 11.8 ± 0.66 µM for compound 2. auto_single_measurement only accepted activity measurement [1] 1 structures\9DEW\9DEW_metadata.json point structures/9DEW/9dew_protein.pdb structures/9DEW/9dew_pocket.pdb structures/9DEW/9dew_ligand.sdf structures/9DEW/9dew_ligand.pdb structures/9DEW/9dew_ligand.cif structures/9DEW/9dew_complex.pdb structures/9DEW/9dew_complex.cif 9DFW classic TvVip1 CTP-swap V2 (engineered viperin-like enzyme) Trichoderma virens Crystallographic model: chains A and B residues 18-311; chain C residues 18-300 TvVip1 CTP-swap V2, engineered beta-8 loop swap variant CTP "[""CTP""]" 2 Ki Ki = = 0.22 μM 220.0 [] unit_conversion 6.657577319177793 success True biochemical_inhibition Ki derived from IC50 and Km using the Cheng-Prusoff equation, assuming CTP and UTP are competitive inhibitors. 32 Table 3 reports Ki (CTP) = 0.22 μM for TvVip1 CTP-swap V2. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9DFW\9DFW_metadata.json point structures/9DFW/9dfw_protein.pdb structures/9DFW/9dfw_pocket.pdb structures/9DFW/9dfw_ligand.sdf structures/9DFW/9dfw_ligand.pdb structures/9DFW/9dfw_ligand.cif structures/9DFW/9dfw_complex.pdb structures/9DFW/9dfw_complex.cif 9DGW classic TvVip1 (viperin-like enzyme) Trichoderma virens Crystallographic model: chain A residues 17-295; chain B residues 17-298; chain C residues 18-297 Na CTP "[""CTP""]" 2 Ki Ki > > 360 μM 360000.0 [] unit_conversion 3.443697499232713 success True biochemical_inhibition Ki derived from IC50 and Km using the Cheng-Prusoff equation, assuming CTP and UTP are competitive inhibitors. 32 Table 3 reports Ki (CTP) >360 μM for TvVip1 Wt. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9DGW\9DGW_metadata.json point structures/9DGW/9dgw_protein.pdb structures/9DGW/9dgw_pocket.pdb structures/9DGW/9dgw_ligand.sdf structures/9DGW/9dgw_ligand.pdb structures/9DGW/9dgw_ligand.cif structures/9DGW/9dgw_complex.pdb structures/9DGW/9dgw_complex.cif 9DH0 classic human UDP-glucose dehydrogenase (hUGDH) human recombinant hUGDH with an N-terminal histidine tag Na UDP-4-keto-xylose (UX4O) "[""A1BCU""]" 1 Ki Ki = = 0.75 ± 0.06 μM 750.0 [] unit_conversion 6.1249387366083 success True biochemical_inhibition Global analysis of competitive inhibition of recombinant hUGDH by UX4O using UDP-glucose substrate-saturation curves; Table 3. 11 Table 3, “Global Analysis of Competitive Inhibition,” reports for hUGDH with UX4O: Ki = 0.75 ± 0.06 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9DH0\9DH0_metadata.json point structures/9DH0/9dh0_protein.pdb structures/9DH0/9dh0_pocket.pdb structures/9DH0/9dh0_ligand.sdf structures/9DH0/9dh0_ligand.pdb structures/9DH0/9dh0_ligand.cif structures/9DH0/9dh0_complex.pdb structures/9DH0/9dh0_complex.cif 9DHK extended RMI1-RMI2 Na Na Na RMI-L3 "[""CHAIN:C"", ""CHAIN:F"", ""CHAIN:I"", ""CHAIN:L""]" 1 Kd Kd = = 10 ± 5 nM 10.0 [] unit_conversion 8.0 success True direct_binding Surface plasmon resonance binding assay. 4 Figure 3D reports RMI-L3 K_D = 10 ± 5 nM; page 5 identifies RMI-L3 as PDB 9DHK. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9DHK\9DHK_metadata.json point structures/9DHK/9dhk_protein.pdb structures/9DHK/9dhk_pocket.pdb structures/9DHK/9dhk_ligand.pdb structures/9DHK/9dhk_ligand.cif structures/9DHK/9dhk_complex.pdb structures/9DHK/9dhk_complex.cif 9DI4 extended RMI1-RMI2 Na Na Na RMI-L4 "[""CHAIN:C""]" 1 Kd Kd = = 2.5 ± 1 nM 2.5 [] unit_conversion 8.602059991327963 success True direct_binding Surface plasmon resonance binding assay. 4 Figure 3D reports RMI-L4 K_D = 2.5 ± 1 nM; page 5 identifies RMI-L4 as PDB 9DI4. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9DI4\9DI4_metadata.json point structures/9DI4/9di4_protein.pdb structures/9DI4/9di4_pocket.pdb structures/9DI4/9di4_ligand.pdb structures/9DI4/9di4_ligand.cif structures/9DI4/9di4_complex.pdb structures/9DI4/9di4_complex.cif 9DI9 classic branched-chain ketoacid dehydrogenase kinase (BDK) rat Na Na compound 6 (PF-07328948) "[""A1A40""]" 2 Kd Kd = = 4.8 ± 1.6 nM 4.8 [] unit_conversion 8.318758762624412 success True direct_binding Surface plasmon resonance assay with affixed BDK. 5 “The K_D was determined to be 4.8 ± 1.6 nM.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9DI9\9DI9_metadata.json point structures/9DI9/9di9_protein.pdb structures/9DI9/9di9_pocket.pdb structures/9DI9/9di9_ligand.sdf structures/9DI9/9di9_ligand.pdb structures/9DI9/9di9_ligand.cif structures/9DI9/9di9_complex.pdb structures/9DI9/9di9_complex.cif 9DIN extended ClpC1 N-terminal domain Na ClpC1-NTD residues 1-145 plus a C-terminal His tag Na compound 11; syn. Ruf-But4-Cl "[""CHAIN:C""]" 1 Kd Kd = = 0.027 µM 27.0 [] unit_conversion 7.568636235841012 success True direct_binding Surface plasmon resonance (SPR), ClpC1-NTD binding. 5 Table 2 reports compound 11: K_D NTD = 0.027 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9DIN\9DIN_metadata.json point structures/9DIN/9din_protein.pdb structures/9DIN/9din_pocket.pdb structures/9DIN/9din_ligand.pdb structures/9DIN/9din_ligand.cif structures/9DIN/9din_complex.pdb structures/9DIN/9din_complex.cif 9DL1 extended Target-specific TRACeR-I bound to HLA-A*02:01 Na Domain-swapped dimeric TRACeR-I (MAM-TRACeR) complexed with HLA-A*02:01/NY-ESO-1 pMHC-I Na NY-ESO-1 peptide SLLMWITQV "[""CHAIN:E"", ""CHAIN:H""]" 1 Kd Kd = = 22 nM 22.0 [] unit_conversion 7.657577319177793 success True direct_binding Bio-layer interferometry (BLI) binding kinetics of TRACeR (A*02:01 NY-ESO-1) to monomeric pMHC target. 3 Fig. 1f labels the TRACeR (A02 NY-ESO-1) BLI sensorgram with “K_D = 22 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9DL1\9DL1_metadata.json point structures/9DL1/9dl1_protein.pdb structures/9DL1/9dl1_pocket.pdb structures/9DL1/9dl1_ligand.pdb structures/9DL1/9dl1_ligand.cif structures/9DL1/9dl1_complex.pdb structures/9DL1/9dl1_complex.cif 9DL2 classic proline utilization A (PutA) Sinorhizobium meliloti Na Na compound 7; 2,3-dihydro-1,4-benzodioxine-5-carboxylic acid "[""53E""]" 1 Ki Ki = = 0.32 ± 0.02 mM 320000.0 [] unit_conversion 3.4948500216800937 success True biochemical_inhibition Competitive inhibition model with L-P5C/GSAL as variable substrate and NAD+ fixed at 0.2 mM. 10 Global competitive-inhibition fitting gave Ki = 0.32 mM ± 0.02 mM for compound 7. auto_single_measurement only accepted activity measurement [1] 1 structures\9DL2\9DL2_metadata.json point structures/9DL2/9dl2_protein.pdb structures/9DL2/9dl2_pocket.pdb structures/9DL2/9dl2_ligand.sdf structures/9DL2/9dl2_ligand.pdb structures/9DL2/9dl2_ligand.cif structures/9DL2/9dl2_complex.pdb structures/9DL2/9dl2_complex.cif 9DLW classic DCAF1 and WDR5 Na N-terminal His-tagged DCAF1(1077-1390); N-His-tagged WDR5(24-334) Na OICR-41114 "[""A1BAF""]" 1 Kd Kd = = 5 ± 0.4 nM 5.0 [] unit_conversion 8.301029995663981 success True direct_binding SPR assessment of ternary-complex formation: immobilized DCAF1, with WDR5 plus PROTAC 4. 6 Table 1 reports WDR5 + PROTAC 4 K_D = 5 ± 0.4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9DLW\9DLW_metadata.json point structures/9DLW/9dlw_protein.pdb structures/9DLW/9dlw_pocket.pdb structures/9DLW/9dlw_ligand.sdf structures/9DLW/9dlw_ligand.pdb structures/9DLW/9dlw_ligand.cif structures/9DLW/9dlw_complex.pdb structures/9DLW/9dlw_complex.cif 9DN3 classic Human inositol 1,3,4-trisphosphate 5/6-kinase (ITPK1) Human Residues 1-328 Na Compound 1 (9-cyclopentyladenine; 9-CPA; CAS # 715-91-3) "[""A1A7Y""]" 1 Kd Kd = = 52 ± 2 nM 52.0 [] unit_conversion 7.2839966563652006 success True direct_binding Isothermal titration calorimetry (ITC) direct binding 5 The text reports that ITC measured the compound 1–ITPK1 Kd as 52 ± 2 nM with 1:1 stoichiometry. auto_single_measurement only accepted activity measurement [1] 1 structures\9DN3\9DN3_metadata.json point structures/9DN3/9dn3_protein.pdb structures/9DN3/9dn3_pocket.pdb structures/9DN3/9dn3_ligand.sdf structures/9DN3/9dn3_ligand.pdb structures/9DN3/9dn3_ligand.cif structures/9DN3/9dn3_complex.pdb structures/9DN3/9dn3_complex.cif 9DNM classic beta-arrestin 1 rat beta-arrestin 1-BRIL, with BRIL inserted at the hinge region Na Cmpd-5 "[""ODN""]" 1 Kd Kd = = 362 ± 65 nM 362.0 [] unit_conversion 6.441291429466834 success True direct_binding ITC, one-site binding model; β-arrestin1 with Cmpd-5. 17 Fig. 1h reports ITC dissociation constants for all compounds with βarr1 or βarr2; the table lists Cmpd-5–βarr1 KD = 362 ± 65 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9DNM\9DNM_metadata.json point structures/9DNM/9dnm_protein.pdb structures/9DNM/9dnm_pocket.pdb structures/9DNM/9dnm_ligand.sdf structures/9DNM/9dnm_ligand.pdb structures/9DNM/9dnm_ligand.cif structures/9DNM/9dnm_complex.pdb structures/9DNM/9dnm_complex.cif 9DNV classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun13308 "[""A1BEH""]" 2 Ki Ki = = 19.3 ± 3.0 nM 19.3 [] unit_conversion 7.714442690992226 success True biochemical_inhibition FRET enzymatic assay 3 Fig. 2 reports Jun13308 Ki = 19.3 ± 3.0 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9DNV\9DNV_metadata.json point structures/9DNV/9dnv_protein.pdb structures/9DNV/9dnv_pocket.pdb structures/9DNV/9dnv_ligand.sdf structures/9DNV/9dnv_ligand.pdb structures/9DNV/9dnv_ligand.cif structures/9DNV/9dnv_complex.pdb structures/9DNV/9dnv_complex.cif 9DO1 classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun13307 (PDB component A1BF2) "[""A1BF2""]" 2 Ki Ki = = 25.4 ± 3.0 nM 25.4 [] unit_conversion 7.5951662833800615 success True biochemical_inhibition PLpro FRET enzymatic inhibition assay. 3 Figure 2 reports Jun13307 Ki 25.4 ± 3.0 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9DO1\9DO1_metadata.json point structures/9DO1/9do1_protein.pdb structures/9DO1/9do1_pocket.pdb structures/9DO1/9do1_ligand.sdf structures/9DO1/9do1_ligand.pdb structures/9DO1/9do1_ligand.cif structures/9DO1/9do1_complex.pdb structures/9DO1/9do1_complex.cif 9DO3 classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun13317 "[""A1BEF""]" 2 Ki Ki = = 47.4 ± 5.0 nM 47.4 [] unit_conversion 7.324221658325915 success True biochemical_inhibition FRET enzymatic assay 3 Fig. 2 reports Jun13317 Ki = 47.4 ± 5.0 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9DO3\9DO3_metadata.json point structures/9DO3/9do3_protein.pdb structures/9DO3/9do3_pocket.pdb structures/9DO3/9do3_ligand.sdf structures/9DO3/9do3_ligand.pdb structures/9DO3/9do3_ligand.cif structures/9DO3/9do3_complex.pdb structures/9DO3/9do3_complex.cif 9DO5 classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun12665 "[""A1BEE""]" 2 Ki Ki = = 32.1 ± 1.0 nM 32.1 [] unit_conversion 7.493494967595128 success True biochemical_inhibition FRET enzymatic assay 3 Fig. 2 reports Jun12665 Ki = 32.1 ± 1.0 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9DO5\9DO5_metadata.json point structures/9DO5/9do5_protein.pdb structures/9DO5/9do5_pocket.pdb structures/9DO5/9do5_ligand.sdf structures/9DO5/9do5_ligand.pdb structures/9DO5/9do5_ligand.cif structures/9DO5/9do5_complex.pdb structures/9DO5/9do5_complex.cif 9DOI classic SARS-CoV-2 papain-like protease (PLpro) SARS-CoV-2 Na Na Jun13306 (PDB component A1BEL) "[""A1BEL""]" 2 Ki Ki = = 25.8 ± 2.0 nM 25.8 [] unit_conversion 7.58838029403677 success True biochemical_inhibition PLpro FRET enzymatic inhibition assay. 3 Figure 2 reports Jun13306 Ki 25.8 ± 2.0 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9DOI\9DOI_metadata.json point structures/9DOI/9doi_protein.pdb structures/9DOI/9doi_pocket.pdb structures/9DOI/9doi_ligand.sdf structures/9DOI/9doi_ligand.pdb structures/9DOI/9doi_ligand.cif structures/9DOI/9doi_complex.pdb structures/9DOI/9doi_complex.cif 9DON classic eIF4E Na Na Na 5-PA (Compound 5-PA) "[""A1A8P""]" 1 IC50 IC50 = = 4.1 μM 4100.0 [] unit_conversion 5.3872161432802645 success True direct_binding Fluorescence-polarization competitive binding assay using fluorescently labeled m7GTP as a competitive probe; 5-PA was tested against eIF4E. 3 “In FP, 5-PA displayed single digit micromolar competitive binding activity with an IC50 value of 4.1 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9DON\9DON_metadata.json point structures/9DON/9don_protein.pdb structures/9DON/9don_pocket.pdb structures/9DON/9don_ligand.sdf structures/9DON/9don_ligand.pdb structures/9DON/9don_ligand.cif structures/9DON/9don_complex.pdb structures/9DON/9don_complex.cif 9DQA classic RPE65 bovine Na Na EYE-002; compound 6 "[""A1BEO""]" 1 IC50 IC50 = = 0.069 ± 0.015 µM 69.0 [] unit_conversion 7.161150909262744 success True biochemical_inhibition In vitro RPE65 inhibition using bovine RPE microsomes; Table 1 reports compound 6 potency. 3 Table 1 lists compound 6 with IC50 toward RPE65 of 0.069 ± 0.015 µM. The text states compounds 5–7 were tested using bovine RPE microsomes as the enzyme source. auto_single_measurement only accepted activity measurement [1] 1 structures\9DQA\9DQA_metadata.json point structures/9DQA/9dqa_protein.pdb structures/9DQA/9dqa_pocket.pdb structures/9DQA/9dqa_ligand.sdf structures/9DQA/9dqa_ligand.pdb structures/9DQA/9dqa_ligand.cif structures/9DQA/9dqa_complex.pdb structures/9DQA/9dqa_complex.cif 9DQD extended Cereblon/DDB1 human Na Na compound 6; (S)-enantiomer of Boc-deprotected 2d "[""A1BEP""]" 1 IC50 IC50 = = 0.03 μM 30.0 [] unit_conversion 7.522878745280337 success True direct_binding CRBN binding; the paper describes its library as evaluated in an established CRBN FRET-based binding/displacement assay. 3 “compound 6, the (S)-enantiomer of the Boc-deprotected 2d, which had both strong CRBN binding (IC50 = 0.03 μM)” auto_single_measurement only accepted activity measurement [1] 1 structures\9DQD\9DQD_metadata.json point structures/9DQD/9dqd_protein.pdb structures/9DQD/9dqd_pocket.pdb structures/9DQD/9dqd_ligand.pdb structures/9DQD/9dqd_ligand.cif structures/9DQD/9dqd_complex.pdb structures/9DQD/9dqd_complex.cif 9DRK classic Mycobacterium tuberculosis biotin protein ligase (MtBPL) Mycobacterium tuberculosis Na Na Bio-1 "[""A1BGE""]" 1 Kd Kd = = 0.023 µM 23.0 [] unit_conversion 7.638272163982407 success True direct_binding Isothermal titration calorimetry (ITC) direct binding; Table 1 reports MtBPL affinity. 7 Table 1 lists Bio-1 with K_D = 0.023 µM; the table footnote states ITC experiments used 20 µM MtBPL and 200 µM ligand. auto_single_measurement only accepted activity measurement [1] 1 structures\9DRK\9DRK_metadata.json point structures/9DRK/9drk_protein.pdb structures/9DRK/9drk_pocket.pdb structures/9DRK/9drk_ligand.sdf structures/9DRK/9drk_ligand.pdb structures/9DRK/9drk_ligand.cif structures/9DRK/9drk_complex.pdb structures/9DRK/9drk_complex.cif 9DRN classic Mycobacterium tuberculosis biotin protein ligase (MtBPL) Mycobacterium tuberculosis Na Na Bio-4 "[""A1BGF""]" 1 Kd Kd = = 0.062 µM 62.0 [] unit_conversion 7.207608310501746 success True direct_binding Isothermal titration calorimetry (ITC) direct binding; Table 1 reports MtBPL affinity. 7 Table 1 lists Bio-4 with K_D = 0.062 µM; the table footnote states ITC experiments used 20 µM MtBPL and 200 µM ligand. auto_single_measurement only accepted activity measurement [1] 1 structures\9DRN\9DRN_metadata.json point structures/9DRN/9drn_protein.pdb structures/9DRN/9drn_pocket.pdb structures/9DRN/9drn_ligand.sdf structures/9DRN/9drn_ligand.pdb structures/9DRN/9drn_ligand.cif structures/9DRN/9drn_complex.pdb structures/9DRN/9drn_complex.cif 9DTJ classic KPC-2 Na Na Na compound 13 "[""A1A3B""]" 1 IC50 IC50 = = 0.357 ± 0.075 µM 357.0 [] unit_conversion 6.447331783887806 success True biochemical_inhibition Purified-enzyme inhibition; Table 1. 2 Table 1 reports KPC-2 IC50 = 0.357 ± 0.075 µM for compound 13. auto_single_measurement only accepted activity measurement [1] 1 structures\9DTJ\9DTJ_metadata.json point structures/9DTJ/9dtj_protein.pdb structures/9DTJ/9dtj_pocket.pdb structures/9DTJ/9dtj_ligand.sdf structures/9DTJ/9dtj_ligand.pdb structures/9DTJ/9dtj_ligand.cif structures/9DTJ/9dtj_complex.pdb structures/9DTJ/9dtj_complex.cif 9DUJ extended RufO Na Untagged RufO after His6-tag cleavage by TEV protease Na Nle-RYLH "[""CHAIN:B""]" 1 Kd Kd = = 1.60 µM 1600.0 [] unit_conversion 5.795880017344075 success True direct_binding Isothermal titration calorimetry; endothermic binding of alternate peptide Nle-RYLH to RufO (supporting Figure S3D referenced). 4 “The endothermic binding was also observed for Nle-RYLH (Figure S3D), which showed a comparable binding affinity (KD = 1.60 μM) but a larger ΔH.” Page 12 maps 9DUJ to Nle-RYLH-bound RufO. auto_single_measurement only accepted activity measurement [1] 1 structures\9DUJ\9DUJ_metadata.json point structures/9DUJ/9duj_protein.pdb structures/9DUJ/9duj_pocket.pdb structures/9DUJ/9duj_ligand.pdb structures/9DUJ/9duj_ligand.cif structures/9DUJ/9duj_complex.pdb structures/9DUJ/9duj_complex.cif 9DYA extended CHIP-TPR Na CHIP-TPR (residues 21-154) Na EEVD peptide "[""CHAIN:B""]" 1 Kd Kd = = 5.2 µM 5200.0 [] unit_conversion 5.2839966563652006 success True direct_binding Biolayer interferometry of isolated CHIP TPR (residues 21–154) binding biotin-EEVD peptide. 12 “The binding affinity of the CHIP TPR decreased nearly 10-fold towards the phosphorylated EEVD tail of HSP70 (Kd = 0.6 vs. 5.2 µM pEEVD vs. EEVD, respectively).” auto_single_measurement only accepted activity measurement [1] 1 structures\9DYA\9DYA_metadata.json point structures/9DYA/9dya_protein.pdb structures/9DYA/9dya_pocket.pdb structures/9DYA/9dya_ligand.pdb structures/9DYA/9dya_ligand.cif structures/9DYA/9dya_complex.pdb structures/9DYA/9dya_complex.cif 9DYB extended CHIP-TPR Na CHIP-TPR (residues 21-154) Na pEEVD peptide (phosphorylated HSP70 tail) "[""CHAIN:B""]" 1 Kd Kd = = 0.6 µM 600.0 [] unit_conversion 6.221848749616356 success True direct_binding Biolayer interferometry of isolated CHIP TPR (residues 21–154) binding biotin-pEEVD peptide. 12 “The binding affinity of the CHIP TPR decreased nearly 10-fold towards the phosphorylated EEVD tail of HSP70 (Kd = 0.6 vs. 5.2 µM pEEVD vs. EEVD, respectively).” auto_single_measurement only accepted activity measurement [1] 1 structures\9DYB\9DYB_metadata.json point structures/9DYB/9dyb_protein.pdb structures/9DYB/9dyb_pocket.pdb structures/9DYB/9dyb_ligand.pdb structures/9DYB/9dyb_ligand.cif structures/9DYB/9dyb_complex.pdb structures/9DYB/9dyb_complex.cif 9E0Q classic Inducible lysine decarboxylase Ldc1 Hafnia alvei Na Na D-hydrazino-Lys analogue (D-hydrazone) "[""A1BD0""]" 1 Ki Ki = = 4.2 ± 1.0 μM 4200.0 [] unit_conversion 5.376750709602099 success True biochemical_inhibition Competitive inhibition versus L-Lys; inhibition kinetics with H. alvei Ldc1. 5 “With H. alvei LdcI, both α-hydrazino acid enantiomers demonstrated competitive inhibition vs L-Lys with Ki’s of 5.9 ± 1.4 and 4.2 ± 1.0 μM for the L- and D-enantiomers, respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\9E0Q\9E0Q_metadata.json point structures/9E0Q/9e0q_protein.pdb structures/9E0Q/9e0q_pocket.pdb structures/9E0Q/9e0q_ligand.sdf structures/9E0Q/9e0q_ligand.pdb structures/9E0Q/9e0q_ligand.cif structures/9E0Q/9e0q_complex.pdb structures/9E0Q/9e0q_complex.cif 9E3T classic Ricin toxin A subunit (RTA) Na Na Na RU-NT-165 "[""A1BH4""]" 1 Ki Ki = = 2 µM 2000.0 [] unit_conversion 5.698970004336019 success True direct_binding Fluorescence-anisotropy competitive binding assay measuring displacement of fluorescent P11 peptide from RTA; Ki calculated from IC50. 2 Table 1 reports RU-NT-165 Ki = 2 µM; footnote b states Ki values were measured by fluorescence anisotropy using RTA/P11 displacement. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\9E3T\9E3T_metadata.json point structures/9E3T/9e3t_protein.pdb structures/9E3T/9e3t_pocket.pdb structures/9E3T/9e3t_ligand.sdf structures/9E3T/9e3t_ligand.pdb structures/9E3T/9e3t_ligand.cif structures/9E3T/9e3t_complex.pdb structures/9E3T/9e3t_complex.cif 9E42 classic Ricin toxin A subunit (RTA) Na Na Na RU-NT-192 "[""A1BH2""]" 1 Ki Ki = = 1 µM 1000.0 [] unit_conversion 6.0 success True direct_binding Fluorescence-anisotropy competitive binding assay measuring displacement of fluorescent P11 peptide from RTA; Ki calculated from IC50. 2 Table 1 reports RU-NT-192 Ki = 1 µM; footnote b states Ki values were measured by fluorescence anisotropy using RTA/P11 displacement. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\9E42\9E42_metadata.json point structures/9E42/9e42_protein.pdb structures/9E42/9e42_pocket.pdb structures/9E42/9e42_ligand.sdf structures/9E42/9e42_ligand.pdb structures/9E42/9e42_ligand.cif structures/9E42/9e42_complex.pdb structures/9E42/9e42_complex.cif 9E4U classic CarI terminal amidation domain (TAD) Moorena producens 3L CarI TAD, residues 1888-2303 Na NADH "[""NAI""]" 1 Kd Kd = = 85 ± 7 µM 85000.0 [] unit_conversion 4.070581074285707 success True direct_binding Intrinsic tryptophan fluorescence quenching; CarI TAD binding curve, three replicates. 22 Figure 4 caption reports the binding curve for CarI TAD and NADH as 85 ± 7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9E4U\9E4U_metadata.json point structures/9E4U/9e4u_protein.pdb structures/9E4U/9e4u_pocket.pdb structures/9E4U/9e4u_ligand.sdf structures/9E4U/9e4u_ligand.pdb structures/9E4U/9e4u_ligand.cif structures/9E4U/9e4u_complex.pdb structures/9E4U/9e4u_complex.cif 9E4W classic Bacillus phage SPO1 anti-CBASS 4 (Acb4) Bacillus phage SPO1 Na Na 3'3'-cGAMP "[""4BW""]" 2 Kd Kd = = 157.2 nM 157.2 [] unit_conversion 6.803547458296611 success True direct_binding EMSA titration of recombinant Acb4 with 3'3'-cGAMP; fraction bound fit to a single-binding model. 44 Figure 3E reports K_D [nM] = 157.2 for 3'3'-cGAMP. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\9E4W\9E4W_metadata.json point structures/9E4W/9e4w_protein.pdb structures/9E4W/9e4w_pocket.pdb structures/9E4W/9e4w_ligand.sdf structures/9E4W/9e4w_ligand.pdb structures/9E4W/9e4w_ligand.cif structures/9E4W/9e4w_complex.pdb structures/9E4W/9e4w_complex.cif 9E5F classic KRAS Na Na G12D 3 "[""A1BEJ""]" 1 IC50 IC50 = = 671 nM 671.0 [] unit_conversion 6.1732774798310075 success True biochemical_inhibition In-house biochemical KRAS G12D exchange assay measuring exchange of a fluorescently labeled GDP analog for a nonhydrolyzable GTP analog in the presence of SOS1. 2 “a screen of rigid amines identified compound 3 ... as a promising hit with an exchange IC50 of 671 nM.” Figure 3 maps compound 3 bound to KRAS-G12D to PDB 9E5F. auto_single_measurement only accepted activity measurement [1] 1 structures\9E5F\9E5F_metadata.json point structures/9E5F/9e5f_protein.pdb structures/9E5F/9e5f_pocket.pdb structures/9E5F/9e5f_ligand.sdf structures/9E5F/9e5f_ligand.pdb structures/9E5F/9e5f_ligand.cif structures/9E5F/9e5f_complex.pdb structures/9E5F/9e5f_complex.cif 9E7A extended Pmt4 Saccharomyces cerevisiae Pmt4 MIR domain residues 330-521, expressed as an N-terminal 6xHis-SUMO fusion and cleaved Na Ccw5 peptide "[""CHAIN:D"", ""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 12 ± 0.9 μM 12000.0 [] unit_conversion 4.920818753952375 success True direct_binding Isothermal titration calorimetry of purified Pmt4 MIR domain with Ccw5 peptide. 6 Fig. 3g reports WT MIR-domain binding to Ccw5 peptide: Kd = 12 ± 0.9 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9E7A\9E7A_metadata.json point structures/9E7A/9e7a_protein.pdb structures/9E7A/9e7a_pocket.pdb structures/9E7A/9e7a_ligand.pdb structures/9E7A/9e7a_ligand.cif structures/9E7A/9e7a_complex.pdb structures/9E7A/9e7a_complex.cif 9E81 classic COP9 signalosome (CSN) Homo sapiens CSN5i-3-CSN Na CSN5i-3 "[""6LT""]" 1 Kd Kd = = 4.7 ± 0.2 μM 4700.0 [] unit_conversion 5.327902142064282 success True direct_binding Bio-layer interferometry measurement against free eight-subunit CSN. 4 Fig. 2d prints Kd = 4.7 ± 0.2 μM; the text identifies this as affinity towards free eight-subunit CSN. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9E81\9E81_metadata.json point structures/9E81/9e81_protein.pdb structures/9E81/9e81_pocket.pdb structures/9E81/9e81_ligand.sdf structures/9E81/9e81_ligand.pdb structures/9E81/9e81_ligand.cif structures/9E81/9e81_complex.pdb structures/9E81/9e81_complex.cif 9EBY extended RufO Na Untagged RufO after His6-tag cleavage by TEV protease Na MRYLH "[""CHAIN:B""]" 1 Kd Kd = = 0.78 ± 0.30 µM 780.0 [] unit_conversion 6.107905397309519 success True direct_binding Isothermal titration calorimetry of MRYLH peptide binding to RufO; single-binding-site fit at 20 °C. 3 Figure 2 reports “KD = 0.78 ± 0.30 μM” for titration of peptide MRYLH binding to RufO; page 12 maps 9EBY to MRYLH-bound RufO. auto_single_measurement only accepted activity measurement [1] 1 structures\9EBY\9EBY_metadata.json point structures/9EBY/9eby_protein.pdb structures/9EBY/9eby_pocket.pdb structures/9EBY/9eby_ligand.pdb structures/9EBY/9eby_ligand.cif structures/9EBY/9eby_complex.pdb structures/9EBY/9eby_complex.cif 9ECV extended Respiratory syncytial virus polymerase (RSV L+P complex) Respiratory syncytial virus (RSV) RSV L protein with an N-terminal Twin-Strep tag and RSV P protein residues 1-241 with a C-terminal 6xHis tag Na compound 16 "[""CHAIN:G""]" 1 Kd Kd = = 43 nM 43.0 [] unit_conversion 7.366531544420414 success True direct_binding Surface plasmon resonance (SPR) binding of compound 16 to RSV polymerase; 1:1 Langmuir model. 4 Figure 3a reports SPR association of RSV polymerase and compound 16, K_D = 43 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9ECV\9ECV_metadata.json point structures/9ECV/9ecv_protein.pdb structures/9ECV/9ecv_pocket.pdb structures/9ECV/9ecv_ligand.pdb structures/9ECV/9ecv_ligand.cif structures/9ECV/9ecv_complex.pdb structures/9ECV/9ecv_complex.cif 9ED2 extended Respiratory syncytial virus polymerase (RSV L+P complex) Respiratory syncytial virus (RSV) RSV L protein with an N-terminal Twin-Strep tag and RSV P protein residues 1-241 with a C-terminal 6xHis tag Na compound 21 "[""CHAIN:G""]" 1 IC50 IC50 = = 0.0034 µM 3.4 [] unit_conversion 8.468521082957745 success True biochemical_inhibition SPA primer-extension enzymatic assay. 6 Table 1 reports compound 21 SPA IC50 = 0.0034 µM; the table footnote defines this as biochemical activity in the SPA primer-extension enzymatic assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9ED2\9ED2_metadata.json point structures/9ED2/9ed2_protein.pdb structures/9ED2/9ed2_pocket.pdb structures/9ED2/9ed2_ligand.pdb structures/9ED2/9ed2_ligand.cif structures/9ED2/9ed2_complex.pdb structures/9ED2/9ed2_complex.cif 9EDV classic Yck2 Candida albicans Residues 37-345 with an N-terminal His6 tag and TEV protease site Na 1e (2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine-7-carbonitrile) "[""A1BIQ""]" 1 IC50 IC50 = = 0.10 µM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition Purified recombinant CaYck2 kinase-domain ADP-Glo assay with casein kinase I peptide substrate and ATP. 4 Table 1 reports CaYck2 IC50 = 0.10 µM for 1e; the methods describe the purified-kinase ADP-Glo inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9EDV\9EDV_metadata.json point structures/9EDV/9edv_protein.pdb structures/9EDV/9edv_pocket.pdb structures/9EDV/9edv_ligand.sdf structures/9EDV/9edv_ligand.pdb structures/9EDV/9edv_ligand.cif structures/9EDV/9edv_complex.pdb structures/9EDV/9edv_complex.cif 9EDW classic Yck2 Candida albicans Residues 37-345 with an N-terminal His6 tag and TEV protease site Na 1f (7-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine) "[""A1BIP""]" 1 IC50 IC50 = = 0.06 µM 60.0 [] unit_conversion 7.221848749616356 success True biochemical_inhibition Purified recombinant CaYck2 kinase-domain ADP-Glo assay with casein kinase I peptide substrate and ATP. 4 Table 1 reports CaYck2 IC50 = 0.06 µM for 1f; the methods describe the purified-kinase ADP-Glo inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9EDW\9EDW_metadata.json point structures/9EDW/9edw_protein.pdb structures/9EDW/9edw_pocket.pdb structures/9EDW/9edw_ligand.sdf structures/9EDW/9edw_ligand.pdb structures/9EDW/9edw_ligand.cif structures/9EDW/9edw_complex.pdb structures/9EDW/9edw_complex.cif 9EDX classic Yck2 Candida albicans Residues 37-345 with an N-terminal His6 tag and TEV protease site Na 2a (2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine-6-carbonitrile) "[""A1BIO""]" 1 IC50 IC50 = = 0.08 µM 80.0 [] unit_conversion 7.096910013008056 success True biochemical_inhibition Purified recombinant CaYck2 kinase-domain ADP-Glo assay with casein kinase I peptide substrate and ATP. 4 Table 1 reports CaYck2 IC50 = 0.08 µM for 2a; the methods describe the purified-kinase ADP-Glo inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9EDX\9EDX_metadata.json point structures/9EDX/9edx_protein.pdb structures/9EDX/9edx_pocket.pdb structures/9EDX/9edx_ligand.sdf structures/9EDX/9edx_ligand.pdb structures/9EDX/9edx_ligand.cif structures/9EDX/9edx_complex.pdb structures/9EDX/9edx_complex.cif 9EDY classic Yck2 Candida albicans Residues 37-345 with an N-terminal His6 tag and TEV protease site Na 2b (6-fluoro-2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyridine) "[""A1BIN""]" 1 IC50 IC50 = = 0.13 µM 130.0 [] unit_conversion 6.886056647693163 success True biochemical_inhibition Purified recombinant CaYck2 kinase-domain ADP-Glo assay with casein kinase I peptide substrate and ATP. 4 Table 1 reports CaYck2 IC50 = 0.13 µM for 2b; the methods describe the purified-kinase ADP-Glo inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9EDY\9EDY_metadata.json point structures/9EDY/9edy_protein.pdb structures/9EDY/9edy_pocket.pdb structures/9EDY/9edy_ligand.sdf structures/9EDY/9edy_ligand.pdb structures/9EDY/9edy_ligand.cif structures/9EDY/9edy_complex.pdb structures/9EDY/9edy_complex.cif 9EEV classic SARS-CoV-2 Omicron nsp5 main protease (Mpro) SARS-CoV-2 E166V-nsp5BA.1 E166V Nirmatrelvir (NIR; PF-07321332) "[""4WI""]" 1 Kd Kd = = 3370 ± 60 nM 3370.0 [] unit_conversion 5.4723700991286615 success True direct_binding Biolayer interferometry (BLI); purified E166V-nsp5BA.1 with NIR. 6 Table 3 reports E166V-nsp5BA.1 + NIR: Kd 3370 ± 60 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9EEV\9EEV_metadata.json point structures/9EEV/9eev_protein.pdb structures/9EEV/9eev_pocket.pdb structures/9EEV/9eev_ligand.sdf structures/9EEV/9eev_ligand.pdb structures/9EEV/9eev_ligand.cif structures/9EEV/9eev_complex.pdb structures/9EEV/9eev_complex.cif 9EFC classic Danio rerio histone deacetylase 6 Danio rerio catalytic domain 2, residues S440-R798, with an N-terminal His-SUMO tag Na TO-588; compound 1 "[""A1BHY""]" 1 IC50 IC50 = = 4.1 nM 4.1 [] unit_conversion 8.387216143280265 success True biochemical_inhibition In vitro HDAC activity inhibition assay (EMSA/Nanosyn); Table 1 reports HDAC6 IC50 values. 3 Table 1 lists compound 1 with HDAC6 IC50 = 4.1 nM. Figure 3 maps compound 1 to HDAC6 PDB 9EFC. auto_single_measurement only accepted activity measurement [1] 1 structures\9EFC\9EFC_metadata.json point structures/9EFC/9efc_protein.pdb structures/9EFC/9efc_pocket.pdb structures/9EFC/9efc_ligand.sdf structures/9EFC/9efc_ligand.pdb structures/9EFC/9efc_ligand.cif structures/9EFC/9efc_complex.pdb structures/9EFC/9efc_complex.cif 9EFR classic Danio rerio histone deacetylase 6 Danio rerio catalytic domain 2, residues S440-R798, with an N-terminal His-SUMO tag Na TO-600; compound 3 "[""A1BHX""]" 1 IC50 IC50 = = 1.7 nM 1.7 [] unit_conversion 8.769551078621726 success True biochemical_inhibition In vitro HDAC activity inhibition assay (EMSA/Nanosyn); Table 1 reports HDAC6 IC50 values. 3 Table 1 lists compound 3 with HDAC6 IC50 = 1.7 nM. Figure 3 maps compound 3 to HDAC6 PDB 9EFR. auto_single_measurement only accepted activity measurement [1] 1 structures\9EFR\9EFR_metadata.json point structures/9EFR/9efr_protein.pdb structures/9EFR/9efr_pocket.pdb structures/9EFR/9efr_ligand.sdf structures/9EFR/9efr_ligand.pdb structures/9EFR/9efr_ligand.cif structures/9EFR/9efr_complex.pdb structures/9EFR/9efr_complex.cif 9EFV classic COP9 signalosome (CSN)-N8~CRL1 complex Homo sapiens CSN5i-3-CSN-N8~CRL1 Na CSN5i-3 "[""6LT""]" 1 IC50 IC50 = = 29 nM 29.0 [] unit_conversion 7.537602002101044 success True biochemical_inhibition CSN iso-peptidase activity towards N8~CRL1 in vitro. 4 Fig. 2e prints IC50 = 29 nM for CSN5i-3; the substrate is N8~CRL1 and enzyme is CSN. auto_single_measurement only accepted activity measurement [1] 1 structures\9EFV\9EFV_metadata.json point structures/9EFV/9efv_protein.pdb structures/9EFV/9efv_pocket.pdb structures/9EFV/9efv_ligand.sdf structures/9EFV/9efv_ligand.pdb structures/9EFV/9efv_ligand.cif structures/9EFV/9efv_complex.pdb structures/9EFV/9efv_complex.cif 9EFX classic Danio rerio histone deacetylase 6 Danio rerio catalytic domain 2, residues S440-R798, with an N-terminal His-SUMO tag Na TO-584; compound 6 "[""A1BHW""]" 1 IC50 IC50 = = 5.4 nM 5.4 [] unit_conversion 8.267606240177031 success True biochemical_inhibition In vitro HDAC activity inhibition assay (EMSA/Nanosyn); Table 1 reports HDAC6 IC50 values. 3 Table 1 lists compound 6 with HDAC6 IC50 = 5.4 nM. Figure 3 maps compound 6 to HDAC6 PDB 9EFX. auto_single_measurement only accepted activity measurement [1] 1 structures\9EFX\9EFX_metadata.json point structures/9EFX/9efx_protein.pdb structures/9EFX/9efx_pocket.pdb structures/9EFX/9efx_ligand.sdf structures/9EFX/9efx_ligand.pdb structures/9EFX/9efx_ligand.cif structures/9EFX/9efx_complex.pdb structures/9EFX/9efx_complex.cif 9EGF classic Danio rerio histone deacetylase 6 Danio rerio catalytic domain 2, residues S440-R798, with an N-terminal His-SUMO tag Na TO-589; compound 2 "[""A1BH8""]" 1 IC50 IC50 = = 3.1 nM 3.1 [] unit_conversion 8.508638306165727 success True biochemical_inhibition In vitro HDAC activity inhibition assay (EMSA/Nanosyn); Table 1 reports HDAC6 IC50 values. 3 Table 1 lists compound 2 with HDAC6 IC50 = 3.1 nM. Figure 3 maps compound 2 to HDAC6 PDB 9EGF. auto_single_measurement only accepted activity measurement [1] 1 structures\9EGF\9EGF_metadata.json point structures/9EGF/9egf_protein.pdb structures/9EGF/9egf_pocket.pdb structures/9EGF/9egf_ligand.sdf structures/9EGF/9egf_ligand.pdb structures/9EGF/9egf_ligand.cif structures/9EGF/9egf_complex.pdb structures/9EGF/9egf_complex.cif 9EGU classic Danio rerio histone deacetylase 6 Danio rerio catalytic domain 2, residues S440-R798, with an N-terminal His-SUMO tag Na TO-599; compound 10 "[""A1BH9""]" 1 IC50 IC50 = = 0.6 nM 0.6 [] unit_conversion 9.221848749616356 success True biochemical_inhibition In vitro HDAC activity inhibition assay (EMSA/Nanosyn); Table 1 reports HDAC6 IC50 values. 3 Table 1 lists compound 10 with HDAC6 IC50 = 0.6 nM. Figure 3 maps compound 10 to HDAC6 PDB 9EGU. auto_single_measurement only accepted activity measurement [1] 1 structures\9EGU\9EGU_metadata.json point structures/9EGU/9egu_protein.pdb structures/9EGU/9egu_pocket.pdb structures/9EGU/9egu_ligand.sdf structures/9EGU/9egu_ligand.pdb structures/9EGU/9egu_ligand.cif structures/9EGU/9egu_complex.pdb structures/9EGU/9egu_complex.cif 9EHI extended ENL Na ENL YEATS residues 1-148 with an N-terminal 6xHis tag Na H3K18mc (histone H3 peptide methacrylated at K18) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 13 ± 1 µM 13000.0 [] unit_conversion 4.886056647693163 success True direct_binding Tryptophan fluorescence measurement of ENL_YEATS binding to H3K18mc peptide; average of three separate experiments, error reported as SD. 4 The paper states that the dissociation constant (Kd) of 13 µM was measured for ENL_YEATS interaction with H3K18mc by tryptophan fluorescence; Figure 2c prints Kd = 13 ± 1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9EHI\9EHI_metadata.json point structures/9EHI/9ehi_protein.pdb structures/9EHI/9ehi_pocket.pdb structures/9EHI/9ehi_ligand.pdb structures/9EHI/9ehi_ligand.cif structures/9EHI/9ehi_complex.pdb structures/9EHI/9ehi_complex.cif 9EO6 extended SARS-CoV-2 major protease (Mpro) SARS-CoV-2 Mpro residues S1-Q306 from the Chinese isolate (NCBI accession YP_009725301) Na SLL11 "[""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L""]" 1 IC50 IC50 = = 0.03 µM 30.0 [] unit_conversion 7.522878745280337 success True biochemical_inhibition In vitro FRET-based enzymatic inhibition assay against recombinant SARS-CoV-2 Mpro. 9 Table 1 lists SLL11 with Mpro IC50 = 0.03 µM; the text identifies PDB 9EO6 as the SLL11 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9EO6\9EO6_metadata.json point structures/9EO6/9eo6_protein.pdb structures/9EO6/9eo6_pocket.pdb structures/9EO6/9eo6_ligand.pdb structures/9EO6/9eo6_ligand.cif structures/9EO6/9eo6_complex.pdb structures/9EO6/9eo6_complex.cif 9EOL classic N-acetylglucosamine 6-phosphate dehydratase (NagS) Streptomyces coelicolor N-terminally His6-tagged NagS Na 6-phosphogluconate (6-PG) "[""6PG""]" 1 Ki Ki = = 0.28 ± 0.03 mM 280000.0 [] unit_conversion 3.5528419686577806 success True biochemical_inhibition Purified NagS kinetic analysis established 6-PG as a competitive inhibitor of GlcNAc-6P conversion. 8 “The inhibition constant (Ki) for 6-PG was determined to be 0.28 ± 0.03 mM, supporting its role as a competitive inhibitor.” auto_single_measurement only accepted activity measurement [1] 1 structures\9EOL\9EOL_metadata.json point structures/9EOL/9eol_protein.pdb structures/9EOL/9eol_pocket.pdb structures/9EOL/9eol_ligand.sdf structures/9EOL/9eol_ligand.pdb structures/9EOL/9eol_ligand.cif structures/9EOL/9eol_complex.pdb structures/9EOL/9eol_complex.cif 9EOR extended SARS-CoV-2 major protease (Mpro) SARS-CoV-2 Mpro residues S1-Q306 from the Chinese isolate (NCBI accession YP_009725301) Na SLL12 "[""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L""]" 1 IC50 IC50 = = 0.053 µM 53.0 [] unit_conversion 7.275724130399211 success True biochemical_inhibition In vitro FRET-based enzymatic inhibition assay against recombinant SARS-CoV-2 Mpro. 9 Table 1 lists SLL12 with Mpro IC50 = 0.053 µM; the text identifies PDB 9EOR as the SLL12 complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9EOR\9EOR_metadata.json point structures/9EOR/9eor_protein.pdb structures/9EOR/9eor_pocket.pdb structures/9EOR/9eor_ligand.pdb structures/9EOR/9eor_ligand.cif structures/9EOR/9eor_complex.pdb structures/9EOR/9eor_complex.cif 9EOU extended neuropilin-1 (NRP-1) human b1b2 domains Na FOL-026 "[""CHAIN:P""]" 1 Kd Kd = = 7704 nM 7704.0 [] unit_conversion 5.113283725883521 success True direct_binding Microscale thermophoresis (MST) of labeled human NRP-1 b1b2 structural variant with non-labeled FOL-026. 4 Fig. 1 legend reports an MST-derived Kd of 7704 nM for the FOL-026/NRP-1 b1b2 interaction (n=3). auto_single_measurement only accepted activity measurement [1] 1 structures\9EOU\9EOU_metadata.json point structures/9EOU/9eou_protein.pdb structures/9EOU/9eou_pocket.pdb structures/9EOU/9eou_ligand.pdb structures/9EOU/9eou_ligand.cif structures/9EOU/9eou_complex.pdb structures/9EOU/9eou_complex.cif 9EOX extended SARS-CoV-2 major protease (Mpro) SARS-CoV-2 Mpro residues S1-Q306 from the Chinese isolate (NCBI accession YP_009725301) Na MP9 "[""CHAIN:G"", ""CHAIN:H"", ""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L""]" 1 IC50 IC50 = = 0.139 ± 0.049 µM 139.0 [] unit_conversion 6.856985199745905 success True biochemical_inhibition In vitro FRET-based enzymatic inhibition assay against recombinant SARS-CoV-2 Mpro; value reported as IC50 ± SEM. 11 Table 2 lists MP9 with Mpro IC50 ± SEM = 0.139 ± 0.049 µM. The crystallography methods map MP9 to PDB 9EOX. auto_single_measurement only accepted activity measurement [1] 1 structures\9EOX\9EOX_metadata.json point structures/9EOX/9eox_protein.pdb structures/9EOX/9eox_pocket.pdb structures/9EOX/9eox_ligand.pdb structures/9EOX/9eox_ligand.cif structures/9EOX/9eox_complex.pdb structures/9EOX/9eox_complex.cif 9EP2 extended human carbonic anhydrase I human Na Na 4e; 4-sulfamoylphenyl 3-(p-tolylthio)propanoate "[""A1H6C""]" 1 Ki Ki = = 7.8 nM 7.8 [] unit_conversion 8.10790539730952 success True biochemical_inhibition Stopped-flow CO2 hydrase inhibition assay; Table 1 reports inhibition data for human CA isoforms. 3 Table 1 reports compound 4e Ki = 7.8 nM against hCA I. The paper identifies the PDB 9EP2 complex as hCA I with 4e bound. auto_single_measurement only accepted activity measurement [1] 1 structures\9EP2\9EP2_metadata.json point structures/9EP2/9ep2_ligand.sdf structures/9EP2/9ep2_ligand.cif structures/9EP2/9ep2_complex.cif 9ERZ extended CBL TKBD Na CBL residues 47-355 Na Ubiquitin-fused CBLock peptide (Ub-peptide10) "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.27 ± 0.02 µM 270.0 [] unit_conversion 6.568636235841012 success True direct_binding SPR equilibrium dissociation constant for immobilized GST-CBL TKBD residues 47–355 and ubiquitin-fused peptide10-M16R (Ub-CBLock). 4 Table 1 reports “Ub-peptide10 M16R (Ub-CBLock)” with K_D 0.27 ± 0.02 µM; the text identifies peptide10-M16R as CBLock. auto_single_measurement only accepted activity measurement [1] 1 structures\9ERZ\9ERZ_metadata.json point structures/9ERZ/9erz_protein.pdb structures/9ERZ/9erz_pocket.pdb structures/9ERZ/9erz_ligand.pdb structures/9ERZ/9erz_ligand.cif structures/9ERZ/9erz_complex.pdb structures/9ERZ/9erz_complex.cif 9EU0 classic HDAC6 Danio rerio CD2 Na ITF7738; hydrolyzed DFMO/acyl-hydrazide derivative of ITF7209 "[""A1H7I""]" 1 IC50 IC50 = = (72 ± 2) × 10^3 nM 72000.0 [] unit_conversion 4.142667503568732 success True biochemical_inhibition Inhibitory profile on zHDAC6-CD2 (Table 1). 6 Table 1 reports ITF7738 IC50 = (72 ± 2) × 10^3 nM on zHDAC6-CD2. Figure 2 identifies ITF7738 as the acyl-hydrazide (DFAcH) derivative of ITF7209; pages 8–9 assign PDB 9EU0 to this DFAcH complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9EU0\9EU0_metadata.json point structures/9EU0/9eu0_protein.pdb structures/9EU0/9eu0_pocket.pdb structures/9EU0/9eu0_ligand.sdf structures/9EU0/9eu0_ligand.pdb structures/9EU0/9eu0_ligand.cif structures/9EU0/9eu0_complex.pdb structures/9EU0/9eu0_complex.cif 9EU6 classic FKBP51 Na Na Na SAFit-analog 23j "[""A1H7U""]" 1 Ki Ki = = 0.92 ± 0.06 μM 920.0 [] unit_conversion 6.036212172654444 success True direct_binding Competitive fluorescence polarization assay. 7 Table 4 reports FKBP51 Ki = 0.92 ± 0.06 μM for 23j; Figure 2 maps 23j to PDB 9EU6. auto_single_measurement only accepted activity measurement [1] 1 structures\9EU6\9EU6_metadata.json point structures/9EU6/9eu6_protein.pdb structures/9EU6/9eu6_pocket.pdb structures/9EU6/9eu6_ligand.sdf structures/9EU6/9eu6_ligand.pdb structures/9EU6/9eu6_ligand.cif structures/9EU6/9eu6_complex.pdb structures/9EU6/9eu6_complex.cif 9EU7 classic FKBP51 Na Na Na SAFit-analog 15b "[""A1H7A""]" 1 Ki Ki = = 0.24 ± 0.02 μM 240.0 [] unit_conversion 6.619788758288394 success True direct_binding Competitive fluorescence polarization assay. 4 Table 3 reports FKBP51 Ki = 0.24 ± 0.02 μM for 15b; Figure 2 maps 15b to PDB 9EU7. auto_single_measurement only accepted activity measurement [1] 1 structures\9EU7\9EU7_metadata.json point structures/9EU7/9eu7_protein.pdb structures/9EU7/9eu7_pocket.pdb structures/9EU7/9eu7_ligand.sdf structures/9EU7/9eu7_ligand.pdb structures/9EU7/9eu7_ligand.cif structures/9EU7/9eu7_complex.pdb structures/9EU7/9eu7_complex.cif 9EU8 classic FKBP51 Na Na Na SAFit-analog 15h "[""A1H7B""]" 1 Ki Ki = = 0.26 ± 0.02 μM 260.0 [] unit_conversion 6.585026652029182 success True direct_binding Competitive fluorescence polarization assay. 4 Table 3 reports FKBP51 Ki = 0.26 ± 0.02 μM for 15h; Figure 2 maps 15h to PDB 9EU8. auto_single_measurement only accepted activity measurement [1] 1 structures\9EU8\9EU8_metadata.json point structures/9EU8/9eu8_protein.pdb structures/9EU8/9eu8_pocket.pdb structures/9EU8/9eu8_ligand.sdf structures/9EU8/9eu8_ligand.pdb structures/9EU8/9eu8_ligand.cif structures/9EU8/9eu8_complex.pdb structures/9EU8/9eu8_complex.cif 9EU9 classic FKBP51 Na Na Na SAFit-analog 15i "[""A1H7C""]" 1 Ki Ki = = 0.46 ± 0.06 μM 460.0 [] unit_conversion 6.337242168318426 success True direct_binding Competitive fluorescence polarization assay. 4 Table 3 reports FKBP51 Ki = 0.46 ± 0.06 μM for 15i; Figure 2 maps 15i to PDB 9EU9. auto_single_measurement only accepted activity measurement [1] 1 structures\9EU9\9EU9_metadata.json point structures/9EU9/9eu9_protein.pdb structures/9EU9/9eu9_pocket.pdb structures/9EU9/9eu9_ligand.sdf structures/9EU9/9eu9_ligand.pdb structures/9EU9/9eu9_ligand.cif structures/9EU9/9eu9_complex.pdb structures/9EU9/9eu9_complex.cif 9EUA classic FKBP51 Na Na Na SAFit-analog 23d "[""A1H7D""]" 1 Ki Ki = = 0.077 ± 0.003 μM 77.0 [] unit_conversion 7.113509274827518 success True direct_binding Competitive fluorescence polarization assay. 7 Table 4 reports FKBP51 Ki = 0.077 ± 0.003 μM for 23d; Figure 2 maps 23d to PDB 9EUA. auto_single_measurement only accepted activity measurement [1] 1 structures\9EUA\9EUA_metadata.json point structures/9EUA/9eua_protein.pdb structures/9EUA/9eua_pocket.pdb structures/9EUA/9eua_ligand.sdf structures/9EUA/9eua_ligand.pdb structures/9EUA/9eua_ligand.cif structures/9EUA/9eua_complex.pdb structures/9EUA/9eua_complex.cif 9EUB classic FKBP51 Na Na Na SAFit-analog 24e "[""A1H7E""]" 1 Ki Ki = = 0.27 ± 0.009 μM 270.0 [] unit_conversion 6.568636235841012 success True direct_binding Competitive fluorescence polarization assay. 7 Table 4 reports FKBP51 Ki = 0.27 ± 0.009 μM for 24e; Figure 2 maps 24e to PDB 9EUB. auto_single_measurement only accepted activity measurement [1] 1 structures\9EUB\9EUB_metadata.json point structures/9EUB/9eub_protein.pdb structures/9EUB/9eub_pocket.pdb structures/9EUB/9eub_ligand.sdf structures/9EUB/9eub_ligand.pdb structures/9EUB/9eub_ligand.cif structures/9EUB/9eub_complex.pdb structures/9EUB/9eub_complex.cif 9EUC classic FKBP51 Na Na Na SAFit-analog 23b "[""A1H7F""]" 1 Ki Ki = = 0.12 ± 0.001 μM 120.0 [] unit_conversion 6.920818753952375 success True direct_binding Competitive fluorescence polarization assay. 7 Table 4 reports FKBP51 Ki = 0.12 ± 0.001 μM for 23b; Figure 2 maps 23b to PDB 9EUC. auto_single_measurement only accepted activity measurement [1] 1 structures\9EUC\9EUC_metadata.json point structures/9EUC/9euc_protein.pdb structures/9EUC/9euc_pocket.pdb structures/9EUC/9euc_ligand.sdf structures/9EUC/9euc_ligand.pdb structures/9EUC/9euc_ligand.cif structures/9EUC/9euc_complex.pdb structures/9EUC/9euc_complex.cif 9EUD classic FKBP51 Na Na Na SAFit-analog 23c "[""A1H7G""]" 1 Ki Ki = = 0.087 ± 0.003 μM 87.0 [] unit_conversion 7.060480747381382 success True direct_binding Competitive fluorescence polarization assay. 7 Table 4 reports FKBP51 Ki = 0.087 ± 0.003 μM for 23c; Figure 2 maps 23c to PDB 9EUD. auto_single_measurement only accepted activity measurement [1] 1 structures\9EUD\9EUD_metadata.json point structures/9EUD/9eud_protein.pdb structures/9EUD/9eud_pocket.pdb structures/9EUD/9eud_ligand.sdf structures/9EUD/9eud_ligand.pdb structures/9EUD/9eud_ligand.cif structures/9EUD/9eud_complex.pdb structures/9EUD/9eud_complex.cif 9EUE classic FKBP51 Na Na Na SAFit-analog 23a "[""A1H68""]" 1 Ki Ki = = 0.27 ± 0.01 μM 270.0 [] unit_conversion 6.568636235841012 success True direct_binding Competitive fluorescence polarization assay. 7 Table 4 reports FKBP51 Ki = 0.27 ± 0.01 μM for 23a; Figure 2 maps 23a to PDB 9EUE. auto_single_measurement only accepted activity measurement [1] 1 structures\9EUE\9EUE_metadata.json point structures/9EUE/9eue_protein.pdb structures/9EUE/9eue_pocket.pdb structures/9EUE/9eue_ligand.sdf structures/9EUE/9eue_ligand.pdb structures/9EUE/9eue_ligand.cif structures/9EUE/9eue_complex.pdb structures/9EUE/9eue_complex.cif 9EW6 extended 14-3-3s Na Na Na BRAF phosphopeptide (pS365) "[""CHAIN:P""]" 1 Kd Kd = = 2.7 ± 0.1 μM 2700.0 [] unit_conversion 5.568636235841012 success True direct_binding SPR analysis of the binary interaction between 14-3-3σ and a 12-mer B-RAF phosphopeptide. 9 Figure 5B prints KD = 2.7 ± 0.1 μM for the binary 14-3-3σ/B-RAF 12-mer interaction. auto_single_measurement only accepted activity measurement [1] 1 structures\9EW6\9EW6_metadata.json point structures/9EW6/9ew6_protein.pdb structures/9EW6/9ew6_pocket.pdb structures/9EW6/9ew6_ligand.pdb structures/9EW6/9ew6_ligand.cif structures/9EW6/9ew6_complex.pdb structures/9EW6/9ew6_complex.cif 9EW7 extended 14-3-3s Na Na Na CRAF phosphopeptide (pS259) "[""CHAIN:P""]" 1 Kd Kd = = 2.6 ± 0.3 μM 2600.0 [] unit_conversion 5.585026652029182 success True direct_binding SPR analysis of the binary interaction between 14-3-3σ and a 12-mer C-RAF phosphopeptide. 9 Figure 5B prints KD = 2.6 ± 0.3 μM for the binary 14-3-3σ/C-RAF 12-mer interaction. auto_single_measurement only accepted activity measurement [1] 1 structures\9EW7\9EW7_metadata.json point structures/9EW7/9ew7_protein.pdb structures/9EW7/9ew7_pocket.pdb structures/9EW7/9ew7_ligand.pdb structures/9EW7/9ew7_ligand.cif structures/9EW7/9ew7_complex.pdb structures/9EW7/9ew7_complex.cif 9EWU classic human butyrylcholinesterase human Na Na compound 6; (2R,3S)-1-[(cyclopropylmethyl)amino]-3-[(9H-fluoren-9-yl)amino]-4-phenylbutan-2-ol "[""A1H77""]" 1 IC50 IC50 = = 0.21 ± 0.01 µM 210.0 [] unit_conversion 6.6777807052660805 success True biochemical_inhibition Inhibition of hBuChE by compound 6; Table 1 reports IC50 values. 3 Table 1 lists compound 6 with hBuChE IC50 = 0.21 ± 0.01 µM; the text states that compound 6 was structurally determined bound to hBuChE. auto_single_measurement only accepted activity measurement [1] 1 structures\9EWU\9EWU_metadata.json point structures/9EWU/9ewu_protein.pdb structures/9EWU/9ewu_pocket.pdb structures/9EWU/9ewu_ligand.sdf structures/9EWU/9ewu_ligand.pdb structures/9EWU/9ewu_ligand.cif structures/9EWU/9ewu_complex.pdb structures/9EWU/9ewu_complex.cif 9EXW classic NSD2 human NSD2 residues 208-368 wild-type compound 17 "[""A1H7X""]" 1 pIC50 IC50 = = 7.2 unitless 63.0957344480193 [] p_metric_transform 7.2 success True biochemical_inhibition NSD2 biochemical binding (TR-FRET) assay; Table 3 reports pIC50 for compound 17. 4 Table 3 lists compound 17 with NSD2 biochemical pIC50 7.2. auto_single_measurement only accepted activity measurement [1] 1 structures\9EXW\9EXW_metadata.json point structures/9EXW/9exw_protein.pdb structures/9EXW/9exw_pocket.pdb structures/9EXW/9exw_ligand.sdf structures/9EXW/9exw_ligand.pdb structures/9EXW/9exw_ligand.cif structures/9EXW/9exw_complex.pdb structures/9EXW/9exw_complex.cif 9EXX classic NSD2 human NSD2 residues 208-368 wild-type compound 18 "[""A1H7Y""]" 2 pKd Kd = = 6.6 unitless 251.18864315095823 [] p_metric_transform 6.6 success True direct_binding NSD2 SPR direct-binding assay; Table 4. 6 Table 4 lists compound 18 with NSD2 SPR pKd 6.6. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9EXX\9EXX_metadata.json point structures/9EXX/9exx_protein.pdb structures/9EXX/9exx_pocket.pdb structures/9EXX/9exx_ligand.sdf structures/9EXX/9exx_ligand.pdb structures/9EXX/9exx_ligand.cif structures/9EXX/9exx_complex.pdb structures/9EXX/9exx_complex.cif 9EY3 classic FKBP51 Na Na Na compound 3; (3S,11S,11aS)-12-((3,5-dichlorophenyl)sulfonyl)-5-oxo-11-vinyldecahydro-1H-6,10-epiminopyrrolo[1,2-a]azonine-3-carboxylic acid "[""A1H70""]" 1 Ki Ki = = 698 ± 49 nM 698.0 [] unit_conversion 6.156144577376839 success True direct_binding Competitive fluorescence-polarization binding assay with purified human FKBP51. 3 Table 1 reports compound 3: FKBP51 Ki = 698 ± 49 nM. Figure 2 identifies compound 3 in complex with FKBP51 as PDB 9EY3. auto_single_measurement only accepted activity measurement [1] 1 structures\9EY3\9EY3_metadata.json point structures/9EY3/9ey3_protein.pdb structures/9EY3/9ey3_pocket.pdb structures/9EY3/9ey3_ligand.sdf structures/9EY3/9ey3_ligand.pdb structures/9EY3/9ey3_ligand.cif structures/9EY3/9ey3_complex.pdb structures/9EY3/9ey3_complex.cif 9EY4 classic FKBP51 Na Na Na compound 21; (3S,11S)-12-((3,5-dichlorophenyl)sulfonyl)-5-oxo-11-vinyldecahydro-1H-6,10-epiminopyrrolo[1,2-a]azonine-3-carboxamide "[""A1H78""]" 1 Ki Ki = = 18 ± 3.0 nM 18.0 [] unit_conversion 7.7447274948966935 success True direct_binding Competitive fluorescence-polarization binding assay with purified human FKBP51. 3 Table 1 reports compound 21: FKBP51 Ki = 18 ± 3.0 nM. Figure 3 identifies compound 21 in complex with FKBP51 as PDB 9EY4. auto_single_measurement only accepted activity measurement [1] 1 structures\9EY4\9EY4_metadata.json point structures/9EY4/9ey4_protein.pdb structures/9EY4/9ey4_pocket.pdb structures/9EY4/9ey4_ligand.sdf structures/9EY4/9ey4_ligand.pdb structures/9EY4/9ey4_ligand.cif structures/9EY4/9ey4_complex.pdb structures/9EY4/9ey4_complex.cif 9EYU classic Human PRMT5 human Na Na AZ compound 1; compound 1 "[""A1H8A""]" 2 Kd Kd = = 1.0 nM 1.0 [] unit_conversion 9.0 success True direct_binding SPR binding of compound 1 to PRMT5 in the presence of MTA. 5 Text states a 6-fold affinity increase with MTA “(Kd = 1.0 nM)” in orthogonal SPR binding assays. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9EYU\9EYU_metadata.json point structures/9EYU/9eyu_protein.pdb structures/9EYU/9eyu_pocket.pdb structures/9EYU/9eyu_ligand.sdf structures/9EYU/9eyu_ligand.pdb structures/9EYU/9eyu_ligand.cif structures/9EYU/9eyu_complex.pdb structures/9EYU/9eyu_complex.cif 9EYV extended Human PRMT5 human Na Na AZ compound 12; compound 12 "[""A1H76""]" 1 IC50 IC50 = = 0.107 µM 107.0 [] unit_conversion 6.97061622231479 success True biochemical_inhibition PRMT5 biochemical assay with MTA; Table 3. 7 Table 3, compound 12, prints PRMT5 IC50 (+MTA) = 0.107 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9EYV\9EYV_metadata.json point structures/9EYV/9eyv_protein.pdb structures/9EYV/9eyv_pocket.pdb structures/9EYV/9eyv_ligand.pdb structures/9EYV/9eyv_ligand.cif structures/9EYV/9eyv_complex.pdb structures/9EYV/9eyv_complex.cif 9EYW extended Human PRMT5 human Na Na AZ compound 21; compound 21 "[""A1H8B""]" 1 IC50 IC50 = = 0.0029 µM 2.9 [] unit_conversion 8.537602002101044 success True biochemical_inhibition PRMT5 biochemical assay with MTA; Table 4. 9 Table 4, compound 21, prints PRMT5 IC50 (+MTA) = 0.0029 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9EYW\9EYW_metadata.json point structures/9EYW/9eyw_protein.pdb structures/9EYW/9eyw_pocket.pdb structures/9EYW/9eyw_ligand.pdb structures/9EYW/9eyw_ligand.cif structures/9EYW/9eyw_complex.pdb structures/9EYW/9eyw_complex.cif 9EZG classic human Casein Kinase II subunit alpha (CK2a1) human Na Na compound 53; 5-((4-((2-aminoethyl)(ethyl)amino)-3-(4H-1,2,4-triazol-4-yl)phenyl)amino)-7-(cyclopropylamino)pyrazolo[1,5-a]pyrimidine-3-carbonitrile "[""A1H8C""]" 1 IC50 IC50 = = 1.7 nM 1.7 [] unit_conversion 8.769551078621726 success True biochemical_inhibition Eurofins KinaseProfiler in vitro radiometric enzyme assay performed at ATP Km. 9 The paper states that compound 53 inhibited CSNK2A1 with an IC50 of 1.7 nM; page 50 maps compound 53 to PDB 9EZG. auto_single_measurement only accepted activity measurement [1] 1 structures\9EZG\9EZG_metadata.json point structures/9EZG/9ezg_protein.pdb structures/9EZG/9ezg_pocket.pdb structures/9EZG/9ezg_ligand.sdf structures/9EZG/9ezg_ligand.pdb structures/9EZG/9ezg_ligand.cif structures/9EZG/9ezg_complex.pdb structures/9EZG/9ezg_complex.cif 9F19 classic USP30 chimera Homo sapiens USP30 chimera ch3 (USP14-USP35), containing USP14 fingers and the USP35 box 4/5 insertion F348D NK036 "[""A1H8X""]" 1 IC50 IC50 = = 4.1 ± 0.3 nM 4.1 [] unit_conversion 8.387216143280265 success True biochemical_inhibition Ub–RhoG cleavage inhibition assay of USP30 ch3. 2 Fig. 1l reports USP30ch3 inhibition by NK036 with IC50 = 4.1 ± 0.3 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9F19\9F19_metadata.json point structures/9F19/9f19_protein.pdb structures/9F19/9f19_pocket.pdb structures/9F19/9f19_ligand.sdf structures/9F19/9f19_ligand.pdb structures/9F19/9f19_ligand.cif structures/9F19/9f19_complex.pdb structures/9F19/9f19_complex.cif 9F1A classic human soluble epoxide hydrolase human C-terminal domain, amino acids 230-555 Na compound 20 "[""A1H8Y""]" 1 IC50 IC50 = = 0.4 nM 0.4 [] unit_conversion 9.397940008672037 success True biochemical_inhibition Table 1: IC50 in human sEH; in-vitro inhibitory activity assay. 6 Table 1 reports compound 20 with human sEH IC50 = 0.4 nM. The paper identifies PDB 9F1A as the crystal structure of compound 20 bound to hsEH C-terminal domain. auto_single_measurement only accepted activity measurement [1] 1 structures\9F1A\9F1A_metadata.json point structures/9F1A/9f1a_protein.pdb structures/9F1A/9f1a_pocket.pdb structures/9F1A/9f1a_ligand.sdf structures/9F1A/9f1a_ligand.pdb structures/9F1A/9f1a_ligand.cif structures/9F1A/9f1a_complex.pdb structures/9F1A/9f1a_complex.cif 9F1J extended BRD4 human N-terminal bromodomain of BRD4, residues N44-E168, expressed in pNIC28-Bsa4 with an N-terminal His6 tag and TEV cleavage site Na ISOX-DUAL-based degrader 14 "[""A1H84""]" 1 IC50 IC50 = = 1.84 ± 0.04 µM 1840.0 [] unit_conversion 5.735182176990463 success True direct_binding Biochemical FRET binding assay. 4 Table 2 reports BRD4 IC50 = 1.84 ± 0.04 µM for compound 14; page 21 maps PDB 9F1J to degrader 14. auto_single_measurement only accepted activity measurement [1] 1 structures\9F1J\9F1J_metadata.json point structures/9F1J/9f1j_protein.pdb structures/9F1J/9f1j_pocket.pdb structures/9F1J/9f1j_ligand.pdb structures/9F1J/9f1j_ligand.cif structures/9F1J/9f1j_complex.pdb structures/9F1J/9f1j_complex.cif 9F2H classic SARS-CoV-2 N-protein C-terminal domain SARS-CoV-2 SARS-CoV-2 N_CTD residues 255-364 Na riluzole "[""657""]" 1 Kd Kd = = 1118 ± 45 μM 1118000.0 [] unit_conversion 2.9515581964495956 success True direct_binding Intrinsic Trp fluorescence-quenching titration of N_CTD; reported as apparent K_D (K_Dapp). 5 Figure 2C reports the calculated apparent K_D for riluzole as 1118 ± 45 μM; the caption identifies this as fluorescence binding analysis with SARS-CoV-2 N_CTD. auto_single_measurement only accepted activity measurement [1] 1 structures\9F2H\9F2H_metadata.json point structures/9F2H/9f2h_protein.pdb structures/9F2H/9f2h_pocket.pdb structures/9F2H/9f2h_ligand.sdf structures/9F2H/9f2h_ligand.pdb structures/9F2H/9f2h_ligand.cif structures/9F2H/9f2h_complex.pdb structures/9F2H/9f2h_complex.cif 9F2I classic SARS-CoV-2 N-protein C-terminal domain SARS-CoV-2 SARS-CoV-2 N_CTD residues 255-364 Na 2-amino-1,3-benzothiazol-6-ol (6OH-BZT; compound 1) "[""A1H88""]" 1 Kd Kd = = 586 ± 45 μM 586000.0 [] unit_conversion 3.2321023839819096 success True direct_binding Intrinsic Trp fluorescence-quenching titration of N_CTD; reported as apparent K_D (K_Dapp). 4 The text states that 6OH-BZT binds N_CTD with K_Dapp = 586 ± 45 μM in the Trp-emission fluorescence binding analysis. auto_single_measurement only accepted activity measurement [1] 1 structures\9F2I\9F2I_metadata.json point structures/9F2I/9f2i_protein.pdb structures/9F2I/9f2i_pocket.pdb structures/9F2I/9f2i_ligand.sdf structures/9F2I/9f2i_ligand.pdb structures/9F2I/9f2i_ligand.cif structures/9F2I/9f2i_complex.pdb structures/9F2I/9f2i_complex.cif 9F2N classic carbonic anhydrase XII human Na Na compound 10 (3-(cyclooctylamino)-2,6-difluoro-4-((3-hydroxypropyl)sulfonyl)-5-(piperidin-1-yl)benzenesulfonamide) "[""A1H9A""]" 1 Kd Kd = = 36 nM 36.0 [] unit_conversion 7.443697499232712 success True direct_binding FTSA, 37 °C, pH 7.0; human recombinant CA isozymes. 4 Table 1 reports compound 10 Kd,obs = 36 nM for CA XII. The text maps CA XII–10 structures to PDB IDs 9F2N and 9R0L. auto_single_measurement only accepted activity measurement [1] 1 structures\9F2N\9F2N_metadata.json point structures/9F2N/9f2n_protein.pdb structures/9F2N/9f2n_pocket.pdb structures/9F2N/9f2n_ligand.sdf structures/9F2N/9f2n_ligand.pdb structures/9F2N/9f2n_ligand.cif structures/9F2N/9f2n_complex.pdb structures/9F2N/9f2n_complex.cif 9F2O classic carbonic anhydrase XII human Na Na compound 13 (3-(cyclooctylamino)-2,6-difluoro-4-((3-hydroxypropyl)sulfonyl)-5-methoxybenzenesulfonamide) "[""A1H89""]" 1 Kd Kd = = 0.050 nM 0.05 [] unit_conversion 10.301029995663981 success True direct_binding FTSA, 37 °C, pH 7.0; human recombinant CA isozymes. 4 Table 1 reports compound 13 Kd,obs = 0.050 nM for CA XII (95% confidence interval [0.031; 0.071]). The text maps CA XII–13 structures to PDB IDs 9F2O and 9R31. auto_single_measurement only accepted activity measurement [1] 1 structures\9F2O\9F2O_metadata.json point structures/9F2O/9f2o_protein.pdb structures/9F2O/9f2o_pocket.pdb structures/9F2O/9f2o_ligand.sdf structures/9F2O/9f2o_ligand.pdb structures/9F2O/9f2o_ligand.cif structures/9F2O/9f2o_complex.pdb structures/9F2O/9f2o_complex.cif 9F30 classic carbonic anhydrase XII human Na Na compound 14 (3-(cyclooctylamino)-5-ethoxy-2,6-difluoro-4-((3-hydroxypropyl)sulfonyl)benzenesulfonamide) "[""A1H92""]" 1 Kd Kd = = 0.11 nM 0.11 [] unit_conversion 9.958607314841775 success True direct_binding FTSA, 37 °C, pH 7.0; human recombinant CA isozymes. 4 Table 1 reports compound 14 Kd,obs = 0.11 nM for CA XII (95% confidence interval [0.096; 0.17]). The text identifies CA XII–14 structures as PDB IDs 9F30 and 9R0U. auto_single_measurement only accepted activity measurement [1] 1 structures\9F30\9F30_metadata.json point structures/9F30/9f30_protein.pdb structures/9F30/9f30_pocket.pdb structures/9F30/9f30_ligand.sdf structures/9F30/9f30_ligand.pdb structures/9F30/9f30_ligand.cif structures/9F30/9f30_complex.pdb structures/9F30/9f30_complex.cif 9F35 extended 14-3-3sigma Na Na Na B-Raf pS365 phosphopeptide (360-RDRSS(pS)APNVH-370) "[""CHAIN:B""]" 1 Kd Kd = = 7.0 ± 0.2 µM 7000.0 [] unit_conversion 5.154901959985743 success True direct_binding Protein–peptide interaction between 14-3-3 and the selected B-Raf pSer365 peptide; the paper explicitly prints its K_D. 3 “The pSer365 peptide (sequence: 360-RDRSS(pS)APNVH-370, K_D = 7.0 ± 0.2 µM, Fig. S1A†) contains a histidine (His370) at the C-terminus of the peptide.” Page 4 maps the co-crystal structure to PDB ID 9F35. auto_single_measurement only accepted activity measurement [1] 1 structures\9F35\9F35_metadata.json point structures/9F35/9f35_protein.pdb structures/9F35/9f35_pocket.pdb structures/9F35/9f35_ligand.pdb structures/9F35/9f35_ligand.cif structures/9F35/9f35_complex.pdb structures/9F35/9f35_complex.cif 9F3G classic carbonic anhydrase XII human Na Na compound 9 (3-(cyclooctylamino)-2,6-difluoro-4-((3-hydroxypropyl)sulfonyl)-5-((4-hydroxybutyl)amino)benzenesulfonamide) "[""A1H91""]" 1 Kd Kd = = 91 nM 91.0 [] unit_conversion 7.040958607678906 success True direct_binding FTSA, 37 °C, pH 7.0; human recombinant CA isozymes. 4 Table 1 reports compound 9 Kd,obs = 91 nM for CA XII. Figure 3 identifies compound 9 as the CA XII complex with PDB ID 9F3G. auto_single_measurement only accepted activity measurement [1] 1 structures\9F3G\9F3G_metadata.json point structures/9F3G/9f3g_protein.pdb structures/9F3G/9f3g_pocket.pdb structures/9F3G/9f3g_ligand.sdf structures/9F3G/9f3g_ligand.pdb structures/9F3G/9f3g_ligand.cif structures/9F3G/9f3g_complex.pdb structures/9F3G/9f3g_complex.cif 9F3V classic RIPK2 (RIP2K) human kinase domain, residues 1-317 wild-type compound 37 (N399) "[""A1H90""]" 1 IC50 IC50 = = 1.52 ± 0.91 nM 1.52 [] unit_conversion 8.818156412055227 success True biochemical_inhibition ADP-Glo RIPK2 kinase assay measuring ADP formed during kinase activation; compound 37. Recombinant human RIPK2 residues 1–317 was used. 7 Table 4 reports compound 37 RIPK2 IC50 = 1.52 ± 0.91 nM. The experimental section describes recombinant human RIPK2 protein and the ADP-Glo RIPK2 kinase assay; Figure 6 identifies the RIPK2–compound 37 complex as PDB 9F3V. auto_single_measurement only accepted activity measurement [1] 1 structures\9F3V\9F3V_metadata.json point structures/9F3V/9f3v_protein.pdb structures/9F3V/9f3v_pocket.pdb structures/9F3V/9f3v_ligand.sdf structures/9F3V/9f3v_ligand.pdb structures/9F3V/9f3v_ligand.cif structures/9F3V/9f3v_complex.pdb structures/9F3V/9f3v_complex.cif 9F6B classic neuropilin-1 human NRP1 b1 domain Na 12d "[""A1IAT""]" 1 Kd Kd = = 0.65 ± 0.05 μM 650.0 [] unit_conversion 6.187086643357144 success True direct_binding SPR-derived equilibrium binding constant for compound 12d binding immobilized NRP1 b1 domain. 7 Table 1 reports for 12d (EG01440) an SPR NRP1 b1-domain equilibrium KD of 0.65 ± 0.05 μM. The text identifies 12d as the NRP1 b1 complex deposited as PDB 9F6B. auto_single_measurement only accepted activity measurement [1] 1 structures\9F6B\9F6B_metadata.json point structures/9F6B/9f6b_protein.pdb structures/9F6B/9f6b_pocket.pdb structures/9F6B/9f6b_ligand.sdf structures/9F6B/9f6b_ligand.pdb structures/9F6B/9f6b_ligand.cif structures/9F6B/9f6b_complex.pdb structures/9F6B/9f6b_complex.cif 9F8I classic PhzA/B (BcPhzB) Burkholderia cepacia R18194 Na Na 10d ((4-chlorophenyl)[6-hydroxy-2-(4-hydroxyphenyl)benzo[b]thiophen-3-yl]methanone) "[""A1IAE""]" 1 Kd Kd = = 1.64 ± 0.07 µM 1640.0 [] unit_conversion 5.785156151952302 success True direct_binding Isothermal titration calorimetry (ITC) of ligand binding to BcPhzB. 6 Figure 3C reports Kd for 10d with BcPhzB as 1.64 ± 0.07 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9F8I\9F8I_metadata.json point structures/9F8I/9f8i_protein.pdb structures/9F8I/9f8i_pocket.pdb structures/9F8I/9f8i_ligand.sdf structures/9F8I/9f8i_ligand.pdb structures/9F8I/9f8i_ligand.cif structures/9F8I/9f8i_complex.pdb structures/9F8I/9f8i_complex.cif 9F8L classic PhzA/B (BcPhzB) Burkholderia cepacia R18194 Na Na 10j ([6-hydroxy-2-(4-hydroxyphenyl)benzo[b]thiophen-3-yl](3-hydroxyphenyl)methanone) "[""A1IAL""]" 1 Kd Kd = = 1.34 ± 0.06 µM 1340.0 [] unit_conversion 5.872895201635192 success True direct_binding Isothermal titration calorimetry (ITC) of ligand binding to BcPhzB. 6 Figure 3C reports Kd for 10j with BcPhzB as 1.34 ± 0.06 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9F8L\9F8L_metadata.json point structures/9F8L/9f8l_protein.pdb structures/9F8L/9f8l_pocket.pdb structures/9F8L/9f8l_ligand.sdf structures/9F8L/9f8l_ligand.pdb structures/9F8L/9f8l_ligand.cif structures/9F8L/9f8l_complex.pdb structures/9F8L/9f8l_complex.cif 9F8P classic PhzA/B (BcPhzB) Burkholderia cepacia R18194 Na Na 13a ([6-hydroxy-2-(4-hydroxyphenyl)benzo[b]thiophen-3-yl](4-hydroxyphenyl)methanone) "[""A1IAI""]" 1 Kd Kd = = 2.17 ± 0.06 µM 2170.0 [] unit_conversion 5.66354026615147 success True direct_binding Isothermal titration calorimetry (ITC) of ligand binding to BcPhzB. 6 Figure 3C reports Kd for 13a with BcPhzB as 2.17 ± 0.06 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9F8P\9F8P_metadata.json point structures/9F8P/9f8p_protein.pdb structures/9F8P/9f8p_pocket.pdb structures/9F8P/9f8p_ligand.sdf structures/9F8P/9f8p_ligand.pdb structures/9F8P/9f8p_ligand.cif structures/9F8P/9f8p_complex.pdb structures/9F8P/9f8p_complex.cif 9F8Q classic PhzA/B (BcPhzB) Burkholderia cepacia R18194 Na Na 13d ([6-hydroxy-2-(4-hydroxyphenyl)benzo[b]thiophen-3-yl](2-hydroxyphenyl)methanone) "[""A1IAJ""]" 1 Kd Kd = = 0.92 ± 0.14 µM 920.0 [] unit_conversion 6.036212172654444 success True direct_binding Isothermal titration calorimetry (ITC) of ligand binding to BcPhzB. 6 Figure 3C reports Kd for 13d with BcPhzB as 0.92 ± 0.14 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9F8Q\9F8Q_metadata.json point structures/9F8Q/9f8q_protein.pdb structures/9F8Q/9f8q_pocket.pdb structures/9F8Q/9f8q_ligand.sdf structures/9F8Q/9f8q_ligand.pdb structures/9F8Q/9f8q_ligand.cif structures/9F8Q/9f8q_complex.pdb structures/9F8Q/9f8q_complex.cif 9F93 classic phenazine biosynthesis enzyme PhzF Pseudomonas synxantha 2-79 N-terminal His-tagged PsPhzF Na 2-amino-5-(4-fluorophenyl)benzoic acid (17c) "[""A1IAV""]" 1 Kd Kd = = 2180 ± 217 µM 2180000.0 [] unit_conversion 2.661543506395395 success True direct_binding Isothermal differential scanning fluorimetry (DSF) affinity determination of the 5-phenyl-substituted derivative. 9 Table 2 lists compound 17c with dissociation constant (Kd) 2180 ± 217 µM, determined by isothermal DSF. auto_single_measurement only accepted activity measurement [1] 1 structures\9F93\9F93_metadata.json point structures/9F93/9f93_protein.pdb structures/9F93/9f93_pocket.pdb structures/9F93/9f93_ligand.sdf structures/9F93/9f93_ligand.pdb structures/9F93/9f93_ligand.cif structures/9F93/9f93_complex.pdb structures/9F93/9f93_complex.cif 9F94 classic phenazine biosynthesis enzyme PhzF Pseudomonas synxantha 2-79 N-terminal His-tagged PsPhzF Na 2-amino-5-(3-hydroxyphenyl)benzoic acid (17e) "[""A1IAY""]" 1 Kd Kd = = 308 ± 40 µM 308000.0 [] unit_conversion 3.511449283499556 success True direct_binding Isothermal differential scanning fluorimetry (DSF) affinity determination of the 5-phenyl-substituted derivative. 9 Table 2 lists compound 17e with dissociation constant (Kd) 308 ± 40 µM, determined by isothermal DSF. auto_single_measurement only accepted activity measurement [1] 1 structures\9F94\9F94_metadata.json point structures/9F94/9f94_protein.pdb structures/9F94/9f94_pocket.pdb structures/9F94/9f94_ligand.sdf structures/9F94/9f94_ligand.pdb structures/9F94/9f94_ligand.cif structures/9F94/9f94_complex.pdb structures/9F94/9f94_complex.cif 9F95 classic phenazine biosynthesis enzyme PhzF Pseudomonas synxantha 2-79 N-terminal His-tagged PsPhzF Na 2-amino-3-hydroxy-5-(3-hydroxyphenyl)benzoic acid (19e) "[""A1IAU""]" 1 Kd Kd = = 764 ± 54 µM 764000.0 [] unit_conversion 3.1169066414243103 success True direct_binding Isothermal differential scanning fluorimetry (DSF) affinity determination of the 5-phenyl-substituted derivative. 9 Table 2 lists compound 19e with dissociation constant (Kd) 764 ± 54 µM, determined by isothermal DSF. auto_single_measurement only accepted activity measurement [1] 1 structures\9F95\9F95_metadata.json point structures/9F95/9f95_protein.pdb structures/9F95/9f95_pocket.pdb structures/9F95/9f95_ligand.sdf structures/9F95/9f95_ligand.pdb structures/9F95/9f95_ligand.cif structures/9F95/9f95_complex.pdb structures/9F95/9f95_complex.cif 9F96 classic phenazine biosynthesis enzyme PhzF Pseudomonas synxantha 2-79 N-terminal His-tagged PsPhzF Na 2-amino-3-ethoxybenzoic acid (15a) "[""A1IAW""]" 1 Kd Kd = = 15.6 ± 1.1 µM 15600.0 [] unit_conversion 4.806875401645539 success True direct_binding FRET-based affinity determination of the small 3-HAA derivative. 6 Table 1 lists compound 15a with dissociation constant (Kd) 15.6 ± 1.1 µM; footnote [a] states values were determined by FRET. auto_single_measurement only accepted activity measurement [1] 1 structures\9F96\9F96_metadata.json point structures/9F96/9f96_protein.pdb structures/9F96/9f96_pocket.pdb structures/9F96/9f96_ligand.sdf structures/9F96/9f96_ligand.pdb structures/9F96/9f96_ligand.cif structures/9F96/9f96_complex.pdb structures/9F96/9f96_complex.cif 9F99 classic MUS81-EME1 Na MUS81 residues 246-462 and EME1 residues 246-455, referred to as MUS81-EME1N truncation Na compound 10 "[""A1IA5""]" 2 Kd Kd = = 1.1 (0.52) µM 1100.0 [] unit_conversion 5.958607314841775 success True direct_binding Surface plasmon resonance (SPR); Table 1 reports geometric mean with geometric standard deviation in parentheses. 2 Table 1, compound 10: SPR Kd 1.1 (0.52) µM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9F99\9F99_metadata.json point structures/9F99/9f99_protein.pdb structures/9F99/9f99_pocket.pdb structures/9F99/9f99_ligand.sdf structures/9F99/9f99_ligand.pdb structures/9F99/9f99_ligand.cif structures/9F99/9f99_complex.pdb structures/9F99/9f99_complex.cif 9F9A classic MUS81-EME1 Na MUS81 residues 246-462 and EME1 residues 246-455, referred to as MUS81-EME1N truncation Na compound 12 "[""A1IA6""]" 2 Kd Kd = = 1.3 (0.72) µM 1300.0 [] unit_conversion 5.886056647693163 success True direct_binding Surface plasmon resonance (SPR); Table 1 reports geometric mean with geometric standard deviation in parentheses. 2 Table 1, compound 12: SPR Kd 1.3 (0.72) µM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9F9A\9F9A_metadata.json point structures/9F9A/9f9a_protein.pdb structures/9F9A/9f9a_pocket.pdb structures/9F9A/9f9a_ligand.sdf structures/9F9A/9f9a_ligand.pdb structures/9F9A/9f9a_ligand.cif structures/9F9A/9f9a_complex.pdb structures/9F9A/9f9a_complex.cif 9F9K classic MUS81-EME1 Na MUS81 residues 246-462 and EME1 residues 246-455, referred to as MUS81-EME1N truncation Na compound 15 "[""A1IA7""]" 2 Kd Kd = = 0.72 (0.83) µM 720.0 [] unit_conversion 6.142667503568731 success True direct_binding Surface plasmon resonance (SPR); Table 2 reports geometric mean with geometric standard deviation in parentheses. 3 Table 2, compound 15: SPR Kd 0.72 (0.83) µM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9F9K\9F9K_metadata.json point structures/9F9K/9f9k_protein.pdb structures/9F9K/9f9k_pocket.pdb structures/9F9K/9f9k_ligand.sdf structures/9F9K/9f9k_ligand.pdb structures/9F9K/9f9k_ligand.cif structures/9F9K/9f9k_complex.pdb structures/9F9K/9f9k_complex.cif 9F9L classic MUS81-EME1 Na MUS81 residues 246-462 and EME1 residues 246-455, referred to as MUS81-EME1N truncation Na compound 16 "[""A1IA8""]" 2 Kd Kd = = 0.54 (0.88) µM 540.0 [] unit_conversion 6.267606240177031 success True direct_binding Surface plasmon resonance (SPR); Table 1 reports geometric mean with geometric standard deviation in parentheses. 2 Table 1, compound 16: SPR Kd 0.54 (0.88) µM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9F9L\9F9L_metadata.json point structures/9F9L/9f9l_protein.pdb structures/9F9L/9f9l_pocket.pdb structures/9F9L/9f9l_ligand.sdf structures/9F9L/9f9l_ligand.pdb structures/9F9L/9f9l_ligand.cif structures/9F9L/9f9l_complex.pdb structures/9F9L/9f9l_complex.cif 9F9M classic MUS81-EME1 Na MUS81 residues 246-462 and EME1 residues 246-455, referred to as MUS81-EME1N truncation Na compound 21 "[""A1IA4""]" 2 Kd Kd = = 2.0 (0.77) µM 2000.0 [] unit_conversion 5.698970004336019 success True direct_binding Surface plasmon resonance (SPR); Table 3 reports geometric mean with geometric standard deviation in parentheses. 4 Table 3, compound 21: SPR Kd 2.0 (0.77) µM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9F9M\9F9M_metadata.json point structures/9F9M/9f9m_protein.pdb structures/9F9M/9f9m_pocket.pdb structures/9F9M/9f9m_ligand.sdf structures/9F9M/9f9m_ligand.pdb structures/9F9M/9f9m_ligand.cif structures/9F9M/9f9m_complex.pdb structures/9F9M/9f9m_complex.cif 9FA3 classic GCase (beta-glucocerebrosidase) Na Na Na Na "[""A1IBC""]" 1 Kd Kd = = 410 µM 410000.0 [] unit_conversion 3.3872161432802645 success True direct_binding ITC measurement of fragment 14 binding to GCase. 4 Table 1 reports compound 14 ITC Kd 410 µM; page 12 maps compound 14 to PDB 9FA3. auto_single_measurement only accepted activity measurement [1] 1 structures\9FA3\9FA3_metadata.json point structures/9FA3/9fa3_protein.pdb structures/9FA3/9fa3_pocket.pdb structures/9FA3/9fa3_ligand.sdf structures/9FA3/9fa3_ligand.pdb structures/9FA3/9fa3_ligand.cif structures/9FA3/9fa3_complex.pdb structures/9FA3/9fa3_complex.cif 9FAZ extended GCase (beta-glucocerebrosidase) Na Na Na Na "[""A1IBP""]" 1 Kd Kd = = 0.30 µM 300.0 [] unit_conversion 6.522878745280337 success True direct_binding ITC measurement of compound 24 binding to GCase. 6 Table 2 reports compound 24 ITC Kd 0.30 µM; page 12 maps compound 24 to PDB 9FAZ. auto_single_measurement only accepted activity measurement [1] 1 structures\9FAZ\9FAZ_metadata.json point structures/9FAZ/9faz_protein.pdb structures/9FAZ/9faz_pocket.pdb structures/9FAZ/9faz_ligand.pdb structures/9FAZ/9faz_ligand.cif structures/9FAZ/9faz_complex.pdb structures/9FAZ/9faz_complex.cif 9FBX classic BRD2 human Na Na compound 42; 5-(1-benzyl-4-chloro-1H-imidazol-2-yl)-1,3-dimethylpyridin-2(1H)-one "[""A1IBV""]" 1 pIC50 IC50 = = 6.6 unitless 251.18864315095823 [] p_metric_transform 6.6 success True biochemical_inhibition BRD2 BD2 TR-FRET assay; Table 1 reports BRD4 BD1/BD2 TR-FRET pIC50 values of 7.5/6.6 for compound 42. 8 Table 1, compound 42: “BRD4 BD1/BD2 TR-FRET pIC50” = “7.5 / 6.6”; the paper identifies 42 as the ligand in the BRD2 BD2 structure 9fbx. auto_single_measurement only accepted activity measurement [1] 1 structures\9FBX\9FBX_metadata.json point structures/9FBX/9fbx_protein.pdb structures/9FBX/9fbx_pocket.pdb structures/9FBX/9fbx_ligand.sdf structures/9FBX/9fbx_ligand.pdb structures/9FBX/9fbx_ligand.cif structures/9FBX/9fbx_complex.pdb structures/9FBX/9fbx_complex.cif 9FBY classic BRD4 human Na Na compound 70; 5-(4-chloro-1-((tetrahydro-2H-pyran-4-yl)methyl)-1H-imidazol-2-yl)-1,3-dimethylpyridin-2(1H)-one "[""A1IB5""]" 2 pKd Kd = = 7.4 unitless 39.81071705534969 [] p_metric_transform 7.4 success True direct_binding BRD4 BD1 isothermal titration calorimetry (ITC) direct-binding measurement for compound 70. 12 Table 4, compound 70: “BRD4 BD1 ITC pKd” = “7.4”. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9FBY\9FBY_metadata.json point structures/9FBY/9fby_protein.pdb structures/9FBY/9fby_pocket.pdb structures/9FBY/9fby_ligand.sdf structures/9FBY/9fby_ligand.pdb structures/9FBY/9fby_ligand.cif structures/9FBY/9fby_complex.pdb structures/9FBY/9fby_complex.cif 9FD4 classic flavin reductase ThdF Streptomyces albogriseolus Proteolytically processed ThdF, modeled as residues 7-167 Na FAD; FAD "[""FAD""]" 1 Kd Kd = = 6.8 ± 0.2 µM 6800.0 [] unit_conversion 5.167491087293763 success True direct_binding Fluorescence-anisotropy binding of FAD to apoThdF; cooperative binding model. 9 Fitting the FAD binding curve gave a dissociation constant of 6.8 ± 0.2 µM for binding of FAD to ThdF. auto_single_measurement only accepted activity measurement [1] 1 structures\9FD4\9FD4_metadata.json point structures/9FD4/9fd4_protein.pdb structures/9FD4/9fd4_pocket.pdb structures/9FD4/9fd4_ligand.sdf structures/9FD4/9fd4_ligand.pdb structures/9FD4/9fd4_ligand.cif structures/9FD4/9fd4_complex.pdb structures/9FD4/9fd4_complex.cif 9FD5 classic flavin reductase ThdF Streptomyces albogriseolus Proteolytically processed ThdF, modeled as residues 7-167 Na FAD; FAD "[""FAD""]" 1 Kd Kd = = 6.8 ± 0.2 µM 6800.0 [] unit_conversion 5.167491087293763 success True direct_binding Fluorescence-anisotropy binding of FAD to apoThdF; cooperative binding model. 9 Fitting the FAD binding curve gave a dissociation constant of 6.8 ± 0.2 µM for binding of FAD to ThdF. auto_single_measurement only accepted activity measurement [1] 1 structures\9FD5\9FD5_metadata.json point structures/9FD5/9fd5_protein.pdb structures/9FD5/9fd5_pocket.pdb structures/9FD5/9fd5_ligand.sdf structures/9FD5/9fd5_ligand.pdb structures/9FD5/9fd5_ligand.cif structures/9FD5/9fd5_complex.pdb structures/9FD5/9fd5_complex.cif 9FDB classic Galectin-3 human Na Na compound 4 "[""A1IB3""]" 1 IC50 IC50 = = 412 nM 412.0 [] unit_conversion 6.3851027839668655 success True biochemical_inhibition Asialofetuin (ASF) competitive binding assay; Table 1 reports hGal-3 IC50. 3 Table 1 lists compound 4 with hGal-3 IC50 412 [2.05] nM; the text identifies the assay as an ASF competitive binding assay. Figure 4 maps compound 4 to PDB 9FDB. auto_single_measurement only accepted activity measurement [1] 1 structures\9FDB\9FDB_metadata.json point structures/9FDB/9fdb_protein.pdb structures/9FDB/9fdb_pocket.pdb structures/9FDB/9fdb_ligand.sdf structures/9FDB/9fdb_ligand.pdb structures/9FDB/9fdb_ligand.cif structures/9FDB/9fdb_complex.pdb structures/9FDB/9fdb_complex.cif 9FDC classic Galectin-3 human Na Na compound 3 "[""A1IB4""]" 1 IC50 IC50 = = 82 nM 82.0 [] unit_conversion 7.086186147616283 success True biochemical_inhibition Asialofetuin (ASF) competitive binding assay; Table 1 reports hGal-3 IC50. 3 Table 1 lists compound 3 with hGal-3 IC50 82 [1.27] nM; the text identifies the assay as an ASF competitive binding assay. Figure 4 maps compound 3 to PDB 9FDC. auto_single_measurement only accepted activity measurement [1] 1 structures\9FDC\9FDC_metadata.json point structures/9FDC/9fdc_protein.pdb structures/9FDC/9fdc_pocket.pdb structures/9FDC/9fdc_ligand.sdf structures/9FDC/9fdc_ligand.pdb structures/9FDC/9fdc_ligand.cif structures/9FDC/9fdc_complex.pdb structures/9FDC/9fdc_complex.cif 9FDT classic human Sirt2 human human Sirt2_56-356; His10 tag cleaved before crystallization Na compound 2 (pyrazole-based fragment inhibitor) "[""A1IBW""]" 1 IC50 IC50 = = 458 ± 54 µM 458000.0 [] unit_conversion 3.3391345219961304 success True biochemical_inhibition Fluorescence-polarization inhibition assay using human Sirt2(56–356) and SirReal–TAMRA; compound 2 is the pyrazole-based fragment inhibitor. 4 Figure 3B identifies the Sirt2–2 complex as PDB 9FDT and prints “IC50 = 458 ± 54 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9FDT\9FDT_metadata.json point structures/9FDT/9fdt_protein.pdb structures/9FDT/9fdt_pocket.pdb structures/9FDT/9fdt_ligand.sdf structures/9FDT/9fdt_ligand.pdb structures/9FDT/9fdt_ligand.cif structures/9FDT/9fdt_complex.pdb structures/9FDT/9fdt_complex.cif 9FDU classic human Sirt2 human human Sirt2_56-356; His10 tag cleaved before crystallization Na compound 1 (pyridine-3-carbothioamide-based fragment inhibitor) "[""A1IBX""]" 1 IC50 IC50 = = 286 ± 10 µM 286000.0 [] unit_conversion 3.5436339668709573 success True biochemical_inhibition Fluorescence-polarization inhibition assay using human Sirt2(56–356) and SirReal–TAMRA; compound 1 is the pyridine-3-carbothioamide fragment inhibitor. 4 Figure 3A identifies the Sirt2–1 complex as PDB 9FDU and prints “IC50 = 286 ± 10 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9FDU\9FDU_metadata.json point structures/9FDU/9fdu_protein.pdb structures/9FDU/9fdu_pocket.pdb structures/9FDU/9fdu_ligand.sdf structures/9FDU/9fdu_ligand.pdb structures/9FDU/9fdu_ligand.cif structures/9FDU/9fdu_complex.pdb structures/9FDU/9fdu_complex.cif 9FDW classic human Sirt2 human human Sirt2_56-356; His10 tag cleaved before crystallization Na compound 3 (3-chlorobenzamide-based fragment inhibitor) "[""A1IBY""]" 1 IC50 IC50 = = 565 ± 95 µM 565000.0 [] unit_conversion 3.2479515521805613 success True biochemical_inhibition Fluorescence-polarization inhibition assay using human Sirt2(56–356) and SirReal–TAMRA; compound 3 is the 3-chlorobenzamide-based fragment inhibitor. 4 Figure 3C identifies the Sirt2–3 complex as PDB 9FDW and prints “IC50 = 565 ± 95 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9FDW\9FDW_metadata.json point structures/9FDW/9fdw_protein.pdb structures/9FDW/9fdw_pocket.pdb structures/9FDW/9fdw_ligand.sdf structures/9FDW/9fdw_ligand.pdb structures/9FDW/9fdw_ligand.cif structures/9FDW/9fdw_complex.pdb structures/9FDW/9fdw_complex.cif 9FEG classic PARP15 Na residues 481-678 Na EXQ-1e (compound 49) "[""A1H44""]" 1 pIC50 IC50 = = 6.47 ± 0.03 unitless 338.84415613920277 [] p_metric_transform 6.47 success True biochemical_inhibition PARP/TNKS profiling biochemical activity assay; Table 4 reports pIC50 ± SEM (n = 3). 8 Table 4 reports EXQ-1e (49) against PARP15: pIC50 = 6.47 ± 0.03 (n = 3). Figure 3 identifies the EXQ-1e–PARP15 crystal structure as PDB 9FEG. auto_single_measurement only accepted activity measurement [1] 1 structures\9FEG\9FEG_metadata.json point structures/9FEG/9feg_protein.pdb structures/9FEG/9feg_pocket.pdb structures/9FEG/9feg_ligand.sdf structures/9FEG/9feg_ligand.pdb structures/9FEG/9feg_ligand.cif structures/9FEG/9feg_complex.pdb structures/9FEG/9feg_complex.cif 9FF8 classic Human transthyretin (TTR) human recombinant wild-type TTR wild-type (wt-TTR) 1d; Lic166; (E)-2-((((2-chlorobenzyl)oxy)imino)methyl)benzoic acid "[""A1ICF""]" 2 Kd Kd = = 480 ± 160 nM 480.0 [] unit_conversion 6.318758762624412 success True direct_binding Isothermal titration calorimetry (ITC) of compound 1d with recombinant wt-TTR. 7 Table 2 reports the ITC Kd for compound 1d with TTR WT as 480 ± 160 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9FF8\9FF8_metadata.json point structures/9FF8/9ff8_protein.pdb structures/9FF8/9ff8_pocket.pdb structures/9FF8/9ff8_ligand.sdf structures/9FF8/9ff8_ligand.pdb structures/9FF8/9ff8_ligand.cif structures/9FF8/9ff8_complex.pdb structures/9FF8/9ff8_complex.cif 9FHA classic Human transthyretin (TTR) human recombinant wild-type TTR wild-type (wt-TTR) 1a; (E)-2-((((2-(trifluoromethyl)benzyl)oxy)imino)methyl)benzoic acid "[""A1IC9""]" 2 Kd Kd = = 450 ± 120 nM 450.0 [] unit_conversion 6.346787486224656 success True direct_binding Isothermal titration calorimetry (ITC) of compound 1a with recombinant wt-TTR. 7 Table 2 reports the ITC Kd for compound 1a with TTR WT as 450 ± 120 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9FHA\9FHA_metadata.json point structures/9FHA/9fha_protein.pdb structures/9FHA/9fha_pocket.pdb structures/9FHA/9fha_ligand.sdf structures/9FHA/9fha_ligand.pdb structures/9FHA/9fha_ligand.cif structures/9FHA/9fha_complex.pdb structures/9FHA/9fha_complex.cif 9FHD extended hKHK-C Na Na Na BI-9787; compound 8 "[""A1ICK""]" 1 IC50 IC50 = = 12.8 nM 12.8 [] unit_conversion 7.892790030352131 success True biochemical_inhibition hKHK-C enzymatic inhibition assay (Table 2). 6 Table 2 reports compound 8 (BI-9787) with hKHK-C IC50 = 12.8 nM; the text explicitly identifies compound 8 as BI-9787 and its X-ray co-crystal structure as PDB 9FHD. auto_single_measurement only accepted activity measurement [1] 1 structures\9FHD\9FHD_metadata.json point structures/9FHD/9fhd_protein.pdb structures/9FHD/9fhd_pocket.pdb structures/9FHD/9fhd_ligand.pdb structures/9FHD/9fhd_ligand.cif structures/9FHD/9fhd_complex.pdb structures/9FHD/9fhd_complex.cif 9FHE extended hKHK-C Na Na Na BI-9787; compound 8 "[""A1ICK""]" 1 IC50 IC50 = = 12.8 nM 12.8 [] unit_conversion 7.892790030352131 success True biochemical_inhibition hKHK-C enzymatic inhibition assay (Table 2); PDB 9FHE is the pH 5.5 crystal form. 6 Table 2 reports compound 8 (BI-9787) with hKHK-C IC50 = 12.8 nM. The text identifies the pH 5.5 crystal form of compound 8 as PDB 9FHE. auto_single_measurement only accepted activity measurement [1] 1 structures\9FHE\9FHE_metadata.json point structures/9FHE/9fhe_protein.pdb structures/9FHE/9fhe_pocket.pdb structures/9FHE/9fhe_ligand.pdb structures/9FHE/9fhe_ligand.cif structures/9FHE/9fhe_complex.pdb structures/9FHE/9fhe_complex.cif 9FIO classic USP7 human N-terminal double His-tagged catalytic domain, residues 208-560 Na compound 1 "[""R4D""]" 1 Ki Ki = = 12 μM 12000.0 [] unit_conversion 4.920818753952375 success True biochemical_inhibition FLINT purified-protein USP7 inhibition assay; double-His-tagged USP7(208–560)(C315A) was used for the functional assay. 2 Figure 1 assigns compound 1 to PDB 9FIO, and the text states that compound 1 registered 12 μM in the FLINT assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9FIO\9FIO_metadata.json point structures/9FIO/9fio_protein.pdb structures/9FIO/9fio_pocket.pdb structures/9FIO/9fio_ligand.sdf structures/9FIO/9fio_ligand.pdb structures/9FIO/9fio_ligand.cif structures/9FIO/9fio_complex.pdb structures/9FIO/9fio_complex.cif 9FIP classic USP7 human N-terminal double His-tagged catalytic domain, residues 208-560 Na compound 15 "[""A1ICU""]" 1 Ki Ki = = 0.240 μM 240.0 [] unit_conversion 6.619788758288394 success True biochemical_inhibition FLINT purified-protein USP7 inhibition assay; double-His-tagged USP7(208–560)(C315A) was used for the functional assay. 4 Table 3 reports compound 15 FLINT Ki = 0.240 μM; Figure 2 assigns compound 15 to PDB 9FIP. auto_single_measurement only accepted activity measurement [1] 1 structures\9FIP\9FIP_metadata.json point structures/9FIP/9fip_protein.pdb structures/9FIP/9fip_pocket.pdb structures/9FIP/9fip_ligand.sdf structures/9FIP/9fip_ligand.pdb structures/9FIP/9fip_ligand.cif structures/9FIP/9fip_complex.pdb structures/9FIP/9fip_complex.cif 9FIQ classic USP7 human N-terminal double His-tagged catalytic domain, residues 208-560 Na compound 16 "[""A1ICV""]" 1 Ki Ki = = 0.190 μM 190.0 [] unit_conversion 6.721246399047171 success True biochemical_inhibition FLINT purified-protein USP7 inhibition assay; double-His-tagged USP7(208–560)(C315A) was used for the functional assay. 4 Table 3 reports compound 16 FLINT Ki = 0.190 μM; Figure 2 assigns compound 16 to PDB 9FIQ. auto_single_measurement only accepted activity measurement [1] 1 structures\9FIQ\9FIQ_metadata.json point structures/9FIQ/9fiq_protein.pdb structures/9FIQ/9fiq_pocket.pdb structures/9FIQ/9fiq_ligand.sdf structures/9FIQ/9fiq_ligand.pdb structures/9FIQ/9fiq_ligand.cif structures/9FIQ/9fiq_complex.pdb structures/9FIQ/9fiq_complex.cif 9FIR classic USP7 human N-terminal double His-tagged catalytic domain, residues 208-560 Na compound 17 "[""A1ICS""]" 1 Ki Ki = = 1.28 μM 1280.0 [] unit_conversion 5.892790030352131 success True biochemical_inhibition FLINT purified-protein USP7 inhibition assay; double-His-tagged USP7(208–560)(C315A) was used for the functional assay. 4 Table 3 reports compound 17 FLINT Ki = 1.28 μM; Figure 2 assigns compound 17 to PDB 9FIR. auto_single_measurement only accepted activity measurement [1] 1 structures\9FIR\9FIR_metadata.json point structures/9FIR/9fir_protein.pdb structures/9FIR/9fir_pocket.pdb structures/9FIR/9fir_ligand.sdf structures/9FIR/9fir_ligand.pdb structures/9FIR/9fir_ligand.cif structures/9FIR/9fir_complex.pdb structures/9FIR/9fir_complex.cif 9FJQ classic human carbonic anhydrase II human Na Na compound 7j (4-benzyl-5,7,8-trifluoro-3,4-dihydro-2H-benzo[b][1,4]thiazine-6-sulfonamide 1,1-dioxide) "[""A1IDL""]" 1 Kd Kd = = 50 nM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding Fluorescent thermal shift assay (FTSA) using purified recombinant human CA isozymes. 6 Table 1 lists compound 7j with CAII Kd = 50 nM; the table states dissociation constants were obtained by FTSA. auto_single_measurement only accepted activity measurement [1] 1 structures\9FJQ\9FJQ_metadata.json point structures/9FJQ/9fjq_protein.pdb structures/9FJQ/9fjq_pocket.pdb structures/9FJQ/9fjq_ligand.sdf structures/9FJQ/9fjq_ligand.pdb structures/9FJQ/9fjq_ligand.cif structures/9FJQ/9fjq_complex.pdb structures/9FJQ/9fjq_complex.cif 9FJV classic human carbonic anhydrase II human Na Na compound 7f (4-(cyclooctylmethyl)-5,7,8-trifluoro-3,4-dihydro-2H-benzo[b][1,4]thiazine-6-sulfonamide 1,1-dioxide) "[""A1IDN""]" 1 Kd Kd = = 200 nM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Fluorescent thermal shift assay (FTSA) using purified recombinant human CA isozymes. 6 Table 1 lists compound 7f with CAII Kd = 200 nM; the table states dissociation constants were obtained by FTSA. auto_single_measurement only accepted activity measurement [1] 1 structures\9FJV\9FJV_metadata.json point structures/9FJV/9fjv_protein.pdb structures/9FJV/9fjv_pocket.pdb structures/9FJV/9fjv_ligand.sdf structures/9FJV/9fjv_ligand.pdb structures/9FJV/9fjv_ligand.cif structures/9FJV/9fjv_complex.pdb structures/9FJV/9fjv_complex.cif 9FKD classic DB3 Fab; DBPro1156_2 Na Chimeric DB3 Fab; anti-kappa light-chain Fab; computationally designed DBPro1156_2 Y12W; S16G Progesterone "[""STR""]" 1 Kd Kd = = 18 nM 18.0 [] unit_conversion 7.7447274948966935 success True direct_binding Bio-layer interferometry measurement of DBPro1156_2 binding to DB3 Fab in the presence of progesterone. 6 Fig. 4b labels DBPro1156_2, reports progesterone Kd = 18 nM, and states that measurements were obtained by bio-layer interferometry in the presence or absence of the respective small molecule. The adjacent text identifies Y12W and S16G in DBPro1156_2. auto_single_measurement only accepted activity measurement [1] 1 structures\9FKD\9FKD_metadata.json point structures/9FKD/9fkd_protein.pdb structures/9FKD/9fkd_pocket.pdb structures/9FKD/9fkd_ligand.sdf structures/9FKD/9fkd_ligand.pdb structures/9FKD/9fkd_ligand.cif structures/9FKD/9fkd_complex.pdb structures/9FKD/9fkd_complex.cif 9FKR classic KAT6A Na Na Na BAY-184; compound 29 "[""A1IDR""]" 1 IC50 IC50 = = 71 nM 71.0 [] unit_conversion 7.1487416512809245 success True biochemical_inhibition KAT6A biochemical activity, TR-FRET HAT-domain assay. 11 “BAY-184 (29) exhibited a dose-dependent inhibition of KAT6A activity, yielding an IC50 of 71 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9FKR\9FKR_metadata.json point structures/9FKR/9fkr_protein.pdb structures/9FKR/9fkr_pocket.pdb structures/9FKR/9fkr_ligand.sdf structures/9FKR/9fkr_ligand.pdb structures/9FKR/9fkr_ligand.cif structures/9FKR/9fkr_complex.pdb structures/9FKR/9fkr_complex.cif 9FL8 extended NOT9-NOT1 complex Na Na Na NIP-2-Ac "[""POLYMER_ENTITY:1""]" 1 IC50 IC50 = = 450 ± 46 nM 450.0 [] unit_conversion 6.346787486224656 success True biochemical_inhibition Competitive fluorescence-polarization assay in which NIP-2-Ac competed with fluorescent NIP-WT-F for purified NOT9-NOT1 complex binding. 3 Figure 2D reports an IC50 of 450 ± 46 nM for NIP-2-Ac; the caption specifies competitive fluorescence polarization against NIP-WT-F bound to NOT9-NOT1. auto_single_measurement only accepted activity measurement [1] 1 structures\9FL8\9FL8_metadata.json point structures/9FL8/9fl8_protein.pdb structures/9FL8/9fl8_pocket.pdb structures/9FL8/9fl8_ligand.pdb structures/9FL8/9fl8_ligand.cif structures/9FL8/9fl8_complex.pdb structures/9FL8/9fl8_complex.cif 9FLB classic Haspin (GSG2) Na Na Na MU1464 "[""A1IDB""]" 1 IC50 IC50 = = 89 nM 89.0 [] unit_conversion 7.050609993355087 success True biochemical_inhibition Radiometric kinase assay at ATP concentration Km (Eurofins). 4 Table 1 reports compound 4 (MU1464) Haspin IC50 = 89 nM; table caption specifies radiometric assays at ATP concentrations at Km (Eurofins). Figure 2 also prints IC50 (Haspin) = 89 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9FLB\9FLB_metadata.json point structures/9FLB/9flb_protein.pdb structures/9FLB/9flb_pocket.pdb structures/9FLB/9flb_ligand.sdf structures/9FLB/9flb_ligand.pdb structures/9FLB/9flb_ligand.cif structures/9FLB/9flb_complex.pdb structures/9FLB/9flb_complex.cif 9FLC classic Haspin (GSG2) Na Na Na MU1668 "[""A1IDA""]" 1 IC50 IC50 = = 212 nM 212.0 [] unit_conversion 6.673664139071249 success True biochemical_inhibition Radiometric kinase assay at ATP concentration Km (Eurofins). 4 Table 1 reports compound 5 (MU1668) Haspin IC50 = 212 nM; table caption specifies radiometric assays at ATP concentrations at Km (Eurofins). Figure 2 also prints IC50 (Haspin) = 212 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9FLC\9FLC_metadata.json point structures/9FLC/9flc_protein.pdb structures/9FLC/9flc_pocket.pdb structures/9FLC/9flc_ligand.sdf structures/9FLC/9flc_ligand.pdb structures/9FLC/9flc_ligand.cif structures/9FLC/9flc_complex.pdb structures/9FLC/9flc_complex.cif 9FLR extended Human Haspin (GSG2) kinase Homo sapiens Na Na MU1963 "[""A1IDE""]" 1 IC50 IC50 = = 60 nM 60.0 [] unit_conversion 7.221848749616356 success True biochemical_inhibition Haspin inhibition; Figure 2 compares compounds tested in a 413-human-kinase panel at ATP concentrations at Km (Eurofins). 5 Figure 2 identifies compound 3 as MU1963 and prints IC50 (Haspin) = 60 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9FLR\9FLR_metadata.json point structures/9FLR/9flr_protein.pdb structures/9FLR/9flr_pocket.pdb structures/9FLR/9flr_ligand.pdb structures/9FLR/9flr_ligand.cif structures/9FLR/9flr_complex.pdb structures/9FLR/9flr_complex.cif 9FLT classic Human Haspin (GSG2) kinase Homo sapiens Na Na MU1920 "[""A1IDF""]" 1 IC50 IC50 = = 6 nM 6.0 [] unit_conversion 8.221848749616356 success True biochemical_inhibition Radiometric kinase assay at ATP concentration Km (Eurofins). 4 Table 1 reports compound 9 (MU1920) Haspin IC50 = 6 nM; table caption specifies radiometric assays at ATP concentrations at Km (Eurofins). Figure 3 also prints IC50 (Haspin) = 6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9FLT\9FLT_metadata.json point structures/9FLT/9flt_protein.pdb structures/9FLT/9flt_pocket.pdb structures/9FLT/9flt_ligand.sdf structures/9FLT/9flt_ligand.pdb structures/9FLT/9flt_ligand.cif structures/9FLT/9flt_complex.pdb structures/9FLT/9flt_complex.cif 9FN7 classic human carbonic anhydrase XII human Na Na compound 7c (5,7,8-trifluoro-4-(3-propylhexyl)-3,4-dihydro-2H-benzo[b][1,4]thiazine-6-sulfonamide 1,1-dioxide) "[""A1ID0""]" 1 Kd Kd = = 80 nM 80.0 [] unit_conversion 7.096910013008056 success True direct_binding Fluorescent thermal shift assay (FTSA) using purified recombinant human CA isozymes. 6 Table 1 lists compound 7c with CAXII Kd = 80 nM; the table states dissociation constants were obtained by FTSA. auto_single_measurement only accepted activity measurement [1] 1 structures\9FN7\9FN7_metadata.json point structures/9FN7/9fn7_protein.pdb structures/9FN7/9fn7_pocket.pdb structures/9FN7/9fn7_ligand.sdf structures/9FN7/9fn7_ligand.pdb structures/9FN7/9fn7_ligand.cif structures/9FN7/9fn7_complex.pdb structures/9FN7/9fn7_complex.cif 9FN8 classic human carbonic anhydrase XII human Na Na compound 7j (4-benzyl-5,7,8-trifluoro-3,4-dihydro-2H-benzo[b][1,4]thiazine-6-sulfonamide 1,1-dioxide) "[""A1IDL""]" 1 Kd Kd = = 20 nM 20.0 [] unit_conversion 7.698970004336019 success True direct_binding Fluorescent thermal shift assay (FTSA) using purified recombinant human CA isozymes. 6 Table 1 lists compound 7j with CAXII Kd = 20 nM; the table states dissociation constants were obtained by FTSA. auto_single_measurement only accepted activity measurement [1] 1 structures\9FN8\9FN8_metadata.json point structures/9FN8/9fn8_protein.pdb structures/9FN8/9fn8_pocket.pdb structures/9FN8/9fn8_ligand.sdf structures/9FN8/9fn8_ligand.pdb structures/9FN8/9fn8_ligand.cif structures/9FN8/9fn8_complex.pdb structures/9FN8/9fn8_complex.cif 9FOA classic streptavidin Na wild type streptavidin WT (wild type) PC1; anthraquinone cofactor "[""A1ID2""]" 1 Kd Kd = = 38 nM 38.0 [] unit_conversion 7.42021640338319 success True direct_binding ITC determination of biotinylated cofactor binding to Sav. 7 All three cofactors were strong binders, with dissociation constants (Kd) of 38 nM, 41 nM, and 70 nM, respectively, for PC1, Mn1, and Ni5. auto_single_measurement only accepted activity measurement [1] 1 structures\9FOA\9FOA_metadata.json point structures/9FOA/9foa_protein.pdb structures/9FOA/9foa_pocket.pdb structures/9FOA/9foa_ligand.sdf structures/9FOA/9foa_ligand.pdb structures/9FOA/9foa_ligand.cif structures/9FOA/9foa_complex.pdb structures/9FOA/9foa_complex.cif 9FOZ classic human IDO human Na Na (R)-100; imidazo[1,5-a]pyrazine "[""A1H93""]" 1 IC50 IC50 = = 6.4 nM 6.4 [] unit_conversion 8.193820026016112 success True biochemical_inhibition Human IDO1 enzymatic potency; geometric mean of at least two replicates. 12 Table 11 reports (R)-100 with human IDO1 enzymatic IC50 = 6.4 nM; the same page identifies the human IDO1-bound structure of (R)-100 as PDB 9FOZ. auto_single_measurement only accepted activity measurement [1] 1 structures\9FOZ\9FOZ_metadata.json point structures/9FOZ/9foz_protein.pdb structures/9FOZ/9foz_pocket.pdb structures/9FOZ/9foz_ligand.sdf structures/9FOZ/9foz_ligand.pdb structures/9FOZ/9foz_ligand.cif structures/9FOZ/9foz_complex.pdb structures/9FOZ/9foz_complex.cif 9FPE extended Purine Nucleoside Phosphorylase Escherichia coli Na wild type N2,3-etheno-2-aminopurine (N2,3-e2APu) "[""A1IEC""]" 1 Kd Kd = = 36.16 µM 36160.0 [] unit_conversion 4.441771578196675 success True direct_binding Isothermal titration calorimetry; one-binding-site model fitted to E. coli WT PNP titrations. 9 “Finally, for the N²,3-ε2APu (II), we obtained Kd = 36.16 µM, with the asymmetric confidence intervals (29.33–45.89) µM.” The preceding figure caption identifies the assay as calorimetric titrations of E. coli WT PNP with N²,3-ε2APu. auto_single_measurement only accepted activity measurement [1] 1 structures\9FPE\9FPE_metadata.json point structures/9FPE/9fpe_protein.pdb structures/9FPE/9fpe_pocket.pdb structures/9FPE/9fpe_ligand.pdb structures/9FPE/9fpe_ligand.cif structures/9FPE/9fpe_complex.pdb structures/9FPE/9fpe_complex.cif 9FQD classic Pseudomonas aeruginosa Elastase Pseudomonas aeruginosa Na Na compound 9 "[""A1IEX""]" 1 IC50 IC50 = = 5.1 ± 0.2 nM 5.1 [] unit_conversion 8.292429823902063 success True biochemical_inhibition LasB inhibition assay, Table 1. 4 Table 1 prints IC50 = 5.1 ± 0.2 nM for compound 9; Figure 2 maps compound 9 to PDB 9FQD. auto_single_measurement only accepted activity measurement [1] 1 structures\9FQD\9FQD_metadata.json point structures/9FQD/9fqd_protein.pdb structures/9FQD/9fqd_pocket.pdb structures/9FQD/9fqd_ligand.sdf structures/9FQD/9fqd_ligand.pdb structures/9FQD/9fqd_ligand.cif structures/9FQD/9fqd_complex.pdb structures/9FQD/9fqd_complex.cif 9FQH classic E3 ligase Cbl-b Na Na Na compound 1 "[""A1IEW""]" 1 IC50 IC50 = = 0.011 μM 11.0 [] unit_conversion 7.958607314841775 success True direct_binding Cbl-b TR-FRET probe displacement assay; average of at least two determinations. 3 Table 1 reports compound 1 Cbl-b TR-FRET IC50 = 0.011 μM; Figure 2 identifies compound 1 crystal structure as PDB 9FQH. auto_single_measurement only accepted activity measurement [1] 1 structures\9FQH\9FQH_metadata.json point structures/9FQH/9fqh_protein.pdb structures/9FQH/9fqh_pocket.pdb structures/9FQH/9fqh_ligand.sdf structures/9FQH/9fqh_ligand.pdb structures/9FQH/9fqh_ligand.cif structures/9FQH/9fqh_complex.pdb structures/9FQH/9fqh_complex.cif 9FQI extended E3 ligase Cbl-b Na Na Na compound 7 "[""A1IEV""]" 1 IC50 IC50 = = 1.2 μM 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding Cbl-b TR-FRET probe displacement assay; average of at least two determinations. 4 Table 2 reports compound 7 Cbl-b TR-FRET IC50 = 1.2 μM; Figure 3 identifies compound 7 crystal structure as PDB 9FQI. auto_single_measurement only accepted activity measurement [1] 1 structures\9FQI\9FQI_metadata.json point structures/9FQI/9fqi_protein.pdb structures/9FQI/9fqi_pocket.pdb structures/9FQI/9fqi_ligand.pdb structures/9FQI/9fqi_ligand.cif structures/9FQI/9fqi_complex.pdb structures/9FQI/9fqi_complex.cif 9FQJ classic E3 ligase Cbl-b Na Na Na compound 12 "[""A1IE5""]" 1 IC50 IC50 = = 4.8 μM 4800.0 [] unit_conversion 5.318758762624412 success True direct_binding Cbl-b TR-FRET probe displacement assay; average of at least two determinations. 5 Table 3 reports compound 12 Cbl-b TR-FRET IC50 = 4.8 μM; Figure 3 identifies compound 12 crystal structure as PDB 9FQJ. auto_single_measurement only accepted activity measurement [1] 1 structures\9FQJ\9FQJ_metadata.json point structures/9FQJ/9fqj_protein.pdb structures/9FQJ/9fqj_pocket.pdb structures/9FQJ/9fqj_ligand.sdf structures/9FQJ/9fqj_ligand.pdb structures/9FQJ/9fqj_ligand.cif structures/9FQJ/9fqj_complex.pdb structures/9FQJ/9fqj_complex.cif 9FQL extended hDM2 Na Na Na compound 3 "[""POLYMER_ENTITY:2""]" 1 IC50 IC50 = = 54 ± 17 nM 54.0 [] unit_conversion 7.267606240177031 success True biochemical_inhibition TR-FRET inhibition of the p53-hDM2 interaction at 100 nM. 2 Compound 3 was reported to inhibit the interaction with hDM2 with an IC50 of 54 ± 17 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9FQL\9FQL_metadata.json point structures/9FQL/9fql_protein.pdb structures/9FQL/9fql_pocket.pdb structures/9FQL/9fql_ligand.pdb structures/9FQL/9fql_ligand.cif structures/9FQL/9fql_complex.pdb structures/9FQL/9fql_complex.cif 9FQY classic Pseudomonas aeruginosa Elastase Pseudomonas aeruginosa Na Na compound 31 "[""A1IFN""]" 1 IC50 IC50 = = 21.7 ± 0.6 nM 21.7 [] unit_conversion 7.66354026615147 success True biochemical_inhibition LasB inhibition assay, Table 2. 6 Table 2 prints IC50 = 21.7 ± 0.6 nM for compound 31; Figure 2 maps compound 31 to PDB 9FQY. auto_single_measurement only accepted activity measurement [1] 1 structures\9FQY\9FQY_metadata.json point structures/9FQY/9fqy_protein.pdb structures/9FQY/9fqy_pocket.pdb structures/9FQY/9fqy_ligand.sdf structures/9FQY/9fqy_ligand.pdb structures/9FQY/9fqy_ligand.cif structures/9FQY/9fqy_complex.pdb structures/9FQY/9fqy_complex.cif 9FRV classic arginase 2 (hArg2) human Na Na compound 21 "[""A1IFX""]" 1 IC50 IC50 = = 0.224 ± 0.05 µM 224.0 [] unit_conversion 6.649751981665837 success True biochemical_inhibition Biochemical Arg2 inhibition assay; Table 1 reports geometric mean ± standard deviation. 4 Table 1 reports compound 21: Arg2 IC50 0.224 ± 0.05 µM. Figure 3 directly maps compound 21 bound to hArg2 to PDB 9FRV. auto_single_measurement only accepted activity measurement [1] 1 structures\9FRV\9FRV_metadata.json point structures/9FRV/9frv_protein.pdb structures/9FRV/9frv_pocket.pdb structures/9FRV/9frv_ligand.sdf structures/9FRV/9frv_ligand.pdb structures/9FRV/9frv_ligand.cif structures/9FRV/9frv_complex.pdb structures/9FRV/9frv_complex.cif 9FSN classic factor inhibiting hypoxia-inducible factor-alpha (FIH) human Na Na Enarodustat "[""A1IF7""]" 1 IC50 IC50 = = 10.9 ± 1.7 µM 10900.0 [] unit_conversion 4.962573502059376 success True biochemical_inhibition Inhibition of isolated recombinant human FIH; SPE-MS assay (Table 1). 6 Table 1 reports Enarodustat FIH IC50 = 10.9 ± 1.7 µM; Figure 2b maps the FIH:Mn:Enarodustat structure to PDB 9FSN. auto_single_measurement only accepted activity measurement [1] 1 structures\9FSN\9FSN_metadata.json point structures/9FSN/9fsn_protein.pdb structures/9FSN/9fsn_pocket.pdb structures/9FSN/9fsn_ligand.sdf structures/9FSN/9fsn_ligand.pdb structures/9FSN/9fsn_ligand.cif structures/9FSN/9fsn_complex.pdb structures/9FSN/9fsn_complex.cif 9FTQ extended Drosophila Golgi alpha-mannosidase II (dGMII) Drosophila Na Na compound 5; swainsonine-configured alkyl indolizidine "[""A1IGC""]" 1 Ki Ki = = 167 ± 13 μM 167000.0 [] unit_conversion 3.7772835288524167 success True biochemical_inhibition Fluorogenic substrate inhibition assay of dGMII using 4-methylumbelliferyl-α-D-mannoside; Table 1A. 4 Table 1A reports compound 5: dGMII Ki = 167 ± 13 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9FTQ\9FTQ_metadata.json point structures/9FTQ/9ftq_protein.pdb structures/9FTQ/9ftq_pocket.pdb structures/9FTQ/9ftq_ligand.pdb structures/9FTQ/9ftq_ligand.cif structures/9FTQ/9ftq_complex.pdb structures/9FTQ/9ftq_complex.cif 9FTZ extended CIII2/CIV respiratory supercomplex Mycobacterium smegmatis Na Na lansoprazole sulfide (LPZS) "[""A1IGA""]" 1 IC50 IC50 = = 0.5 ± 0.2 µM 500.0 [] unit_conversion 6.301029995663981 success True biochemical_inhibition Purified supercomplex oxygen-reduction/menaquinol oxidoreduction activity titration as a function of LPZS concentration. 5 “Titrations of CIII2CIV2 activity as a function of LPZS concentration show an IC50 of 0.5 ± 0.2 µM for the purified WT supercomplex.” auto_single_measurement only accepted activity measurement [1] 1 structures\9FTZ\9FTZ_metadata.json point structures/9FTZ/9ftz_protein.pdb structures/9FTZ/9ftz_pocket.pdb structures/9FTZ/9ftz_ligand.pdb structures/9FTZ/9ftz_ligand.cif structures/9FTZ/9ftz_complex.pdb structures/9FTZ/9ftz_complex.cif 9FUM extended 14-3-3 zeta Na Dimeric 14-3-3 zeta, residues 1-245, pseudo-wild-type C25A/C189A C25A/C189A MAP2c SP-(432-439) peptide, RRL(pS)NVSS, containing pS435 "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 0.2 ± 0.4 µM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Isothermal titration calorimetry of MAP2c SP-(432–439) peptide with dimeric 14-3-3ζ. 7 ITC showed that the SP-(432–439) and UP-(333–362) peptides bind with K_D values of (0.2 ± 0.4) and (1.8 ± 0.1) µM, respectively; 9FUM is mapped to SP-(432–439). auto_single_measurement only accepted activity measurement [1] 1 structures\9FUM\9FUM_metadata.json point structures/9FUM/9fum_protein.pdb structures/9FUM/9fum_pocket.pdb structures/9FUM/9fum_ligand.pdb structures/9FUM/9fum_ligand.cif structures/9FUM/9fum_complex.pdb structures/9FUM/9fum_complex.cif 9FVE classic VcSiaP substrate-binding protein Vibrio cholerae VcSiaP W73A mutant W73A Neu5Ac (sialic acid) "[""SLB""]" 1 Kd Kd = = 1.2 µM 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding ITC titration of Neu5Ac against VcSiaP W73A pre-bound to VHH_VcP #2. 5 VcSiaP W73A[VHH_VcP #2] bound Neu5Ac with K_D = 1.2 µM; Fig. 6d identifies the green curve as Neu5Ac versus VcSiaP W73A[VHH_VcP #2]. auto_single_measurement only accepted activity measurement [1] 1 structures\9FVE\9FVE_metadata.json point structures/9FVE/9fve_protein.pdb structures/9FVE/9fve_pocket.pdb structures/9FVE/9fve_ligand.sdf structures/9FVE/9fve_ligand.pdb structures/9FVE/9fve_ligand.cif structures/9FVE/9fve_complex.pdb structures/9FVE/9fve_complex.cif 9FVL extended 14-3-3 zeta Na Dimeric 14-3-3 zeta, residues 1-245, pseudo-wild-type C25A/C189A C25A/C189A MAP2c UP-(333-362) unphosphorylated peptide, QIVTKKIDLSHVTSKCGSLKNIRHRPGGGR "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 1.8 ± 0.1 µM 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding Isothermal titration calorimetry of MAP2c UP-(333–362) peptide with dimeric 14-3-3ζ. 7 ITC showed that the SP-(432–439) and UP-(333–362) peptides bind with K_D values of (0.2 ± 0.4) and (1.8 ± 0.1) µM, respectively; 9FVL is mapped to UP-(333–362). auto_single_measurement only accepted activity measurement [1] 1 structures\9FVL\9FVL_metadata.json point structures/9FVL/9fvl_protein.pdb structures/9FVL/9fvl_pocket.pdb structures/9FVL/9fvl_ligand.pdb structures/9FVL/9fvl_ligand.cif structures/9FVL/9fvl_complex.pdb structures/9FVL/9fvl_complex.cif 9FWD classic indole-3-acetic acid-amido synthetase GH3.6 (AtGH3.6) A. thaliana pETM11-AtGH3.6 expression construct; His-tagged recombinant protein Na AMP "[""AMP""]" 1 Kd Kd = = 6.3 mM 6300000.0 [] unit_conversion 2.200659450546418 success True direct_binding Microscale thermophoresis of fluorescently labelled recombinant AtGH3.6; AMP affinity measurement. 10 Fig. 3B visibly labels the AMP binding curve with Kd 6.3 mM; the figure caption identifies MST measurements for AtGH3.6. auto_single_measurement only accepted activity measurement [1] 1 structures\9FWD\9FWD_metadata.json point structures/9FWD/9fwd_protein.pdb structures/9FWD/9fwd_pocket.pdb structures/9FWD/9fwd_ligand.sdf structures/9FWD/9fwd_ligand.pdb structures/9FWD/9fwd_ligand.cif structures/9FWD/9fwd_complex.pdb structures/9FWD/9fwd_complex.cif 9FXD classic indole-3-acetic acid-amido synthetase GH3.6 (AtGH3.6) A. thaliana pETM11-AtGH3.6 expression construct; His-tagged recombinant protein Na aspartate "[""ASP""]" 1 Kd Kd = = 0.68 mM 680000.0 [] unit_conversion 3.1674910872937634 success True direct_binding Microscale thermophoresis of fluorescently labelled recombinant AtGH3.6; aspartate was measured in the AMP condition. 10 Fig. 3B visibly labels Asp (AMP) with Kd 0.68 mM; the caption identifies MST binding-affinity measurements for AtGH3.6. auto_single_measurement only accepted activity measurement [1] 1 structures\9FXD\9FXD_metadata.json point structures/9FXD/9fxd_protein.pdb structures/9FXD/9fxd_pocket.pdb structures/9FXD/9fxd_ligand.sdf structures/9FXD/9fxd_ligand.pdb structures/9FXD/9fxd_ligand.cif structures/9FXD/9fxd_complex.pdb structures/9FXD/9fxd_complex.cif 9FXZ classic Galectin-8 N-terminal carbohydrate recognition domain Na galectin-8N (Met56) Na compound 10; 4-(bromophenyl)phthalazinone D-galactal "[""V19""]" 1 Kd Kd = = 34 ± 3.2 μM 34000.0 [] unit_conversion 4.468521082957745 success True direct_binding Competitive fluorescence anisotropy assay; Table 1 reports the mean ± SEM (n = 4–8 unless otherwise stated). 3 Table 1 lists compound 10 (Ph-Br) with a Kd of 34 ± 3.2 μM for galectin 8N; the text identifies compound 10 as the p-bromophenyl derivative and states that affinities were determined by competitive fluorescence anisotropy. auto_single_measurement only accepted activity measurement [1] 1 structures\9FXZ\9FXZ_metadata.json point structures/9FXZ/9fxz_protein.pdb structures/9FXZ/9fxz_pocket.pdb structures/9FXZ/9fxz_ligand.sdf structures/9FXZ/9fxz_ligand.pdb structures/9FXZ/9fxz_ligand.cif structures/9FXZ/9fxz_complex.pdb structures/9FXZ/9fxz_complex.cif 9FY5 classic human monoacylglycerol lipase (MAGL) human human recombinant MAGL Na compound 1 "[""A1IG3""]" 1 IC50 IC50 = = 2.3 nM 2.3 [] unit_conversion 8.638272163982407 success True biochemical_inhibition RapidFire MS native-substrate assay on purified human MAGL enzyme (n≥3; values are means). 3 Table 1 reports compound 1 with biochemical human MAGL IC50 of 2.3 nM; its footnote specifies a RapidFire MS native substrate assay on purified human MAGL enzyme. auto_single_measurement only accepted activity measurement [1] 1 structures\9FY5\9FY5_metadata.json point structures/9FY5/9fy5_protein.pdb structures/9FY5/9fy5_pocket.pdb structures/9FY5/9fy5_ligand.sdf structures/9FY5/9fy5_ligand.pdb structures/9FY5/9fy5_ligand.cif structures/9FY5/9fy5_complex.pdb structures/9FY5/9fy5_complex.cif 9FZS classic EGFR Na Na wild-type compound 16 (R-enantiomer) "[""A1IHD""]" 2 Ki Ki = = 1.60 ± 0.05 nM 1.6 [] unit_conversion 8.795880017344075 success True direct_binding Kinetic characterisation of binding of enantiomers 16 and 17 to WT EGFR. 6 Table 4 reports Ki = 1.60 ± 0.05 nM for compound 16 against WT EGFR. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9FZS\9FZS_metadata.json point structures/9FZS/9fzs_protein.pdb structures/9FZS/9fzs_pocket.pdb structures/9FZS/9fzs_ligand.sdf structures/9FZS/9fzs_ligand.pdb structures/9FZS/9fzs_ligand.cif structures/9FZS/9fzs_complex.pdb structures/9FZS/9fzs_complex.cif 9G05 extended MadB Clostridium maddingley His6-MadB Na MadL3 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.15 ± 0.01 μM 150.0 [] unit_conversion 6.823908740944319 success True direct_binding ITC measurement of MadB binding the maddingley leader-peptide variant MadL3; reported MadB dimer:substrate stoichiometry was 1:1. 2 “MadL3 led to an even larger increase in affinity (KD value (MadL1): 0.41 ± 0.04 μM; KD value (MadL3): 0.15 ± 0.01 μM)” and the preceding ITC analysis identifies specific MadB binding to MadL3. auto_single_measurement only accepted activity measurement [1] 1 structures\9G05\9G05_metadata.json point structures/9G05/9g05_protein.pdb structures/9G05/9g05_pocket.pdb structures/9G05/9g05_ligand.pdb structures/9G05/9g05_ligand.cif structures/9G05/9g05_complex.pdb structures/9G05/9g05_complex.cif 9G0H extended SARS-CoV-2 main protease (MPro) SARS-CoV-2 Na Na C5N17A "[""A1IHT""]" 1 IC50 IC50 = = 3.18 ± 0.12 μM 3180.0 [] unit_conversion 5.497572880015568 success True biochemical_inhibition Mpro enzymatic inhibition following chiral HPLC separation of racemic C5N17; C5N17A is the (S)-enantiomer. 8 The paper states that the (S)-configured C5N17A had IC50 = 3.18 ± 0.12 μM in the enzyme assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9G0H\9G0H_metadata.json point structures/9G0H/9g0h_protein.pdb structures/9G0H/9g0h_pocket.pdb structures/9G0H/9g0h_ligand.pdb structures/9G0H/9g0h_ligand.cif structures/9G0H/9g0h_complex.pdb structures/9G0H/9g0h_complex.cif 9G0I extended SARS-CoV-2 main protease (MPro) SARS-CoV-2 Na Na C5N17B "[""A1IHV""]" 2 Ki Ki = = 26.6 nM 26.6 [] unit_conversion 7.575118363368933 success True biochemical_inhibition Mpro inhibition Ki determined using the reported Km value and the Cheng-Prusoff equation. 8 The paper reports that C5N17B displayed a Ki value of 26.6 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9G0I\9G0I_metadata.json point structures/9G0I/9g0i_protein.pdb structures/9G0I/9g0i_pocket.pdb structures/9G0I/9g0i_ligand.pdb structures/9G0I/9g0i_ligand.cif structures/9G0I/9g0i_complex.pdb structures/9G0I/9g0i_complex.cif 9G0U classic human LTC4 synthase human full-length LTC4 synthase with an N-terminal His6 tag Na AZD9898 "[""A1IHJ""]" 1 IC50 IC50 < < 1 nM 1.0 [] unit_conversion 9.0 success True biochemical_inhibition Human LTC4S enzyme inhibition assay assessing conversion of LTA4 into LTC4; Table 1 reports IC50 values in nM (AZD9898, n = 2). 3 Table 1 lists AZD9898: LTC4S Enz IC50 <1 (n = 2); footnote a defines the LTC4S enzyme inhibition assay. Figure 2 maps AZD9898 to PDB 9G0U. auto_single_measurement only accepted activity measurement [1] 1 structures\9G0U\9G0U_metadata.json point structures/9G0U/9g0u_protein.pdb structures/9G0U/9g0u_pocket.pdb structures/9G0U/9g0u_ligand.sdf structures/9G0U/9g0u_ligand.pdb structures/9G0U/9g0u_ligand.cif structures/9G0U/9g0u_complex.pdb structures/9G0U/9g0u_complex.cif 9G0V classic human LTC4 synthase human full-length LTC4 synthase with an N-terminal His6 tag Na compound 1 (GJG057) "[""A1IHO""]" 1 IC50 IC50 = = 14 ± 7.0 nM 14.0 [] unit_conversion 7.853871964321762 success True biochemical_inhibition Human LTC4S enzyme inhibition assay assessing conversion of LTA4 into LTC4; Table 1 reports IC50 values in nM. 3 Table 1 lists GJG057 (1): LTC4S Enz IC50 14 ± 7.0 nM; footnote a defines the LTC4S enzyme inhibition assay. Figure 2 maps GJG057 (1) to PDB 9G0V. auto_single_measurement only accepted activity measurement [1] 1 structures\9G0V\9G0V_metadata.json point structures/9G0V/9g0v_protein.pdb structures/9G0V/9g0v_pocket.pdb structures/9G0V/9g0v_ligand.sdf structures/9G0V/9g0v_ligand.pdb structures/9G0V/9g0v_ligand.cif structures/9G0V/9g0v_complex.pdb structures/9G0V/9g0v_complex.cif 9G14 classic human LTC4 synthase human full-length LTC4 synthase with an N-terminal His6 tag Na compound 2 (screening hit 2) "[""A1IHS""]" 1 IC50 IC50 = = 220 ± 300 nM 220.0 [] unit_conversion 6.657577319177793 success True biochemical_inhibition Human LTC4S enzyme inhibition assay assessing conversion of LTA4 into LTC4; Table 1 reports IC50 values in nM. 3 Table 1 lists compound 2: LTC4S Enz IC50 220 ± 300 nM; footnote a defines the LTC4S enzyme inhibition assay. Figure 2 maps screening hit 2 to PDB 9G14. auto_single_measurement only accepted activity measurement [1] 1 structures\9G14\9G14_metadata.json point structures/9G14/9g14_protein.pdb structures/9G14/9g14_pocket.pdb structures/9G14/9g14_ligand.sdf structures/9G14/9g14_ligand.pdb structures/9G14/9g14_ligand.cif structures/9G14/9g14_complex.pdb structures/9G14/9g14_complex.cif 9G1T classic human LTC4 synthase human full-length LTC4 synthase with an N-terminal His6 tag Na compound 5 "[""A1IH0""]" 1 IC50 IC50 = = 27 nM 27.0 [] unit_conversion 7.568636235841012 success True biochemical_inhibition Human LTC4S enzyme inhibition assay assessing conversion of LTA4 into LTC4; Table 1 reports IC50 values in nM (compound 5, n = 2). 3 Table 1 lists compound 5: LTC4S Enz IC50 27 (n = 2) nM; footnote a defines the LTC4S enzyme inhibition assay. Figure 2 maps compound 5 to PDB 9G1T. auto_single_measurement only accepted activity measurement [1] 1 structures\9G1T\9G1T_metadata.json point structures/9G1T/9g1t_protein.pdb structures/9G1T/9g1t_pocket.pdb structures/9G1T/9g1t_ligand.sdf structures/9G1T/9g1t_ligand.pdb structures/9G1T/9g1t_ligand.cif structures/9G1T/9g1t_complex.pdb structures/9G1T/9g1t_complex.cif 9G38 classic human carbonic anhydrase II human Na Na salvianolic acid P (compound 2) "[""A1IH2""]" 1 Ki Ki = = 78.9 µM 78900.0 [] unit_conversion 4.102922996790579 success True biochemical_inhibition Stopped-flow CO2 hydration inhibition assay; Table 2 reports mean of three assays. 7 Table 2 lists compound 2 with Ki = 78.9 µM against hCA II. The paper identifies compound 2 as salvianolic acid P and reports the hCA II/salvianolic acid P complex as PDB 9G38. auto_single_measurement only accepted activity measurement [1] 1 structures\9G38\9G38_metadata.json point structures/9G38/9g38_protein.pdb structures/9G38/9g38_pocket.pdb structures/9G38/9g38_ligand.sdf structures/9G38/9g38_ligand.pdb structures/9G38/9g38_ligand.cif structures/9G38/9g38_complex.pdb structures/9G38/9g38_complex.cif 9G3K classic LecB Pseudomonas aeruginosa Recombinant LecB from strain PAO1, expressed in E. coli BL21(DE3) from pET25-pAIL Na compound 2 "[""R7E""]" 1 IC50 IC50 = = 0.35 ± 0.02 µM 350.0 [] unit_conversion 6.455931955649724 success True biochemical_inhibition Competitive LecB fluorescence-polarization binding assay. 3 Table 1 reports LecB IC50 0.35 ± 0.02 µM for compound 2; Figure 2 identifies this as a competitive LecB binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9G3K\9G3K_metadata.json point structures/9G3K/9g3k_protein.pdb structures/9G3K/9g3k_pocket.pdb structures/9G3K/9g3k_ligand.sdf structures/9G3K/9g3k_ligand.pdb structures/9G3K/9g3k_ligand.cif structures/9G3K/9g3k_complex.pdb structures/9G3K/9g3k_complex.cif 9G3L extended LecB Pseudomonas aeruginosa Recombinant LecB from strain PAO1, expressed in E. coli BL21(DE3) from pET25-pAIL Na compound 9 "[""A1IH4""]" 1 IC50 IC50 = = 0.09 ± 0.01 µM 90.0 [] unit_conversion 7.045757490560675 success True biochemical_inhibition Competitive LecB fluorescence-polarization binding assay. 3 Table 1 reports LecB IC50 0.09 ± 0.01 µM for compound 9; Figure 2 identifies this as a competitive LecB binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9G3L\9G3L_metadata.json point structures/9G3L/9g3l_protein.pdb structures/9G3L/9g3l_pocket.pdb structures/9G3L/9g3l_ligand.pdb structures/9G3L/9g3l_ligand.cif structures/9G3L/9g3l_complex.pdb structures/9G3L/9g3l_complex.cif 9G3R extended LecA Pseudomonas aeruginosa Na Na compound 14; thio-L-Fuc-alpha(1,1)beta-D-Gal "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 115 µM 115000.0 [] unit_conversion 3.939302159646388 success True direct_binding Isothermal titration calorimetry (ITC); Table 2. 6 Table 2 reports for compound 14 with LecA: n* 0.62 and KD 115 µM; the text identifies ITC as the assay. Page 7 maps LecA-14 to PDB 9G3R. auto_single_measurement only accepted activity measurement [1] 1 structures\9G3R\9G3R_metadata.json point structures/9G3R/9g3r_protein.pdb structures/9G3R/9g3r_pocket.pdb structures/9G3R/9g3r_ligand.pdb structures/9G3R/9g3r_ligand.cif structures/9G3R/9g3r_complex.pdb structures/9G3R/9g3r_complex.cif 9G4M classic human monoacylglycerol lipase (hMAGL) human Na Na compound 9 (BODIPY-FL labeled probe) "[""A1IIH""]" 1 IC50 IC50 = = 0.12 ± 0.05 nM 0.12 [] unit_conversion 9.920818753952375 success True biochemical_inhibition In vitro characterization; mean from three independent measurements ± SD. 6 Table 2 lists compound 9 (BODIPY-FL), hMAGL IC50 = 0.12 ± 0.05 nM. Figure 2 identifies compound 9 in complex with hMAGL as PDB 9G4M. auto_single_measurement only accepted activity measurement [1] 1 structures\9G4M\9G4M_metadata.json point structures/9G4M/9g4m_protein.pdb structures/9G4M/9g4m_pocket.pdb structures/9G4M/9g4m_ligand.sdf structures/9G4M/9g4m_ligand.pdb structures/9G4M/9g4m_ligand.cif structures/9G4M/9g4m_complex.pdb structures/9G4M/9g4m_complex.cif 9G4S classic human METTL3-METTL14 human truncated METTL3/14 protein Na Compound 56 "[""A1III""]" 1 IC50 IC50 = = 2 nM 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition SPA primary assay. 10 Table 7 reports Compound 56 SPA IC50 = 2 nM. Page 20 maps Compound 56 (EP652) to PDB 9G4S. auto_single_measurement only accepted activity measurement [1] 1 structures\9G4S\9G4S_metadata.json point structures/9G4S/9g4s_protein.pdb structures/9G4S/9g4s_pocket.pdb structures/9G4S/9g4s_ligand.sdf structures/9G4S/9g4s_ligand.pdb structures/9G4S/9g4s_ligand.cif structures/9G4S/9g4s_complex.pdb structures/9G4S/9g4s_complex.cif 9G4U classic human METTL3-METTL14 human truncated METTL3/14 protein Na Compound 31 "[""A1IIK""]" 1 IC50 IC50 = = 2 nM 2.0 [] unit_conversion 8.698970004336019 success True biochemical_inhibition SPA primary assay. 7 Table 4 reports Compound 31 SPA IC50 = 2 nM. Page 20 maps Compound 31 to PDB 9G4U. auto_single_measurement only accepted activity measurement [1] 1 structures\9G4U\9G4U_metadata.json point structures/9G4U/9g4u_protein.pdb structures/9G4U/9g4u_pocket.pdb structures/9G4U/9g4u_ligand.sdf structures/9G4U/9g4u_ligand.pdb structures/9G4U/9g4u_ligand.cif structures/9G4U/9g4u_complex.pdb structures/9G4U/9g4u_complex.cif 9G4W classic human METTL3-METTL14 human truncated METTL3/14 protein Na Compound 59 "[""A1IIM""]" 1 IC50 IC50 = = 1 nM 1.0 [] unit_conversion 9.0 success True biochemical_inhibition SPA primary assay. 10 Table 7 reports Compound 59 SPA IC50 = 1 nM. Page 20 maps Compound 59 to PDB 9G4W. auto_single_measurement only accepted activity measurement [1] 1 structures\9G4W\9G4W_metadata.json point structures/9G4W/9g4w_protein.pdb structures/9G4W/9g4w_pocket.pdb structures/9G4W/9g4w_ligand.sdf structures/9G4W/9g4w_ligand.pdb structures/9G4W/9g4w_ligand.cif structures/9G4W/9g4w_complex.pdb structures/9G4W/9g4w_complex.cif 9G8J classic K+-dependent Na+-PPase (TmPPase) Thermotoga maritima Na Na Zoledronate (ZLD) "[""ZOL""]" 1 IC50 IC50 > > 200 µM 200000.0 [] unit_conversion 3.6989700043360187 success True biochemical_inhibition Molybdenum blue TmPPase activity inhibition assay; zoledronate. 2 Figure 1B prints “Zoledronate IC50 > 200 µM” for inhibition against TmPPase. Page 21 maps PDB 9G8J to the TmPPase:zoledronate complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9G8J\9G8J_metadata.json point structures/9G8J/9g8j_protein.pdb structures/9G8J/9g8j_pocket.pdb structures/9G8J/9g8j_ligand.sdf structures/9G8J/9g8j_ligand.pdb structures/9G8J/9g8j_ligand.cif structures/9G8J/9g8j_complex.pdb structures/9G8J/9g8j_complex.cif 9G8K classic K+-dependent Na+-PPase (TmPPase) Thermotoga maritima Na Na Etidronate (ETD) "[""911""]" 1 IC50 IC50 = = 138 ± 8.8 µM 138000.0 [] unit_conversion 3.860120913598763 success True biochemical_inhibition Molybdenum blue TmPPase activity inhibition assay; etidronate. 2 Figure 1B prints “Etidronate IC50 = 138 ± 8.8 µM” for inhibition against TmPPase. Page 21 maps PDB 9G8K to the TmPPase:etidronate complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9G8K\9G8K_metadata.json point structures/9G8K/9g8k_protein.pdb structures/9G8K/9g8k_pocket.pdb structures/9G8K/9g8k_ligand.sdf structures/9G8K/9g8k_ligand.pdb structures/9G8K/9g8k_ligand.cif structures/9G8K/9g8k_complex.pdb structures/9G8K/9g8k_complex.cif 9G9Q classic PbdA Rhodococcus jostii RHA1 PbdA expressed as an N-terminal hexahistidine-tagged protein in Escherichia coli BL21-A1(DE3); the tag was removed before crystallization Na p-methoxybenzoate (p-MBA) "[""ANN""]" 1 Kd Kd = = 3.8 (0.6) μM 3800.0 [] unit_conversion 5.42021640338319 success True direct_binding Purified PbdA ligand titration by type I spectral shift; Table 1 binding constant. 3 Table 1 reports p-MBA Kd 3.8 (0.6) μM; Figure 2 describes PbdA titration with p-MBA and its fitted binding curve. The paper maps PbdA–p-MBA to 9G9Q. auto_single_measurement only accepted activity measurement [1] 1 structures\9G9Q\9G9Q_metadata.json point structures/9G9Q/9g9q_protein.pdb structures/9G9Q/9g9q_pocket.pdb structures/9G9Q/9g9q_ligand.sdf structures/9G9Q/9g9q_ligand.pdb structures/9G9Q/9g9q_ligand.cif structures/9G9Q/9g9q_complex.pdb structures/9G9Q/9g9q_complex.cif 9G9R classic PbdA Rhodococcus jostii RHA1 PbdA expressed as an N-terminal hexahistidine-tagged protein in Escherichia coli BL21-A1(DE3); the tag was removed before crystallization Na p-ethylbenzoate (p-EB) "[""EGM""]" 1 Kd Kd = = 6.0 (0.7) μM 6000.0 [] unit_conversion 5.221848749616356 success True direct_binding Purified PbdA ligand titration by type I spectral shift; Table 1 binding constant. 3 Table 1 reports p-EB Kd 6.0 (0.7) μM. The paper maps PbdA–p-EB to 9G9R. auto_single_measurement only accepted activity measurement [1] 1 structures\9G9R\9G9R_metadata.json point structures/9G9R/9g9r_protein.pdb structures/9G9R/9g9r_pocket.pdb structures/9G9R/9g9r_ligand.sdf structures/9G9R/9g9r_ligand.pdb structures/9G9R/9g9r_ligand.cif structures/9G9R/9g9r_complex.pdb structures/9G9R/9g9r_complex.cif 9G9S classic PbdA Rhodococcus jostii RHA1 PbdA expressed as an N-terminal hexahistidine-tagged protein in Escherichia coli BL21-A1(DE3); the tag was removed before crystallization Na veratrate "[""TWO""]" 1 Kd Kd = = 18 (3) μM 18000.0 [] unit_conversion 4.7447274948966935 success True direct_binding Purified PbdA ligand titration by type I spectral shift; Table 1 binding constant. 3 Table 1 reports veratrate Kd 18 (3) μM. The paper maps PbdA–veratrate to 9G9S. auto_single_measurement only accepted activity measurement [1] 1 structures\9G9S\9G9S_metadata.json point structures/9G9S/9g9s_protein.pdb structures/9G9S/9g9s_pocket.pdb structures/9G9S/9g9s_ligand.sdf structures/9G9S/9g9s_ligand.pdb structures/9G9S/9g9s_ligand.cif structures/9G9S/9g9s_complex.pdb structures/9G9S/9g9s_complex.cif 9GBE classic Human anaplastic lymphoma kinase (ALK) Human ALK kinase domain residues 1086-1401, fused to an N-terminal TEV-cleavable His-GST fusion tag G1202R/L1196M NVL-655 "[""A1IJ8""]" 1 IC50 IC50 = = 1.8 nmol/L 1.8 [] unit_conversion 8.744727494896694 success True biochemical_inhibition Biochemical phosphorylation assay against recombinant ALK domain; comparison of ALK TKIs. 3 “NVL-655 potently inhibited ALK G1202R/L1196M with an IC50 of 1.8 nmol/L.” auto_single_measurement only accepted activity measurement [1] 1 structures\9GBE\9GBE_metadata.json point structures/9GBE/9gbe_protein.pdb structures/9GBE/9gbe_pocket.pdb structures/9GBE/9gbe_ligand.sdf structures/9GBE/9gbe_ligand.pdb structures/9GBE/9gbe_ligand.cif structures/9GBE/9gbe_complex.pdb structures/9GBE/9gbe_complex.cif 9GC1 extended human chymase human Na Na compound 8 "[""A1IJO""]" 1 IC50 IC50 = = 720 nM 720.0 [] unit_conversion 6.142667503568731 success True biochemical_inhibition Analogue enzyme-inhibition table. 3 Table 2 lists compound 8 with human chymase activity of 720 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9GC1\9GC1_metadata.json point structures/9GC1/9gc1_ligand.sdf structures/9GC1/9gc1_ligand.cif structures/9GC1/9gc1_complex.cif 9GC9 extended human chymase human Na Na compound 27 "[""A1IJ3""]" 1 IC50 IC50 = = 37 nM 37.0 [] unit_conversion 7.431798275933005 success True biochemical_inhibition Early R1-variation enzyme-inhibition table. 5 Table 3 lists compound 27 with human chymase activity of 37 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9GC9\9GC9_metadata.json point structures/9GC9/9gc9_ligand.sdf structures/9GC9/9gc9_ligand.cif structures/9GC9/9gc9_complex.cif 9GCC extended human chymase human Na Na compound 47 "[""A1IJ0""]" 1 IC50 IC50 = = 23 nM 23.0 [] unit_conversion 7.638272163982407 success True biochemical_inhibition Bicyclic R1-group comparison table. 7 Table 5 lists compound 47 with human chymase activity of 23 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9GCC\9GCC_metadata.json point structures/9GCC/9gcc_ligand.sdf structures/9GCC/9gcc_ligand.cif structures/9GCC/9gcc_complex.cif 9GCD extended human chymase human Na Na Fulacimstat (BAY 1142524; compound 86) "[""A1IJ2""]" 1 IC50 IC50 = = 4 nM 4.0 [] unit_conversion 8.397940008672037 success True biochemical_inhibition Core and R1 variation table. 11 Table 8 lists compound 86 with human chymase activity of 4 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9GCD\9GCD_metadata.json point structures/9GCD/9gcd_ligand.sdf structures/9GCD/9gcd_ligand.cif structures/9GCD/9gcd_complex.cif 9GCF classic human PI3Kdelta human Na Na CHF-6523; compound 18 "[""A1IJ5""]" 1 pKi Ki = = 9.07 ± 0.02 Na 0.8511380382023759 [] p_metric_transform 9.07 success True biochemical_inhibition In vitro ADP-Glo enzymatic assay of recombinant human PI3K isoforms. 9 Table 6 reports compound 18 (CHF-6523) PI3Kδ pKi 9.07 ± 0.02; the paper identifies 9GCF as compound 18 bound to hPI3Kδ. auto_single_measurement only accepted activity measurement [1] 1 structures\9GCF\9GCF_metadata.json point structures/9GCF/9gcf_protein.pdb structures/9GCF/9gcf_pocket.pdb structures/9GCF/9gcf_ligand.sdf structures/9GCF/9gcf_ligand.pdb structures/9GCF/9gcf_ligand.cif structures/9GCF/9gcf_complex.pdb structures/9GCF/9gcf_complex.cif 9GDI classic human PI3Kdelta human Na Na compound 10 "[""A1IJ1""]" 1 pKi Ki = = 9.13 ± 0.09 Na 0.7413102413009162 [] p_metric_transform 9.13 success True biochemical_inhibition In vitro ADP-Glo enzymatic assay of recombinant human PI3K isoforms. 7 Table 5 reports compound 10 PI3Kδ pKi 9.13 ± 0.09; the paper identifies 9GDI as compound 10 bound to hPI3Kδ. auto_single_measurement only accepted activity measurement [1] 1 structures\9GDI\9GDI_metadata.json point structures/9GDI/9gdi_protein.pdb structures/9GDI/9gdi_pocket.pdb structures/9GDI/9gdi_ligand.sdf structures/9GDI/9gdi_ligand.pdb structures/9GDI/9gdi_ligand.cif structures/9GDI/9gdi_complex.pdb structures/9GDI/9gdi_complex.cif 9GFK extended human MDM2 (hDM2) human Na Na compound 8a "[""POLYMER_ENTITY:2""]" 1 IC50 IC50 = = 1.91 ± 0.05 nM 1.91 [] unit_conversion 8.718966632752272 success True biochemical_inhibition TR-FRET inhibition of the p53-hDM2 interaction at 100 nM. 3 Macrocycles with i,i+7 crosslinks (8a and 8b) were the best hDM2 binders; compound 8a had an IC50 of 1.91 ± 0.05 nM for inhibition of the p53-hDM2 interaction. auto_single_measurement only accepted activity measurement [1] 1 structures\9GFK\9GFK_metadata.json point structures/9GFK/9gfk_protein.pdb structures/9GFK/9gfk_pocket.pdb structures/9GFK/9gfk_ligand.pdb structures/9GFK/9gfk_ligand.cif structures/9GFK/9gfk_complex.pdb structures/9GFK/9gfk_complex.cif 9GG9 classic human PI3Kgamma human Na Na compound 11 "[""A1IKW""]" 1 pKi Ki = = 7.62 ± 0.02 Na 23.9883291901949 [] p_metric_transform 7.62 success True biochemical_inhibition In vitro ADP-Glo enzymatic assay of recombinant human PI3K isoforms. 7 Table 5 reports compound 11 PI3Kγ pKi 7.62 ± 0.02; the paper identifies 9GG9 as compound 11 bound to hPI3Kγ. auto_single_measurement only accepted activity measurement [1] 1 structures\9GG9\9GG9_metadata.json point structures/9GG9/9gg9_protein.pdb structures/9GG9/9gg9_pocket.pdb structures/9GG9/9gg9_ligand.sdf structures/9GG9/9gg9_ligand.pdb structures/9GG9/9gg9_ligand.cif structures/9GG9/9gg9_complex.pdb structures/9GG9/9gg9_complex.cif 9GGB classic human mitochondrial DNA polymerase gamma human Na G848S PZL-A (A1K1) "[""A1IK1""]" 1 Kd Kd = = 25.7±3.8 nM 25.7 [] unit_conversion 7.590066876668706 success True direct_binding Apparent dissociation constant (Kd,app,PZL-A) from time-course experiments for PZL-A interaction with POLγ; Table 1. 3 Table 1 reports G848S Kd,app,PZL-A = 25.7±3.8 nM; the table note states this was determined by time-course experiments, and Methods identifies it as PZL-A–POLγ interaction. auto_single_measurement only accepted activity measurement [1] 1 structures\9GGB\9GGB_metadata.json point structures/9GGB/9ggb_protein.pdb structures/9GGB/9ggb_pocket.pdb structures/9GGB/9ggb_ligand.sdf structures/9GGB/9ggb_ligand.pdb structures/9GGB/9ggb_ligand.cif structures/9GGB/9ggb_complex.pdb structures/9GGB/9ggb_complex.cif 9GGD classic human mitochondrial DNA polymerase gamma human Na A467T PZL-A (A1K1) "[""A1IK1""]" 1 Kd Kd = = 57.1±7.4 nM 57.1 [] unit_conversion 7.243363891754152 success True direct_binding Apparent dissociation constant (Kd,app,PZL-A) from time-course experiments for PZL-A interaction with POLγ; Table 1. 3 Table 1 reports A467T Kd,app,PZL-A = 57.1±7.4 nM; the table note states this was determined by time-course experiments, and Methods identifies it as PZL-A–POLγ interaction. auto_single_measurement only accepted activity measurement [1] 1 structures\9GGD\9GGD_metadata.json point structures/9GGD/9ggd_protein.pdb structures/9GGD/9ggd_pocket.pdb structures/9GGD/9ggd_ligand.sdf structures/9GGD/9ggd_ligand.pdb structures/9GGD/9ggd_ligand.cif structures/9GGD/9ggd_complex.pdb structures/9GGD/9ggd_complex.cif 9GH7 extended human TfR1 human human His6-TfR1 Na BCY15466 "[""CHAIN:P""]" 1 Kd Kd = = 27 nM 27.0 [] unit_conversion 7.568636235841012 success True direct_binding SPR binding measurement against human TfR1. 5 Figure 1 lists BCY15466 with “SPR K_D (nM)” of 27; its caption states that binding was measured using surface plasmon resonance against human TfR1. The Results text identifies the crystallized complex as human His6-TfR1 with BCY15466. auto_single_measurement only accepted activity measurement [1] 1 structures\9GH7\9GH7_metadata.json point structures/9GH7/9gh7_protein.pdb structures/9GH7/9gh7_pocket.pdb structures/9GH7/9gh7_ligand.pdb structures/9GH7/9gh7_ligand.cif structures/9GH7/9gh7_complex.pdb structures/9GH7/9gh7_complex.cif 9GHY extended Cyclophilin A (CyPA) Na Na Na 19c; (2R,3S,7S,10E)-10-(3-aminopropyl)-2,7-dimethylspiro[3,8,11-triaza-1(2,7)-quinolina-5(3,1)-pyridazinacyclopentadecaphanene-13,5'-[1,3]dioxan]-14-ene-4,6,9,12-tetraone "[""A1ILH""]" 1 Ki Ki = = 5.2±1.5 μM 5200.0 [] unit_conversion 5.2839966563652006 success True direct_binding Fluorescence polarization (FP) assay; Table 1. 4 Table 1 reports Kᵢ,FP for compound 19c against CyPA as 5.2±1.5 μM; Figure 2 maps the CyPA–19c crystal structure to PDB-ID 9GHY. auto_single_measurement only accepted activity measurement [1] 1 structures\9GHY\9GHY_metadata.json point structures/9GHY/9ghy_protein.pdb structures/9GHY/9ghy_pocket.pdb structures/9GHY/9ghy_ligand.pdb structures/9GHY/9ghy_ligand.cif structures/9GHY/9ghy_complex.pdb structures/9GHY/9ghy_complex.cif 9GIJ classic SARS-CoV-2 Mpro SARS-CoV-2 SARS-CoV-2 Mpro residues 1-306 with a C-terminal histidine tag, cloned into pGEX-6P Na compound 5 "[""A1IL0""]" 2 Ki Ki = = 0.028 ± 0.007 μM 28.0 [] unit_conversion 7.552841968657781 success True biochemical_inhibition Purified SARS-CoV-2 Mpro inhibition (Ki) in the Table 5 in-vitro profile. 9 Table 5 reports SARS-CoV-2 Mpro WT Ki = 0.028 ± 0.007 μM for compound 5. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9GIJ\9GIJ_metadata.json point structures/9GIJ/9gij_protein.pdb structures/9GIJ/9gij_pocket.pdb structures/9GIJ/9gij_ligand.sdf structures/9GIJ/9gij_ligand.pdb structures/9GIJ/9gij_ligand.cif structures/9GIJ/9gij_complex.pdb structures/9GIJ/9gij_complex.cif 9GIL classic SARS-CoV-2 Mpro SARS-CoV-2 SARS-CoV-2 Mpro residues 1-306 with a C-terminal histidine tag, cloned into pGEX-6P Na compound 12 "[""A1IL7""]" 1 IC50 IC50 = = 0.018 ± 0.011 μM 18.0 [] unit_conversion 7.7447274948966935 success True biochemical_inhibition Enzyme-activity dose-response assay after 30 min incubation. 6 Table 3 reports compound 12 SARS-CoV-2 Mpro IC50 = 0.018 ± 0.011 μM; footnote a refers to the Table 1 assay definitions. auto_single_measurement only accepted activity measurement [1] 1 structures\9GIL\9GIL_metadata.json point structures/9GIL/9gil_protein.pdb structures/9GIL/9gil_pocket.pdb structures/9GIL/9gil_ligand.sdf structures/9GIL/9gil_ligand.pdb structures/9GIL/9gil_ligand.cif structures/9GIL/9gil_complex.pdb structures/9GIL/9gil_complex.cif 9GIN classic SOS2 Na SOS2 residues 562-1047, with an N-terminal GST tag and TEV cleavage site; GST tag cleaved before crystallization Na compound 11 "[""A1IL1""]" 1 Kd Kd = = 331 µM 331000.0 [] unit_conversion 3.480172006224281 success True direct_binding ITC direct-binding measurement of compound 11 with SOS2. 1 The graphical abstract explicitly prints “SOS2 ITC K_D 331 µM” for compound 11; Figure 3 maps compound 11 to PDB 9GIN. auto_single_measurement only accepted activity measurement [1] 1 structures\9GIN\9GIN_metadata.json point structures/9GIN/9gin_protein.pdb structures/9GIN/9gin_pocket.pdb structures/9GIN/9gin_ligand.sdf structures/9GIN/9gin_ligand.pdb structures/9GIN/9gin_ligand.cif structures/9GIN/9gin_complex.pdb structures/9GIN/9gin_complex.cif 9GJN classic ERAP1 Na Na Na compound 1; 1-[2-(3-oxo-3,4-dihydro-2H-1,4-benzothiazin-4-yl)acetamido]cyclohexane-1-carboxylic acid "[""A1IMK""]" 1 pIC50 IC50 = = 5.5 3162.2776601683795 [] p_metric_transform 5.5 success True biochemical_inhibition High-throughput mass-spectrometry ERAP1 peptide-cleavage assay; Table 1 enzymatic ERAP1 pIC50. 3 Table 1 reports ERAP1 pIC50 = 5.5 for compound 1; Figure 2 maps compound 1 to PDB 9GJN. auto_single_measurement only accepted activity measurement [1] 1 structures\9GJN\9GJN_metadata.json point structures/9GJN/9gjn_protein.pdb structures/9GJN/9gjn_pocket.pdb structures/9GJN/9gjn_ligand.sdf structures/9GJN/9gjn_ligand.pdb structures/9GJN/9gjn_ligand.cif structures/9GJN/9gjn_complex.pdb structures/9GJN/9gjn_complex.cif 9GJS classic ERAP1 Na Na Na compound 7; 1-[2-(6-bromo-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-4-yl)acetamido]-4,4-difluorocyclohexane-1-carboxylic acid "[""A1IMJ""]" 1 pIC50 IC50 = = 7.7 19.952623149688787 [] p_metric_transform 7.7 success True biochemical_inhibition High-throughput mass-spectrometry ERAP1 peptide-cleavage assay; Table 1 enzymatic ERAP1 pIC50. 3 Table 1 reports ERAP1 pIC50 = 7.7 for compound 7; Figure 5 maps compound 7 to PDB 9GJS. auto_single_measurement only accepted activity measurement [1] 1 structures\9GJS\9GJS_metadata.json point structures/9GJS/9gjs_protein.pdb structures/9GJS/9gjs_pocket.pdb structures/9GJS/9gjs_ligand.sdf structures/9GJS/9gjs_ligand.pdb structures/9GJS/9gjs_ligand.cif structures/9GJS/9gjs_complex.pdb structures/9GJS/9gjs_complex.cif 9GK6 classic ERAP1 Na Na Na compound 2; 1-[2-(6-chloro-3-oxo-3,4-dihydro-2H-1,4-benzothiazin-4-yl)acetamido]cyclohexane-1-carboxylic acid "[""A1IMM""]" 1 pIC50 IC50 = = 6.7 199.52623149688787 [] p_metric_transform 6.7 success True biochemical_inhibition High-throughput mass-spectrometry ERAP1 peptide-cleavage assay; Table 1 enzymatic ERAP1 pIC50. 3 Table 1 reports ERAP1 pIC50 = 6.7 for compound 2; Figure 4 maps compound 2 to PDB 9GK6. auto_single_measurement only accepted activity measurement [1] 1 structures\9GK6\9GK6_metadata.json point structures/9GK6/9gk6_protein.pdb structures/9GK6/9gk6_pocket.pdb structures/9GK6/9gk6_ligand.sdf structures/9GK6/9gk6_ligand.pdb structures/9GK6/9gk6_ligand.cif structures/9GK6/9gk6_complex.pdb structures/9GK6/9gk6_complex.cif 9GKE classic ERAP1 Na Na Na compound 13; 1-[2-(2-oxo-5-phenyl-2,3-dihydro-1,3-benzothiazol-3-yl)acetamido]cyclohexane-1-carboxylic acid "[""A1IML""]" 1 pIC50 IC50 = = 8.6 2.5118864315095824 [] p_metric_transform 8.6 success True biochemical_inhibition High-throughput mass-spectrometry ERAP1 peptide-cleavage assay; Table 2 enzymatic ERAP1 pIC50. 3 Table 2 reports ERAP1 pIC50 = 8.6 for compound 13; Figure 5 maps compound 13 to PDB 9GKE. auto_single_measurement only accepted activity measurement [1] 1 structures\9GKE\9GKE_metadata.json point structures/9GKE/9gke_protein.pdb structures/9GKE/9gke_pocket.pdb structures/9GKE/9gke_ligand.sdf structures/9GKE/9gke_ligand.pdb structures/9GKE/9gke_ligand.cif structures/9GKE/9gke_complex.pdb structures/9GKE/9gke_complex.cif 9GKX classic Dimethoate hydrolase (DmhA) Rhizorhabdus wittichii Na Na SAHA "[""SHH""]" 2 Ki Ki = = 41.6 nM 41.6 [] unit_conversion 7.380906669373257 success True biochemical_inhibition Dose-response inhibition assay; Table 2. 17 Table 2 reports RwDmhA (1b) SAHA Ki 41.6 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9GKX\9GKX_metadata.json point structures/9GKX/9gkx_protein.pdb structures/9GKX/9gkx_pocket.pdb structures/9GKX/9gkx_ligand.sdf structures/9GKX/9gkx_ligand.pdb structures/9GKX/9gkx_ligand.cif structures/9GKX/9gkx_complex.pdb structures/9GKX/9gkx_complex.cif 9GLA classic CDK2m7 (CDK2-based CDK7 mimic) Na Thr160-phosphorylated CDK2m7 in complex with a cyclin A2 fragment spanning residues 175-432 E8D; K9F; I10L; T14Q; Y15F; V64I; L83M; H84E; Q85T; K88E; K89V; Q131N SY5609 "[""YNK""]" 1 IC50 IC50 = = 0.041 µM 41.0 [] unit_conversion 7.3872161432802645 success True biochemical_inhibition Kinase inhibition assay using CDK2m7/cyclin A2; IC50 measured in at least triplicate. 4 Fig. 3 reports SY5609 IC50 = 0.041 µM for the CDK2m7/A2 mimic; the text identifies this as inhibition of CDK2m7. auto_single_measurement only accepted activity measurement [1] 1 structures\9GLA\9GLA_metadata.json point structures/9GLA/9gla_protein.pdb structures/9GLA/9gla_pocket.pdb structures/9GLA/9gla_ligand.sdf structures/9GLA/9gla_ligand.pdb structures/9GLA/9gla_ligand.cif structures/9GLA/9gla_complex.pdb structures/9GLA/9gla_complex.cif 9GN6 classic Deacetylase (HdaH) Klebsiella pneumoniae subsp. ozaenae Na Na SAHA "[""SHH""]" 2 Ki Ki = = 22.4 nM 22.4 [] unit_conversion 7.649751981665837 success True biochemical_inhibition Dose-response inhibition assay; Table 2. 17 Table 2 reports KpHdaH (1b) SAHA Ki 22.4 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9GN6\9GN6_metadata.json point structures/9GN6/9gn6_protein.pdb structures/9GN6/9gn6_pocket.pdb structures/9GN6/9gn6_ligand.sdf structures/9GN6/9gn6_ligand.pdb structures/9GN6/9gn6_ligand.cif structures/9GN6/9gn6_complex.pdb structures/9GN6/9gn6_complex.cif 9GN7 classic Deacetylase (HdaH) Klebsiella pneumoniae subsp. ozaenae Na Na TSA "[""TSN""]" 2 Ki Ki <= <= 2.47 nM 2.47 [] unit_conversion 8.607303046740334 success True biochemical_inhibition Dose-response inhibition assay; Table 2. 17 Table 2 reports KpHdaH (1b) TSA Ki ≤2.47 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9GN7\9GN7_metadata.json point structures/9GN7/9gn7_protein.pdb structures/9GN7/9gn7_pocket.pdb structures/9GN7/9gn7_ligand.sdf structures/9GN7/9gn7_ligand.pdb structures/9GN7/9gn7_ligand.cif structures/9GN7/9gn7_complex.pdb structures/9GN7/9gn7_complex.cif 9GOO extended human carbonic anhydrase II human Na Na PCI-27483 "[""A1IOK""]" 1 Ki Ki = = 68065 nM 68065.0 [] unit_conversion 4.167076151146024 success True biochemical_inhibition Stopped-flow CO2 hydration assay; Table 1 reports inhibition data for catalytically active human CA isoforms. 2 Table 1 lists PCI-27483 Ki = 68065 nM for hCA II. The text identifies the hCA II–PCI-27483 crystal structure as PDB 9GOO. auto_single_measurement only accepted activity measurement [1] 1 structures\9GOO\9GOO_metadata.json point structures/9GOO/9goo_ligand.cif structures/9GOO/9goo_complex.cif 9GOW classic human IRE1alpha (phosphorylated IRE1alpha) human IRE1alpha kinase and RNase domains, residues 547-977, His-tagged with a TEV cleavage site Na IA107 "[""A1IOO""]" 2 Kd Kd = = 0.152 ± 0.032 µM 152.0 [] unit_conversion 6.818156412055227 success True direct_binding Microscale thermophoresis binding assay with phosphorylated IRE1α. 6 Fig. 4g reports IA107 binding to p-IRE1α by MST, KD = 0.152 ± 0.032 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9GOW\9GOW_metadata.json point structures/9GOW/9gow_protein.pdb structures/9GOW/9gow_pocket.pdb structures/9GOW/9gow_ligand.sdf structures/9GOW/9gow_ligand.pdb structures/9GOW/9gow_ligand.cif structures/9GOW/9gow_complex.pdb structures/9GOW/9gow_complex.cif 9GOZ classic 4-allyl syringol oxidase (Sc4ASO) Streptomyces cavernae Na Na eugenol "[""EOL""]" 1 Kd Kd = = 2.2 μM 2200.0 [] unit_conversion 5.657577319177793 success True direct_binding Dissociation constant determined from a Lineweaver–Burk plot of the apparent FAD-reduction rate (k1′), following the approach used for PsVAO. 7 “a value of 2.2 μM was determined for eugenol (2)” auto_single_measurement only accepted activity measurement [1] 1 structures\9GOZ\9GOZ_metadata.json point structures/9GOZ/9goz_protein.pdb structures/9GOZ/9goz_pocket.pdb structures/9GOZ/9goz_ligand.sdf structures/9GOZ/9goz_ligand.pdb structures/9GOZ/9goz_ligand.cif structures/9GOZ/9goz_complex.pdb structures/9GOZ/9goz_complex.cif 9GPK classic FKBP51 human FK1 domain Na 12c/j "[""A1INK""]" 1 Ki Ki = = 224 ± 13 nM 224.0 [] unit_conversion 6.649751981665837 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12c/j: Ki = 224 ± 13 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPK\9GPK_metadata.json point structures/9GPK/9gpk_protein.pdb structures/9GPK/9gpk_pocket.pdb structures/9GPK/9gpk_ligand.sdf structures/9GPK/9gpk_ligand.pdb structures/9GPK/9gpk_ligand.cif structures/9GPK/9gpk_complex.pdb structures/9GPK/9gpk_complex.cif 9GPL classic FKBP51 human FK1 domain Na 11c/i "[""A1INL""]" 1 Ki Ki = = 480 ± 14 nM 480.0 [] unit_conversion 6.318758762624412 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 3 Table 1 reports 11c/i: Ki = 480 ± 14 nM for FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPL\9GPL_metadata.json point structures/9GPL/9gpl_protein.pdb structures/9GPL/9gpl_pocket.pdb structures/9GPL/9gpl_ligand.sdf structures/9GPL/9gpl_ligand.pdb structures/9GPL/9gpl_ligand.cif structures/9GPL/9gpl_complex.pdb structures/9GPL/9gpl_complex.cif 9GPM classic FKBP51 human FK1 domain Na 12c/i "[""A1INM""]" 1 Ki Ki = = 524 ± 1 nM 524.0 [] unit_conversion 6.280668713016274 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 3 Table 1 reports 12c/i: Ki = 524 ± 1 nM for FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPM\9GPM_metadata.json point structures/9GPM/9gpm_protein.pdb structures/9GPM/9gpm_pocket.pdb structures/9GPM/9gpm_ligand.sdf structures/9GPM/9gpm_ligand.pdb structures/9GPM/9gpm_ligand.cif structures/9GPM/9gpm_complex.pdb structures/9GPM/9gpm_complex.cif 9GPN classic FKBP51 human FK1 domain Na 11b/j "[""A1INN""]" 1 Ki Ki = = 409 ± 36 nM 409.0 [] unit_conversion 6.388276691992658 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 3 Table 1 reports 11b/j: Ki = 409 ± 36 nM for FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPN\9GPN_metadata.json point structures/9GPN/9gpn_protein.pdb structures/9GPN/9gpn_pocket.pdb structures/9GPN/9gpn_ligand.sdf structures/9GPN/9gpn_ligand.pdb structures/9GPN/9gpn_ligand.cif structures/9GPN/9gpn_complex.pdb structures/9GPN/9gpn_complex.cif 9GPO classic FKBP51 human FK1 domain Na 12c/n "[""A1INU""]" 1 Ki Ki = = 282 ± 39 nM 282.0 [] unit_conversion 6.549750891680639 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12c/n: Ki = 282 ± 39 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPO\9GPO_metadata.json point structures/9GPO/9gpo_protein.pdb structures/9GPO/9gpo_pocket.pdb structures/9GPO/9gpo_ligand.sdf structures/9GPO/9gpo_ligand.pdb structures/9GPO/9gpo_ligand.cif structures/9GPO/9gpo_complex.pdb structures/9GPO/9gpo_complex.cif 9GPP classic FKBP51 human FK1 domain Na 12c/o "[""A1INO""]" 1 Ki Ki = = 23 ± 1 nM 23.0 [] unit_conversion 7.638272163982407 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12c/o: Ki = 23 ± 1 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPP\9GPP_metadata.json point structures/9GPP/9gpp_protein.pdb structures/9GPP/9gpp_pocket.pdb structures/9GPP/9gpp_ligand.sdf structures/9GPP/9gpp_ligand.pdb structures/9GPP/9gpp_ligand.cif structures/9GPP/9gpp_complex.pdb structures/9GPP/9gpp_complex.cif 9GPQ classic FKBP51 human FK1 domain Na 12h/p "[""A1INQ""]" 1 Ki Ki = = 1305 ± 86 nM 1305.0 [] unit_conversion 5.8843894883257 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12h/p: Ki = 1305 ± 86 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPQ\9GPQ_metadata.json point structures/9GPQ/9gpq_protein.pdb structures/9GPQ/9gpq_pocket.pdb structures/9GPQ/9gpq_ligand.sdf structures/9GPQ/9gpq_ligand.pdb structures/9GPQ/9gpq_ligand.cif structures/9GPQ/9gpq_complex.pdb structures/9GPQ/9gpq_complex.cif 9GPR classic FKBP51 human FK1 domain Na 12h/m "[""A1INP""]" 1 Ki Ki = = 274 ± 2 nM 274.0 [] unit_conversion 6.562249437179612 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12h/m: Ki = 274 ± 2 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPR\9GPR_metadata.json point structures/9GPR/9gpr_protein.pdb structures/9GPR/9gpr_pocket.pdb structures/9GPR/9gpr_ligand.sdf structures/9GPR/9gpr_ligand.pdb structures/9GPR/9gpr_ligand.cif structures/9GPR/9gpr_complex.pdb structures/9GPR/9gpr_complex.cif 9GPS classic FKBP51 human FK1 domain Na 12c/p "[""A1INV""]" 1 Ki Ki = = 1833 ± 124 nM 1833.0 [] unit_conversion 5.736837535037783 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12c/p: Ki = 1833 ± 124 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPS\9GPS_metadata.json point structures/9GPS/9gps_protein.pdb structures/9GPS/9gps_pocket.pdb structures/9GPS/9gps_ligand.sdf structures/9GPS/9gps_ligand.pdb structures/9GPS/9gps_ligand.cif structures/9GPS/9gps_complex.pdb structures/9GPS/9gps_complex.cif 9GPT classic FKBP51 human FK1 domain Na 12c/k "[""A1INR""]" 1 Ki Ki = = 94 ± 2 nM 94.0 [] unit_conversion 7.026872146400302 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12c/k: Ki = 94 ± 2 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPT\9GPT_metadata.json point structures/9GPT/9gpt_protein.pdb structures/9GPT/9gpt_pocket.pdb structures/9GPT/9gpt_ligand.sdf structures/9GPT/9gpt_ligand.pdb structures/9GPT/9gpt_ligand.cif structures/9GPT/9gpt_complex.pdb structures/9GPT/9gpt_complex.cif 9GPU classic FKBP51 human FK1 domain Na 12h/k "[""A1INS""]" 1 Ki Ki = = 163 ± 8 nM 163.0 [] unit_conversion 6.787812395596042 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12h/k: Ki = 163 ± 8 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPU\9GPU_metadata.json point structures/9GPU/9gpu_protein.pdb structures/9GPU/9gpu_pocket.pdb structures/9GPU/9gpu_ligand.sdf structures/9GPU/9gpu_ligand.pdb structures/9GPU/9gpu_ligand.cif structures/9GPU/9gpu_complex.pdb structures/9GPU/9gpu_complex.cif 9GPV classic FKBP51 human FK1 domain Na 12c/l "[""A1INT""]" 1 Ki Ki = = 40 ± 0 nM 40.0 [] unit_conversion 7.3979400086720375 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12c/l: Ki = 40 ± 0 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPV\9GPV_metadata.json point structures/9GPV/9gpv_protein.pdb structures/9GPV/9gpv_pocket.pdb structures/9GPV/9gpv_ligand.sdf structures/9GPV/9gpv_ligand.pdb structures/9GPV/9gpv_ligand.cif structures/9GPV/9gpv_complex.pdb structures/9GPV/9gpv_complex.cif 9GPW classic FKBP51 human FK1 domain Na 12f/j "[""A1INW""]" 1 Ki Ki = = 145 ± 0.01 nM 145.0 [] unit_conversion 6.838631997765026 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12f/j: Ki = 145 ± 0.01 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPW\9GPW_metadata.json point structures/9GPW/9gpw_protein.pdb structures/9GPW/9gpw_pocket.pdb structures/9GPW/9gpw_ligand.sdf structures/9GPW/9gpw_ligand.pdb structures/9GPW/9gpw_ligand.cif structures/9GPW/9gpw_complex.pdb structures/9GPW/9gpw_complex.cif 9GPX classic FKBP51 human FK1 domain Na 12f/l "[""A1INX""]" 1 Ki Ki = = 44 ± 0.2 nM 44.0 [] unit_conversion 7.356547323513812 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12f/l: Ki = 44 ± 0.2 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPX\9GPX_metadata.json point structures/9GPX/9gpx_protein.pdb structures/9GPX/9gpx_pocket.pdb structures/9GPX/9gpx_ligand.sdf structures/9GPX/9gpx_ligand.pdb structures/9GPX/9gpx_ligand.cif structures/9GPX/9gpx_complex.pdb structures/9GPX/9gpx_complex.cif 9GPY classic FKBP51 human FK1 domain Na 12g/j "[""A1INZ""]" 1 Ki Ki = = 125 ± 3 nM 125.0 [] unit_conversion 6.903089986991944 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12g/j: Ki = 125 ± 3 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPY\9GPY_metadata.json point structures/9GPY/9gpy_protein.pdb structures/9GPY/9gpy_pocket.pdb structures/9GPY/9gpy_ligand.sdf structures/9GPY/9gpy_ligand.pdb structures/9GPY/9gpy_ligand.cif structures/9GPY/9gpy_complex.pdb structures/9GPY/9gpy_complex.cif 9GPZ classic FKBP51 human FK1 domain Na 12f/o "[""A1INY""]" 1 Ki Ki = = 56 ± 1 nM 56.0 [] unit_conversion 7.251811972993799 success True direct_binding Competitive fluorescence-polarization assay; macrocyclic C/N compound. 5 Table 2 reports 12f/o: Ki = 56 ± 1 nM for human FKBP51. auto_single_measurement only accepted activity measurement [1] 1 structures\9GPZ\9GPZ_metadata.json point structures/9GPZ/9gpz_protein.pdb structures/9GPZ/9gpz_pocket.pdb structures/9GPZ/9gpz_ligand.sdf structures/9GPZ/9gpz_ligand.pdb structures/9GPZ/9gpz_ligand.cif structures/9GPZ/9gpz_complex.pdb structures/9GPZ/9gpz_complex.cif 9GRM extended Cdc42 Na Cdc42 Q61L Delta7 Q61L P7 W14A peptide "[""CHAIN:B""]" 1 Kd Kd = = 14 ± 4 nM 14.0 [] unit_conversion 7.853871964321762 success True direct_binding Competition scintillation-proximity assay measuring P7 W14A affinity against a Cdc42–WASP complex. 4 Table 1 prints Kd = 14 ± 4 nM for P7 W14A. Figure 2 identifies 9grm as the Cdc42:P7 W14A complex; the methods describe Cdc42 Q61L Δ7 protein. auto_single_measurement only accepted activity measurement [1] 1 structures\9GRM\9GRM_metadata.json point structures/9GRM/9grm_protein.pdb structures/9GRM/9grm_pocket.pdb structures/9GRM/9grm_ligand.pdb structures/9GRM/9grm_ligand.cif structures/9GRM/9grm_complex.pdb structures/9GRM/9grm_complex.cif 9GRZ classic SLC35B1 human Full-length SLC35B1 residues 1-322 with a C-terminal TEV-GFP-His8 tag wild-type AMP-PNP "[""ANP""]" 1 IC50 IC50 = = 12.0 ± 2.1 μM 12000.0 [] unit_conversion 4.920818753952375 success True biochemical_inhibition Cold AMP-PNP competition of [3H]ADP uptake by wild-type SLC35B1 proteoliposomes preloaded with nucleotide. 15 Extended Data Fig. 1f reports “AMP-PNP IC50 = 12.0 ± 2.1 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9GRZ\9GRZ_metadata.json point structures/9GRZ/9grz_protein.pdb structures/9GRZ/9grz_pocket.pdb structures/9GRZ/9grz_ligand.sdf structures/9GRZ/9grz_ligand.pdb structures/9GRZ/9grz_ligand.cif structures/9GRZ/9grz_complex.pdb structures/9GRZ/9grz_complex.cif 9GSV classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (rhGAA) Na compound 4c "[""A1IO6""]" 1 Ki Ki = = 7.6 µM 7600.0 [] unit_conversion 5.119186407719209 success True biochemical_inhibition In vitro rhGAA inhibition assay at pH 4.0 using 4-nitrophenyl-α-D-glucopyranoside; Ki determined from four kinetic curves. 3 Table 2 prints Ki = 7.6 µM for compound 4c; the paper maps 4c to PDB 9GSV in its data-availability statement (PDF p.15). auto_single_measurement only accepted activity measurement [1] 1 structures\9GSV\9GSV_metadata.json point structures/9GSV/9gsv_protein.pdb structures/9GSV/9gsv_pocket.pdb structures/9GSV/9gsv_ligand.sdf structures/9GSV/9gsv_ligand.pdb structures/9GSV/9gsv_ligand.cif structures/9GSV/9gsv_complex.pdb structures/9GSV/9gsv_complex.cif 9GSW classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (rhGAA) Na compound 4d "[""A1IO5""]" 1 Ki Ki = = 13.7 µM 13700.0 [] unit_conversion 4.863279432843593 success True biochemical_inhibition In vitro rhGAA inhibition assay at pH 4.0 using 4-nitrophenyl-α-D-glucopyranoside; Ki determined from four kinetic curves. 3 Table 2 prints Ki = 13.7 µM for compound 4d; the paper maps 4d to PDB 9GSW (PDF p.15). auto_single_measurement only accepted activity measurement [1] 1 structures\9GSW\9GSW_metadata.json point structures/9GSW/9gsw_protein.pdb structures/9GSW/9gsw_pocket.pdb structures/9GSW/9gsw_ligand.sdf structures/9GSW/9gsw_ligand.pdb structures/9GSW/9gsw_ligand.cif structures/9GSW/9gsw_complex.pdb structures/9GSW/9gsw_complex.cif 9GTC classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (rhGAA) Na compound 4g "[""A1IO7""]" 1 Ki Ki = = 10.8 µM 10800.0 [] unit_conversion 4.966576244513051 success True biochemical_inhibition In vitro rhGAA inhibition assay at pH 4.0 using 4-nitrophenyl-α-D-glucopyranoside; Ki determined from four kinetic curves. 3 Table 2 prints Ki = 10.8 µM for compound 4g; the paper maps 4g to PDB 9GTC (PDF p.15). auto_single_measurement only accepted activity measurement [1] 1 structures\9GTC\9GTC_metadata.json point structures/9GTC/9gtc_protein.pdb structures/9GTC/9gtc_pocket.pdb structures/9GTC/9gtc_ligand.sdf structures/9GTC/9gtc_ligand.pdb structures/9GTC/9gtc_ligand.cif structures/9GTC/9gtc_complex.pdb structures/9GTC/9gtc_complex.cif 9GTD classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (rhGAA) Na compound 4i "[""A1IO8""]" 1 Ki Ki = = 14.8 µM 14800.0 [] unit_conversion 4.8297382846050425 success True biochemical_inhibition In vitro rhGAA inhibition assay at pH 4.0 using 4-nitrophenyl-α-D-glucopyranoside; Ki determined from four kinetic curves. 3 Table 2 prints Ki = 14.8 µM for compound 4i; the paper maps 4i to PDB 9GTD (PDF p.15). auto_single_measurement only accepted activity measurement [1] 1 structures\9GTD\9GTD_metadata.json point structures/9GTD/9gtd_protein.pdb structures/9GTD/9gtd_pocket.pdb structures/9GTD/9gtd_ligand.sdf structures/9GTD/9gtd_ligand.pdb structures/9GTD/9gtd_ligand.cif structures/9GTD/9gtd_complex.pdb structures/9GTD/9gtd_complex.cif 9GTE classic TRIM21 Mus musculus PRYSPRY domain, residues Val291-Met470, with an N-terminal His6-tag Na Suramin "[""SVR""]" 1 Kd Kd = = 9.1 ± 2.0 µM 9100.0 [] unit_conversion 5.040958607678906 success True direct_binding Isothermal titration calorimetry (ITC) of suramin binding to murine TRIM21 PRYSPRY domain. 4 Figure 2b reports the ITC curve for suramin binding to murine TRIM21 and prints Kd (µM) 9.1 ± 2.0. auto_single_measurement only accepted activity measurement [1] 1 structures\9GTE\9GTE_metadata.json point structures/9GTE/9gte_protein.pdb structures/9GTE/9gte_pocket.pdb structures/9GTE/9gte_ligand.sdf structures/9GTE/9gte_ligand.pdb structures/9GTE/9gte_ligand.cif structures/9GTE/9gte_complex.pdb structures/9GTE/9gte_complex.cif 9GTL classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (rhGAA) Na compound 4j "[""A1IO9""]" 1 Ki Ki = = 13 µM 13000.0 [] unit_conversion 4.886056647693163 success True biochemical_inhibition In vitro rhGAA inhibition assay at pH 4.0 using 4-nitrophenyl-α-D-glucopyranoside; Ki determined from four kinetic curves. 3 Table 2 prints Ki = 13 µM for compound 4j; the paper maps 4j to PDB 9GTL (PDF p.15). auto_single_measurement only accepted activity measurement [1] 1 structures\9GTL\9GTL_metadata.json point structures/9GTL/9gtl_protein.pdb structures/9GTL/9gtl_pocket.pdb structures/9GTL/9gtl_ligand.sdf structures/9GTL/9gtl_ligand.pdb structures/9GTL/9gtl_ligand.cif structures/9GTL/9gtl_complex.pdb structures/9GTL/9gtl_complex.cif 9GTN classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (rhGAA) Na compound 4k "[""A1IPA""]" 1 Ki Ki = = 18.3 µM 18300.0 [] unit_conversion 4.73754891026957 success True biochemical_inhibition In vitro rhGAA inhibition assay at pH 4.0 using 4-nitrophenyl-α-D-glucopyranoside; Ki determined from four kinetic curves. 3 Table 2 prints Ki = 18.3 µM for compound 4k; the paper maps 4k to PDB 9GTN (PDF p.15). auto_single_measurement only accepted activity measurement [1] 1 structures\9GTN\9GTN_metadata.json point structures/9GTN/9gtn_protein.pdb structures/9GTN/9gtn_pocket.pdb structures/9GTN/9gtn_ligand.sdf structures/9GTN/9gtn_ligand.pdb structures/9GTN/9gtn_ligand.cif structures/9GTN/9gtn_complex.pdb structures/9GTN/9gtn_complex.cif 9GTT classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (rhGAA) Na compound 4l "[""A1IPB""]" 1 Ki Ki = = 20 µM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition In vitro rhGAA inhibition assay at pH 4.0 using 4-nitrophenyl-α-D-glucopyranoside; Ki determined from four kinetic curves. 3 Table 2 prints Ki = 20 µM for compound 4l; the paper maps 4l to PDB 9GTT (PDF p.15). auto_single_measurement only accepted activity measurement [1] 1 structures\9GTT\9GTT_metadata.json point structures/9GTT/9gtt_protein.pdb structures/9GTT/9gtt_pocket.pdb structures/9GTT/9gtt_ligand.sdf structures/9GTT/9gtt_ligand.pdb structures/9GTT/9gtt_ligand.cif structures/9GTT/9gtt_complex.pdb structures/9GTT/9gtt_complex.cif 9GTW classic human lysosomal acid-alpha-glucosidase (GAA) human proteolytically digested recombinant human GAA (rhGAA) Na compound 3g "[""A1IPC""]" 1 IC50 IC50 = = 240 ± 1 µM 240000.0 [] unit_conversion 3.6197887582883936 success True biochemical_inhibition In vitro rhGAA inhibition; Table 2 lists Ki as not determined and explicitly footnotes IC50 for compound 3g. 3 Table 2 lists compound 3g with Ki N.D. and footnote b: IC50, 240 ± 1 µM; the paper maps 3g to PDB 9GTW (PDF p.15). auto_single_measurement only accepted activity measurement [1] 1 structures\9GTW\9GTW_metadata.json point structures/9GTW/9gtw_protein.pdb structures/9GTW/9gtw_pocket.pdb structures/9GTW/9gtw_ligand.sdf structures/9GTW/9gtw_ligand.pdb structures/9GTW/9gtw_ligand.cif structures/9GTW/9gtw_complex.pdb structures/9GTW/9gtw_complex.cif 9GU7 extended human carbonic anhydrase II human Na Na 3a; N-phenyl-2-(1H-tetrazol-5-yl)acetamide "[""A1IOX""]" 1 Ki Ki = = 3.64 µM 3640.0 [] unit_conversion 5.438898616350944 success True biochemical_inhibition CO2 hydrase stopped-flow kinetic inhibition assay using acetazolamide as a reference drug; mean of three assays. 2 Table 2 reports compound 3a Ki = 3.64 µM against hCA II. Figure 1 maps the hCA II/3a complex to PDB 9GU7. auto_single_measurement only accepted activity measurement [1] 1 structures\9GU7\9GU7_metadata.json point structures/9GU7/9gu7_ligand.cif structures/9GU7/9gu7_complex.cif 9GUB extended SARS-CoV-2 Mac1 SARS-CoV-2 Na Na MCD-628 (compound 4a) "[""A1IO2""]" 1 IC50 IC50 = = 6.1 μM 6100.0 [] unit_conversion 5.214670164989233 success True biochemical_inhibition AlphaScreen competition assay measuring inhibition of the interaction between SARS-CoV-2 Mac1 and an ADP-ribosylated peptide. 5 Figure 2C reports compound 4a Mac1 IC50 = 6.1 μM (SD 0.02); the caption states competition assays tested blockade of the Mac1–ADP-ribosylated peptide interaction. auto_single_measurement only accepted activity measurement [1] 1 structures\9GUB\9GUB_metadata.json point structures/9GUB/9gub_protein.pdb structures/9GUB/9gub_pocket.pdb structures/9GUB/9gub_ligand.pdb structures/9GUB/9gub_ligand.cif structures/9GUB/9gub_complex.pdb structures/9GUB/9gub_complex.cif 9GUM extended human carbonic anhydrase II human Na Na 3o; N-phenethyl-2-(1H-tetrazol-5-yl)acetamide "[""A1IO3""]" 1 Ki Ki = = 3.06 µM 3060.0 [] unit_conversion 5.514278573518419 success True biochemical_inhibition CO2 hydrase stopped-flow kinetic inhibition assay using acetazolamide as a reference drug; mean of three assays. 2 Table 2 reports compound 3o Ki = 3.06 µM against hCA II. Figure 1 maps the hCA II/3o complex to PDB 9GUM. auto_single_measurement only accepted activity measurement [1] 1 structures\9GUM\9GUM_metadata.json point structures/9GUM/9gum_ligand.cif structures/9GUM/9gum_complex.cif 9GVM classic NNMT Na Na Na 20p "[""A1IPM""]" 1 pKd Kd = = 8.6 -log10(M) 2.5118864315095824 [] p_metric_transform 8.6 success True direct_binding Product binding to NNMT-SAH; Table 3 reports methylated NAM analogue values. 5 Table 3 lists 20p: pKd 8.6. auto_single_measurement only accepted activity measurement [1] 1 structures\9GVM\9GVM_metadata.json point structures/9GVM/9gvm_protein.pdb structures/9GVM/9gvm_pocket.pdb structures/9GVM/9gvm_ligand.sdf structures/9GVM/9gvm_ligand.pdb structures/9GVM/9gvm_ligand.cif structures/9GVM/9gvm_complex.pdb structures/9GVM/9gvm_complex.cif 9GVW classic NNMT Na Na Na 4 "[""A1IPO""]" 1 pKd Kd = = 6.5 -log10(M) 316.22776601683796 [] p_metric_transform 6.5 success True direct_binding Binding of compound 4 to NNMT-SAH. 3 Figure 3 lists compound 4: pKd(SAH) = 6.5. auto_single_measurement only accepted activity measurement [1] 1 structures\9GVW\9GVW_metadata.json point structures/9GVW/9gvw_protein.pdb structures/9GVW/9gvw_pocket.pdb structures/9GVW/9gvw_ligand.sdf structures/9GVW/9gvw_ligand.pdb structures/9GVW/9gvw_ligand.cif structures/9GVW/9gvw_complex.pdb structures/9GVW/9gvw_complex.cif 9GWA classic NNMT Na Na Na 5 "[""A1IQR""]" 1 pKd Kd = = 7.2 -log10(M) 63.0957344480193 [] p_metric_transform 7.2 success True direct_binding Binding of compound 5 to NNMT-SAH. 3 Figure 3 lists compound 5: pKd(SAH) = 7.2. auto_single_measurement only accepted activity measurement [1] 1 structures\9GWA\9GWA_metadata.json point structures/9GWA/9gwa_protein.pdb structures/9GWA/9gwa_pocket.pdb structures/9GWA/9gwa_ligand.sdf structures/9GWA/9gwa_ligand.pdb structures/9GWA/9gwa_ligand.cif structures/9GWA/9gwa_complex.pdb structures/9GWA/9gwa_complex.cif 9GY3 classic CRBN Na His6-tagged CRBNmidi Na (S)-dHTC1 (compound 7) "[""A1IQT""]" 1 Kd Kd = = 63 µM 63000.0 [] unit_conversion 4.200659450546418 success True direct_binding Binary CRBNmidi surface-plasmon-resonance assay. 27 Extended Data Fig. 4f prints Kd = 63 µM for (S)-dHTC1 in the CRBNmidi SPR (binary) assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9GY3\9GY3_metadata.json point structures/9GY3/9gy3_protein.pdb structures/9GY3/9gy3_pocket.pdb structures/9GY3/9gy3_ligand.sdf structures/9GY3/9gy3_ligand.pdb structures/9GY3/9gy3_ligand.cif structures/9GY3/9gy3_complex.pdb structures/9GY3/9gy3_complex.cif 9GY6 classic M. smegmatis Mtb-like cytochrome bc1:aa3 Mycobacterium smegmatis M. smegmatis cytochrome bc Mtb-like complex with an M. tuberculosis-like Qp binding site F156Y; I182M; M189L; D309E; I312A JNJ-2901 "[""A1IRE""]" 1 IC50 IC50 = = 17.4 (±4.8) nM 17.4 [] unit_conversion 7.7594507517174005 success True biochemical_inhibition Oxygen-consumption inhibition assay on purified isolated M. smegmatis cytochrome bc Mtb-like protein; values from three independent experiments. 3 “the inhibitory action of both inhibitors on cytochrome bcMtb-like are similar, with IC50 values of 17.4 (±4.8) and 22.4 (±8.4) nM, respectively” for JNJ-2901 and Q203. auto_single_measurement only accepted activity measurement [1] 1 structures\9GY6\9GY6_metadata.json point structures/9GY6/9gy6_protein.pdb structures/9GY6/9gy6_pocket.pdb structures/9GY6/9gy6_ligand.sdf structures/9GY6/9gy6_ligand.pdb structures/9GY6/9gy6_ligand.cif structures/9GY6/9gy6_complex.pdb structures/9GY6/9gy6_complex.cif 9GYP extended Histidine Triad Nucleotide-Binding Protein 1 (HINT1) human Na Na KV24 (KV-24) "[""A1IQU""]" 1 IC50 IC50 = = 12.3 μM 12300.0 [] unit_conversion 4.910094888560602 success True biochemical_inhibition Recombinant HINT1 enzyme activity assay; inhibition of HINT1 activity. 5 Both compounds effectively inhibited HINT1 activity, with IC50 = 12.3 μM for KV-24; page 6 identifies the KV-24–bound HINT1 cocrystal as PDB 9GYP. auto_single_measurement only accepted activity measurement [1] 1 structures\9GYP\9GYP_metadata.json point structures/9GYP/9gyp_protein.pdb structures/9GYP/9gyp_pocket.pdb structures/9GYP/9gyp_ligand.pdb structures/9GYP/9gyp_ligand.cif structures/9GYP/9gyp_complex.pdb structures/9GYP/9gyp_complex.cif 9GYQ classic Histidine Triad Nucleotide-Binding Protein 1 (HINT1) human Na Na KV30 (KV-30) "[""A1IQV""]" 1 IC50 IC50 = = 12.6 μM 12600.0 [] unit_conversion 4.8996294548824375 success True biochemical_inhibition Recombinant HINT1 enzyme activity assay; inhibition of HINT1 activity. 5 Both compounds effectively inhibited HINT1 activity, with IC50 = 12.6 μM for KV-30; page 6 identifies the KV-30–bound HINT1 cocrystal as PDB 9GYQ. auto_single_measurement only accepted activity measurement [1] 1 structures\9GYQ\9GYQ_metadata.json point structures/9GYQ/9gyq_protein.pdb structures/9GYQ/9gyq_pocket.pdb structures/9GYQ/9gyq_ligand.sdf structures/9GYQ/9gyq_ligand.pdb structures/9GYQ/9gyq_ligand.cif structures/9GYQ/9gyq_complex.pdb structures/9GYQ/9gyq_complex.cif 9GZ1 classic human beta-cardiac heavy meromyosin (cHMM; MYH7) Human cHMM encoding MYH7 residues 1-1137, with 42 heptad repeats of S2 and a C-terminal FLAG tag at residues 1138-1146 Na mavacamten "[""XB2""]" 1 IC50 IC50 = = 0.14 ± 0.01 μM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition In vitro actin-filament gliding/motility assay with cHMM; Supplementary Table 1 reports inhibition of cardiac myosin motor activity by mavacamten. 37 Supplementary Table 1 lists cHMM IC50 = 0.14 ± 0.01 μM; the Results text identifies 0.14 μM as the concentration reducing cHMM motility by 50%. auto_single_measurement only accepted activity measurement [1] 1 structures\9GZ1\9GZ1_metadata.json point structures/9GZ1/9gz1_protein.pdb structures/9GZ1/9gz1_pocket.pdb structures/9GZ1/9gz1_ligand.sdf structures/9GZ1/9gz1_ligand.pdb structures/9GZ1/9gz1_ligand.cif structures/9GZ1/9gz1_complex.pdb structures/9GZ1/9gz1_complex.cif 9GZ2 classic human beta-cardiac heavy meromyosin (cHMM; MYH7) Human cHMM encoding MYH7 residues 1-1137, with 42 heptad repeats of S2 and a C-terminal FLAG tag at residues 1138-1146 Na mavacamten "[""XB2""]" 1 IC50 IC50 = = 0.14 ± 0.01 μM 140.0 [] unit_conversion 6.853871964321762 success True biochemical_inhibition In vitro actin-filament gliding/motility assay with cHMM; Supplementary Table 1 reports inhibition of cardiac myosin motor activity by mavacamten. 37 Supplementary Table 1 lists cHMM IC50 = 0.14 ± 0.01 μM; the Results text identifies 0.14 μM as the concentration reducing cHMM motility by 50%. auto_single_measurement only accepted activity measurement [1] 1 structures\9GZ2\9GZ2_metadata.json point structures/9GZ2/9gz2_protein.pdb structures/9GZ2/9gz2_pocket.pdb structures/9GZ2/9gz2_ligand.sdf structures/9GZ2/9gz2_ligand.pdb structures/9GZ2/9gz2_ligand.cif structures/9GZ2/9gz2_complex.pdb structures/9GZ2/9gz2_complex.cif 9H0P extended Fucosylated Lacto-N-biose binding protein (BiGFL-BP; Blon_0883) Bifidobacterium longum subsp. infantis Mature Blon_0883 peptide, amino acids 24-460 Na H1 trisaccharide (H type 1 trisaccharide) "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 158 ± 9.0 nM 158.0 [] unit_conversion 6.801342913045577 success True direct_binding Steady-state surface plasmon resonance analysis at 25°C; the H1 trisaccharide was not analyzed by ITC. 5 Table 1 lists H1 Kd as [158 ± 9.0] nM; footnote a assigns bracketed Kd values to steady-state SPR, and footnote b states H1 trisaccharides were not analyzed by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\9H0P\9H0P_metadata.json point structures/9H0P/9h0p_protein.pdb structures/9H0P/9h0p_pocket.pdb structures/9H0P/9h0p_ligand.pdb structures/9H0P/9h0p_ligand.cif structures/9H0P/9h0p_complex.pdb structures/9H0P/9h0p_complex.cif 9H0Q classic BC2L-C lectin, N-terminal domain (BC2L-C-Nt) Burkholderia cenocepacia Recombinant BC2L-C-Nt expressed in E. coli BL21star(DE3) from pCold-TF-TF-BC2L-C-Nt Na compound 1; N-(beta-L-Fucopyranosyl)-biphenyl-3-carboxamide "[""MJO""]" 1 Kd Kd = = 330 ± 42 µM 330000.0 [] unit_conversion 3.481486060122113 success True direct_binding Direct-interaction SPR assay with immobilized BC2L-C-Nt. 3 Table 1 reports BC2L-C-Nt KD 330 ± 42 µM for compound 1. auto_single_measurement only accepted activity measurement [1] 1 structures\9H0Q\9H0Q_metadata.json point structures/9H0Q/9h0q_protein.pdb structures/9H0Q/9h0q_pocket.pdb structures/9H0Q/9h0q_ligand.sdf structures/9H0Q/9h0q_ligand.pdb structures/9H0Q/9h0q_ligand.cif structures/9H0Q/9h0q_complex.pdb structures/9H0Q/9h0q_complex.cif 9H0S classic Cyclophilin D (CypD) Na Na Na compound 12a "[""9CK""]" 2 Kd Kd = = 60 ± 4 nM 60.0 [] unit_conversion 7.221848749616356 success True direct_binding Isothermal titration calorimetry (ITC). 4 Table 1 reports compound 12a: Kd = 60 ± 4 nM; the table footnote states Kd was measured by ITC. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9H0S\9H0S_metadata.json point structures/9H0S/9h0s_protein.pdb structures/9H0S/9h0s_pocket.pdb structures/9H0S/9h0s_ligand.sdf structures/9H0S/9h0s_ligand.pdb structures/9H0S/9h0s_ligand.cif structures/9H0S/9h0s_complex.pdb structures/9H0S/9h0s_complex.cif 9H0W classic Human Carbonic Anhydrase II human Na Na beta-Thujaplicin (2-hydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one; beta-TJP) "[""A1IRU""]" 1 Ki Ki = = 90.6 µM 90600.0 [] unit_conversion 4.042871802323187 success True biochemical_inhibition Stopped-flow CO2 hydration inhibition assay. 6 Table 1 reports β-TJP (TJP) Ki = 90.6 µM against hCA II; page 15 specifies the stopped-flow CO2 hydration assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9H0W\9H0W_metadata.json point structures/9H0W/9h0w_protein.pdb structures/9H0W/9h0w_pocket.pdb structures/9H0W/9h0w_ligand.sdf structures/9H0W/9h0w_ligand.pdb structures/9H0W/9h0w_ligand.cif structures/9H0W/9h0w_complex.pdb structures/9H0W/9h0w_complex.cif 9H0X classic ProA Legionella pneumophila native ProA Na inhibitor 6 "[""A1IRK""]" 1 IC50 IC50 = = 1.015 µM 1014.9999999999999 [] unit_conversion 5.993533957750769 success True biochemical_inhibition Azocasein protease-activity assay using 0.5 µM ProA; four-parameter nonlinear regression of OD420 versus compound concentration. 5 Fig. 2B prints an IC50 of 1.015 µM for compound 6; the caption identifies this as inhibitory activity of L. pneumophila ProA in an azocasein assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9H0X\9H0X_metadata.json point structures/9H0X/9h0x_protein.pdb structures/9H0X/9h0x_pocket.pdb structures/9H0X/9h0x_ligand.sdf structures/9H0X/9h0x_ligand.pdb structures/9H0X/9h0x_ligand.cif structures/9H0X/9h0x_complex.pdb structures/9H0X/9h0x_complex.cif 9H0Y classic ProA Legionella pneumophila native ProA Na inhibitor 7 "[""A1IRL""]" 1 IC50 IC50 = = 0.9641 µM 964.0999999999999 [] unit_conversion 6.01587791713889 success True biochemical_inhibition Azocasein protease-activity assay using 0.5 µM ProA; four-parameter nonlinear regression of OD420 versus compound concentration. 5 Fig. 2B prints an IC50 of 0.9641 µM for compound 7; the caption identifies this as inhibitory activity of L. pneumophila ProA in an azocasein assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9H0Y\9H0Y_metadata.json point structures/9H0Y/9h0y_protein.pdb structures/9H0Y/9h0y_pocket.pdb structures/9H0Y/9h0y_ligand.sdf structures/9H0Y/9h0y_ligand.pdb structures/9H0Y/9h0y_ligand.cif structures/9H0Y/9h0y_complex.pdb structures/9H0Y/9h0y_complex.cif 9H4D classic IL-17A homodimer Na Na Na compound 18 "[""A1ISH""]" 1 IC50 IC50 = = 0.094* µM 94.0 [] unit_conversion 7.026872146400302 success True biochemical_inhibition TR-FRET assay measuring binding of IL-17A to IL-17RA; single measurement. 4 Table 2 lists compound 18 with IL-17A IC50 0.094* µM. Its footnote defines the IL-17A assay as a TR-FRET assay measuring IL-17A binding to IL-17RA; the asterisk denotes a single measurement. Figure 4 assigns compound 18 to PDB 9H4D. auto_single_measurement only accepted activity measurement [1] 1 structures\9H4D\9H4D_metadata.json point structures/9H4D/9h4d_protein.pdb structures/9H4D/9h4d_pocket.pdb structures/9H4D/9h4d_ligand.sdf structures/9H4D/9h4d_ligand.pdb structures/9H4D/9h4d_ligand.cif structures/9H4D/9h4d_complex.pdb structures/9H4D/9h4d_complex.cif 9H4O classic IL-17A homodimer Na Na Na compound 11 "[""A1ISG""]" 1 IC50 IC50 = = 0.035 ± 0.003 µM 35.0 [] unit_conversion 7.455931955649724 success True biochemical_inhibition TR-FRET assay measuring binding of IL-17A to IL-17RA. 3 Table 1 lists compound 11 with IL-17A IC50 0.035 ± 0.003 µM. The Table 1 footnote defines this as a TR-FRET assay measuring binding of IL-17A to IL-17RA. Figure 3 assigns compound 11 to PDB 9H4O. auto_single_measurement only accepted activity measurement [1] 1 structures\9H4O\9H4O_metadata.json point structures/9H4O/9h4o_protein.pdb structures/9H4O/9h4o_pocket.pdb structures/9H4O/9h4o_ligand.sdf structures/9H4O/9h4o_ligand.pdb structures/9H4O/9h4o_ligand.cif structures/9H4O/9h4o_complex.pdb structures/9H4O/9h4o_complex.cif 9H5E classic NNMT Na Na Na 1p "[""A1ISJ""]" 1 pKd Kd = = 8.2 -log10(M) 6.309573444801943 [] p_metric_transform 8.2 success True direct_binding Product binding to NNMT-SAH; Table 3 reports methylated NAM analogue values. 5 Table 3 lists 1p: pKd 8.2. auto_single_measurement only accepted activity measurement [1] 1 structures\9H5E\9H5E_metadata.json point structures/9H5E/9h5e_protein.pdb structures/9H5E/9h5e_pocket.pdb structures/9H5E/9h5e_ligand.sdf structures/9H5E/9h5e_ligand.pdb structures/9H5E/9h5e_ligand.cif structures/9H5E/9h5e_complex.pdb structures/9H5E/9h5e_complex.cif 9H5O classic NNMT Na Na Na 20s "[""A1IPM""]" 1 pIC50 IC50 = = 6.6 -log10(M) 251.18864315095823 [] p_metric_transform 6.6 success True biochemical_inhibition Biochemical inhibition by R6-methylamine substrate analogue 20s; the paper identifies this inhibitor class as NAM-competitive and SAM-uncompetitive. 5 Table 2 lists 20s (R6 = NHCH3, R4 = CH3): pIC50 6.6. auto_single_measurement only accepted activity measurement [1] 1 structures\9H5O\9H5O_metadata.json point structures/9H5O/9h5o_protein.pdb structures/9H5O/9h5o_pocket.pdb structures/9H5O/9h5o_ligand.sdf structures/9H5O/9h5o_ligand.pdb structures/9H5O/9h5o_ligand.cif structures/9H5O/9h5o_complex.pdb structures/9H5O/9h5o_complex.cif 9H7A classic Transthyretin Human Na Na 3,5-Dichlorobenzenesulfonamide; SFL000006 (DSF) "[""6OT""]" 1 IC50 IC50 = = 8880.24 ± 3670.65 µM 8880240.0 [] unit_conversion 2.051575296691314 success True biochemical_inhibition 125I-thyroxine displacement assay in neat normal human plasma; mean ± SD, N=3. 17 Table 3 reports SFL000006 (DSF) mean 125I-T4 IC50 of 8880.24 ± 3670.65 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9H7A\9H7A_metadata.json point structures/9H7A/9h7a_protein.pdb structures/9H7A/9h7a_pocket.pdb structures/9H7A/9h7a_ligand.sdf structures/9H7A/9h7a_ligand.pdb structures/9H7A/9h7a_ligand.cif structures/9H7A/9h7a_complex.pdb structures/9H7A/9h7a_complex.cif 9H7D classic Transthyretin Human Na Na 2-(Phenylamino)benzoic Acid "[""EHO""]" 1 IC50 IC50 = = 179.67 ± 61.77 µM 179670.0 [] unit_conversion 3.745524432196129 success True biochemical_inhibition 125I-thyroxine displacement assay in neat normal human plasma; mean ± SD, N=3. 17 Table 3 reports N-Phenylanthranilic Acid mean 125I-T4 IC50 of 179.67 ± 61.77 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9H7D\9H7D_metadata.json point structures/9H7D/9h7d_protein.pdb structures/9H7D/9h7d_pocket.pdb structures/9H7D/9h7d_ligand.sdf structures/9H7D/9h7d_ligand.pdb structures/9H7D/9h7d_ligand.cif structures/9H7D/9h7d_complex.pdb structures/9H7D/9h7d_complex.cif 9H7F classic Transthyretin Human Na Na 3,5-Dichloroaniline "[""A1ISU""]" 1 IC50 IC50 = = 802.42 ± 319.39 µM 802420.0 [] unit_conversion 3.0955982552351573 success True biochemical_inhibition 125I-thyroxine displacement assay in neat normal human plasma; mean ± SD, N=3. 17 Table 3 reports 3,5-Dichloroaniline mean 125I-T4 IC50 of 802.42 ± 319.39 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9H7F\9H7F_metadata.json point structures/9H7F/9h7f_protein.pdb structures/9H7F/9h7f_pocket.pdb structures/9H7F/9h7f_ligand.sdf structures/9H7F/9h7f_ligand.pdb structures/9H7F/9h7f_ligand.cif structures/9H7F/9h7f_complex.pdb structures/9H7F/9h7f_complex.cif 9H81 extended human carbonic anhydrase I human Na Na Sonepiprazole "[""A1IS9""]" 1 Ki Ki = = 89.6 nM 89.6 [] unit_conversion 7.047691990337874 success True biochemical_inhibition Stopped-flow CO2 hydration assay; Table 1 reports Ki values as means from three different assays. 2 Table 1, “Inhibition Data of All Catalytically Active Human CA Isoforms for Sonepiprazole,” reports hCA I Ki = 89.6 nM. The table caption specifies a stopped-flow CO2 hydration assay. Figure 2 identifies the sonepiprazole-bound hCA I structure as PDB 9H81. auto_single_measurement only accepted activity measurement [1] 1 structures\9H81\9H81_metadata.json point structures/9H81/9h81_ligand.sdf structures/9H81/9h81_ligand.cif structures/9H81/9h81_complex.cif 9H8U extended SorD Penicillium chrysogenum C-terminally His6-tagged SorD Na sorbicillin "[""A1ITD""]" 1 Kd Kd = = 1.2 ± 1.6 µM 1200.0 [] unit_conversion 5.920818753952375 success True direct_binding Microscale thermophoresis binding analysis. 8 “Binding analysis using microscale thermophoresis also showed that SorD could bind to sorbicillin with a KD of 1.2 ± 1.6 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9H8U\9H8U_metadata.json point structures/9H8U/9h8u_protein.pdb structures/9H8U/9h8u_pocket.pdb structures/9H8U/9h8u_ligand.pdb structures/9H8U/9h8u_ligand.cif structures/9H8U/9h8u_complex.pdb structures/9H8U/9h8u_complex.cif 9H8Z extended SorC Penicillium chrysogenum N-terminally His6- and SUMO-tagged SorC Na sorbicillin "[""A1ITD""]" 1 Kd Kd = = 940 ± 93 nM 940.0 [] unit_conversion 6.026872146400301 success True direct_binding Microscale thermophoresis binding analysis. 6 “Binding between SorC and sorbicillin ... confirmed using microscale thermophoresis, with a KD of 940 ± 93 nM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9H8Z\9H8Z_metadata.json point structures/9H8Z/9h8z_protein.pdb structures/9H8Z/9h8z_pocket.pdb structures/9H8Z/9h8z_ligand.pdb structures/9H8Z/9h8z_ligand.cif structures/9H8Z/9h8z_complex.pdb structures/9H8Z/9h8z_complex.cif 9HB0 classic Plasmodium falciparum plasmepsin X (PMX) Plasmodium falciparum Recombinant PMX from a codon-optimized P. falciparum 3D7 PMX gene, with native signal sequence and a C-terminal EPEA C-tag, expressed in Spodoptera frugiperda Sf21 cells Na 7k "[""A1ITU""]" 2 Kd Kd = = 0.60 ± 0.09 nM 0.6 [] unit_conversion 9.221848749616356 success True direct_binding Surface plasmon resonance binding of 7k to surface-immobilised rPMX; table reports mean ± SEM from multiple independent assays (n=4 for 7k). 4 Figure 2A SPR table reports for 7k: KD = 0.60 ± 0.09 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9HB0\9HB0_metadata.json point structures/9HB0/9hb0_protein.pdb structures/9HB0/9hb0_pocket.pdb structures/9HB0/9hb0_ligand.sdf structures/9HB0/9hb0_ligand.pdb structures/9HB0/9hb0_ligand.cif structures/9HB0/9hb0_complex.pdb structures/9HB0/9hb0_complex.cif 9HD2 classic human TRF1 human TRF1_TRFH residues 47-268 with an N-terminal His6-MBP tag Na compound 40 "[""A1ITY""]" 1 Kd Kd = = 29 µM 29000.0 [] unit_conversion 4.5376020021010435 success True direct_binding LO-NMR R2KD assay; six aromatic proton peak relaxation rates. 11 Figure 5 caption reports LO-NMR R2KD K_D of 29 µM (95% CI: 20–41 µM) for compound 40. auto_single_measurement only accepted activity measurement [1] 1 structures\9HD2\9HD2_metadata.json point structures/9HD2/9hd2_protein.pdb structures/9HD2/9hd2_pocket.pdb structures/9HD2/9hd2_ligand.sdf structures/9HD2/9hd2_ligand.pdb structures/9HD2/9hd2_ligand.cif structures/9HD2/9hd2_complex.pdb structures/9HD2/9hd2_complex.cif 9HD3 classic human TRF1 human TRF1_TRFH residues 47-268 with an N-terminal His6-MBP tag Na compound 27 "[""A1ITX""]" 1 Kd Kd = = 280 µM 280000.0 [] unit_conversion 3.5528419686577806 success True direct_binding LO-NMR R2KD assay. 5 The R2KD assay for NMR fragment-screen hit 27 revealed K_D 280 µM (95% CI: 230–350 µM). auto_single_measurement only accepted activity measurement [1] 1 structures\9HD3\9HD3_metadata.json point structures/9HD3/9hd3_protein.pdb structures/9HD3/9hd3_pocket.pdb structures/9HD3/9hd3_ligand.sdf structures/9HD3/9hd3_ligand.pdb structures/9HD3/9hd3_ligand.cif structures/9HD3/9hd3_complex.pdb structures/9HD3/9hd3_complex.cif 9HDV classic Orotidine 5'-monophosphate decarboxylase domain of human UMPS human Orotidine 5'-monophosphate decarboxylase domain of human UMPS Na YMP (1-(beta-D-ribofuranosyl) cyanuric acid-5'-monophosphate) "[""A1IT4""]" 1 Kd Kd = = 57.2 ± 10.2 nM 57.2 [] unit_conversion 7.242603971206976 success True direct_binding ITC at 25 °C. 4 Table 1 reports YMP K_D = 57.2 ± 10.2 nM for human OMPDCase. auto_single_measurement only accepted activity measurement [1] 1 structures\9HDV\9HDV_metadata.json point structures/9HDV/9hdv_protein.pdb structures/9HDV/9hdv_pocket.pdb structures/9HDV/9hdv_ligand.sdf structures/9HDV/9hdv_ligand.pdb structures/9HDV/9hdv_ligand.cif structures/9HDV/9hdv_complex.pdb structures/9HDV/9hdv_complex.cif 9HDX classic Orotidine 5'-monophosphate decarboxylase domain of human UMPS human Orotidine 5'-monophosphate decarboxylase domain of human UMPS wild-type dTMP (TMP) "[""TMP""]" 1 Kd Kd = = 118.6 ± 8.8 μM 118600.0 [] unit_conversion 3.9259153109717566 success True direct_binding ITC at 25 °C. 4 Table 1 reports dTMP K_D = 118.6 ± 8.8 μM; the main text identifies wild-type OMPDC with dTMP. auto_single_measurement only accepted activity measurement [1] 1 structures\9HDX\9HDX_metadata.json point structures/9HDX/9hdx_protein.pdb structures/9HDX/9hdx_pocket.pdb structures/9HDX/9hdx_ligand.sdf structures/9HDX/9hdx_ligand.pdb structures/9HDX/9hdx_ligand.cif structures/9HDX/9hdx_complex.pdb structures/9HDX/9hdx_complex.cif 9HEH classic MkcA (DSOMK10_RS0100305) Dickeya solani MK10 MkcA ligand-binding domain, residues 54-340 Na choline "[""CHT""]" 1 Kd Kd = = 2.8 ± 0.3 µM 2800.0 [] unit_conversion 5.552841968657781 success True direct_binding Isothermal titration calorimetry (ITC) of purified MkcA-LBD. 6 Table 1 reports MkcA-LBD binding choline by ITC with Kd 2.8 ± 0.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9HEH\9HEH_metadata.json point structures/9HEH/9heh_protein.pdb structures/9HEH/9heh_pocket.pdb structures/9HEH/9heh_ligand.sdf structures/9HEH/9heh_ligand.pdb structures/9HEH/9heh_ligand.cif structures/9HEH/9heh_complex.pdb structures/9HEH/9heh_complex.cif 9HF4 classic human TRF1 human TRF1_TRFH residues 47-268 with an N-terminal His6-MBP tag Na compound 32 "[""A1IUC""]" 1 Kd Kd = = 61 µM 61000.0 [] unit_conversion 4.214670164989233 success True direct_binding R2KD LO-NMR; global K_D shared across at least four 1H-NMR peaks. 10 Table 2 lists compound 32 K_D 61 µM (95% CI: 45–82 µM). auto_single_measurement only accepted activity measurement [1] 1 structures\9HF4\9HF4_metadata.json point structures/9HF4/9hf4_protein.pdb structures/9HF4/9hf4_pocket.pdb structures/9HF4/9hf4_ligand.sdf structures/9HF4/9hf4_ligand.pdb structures/9HF4/9hf4_ligand.cif structures/9HF4/9hf4_complex.pdb structures/9HF4/9hf4_complex.cif 9HFU extended SPOP (speckle-type BTB/POZ protein) Homo sapiens SPOP MATH domain, residues 28-116 Na Caprin1 peptide, 426QPEATQVPLVSSTSEGY442 "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 ~ ~ 2.6 ± 1.3 µM 2600.0 [] unit_conversion 5.585026652029182 success True direct_binding Fluorescence-polarization competition assay with a 17-mer Caprin1 peptide. 10 Figure 5C reports Caprin1 QPEATQVPLVSSTSEGY, IC50 ~2.6 ± 1.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9HFU\9HFU_metadata.json point structures/9HFU/9hfu_protein.pdb structures/9HFU/9hfu_pocket.pdb structures/9HFU/9hfu_ligand.pdb structures/9HFU/9hfu_ligand.cif structures/9HFU/9hfu_complex.pdb structures/9HFU/9hfu_complex.cif 9HFW extended SPOP (speckle-type BTB/POZ protein) Homo sapiens SPOP MATH domain, residues 28-116 Na SRC-3 (NCoA-3) peptide, 91NDDDVQKADVSSTGQGV107 "[""CHAIN:B""]" 1 IC50 IC50 ~ ~ 16.9 ± 2.7 µM 16900.0 [] unit_conversion 4.772113295386326 success True direct_binding Fluorescence-polarization competition assay with a 17-mer SRC-3 peptide. 10 Figure 5C reports SRC-3 NDDDVQKADVSSTGQGV, IC50 ~16.9 ± 2.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9HFW\9HFW_metadata.json point structures/9HFW/9hfw_protein.pdb structures/9HFW/9hfw_pocket.pdb structures/9HFW/9hfw_ligand.pdb structures/9HFW/9hfw_ligand.cif structures/9HFW/9hfw_complex.pdb structures/9HFW/9hfw_complex.cif 9HGD extended GABARAP human GST fusion protein; thrombin-cleaved 119-aa protein with an N-terminal Gly-Ser extension Na GAB_D23 "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 36.0 nM 36.0 [] unit_conversion 7.443697499232712 success True direct_binding SPR nine-point single-cycle kinetics experiment. 5 Fig. 3e reports affinity determination of GAB_D23 using SPR and prints Kd 36.0 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 3 structures\9HGD\9HGD_metadata.json point structures/9HGD/9hgd_protein.pdb structures/9HGD/9hgd_pocket.pdb structures/9HGD/9hgd_ligand.pdb structures/9HGD/9hgd_ligand.cif structures/9HGD/9hgd_complex.pdb structures/9HGD/9hgd_complex.cif 9HGG extended SPOP (speckle-type BTB/POZ protein) Homo sapiens SPOP MATH domain, residues 28-116 Na SETD2 peptide, 363DKGSVQAPEISSNSIKD1379 "[""CHAIN:B""]" 1 IC50 IC50 ~ ~ 699 ± 748.7 µM 699000.0 [] unit_conversion 3.1555228242543185 success True direct_binding Fluorescence-polarization competition assay with a 17-mer SETD2 peptide. 10 Figure 5C reports SETD2 DKGSVQAPEISSNSIKD, IC50 ~699 ± 748.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9HGG\9HGG_metadata.json point structures/9HGG/9hgg_protein.pdb structures/9HGG/9hgg_pocket.pdb structures/9HGG/9hgg_ligand.pdb structures/9HGG/9hgg_ligand.cif structures/9HGG/9hgg_complex.pdb structures/9HGG/9hgg_complex.cif 9HGM classic human DNMT2 human DNMT2Δ47, lacking residues 191-237 deletion of residues 191-237 (Δ47) compound 3 "[""A1IUL""]" 1 Kd Kd = = 10 ± 2 µM 10000.0 [] unit_conversion 5.0 success True direct_binding MST binding measurement; comparison states compound 3 affinity against wild-type versus DNMT2Δ47 enzyme. 5 “compound 3 displays medium-range micromolar affinity (48 vs. 10 ±2 µM) against both wild-type and DNMT2Δ47 enzymes (Figure 1E vs. Figure S3G).” auto_single_measurement only accepted activity measurement [1] 1 structures\9HGM\9HGM_metadata.json point structures/9HGM/9hgm_protein.pdb structures/9HGM/9hgm_pocket.pdb structures/9HGM/9hgm_ligand.sdf structures/9HGM/9hgm_ligand.pdb structures/9HGM/9hgm_ligand.cif structures/9HGM/9hgm_complex.pdb structures/9HGM/9hgm_complex.cif 9HH5 classic SARS-CoV-2 Nsp15 endoribonuclease SARS-CoV-2 Na Na Sepantronium (YM-155) "[""GXU""]" 1 IC50 IC50 = = 1.2 (0.001–162.4) µM 1200.0 [] unit_conversion 5.920818753952375 success True biochemical_inhibition Nsp15 enzymatic inhibition assay in DTT-containing buffer; Table 1 reports IC50 ± DTT. 5 Table 1 lists YM-155 with IC50 ± DTT of 1.2 (0.001–162.4) µM. Table 2 maps PDB 9HH5 to the Nsp15–YM-155 structure. auto_single_measurement only accepted activity measurement [1] 1 structures\9HH5\9HH5_metadata.json point structures/9HH5/9hh5_protein.pdb structures/9HH5/9hh5_pocket.pdb structures/9HH5/9hh5_ligand.sdf structures/9HH5/9hh5_ligand.pdb structures/9HH5/9hh5_ligand.cif structures/9HH5/9hh5_complex.pdb structures/9HH5/9hh5_complex.cif 9HH6 classic SARS-CoV-2 Nsp15 endoribonuclease SARS-CoV-2 Na Na TAS-103 "[""A1IUV""]" 1 IC50 IC50 = = 6.6 (3.9–8.4) µM 6600.0 [] unit_conversion 5.180456064458131 success True biochemical_inhibition Nsp15 enzymatic inhibition assay in DTT-containing buffer; Table 1 reports IC50 ± DTT. 5 Table 1 lists TAS-103 (dihydrochloride) with IC50 ± DTT of 6.6 (3.9–8.4) µM. Table 2 maps PDB 9HH6 to the Nsp15–TAS-103 structure. auto_single_measurement only accepted activity measurement [1] 1 structures\9HH6\9HH6_metadata.json point structures/9HH6/9hh6_protein.pdb structures/9HH6/9hh6_pocket.pdb structures/9HH6/9hh6_ligand.sdf structures/9HH6/9hh6_ligand.pdb structures/9HH6/9hh6_ligand.cif structures/9HH6/9hh6_complex.pdb structures/9HH6/9hh6_complex.cif 9HH7 extended PfBDP1 Plasmodium falciparum Na Na RMM23 "[""A1IUW""]" 1 Kd Kd = = 1.24 µM 1240.0 [] unit_conversion 5.906578314837764 success True direct_binding ITC characterization of synthesized compounds with PfBDP1-BRD. 2 Table 1 reports RMM23 K_D = 1.24 µM for PfBDP1-BRD by ITC; page 3 identifies PfBDP1-BRD–RMM23 as PDB 9HH7. auto_single_measurement only accepted activity measurement [1] 1 structures\9HH7\9HH7_metadata.json point structures/9HH7/9hh7_protein.pdb structures/9HH7/9hh7_pocket.pdb structures/9HH7/9hh7_ligand.pdb structures/9HH7/9hh7_ligand.cif structures/9HH7/9hh7_complex.pdb structures/9HH7/9hh7_complex.cif 9HHC classic PfBDP1 Plasmodium falciparum Na Na MPM2 "[""I5K""]" 1 Kd Kd = = 6.74 µM 6740.0 [] unit_conversion 5.17134010346468 success True direct_binding ITC characterization of synthesized compounds with PfBDP1-BRD. 2 Table 1 reports MPM2 K_D = 6.74 µM for PfBDP1-BRD by ITC; page 2 identifies the PfBDP1-BRD–MPM2 co-crystal as PDB 9HHC. auto_single_measurement only accepted activity measurement [1] 1 structures\9HHC\9HHC_metadata.json point structures/9HHC/9hhc_protein.pdb structures/9HHC/9hhc_pocket.pdb structures/9HHC/9hhc_ligand.sdf structures/9HHC/9hhc_ligand.pdb structures/9HHC/9hhc_ligand.cif structures/9HHC/9hhc_complex.pdb structures/9HHC/9hhc_complex.cif 9HHD extended PfBDP1 Plasmodium falciparum Na Na RMM2 "[""A1IUZ""]" 1 Kd Kd = = 3.94 µM 3940.0 [] unit_conversion 5.404503778174426 success True direct_binding ITC characterization of synthesized compounds with PfBDP1-BRD. 2 Table 1 reports RMM2 K_D = 3.94 µM for PfBDP1-BRD by ITC; page 2 identifies the PfBDP1-BRD–RMM2 co-crystal as PDB 9HHD. auto_single_measurement only accepted activity measurement [1] 1 structures\9HHD\9HHD_metadata.json point structures/9HHD/9hhd_protein.pdb structures/9HHD/9hhd_pocket.pdb structures/9HHD/9hhd_ligand.pdb structures/9HHD/9hhd_ligand.cif structures/9HHD/9hhd_complex.pdb structures/9HHD/9hhd_complex.cif 9HHY classic 2-methylisocitrate lyase (PrpB) Coxiella burnetii Na Na isocitric acid (isocitrate) "[""ICT""]" 1 Ki Ki = = 11 ± 2 mM 11000000.0 [] unit_conversion 1.9586073148417746 success True biochemical_inhibition Morrison Ki assay using constant 200 nM PrpB and 500 μM 2-MIC; continuous coupled assay with lactate dehydrogenase. 5 “a 2-MIC concentration of 500 μM, gave a Morrison Ki of 11 ± 2 mM (Fig. 3B)” for WT CbPrpB; Figure 3 identifies isocitrate as the inhibitor. auto_single_measurement only accepted activity measurement [1] 1 structures\9HHY\9HHY_metadata.json point structures/9HHY/9hhy_protein.pdb structures/9HHY/9hhy_pocket.pdb structures/9HHY/9hhy_ligand.sdf structures/9HHY/9hhy_ligand.pdb structures/9HHY/9hhy_ligand.cif structures/9HHY/9hhy_complex.pdb structures/9HHY/9hhy_complex.cif 9HIP classic MnmE-MnmG complex E. coli Na Na GppNHp "[""FAD""]" 1 Kd Kd = = 7 ± 1 µM 7000.0 [] unit_conversion 5.154901959985743 success True direct_binding Fluorescence titration of FAD binding to MnmG with MnmE in the GppNHp-bound state. 8 Table 1 reports MnmG + MnmE-GppNHp FAD-binding affinity K_D = 7 ± 1 µM; the text states this condition corresponds to the α2β2 and α4β2 structures. auto_single_measurement only accepted activity measurement [1] 1 structures\9HIP\9HIP_metadata.json point structures/9HIP/9hip_protein.pdb structures/9HIP/9hip_pocket.pdb structures/9HIP/9hip_ligand.sdf structures/9HIP/9hip_ligand.pdb structures/9HIP/9hip_ligand.cif structures/9HIP/9hip_complex.pdb structures/9HIP/9hip_complex.cif 9HIQ classic MnmE-MnmG complex E. coli Na Na GppNHp "[""FAD""]" 1 Kd Kd = = 7 ± 1 µM 7000.0 [] unit_conversion 5.154901959985743 success True direct_binding Fluorescence titration of FAD binding to MnmG with MnmE in the GppNHp-bound state. 8 Table 1 reports MnmG + MnmE-GppNHp FAD-binding affinity K_D = 7 ± 1 µM; the text states this condition corresponds to the α2β2 and α4β2 structures. auto_single_measurement only accepted activity measurement [1] 1 structures\9HIQ\9HIQ_metadata.json point structures/9HIQ/9hiq_protein.pdb structures/9HIQ/9hiq_pocket.pdb structures/9HIQ/9hiq_ligand.sdf structures/9HIQ/9hiq_ligand.pdb structures/9HIQ/9hiq_ligand.cif structures/9HIQ/9hiq_complex.pdb structures/9HIQ/9hiq_complex.cif 9HJG classic human CD73 (ecto-5'-nucleotidase) Homo sapiens (human) construct 8.01S Na compound 26 (N6-disubstituted acyclic ADP analog) "[""A1IVH""]" 1 Ki Ki = = 8.51 ± 0.50 μM 8510.0 [] unit_conversion 5.070070439915412 success True biochemical_inhibition Radioassay using recombinantly expressed soluble human CD73. 6 Table 2 reports compound 26: human CD73 Ki 8.51 ± 0.50 μM; the table footnote specifies a radioassay with recombinantly expressed soluble human CD73. auto_single_measurement only accepted activity measurement [1] 1 structures\9HJG\9HJG_metadata.json point structures/9HJG/9hjg_protein.pdb structures/9HJG/9hjg_pocket.pdb structures/9HJG/9hjg_ligand.sdf structures/9HJG/9hjg_ligand.pdb structures/9HJG/9hjg_ligand.cif structures/9HJG/9hjg_complex.pdb structures/9HJG/9hjg_complex.cif 9HM9 extended F-actin (alpha-actin) rabbit F-actin filaments bound to optimized F-tractin peptide Delta16 N-terminal residues; C33A; A35S; V36A; deletion of five C-terminal alanines and one glycine F-tractin_opt "[""CHAIN:F""]" 1 Kd Kd = = 8.5 ± 1.2 µM 8500.0 [] unit_conversion 5.070581074285707 success True direct_binding High-speed cosedimentation assay of F-actin with F-tractin_opt–mCherry; binding quantified by densitometry versus actin concentration. 4 Figure 2G reports “F-tractinopt, Kd = 8.5 ± 1.2 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9HM9\9HM9_metadata.json point structures/9HM9/9hm9_protein.pdb structures/9HM9/9hm9_pocket.pdb structures/9HM9/9hm9_ligand.pdb structures/9HM9/9hm9_ligand.cif structures/9HM9/9hm9_complex.pdb structures/9HM9/9hm9_complex.cif 9HNF classic BKACE15 beta-keto acid cleavage enzyme Paracoccus denitrificans Na Na acetoacetate "[""AAE""]" 1 IC50 IC50 = = 1.45 ± 0.16 mM 1450000.0 [] unit_conversion 2.8386319977650247 success True biochemical_inhibition Product inhibition of BKACE15 by acetoacetate; activity measured with 5 mM malonate semialdehyde and 1 mM acetyl-CoA while varying acetoacetate. 4 “We noted that the IC50 for acetoacetate was in the same range as the Km value for MSA” and “1.45 ± 0.16 mM (Fig. 2D, Supplementary Fig. 13).” Figure 2 identifies BKACE15 and its acetoacetate inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9HNF\9HNF_metadata.json point structures/9HNF/9hnf_protein.pdb structures/9HNF/9hnf_pocket.pdb structures/9HNF/9hnf_ligand.sdf structures/9HNF/9hnf_ligand.pdb structures/9HNF/9hnf_ligand.cif structures/9HNF/9hnf_complex.pdb structures/9HNF/9hnf_complex.cif 9HPH classic CK2alpha human Recombinant human CK2alpha with a C-terminal His6 tag removed by TEV protease Na KDX1381 "[""A1IWI""]" 2 Kd Kd = = 0.054 µM 54.0 [] unit_conversion 7.267606240177031 success True direct_binding KINOMEscan competitive binding assay; Table 2 SAR value for compound 19, subsequently renamed KDX1381. 4 Table 2 lists compound 19 with CK2α K_D 0.054 µM; the text identifies compound 19 as KDX1381. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [2, 4] 4 structures\9HPH\9HPH_metadata.json point structures/9HPH/9hph_protein.pdb structures/9HPH/9hph_pocket.pdb structures/9HPH/9hph_ligand.sdf structures/9HPH/9hph_ligand.pdb structures/9HPH/9hph_ligand.cif structures/9HPH/9hph_complex.pdb structures/9HPH/9hph_complex.cif 9HPQ extended human type I collagen prolyl 4-hydroxylase human PSB-I Ser143-Glu238 construct Na Pro-Pro-Gly-Pro-Arg-Gly-Pro-Pro-Gly (PPG-PRG-PPG) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G""]" 1 Kd Kd = = 37.0 ± 1.6 µM 37000.0 [] unit_conversion 4.431798275933005 success True direct_binding ITC measurement of PSB-I Ser143-Glu238 construct at 25°C. 8 Table 2 reports K_D = 37.0 ± 1.6 µM for PPG-PRG-PPG with the PSB-I^143–238 construct; Table 1 maps the corresponding PPG-PRG-PPG structure to PDB 9HPQ. auto_single_measurement only accepted activity measurement [1] 1 structures\9HPQ\9HPQ_metadata.json point structures/9HPQ/9hpq_protein.pdb structures/9HPQ/9hpq_pocket.pdb structures/9HPQ/9hpq_ligand.pdb structures/9HPQ/9hpq_ligand.cif structures/9HPQ/9hpq_complex.pdb structures/9HPQ/9hpq_complex.cif 9HRE extended human type I collagen prolyl 4-hydroxylase human PSB-I Ser143-Glu238 construct Na Pro-Hyp-Gly-Pro-Ala-Gly-Pro-Hyp-Gly (POG-PAG-POG) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G""]" 1 Kd Kd = = 79.6 ± 9.6 µM 79600.0 [] unit_conversion 4.099086932262331 success True direct_binding ITC measurement of PSB-I Ser143-Glu238 construct at 25°C. 8 Table 2 reports K_D = 79.6 ± 9.6 µM for POG-PAG-POG with the PSB-I^143–238 construct; Table 1 maps the corresponding POG-PAG-POG structure to PDB 9HRE. auto_single_measurement only accepted activity measurement [1] 1 structures\9HRE\9HRE_metadata.json point structures/9HRE/9hre_protein.pdb structures/9HRE/9hre_pocket.pdb structures/9HRE/9hre_ligand.pdb structures/9HRE/9hre_ligand.cif structures/9HRE/9hre_complex.pdb structures/9HRE/9hre_complex.cif 9HT0 classic BRD4 (BD1) Homo sapiens Residues 44-168 of BRD4 (BD1), with a 6xHis tag and TEV protease cleavage site Na Compound 50 "[""A1IXD""]" 1 IC50 IC50 = = 1129 nM 1129.0 [] unit_conversion 5.947306058075032 success True biochemical_inhibition Competitive HTRF TR-FRET assay measuring disruption of BRD4 (BD1) interaction with an acetylated histone peptide. 5 Compound 50 is reported as a weak binder with IC50 = 1129 nM derived from drug 1 (ABBV-075). auto_single_measurement only accepted activity measurement [1] 1 structures\9HT0\9HT0_metadata.json point structures/9HT0/9ht0_protein.pdb structures/9HT0/9ht0_pocket.pdb structures/9HT0/9ht0_ligand.sdf structures/9HT0/9ht0_ligand.pdb structures/9HT0/9ht0_ligand.cif structures/9HT0/9ht0_complex.pdb structures/9HT0/9ht0_complex.cif 9HT1 classic BRD4 (BD1) Homo sapiens Residues 44-168 of BRD4 (BD1), with a 6xHis tag and TEV protease cleavage site Na Compound 94 "[""A1IXE""]" 1 IC50 IC50 = = 27.9 nM 27.9 [] unit_conversion 7.554395796726403 success True biochemical_inhibition Competitive HTRF TR-FRET assay measuring disruption of BRD4 (BD1) interaction with an acetylated histone peptide. 5 Compound 94 is reported to have IC50 = 27.9 nM; the corresponding IC50 values were obtained by TR-FRET. auto_single_measurement only accepted activity measurement [1] 1 structures\9HT1\9HT1_metadata.json point structures/9HT1/9ht1_protein.pdb structures/9HT1/9ht1_pocket.pdb structures/9HT1/9ht1_ligand.sdf structures/9HT1/9ht1_ligand.pdb structures/9HT1/9ht1_ligand.cif structures/9HT1/9ht1_complex.pdb structures/9HT1/9ht1_complex.cif 9HT2 classic BRD4 (BD1) Homo sapiens Residues 44-168 of BRD4 (BD1), with a 6xHis tag and TEV protease cleavage site Na Compound 92 "[""A1IXF""]" 1 IC50 IC50 = = 621.8 nM 621.8 [] unit_conversion 6.206349282292827 success True biochemical_inhibition Competitive HTRF TR-FRET assay measuring disruption of BRD4 (BD1) interaction with an acetylated histone peptide. 5 X-ray diffraction analysis revealed that compound 92 (IC50 = 621.8 nM) bound with the expected binding mode; the corresponding IC50 values were obtained by TR-FRET. auto_single_measurement only accepted activity measurement [1] 1 structures\9HT2\9HT2_metadata.json point structures/9HT2/9ht2_protein.pdb structures/9HT2/9ht2_pocket.pdb structures/9HT2/9ht2_ligand.sdf structures/9HT2/9ht2_ligand.pdb structures/9HT2/9ht2_ligand.cif structures/9HT2/9ht2_complex.pdb structures/9HT2/9ht2_complex.cif 9HT3 classic PA0884 substrate-binding protein (SBP) component of a TRAP transporter Pseudomonas aeruginosa PAO1 Recombinant PA0884 SBP domain Na itaconate "[""ITN""]" 1 Kd Kd = = 179.6 ± 17.1 μM 179600.0 [] unit_conversion 3.7456936676687143 success True direct_binding Intrinsic tryptophan fluorescence ligand titration of PA0884; hyperbolic fit of binding curve. 4 Figure 3A reports PA0884 + itaconate, K_D = 179.6 μM ± 17.1 μM. The text identifies the itaconate complex as PDB 9HT3. auto_single_measurement only accepted activity measurement [1] 1 structures\9HT3\9HT3_metadata.json point structures/9HT3/9ht3_protein.pdb structures/9HT3/9ht3_pocket.pdb structures/9HT3/9ht3_ligand.sdf structures/9HT3/9ht3_ligand.pdb structures/9HT3/9ht3_ligand.cif structures/9HT3/9ht3_complex.pdb structures/9HT3/9ht3_complex.cif 9HT4 classic PA0884 substrate-binding protein (SBP) component of a TRAP transporter Pseudomonas aeruginosa PAO1 Recombinant PA0884 SBP domain Na succinate "[""SIN""]" 1 Kd Kd = = 32.6 ± 1.5 μM 32600.0 [] unit_conversion 4.486782399932061 success True direct_binding Intrinsic tryptophan fluorescence ligand titration of PA0884; hyperbolic fit of binding curve. 4 Figure 3B reports PA0884 + succinate, K_D = 32.6 μM ± 1.5 μM. The text identifies the succinate complex as PDB 9HT4. auto_single_measurement only accepted activity measurement [1] 1 structures\9HT4\9HT4_metadata.json point structures/9HT4/9ht4_protein.pdb structures/9HT4/9ht4_pocket.pdb structures/9HT4/9ht4_ligand.sdf structures/9HT4/9ht4_ligand.pdb structures/9HT4/9ht4_ligand.cif structures/9HT4/9ht4_complex.pdb structures/9HT4/9ht4_complex.cif 9HT8 extended human type I collagen prolyl 4-hydroxylase human PSB-I Ser143-Glu238 construct Na Pro-Pro-Gly-Pro-Ala-Gly-Pro-Pro-Gly (PPG-PAG-PPG) "[""CHAIN:E"", ""CHAIN:F""]" 1 Kd Kd = = 91.3 ± 3.8 µM 91300.0 [] unit_conversion 4.039529222465701 success True direct_binding ITC measurement of PSB-I Ser143-Glu238 construct at 25°C. 8 Table 2 reports K_D = 91.3 ± 3.8 µM for PPG-PAG-PPG with the PSB-I^143–238 construct; Table 1 maps the corresponding PPG-PAG-PPG structure to PDB 9HT8. auto_single_measurement only accepted activity measurement [1] 1 structures\9HT8\9HT8_metadata.json point structures/9HT8/9ht8_protein.pdb structures/9HT8/9ht8_pocket.pdb structures/9HT8/9ht8_ligand.pdb structures/9HT8/9ht8_ligand.cif structures/9HT8/9ht8_complex.pdb structures/9HT8/9ht8_complex.cif 9HT9 classic TMA Lyase (CutC) Na Na Na compound 1 "[""A1IXC""]" 1 Kd Kd = = 0.013 ± 0.002 μM 13.0 [] unit_conversion 7.886056647693163 success True direct_binding ITC binding affinity; Table 1. 3 Table 1 reports compound 1 ITC Kd = 0.013 ± 0.002 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9HT9\9HT9_metadata.json point structures/9HT9/9ht9_protein.pdb structures/9HT9/9ht9_pocket.pdb structures/9HT9/9ht9_ligand.sdf structures/9HT9/9ht9_ligand.pdb structures/9HT9/9ht9_ligand.cif structures/9HT9/9ht9_complex.pdb structures/9HT9/9ht9_complex.cif 9HTD extended human type II collagen prolyl 4-hydroxylase human PSB-II Met142-Glu236 construct Na Pro-Hyp-Gly-Pro-Ala-Gly-Pro-Hyp-Gly (POG-PAG-POG) "[""CHAIN:C""]" 1 Kd Kd = = 26.2 ± 1.9 µM 26200.0 [] unit_conversion 4.581698708680254 success True direct_binding ITC measurement of PSB-II Met142-Glu236 construct at 25°C. 8 Table 2 reports K_D = 26.2 ± 1.9 µM for POG-PAG-POG with the PSB-II construct; Table 1 maps the corresponding PSB-II POG-PAG-POG structure to PDB 9HTD. auto_single_measurement only accepted activity measurement [1] 1 structures\9HTD\9HTD_metadata.json point structures/9HTD/9htd_protein.pdb structures/9HTD/9htd_pocket.pdb structures/9HTD/9htd_ligand.pdb structures/9HTD/9htd_ligand.cif structures/9HTD/9htd_complex.pdb structures/9HTD/9htd_complex.cif 9HTR classic Cyclophilin D (CypD) Na Na Na compound 18d "[""A1IU3""]" 2 Kd Kd = = 80 ± 40 nM 80.0 [] unit_conversion 7.096910013008056 success True direct_binding Isothermal titration calorimetry (ITC). 4 Table 1 reports compound 18d: Kd = 80 ± 40 nM; the table footnote states Kd was measured by ITC. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9HTR\9HTR_metadata.json point structures/9HTR/9htr_protein.pdb structures/9HTR/9htr_pocket.pdb structures/9HTR/9htr_ligand.sdf structures/9HTR/9htr_ligand.pdb structures/9HTR/9htr_ligand.cif structures/9HTR/9htr_complex.pdb structures/9HTR/9htr_complex.cif 9HUK classic human GSK3b human full-length GSK-3beta Na ARN24161 (compound 1) "[""A1IXL""]" 1 IC50 IC50 = = 561.0 ± 40.5 nM 561.0 [] unit_conversion 6.251037138743838 success True biochemical_inhibition TR-FRET enzymatic inhibition assay using human recombinant GSK-3β; mean of three determinations. 7 Table 1 reports GSK-3β IC50 = 561.0 ± 40.5 nM for compound 1 (ARN24161). auto_single_measurement only accepted activity measurement [1] 1 structures\9HUK\9HUK_metadata.json point structures/9HUK/9huk_protein.pdb structures/9HUK/9huk_pocket.pdb structures/9HUK/9huk_ligand.sdf structures/9HUK/9huk_ligand.pdb structures/9HUK/9huk_ligand.cif structures/9HUK/9huk_complex.pdb structures/9HUK/9huk_complex.cif 9HUL classic human GSK3b human full-length GSK-3beta Na ARN25423 (compound 11) "[""A1IXM""]" 1 IC50 IC50 = = 123.0 ± 9.9 nM 123.0 [] unit_conversion 6.910094888560602 success True biochemical_inhibition TR-FRET enzymatic inhibition assay using human recombinant GSK-3β; mean of three determinations. 8 Table 2 reports GSK-3β IC50 = 123.0 ± 9.9 nM for compound 11; the paper maps PDB 9HUL to compound 11. auto_single_measurement only accepted activity measurement [1] 1 structures\9HUL\9HUL_metadata.json point structures/9HUL/9hul_protein.pdb structures/9HUL/9hul_pocket.pdb structures/9HUL/9hul_ligand.sdf structures/9HUL/9hul_ligand.pdb structures/9HUL/9hul_ligand.cif structures/9HUL/9hul_complex.pdb structures/9HUL/9hul_complex.cif 9HV3 classic human GSK3b human full-length GSK-3beta Na ARN25657 (compound 16) "[""A1IXN""]" 1 IC50 IC50 = = 19.3 ± 2.7 nM 19.3 [] unit_conversion 7.714442690992226 success True biochemical_inhibition TR-FRET enzymatic inhibition assay using human recombinant GSK-3β; mean of three determinations. 8 Table 2 reports GSK-3β IC50 = 19.3 ± 2.7 nM for compound 16 (ARN25657); the paper maps PDB 9HV3 to compound 16. auto_single_measurement only accepted activity measurement [1] 1 structures\9HV3\9HV3_metadata.json point structures/9HV3/9hv3_protein.pdb structures/9HV3/9hv3_pocket.pdb structures/9HV3/9hv3_ligand.sdf structures/9HV3/9hv3_ligand.pdb structures/9HV3/9hv3_ligand.cif structures/9HV3/9hv3_complex.pdb structures/9HV3/9hv3_complex.cif 9HVX classic Toxoplasma gondii GSK3b Toxoplasma gondii Na Na LY2090314 "[""A1IYF""]" 1 Kd Kd = = 33.65 ± 2.69 nM 33.65 [] unit_conversion 7.473014931440004 success True direct_binding Microscale thermophoresis using recombinant wild-type TgGSK3. 10 Figure 4d reports K_D ± SD of 33.65 ± 2.69 nM for WT TgGSK3 with LY2090314. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9HVX\9HVX_metadata.json point structures/9HVX/9hvx_protein.pdb structures/9HVX/9hvx_pocket.pdb structures/9HVX/9hvx_ligand.sdf structures/9HVX/9hvx_ligand.pdb structures/9HVX/9hvx_ligand.cif structures/9HVX/9hvx_complex.pdb structures/9HVX/9hvx_complex.cif 9HWT classic Keap1 Kelch domain Na Na Na compound 24 (internal alias UCAB#985; PDB component A1IX4) "[""A1IX4""]" 1 Ki Ki = = 10 nM 10.0 [] unit_conversion 8.0 success True biochemical_inhibition Keap1-Nrf2 fluorescence-polarization competition assay. 5 The optimization series reports compound 24 Ki 10 nM and maps it to PDB 9HWT. auto_single_measurement only accepted activity measurement [1] 1 structures\9HWT\9HWT_metadata.json point structures/9HWT/9hwt_protein.pdb structures/9HWT/9hwt_pocket.pdb structures/9HWT/9hwt_ligand.sdf structures/9HWT/9hwt_ligand.pdb structures/9HWT/9hwt_ligand.cif structures/9HWT/9hwt_complex.pdb structures/9HWT/9hwt_complex.cif 9HXV classic TET2 Na catalytic domain (CD) Na IOX1 "[""8XQ""]" 1 IC50 IC50 = = 2.45 ± 1.2 μM 2450.0 [] unit_conversion 5.610833915635467 success True biochemical_inhibition In vitro MALDI-MS TET2 activity assay; Figure 3 reports IOX1 inhibition. 5 Figure 3 explicitly prints “IOX1 IC50: 2.45 ± 1.2 μM”; the text states that IOX1 inhibited the representative TET family member TET2 in the MALDI-MS assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9HXV\9HXV_metadata.json point structures/9HXV/9hxv_protein.pdb structures/9HXV/9hxv_pocket.pdb structures/9HXV/9hxv_ligand.sdf structures/9HXV/9hxv_ligand.pdb structures/9HXV/9hxv_ligand.cif structures/9HXV/9hxv_complex.pdb structures/9HXV/9hxv_complex.cif 9HY4 extended CSM8 H-2Db Mus musculus (mouse) Miniaturized CSM8 H-2Db construct with the alpha3 domain and beta2m replaced by the CSM8 stabilizing domain; linked by a poly-GGS linker Na gp33 peptide "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 14.1 ± 0.8 µM 14100.0 [] unit_conversion 4.85078088734462 success True direct_binding SPR equilibrium binding of CSM8 H-2Db/peptide complexes. 4 Table 1 reports a CSM8 H-2Db affinity for gp33 of 14.1 ± 0.8 µM; its footnote defines these as fitted equilibrium-binding SPR K_D values. auto_single_measurement only accepted activity measurement [1] 1 structures\9HY4\9HY4_metadata.json point structures/9HY4/9hy4_protein.pdb structures/9HY4/9hy4_pocket.pdb structures/9HY4/9hy4_ligand.pdb structures/9HY4/9hy4_ligand.cif structures/9HY4/9hy4_complex.pdb structures/9HY4/9hy4_complex.cif 9I03 classic recombinant human butyrylcholinesterase human Na Na (R)-N-((1-benzylpyrrolidin-3-yl)methyl)-N-methylnaphthalene-2-sulfonamide; compound (R)-(-)-3 "[""A1IYQ""]" 2 Ki Ki = = 6.6 nM 6.6 [] unit_conversion 8.18045606445813 success True biochemical_inhibition Characteristic kinetic parameters determined with purified hBChE in the presence of 50 μM butyrylthiocholine; Ki for binding to free hBChE. 9 Table 4 reports Ki = 6.6 nM for (R)-(-)-3 binding to free hBChE. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9I03\9I03_metadata.json point structures/9I03/9i03_protein.pdb structures/9I03/9i03_pocket.pdb structures/9I03/9i03_ligand.sdf structures/9I03/9i03_ligand.pdb structures/9I03/9i03_ligand.cif structures/9I03/9i03_complex.pdb structures/9I03/9i03_complex.cif 9I0U classic PD-L1 human Na Na Evixapodlin "[""A1IZJ""]" 1 IC50 IC50 = = 1.74 ± 0.15 nM 1.74 [] unit_conversion 8.7594507517174 success True biochemical_inhibition Homogeneous time-resolved fluorescence (HTRF) assay measuring disruption of the human PD-1/PD-L1 complex. 2 Table 1 reports Evixapodlin IC50 (HTRF) of 1.74 ± 0.15 nM; the text states the compounds were tested for potency disrupting the human PD-1/PD-L1 complex using HTRF. auto_single_measurement only accepted activity measurement [1] 1 structures\9I0U\9I0U_metadata.json point structures/9I0U/9i0u_protein.pdb structures/9I0U/9i0u_pocket.pdb structures/9I0U/9i0u_ligand.sdf structures/9I0U/9i0u_ligand.pdb structures/9I0U/9i0u_ligand.cif structures/9I0U/9i0u_complex.pdb structures/9I0U/9i0u_complex.cif 9I0W classic PD-L1 human Na Na INCB086550 "[""A1IZP""]" 1 IC50 IC50 = = 2.59 ± 0.09 nM 2.59 [] unit_conversion 8.586700235918748 success True biochemical_inhibition Homogeneous time-resolved fluorescence (HTRF) assay measuring disruption of the human PD-1/PD-L1 complex. 2 Table 1 reports INCB086550 IC50 (HTRF) of 2.59 ± 0.09 nM; the text states the compounds were tested for potency disrupting the human PD-1/PD-L1 complex using HTRF. auto_single_measurement only accepted activity measurement [1] 1 structures\9I0W\9I0W_metadata.json point structures/9I0W/9i0w_protein.pdb structures/9I0W/9i0w_pocket.pdb structures/9I0W/9i0w_ligand.sdf structures/9I0W/9i0w_ligand.pdb structures/9I0W/9i0w_ligand.cif structures/9I0W/9i0w_complex.pdb structures/9I0W/9i0w_complex.cif 9I1M classic AauA Na Na Na D-ribulose "[""A1IZL""]" 1 Kd Kd = = 1.98 ± 0.3 μM 1980.0 [] unit_conversion 5.703334809738469 success True direct_binding Isothermal titration calorimetry of purified recombinant AauA with D-ribulose. 3 ITC showed D-ribulose binding to AauA with Kd = 1.98 ± 0.3 μM; Fig. 2c. auto_single_measurement only accepted activity measurement [1] 1 structures\9I1M\9I1M_metadata.json point structures/9I1M/9i1m_protein.pdb structures/9I1M/9i1m_pocket.pdb structures/9I1M/9i1m_ligand.sdf structures/9I1M/9i1m_ligand.pdb structures/9I1M/9i1m_ligand.cif structures/9I1M/9i1m_complex.pdb structures/9I1M/9i1m_complex.cif 9I20 classic SLC35B1 human Full-length SLC35B1 residues 1-322 with a C-terminal TEV-GFP-His8 tag wild-type ADP "[""ADP""]" 1 IC50 IC50 = = 1.6 ± 0.3 μM 1600.0 [] unit_conversion 5.795880017344075 success True biochemical_inhibition Cold ADP competition of [3H]ADP uptake by wild-type SLC35B1 proteoliposomes preloaded with nucleotide. 15 Extended Data Fig. 1f reports “ADP IC50 = 1.6 ± 0.3 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9I20\9I20_metadata.json point structures/9I20/9i20_protein.pdb structures/9I20/9i20_pocket.pdb structures/9I20/9i20_ligand.sdf structures/9I20/9i20_ligand.pdb structures/9I20/9i20_ligand.cif structures/9I20/9i20_complex.pdb structures/9I20/9i20_complex.cif 9I2U classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type ibuprofenoyl-CoA (compound 1) "[""SFC""]" 2 Ki Ki = = 3.04 ± 0.34 µM 3040.0 [] unit_conversion 5.517126416391246 success True biochemical_inhibition Competitive inhibition kinetic assay; mean ± SEM, n = 3. 10 The text states that competitive inhibition gave a Ki value of 3.04 ± 0.34 µM (mean ± SEM, n = 3). auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9I2U\9I2U_metadata.json point structures/9I2U/9i2u_protein.pdb structures/9I2U/9i2u_pocket.pdb structures/9I2U/9i2u_ligand.sdf structures/9I2U/9i2u_ligand.pdb structures/9I2U/9i2u_ligand.cif structures/9I2U/9i2u_complex.pdb structures/9I2U/9i2u_complex.cif 9I2V classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type fenoprofenoyl-CoA (compound 2) "[""A1IY9""]" 1 pIC50 IC50 = = 5.43 ± 0.07 unitless 3715.3522909717276 [] p_metric_transform 5.43 success True biochemical_inhibition Colorimetric MCR inhibition assay; mean ± SEM, n = 3. 2 Figure 1 prints “±-Fenoprofenoyl-CoA 2, pIC50 = 5.43 ± 0.07.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I2V\9I2V_metadata.json point structures/9I2V/9i2v_protein.pdb structures/9I2V/9i2v_pocket.pdb structures/9I2V/9i2v_ligand.sdf structures/9I2V/9i2v_ligand.pdb structures/9I2V/9i2v_ligand.cif structures/9I2V/9i2v_complex.pdb structures/9I2V/9i2v_complex.cif 9I2W classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type flurbiprofenoyl-CoA (compound 4) "[""A1IZA""]" 1 pIC50 IC50 = = 5.34 ± 0.07 unitless 4570.881896148751 [] p_metric_transform 5.34 success True biochemical_inhibition Colorimetric MCR inhibition assay; mean ± SEM, n = 3. 2 Figure 1 prints “±-Flurbiprofenoyl-CoA 4, pIC50 = 5.34 ± 0.07.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I2W\9I2W_metadata.json point structures/9I2W/9i2w_protein.pdb structures/9I2W/9i2w_pocket.pdb structures/9I2W/9i2w_ligand.sdf structures/9I2W/9i2w_ligand.pdb structures/9I2W/9i2w_ligand.cif structures/9I2W/9i2w_complex.pdb structures/9I2W/9i2w_complex.cif 9I2X classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type S-naproxenoyl-CoA (compound 5) "[""A1I1O""]" 1 pIC50 IC50 = = 5.38 ± 0.03 unitless 4168.693834703355 [] p_metric_transform 5.38 success True biochemical_inhibition Colorimetric MCR inhibition assay; mean ± SEM, n = 3. 2 Figure 1 prints “S-Naproxenoyl-CoA 5, pIC50 = 5.38 ± 0.03.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I2X\9I2X_metadata.json point structures/9I2X/9i2x_protein.pdb structures/9I2X/9i2x_pocket.pdb structures/9I2X/9i2x_ligand.sdf structures/9I2X/9i2x_ligand.pdb structures/9I2X/9i2x_ligand.cif structures/9I2X/9i2x_complex.pdb structures/9I2X/9i2x_complex.cif 9I2Z classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type S-2-methyldecanoyl-CoA (compound 6) "[""A1IZB""]" 1 pIC50 IC50 = = 4.84 ± 0.05 unitless 14454.39770745928 [] p_metric_transform 4.84 success True biochemical_inhibition Colorimetric MCR inhibition assay; mean ± SEM, n = 3. 2 Figure 1 prints “S-2-Methyldecanoyl-CoA 6, pIC50 = 4.84 ± 0.05.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I2Z\9I2Z_metadata.json point structures/9I2Z/9i2z_protein.pdb structures/9I2Z/9i2z_pocket.pdb structures/9I2Z/9i2z_ligand.sdf structures/9I2Z/9i2z_ligand.pdb structures/9I2Z/9i2z_ligand.cif structures/9I2Z/9i2z_complex.pdb structures/9I2Z/9i2z_complex.cif 9I30 classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type S-ketoprofenoyl-CoA (compound 3) "[""A1IZD""]" 1 pIC50 IC50 = = 5.11 ± 0.005 unitless 7762.471166286911 [] p_metric_transform 5.11 success True biochemical_inhibition Colorimetric MCR inhibition assay; mean ± SEM, n = 3. 2 Figure 1 prints “S-Ketoprofenoyl-CoA 3, pIC50 = 5.11 ± 0.005.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I30\9I30_metadata.json point structures/9I30/9i30_protein.pdb structures/9I30/9i30_pocket.pdb structures/9I30/9i30_ligand.sdf structures/9I30/9i30_ligand.pdb structures/9I30/9i30_ligand.cif structures/9I30/9i30_complex.pdb structures/9I30/9i30_complex.cif 9I31 classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type acetyl-CoA (compound 11) "[""ACO""]" 1 pIC50 IC50 ~ ~ 3.4 unitless 398107.1705534969 [] p_metric_transform 3.4000000000000004 success True biochemical_inhibition Colorimetric MCR inhibition assay. 2 Figure 1 prints “Acetyl-CoA 11, pIC50 ≈ 3.4.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I31\9I31_metadata.json point structures/9I31/9i31_protein.pdb structures/9I31/9i31_pocket.pdb structures/9I31/9i31_ligand.sdf structures/9I31/9i31_ligand.pdb structures/9I31/9i31_ligand.cif structures/9I31/9i31_complex.pdb structures/9I31/9i31_complex.cif 9I32 classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type isobutanoyl-CoA (compound 12) "[""CO6""]" 1 pIC50 IC50 ~ ~ 3.4 unitless 398107.1705534969 [] p_metric_transform 3.4000000000000004 success True biochemical_inhibition Colorimetric MCR inhibition assay. 2 Figure 1 prints “Isobutanoyl-CoA 12, pIC50 ≈ 3.4.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I32\9I32_metadata.json point structures/9I32/9i32_protein.pdb structures/9I32/9i32_pocket.pdb structures/9I32/9i32_ligand.sdf structures/9I32/9i32_ligand.pdb structures/9I32/9i32_ligand.cif structures/9I32/9i32_complex.pdb structures/9I32/9i32_complex.cif 9I33 classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type butanoyl-CoA (compound 10) "[""BCO""]" 1 pIC50 IC50 ~ ~ 4.4 unitless 39810.71705534969 [] p_metric_transform 4.4 success True biochemical_inhibition Colorimetric MCR inhibition assay. 2 Figure 1 prints “n-Butanoyl-CoA 10, pIC50 ≈ 4.4.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I33\9I33_metadata.json point structures/9I33/9i33_protein.pdb structures/9I33/9i33_pocket.pdb structures/9I33/9i33_ligand.sdf structures/9I33/9i33_ligand.pdb structures/9I33/9i33_ligand.cif structures/9I33/9i33_complex.pdb structures/9I33/9i33_complex.cif 9I34 classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type hexanoyl-CoA (compound 9) "[""HXC""]" 1 pIC50 IC50 ~ ~ 4.1 unitless 79432.82347242821 [] p_metric_transform 4.1 success True biochemical_inhibition Colorimetric MCR inhibition assay. 2 Figure 1 prints “Hexanoyl-CoA 9, pIC50 ≈ 4.1.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I34\9I34_metadata.json point structures/9I34/9i34_protein.pdb structures/9I34/9i34_pocket.pdb structures/9I34/9i34_ligand.sdf structures/9I34/9i34_ligand.pdb structures/9I34/9i34_ligand.cif structures/9I34/9i34_complex.pdb structures/9I34/9i34_complex.cif 9I35 classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type octanoyl-CoA (compound 8) "[""CO8""]" 1 pIC50 IC50 ~ ~ 4.0 unitless 100000.0 [] p_metric_transform 4.0 success True biochemical_inhibition Colorimetric MCR inhibition assay. 2 Figure 1 prints “Octanoyl-CoA 8, pIC50 ≈ 4.0.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I35\9I35_metadata.json point structures/9I35/9i35_protein.pdb structures/9I35/9i35_pocket.pdb structures/9I35/9i35_ligand.sdf structures/9I35/9i35_ligand.pdb structures/9I35/9i35_ligand.cif structures/9I35/9i35_complex.pdb structures/9I35/9i35_complex.cif 9I36 classic Alpha-Methylacyl-CoA racemase (MCR) Mycobacterium tuberculosis Na wild-type decanoyl-CoA (compound 7) "[""MFK""]" 1 pIC50 IC50 ~ ~ 4.5 unitless 31622.776601683792 [] p_metric_transform 4.5 success True biochemical_inhibition Colorimetric MCR inhibition assay. 2 Figure 1 prints “Decanoyl-CoA 7, pIC50 ≈ 4.5.” auto_single_measurement only accepted activity measurement [1] 1 structures\9I36\9I36_metadata.json point structures/9I36/9i36_protein.pdb structures/9I36/9i36_pocket.pdb structures/9I36/9i36_ligand.sdf structures/9I36/9i36_ligand.pdb structures/9I36/9i36_ligand.cif structures/9I36/9i36_complex.pdb structures/9I36/9i36_complex.cif 9I3Q classic DNPH1 Na Na Na compound 2 "[""A1IZR""]" 2 Kd Kd = = 7.5 µM 7500.0 [] unit_conversion 5.1249387366083 success True direct_binding Surface plasmon resonance (SPR) binding assay. 2 The text states that compound 2 bound DNPH1 by SPR with a binding constant Kd of 7.5 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 3 structures\9I3Q\9I3Q_metadata.json point structures/9I3Q/9i3q_protein.pdb structures/9I3Q/9i3q_pocket.pdb structures/9I3Q/9i3q_ligand.sdf structures/9I3Q/9i3q_ligand.pdb structures/9I3Q/9i3q_ligand.cif structures/9I3Q/9i3q_complex.pdb structures/9I3Q/9i3q_complex.cif 9I5O classic butyrylcholinesterase human C-terminus truncated form with lower N-glycosylation sites Na compound 95, 1-(cyclohexylmethyl)-5-(2,4-difluorobenzyl)-N-(2-(dimethylamino)ethyl)-1H-indazole-6-carboxamide "[""A1A2L""]" 1 IC50 IC50 = = 0.772 ± 0.057 μM 772.0 [] unit_conversion 6.1123826996642645 success True biochemical_inhibition Modified Ellman enzymatic inhibition assay using recombinant human hBChE. 5 Table 1 reports compound 95 hBChE IC50 = 0.772 ± 0.057 μM. Figure 5 and its caption assign compound 95 to hBChE PDB 9I5O; this resolves the accession-order transposition elsewhere in the paper. auto_single_measurement only accepted activity measurement [1] 1 structures\9I5O\9I5O_metadata.json point structures/9I5O/9i5o_protein.pdb structures/9I5O/9i5o_pocket.pdb structures/9I5O/9i5o_ligand.sdf structures/9I5O/9i5o_ligand.pdb structures/9I5O/9i5o_ligand.cif structures/9I5O/9i5o_complex.pdb structures/9I5O/9i5o_complex.cif 9I5Q classic butyrylcholinesterase human C-terminus truncated form with lower N-glycosylation sites Na compound 102, 2-(cyclohexylmethyl)-5-(2,4-difluorophenoxy)-N-(2-(3-(methoxymethyl)piperidin-1-yl)ethyl)-2H-indazole-6-carboxamide "[""A1IZ3""]" 1 IC50 IC50 = = 0.021 ± 0.002 μM 21.0 [] unit_conversion 7.6777807052660805 success True biochemical_inhibition Modified Ellman enzymatic inhibition assay using recombinant human hBChE. 5 Table 1 reports compound 102 hBChE IC50 = 0.021 ± 0.002 μM. The crystal-structure methods and accession listing identify compound 102 with hBChE as PDB 9I5Q. auto_single_measurement only accepted activity measurement [1] 1 structures\9I5Q\9I5Q_metadata.json point structures/9I5Q/9i5q_protein.pdb structures/9I5Q/9i5q_pocket.pdb structures/9I5Q/9i5q_ligand.sdf structures/9I5Q/9i5q_ligand.pdb structures/9I5Q/9i5q_ligand.cif structures/9I5Q/9i5q_complex.pdb structures/9I5Q/9i5q_complex.cif 9I68 extended human Cdc20 human Cdc20 WD40 domain, residues 161-477 Na D21 "[""CHAIN:B""]" 1 Kd Kd = = 0.52±0.01 µM 520.0 [] unit_conversion 6.2839966563652006 success True direct_binding Surface plasmon resonance; Table 2 reports triplicate measurements. 9 Table 2 lists D21 with K_D 0.52±0.01 µM for binding to Cdc20WD40 measured by surface plasmon resonance. auto_single_measurement only accepted activity measurement [1] 1 structures\9I68\9I68_metadata.json point structures/9I68/9i68_protein.pdb structures/9I68/9i68_pocket.pdb structures/9I68/9i68_ligand.pdb structures/9I68/9i68_ligand.cif structures/9I68/9i68_complex.pdb structures/9I68/9i68_complex.cif 9I69 extended human Cdc20 human Cdc20 WD40 domain, residues 161-477 Na D20 "[""CHAIN:B""]" 1 Kd Kd = = 0.90±0.01 µM 900.0 [] unit_conversion 6.045757490560675 success True direct_binding Surface plasmon resonance; Table 2 reports triplicate measurements. 9 Table 2 lists D20 with K_D 0.90±0.01 µM for binding to Cdc20WD40 measured by surface plasmon resonance. auto_single_measurement only accepted activity measurement [1] 1 structures\9I69\9I69_metadata.json point structures/9I69/9i69_protein.pdb structures/9I69/9i69_pocket.pdb structures/9I69/9i69_ligand.pdb structures/9I69/9i69_ligand.cif structures/9I69/9i69_complex.pdb structures/9I69/9i69_complex.cif 9I6A extended human Cdc20 human Cdc20 WD40 domain, residues 161-477 Na D7 "[""CHAIN:B""]" 1 Kd Kd = = 3.1±0.1 µM 3100.0 [] unit_conversion 5.508638306165727 success True direct_binding Surface plasmon resonance; Table 2 reports triplicate measurements. 9 Table 2 lists D7 with K_D 3.1±0.1 µM for binding to Cdc20WD40 measured by surface plasmon resonance. auto_single_measurement only accepted activity measurement [1] 1 structures\9I6A\9I6A_metadata.json point structures/9I6A/9i6a_protein.pdb structures/9I6A/9i6a_pocket.pdb structures/9I6A/9i6a_ligand.pdb structures/9I6A/9i6a_ligand.cif structures/9I6A/9i6a_complex.pdb structures/9I6A/9i6a_complex.cif 9I6C extended StmPr1 Stenotrophomonas maltophilia 36 kDa StmPr1 Na Leupeptin "[""CHAIN:B""]" 1 IC50 IC50 = = 130.3 µM 130300.00000000001 [] unit_conversion 3.8850555842874153 success True biochemical_inhibition StmPr1 36 kDa activity assay against Leupeptin. 5 “Leupeptin even shows a higher IC50 with 130,3 µM”. Figure 3 and Table 1 identify the StmPr1-Leupeptin complex as PDB 9I6C. auto_single_measurement only accepted activity measurement [1] 1 structures\9I6C\9I6C_metadata.json point structures/9I6C/9i6c_protein.pdb structures/9I6C/9i6c_pocket.pdb structures/9I6C/9i6c_ligand.pdb structures/9I6C/9i6c_ligand.cif structures/9I6C/9i6c_complex.pdb structures/9I6C/9i6c_complex.cif 9I76 classic Pseudomonas aeruginosa FabF Pseudomonas aeruginosa FabF C164A C164A 137; 4-(1H-pyrazole-3-carboxamido)butanoic acid "[""A1I0O""]" 1 Kd Kd = = 880 ± 50 µM 880000.0 [] unit_conversion 3.0555173278498318 success True direct_binding Bio-layer interferometry (BLI); Table 4 reports the KD as an average of two experiments for compound 137. 13 Table 4 lists compound 137 with KD 880 ± 50 µM and PDB ID 9I76; the table states values were determined using PaFabF C164A. auto_single_measurement only accepted activity measurement [1] 1 structures\9I76\9I76_metadata.json point structures/9I76/9i76_protein.pdb structures/9I76/9i76_pocket.pdb structures/9I76/9i76_ligand.sdf structures/9I76/9i76_ligand.pdb structures/9I76/9i76_ligand.cif structures/9I76/9i76_complex.pdb structures/9I76/9i76_complex.cif 9I7Z classic LecA Pseudomonas aeruginosa Na Na compound 33 "[""A1IZM""]" 2 Kd Kd = = 15.0 ± 2.1 µM 15000.0 [] unit_conversion 4.823908740944319 success True direct_binding Isothermal titration calorimetry of compound 33 binding to LecA. 7 Figure 5b tabulates KD = 15.0 ± 2.1 µM for compound 33; its caption identifies ITC titration data of catechols to LecA. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9I7Z\9I7Z_metadata.json point structures/9I7Z/9i7z_protein.pdb structures/9I7Z/9i7z_pocket.pdb structures/9I7Z/9i7z_ligand.sdf structures/9I7Z/9i7z_ligand.pdb structures/9I7Z/9i7z_ligand.cif structures/9I7Z/9i7z_complex.pdb structures/9I7Z/9i7z_complex.cif 9I80 classic LecA Pseudomonas aeruginosa Na Na compound 34 "[""A1I1G""]" 1 IC50 IC50 = = 63 ± 7 µM 63000.0 [] unit_conversion 4.200659450546418 success True biochemical_inhibition Competitive fluorescence-polarisation LecA inhibition assay. 7 Figure 5a lists compound 34 (meta) with IC50 = 63 ± 7 µM; the caption specifies a competitive binding assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9I80\9I80_metadata.json point structures/9I80/9i80_protein.pdb structures/9I80/9i80_pocket.pdb structures/9I80/9i80_ligand.sdf structures/9I80/9i80_ligand.pdb structures/9I80/9i80_ligand.cif structures/9I80/9i80_complex.pdb structures/9I80/9i80_complex.cif 9I81 classic SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) SARS-CoV-2 nsp12, nsp7, and two copies of nsp8 Na HeE1-2Tyr; HeE1-2Tyr; HeE1-2Tyr "[""6CJ""]" 1 IC50 IC50 = = 5.5 μM 5500.0 [] unit_conversion 5.259637310505756 success True biochemical_inhibition RNA elongation assay using coexpressed RdRp and a minimal RNA hairpin; inhibition of RNA extension after 5 min. 2 Quantitative analysis of three independent experiments fitting the dose-response curve resulted in an IC50 of 5.5 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9I81\9I81_metadata.json point structures/9I81/9i81_protein.pdb structures/9I81/9i81_pocket.pdb structures/9I81/9i81_ligand.sdf structures/9I81/9i81_ligand.pdb structures/9I81/9i81_ligand.cif structures/9I81/9i81_complex.pdb structures/9I81/9i81_complex.cif 9I9Q extended DNPH1 Na Na Na compound 2 "[""A1I1M""]" 1 IC50 IC50 = = 8.3 μM 8300.0 [] unit_conversion 5.080921907623926 success True direct_binding DNPH1 binding FRET assay; geometric means of at least three IC50 determinations per compound. 3 Table 1 lists compound 2 with DNPH1 binding IC50 = 8.3 μM; footnote identifies a DNPH1 binding (FRET) assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9I9Q\9I9Q_metadata.json point structures/9I9Q/9i9q_protein.pdb structures/9I9Q/9i9q_pocket.pdb structures/9I9Q/9i9q_ligand.pdb structures/9I9Q/9i9q_ligand.cif structures/9I9Q/9i9q_complex.pdb structures/9I9Q/9i9q_complex.cif 9IA6 extended DNPH1 Na Na Na compound 3 "[""A1I1U""]" 1 IC50 IC50 = = 0.54 μM 540.0 [] unit_conversion 6.267606240177031 success True direct_binding DNPH1 binding FRET assay; geometric means of at least three IC50 determinations per compound. 3 Table 1 lists compound 3 with DNPH1 binding IC50 = 0.54 μM; footnote identifies a DNPH1 binding (FRET) assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9IA6\9IA6_metadata.json point structures/9IA6/9ia6_protein.pdb structures/9IA6/9ia6_pocket.pdb structures/9IA6/9ia6_ligand.pdb structures/9IA6/9ia6_ligand.cif structures/9IA6/9ia6_complex.pdb structures/9IA6/9ia6_complex.cif 9IBY classic Zika virus NS2B-NS3 protease Zika virus (ZIKV) NS2B residues 45-96 linked via a flexible GGGGSGGG linker to NS3 residues 1-177; N-terminal hexahistidine tag with thrombin cleavage site Na IRBM-Z-2 (compound 2) "[""A1I16""]" 2 Kd Kd = = 21 ± 5 nM 21.0 [] unit_conversion 7.6777807052660805 success True direct_binding Biolayer interferometry (BLI), 1:1 fitting of IRBM-Z-2–ZIKV NS2B-NS3 interaction. 6 Fig. 3b reports BLI binding parameters for IRBM-Z-2 and ZIKV NS2B-NS3: KD (nM) = 21 ± 5. auto_metric_priority unique highest-priority metric family: Kd [2] 3 structures\9IBY\9IBY_metadata.json point structures/9IBY/9iby_protein.pdb structures/9IBY/9iby_pocket.pdb structures/9IBY/9iby_ligand.sdf structures/9IBY/9iby_ligand.pdb structures/9IBY/9iby_ligand.cif structures/9IBY/9iby_complex.pdb structures/9IBY/9iby_complex.cif 9IC2 extended AMPK-alpha2 kinase domain human AMPK-alpha2 kinase domain, residues 6-280 wild-type (WT) BAY-3827 "[""A1I1Y""]" 1 Kd Kd = = 1.23 µM 1230.0 [] unit_conversion 5.910094888560602 success True direct_binding Spectral shift binding assay of BAY-3827 with WT α2KD. 5 “BAY-3827 binds into the conserved ATP-binding pocket… binding with a dissociation constant (Kd) value of 1.23 µM as measured by a spectral shift binding assay.” auto_single_measurement only accepted activity measurement [1] 1 structures\9IC2\9IC2_metadata.json point structures/9IC2/9ic2_protein.pdb structures/9IC2/9ic2_pocket.pdb structures/9IC2/9ic2_ligand.pdb structures/9IC2/9ic2_ligand.cif structures/9IC2/9ic2_complex.pdb structures/9IC2/9ic2_complex.cif 9II5 classic human TRIM21 human TRIM21 PRYSPRY domain, residues 287-465 Na compound 1 "[""A1D9F""]" 1 Kd Kd = = 0.193 µM 193.0 [] unit_conversion 6.714442690992226 success True direct_binding Surface plasmon resonance (SPR) toward Strep II-tagged TRIM21 protein. 3 “Compound 1 was synthesized and validated with a dissociation constant (K_D) of 193 nM by SPR toward Strep II-tagged TRIM21 proteins (Figure 1b).” Table 1 prints TRIM21 K_D = 0.193 µM for compound 1. auto_single_measurement only accepted activity measurement [1] 1 structures\9II5\9II5_metadata.json point structures/9II5/9ii5_protein.pdb structures/9II5/9ii5_pocket.pdb structures/9II5/9ii5_ligand.sdf structures/9II5/9ii5_ligand.pdb structures/9II5/9ii5_ligand.cif structures/9II5/9ii5_complex.pdb structures/9II5/9ii5_complex.cif 9IIF classic factor inhibiting hypoxia-inducible factor-alpha (FIH) human Na Na Desidustat "[""A1L2L""]" 1 IC50 IC50 = = 21.7 ± 2.9 µM 21700.0 [] unit_conversion 4.663540266151471 success True biochemical_inhibition Inhibition of isolated recombinant human FIH; SPE-MS assay (Table 1). 6 Table 1 reports Desidustat FIH IC50 = 21.7 ± 2.9 µM; Figure 2a maps the FIH:Zn:Desidustat structure to PDB 9IIF. auto_single_measurement only accepted activity measurement [1] 1 structures\9IIF\9IIF_metadata.json point structures/9IIF/9iif_protein.pdb structures/9IIF/9iif_pocket.pdb structures/9IIF/9iif_ligand.sdf structures/9IIF/9iif_ligand.pdb structures/9IIF/9iif_ligand.cif structures/9IIF/9iif_complex.pdb structures/9IIF/9iif_complex.cif 9IM7 extended mouse Polo-like kinase 1 (PLK1) mouse Polo-box domain residues 367-603 with an N-terminal 6xHis tag and TEV protease cleavage site Na R12-4j compound (NC1) "[""CHAIN:B""]" 1 Kd Kd = = 6.06 µM 6060.0 [] unit_conversion 5.217527375833714 success True direct_binding Isothermal titration calorimetry of purified mouse PLK1 PBD with NC1; Figure 3b reports the fitted binding constant. 10 “Prior to PLK1 degradation by NC1, the binding affinity between NC1 and PLK1 PBD was investigated using ITC, revealing a Kd of 6.06 µM (Figure 3b).” auto_single_measurement only accepted activity measurement [1] 1 structures\9IM7\9IM7_metadata.json point structures/9IM7/9im7_protein.pdb structures/9IM7/9im7_pocket.pdb structures/9IM7/9im7_ligand.pdb structures/9IM7/9im7_ligand.cif structures/9IM7/9im7_complex.pdb structures/9IM7/9im7_complex.cif 9INU classic PD-L1 human PD-L1 protein fragment encompassing residues 18-134 with a C-terminal histidine tag Na P17 "[""A1D9R""]" 1 IC50 IC50 = = 0.1492 μM 149.2 [] unit_conversion 6.826231176863351 success True biochemical_inhibition TR-FRET inhibition assay of the PD-1/PD-L1 interaction. 5 Table 1 reports P17 PD-L1 activity of 0.1492 μM; footnote a states PD-1/PD-L1 interaction inhibition was evaluated using the TR-FRET assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9INU\9INU_metadata.json point structures/9INU/9inu_protein.pdb structures/9INU/9inu_pocket.pdb structures/9INU/9inu_ligand.sdf structures/9INU/9inu_ligand.pdb structures/9INU/9inu_ligand.cif structures/9INU/9inu_complex.pdb structures/9INU/9inu_complex.cif 9IPT classic AmvR Acinetobacter baumannii AmvR residues 4-192 Na spermidine (SPD) "[""SPD""]" 1 Kd Kd = = 0.73 µM 730.0 [] unit_conversion 6.136677139879544 success True direct_binding Isothermal titration calorimetry of spermidine with apo AmvR; Fig. 3A reports the equilibrium dissociation constant. 6 The text states that spermidine had the highest affinity for AmvR (0.73 µM), and Fig. 3A prints Kd 0.73 µM for spermidine. auto_single_measurement only accepted activity measurement [1] 1 structures\9IPT\9IPT_metadata.json point structures/9IPT/9ipt_protein.pdb structures/9IPT/9ipt_pocket.pdb structures/9IPT/9ipt_ligand.sdf structures/9IPT/9ipt_ligand.pdb structures/9IPT/9ipt_ligand.cif structures/9IPT/9ipt_complex.pdb structures/9IPT/9ipt_complex.cif 9IQQ classic PKM2 Na Na Na GSH (glutathione) "[""GSH""]" 1 Kd Kd = = 1.38 ± 0.20 µM 1380.0 [] unit_conversion 5.860120913598763 success True direct_binding Microscale thermophoresis (MST) using EGFP-tagged PKM2; n = 3. 3 Figure 1 caption: “MST assay conducted with EGFP-tagged PKM2 to measure the binding affinity (n = 3) ... The Kd for GSH was calculated using the ‘One site-specific binding’ model and recorded as 1.38 ± 0.20 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9IQQ\9IQQ_metadata.json point structures/9IQQ/9iqq_protein.pdb structures/9IQQ/9iqq_pocket.pdb structures/9IQQ/9iqq_ligand.sdf structures/9IQQ/9iqq_ligand.pdb structures/9IQQ/9iqq_ligand.cif structures/9IQQ/9iqq_complex.pdb structures/9IQQ/9iqq_complex.cif 9ISD classic human secretory glutaminyl cyclase (sQC) human amino acids 33-361 Na compound 5; N-(1H-benzo[d]imidazol-5-yl)-1-phenylmethanesulfonamide; STK936575 "[""A1D93""]" 2 Ki Ki = = 6.71 μM 6710.0 [] unit_conversion 5.1732774798310075 success True biochemical_inhibition Purified sQC inhibition activity assay; all determinations tested in triplicate. 8 Compound 5 manifested Ki = 6.71 μM to sQC; page 10 maps sQC:5 to PDB 9ISD. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9ISD\9ISD_metadata.json point structures/9ISD/9isd_protein.pdb structures/9ISD/9isd_pocket.pdb structures/9ISD/9isd_ligand.sdf structures/9ISD/9isd_ligand.pdb structures/9ISD/9isd_ligand.cif structures/9ISD/9isd_complex.pdb structures/9ISD/9isd_complex.cif 9ISE classic MTHFD1 human residues 1-301 with a C-terminal 6xHis tag Na LY374571 "[""9L9""]" 1 IC50 IC50 = = 630 ± 60 nM 630.0 [] unit_conversion 6.200659450546418 success True biochemical_inhibition Enzyme-based inhibition assay; Table 1. Assay methods describe purified human MTHFD1 residues 1–301 with a C-terminal His tag in an enzymatic reaction with cofactor and inhibitor. 5 Table 1 reports LY374571: MTHFD1 IC50 = 630 ± 60 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9ISE\9ISE_metadata.json point structures/9ISE/9ise_protein.pdb structures/9ISE/9ise_pocket.pdb structures/9ISE/9ise_ligand.sdf structures/9ISE/9ise_ligand.pdb structures/9ISE/9ise_ligand.cif structures/9ISE/9ise_complex.pdb structures/9ISE/9ise_complex.cif 9ISL classic MTHFD1 human residues 1-301 with a C-terminal 6xHis tag Na compound 16e "[""A1L23""]" 1 IC50 IC50 = = 1790 ± 100 nM 1790.0 [] unit_conversion 5.747146969020107 success True biochemical_inhibition Enzyme-based inhibition assay; Table 1. Assay methods describe purified human MTHFD1 residues 1–301 with a C-terminal His tag in an enzymatic reaction with cofactor and inhibitor. 5 Table 1 reports compound 16e: MTHFD1 IC50 = 1790 ± 100 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9ISL\9ISL_metadata.json point structures/9ISL/9isl_protein.pdb structures/9ISL/9isl_pocket.pdb structures/9ISL/9isl_ligand.sdf structures/9ISL/9isl_ligand.pdb structures/9ISL/9isl_ligand.cif structures/9ISL/9isl_complex.pdb structures/9ISL/9isl_complex.cif 9ISR extended MTHFD1 human residues 1-301 with a C-terminal 6xHis tag Na compound 16g "[""A1L24""]" 1 IC50 IC50 = = 230 ± 0 nM 230.0 [] unit_conversion 6.638272163982407 success True biochemical_inhibition Enzyme-based inhibition assay; Table 1. Assay methods describe purified human MTHFD1 residues 1–301 with a C-terminal His tag in an enzymatic reaction with cofactor and inhibitor. 5 Table 1 reports compound 16g: MTHFD1 IC50 = 230 ± 0 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9ISR\9ISR_metadata.json point structures/9ISR/9isr_protein.pdb structures/9ISR/9isr_pocket.pdb structures/9ISR/9isr_ligand.pdb structures/9ISR/9isr_ligand.cif structures/9ISR/9isr_complex.pdb structures/9ISR/9isr_complex.cif 9ITD extended MTHFD1 human residues 1-301 with a C-terminal 6xHis tag Na compound 16a "[""A1L22""]" 1 IC50 IC50 = = 120 ± 0 nM 120.0 [] unit_conversion 6.920818753952375 success True biochemical_inhibition Enzyme-based inhibition assay; Table 1. Assay methods describe purified human MTHFD1 residues 1–301 with a C-terminal His tag in an enzymatic reaction with cofactor and inhibitor. 5 Table 1 reports compound 16a: MTHFD1 IC50 = 120 ± 0 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9ITD\9ITD_metadata.json point structures/9ITD/9itd_protein.pdb structures/9ITD/9itd_pocket.pdb structures/9ITD/9itd_ligand.pdb structures/9ITD/9itd_ligand.cif structures/9ITD/9itd_complex.pdb structures/9ITD/9itd_complex.cif 9IUO classic MTHFD1 human residues 1-301 with a C-terminal 6xHis tag Na compound 16d "[""A1L25""]" 1 IC50 IC50 = = 5160 ± 1170 nM 5160.0 [] unit_conversion 5.287350298372789 success True biochemical_inhibition Enzyme-based inhibition assay; Table 1. Assay methods describe purified human MTHFD1 residues 1–301 with a C-terminal His tag in an enzymatic reaction with cofactor and inhibitor. 5 Table 1 reports compound 16d: MTHFD1 IC50 = 5160 ± 1170 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9IUO\9IUO_metadata.json point structures/9IUO/9iuo_protein.pdb structures/9IUO/9iuo_pocket.pdb structures/9IUO/9iuo_ligand.sdf structures/9IUO/9iuo_ligand.pdb structures/9IUO/9iuo_ligand.cif structures/9IUO/9iuo_complex.pdb structures/9IUO/9iuo_complex.cif 9IVB classic c-Met kinase domain human residues 1038-1346 with an N-terminal His-SUMO tag Na bozitinib (PLB-1001) "[""A1L3A""]" 1 IC50 IC50 = = 2.2 nM 2.2 [] unit_conversion 8.657577319177793 success True biochemical_inhibition ADP-Glo kinase inhibition assay using purified c-Met kinase domain. 5 Fig. 3B reports bozitinib IC50 of 2.2 nM for c-Met; the text identifies this as purified c-Met kinase-domain inhibition. auto_single_measurement only accepted activity measurement [1] 1 structures\9IVB\9IVB_metadata.json point structures/9IVB/9ivb_protein.pdb structures/9IVB/9ivb_pocket.pdb structures/9IVB/9ivb_ligand.sdf structures/9IVB/9ivb_ligand.pdb structures/9IVB/9ivb_ligand.cif structures/9IVB/9ivb_complex.pdb structures/9IVB/9ivb_complex.cif 9IVC extended Aur1-Kei1 inositol phosphorylceramide synthase complex Saccharomyces cerevisiae Na Na aureobasidin A (AbA) "[""POLYMER_ENTITY:3""]" 3 Kd Kd = = 57.70 ± 15.14 nM 57.7 [] unit_conversion 7.238824186844269 success True direct_binding Microscale thermophoresis measurement of AbA binding to WT Aur1-Kei1 complex. 8 Fig. 6B prints WT Kd = 57.70 ± 15.14 nM for Aur1-Kei1 binding to AbA. auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\9IVC\9IVC_metadata.json point structures/9IVC/9ivc_protein.pdb structures/9IVC/9ivc_pocket.pdb structures/9IVC/9ivc_ligand.pdb structures/9IVC/9ivc_ligand.cif structures/9IVC/9ivc_complex.pdb structures/9IVC/9ivc_complex.cif 9IVQ extended G3BP1 Homo sapiens (human) G3BP1 NTF2L domain, residues 1-138 Na CHIKV-43 "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 0.078 ± 0.005 µM 78.0 [] unit_conversion 7.107905397309519 success True direct_binding ITC of purified CHIKV-43 peptide with purified NTF2L. 6 Fig. 2C prints Kd = 0.078 ± 0.005 µM for CHIKV-43 / NTF2L. auto_single_measurement only accepted activity measurement [1] 1 structures\9IVQ\9IVQ_metadata.json point structures/9IVQ/9ivq_protein.pdb structures/9IVQ/9ivq_pocket.pdb structures/9IVQ/9ivq_ligand.pdb structures/9IVQ/9ivq_ligand.cif structures/9IVQ/9ivq_complex.pdb structures/9IVQ/9ivq_complex.cif 9IVR extended G3BP1 Homo sapiens (human) G3BP1 NTF2L domain, residues 1-138 Na CHIKV-43 "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L"", ""CHAIN:U"", ""CHAIN:V"", ""CHAIN:W"", ""CHAIN:X""]" 1 Kd Kd = = 0.078 ± 0.005 µM 78.0 [] unit_conversion 7.107905397309519 success True direct_binding ITC of purified CHIKV-43 peptide with purified NTF2L. 6 Fig. 2C prints Kd = 0.078 ± 0.005 µM for CHIKV-43 / NTF2L. auto_single_measurement only accepted activity measurement [1] 1 structures\9IVR\9IVR_metadata.json point structures/9IVR/9ivr_protein.pdb structures/9IVR/9ivr_pocket.pdb structures/9IVR/9ivr_ligand.pdb structures/9IVR/9ivr_ligand.cif structures/9IVR/9ivr_complex.pdb structures/9IVR/9ivr_complex.cif 9IVS extended G3BP1 Homo sapiens (human) G3BP1 NTF2L domain, residues 1-138 Na CHIKV-43 "[""CHAIN:I"", ""CHAIN:J"", ""CHAIN:K"", ""CHAIN:L"", ""CHAIN:U"", ""CHAIN:V"", ""CHAIN:W"", ""CHAIN:X""]" 1 Kd Kd = = 0.078 ± 0.005 µM 78.0 [] unit_conversion 7.107905397309519 success True direct_binding ITC of purified CHIKV-43 peptide with purified NTF2L. 6 Fig. 2C prints Kd = 0.078 ± 0.005 µM for CHIKV-43 / NTF2L. auto_single_measurement only accepted activity measurement [1] 1 structures\9IVS\9IVS_metadata.json point structures/9IVS/9ivs_protein.pdb structures/9IVS/9ivs_pocket.pdb structures/9IVS/9ivs_ligand.pdb structures/9IVS/9ivs_ligand.cif structures/9IVS/9ivs_complex.pdb structures/9IVS/9ivs_complex.cif 9IVV extended human secretory glutaminyl cyclase (sQC) human amino acids 33-361 Na compound 13; 3-((2-(1H-imidazol-5-yl)ethyl)carbamoyl)-4-amino-1,2,5-oxadiazole 2-oxide; STK779818 "[""A1D94""]" 2 Ki Ki = = 3.33 μM 3330.0 [] unit_conversion 5.47755576649368 success True biochemical_inhibition Purified sQC inhibition activity assay; all determinations tested in triplicate. 8 Compound 13 manifested Ki = 3.33 μM to sQC; page 10 maps sQC:13 to PDB 9IVV. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9IVV\9IVV_metadata.json point structures/9IVV/9ivv_protein.pdb structures/9IVV/9ivv_pocket.pdb structures/9IVV/9ivv_ligand.pdb structures/9IVV/9ivv_ligand.cif structures/9IVV/9ivv_complex.pdb structures/9IVV/9ivv_complex.cif 9IZL classic hVanin-1 human Codon-optimized hVanin-1 residues 22-493 with a C-terminal His tag Na X17 "[""A1EAG""]" 2 Kd Kd = = 47.8 nM 47.8 [] unit_conversion 7.320572103387882 success True direct_binding Surface plasmon resonance (SPR) binding analysis of X17 with hVanin-1. 9 The Binding Affinity section states that SPR gave a calculated KD of 47.8 nM for X17 binding to hVanin-1. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9IZL\9IZL_metadata.json point structures/9IZL/9izl_protein.pdb structures/9IZL/9izl_pocket.pdb structures/9IZL/9izl_ligand.sdf structures/9IZL/9izl_ligand.pdb structures/9IZL/9izl_ligand.cif structures/9IZL/9izl_complex.pdb structures/9IZL/9izl_complex.cif 9J0A extended ANKRD11/STAG2/RAD21 Na ANKRD11 residues 342-378 bound to the STAG2-RAD21 subcomplex Na Na "[""CHAIN:C"", ""CHAIN:F""]" 1 Kd Kd = = 0.10±0.01 µM 100.0 [] unit_conversion 7.0 success True direct_binding ITC measurement of ANKRD11 342–378 binding to purified STAG2–RAD21. 2 Fig. 1I lists ANKRD11 342–378 with Kd 0.10±0.01 µM; the figure caption states binding was determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\9J0A\9J0A_metadata.json point structures/9J0A/9j0a_protein.pdb structures/9J0A/9j0a_pocket.pdb structures/9J0A/9j0a_ligand.pdb structures/9J0A/9j0a_ligand.cif structures/9J0A/9j0a_complex.pdb structures/9J0A/9j0a_complex.cif 9J14 classic AZG2 Arabidopsis thaliana wild-type AZG2 wild-type trans-zeatin (tZ) "[""ZEA""]" 1 Kd Kd = = 0.39 ± 0.09 μM 390.0 [] unit_conversion 6.4089353929735005 success True direct_binding Isothermal titration calorimetry (ITC) using purified AZG2 at pH 5.5. 2 At pH 5.5, the dissociation constant (Kd) was 0.39 ± 0.09 μM for tZ. auto_single_measurement only accepted activity measurement [1] 1 structures\9J14\9J14_metadata.json point structures/9J14/9j14_protein.pdb structures/9J14/9j14_pocket.pdb structures/9J14/9j14_ligand.sdf structures/9J14/9j14_ligand.pdb structures/9J14/9j14_ligand.cif structures/9J14/9j14_complex.pdb structures/9J14/9j14_complex.cif 9J15 classic AZG2 Arabidopsis thaliana wild-type AZG2 wild-type adenine "[""ADE""]" 1 Kd Kd = = 0.77 ± 0.09 μM 770.0 [] unit_conversion 6.113509274827518 success True direct_binding Isothermal titration calorimetry (ITC) using purified AZG2 at pH 5.5. 2 At pH 5.5, the dissociation constant (Kd) was 0.77 ± 0.09 μM for adenine. auto_single_measurement only accepted activity measurement [1] 1 structures\9J15\9J15_metadata.json point structures/9J15/9j15_protein.pdb structures/9J15/9j15_pocket.pdb structures/9J15/9j15_ligand.sdf structures/9J15/9j15_ligand.pdb structures/9J15/9j15_ligand.cif structures/9J15/9j15_complex.pdb structures/9J15/9j15_complex.cif 9J16 classic AZG2 Arabidopsis thaliana wild-type AZG2 wild-type adenine "[""ADE""]" 1 Kd Kd = = 6.67 ± 2.78 μM 6670.0 [] unit_conversion 5.175874166083451 success True direct_binding Isothermal titration calorimetry (ITC) using purified AZG2 at pH 7.4. 2 At pH 7.4, binding affinities were reduced for adenine, with Kd 6.67 ± 2.78 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9J16\9J16_metadata.json point structures/9J16/9j16_protein.pdb structures/9J16/9j16_pocket.pdb structures/9J16/9j16_ligand.sdf structures/9J16/9j16_ligand.pdb structures/9J16/9j16_ligand.cif structures/9J16/9j16_complex.pdb structures/9J16/9j16_complex.cif 9J17 classic AZG2 Arabidopsis thaliana wild-type AZG2 wild-type trans-zeatin (tZ) "[""ZEA""]" 1 Kd Kd = = 13.40 ± 71.00 μM 13400.0 [] unit_conversion 4.872895201635193 success True direct_binding Isothermal titration calorimetry (ITC) using purified AZG2 at pH 7.4. 2 At pH 7.4, binding affinities were reduced for tZ, with Kd 13.40 ± 71.00 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9J17\9J17_metadata.json point structures/9J17/9j17_protein.pdb structures/9J17/9j17_pocket.pdb structures/9J17/9j17_ligand.sdf structures/9J17/9j17_ligand.pdb structures/9J17/9j17_ligand.cif structures/9J17/9j17_complex.pdb structures/9J17/9j17_complex.cif 9J18 classic AZG2 Arabidopsis thaliana wild-type AZG2 wild-type trans-zeatin (tZ) "[""ZEA""]" 1 Kd Kd = = 13.40 ± 71.00 μM 13400.0 [] unit_conversion 4.872895201635193 success True direct_binding Isothermal titration calorimetry (ITC) using purified AZG2 at pH 7.4. 2 At pH 7.4, binding affinities were reduced for tZ, with Kd 13.40 ± 71.00 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9J18\9J18_metadata.json point structures/9J18/9j18_protein.pdb structures/9J18/9j18_pocket.pdb structures/9J18/9j18_ligand.sdf structures/9J18/9j18_ligand.pdb structures/9J18/9j18_ligand.cif structures/9J18/9j18_complex.pdb structures/9J18/9j18_complex.cif 9J19 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na minocycline "[""MIY""]" 1 Kd Kd = = 57.50 µM 57500.0 [] unit_conversion 4.2403321553103694 success True direct_binding SPR direct binding of minocycline hydrochloride to purified SARS-CoV-2 Mpro. 6 Table 1 reports minocycline hydrochloride binding affinity K_D = 57.50 µM from the SPR experiment; Figure 3 describes direct binding of selected molecules to purified SARS-CoV-2 Mpro. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9J19\9J19_metadata.json point structures/9J19/9j19_protein.pdb structures/9J19/9j19_pocket.pdb structures/9J19/9j19_ligand.sdf structures/9J19/9j19_ligand.pdb structures/9J19/9j19_ligand.cif structures/9J19/9j19_complex.pdb structures/9J19/9j19_complex.cif 9J20 extended WDR5 human WDR5 residues 24-334; complexed with Kif2A114-122 peptide Na Kif2A114-122 peptide (GSARARPSQ) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.78 ± 0.05 μM 780.0 [] unit_conversion 6.107905397309519 success True direct_binding ITC in 200 mM NaCl solution; WDR5 titrated with Kif2A114-122 peptide; experiments performed in duplicate. 3 Table 1 reports WDR5–Kif2A K_D = 0.78 ± 0.05 μM; the Results text identifies the synthetic Kif2A residues 114–122 peptide as GSARARPSQ. auto_single_measurement only accepted activity measurement [1] 1 structures\9J20\9J20_metadata.json point structures/9J20/9j20_protein.pdb structures/9J20/9j20_pocket.pdb structures/9J20/9j20_ligand.pdb structures/9J20/9j20_ligand.cif structures/9J20/9j20_complex.pdb structures/9J20/9j20_complex.cif 9J2Y classic cGAS Human h-cGASCD, residues 157-522 Na G150 "[""JUJ""]" 1 IC50 IC50 = = 0.06 ± 0.01 µM 60.0 [] unit_conversion 7.221848749616356 success True biochemical_inhibition PPI assay; molecular-level enzymatic inhibition reported in the Figure 7 table. 11 Figure 7 table reports G150: IC50 (PPI assay) 0.06 ± 0.01 µM (h-cGAS). auto_single_measurement only accepted activity measurement [1] 1 structures\9J2Y\9J2Y_metadata.json point structures/9J2Y/9j2y_protein.pdb structures/9J2Y/9j2y_pocket.pdb structures/9J2Y/9j2y_ligand.sdf structures/9J2Y/9j2y_ligand.pdb structures/9J2Y/9j2y_ligand.cif structures/9J2Y/9j2y_complex.pdb structures/9J2Y/9j2y_complex.cif 9J3U classic tyrosine phenol-lyase (TPL) Morganella morganii subsp. morganii Na Na 3,5-dihydroxybenzoic acid (3,5DHBA) "[""34D""]" 1 Ki Ki = = 25.7 μM 25700.0 [] unit_conversion 4.590066876668706 success True biochemical_inhibition TPL-catalyzed phenol-production kinetics; competitive inhibition determined using double-reciprocal plots in the presence of 3,5DHBA. 3 Table 1 reports 3,5DHBA Ki = 25.7 μM, competitive. The text states that 3,5DHBA showed the strongest TPL inhibition with a Ki value of 25.7 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9J3U\9J3U_metadata.json point structures/9J3U/9j3u_protein.pdb structures/9J3U/9j3u_pocket.pdb structures/9J3U/9j3u_ligand.sdf structures/9J3U/9j3u_ligand.pdb structures/9J3U/9j3u_ligand.cif structures/9J3U/9j3u_complex.pdb structures/9J3U/9j3u_complex.cif 9J40 classic LYCHOS human Na Na indoxyl sulfate (IS) "[""IOS""]" 1 Kd Kd ~ ~ 150 µM 150000.0 [] unit_conversion 3.8239087409443187 success True direct_binding Quantitative surface plasmon resonance measurement using purified WT LYCHOS; the paper states that IS binds LYCHOS with a dissociation constant of about 150 µM. 5 “LYCHOS evidently binds to IS with a dissociation constant (Kd) at about 150 μM after quantitative measurement.” auto_single_measurement only accepted activity measurement [1] 1 structures\9J40\9J40_metadata.json point structures/9J40/9j40_protein.pdb structures/9J40/9j40_pocket.pdb structures/9J40/9j40_ligand.sdf structures/9J40/9j40_ligand.pdb structures/9J40/9j40_ligand.cif structures/9J40/9j40_complex.pdb structures/9J40/9j40_complex.cif 9J4G extended serine hydroxymethyltransferase (efmSHMT/SHMT) Enterococcus faecium Na Na (+)-SHIN-2 "[""A1L3N""]" 1 Ki Ki = = 2.0 × 10^-8 M 20.0 [] unit_conversion 7.698970004336019 success True direct_binding Competitive binding assay with efmSHMT, Gly, Ser, and Me-THF; (+)-SHIN-2 displaced Me-THF. 3 The paper reports Ki values of 2.1 × 10^-8 and 2.0 × 10^-8 M for (±)- and (+)-SHIN-2, respectively, in the presence of Gly and Ser. auto_single_measurement only accepted activity measurement [1] 1 structures\9J4G\9J4G_metadata.json point structures/9J4G/9j4g_protein.pdb structures/9J4G/9j4g_pocket.pdb structures/9J4G/9j4g_ligand.pdb structures/9J4G/9j4g_ligand.cif structures/9J4G/9j4g_complex.pdb structures/9J4G/9j4g_complex.cif 9J54 extended FIP200 Claw human FIP200 residues 1490-1594 complexed with ATG16L1 residues 235-247 Na ATG16L1 FIR peptide, residues 235-247 "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 1.33 ± 0.26 µM 1330.0 [] unit_conversion 5.876148359032914 success True direct_binding Fluorescence-polarization binding assay of FITC-labelled ATG16L1(235–247) with FIP200 Claw. 2 Fig. 1e reports: “Kd = 1.33 ± 0.26 μM” for the binding affinity of FIP200 Claw with FITC-labeled ATG16L1 FIR. auto_single_measurement only accepted activity measurement [1] 1 structures\9J54\9J54_metadata.json point structures/9J54/9j54_protein.pdb structures/9J54/9j54_pocket.pdb structures/9J54/9j54_ligand.pdb structures/9J54/9j54_ligand.cif structures/9J54/9j54_complex.pdb structures/9J54/9j54_complex.cif 9J5S extended G3BP1 Homo sapiens (human) G3BP1 NTF2L domain, residues 1-138 Na CHIKV-26 "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 7.8 ± 0.8 µM 7800.0 [] unit_conversion 5.107905397309519 success True direct_binding ITC of purified CHIKV-26 peptide with purified NTF2L. 6 Fig. 2D prints Kd = 7.8 ± 0.8 µM for CHIKV-26 / NTF2L. auto_single_measurement only accepted activity measurement [1] 1 structures\9J5S\9J5S_metadata.json point structures/9J5S/9j5s_protein.pdb structures/9J5S/9j5s_pocket.pdb structures/9J5S/9j5s_ligand.pdb structures/9J5S/9j5s_ligand.cif structures/9J5S/9j5s_complex.pdb structures/9J5S/9j5s_complex.cif 9J6N classic beta-D-galactofuranosidase ORF1110 Streptomyces sp. JHA19 N-terminally His6-tagged ORF1110, residues 45-635 wild-type; Y585H mutation reverted by H585Y D-iminogalactitol (IGT) "[""A1L3Z""]" 1 Ki Ki = = 65 μM 65000.0 [] unit_conversion 4.187086643357144 success True biochemical_inhibition Competitive inhibition of ORF1110 using pNP-β-D-Galf substrate; reaction at pH 4.5 and 37 °C. 4 “When assayed with pNP-β-D-Galf, IGT competitively and potently inhibited ORF1110 with Ki = 65 μM.” The assay methods specify ORF1110 residues 45–635 with no mutation. auto_single_measurement only accepted activity measurement [1] 1 structures\9J6N\9J6N_metadata.json point structures/9J6N/9j6n_protein.pdb structures/9J6N/9j6n_pocket.pdb structures/9J6N/9j6n_ligand.sdf structures/9J6N/9j6n_ligand.pdb structures/9J6N/9j6n_ligand.cif structures/9J6N/9j6n_complex.pdb structures/9J6N/9j6n_complex.cif 9J8A extended antibody BA8 Na recombinant Fab fragment Na sulfated peptide from CCR5 "[""CHAIN:P""]" 1 Kd Kd = = 8.09 × 10⁻¹⁰ mol · L⁻¹ 0.809 [] unit_conversion 9.092051478387727 success True direct_binding SPR analysis of BA8 Fab binding to the fully sulfated CCR5 N-terminal peptide. 4 Table 1 reports the wild-type BA8–sulfated peptide interaction K_D as 8.09 × 10⁻¹⁰ mol · L⁻¹ by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\9J8A\9J8A_metadata.json point structures/9J8A/9j8a_protein.pdb structures/9J8A/9j8a_pocket.pdb structures/9J8A/9j8a_ligand.pdb structures/9J8A/9j8a_ligand.cif structures/9J8A/9j8a_complex.pdb structures/9J8A/9j8a_complex.cif 9J9D extended ALK5 kinase domain Na Na Na HM-279 (compound 19f) "[""A1L30""]" 1 IC50 IC50 = = 4.7 nM 4.7 [] unit_conversion 8.327902142064282 success True biochemical_inhibition TR-FRET biochemical kinase assay; value reported in Table 4 (mean of two separate experiments). 6 Table 4 lists compound 19f with ALK5 IC50 = 4.7 nM; the Experimental Section states ALK5 enzymatic activity was measured by TR-FRET. auto_single_measurement only accepted activity measurement [1] 1 structures\9J9D\9J9D_metadata.json point structures/9J9D/9j9d_protein.pdb structures/9J9D/9j9d_pocket.pdb structures/9J9D/9j9d_ligand.pdb structures/9J9D/9j9d_ligand.cif structures/9J9D/9j9d_complex.pdb structures/9J9D/9j9d_complex.cif 9JA8 classic human phosphodiesterase 10A human catalytic domain of PDE10A Na 2081; N-(2-amino-2-thioxoethyl)-2-(3-(3-(dimethylcarbamoyl)-6-fluoroimidazo[1,2-a]pyridin-2-yl)azetidin-1-yl)quinoline-4-carboxamide "[""A1L31""]" 1 IC50 IC50 = = 3.4 ± 0.2 nmol/L 3.4 [] unit_conversion 8.468521082957745 success True biochemical_inhibition PDE10A enzymatic inhibition assay; catalytic-domain PDE10A (449–770) is described as purified in the experimental section. 3 “compound 2081, which exhibited a potent IC50 value of 3.4 nmol/L against PDE10A (Figure S1).” Figure 2 identifies PDB 9JA8 as the crystal structure of 2081 bound to the catalytic domain of PDE10A. auto_single_measurement only accepted activity measurement [1] 1 structures\9JA8\9JA8_metadata.json point structures/9JA8/9ja8_protein.pdb structures/9JA8/9ja8_pocket.pdb structures/9JA8/9ja8_ligand.sdf structures/9JA8/9ja8_ligand.pdb structures/9JA8/9ja8_ligand.cif structures/9JA8/9ja8_complex.pdb structures/9JA8/9ja8_complex.cif 9JAD classic GMPK Na Na Na GMP "[""5GP""]" 1 Kd Kd = = 7.1 ± 0.3 µM 7100.0 [] unit_conversion 5.1487416512809245 success True direct_binding ITC, GMP binding in 150 mM KCl. 4 Fig. 2b prints “@KCl 7.1 ± 0.3 µM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9JAD\9JAD_metadata.json point structures/9JAD/9jad_protein.pdb structures/9JAD/9jad_pocket.pdb structures/9JAD/9jad_ligand.sdf structures/9JAD/9jad_ligand.pdb structures/9JAD/9jad_ligand.cif structures/9JAD/9jad_complex.pdb structures/9JAD/9jad_complex.cif 9JAG classic GMPK Na Na Na ADP "[""ADP""]" 1 Kd Kd = = 11 ± 2 µM 11000.0 [] unit_conversion 4.958607314841775 success True direct_binding ITC: ADP binding to GMPK. 6 Fig. 4b prints “ADP -> GMPK 11 ± 2 µM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9JAG\9JAG_metadata.json point structures/9JAG/9jag_protein.pdb structures/9JAG/9jag_pocket.pdb structures/9JAG/9jag_ligand.sdf structures/9JAG/9jag_ligand.pdb structures/9JAG/9jag_ligand.cif structures/9JAG/9jag_complex.pdb structures/9JAG/9jag_complex.cif 9JAH classic GMPK Na Na Na GMP; ATPgammaS "[""AGS""]" 1 Kd Kd = = 11 ± 3 µM 11000.0 [] unit_conversion 4.958607314841775 success True direct_binding ITC: ATPγS binding to GMPK-GMP mixtures. 6 Fig. 4b prints “ATPγS -> GMPK+GMP 11 ± 3 µM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9JAH\9JAH_metadata.json point structures/9JAH/9jah_protein.pdb structures/9JAH/9jah_pocket.pdb structures/9JAH/9jah_ligand.sdf structures/9JAH/9jah_ligand.pdb structures/9JAH/9jah_ligand.cif structures/9JAH/9jah_complex.pdb structures/9JAH/9jah_complex.cif 9JAI classic GMPK Na Na Na GMP; ADP "[""ADP""]" 1 Kd Kd = = 14 ± 3 µM 14000.0 [] unit_conversion 4.853871964321762 success True direct_binding ITC: ADP binding to GMPK-GMP mixtures. 6 Fig. 4b prints “ADP -> GMPK+GMP 14 ± 3 µM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9JAI\9JAI_metadata.json point structures/9JAI/9jai_protein.pdb structures/9JAI/9jai_pocket.pdb structures/9JAI/9jai_ligand.sdf structures/9JAI/9jai_ligand.pdb structures/9JAI/9jai_ligand.cif structures/9JAI/9jai_complex.pdb structures/9JAI/9jai_complex.cif 9JAP classic EfAvs5 Escherichia fergusonii N-terminal His6-tagged EfAvs5 Na ATP "[""ATP""]" 1 Ki Ki = = 1.74 ± 0.098 mM 1740000.0 [] unit_conversion 2.7594507517174005 success True biochemical_inhibition Standard kinetic εNAD+-based fluorescence NADase assay of purified EfAvs5 with increasing ATP concentrations; ATP showed non-competitive inhibition. 5 “ATP non-competitively inhibits the NADase activity of EfAvs5. The molecular mechanisms responsible for these observations require further investigation.” The reported inhibition constant is “Ki = 1.74 ± 0.098 mM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9JAP\9JAP_metadata.json point structures/9JAP/9jap_protein.pdb structures/9JAP/9jap_pocket.pdb structures/9JAP/9jap_ligand.sdf structures/9JAP/9jap_ligand.pdb structures/9JAP/9jap_ligand.cif structures/9JAP/9jap_complex.pdb structures/9JAP/9jap_complex.cif 9JDC classic chanoclavine synthase (EasCcf) Claviceps fusiformis Na Na prechanoclavine (PCC) "[""LH6""]" 1 Kd Kd = = 6.21 ± 0.19 μM 6210.0 [] unit_conversion 5.20690839982342 success True direct_binding Isothermal titration calorimetry (ITC) measurement of PCC interaction with EasCcf-WT at 25 °C. 14 ITC measurement of PCC binding showed that EasCcf-WT interacted with PCC; the printed Kd was 6.21 ± 0.19 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9JDC\9JDC_metadata.json point structures/9JDC/9jdc_protein.pdb structures/9JDC/9jdc_pocket.pdb structures/9JDC/9jdc_ligand.sdf structures/9JDC/9jdc_ligand.pdb structures/9JDC/9jdc_ligand.cif structures/9JDC/9jdc_complex.pdb structures/9JDC/9jdc_complex.cif 9JF2 extended GABARAPL1 human GABARAPL1 protein complexed with ATG16L1 residues 235-247 Na ATG16L1 FIR peptide, residues 235-247 "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 4.59 ± 0.44 µM 4590.0 [] unit_conversion 5.338187314462739 success True direct_binding ITC-based direct-binding assay of GABARAPL1 with Trx-tagged ATG16L1 FIR. 5 Fig. 3a reports an ITC-based measurement of GABARAPL1 affinity with Trx-tagged ATG16L1 FIR and labels “Kd = 4.59 ± 0.44 μM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9JF2\9JF2_metadata.json point structures/9JF2/9jf2_protein.pdb structures/9JF2/9jf2_pocket.pdb structures/9JF2/9jf2_ligand.pdb structures/9JF2/9jf2_ligand.cif structures/9JF2/9jf2_complex.pdb structures/9JF2/9jf2_complex.cif 9JFM extended soluble epoxide hydrolase (sEH) Na full-length sEH protein Na (R)-14i (LXZ-42) "[""A1EBK""]" 1 IC50 IC50 = = 1.20±0.00 nM 1.2 [] unit_conversion 8.920818753952375 success True biochemical_inhibition In vitro sEH inhibition assay of chiral compound (R)-14i. 8 Figure 4C reports in vitro inhibitory activities of chiral compounds against sEH; the row for (R)-14i lists IC50±SD = 1.20±0.00 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9JFM\9JFM_metadata.json point structures/9JFM/9jfm_protein.pdb structures/9JFM/9jfm_pocket.pdb structures/9JFM/9jfm_ligand.pdb structures/9JFM/9jfm_ligand.cif structures/9JFM/9jfm_complex.pdb structures/9JFM/9jfm_complex.cif 9JHE classic 3-hydroxybutyryl-CoA dehydrogenase Faecalibacterium prausnitzii strain A2-165 Met1-Leu290; C-terminal 6xHis tag WT (native) NAD+ "[""NAD""]" 1 Kd Kd = = 346.6 ± 60.6 µM 346600.0 [] unit_conversion 3.4601714416221014 success True direct_binding Microscale thermophoresis (MST); BHBD with NAD+. 10 Figure 7b table reports “BHBD with NAD (1 mM)” Kd 346.6 ± 60.6 µM; the text identifies this as the NAD+ binding affinity for A2HBD. auto_single_measurement only accepted activity measurement [1] 1 structures\9JHE\9JHE_metadata.json point structures/9JHE/9jhe_protein.pdb structures/9JHE/9jhe_pocket.pdb structures/9JHE/9jhe_ligand.sdf structures/9JHE/9jhe_ligand.pdb structures/9JHE/9jhe_ligand.cif structures/9JHE/9jhe_complex.pdb structures/9JHE/9jhe_complex.cif 9JIQ classic V30M-TTR Na V30M-TTR with an N-terminal hexahistidine tag V30M bromoxynil; compound 6 "[""A1L36""]" 1 Ki Ki = = 2.6 ± 0.35 μM 2600.0 [] unit_conversion 5.585026652029182 success True biochemical_inhibition Acid-mediated V30M-TTR aggregation assay by turbidity at pH 5.2. 3 Table 1 reports bromoxynil (6) Ki = 2.6 ± 0.35 μM; the text identifies Ki as quantifying V30M-TTR aggregation by turbidity. auto_single_measurement only accepted activity measurement [1] 1 structures\9JIQ\9JIQ_metadata.json point structures/9JIQ/9jiq_protein.pdb structures/9JIQ/9jiq_pocket.pdb structures/9JIQ/9jiq_ligand.sdf structures/9JIQ/9jiq_ligand.pdb structures/9JIQ/9jiq_ligand.cif structures/9JIQ/9jiq_complex.pdb structures/9JIQ/9jiq_complex.cif 9JIR classic V30M-TTR Na V30M-TTR with an N-terminal hexahistidine tag V30M ioxynil; compound 21 "[""A1L37""]" 1 Ki Ki = = 3 ± 0.17 μM 3000.0 [] unit_conversion 5.522878745280337 success True biochemical_inhibition Acid-mediated V30M-TTR aggregation assay by turbidity at pH 5.2. 3 Table 1 reports ioxynil (21) Ki = 3 ± 0.17 μM; the text identifies Ki as quantifying V30M-TTR aggregation by turbidity. auto_single_measurement only accepted activity measurement [1] 1 structures\9JIR\9JIR_metadata.json point structures/9JIR/9jir_protein.pdb structures/9JIR/9jir_pocket.pdb structures/9JIR/9jir_ligand.sdf structures/9JIR/9jir_ligand.pdb structures/9JIR/9jir_ligand.cif structures/9JIR/9jir_complex.pdb structures/9JIR/9jir_complex.cif 9JIS classic V30M-TTR Na V30M-TTR with an N-terminal hexahistidine tag V30M aclonifen; compound 9 "[""A1L38""]" 1 Ki Ki = = 12 ± 0.23 μM 12000.0 [] unit_conversion 4.920818753952375 success True biochemical_inhibition Acid-mediated V30M-TTR aggregation assay by turbidity at pH 5.2. 3 Table 1 reports aclonifen (9) Ki = 12 ± 0.23 μM; the text identifies Ki as quantifying V30M-TTR aggregation by turbidity. auto_single_measurement only accepted activity measurement [1] 1 structures\9JIS\9JIS_metadata.json point structures/9JIS/9jis_protein.pdb structures/9JIS/9jis_pocket.pdb structures/9JIS/9jis_ligand.sdf structures/9JIS/9jis_ligand.pdb structures/9JIS/9jis_ligand.cif structures/9JIS/9jis_complex.pdb structures/9JIS/9jis_complex.cif 9JKL classic Staphylococcus aureus lysyl-tRNA synthetase (SaLysRS) Staphylococcus aureus Na Na lysine (L-lysine) "[""LYS""]" 1 Kd Kd = = 15 ± 0.8 mM 15000000.0 [] unit_conversion 1.8239087409443187 success True direct_binding Intrinsic fluorescence quenching; Table 3 reports dissociation constants for native SaLysRS with cognate and non-cognate amino acids. 5 Table 3 lists Native SaLysRS—Lysine: 15 ± 0.8 mM. The text identifies this as the cognate lysine Kd. auto_single_measurement only accepted activity measurement [1] 1 structures\9JKL\9JKL_metadata.json point structures/9JKL/9jkl_protein.pdb structures/9JKL/9jkl_pocket.pdb structures/9JKL/9jkl_ligand.sdf structures/9JKL/9jkl_ligand.pdb structures/9JKL/9jkl_ligand.cif structures/9JKL/9jkl_complex.pdb structures/9JKL/9jkl_complex.cif 9JPL classic DhdR Na DhdR inducer-binding domain (DhdR-HBD) Na D2HG (D-2-hydroxyglutarate) "[""2HG""]" 1 Kd Kd = = 3.1 ± 1.4 μM 3100.0 [] unit_conversion 5.508638306165727 success True direct_binding Isothermal titration calorimetry of WT DhdR with D2HG; Figure 2D/2F. 5 “The D2HG-binding KD of DhdR was 3.1 ± 1.4 μM”; Figure 2F lists WT, 3.1 ± 1.4 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9JPL\9JPL_metadata.json point structures/9JPL/9jpl_protein.pdb structures/9JPL/9jpl_pocket.pdb structures/9JPL/9jpl_ligand.sdf structures/9JPL/9jpl_ligand.pdb structures/9JPL/9jpl_ligand.cif structures/9JPL/9jpl_complex.pdb structures/9JPL/9jpl_complex.cif 9JSY classic dehydrogenase/isomerase FabX Helicobacter pylori Na Na FBX-1991; inhibitor 1991 "[""A1ECY""]" 1 IC50 IC50 = = 0.158 ± 0.030 × 10⁻⁶ M 157.99999999999997 [] unit_conversion 6.801342913045577 success True biochemical_inhibition FabX–FabI enzyme-coupled biochemical inhibition assay, in vitro. 6 Compound 8p (FBX-1991) exhibited FabX inhibitory activity with an IC₅₀ value of 0.158 ± 0.030 × 10⁻⁶ M in vitro. auto_single_measurement only accepted activity measurement [1] 1 structures\9JSY\9JSY_metadata.json point structures/9JSY/9jsy_protein.pdb structures/9JSY/9jsy_pocket.pdb structures/9JSY/9jsy_ligand.sdf structures/9JSY/9jsy_ligand.pdb structures/9JSY/9jsy_ligand.cif structures/9JSY/9jsy_complex.pdb structures/9JSY/9jsy_complex.cif 9JTX classic Factor inhibiting HIF-1 alpha (FIH) Na Na Na compound 58; 2-(4-hydroxy-2-oxo-1-(thiazol-4-ylmethoxy)-1,2-dihydroquinoline-3-carboxamido)-2-methylpropanoic acid "[""A1L4V""]" 1 IC50 IC50 = = 9.7 ± 0.7 µM 9700.0 [] unit_conversion 5.013228265733755 success True biochemical_inhibition SPE-MS inhibition assay using purified recombinant human FIH; Table 5. 13 Table 5 reports compound 58: FIH IC50 9.7 ± 0.7 µM. The assay footnote specifies SPE-MS inhibition assays; the Experimental Section states the FIH assays used purified recombinant human enzymes. auto_single_measurement only accepted activity measurement [1] 1 structures\9JTX\9JTX_metadata.json point structures/9JTX/9jtx_protein.pdb structures/9JTX/9jtx_pocket.pdb structures/9JTX/9jtx_ligand.sdf structures/9JTX/9jtx_ligand.pdb structures/9JTX/9jtx_ligand.cif structures/9JTX/9jtx_complex.pdb structures/9JTX/9jtx_complex.cif 9JU1 extended VEGF-A Na VEGF-A8-109 Na VS42-LR3 "[""CHAIN:C""]" 1 Kd Kd = = 74.9 ± 0.9 nM 74.9 [] unit_conversion 7.125518182300533 success True direct_binding Surface plasmon resonance binding affinity of VS42-LR3 to VEGF; reported in Table 1. 3 “VS42-LR3” has “K_D (nM)” of “74.9 ± 0.9”; the text states binding affinities were evaluated by surface plasmon resonance. auto_single_measurement only accepted activity measurement [1] 1 structures\9JU1\9JU1_metadata.json point structures/9JU1/9ju1_protein.pdb structures/9JU1/9ju1_pocket.pdb structures/9JU1/9ju1_ligand.pdb structures/9JU1/9ju1_ligand.cif structures/9JU1/9ju1_complex.pdb structures/9JU1/9ju1_complex.cif 9JVZ classic MtbClpP1P2 complex M. tuberculosis Na Na bortezomib (BTZ) "[""BO2""]" 1 IC50 IC50 = = 43 µM 43000.0 [] unit_conversion 4.366531544420414 success True biochemical_inhibition PMK-AMC hydrolysis by purified MtbClpP1P2 complex; IC50 estimated from the inhibition portion of the BTZ dose-response. 3 Fig. 1b visibly prints IC50 = 43 µM for PMK-AMC hydrolysis by the MtbClpP1P2 complex; the text identifies this as BTZ inhibition at high concentration after low-concentration activation. auto_single_measurement only accepted activity measurement [1] 1 structures\9JVZ\9JVZ_metadata.json point structures/9JVZ/9jvz_protein.pdb structures/9JVZ/9jvz_pocket.pdb structures/9JVZ/9jvz_ligand.sdf structures/9JVZ/9jvz_ligand.pdb structures/9JVZ/9jvz_ligand.cif structures/9JVZ/9jvz_complex.pdb structures/9JVZ/9jvz_complex.cif 9JWL classic de novo designed D-allose binding protein Na MSD1 Na D-allose "[""ALL""]" 1 Kd Kd = = 38.4 ± 6.62 μM 38400.0 [] unit_conversion 4.4156687756324695 success True direct_binding Isothermal calorimetry titration (ITC) for binding to D-allose; experimental Kd reported for MSD1. 6 Fig. 3D lists MSD1 with experimental Kd 38.4 ± 6.62 μM; caption states Kd was measured by ITC for binding to D-allose. Page 14 maps 9JWL to the MSD1 holo state. auto_single_measurement only accepted activity measurement [1] 1 structures\9JWL\9JWL_metadata.json point structures/9JWL/9jwl_protein.pdb structures/9JWL/9jwl_pocket.pdb structures/9JWL/9jwl_ligand.sdf structures/9JWL/9jwl_ligand.pdb structures/9JWL/9jwl_ligand.cif structures/9JWL/9jwl_complex.pdb structures/9JWL/9jwl_complex.cif 9JWT classic de novo designed D-allose binding protein Na MSD3 Na D-allose "[""ALL""]" 1 Kd Kd = = 51.2 ± 5.10 μM 51200.0 [] unit_conversion 4.29073003902417 success True direct_binding Isothermal calorimetry titration (ITC) for binding to D-allose; experimental Kd reported for MSD3. 6 Fig. 3D lists MSD3 with experimental Kd 51.2 ± 5.10 μM; caption states Kd was measured by ITC for binding to D-allose. Page 14 maps 9JWT to the MSD3 holo state. auto_single_measurement only accepted activity measurement [1] 1 structures\9JWT\9JWT_metadata.json point structures/9JWT/9jwt_protein.pdb structures/9JWT/9jwt_pocket.pdb structures/9JWT/9jwt_ligand.sdf structures/9JWT/9jwt_ligand.pdb structures/9JWT/9jwt_ligand.cif structures/9JWT/9jwt_complex.pdb structures/9JWT/9jwt_complex.cif 9JWV extended WDR5 human WDR5 residues 24-334; complexed with Kif2A114-122 peptide WDR5 Y191F Kif2A114-122 peptide (GSARARPSQ) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 0.96 ± 0.07 μM 960.0 [] unit_conversion 6.017728766960431 success True direct_binding ITC in 200 mM NaCl solution; WDR5_Y191F titrated with Kif2A114-122 peptide; experiments performed in duplicate. 3 Table 1 reports WDR5_Y191F–Kif2A K_D = 0.96 ± 0.07 μM. Table 2 maps the WDR5_Y191F–Kif2A114-122 structure to PDB 9JWV. auto_single_measurement only accepted activity measurement [1] 1 structures\9JWV\9JWV_metadata.json point structures/9JWV/9jwv_protein.pdb structures/9JWV/9jwv_pocket.pdb structures/9JWV/9jwv_ligand.pdb structures/9JWV/9jwv_ligand.cif structures/9JWV/9jwv_complex.pdb structures/9JWV/9jwv_complex.cif 9K0F extended Amyloid-beta42 (Aβ42) Na Na Na 4b; beta-GalNAc-modified Aβ9-21 glycopeptide "[""CHAIN:K"", ""CHAIN:N"", ""CHAIN:O""]" 1 Kd Kd = = 17.4 µM 17400.0 [] unit_conversion 4.7594507517174005 success True direct_binding BioLayer interferometry (BLI) of biotinylated Aβ42 immobilized on streptavidin biosensors with glycopeptide 4b in kinetic buffer at 30 °C. 3 Fig. 2e explicitly reports K_D = 17.4 µM for peptide 4b with Aβ42; the BLI method is described on page 12. auto_single_measurement only accepted activity measurement [1] 1 structures\9K0F\9K0F_metadata.json point structures/9K0F/9k0f_protein.pdb structures/9K0F/9k0f_pocket.pdb structures/9K0F/9k0f_ligand.pdb structures/9K0F/9k0f_ligand.cif structures/9K0F/9k0f_complex.pdb structures/9K0F/9k0f_complex.cif 9K7H classic dehydrogenase/isomerase FabX Helicobacter pylori Na Na FBX-1872; inhibitor 1872 "[""A1EEQ""]" 2 Kd Kd = = 0.435 ± 0.046 × 10⁻⁶ M 434.99999999999994 [] unit_conversion 6.361510743045363 success True direct_binding Microscale thermophoresis binding-affinity evaluation of FBX-1872 against FabX. 6 FBX-1872 binds to FabX with a Kd value of 0.435 ± 0.046 × 10⁻⁶ M (Figure 4C). auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9K7H\9K7H_metadata.json point structures/9K7H/9k7h_protein.pdb structures/9K7H/9k7h_pocket.pdb structures/9K7H/9k7h_ligand.sdf structures/9K7H/9k7h_ligand.pdb structures/9K7H/9k7h_ligand.cif structures/9K7H/9k7h_complex.pdb structures/9K7H/9k7h_complex.cif 9KD5 extended WDR5 human WDR5 residues 24-334; complexed with Kif2A114-122 peptide Kif2A S121G Kif2A114-122 S121G peptide (GSARARPGQ) "[""POLYMER_ENTITY:2""]" 1 Kd Kd = = 3.72 ± 0.23 μM 3720.0 [] unit_conversion 5.429457060118103 success True direct_binding ITC in 200 mM NaCl solution; WDR5 titrated with Kif2A114-122 S121G peptide; experiments performed in duplicate. 3 Table 1 reports WDR5–Kif2A_S121G K_D = 3.72 ± 0.23 μM. Table 2 maps the WDR5–Kif2A114-122 S121G structure to PDB 9KD5. auto_single_measurement only accepted activity measurement [1] 1 structures\9KD5\9KD5_metadata.json point structures/9KD5/9kd5_protein.pdb structures/9KD5/9kd5_pocket.pdb structures/9KD5/9kd5_ligand.pdb structures/9KD5/9kd5_ligand.cif structures/9KD5/9kd5_complex.pdb structures/9KD5/9kd5_complex.cif 9KG5 classic CYP154C5 Nocardia farcinica Na F92A/R114A/T248D/E282A testosterone "[""TES""]" 1 Kd Kd = = 6.3 × 10⁻8 M 62.99999999999999 [] unit_conversion 7.200659450546418 success True direct_binding Dissociation constant for testosterone reported in Table 1 for the AAA/T248D CYP154C5 mutant. 4 Table 1, “Kinetic Parameters of WT and Typical Mutants for H2O2 and Testosterone and Dissociation Constants (Kd) for Testosterone,” lists Kd = 6.3 × 10⁻8 M for AAA/T248D. The text identifies AAA as F92A/R114A/E282A; page 6 maps AAA/T248D to PDB 9KG5 in complex with testosterone. auto_single_measurement only accepted activity measurement [1] 1 structures\9KG5\9KG5_metadata.json point structures/9KG5/9kg5_protein.pdb structures/9KG5/9kg5_pocket.pdb structures/9KG5/9kg5_ligand.sdf structures/9KG5/9kg5_ligand.pdb structures/9KG5/9kg5_ligand.cif structures/9KG5/9kg5_complex.pdb structures/9KG5/9kg5_complex.cif 9KGJ extended SARS-CoV-2 Mpro SARS-CoV-2 Na Na compound 18 "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 0.008 ± 0.000 μM 8.0 [] unit_conversion 8.096910013008056 success True biochemical_inhibition FRET-based biochemical protease inhibition assay. 5 Table 3 reports SARS-CoV-2 IC50 = 0.008 ± 0.000 μM for compound 18; Figure 4 assigns compound 18 to PDB 9KGJ. auto_single_measurement only accepted activity measurement [1] 1 structures\9KGJ\9KGJ_metadata.json point structures/9KGJ/9kgj_protein.pdb structures/9KGJ/9kgj_pocket.pdb structures/9KGJ/9kgj_ligand.pdb structures/9KGJ/9kgj_ligand.cif structures/9KGJ/9kgj_complex.pdb structures/9KGJ/9kgj_complex.cif 9KGM classic OsHPPD Oryza sativa Na Na MBQ (methyl-benquitrione) "[""92X""]" 1 IC50 IC50 = = 0.085 ± 0.003 μM 85.0 [] unit_conversion 7.070581074285707 success True biochemical_inhibition Purified OsHPPD inhibitor IC50 assay; Figure 3B reports mean ± SD, n = 3. 4 Figure 2B maps PDB 9KGM to OsHPPD_MBQ. Figure 3B reports the WT OsHPPD IC50 against MBQ as 0.085 ± 0.003 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9KGM\9KGM_metadata.json point structures/9KGM/9kgm_protein.pdb structures/9KGM/9kgm_pocket.pdb structures/9KGM/9kgm_ligand.sdf structures/9KGM/9kgm_ligand.pdb structures/9KGM/9kgm_ligand.cif structures/9KGM/9kgm_complex.pdb structures/9KGM/9kgm_complex.cif 9KGN extended SARS-CoV-2 Mpro SARS-CoV-2 Na Na compound 3 "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 0.035 ± 0.001 μM 35.0 [] unit_conversion 7.455931955649724 success True biochemical_inhibition FRET-based biochemical protease inhibition assay. 2 Figure 1 reports SARS-CoV-2 Mpro IC50 = 0.035 ± 0.001 μM for compound 3; Figure 2 assigns compound 3 to PDB 9KGN. auto_single_measurement only accepted activity measurement [1] 1 structures\9KGN\9KGN_metadata.json point structures/9KGN/9kgn_protein.pdb structures/9KGN/9kgn_pocket.pdb structures/9KGN/9kgn_ligand.pdb structures/9KGN/9kgn_ligand.cif structures/9KGN/9kgn_complex.pdb structures/9KGN/9kgn_complex.cif 9KGQ extended SARS-CoV-2 Mpro SARS-CoV-2 Na Na compound 4 "[""CHAIN:C"", ""CHAIN:D""]" 1 IC50 IC50 = = 0.011 ± 0.001 μM 11.0 [] unit_conversion 7.958607314841775 success True biochemical_inhibition FRET-based biochemical protease inhibition assay. 2 Figure 1 reports SARS-CoV-2 Mpro IC50 = 0.011 ± 0.001 μM for compound 4; Figure 2 assigns compound 4 to PDB 9KGQ. auto_single_measurement only accepted activity measurement [1] 1 structures\9KGQ\9KGQ_metadata.json point structures/9KGQ/9kgq_protein.pdb structures/9KGQ/9kgq_pocket.pdb structures/9KGQ/9kgq_ligand.pdb structures/9KGQ/9kgq_ligand.cif structures/9KGQ/9kgq_complex.pdb structures/9KGQ/9kgq_complex.cif 9KGR extended SARS-CoV-2 Mpro SARS-CoV-2 Na Na compound 15 "[""POLYMER_ENTITY:2""]" 1 IC50 IC50 = = 0.010 ± 0.000 μM 10.0 [] unit_conversion 8.0 success True biochemical_inhibition FRET-based biochemical protease inhibition assay. 4 Table 2 reports SARS-CoV-2 IC50 = 0.010 ± 0.000 μM for compound 15; Figure 3 assigns compound 15 to PDB 9KGR. auto_single_measurement only accepted activity measurement [1] 1 structures\9KGR\9KGR_metadata.json point structures/9KGR/9kgr_protein.pdb structures/9KGR/9kgr_pocket.pdb structures/9KGR/9kgr_ligand.pdb structures/9KGR/9kgr_ligand.cif structures/9KGR/9kgr_complex.pdb structures/9KGR/9kgr_complex.cif 9KJG classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37203 "[""A1L5X""]" 1 IC50 IC50 = = 3.80 ± 0.257 µM 3800.0 [] unit_conversion 5.42021640338319 success True biochemical_inhibition Inhibitor-coupled nuclease activity assay against dsDNA; Figure 1D. 6 Figure 1D reports mTREX1 IC50 for NSC37203: 3.80 ± 0.257 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9KJG\9KJG_metadata.json point structures/9KJG/9kjg_protein.pdb structures/9KJG/9kjg_pocket.pdb structures/9KJG/9kjg_ligand.sdf structures/9KJG/9kjg_ligand.pdb structures/9KJG/9kjg_ligand.cif structures/9KJG/9kjg_complex.pdb structures/9KJG/9kjg_complex.cif 9KJH classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37203 "[""A1L5X""]" 1 IC50 IC50 = = 3.80 ± 0.257 µM 3800.0 [] unit_conversion 5.42021640338319 success True biochemical_inhibition Inhibitor-coupled nuclease activity assay against dsDNA; Figure 1D. 6 Figure 1D reports mTREX1 IC50 for NSC37203: 3.80 ± 0.257 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9KJH\9KJH_metadata.json point structures/9KJH/9kjh_protein.pdb structures/9KJH/9kjh_pocket.pdb structures/9KJH/9kjh_ligand.sdf structures/9KJH/9kjh_ligand.pdb structures/9KJH/9kjh_ligand.cif structures/9KJH/9kjh_complex.pdb structures/9KJH/9kjh_complex.cif 9KJI classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37203 "[""A1L5X""]" 1 IC50 IC50 = = 3.80 ± 0.257 µM 3800.0 [] unit_conversion 5.42021640338319 success True biochemical_inhibition Inhibitor-coupled nuclease activity assay against dsDNA; Figure 1D. 6 Figure 1D reports mTREX1 IC50 for NSC37203: 3.80 ± 0.257 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9KJI\9KJI_metadata.json point structures/9KJI/9kji_protein.pdb structures/9KJI/9kji_pocket.pdb structures/9KJI/9kji_ligand.sdf structures/9KJI/9kji_ligand.pdb structures/9KJI/9kji_ligand.cif structures/9KJI/9kji_complex.pdb structures/9KJI/9kji_complex.cif 9KJK classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37204 "[""A1L5Z""]" 1 IC50 IC50 = = 12.33 ± 0.616 µM 12330.0 [] unit_conversion 4.909036923404268 success True biochemical_inhibition Inhibitor-coupled nuclease activity assay against dsDNA; Figure 1D. 6 Figure 1D reports mTREX1 IC50 for NSC37204: 12.33 ± 0.616 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9KJK\9KJK_metadata.json point structures/9KJK/9kjk_protein.pdb structures/9KJK/9kjk_pocket.pdb structures/9KJK/9kjk_ligand.sdf structures/9KJK/9kjk_ligand.pdb structures/9KJK/9kjk_ligand.cif structures/9KJK/9kjk_complex.pdb structures/9KJK/9kjk_complex.cif 9KJL classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37204 "[""A1L5Z""]" 1 IC50 IC50 = = 12.33 ± 0.616 µM 12330.0 [] unit_conversion 4.909036923404268 success True biochemical_inhibition Inhibitor-coupled nuclease activity assay against dsDNA; Figure 1D. 6 Figure 1D reports mTREX1 IC50 for NSC37204: 12.33 ± 0.616 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9KJL\9KJL_metadata.json point structures/9KJL/9kjl_protein.pdb structures/9KJL/9kjl_pocket.pdb structures/9KJL/9kjl_ligand.sdf structures/9KJL/9kjl_ligand.pdb structures/9KJL/9kjl_ligand.cif structures/9KJL/9kjl_complex.pdb structures/9KJL/9kjl_complex.cif 9KJM classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37204 "[""A1L5Z""]" 1 IC50 IC50 = = 12.33 ± 0.616 µM 12330.0 [] unit_conversion 4.909036923404268 success True biochemical_inhibition Inhibitor-coupled nuclease activity assay against dsDNA; Figure 1D. 6 Figure 1D reports mTREX1 IC50 for NSC37204: 12.33 ± 0.616 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9KJM\9KJM_metadata.json point structures/9KJM/9kjm_protein.pdb structures/9KJM/9kjm_pocket.pdb structures/9KJM/9kjm_ligand.sdf structures/9KJM/9kjm_ligand.pdb structures/9KJM/9kjm_ligand.cif structures/9KJM/9kjm_complex.pdb structures/9KJM/9kjm_complex.cif 9KJN classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37215-1 "[""A1L50""]" 2 Kd Kd = = 39.13 ± 1.568 µM 39130.0 [] unit_conversion 4.40749015209932 success True direct_binding Intrinsic tryptophan fluorescence assay; Figure 1F. 6 Figure 1F reports mTREX1 Kd for NSC37215: 39.13 ± 1.568 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 3 structures\9KJN\9KJN_metadata.json point structures/9KJN/9kjn_protein.pdb structures/9KJN/9kjn_pocket.pdb structures/9KJN/9kjn_ligand.sdf structures/9KJN/9kjn_ligand.pdb structures/9KJN/9kjn_ligand.cif structures/9KJN/9kjn_complex.pdb structures/9KJN/9kjn_complex.cif 9KJO classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37215-1 "[""A1L50""]" 2 Kd Kd = = 39.13 ± 1.568 µM 39130.0 [] unit_conversion 4.40749015209932 success True direct_binding Intrinsic tryptophan fluorescence assay; Figure 1F. 6 Figure 1F reports mTREX1 Kd for NSC37215: 39.13 ± 1.568 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 3 structures\9KJO\9KJO_metadata.json point structures/9KJO/9kjo_protein.pdb structures/9KJO/9kjo_pocket.pdb structures/9KJO/9kjo_ligand.sdf structures/9KJO/9kjo_ligand.pdb structures/9KJO/9kjo_ligand.cif structures/9KJO/9kjo_complex.pdb structures/9KJO/9kjo_complex.cif 9KJP classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37215-2 "[""A1L50""]" 2 Kd Kd = = 39.13 ± 1.568 µM 39130.0 [] unit_conversion 4.40749015209932 success True direct_binding Intrinsic tryptophan fluorescence assay; Figure 1F. 6 Figure 1F reports mTREX1 Kd for NSC37215: 39.13 ± 1.568 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 3 structures\9KJP\9KJP_metadata.json point structures/9KJP/9kjp_protein.pdb structures/9KJP/9kjp_pocket.pdb structures/9KJP/9kjp_ligand.sdf structures/9KJP/9kjp_ligand.pdb structures/9KJP/9kjp_ligand.cif structures/9KJP/9kjp_complex.pdb structures/9KJP/9kjp_complex.cif 9KJQ classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37215-2 "[""A1L50""]" 2 Kd Kd = = 39.13 ± 1.568 µM 39130.0 [] unit_conversion 4.40749015209932 success True direct_binding Intrinsic tryptophan fluorescence assay; Figure 1F. 6 Figure 1F reports mTREX1 Kd for NSC37215: 39.13 ± 1.568 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 3 structures\9KJQ\9KJQ_metadata.json point structures/9KJQ/9kjq_protein.pdb structures/9KJQ/9kjq_pocket.pdb structures/9KJQ/9kjq_ligand.sdf structures/9KJQ/9kjq_ligand.pdb structures/9KJQ/9kjq_ligand.cif structures/9KJQ/9kjq_complex.pdb structures/9KJQ/9kjq_complex.cif 9KJS classic mTREX1 Mus musculus Truncated mTREX1, residues 11-242 a.a. Na NSC37215-2 "[""A1L50""]" 2 Kd Kd = = 39.13 ± 1.568 µM 39130.0 [] unit_conversion 4.40749015209932 success True direct_binding Intrinsic tryptophan fluorescence assay; Figure 1F. 6 Figure 1F reports mTREX1 Kd for NSC37215: 39.13 ± 1.568 µM. auto_metric_priority unique highest-priority metric family: Kd [2] 3 structures\9KJS\9KJS_metadata.json point structures/9KJS/9kjs_protein.pdb structures/9KJS/9kjs_pocket.pdb structures/9KJS/9kjs_ligand.sdf structures/9KJS/9kjs_ligand.pdb structures/9KJS/9kjs_ligand.cif structures/9KJS/9kjs_complex.pdb structures/9KJS/9kjs_complex.cif 9KKE classic atABCB19 Na Na Na 2-[4-(Diethylamino)-2-hydroxybenzoyl]benzoic acid (BUM) "[""A1EFV""]" 1 IC50 IC50 = = 0.89 mM 890000.0 [] unit_conversion 3.0506099933550876 success True biochemical_inhibition Concentration-dependent inhibition of nanodisc-embedded ABCB19 ATPase activity by BUM. 4 “BUM demonstrated a concentration-dependent inhibition of ABCB19, with an IC50 value of 0.89 mM (Fig. 4A).” auto_single_measurement only accepted activity measurement [1] 1 structures\9KKE\9KKE_metadata.json point structures/9KKE/9kke_protein.pdb structures/9KKE/9kke_pocket.pdb structures/9KKE/9kke_ligand.sdf structures/9KKE/9kke_ligand.pdb structures/9KKE/9kke_ligand.cif structures/9KKE/9kke_complex.pdb structures/9KKE/9kke_complex.cif 9KNH classic FTO Na N-terminal truncated FTO (FTOΔN31; residues 32-505) Na Dac590 "[""A1EF4""]" 1 IC50 IC50 = = 6.06 ± 0.5 nM 6.06 [] unit_conversion 8.217527375833713 success True biochemical_inhibition Cell-free dot-blot assay quantifying inhibition of FTO demethylase by Dac590. 4 Figure 2B reports quantification of Dac590's IC50 against FTO demethylase using a cell-free dot-blot assay: IC50 = 6.06 ± 0.5 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9KNH\9KNH_metadata.json point structures/9KNH/9knh_protein.pdb structures/9KNH/9knh_pocket.pdb structures/9KNH/9knh_ligand.sdf structures/9KNH/9knh_ligand.pdb structures/9KNH/9knh_ligand.cif structures/9KNH/9knh_complex.pdb structures/9KNH/9knh_complex.cif 9KNI extended fat mass and obesity-associated protein (FTO) Na N-terminal truncated FTO protein lacking 31 residues (FTO_NΔ31) Na 12j "[""A1EF5""]" 1 IC50 IC50 = = 0.68 ± 0.02 µM 680.0 [] unit_conversion 6.167491087293763 success True biochemical_inhibition PAGE-based FTO demethylation assay; IC50 derived from three independent replicates. 6 Table 5 reports compound 12j IC50 = 0.68 ± 0.02 µM; the text identifies 12j as an FTO inhibitor. The methods specify N-terminal truncated FTO lacking 31 residues (FTO_NΔ31) for the PAGE-based assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9KNI\9KNI_metadata.json point structures/9KNI/9kni_protein.pdb structures/9KNI/9kni_pocket.pdb structures/9KNI/9kni_ligand.pdb structures/9KNI/9kni_ligand.cif structures/9KNI/9kni_complex.pdb structures/9KNI/9kni_complex.cif 9KOY classic Oryza sativa HPPD Oryza sativa Recombinant HPPD expressed in E. coli BL21(DE3) with an N-terminal polyhistidine-GFP-bdSUMO fusion tag; the SUMO tag was cleaved before purification. Na iptriazopyrid "[""A1L59""]" 1 Ki Ki = = 33.3 ± 3.3 nM 33.3 [] unit_conversion 7.47755576649368 success True biochemical_inhibition Coupled enzyme inhibitory-kinetics assay; OsHPPD activity was measured from MAA synthesis from HPPA, with iptriazopyrid. Ki obtained by nonlinear-regression analysis of slow-binding inhibition progress curves. 3 Table 1 reports OsHPPD—iptriazopyrid Ki = 33.3 ± 3.3 nM; the Results state this value was obtained by nonlinear-regression analysis of the coupled enzyme assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9KOY\9KOY_metadata.json point structures/9KOY/9koy_protein.pdb structures/9KOY/9koy_pocket.pdb structures/9KOY/9koy_ligand.sdf structures/9KOY/9koy_ligand.pdb structures/9KOY/9koy_ligand.cif structures/9KOY/9koy_complex.pdb structures/9KOY/9koy_complex.cif 9KOZ classic Arabidopsis thaliana HPPD Arabidopsis thaliana Recombinant HPPD expressed in E. coli BL21(DE3) with an N-terminal polyhistidine-GFP-bdSUMO fusion tag; the SUMO tag was cleaved before purification. Na iptriazopyrid "[""A1L59""]" 1 Ki Ki = = 24.3 ± 0.3 nM 24.3 [] unit_conversion 7.614393726401688 success True biochemical_inhibition Coupled enzyme inhibitory-kinetics assay; AtHPPD activity was measured from MAA synthesis from HPPA, with iptriazopyrid. Ki obtained by nonlinear-regression analysis of slow-binding inhibition progress curves. 3 Table 1 reports AtHPPD—iptriazopyrid Ki = 24.3 ± 0.3 nM; the Results state this value was obtained by nonlinear-regression analysis of the coupled enzyme assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9KOZ\9KOZ_metadata.json point structures/9KOZ/9koz_protein.pdb structures/9KOZ/9koz_pocket.pdb structures/9KOZ/9koz_ligand.sdf structures/9KOZ/9koz_ligand.pdb structures/9KOZ/9koz_ligand.cif structures/9KOZ/9koz_complex.pdb structures/9KOZ/9koz_complex.cif 9KQ3 classic Saccharomyces cerevisiae succinate dehydrogenase (ScSDH) Saccharomyces cerevisiae Na Na PYD (pydiflumetofen) "[""A1EE4""]" 2 Ki Ki = = 0.042 ± 0.001 μM 42.0 [] unit_conversion 7.376750709602099 success True biochemical_inhibition Inter-species selectivity experiment; yeast/ScSDH result in Table 2. 7 Table 2 prints PYD Ki = 0.042 ± 0.001 μM for yeast SDH; the text defines the yeast enzyme as ScSDH. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9KQ3\9KQ3_metadata.json point structures/9KQ3/9kq3_protein.pdb structures/9KQ3/9kq3_pocket.pdb structures/9KQ3/9kq3_ligand.sdf structures/9KQ3/9kq3_ligand.pdb structures/9KQ3/9kq3_ligand.cif structures/9KQ3/9kq3_complex.pdb structures/9KQ3/9kq3_complex.cif 9KQK classic Human serum albumin (HSA) Homo sapiens Na Na AmpHecy "[""A1EGK""]" 1 Kd Kd = = 3.4 × 10⁻⁶ M 3399.9999999999995 [] unit_conversion 5.468521082957745 success True direct_binding Isothermal titration calorimetry (ITC) of AmpHecy binding to HSA; stoichiometry 1:1. 6 Figure 3 caption: “The AmpHecy binding thermodynamic parameters determined by isothermal titration calorimetry (ITC): the stoichiometry is calculated to be 1.4, the dissociation constant (Kd) is 3.4 × 10⁻⁶ M.” auto_single_measurement only accepted activity measurement [1] 1 structures\9KQK\9KQK_metadata.json point structures/9KQK/9kqk_protein.pdb structures/9KQK/9kqk_pocket.pdb structures/9KQK/9kqk_ligand.sdf structures/9KQK/9kqk_ligand.pdb structures/9KQK/9kqk_ligand.cif structures/9KQK/9kqk_complex.pdb structures/9KQK/9kqk_complex.cif 9KR5 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Full-length, tag-free SARS-CoV-2 Mpro (NC_045512) P132H Compound 3 "[""A1EGN""]" 1 IC50 IC50 = = 18.6 ± 5.82 nM 18.6 [] unit_conversion 7.730487055782084 success True biochemical_inhibition FRET-based enzyme inhibition assay; Table 1 reports mean ± SD of three independent experiments. 5 Table 1 reports compound 3 IC50 = 18.6 ± 5.82 nM against SARS-CoV-2 Mpro. The methods identify the IC50 assay as FRET-based and describe the expressed Mpro as P132H. auto_single_measurement only accepted activity measurement [1] 1 structures\9KR5\9KR5_metadata.json point structures/9KR5/9kr5_protein.pdb structures/9KR5/9kr5_pocket.pdb structures/9KR5/9kr5_ligand.sdf structures/9KR5/9kr5_ligand.pdb structures/9KR5/9kr5_ligand.cif structures/9KR5/9kr5_complex.pdb structures/9KR5/9kr5_complex.cif 9KRV classic BbMaeB Bdellovibrio bacteriovorus Na Na acetyl-CoA "[""ACO""]" 1 IC50 IC50 = = 0.131 ± 0.004 µM 131.0 [] unit_conversion 6.882728704344236 success True biochemical_inhibition Acetyl-CoA inhibition enzymatic assay of BbMaeB under the current SSB-homolog study. 3 “The IC50 for BbMaeB-SSB (0.131 ± 0.004 μM)” auto_single_measurement only accepted activity measurement [1] 1 structures\9KRV\9KRV_metadata.json point structures/9KRV/9krv_protein.pdb structures/9KRV/9krv_pocket.pdb structures/9KRV/9krv_ligand.sdf structures/9KRV/9krv_ligand.pdb structures/9KRV/9krv_ligand.cif structures/9KRV/9krv_complex.pdb structures/9KRV/9krv_complex.cif 9KRY classic MerTK Na MerTK kinase domain residues 571-864 with PTP1B catalytic domain residues 1-283, expressed as a bicistronic construct with an N-terminal His6 tag and thrombin cleavage site Na compound 1 "[""A1L6J""]" 1 IC50 IC50 = = 26.8 nM 26.8 [] unit_conversion 7.5718652059712115 success True biochemical_inhibition Purified MerTK enzyme inhibition assay; Kinase-Glo assay, 12 μM ATP, incubated 30 °C for 3 h. 3 Table 1 reports compound 1 MerTK IC50 = 26.8 nM; the Experimental Section describes the MerTK enzyme inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9KRY\9KRY_metadata.json point structures/9KRY/9kry_protein.pdb structures/9KRY/9kry_pocket.pdb structures/9KRY/9kry_ligand.sdf structures/9KRY/9kry_ligand.pdb structures/9KRY/9kry_ligand.cif structures/9KRY/9kry_complex.pdb structures/9KRY/9kry_complex.cif 9KRZ classic MerTK Na MerTK kinase domain residues 571-864 with PTP1B catalytic domain residues 1-283, expressed as a bicistronic construct with an N-terminal His6 tag and thrombin cleavage site Na compound 11 "[""A1L6K""]" 1 IC50 IC50 = = 21.5 nM 21.5 [] unit_conversion 7.667561540084394 success True biochemical_inhibition Purified MerTK enzyme inhibition assay; Kinase-Glo assay, 12 μM ATP, incubated 30 °C for 3 h. 7 Table 3 reports compound 11 MerTK IC50 = 21.5 nM; the Experimental Section describes the MerTK enzyme inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9KRZ\9KRZ_metadata.json point structures/9KRZ/9krz_protein.pdb structures/9KRZ/9krz_pocket.pdb structures/9KRZ/9krz_ligand.sdf structures/9KRZ/9krz_ligand.pdb structures/9KRZ/9krz_ligand.cif structures/9KRZ/9krz_complex.pdb structures/9KRZ/9krz_complex.cif 9KS9 classic MerTK Na MerTK kinase domain residues 571-864 with PTP1B catalytic domain residues 1-283, expressed as a bicistronic construct with an N-terminal His6 tag and thrombin cleavage site Na compound 6 "[""A1L6L""]" 1 IC50 IC50 = = 10.4 nM 10.4 [] unit_conversion 7.982966660701219 success True biochemical_inhibition Purified MerTK enzyme inhibition assay; Kinase-Glo assay, 12 μM ATP, incubated 30 °C for 3 h. 3 Table 1 reports compound 6 MerTK IC50 = 10.4 nM; the Experimental Section describes the MerTK enzyme inhibition assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9KS9\9KS9_metadata.json point structures/9KS9/9ks9_protein.pdb structures/9KS9/9ks9_pocket.pdb structures/9KS9/9ks9_ligand.sdf structures/9KS9/9ks9_ligand.pdb structures/9KS9/9ks9_ligand.cif structures/9KS9/9ks9_complex.pdb structures/9KS9/9ks9_complex.cif 9KSH classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Full-length, tag-free SARS-CoV-2 Mpro (NC_045512) P132H Compound 1 "[""A1EGQ""]" 1 IC50 IC50 = = 134.0 ± 15.50 nM 134.0 [] unit_conversion 6.872895201635192 success True biochemical_inhibition FRET-based enzyme inhibition assay; Table 1 reports mean ± SD of three independent experiments. 5 Table 1 reports compound 1 IC50 = 134.0 ± 15.50 nM against SARS-CoV-2 Mpro. The methods identify the IC50 assay as FRET-based and describe the expressed Mpro as P132H. auto_single_measurement only accepted activity measurement [1] 1 structures\9KSH\9KSH_metadata.json point structures/9KSH/9ksh_protein.pdb structures/9KSH/9ksh_pocket.pdb structures/9KSH/9ksh_ligand.sdf structures/9KSH/9ksh_ligand.pdb structures/9KSH/9ksh_ligand.cif structures/9KSH/9ksh_complex.pdb structures/9KSH/9ksh_complex.cif 9KSI classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Full-length, tag-free SARS-CoV-2 Mpro (NC_045512) P132H Compound 5 "[""A1EGP""]" 1 IC50 IC50 = = 50.6 ± 1.02 nM 50.6 [] unit_conversion 7.2958494831602 success True biochemical_inhibition FRET-based enzyme inhibition assay; Table 1 reports mean ± SD of three independent experiments. 5 Table 1 reports compound 5 IC50 = 50.6 ± 1.02 nM against SARS-CoV-2 Mpro. The methods identify the IC50 assay as FRET-based and describe the expressed Mpro as P132H. auto_single_measurement only accepted activity measurement [1] 1 structures\9KSI\9KSI_metadata.json point structures/9KSI/9ksi_protein.pdb structures/9KSI/9ksi_pocket.pdb structures/9KSI/9ksi_ligand.sdf structures/9KSI/9ksi_ligand.pdb structures/9KSI/9ksi_ligand.cif structures/9KSI/9ksi_complex.pdb structures/9KSI/9ksi_complex.cif 9KSJ extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Full-length, tag-free SARS-CoV-2 Mpro (NC_045512) P132H Compound 8 "[""A1EGR""]" 1 IC50 IC50 = = 19.4 ± 1.27 nM 19.4 [] unit_conversion 7.7121982700697735 success True biochemical_inhibition FRET-based enzyme inhibition assay; Table 1 reports mean ± SD of three independent experiments. 5 Table 1 reports compound 8 IC50 = 19.4 ± 1.27 nM against SARS-CoV-2 Mpro. The methods identify the IC50 assay as FRET-based and describe the expressed Mpro as P132H. auto_single_measurement only accepted activity measurement [1] 1 structures\9KSJ\9KSJ_metadata.json point structures/9KSJ/9ksj_protein.pdb structures/9KSJ/9ksj_pocket.pdb structures/9KSJ/9ksj_ligand.pdb structures/9KSJ/9ksj_ligand.cif structures/9KSJ/9ksj_complex.pdb structures/9KSJ/9ksj_complex.cif 9KSK extended SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Full-length, tag-free SARS-CoV-2 Mpro (NC_045512) P132H Compound 10 "[""A1EGS""]" 1 IC50 IC50 = = 9.1 ± 0.98 nM 9.1 [] unit_conversion 8.040958607678906 success True biochemical_inhibition FRET-based enzyme inhibition assay; Table 1 reports mean ± SD of three independent experiments. 5 Table 1 reports compound 10 IC50 = 9.1 ± 0.98 nM against SARS-CoV-2 Mpro. The methods identify the IC50 assay as FRET-based and describe the expressed Mpro as P132H. auto_single_measurement only accepted activity measurement [1] 1 structures\9KSK\9KSK_metadata.json point structures/9KSK/9ksk_protein.pdb structures/9KSK/9ksk_pocket.pdb structures/9KSK/9ksk_ligand.pdb structures/9KSK/9ksk_ligand.cif structures/9KSK/9ksk_complex.pdb structures/9KSK/9ksk_complex.cif 9KUF classic HsClpP (human caseinolytic protease P) Homo sapiens His6-SUMO-HsClpP; tag removed by Ulp1 Na CLPP-2068 "[""A1EG3""]" 1 Kd Kd = = 87.9 nM 87.9 [] unit_conversion 7.056011124926228 success True direct_binding Biolayer interferometry of HsClpP with CLPP-2068 at serial ligand concentrations. 6 Figure 4D prints “CLPP-2068 Kd = 87.9 nM”; the text identifies this as BLI binding affinity of CLPP-2068 to HsClpP. auto_single_measurement only accepted activity measurement [1] 1 structures\9KUF\9KUF_metadata.json point structures/9KUF/9kuf_protein.pdb structures/9KUF/9kuf_pocket.pdb structures/9KUF/9kuf_ligand.sdf structures/9KUF/9kuf_ligand.pdb structures/9KUF/9kuf_ligand.cif structures/9KUF/9kuf_complex.pdb structures/9KUF/9kuf_complex.cif 9KUP classic MCP2201 LBD Comamonas testosteroni MCP2201 LBD, residues 58-203 Na D-malate "[""MLT""]" 1 Kd Kd = = 40.0 ± 3.3 µM 40000.0 [] unit_conversion 4.3979400086720375 success True direct_binding Isothermal titration calorimetry (ITC) measurement of D-malate binding to MCP2201 LBD. 3 “MCP2201 LBD bound to D-malate with a dissociation constant (Kd) of 40.0 ± 3.3 μM ... in an isothermal titration calorimetry (ITC) assay.” auto_single_measurement only accepted activity measurement [1] 1 structures\9KUP\9KUP_metadata.json point structures/9KUP/9kup_protein.pdb structures/9KUP/9kup_pocket.pdb structures/9KUP/9kup_ligand.sdf structures/9KUP/9kup_ligand.pdb structures/9KUP/9kup_ligand.cif structures/9KUP/9kup_complex.pdb structures/9KUP/9kup_complex.cif 9KYT classic TapT Escherichia coli TapT29-219 (residues R29-Q219) Na SAM "[""SAM""]" 1 Kd Kd = = 57.7 ± 3.3 μM 57700.0 [] unit_conversion 4.238824186844268 success True direct_binding ITC binding of wild-type TapT29-219 with SAM. 7 Figure 3A reports: “WT vs SAM … Kd = 57.7 ± 3.3 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9KYT\9KYT_metadata.json point structures/9KYT/9kyt_protein.pdb structures/9KYT/9kyt_pocket.pdb structures/9KYT/9kyt_ligand.sdf structures/9KYT/9kyt_ligand.pdb structures/9KYT/9kyt_ligand.cif structures/9KYT/9kyt_complex.pdb structures/9KYT/9kyt_complex.cif 9KZ5 classic TapT Escherichia coli TapT29-219 (residues R29-Q219) Na MTA "[""MTA""]" 1 Kd Kd ~ ~ 150.0 μM 150000.0 [] unit_conversion 3.8239087409443187 success True direct_binding ITC binding of TapT29-219 with MTA, the TapT product. 6 “ITC analysis gave a roughly dissociation constant of 150.0 μM for MTA.” auto_single_measurement only accepted activity measurement [1] 1 structures\9KZ5\9KZ5_metadata.json point structures/9KZ5/9kz5_protein.pdb structures/9KZ5/9kz5_pocket.pdb structures/9KZ5/9kz5_ligand.sdf structures/9KZ5/9kz5_ligand.pdb structures/9KZ5/9kz5_ligand.cif structures/9KZ5/9kz5_complex.pdb structures/9KZ5/9kz5_complex.cif 9KZA classic TapT Escherichia coli TapT29-219 (residues R29-Q219) Na Sinefungin (SFG) "[""SFG""]" 1 Kd Kd = = 795 μM 795000.0 [] unit_conversion 3.0996328713435295 success True direct_binding SPR measurement of wild-type TapT29-219 binding to SFG. 6 “The dissociation constant of wild-type TapT29-219 bound to SFG measured by SPR experiment is 795 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9KZA\9KZA_metadata.json point structures/9KZA/9kza_protein.pdb structures/9KZA/9kza_pocket.pdb structures/9KZA/9kza_ligand.sdf structures/9KZA/9kza_ligand.pdb structures/9KZA/9kza_ligand.cif structures/9KZA/9kza_complex.pdb structures/9KZA/9kza_complex.cif 9L3C classic Staphylococcus aureus lipase Staphylococcus aureus Na Na Penfluridol "[""A1L60""]" 1 IC50 IC50 = = 7.3 µM 7300.0 [] unit_conversion 5.136677139879544 success True biochemical_inhibition Purified SAL activity assay using p-nitrophenylbutyrate substrate; IC50 determined from inhibitor concentration series. 4 Fig. 2a explicitly reports “IC50 = 7.3 µM” for Penfluridol versus SAL. The paper identifies 9L3C as the SAL/Penfluridol complex crystallized on the ground. auto_single_measurement only accepted activity measurement [1] 1 structures\9L3C\9L3C_metadata.json point structures/9L3C/9l3c_protein.pdb structures/9L3C/9l3c_pocket.pdb structures/9L3C/9l3c_ligand.sdf structures/9L3C/9l3c_ligand.pdb structures/9L3C/9l3c_ligand.cif structures/9L3C/9l3c_complex.pdb structures/9L3C/9l3c_complex.cif 9L3R classic Human PI3Kdelta (p110delta) Human p110delta; bovine p85alpha Human p110delta residues 1-1044 and bovine p85alpha residues 431-600 Na Zandelisib "[""A1L62""]" 1 Kd Kd = = 5.12 × 10^-11 M 0.051199999999999996 [] unit_conversion 10.290730039024169 success True direct_binding Purified PI3Kδ protein immobilized on a Biacore Sensor Chip SA; single-cycle surface plasmon resonance assay, fitted to a 1:1 binding model. 6 Table 1 reports zandelisib K_D = 5.12 × 10^-11 M for binding to PI3Kδ. The methods describe purified PI3Kδ SPR binding kinetics. auto_single_measurement only accepted activity measurement [1] 1 structures\9L3R\9L3R_metadata.json point structures/9L3R/9l3r_protein.pdb structures/9L3R/9l3r_pocket.pdb structures/9L3R/9l3r_ligand.sdf structures/9L3R/9l3r_ligand.pdb structures/9L3R/9l3r_ligand.cif structures/9L3R/9l3r_complex.pdb structures/9L3R/9l3r_complex.cif 9L3S classic Staphylococcus aureus lipase Staphylococcus aureus Na Na Penfluridol "[""A1L60""]" 1 IC50 IC50 = = 7.3 µM 7300.0 [] unit_conversion 5.136677139879544 success True biochemical_inhibition Purified SAL activity assay using p-nitrophenylbutyrate substrate; IC50 determined from inhibitor concentration series. 4 Fig. 2a explicitly reports “IC50 = 7.3 µM” for Penfluridol versus SAL. The paper identifies 9L3S as the SAL/Penfluridol complex crystallized in space. auto_single_measurement only accepted activity measurement [1] 1 structures\9L3S\9L3S_metadata.json point structures/9L3S/9l3s_protein.pdb structures/9L3S/9l3s_pocket.pdb structures/9L3S/9l3s_ligand.sdf structures/9L3S/9l3s_ligand.pdb structures/9L3S/9l3s_ligand.cif structures/9L3S/9l3s_complex.pdb structures/9L3S/9l3s_complex.cif 9L40 classic human ATR-ATRIP complex human Na Na VE-822 "[""A1EIE""]" 1 IC50 IC50 = = 2.25 nmol/L 2.25 [] unit_conversion 8.647817481888637 success True biochemical_inhibition ATR-based kinase assay measuring inhibition of CHK2 phosphorylation; Fig. 5b, mean ± s.e.m., n = 4 independent gold-standard radiolabeled ATP-based kinase assays. 8 Fig. 5b explicitly labels “VE-822 IC50 = 2.25 nmol/L”; caption identifies ATR-based kinase assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9L40\9L40_metadata.json point structures/9L40/9l40_protein.pdb structures/9L40/9l40_pocket.pdb structures/9L40/9l40_ligand.sdf structures/9L40/9l40_ligand.pdb structures/9L40/9l40_ligand.cif structures/9L40/9l40_complex.pdb structures/9L40/9l40_complex.cif 9L45 classic human ATR-ATRIP complex human Na Na VE-822 "[""A1EIE""]" 1 IC50 IC50 = = 2.25 nmol/L 2.25 [] unit_conversion 8.647817481888637 success True biochemical_inhibition ATR-based kinase assay measuring inhibition of CHK2 phosphorylation; Fig. 5b, mean ± s.e.m., n = 4 independent gold-standard radiolabeled ATP-based kinase assays. 8 Fig. 5b explicitly labels “VE-822 IC50 = 2.25 nmol/L”; caption identifies ATR-based kinase assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9L45\9L45_metadata.json point structures/9L45/9l45_protein.pdb structures/9L45/9l45_pocket.pdb structures/9L45/9l45_ligand.sdf structures/9L45/9l45_ligand.pdb structures/9L45/9l45_ligand.cif structures/9L45/9l45_complex.pdb structures/9L45/9l45_complex.cif 9L4B extended human ATR-ATRIP complex human Na Na RP-3500 "[""A1EIK""]" 1 IC50 IC50 = = 1.68 nmol/L 1.68 [] unit_conversion 8.774690718274137 success True biochemical_inhibition ATR-based kinase assay measuring inhibition of CHK2 phosphorylation; Fig. 5b, mean ± s.e.m., n = 4 independent gold-standard radiolabeled ATP-based kinase assays. 8 Fig. 5b explicitly labels “RP3500 IC50 = 1.68 nmol/L”; caption identifies ATR-based kinase assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9L4B\9L4B_metadata.json point structures/9L4B/9l4b_protein.pdb structures/9L4B/9l4b_pocket.pdb structures/9L4B/9l4b_ligand.pdb structures/9L4B/9l4b_ligand.cif structures/9L4B/9l4b_complex.pdb structures/9L4B/9l4b_complex.cif 9L4D extended human ATR-ATRIP complex human Na Na RP-3500 "[""A1EIK""]" 1 IC50 IC50 = = 1.68 nmol/L 1.68 [] unit_conversion 8.774690718274137 success True biochemical_inhibition ATR-based kinase assay measuring inhibition of CHK2 phosphorylation; Fig. 5b, mean ± s.e.m., n = 4 independent gold-standard radiolabeled ATP-based kinase assays. 8 Fig. 5b explicitly labels “RP3500 IC50 = 1.68 nmol/L”; caption identifies ATR-based kinase assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9L4D\9L4D_metadata.json point structures/9L4D/9l4d_protein.pdb structures/9L4D/9l4d_pocket.pdb structures/9L4D/9l4d_ligand.pdb structures/9L4D/9l4d_ligand.cif structures/9L4D/9l4d_complex.pdb structures/9L4D/9l4d_complex.cif 9L4N classic EcMaeB Escherichia coli Na Na acetyl-CoA "[""ACO""]" 1 IC50 IC50 = = 102 ± 4.92 µM 102000.0 [] unit_conversion 3.991399828238082 success True biochemical_inhibition Acetyl-CoA inhibition enzymatic assay of EcMaeB. 3 “The IC50 for ... EcMaeB (102 ± 4.92 μM)” auto_single_measurement only accepted activity measurement [1] 1 structures\9L4N\9L4N_metadata.json point structures/9L4N/9l4n_protein.pdb structures/9L4N/9l4n_pocket.pdb structures/9L4N/9l4n_ligand.sdf structures/9L4N/9l4n_ligand.pdb structures/9L4N/9l4n_ligand.cif structures/9L4N/9l4n_complex.pdb structures/9L4N/9l4n_complex.cif 9LB7 classic trehalose 6-phosphate phosphatase Weissella ceti Na Na beta-Glc1P "[""XGP""]" 1 Kd Kd = = 1.0 ± 0.2 mM 1000000.0 [] unit_conversion 3.0 success True direct_binding Microscale thermophoresis direct-binding assay. 5 The figure reports Kd(βGlc1P) = 1.0 ± 0.2 mM for WcTre6PPase. auto_single_measurement only accepted activity measurement [1] 1 structures\9LB7\9LB7_metadata.json point structures/9LB7/9lb7_protein.pdb structures/9LB7/9lb7_pocket.pdb structures/9LB7/9lb7_ligand.sdf structures/9LB7/9lb7_ligand.pdb structures/9LB7/9lb7_ligand.cif structures/9LB7/9lb7_complex.pdb structures/9LB7/9lb7_complex.cif 9LGL classic PKMYT1 human protein kinase domain Na compound 6 "[""A1EJW""]" 1 IC50 IC50 = = 18.1 nM 18.1 [] unit_conversion 7.7423214251308154 success True biochemical_inhibition PKMYT1 ADP-Glo enzymatic assay. 3 Table 1 reports compound 6: PKMYT1 ADP-Glo IC50 18.1 nM. Figure 2 identifies the compound 6 PKMYT1 cocrystal as PDB 9LGL. auto_single_measurement only accepted activity measurement [1] 1 structures\9LGL\9LGL_metadata.json point structures/9LGL/9lgl_protein.pdb structures/9LGL/9lgl_pocket.pdb structures/9LGL/9lgl_ligand.sdf structures/9LGL/9lgl_ligand.pdb structures/9LGL/9lgl_ligand.cif structures/9LGL/9lgl_complex.pdb structures/9LGL/9lgl_complex.cif 9LGN extended PKMYT1 human protein kinase domain Na compound 40 "[""A1EJU""]" 1 Ki Ki = = 7.0 nM 7.0 [] unit_conversion 8.154901959985743 success True biochemical_inhibition PKMYT1 Morrison Ki assay using the PKMYT1 ADP-Glo assay for a tight binder. 6 Table 3 reports compound 40: PKMYT1 Morrison Ki 7.0 nM. The table footnote defines this as a PKMYT1 ADP-Glo-based Morrison Ki assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9LGN\9LGN_metadata.json point structures/9LGN/9lgn_protein.pdb structures/9LGN/9lgn_pocket.pdb structures/9LGN/9lgn_ligand.pdb structures/9LGN/9lgn_ligand.cif structures/9LGN/9lgn_complex.pdb structures/9LGN/9lgn_complex.cif 9LGU extended BCL-XL human C-terminal 22 residues removed; C-terminal 6xHis tag Na HRKM7-S1 stapled HRK peptide "[""CHAIN:B"", ""CHAIN:D"", ""CHAIN:F"", ""CHAIN:H"", ""CHAIN:L"", ""CHAIN:M""]" 2 Ki Ki < < 1 nM 1.0 [] unit_conversion 9.0 success True biochemical_inhibition Competitive fluorescence-polarization inhibition assay of the BCL-XL/FITC-HRK interaction. 8 The text states that all stapled peptides, including HRKM7-S1, had Ki values close to the FP assay detection limit (Ki<1 nM) against BCL-XL and BCL-2. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9LGU\9LGU_metadata.json point structures/9LGU/9lgu_protein.pdb structures/9LGU/9lgu_pocket.pdb structures/9LGU/9lgu_ligand.pdb structures/9LGU/9lgu_ligand.cif structures/9LGU/9lgu_complex.pdb structures/9LGU/9lgu_complex.cif 9LGV extended PKMYT1 human protein kinase domain Na compound 11 "[""A1EJV""]" 2 Ki Ki = = 1.06 nM 1.06 [] unit_conversion 8.97469413473523 success True biochemical_inhibition PKMYT1 Morrison Ki assay using the PKMYT1 ADP-Glo assay for a tight binder. 5 Table 2 reports compound 11: PKMYT1 Morrison Ki 1.06 nM; its footnote defines the Morrison Ki assay as a PKMYT1 ADP-Glo assay. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9LGV\9LGV_metadata.json point structures/9LGV/9lgv_protein.pdb structures/9LGV/9lgv_pocket.pdb structures/9LGV/9lgv_ligand.pdb structures/9LGV/9lgv_ligand.cif structures/9LGV/9lgv_complex.pdb structures/9LGV/9lgv_complex.cif 9LI8 extended BCL-XL human C-terminal 22 residues removed; C-terminal 6xHis tag Na HRK BH3 peptide "[""CHAIN:B""]" 2 Ki Ki = = 1.8 nM 1.8 [] unit_conversion 8.744727494896694 success True biochemical_inhibition Competitive fluorescence-polarization inhibition assay of the BCL-XL/FITC-HRK interaction. 7 Figure 4A lists the BCL-XL Ki for HRK-WT as 1.8 nM; the Figure 4 caption identifies B–D as competitive FP assays. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9LI8\9LI8_metadata.json point structures/9LI8/9li8_protein.pdb structures/9LI8/9li8_pocket.pdb structures/9LI8/9li8_ligand.pdb structures/9LI8/9li8_ligand.cif structures/9LI8/9li8_complex.pdb structures/9LI8/9li8_complex.cif 9LID extended PKMYT1 human protein kinase domain Na compound 27 "[""A1EJX""]" 1 Ki Ki = = 24.2 nM 24.2 [] unit_conversion 7.616184634019569 success True biochemical_inhibition PKMYT1 Morrison Ki assay using the PKMYT1 ADP-Glo assay for a tight binder. 6 Table 3 reports compound 27: PKMYT1 Morrison Ki 24.2 nM. The table footnote defines this as a PKMYT1 ADP-Glo-based Morrison Ki assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9LID\9LID_metadata.json point structures/9LID/9lid_protein.pdb structures/9LID/9lid_pocket.pdb structures/9LID/9lid_ligand.pdb structures/9LID/9lid_ligand.cif structures/9LID/9lid_complex.pdb structures/9LID/9lid_complex.cif 9LN2 classic alpaca butyrophilin 3 (VpBTN3) alpaca (Vicugna pacos) VpBTN3 B30.2 delta-C domain, residues 323-513 Na DMASPP "[""DST""]" 1 Kd Kd = = 44.7 µM 44700.0 [] unit_conversion 4.349692476868063 success True direct_binding ITC binding of DMASPP to VpBTN3 B30.2 ΔC domain. 5 Figure 4A prints K_D = 44.7 µM for DMASPP–VpBTN3 B30.2 ΔC; the text identifies the DMASPP complex as PDB 9LN2. auto_single_measurement only accepted activity measurement [1] 1 structures\9LN2\9LN2_metadata.json point structures/9LN2/9ln2_protein.pdb structures/9LN2/9ln2_pocket.pdb structures/9LN2/9ln2_ligand.sdf structures/9LN2/9ln2_ligand.pdb structures/9LN2/9ln2_ligand.cif structures/9LN2/9ln2_complex.pdb structures/9LN2/9ln2_complex.cif 9LNR classic ERK2 human full-length ERK2 with His-tag Na SKLB-D18 "[""A1EKR""]" 2 Kd Kd = = 209.8 nM 209.8 [] unit_conversion 6.678194516142461 success True direct_binding Isothermal titration calorimetry of SKLB-D18 with ERK2. 4 Fig. 2d visibly reports for “D18 - ERK2”: Kd = 209.8 nM; the text identifies this as ITC binding affinity. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9LNR\9LNR_metadata.json point structures/9LNR/9lnr_protein.pdb structures/9LNR/9lnr_pocket.pdb structures/9LNR/9lnr_ligand.sdf structures/9LNR/9lnr_ligand.pdb structures/9LNR/9lnr_ligand.cif structures/9LNR/9lnr_complex.pdb structures/9LNR/9lnr_complex.cif 9LNZ classic alpaca butyrophilin 3 (VpBTN3) alpaca (Vicugna pacos) VpBTN3 B30.2 delta-C domain, residues 323-513 Na HMBPP-08 "[""99C""]" 1 Kd Kd = = 55.7 nM 55.7 [] unit_conversion 7.2541448048262716 success True direct_binding ITC binding of HMBPP-08 to VpBTN3 B30.2 ΔC domain. 3 Figure 2A prints K_D = 55.7 nM for HMBPP-08–VpBTN3 B30.2 ΔC; the text identifies this HMBPP-08 complex as PDB 9LNZ. auto_single_measurement only accepted activity measurement [1] 1 structures\9LNZ\9LNZ_metadata.json point structures/9LNZ/9lnz_protein.pdb structures/9LNZ/9lnz_pocket.pdb structures/9LNZ/9lnz_ligand.sdf structures/9LNZ/9lnz_ligand.pdb structures/9LNZ/9lnz_ligand.cif structures/9LNZ/9lnz_complex.pdb structures/9LNZ/9lnz_complex.cif 9LOH classic HIF-2alpha-ARNT heterodimer mouse HIF-2alpha residues 3-361 and ARNT residues 82-464 with GFP tag Na SD-10 "[""A1EJ8""]" 1 Kd Kd = = 664 nM 664.0 [] unit_conversion 6.1778319206319825 success True direct_binding Microscale thermophoresis (MST) binding assay with mouse HIF-2α-ARNT bHLH-PAS-A-PAS-B protein carrying GFP tag; Figure 2 reports the apparent dissociation constant. 6 Figure 2 caption identifies the HIF-2α-ARNT-SD-10 co-crystal as PDB ID 9LOH and states that apparent dissociation constants were determined by MST; panel A prints “SD-10: 664.23 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9LOH\9LOH_metadata.json point structures/9LOH/9loh_protein.pdb structures/9LOH/9loh_pocket.pdb structures/9LOH/9loh_ligand.sdf structures/9LOH/9loh_ligand.pdb structures/9LOH/9loh_ligand.cif structures/9LOH/9loh_complex.pdb structures/9LOH/9loh_complex.cif 9LRO classic PDE4D Na PDE4D residues 86-413 Na T3700; SCH900776 (MK-8776) "[""A1ELI""]" 1 IC50 IC50 = = 725 ± 12 nM 725.0 [] unit_conversion 6.139661993429007 success True biochemical_inhibition In vitro PDE4 inhibition assay; T3700 is reported in Table 1 as the hit/PDE4D inhibitor. 8 Table 1 reports T3700 PDE4 inhibition IC50 = 725.0 ± 12.0 nM; the paper identifies the PDE4D–T3700 cocrystal as PDB 9LRO. auto_single_measurement only accepted activity measurement [1] 1 structures\9LRO\9LRO_metadata.json point structures/9LRO/9lro_protein.pdb structures/9LRO/9lro_pocket.pdb structures/9LRO/9lro_ligand.sdf structures/9LRO/9lro_ligand.pdb structures/9LRO/9lro_ligand.cif structures/9LRO/9lro_complex.pdb structures/9LRO/9lro_complex.cif 9LRP classic PDE4D Na PDE4D residues 86-413 Na 13c; 4-((7-Amino-6-bromo-3-(1-methyl-1H-pyrazol-4-yl)pyrazolo[1,5-a]pyrimidin-5-yl)amino)-N-hydroxybutanamide "[""A1ELB""]" 1 IC50 IC50 = = 2.7 ± 0.2 nM 2.7 [] unit_conversion 8.568636235841012 success True biochemical_inhibition In vitro PDE4 inhibition assay; Table 1 reports 13c potency and Table 2 specifies PDE4D2 (86–413). 8 Table 1 reports 13c PDE4 inhibition IC50 = 2.7 ± 0.2 nM; the paper identifies the PDE4D–13c cocrystal as PDB 9LRP. auto_single_measurement only accepted activity measurement [1] 1 structures\9LRP\9LRP_metadata.json point structures/9LRP/9lrp_protein.pdb structures/9LRP/9lrp_pocket.pdb structures/9LRP/9lrp_ligand.sdf structures/9LRP/9lrp_ligand.pdb structures/9LRP/9lrp_ligand.cif structures/9LRP/9lrp_complex.pdb structures/9LRP/9lrp_complex.cif 9LRR classic Na+-translocating NADH-ubiquinone oxidoreductase Vibrio cholerae NqrB-G141A mutant Na+-NQR complex NqrB-G141A korormicin A "[""IQT""]" 1 Kd Kd = = 450 ± 130 × 10^-8 M 4500.0 [] unit_conversion 5.346787486224656 success True direct_binding Isothermal titration calorimetry at 20 °C; korormicin A titrated into purified mutant Na+-NQR. 21 Table 1 reports Kd = 450 ± 130 × 10^-8 M for NqrB-G141A; the methods and results identify this as korormicin A binding measured by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\9LRR\9LRR_metadata.json point structures/9LRR/9lrr_protein.pdb structures/9LRR/9lrr_pocket.pdb structures/9LRR/9lrr_ligand.sdf structures/9LRR/9lrr_ligand.pdb structures/9LRR/9lrr_ligand.cif structures/9LRR/9lrr_complex.pdb structures/9LRR/9lrr_complex.cif 9LT5 classic dehydrogenase/isomerase FabX Helicobacter pylori Na Na compound 1 (P61G11) "[""A1ELE""]" 2 Kd Kd = = 1.7 µM 1700.0 [] unit_conversion 5.769551078621726 success True direct_binding Isothermal titration calorimetry (ITC) evaluation of compound 1 binding to FabX. 2 Figure 1E prints Kd = 1.7 µM for binding of compound 1 to FabX by ITC. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9LT5\9LT5_metadata.json point structures/9LT5/9lt5_protein.pdb structures/9LT5/9lt5_pocket.pdb structures/9LT5/9lt5_ligand.sdf structures/9LT5/9lt5_ligand.pdb structures/9LT5/9lt5_ligand.cif structures/9LT5/9lt5_complex.pdb structures/9LT5/9lt5_complex.cif 9LT8 classic dehydrogenase/isomerase FabX Helicobacter pylori Na Na compound 35 "[""A1ELH""]" 1 IC50 IC50 = = 0.218 ± 0.011 µM 218.0 [] unit_conversion 6.661543506395395 success True biochemical_inhibition FabX–FabI-coupled enzymatic inhibition assay. 6 Table 2 prints an IC50 of 0.218 ± 0.011 µM for compound 35 against HpFabX. auto_single_measurement only accepted activity measurement [1] 1 structures\9LT8\9LT8_metadata.json point structures/9LT8/9lt8_protein.pdb structures/9LT8/9lt8_pocket.pdb structures/9LT8/9lt8_ligand.sdf structures/9LT8/9lt8_ligand.pdb structures/9LT8/9lt8_ligand.cif structures/9LT8/9lt8_complex.pdb structures/9LT8/9lt8_complex.cif 9LTA classic MAPK7 (ERK5) human residues 48-395 with His and GST tags Na SKLB-D18 "[""A1EKR""]" 2 Kd Kd = = 468.2 nM 468.2 [] unit_conversion 6.329568590639394 success True direct_binding Isothermal titration calorimetry of SKLB-D18 with ERK5. 4 Fig. 2d visibly reports for “D18 - ERK5”: Kd = 468.2 nM; the text identifies this as ITC binding affinity. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9LTA\9LTA_metadata.json point structures/9LTA/9lta_protein.pdb structures/9LTA/9lta_pocket.pdb structures/9LTA/9lta_ligand.sdf structures/9LTA/9lta_ligand.pdb structures/9LTA/9lta_ligand.cif structures/9LTA/9lta_complex.pdb structures/9LTA/9lta_complex.cif 9LVR classic SARS-CoV-2 3CL protease SARS-CoV-2 residues 1-306 with an N-terminal 10-histidine tag followed by a thrombin cleavage site; cloned into pET15b Na compound 1 "[""A1L7P""]" 1 IC50 IC50 = = 143 nM 143.0 [] unit_conversion 6.844663962534938 success True biochemical_inhibition SARS-CoV-2 3CLpro inhibition assay (Table 1). 2 Table 1 reports compound 1 with a SARS-CoV-2 3CLpro IC50 of 143 nM; Figure 1 identifies compound 1 as the 3CLpro complex with PDB 9LVR. auto_single_measurement only accepted activity measurement [1] 1 structures\9LVR\9LVR_metadata.json point structures/9LVR/9lvr_protein.pdb structures/9LVR/9lvr_pocket.pdb structures/9LVR/9lvr_ligand.sdf structures/9LVR/9lvr_ligand.pdb structures/9LVR/9lvr_ligand.cif structures/9LVR/9lvr_complex.pdb structures/9LVR/9lvr_complex.cif 9LWQ classic PI3Kalpha Na Na WT UCL-TRO-1938 (1938) "[""QIH""]" 1 Kd Kd = = 253 ± 69 µM 253000.0 [] unit_conversion 3.5968794788241825 success True direct_binding Surface plasmon resonance (SPR) binding analysis. 3 SPR analysis validated binding of 1938 to PI3Kα WT with K_D = 253 ± 69 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9LWQ\9LWQ_metadata.json point structures/9LWQ/9lwq_protein.pdb structures/9LWQ/9lwq_pocket.pdb structures/9LWQ/9lwq_ligand.sdf structures/9LWQ/9lwq_ligand.pdb structures/9LWQ/9lwq_ligand.cif structures/9LWQ/9lwq_complex.pdb structures/9LWQ/9lwq_complex.cif 9LWW classic dehydrogenase/isomerase FabX Helicobacter pylori Na Na compound 47 "[""A1EMD""]" 1 IC50 IC50 = = 0.128 ± 0.002 µM 128.0 [] unit_conversion 6.892790030352131 success True biochemical_inhibition FabX–FabI-coupled enzymatic inhibition assay. 7 Table 3 prints an IC50 of 0.128 ± 0.002 µM for compound 47 against HpFabX. auto_single_measurement only accepted activity measurement [1] 1 structures\9LWW\9LWW_metadata.json point structures/9LWW/9lww_protein.pdb structures/9LWW/9lww_pocket.pdb structures/9LWW/9lww_ligand.sdf structures/9LWW/9lww_ligand.pdb structures/9LWW/9lww_ligand.cif structures/9LWW/9lww_complex.pdb structures/9LWW/9lww_complex.cif 9M3M classic FSP1 (hFSP1) human nonmyristoylated hFSP1, residues 10-373 Na FSEN1 "[""A1EMU""]" 1 IC50 IC50 = = 34 nM 34.0 [] unit_conversion 7.468521082957745 success True biochemical_inhibition Purified hFSP1 enzymatic activity assay with CoQ1 and NADPH; FSEN1 concentration series; IC50 determined at 1 h. 3 “hFSP1 was highly sensitive to FSEN1, with an IC50 value of 34 nM (Fig. 2C).” auto_single_measurement only accepted activity measurement [1] 1 structures\9M3M\9M3M_metadata.json point structures/9M3M/9m3m_protein.pdb structures/9M3M/9m3m_pocket.pdb structures/9M3M/9m3m_ligand.sdf structures/9M3M/9m3m_ligand.pdb structures/9M3M/9m3m_ligand.cif structures/9M3M/9m3m_complex.pdb structures/9M3M/9m3m_complex.cif 9M3O extended human pyruvate dehydrogenase kinase isoform 1 human Na Na compound 8 "[""A1EMR""]" 1 IC50 IC50 = = 0.13 µM 130.0 [] unit_conversion 6.886056647693163 success True biochemical_inhibition Iterative HTS; PDHK1 IC50 listed in Table 1. 2 Table 1 lists compound 8, iterative HTS, PDHK1 IC50 0.13 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9M3O\9M3O_metadata.json point structures/9M3O/9m3o_protein.pdb structures/9M3O/9m3o_pocket.pdb structures/9M3O/9m3o_ligand.pdb structures/9M3O/9m3o_ligand.cif structures/9M3O/9m3o_complex.pdb structures/9M3O/9m3o_complex.cif 9M6P extended PKMYT1 Na Na Na compound 2 "[""A1EMX""]" 1 IC50 IC50 = = 19 nM 19.0 [] unit_conversion 7.721246399047171 success True direct_binding Biochemical binding-affinity HTRF assay; Figure 1 identifies this as the PKMYT1 binding-affinity IC50 for compound 2. 3 “Compound 2 … PKMYT1 binding affinity: 19 nM”; Fig. 1 caption states biochemical binding affinity was measured by HTRF assay and denotes IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\9M6P\9M6P_metadata.json point structures/9M6P/9m6p_ligand.cif structures/9M6P/9m6p_complex.cif 9MAS classic VIM-2 metallo-beta-lactamase Na Na Na Compound 3 "[""A1ENM""]" 1 IC50 IC50 = = 6.48 μM 6480.0 [] unit_conversion 5.188424994129407 success True biochemical_inhibition Purified-protein MBL/SBL inhibition assay; Table 1 reports IC50 values against VIM-2. 6 Table 1 lists compound 3 with VIM-2 IC50 = 6.48 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MAS\9MAS_metadata.json point structures/9MAS/9mas_protein.pdb structures/9MAS/9mas_pocket.pdb structures/9MAS/9mas_ligand.sdf structures/9MAS/9mas_ligand.pdb structures/9MAS/9mas_ligand.cif structures/9MAS/9mas_complex.pdb structures/9MAS/9mas_complex.cif 9MB4 classic NDM-1 metallo-beta-lactamase Na Na Na Compound 14 "[""A1ENL""]" 1 IC50 IC50 = = 1.10 μM 1100.0 [] unit_conversion 5.958607314841775 success True biochemical_inhibition Purified-protein MBL/SBL inhibition assay; Table 1 reports IC50 values against NDM-1. 6 Table 1 lists compound 14 with NDM-1 IC50 = 1.10 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MB4\9MB4_metadata.json point structures/9MB4/9mb4_protein.pdb structures/9MB4/9mb4_pocket.pdb structures/9MB4/9mb4_ligand.sdf structures/9MB4/9mb4_ligand.pdb structures/9MB4/9mb4_ligand.cif structures/9MB4/9mb4_complex.pdb structures/9MB4/9mb4_complex.cif 9MG0 classic mRNA cap (guanine-N7) methyltransferase Abd1 Kluyveromyces lactis KlAbd1Delta137, residues 138-426 Na SAH "[""SAH""]" 1 IC50 IC50 = = 12.3 ± 4.1 µM 12300.0 [] unit_conversion 4.910094888560602 success True biochemical_inhibition In vitro inhibition of KlAbd1-catalyzed GpppA methylation by SAH. 6 “SAH inhibits KlAbd1 with an IC50 of 12.3 ± 4.1 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9MG0\9MG0_metadata.json point structures/9MG0/9mg0_protein.pdb structures/9MG0/9mg0_pocket.pdb structures/9MG0/9mg0_ligand.sdf structures/9MG0/9mg0_ligand.pdb structures/9MG0/9mg0_ligand.cif structures/9MG0/9mg0_complex.pdb structures/9MG0/9mg0_complex.cif 9MG2 classic mRNA cap (guanine-N7) methyltransferase Abd1 Kluyveromyces lactis KlAbd1Delta137, residues 138-426 Na sinefungin "[""SFG""]" 1 IC50 IC50 = = 52.1 ± 13.1 nM 52.1 [] unit_conversion 7.283162276700476 success True biochemical_inhibition In vitro inhibition of KlAbd1-catalyzed GpppA methylation by sinefungin (SFG). 6 “SFG inhibits KlAbd1 in vitro with an apparent IC50 of 52.1 ± 13.1 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9MG2\9MG2_metadata.json point structures/9MG2/9mg2_protein.pdb structures/9MG2/9mg2_pocket.pdb structures/9MG2/9mg2_ligand.sdf structures/9MG2/9mg2_ligand.pdb structures/9MG2/9mg2_ligand.cif structures/9MG2/9mg2_complex.pdb structures/9MG2/9mg2_complex.cif 9MGM classic PRMT5:MEP50 Na Na Na compound 24 "[""A1BLL""]" 1 Ki Ki = = 0.04 µM 40.0 [] unit_conversion 7.3979400086720375 success True direct_binding Fluorescence-anisotropy peptide-displacement biochemical assay, with MTA. 3 Table 2 reports compound 24 PRMT5 biochemical Ki,app = 0.04 µM with MTA; footnote identifies TAMRA-peptide fluorescence anisotropy. auto_single_measurement only accepted activity measurement [1] 1 structures\9MGM\9MGM_metadata.json point structures/9MGM/9mgm_protein.pdb structures/9MGM/9mgm_pocket.pdb structures/9MGM/9mgm_ligand.sdf structures/9MGM/9mgm_ligand.pdb structures/9MGM/9mgm_ligand.cif structures/9MGM/9mgm_complex.pdb structures/9MGM/9mgm_complex.cif 9MGN extended PRMT5:MEP50 Na Na Na compound 41 "[""A1BLK""]" 1 Ki Ki = = 0.13 µM 130.0 [] unit_conversion 6.886056647693163 success True direct_binding Fluorescence-anisotropy peptide-displacement biochemical assay, with MTA. 4 Table 3 reports compound 41 PRMT5 biochemical Ki,app = 0.13 µM with MTA; Figure 5 maps compound 41 to PDB 9MGN. auto_single_measurement only accepted activity measurement [1] 1 structures\9MGN\9MGN_metadata.json point structures/9MGN/9mgn_protein.pdb structures/9MGN/9mgn_pocket.pdb structures/9MGN/9mgn_ligand.pdb structures/9MGN/9mgn_ligand.cif structures/9MGN/9mgn_complex.pdb structures/9MGN/9mgn_complex.cif 9MGP classic PRMT5:MEP50 Na Na Na compound 46a "[""A1BLI""]" 1 Ki Ki = = 0.2 µM 200.0 [] unit_conversion 6.698970004336019 success True direct_binding Fluorescence-anisotropy peptide-displacement biochemical assay, with MTA. 6 Table 4 reports compound 46a PRMT5 biochemical Ki,app = 0.2 µM with MTA; Figure 7 maps 46a to PDB 9MGP. auto_single_measurement only accepted activity measurement [1] 1 structures\9MGP\9MGP_metadata.json point structures/9MGP/9mgp_protein.pdb structures/9MGP/9mgp_pocket.pdb structures/9MGP/9mgp_ligand.sdf structures/9MGP/9mgp_ligand.pdb structures/9MGP/9mgp_ligand.cif structures/9MGP/9mgp_complex.pdb structures/9MGP/9mgp_complex.cif 9MGR classic PRMT5:MEP50 Na Na Na compound 51 "[""A1BLF""]" 1 Ki Ki < < 0.004 µM 4.0 [] unit_conversion 8.397940008672037 success True direct_binding Fluorescence-anisotropy peptide-displacement biochemical assay, with MTA. 7 Table 6 reports compound 51 biochemical Ki,app < 0.004 µM with MTA; Figure 10 maps compound 51 to PDB 9MGR. auto_single_measurement only accepted activity measurement [1] 1 structures\9MGR\9MGR_metadata.json point structures/9MGR/9mgr_protein.pdb structures/9MGR/9mgr_pocket.pdb structures/9MGR/9mgr_ligand.sdf structures/9MGR/9mgr_ligand.pdb structures/9MGR/9mgr_ligand.cif structures/9MGR/9mgr_complex.pdb structures/9MGR/9mgr_complex.cif 9MHU classic TarGH Staphylococcus aureus Na Na targocil-II "[""A1AV9""]" 1 Kd Kd = = 8.2 ± 3.2 µM 8200.0 [] unit_conversion 5.086186147616283 success True direct_binding Microscale thermophoresis measurement of targocil-II binding to ATP-gamma-S-bound S. aureus TarGH. 6 Fig. 3c reports targocil-II binding to ATPγS-bound TarGH: Kd = 8.2 ± 3.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MHU\9MHU_metadata.json point structures/9MHU/9mhu_protein.pdb structures/9MHU/9mhu_pocket.pdb structures/9MHU/9mhu_ligand.sdf structures/9MHU/9mhu_ligand.pdb structures/9MHU/9mhu_ligand.cif structures/9MHU/9mhu_complex.pdb structures/9MHU/9mhu_complex.cif 9MHZ classic TarGH Staphylococcus aureus Na Na targocil-II "[""A1AV9""]" 1 Kd Kd = = 8.2 ± 3.2 µM 8200.0 [] unit_conversion 5.086186147616283 success True direct_binding Microscale thermophoresis measurement of targocil-II binding to ATP-gamma-S-bound S. aureus TarGH. 6 Fig. 3c reports targocil-II binding to ATPγS-bound TarGH: Kd = 8.2 ± 3.2 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MHZ\9MHZ_metadata.json point structures/9MHZ/9mhz_protein.pdb structures/9MHZ/9mhz_pocket.pdb structures/9MHZ/9mhz_ligand.sdf structures/9MHZ/9mhz_ligand.pdb structures/9MHZ/9mhz_ligand.cif structures/9MHZ/9mhz_complex.pdb structures/9MHZ/9mhz_complex.cif 9MIK extended Mouse importin alpha 2 (IMPalpha2) bound to the Gallid alphaherpesvirus-1 large tegument protein UL36 NLS peptide mouse; Gallid alphaherpesvirus-1 mIMPalpha2DeltaIBB, residues 72-498, lacking the N-terminal importin beta-binding (IBB) domain; His-tagged and TEV-cleavable Na Gallid alphaherpesvirus-1 bipartite NLS peptide (residues 296-319; GaAHV-1 NLS) "[""CHAIN:C""]" 1 Kd Kd = = 593.45 ± 26.26 nM 593.45 [] unit_conversion 6.226615865822845 success True direct_binding Fluorescence-polarization saturation binding assay using FITC-labelled GaAHV-1 NLS peptide and importin proteins; mean ± SE from three separate experiments. 6 Figure 2b explicitly reports IMPα2: 593.45 ± 26.26; its caption identifies these as Kd values from FP binding experiments with FITC-labelled peptide and importin proteins. auto_single_measurement only accepted activity measurement [1] 1 structures\9MIK\9MIK_metadata.json point structures/9MIK/9mik_protein.pdb structures/9MIK/9mik_pocket.pdb structures/9MIK/9mik_ligand.pdb structures/9MIK/9mik_ligand.cif structures/9MIK/9mik_complex.pdb structures/9MIK/9mik_complex.cif 9MIN extended designed mini-TCR mimic (mini-TCRm 1.1) Na mini-TCRm 1.1 complexed with refolded NY-ESO-1-HLA-A*02 and AD01 anti-beta2M nanobody Na NY-ESO-1_157-165 (C9V) peptide "[""CHAIN:C"", ""CHAIN:H""]" 1 Kd Kd = = 9.5 nM 9.5 [] unit_conversion 8.022276394711152 success True direct_binding Surface plasmon resonance: mini-TCRm 1.1 analyte with immobilized NY-ESO-1–HLA-A*02; MART-1–HLA-A*02 control had no detectable affinity. 2 “Surface plasmon resonance (SPR) analysis revealed a Kd of 9.5 nM for NY-ESO-1 HLA-A*02 but no detectable affinity for MART-1 HLA-A*02.” auto_single_measurement only accepted activity measurement [1] 1 structures\9MIN\9MIN_metadata.json point structures/9MIN/9min_protein.pdb structures/9MIN/9min_pocket.pdb structures/9MIN/9min_ligand.pdb structures/9MIN/9min_ligand.cif structures/9MIN/9min_complex.pdb structures/9MIN/9min_complex.cif 9MLM classic dihydrofolate reductase (DHFR; WbDHFR) Wuchereria bancrofti Na Na TSD10 (OED) "[""OED""]" 2 Ki Ki = = 17 µM 17000.0 [] unit_conversion 4.769551078621726 success True biochemical_inhibition WbDHFR inhibition assay; Ki calculated using the Cheung-Prusoff equation. 2 Table 1 lists TSD10 IC50 as 241 ± 99 µM and Ki as 17 µM for WbDHFR. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9MLM\9MLM_metadata.json point structures/9MLM/9mlm_protein.pdb structures/9MLM/9mlm_pocket.pdb structures/9MLM/9mlm_ligand.sdf structures/9MLM/9mlm_ligand.pdb structures/9MLM/9mlm_ligand.cif structures/9MLM/9mlm_complex.pdb structures/9MLM/9mlm_complex.cif 9MLT classic dihydrofolate reductase (DHFR; WbDHFR) Wuchereria bancrofti Na Na TSD25 (OFD) "[""OFD""]" 2 Ki Ki = = 6 µM 6000.0 [] unit_conversion 5.221848749616356 success True biochemical_inhibition WbDHFR inhibition assay; Ki calculated using the Cheung-Prusoff equation. 2 Table 1 lists TSD25 IC50 as 82 ± 20 µM and Ki as 6 µM for WbDHFR. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9MLT\9MLT_metadata.json point structures/9MLT/9mlt_protein.pdb structures/9MLT/9mlt_pocket.pdb structures/9MLT/9mlt_ligand.sdf structures/9MLT/9mlt_ligand.pdb structures/9MLT/9mlt_ligand.cif structures/9MLT/9mlt_complex.pdb structures/9MLT/9mlt_complex.cif 9MRE classic PRMT5:MEP50 Na Na Na AM-9747 "[""A1BQW""]" 1 IC50 IC50 = = 9.5 nM 9.5 [] unit_conversion 8.022276394711152 success True biochemical_inhibition MTase-Glo PRMT5:MEP50 biochemical assay with 5 μM MTA (MTA+). 9 Table 3 reports AM-9747 MTase-Glo IC50 of 9.5 nM in the MTA+ condition; its footnote defines MTA+ as 5 μM MTA. auto_single_measurement only accepted activity measurement [1] 1 structures\9MRE\9MRE_metadata.json point structures/9MRE/9mre_protein.pdb structures/9MRE/9mre_pocket.pdb structures/9MRE/9mre_ligand.sdf structures/9MRE/9mre_ligand.pdb structures/9MRE/9mre_ligand.cif structures/9MRE/9mre_complex.pdb structures/9MRE/9mre_complex.cif 9MSX classic Candida albicans Hsp90 Candida albicans CaHsp90-NTD (residues 7-218) Na TAS116 "[""A1BPC""]" 1 Kd Kd = = 35 nM 35.0 [] unit_conversion 7.455931955649724 success True direct_binding Fluorescence-polarization binding assay of TAS116 with CaHsp90; the graphical abstract explicitly prints CaHsp90 K_D = 35 nM. 2 Graphical abstract explicitly states “CaHsp90 K_D = 35 nM” for TAS116; the paper describes a fluorescence-polarization assay to measure ligand affinities to CaHsp90 and HsHsp90. auto_single_measurement only accepted activity measurement [1] 1 structures\9MSX\9MSX_metadata.json point structures/9MSX/9msx_protein.pdb structures/9MSX/9msx_pocket.pdb structures/9MSX/9msx_ligand.sdf structures/9MSX/9msx_ligand.pdb structures/9MSX/9msx_ligand.cif structures/9MSX/9msx_complex.pdb structures/9MSX/9msx_complex.cif 9MT9 classic Candida albicans Hsp90 Candida albicans CaHsp90-NTD (residues 7-218) Na BTB10184 "[""A8K""]" 1 Kd Kd = = 45.6 ± 17 µM 45600.0 [] unit_conversion 4.341035157335565 success True direct_binding Fluorescence-polarization binding assay of fragment BTB10184 with CaHsp90. 21 Table 1, “Summary of Fragment Screen Hits,” reports BTB10184 CaHsp90 K_D = 45.6 ± 17 µM. The Results text identifies BTB10184 as a CaHsp90-bound fragment and reports its CaHsp90 binding affinity as 45.6 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MT9\9MT9_metadata.json point structures/9MT9/9mt9_protein.pdb structures/9MT9/9mt9_pocket.pdb structures/9MT9/9mt9_ligand.sdf structures/9MT9/9mt9_ligand.pdb structures/9MT9/9mt9_ligand.cif structures/9MT9/9mt9_complex.pdb structures/9MT9/9mt9_complex.cif 9MUM classic GluN1/GluN2A Na GluN1/GluN2A ligand-binding domain heterodimer Na Compound 11 "[""A1BRB""]" 1 Ki Ki = = 8 nM 8.0 [] unit_conversion 8.096910013008056 success True direct_binding In vitro radioligand-binding competition assay in rat hippocampal membranes. 5 The text states that Compound 11 had a Ki in hippocampal neuron membranes of 8 nM; the in vitro tracer-binding Ki determination is described on page 10. auto_single_measurement only accepted activity measurement [1] 1 structures\9MUM\9MUM_metadata.json point structures/9MUM/9mum_protein.pdb structures/9MUM/9mum_pocket.pdb structures/9MUM/9mum_ligand.sdf structures/9MUM/9mum_ligand.pdb structures/9MUM/9mum_ligand.cif structures/9MUM/9mum_complex.pdb structures/9MUM/9mum_complex.cif 9MVM classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na AVI-3318 "[""A1BTM""]" 1 IC50 IC50 = = 4.6 µM 4600.0 [] unit_conversion 5.337242168318426 success True biochemical_inhibition Purified MPro activity assay; AVI-3318 shown in the early structure-based optimization series. 2 Figure 1B visibly reports AVI-3318, IC50 = 4.6 µM; the text identifies its MPro crystal structure as PDB 9MVM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MVM\9MVM_metadata.json point structures/9MVM/9mvm_protein.pdb structures/9MVM/9mvm_pocket.pdb structures/9MVM/9mvm_ligand.sdf structures/9MVM/9mvm_ligand.pdb structures/9MVM/9mvm_ligand.cif structures/9MVM/9mvm_complex.pdb structures/9MVM/9mvm_complex.cif 9MWN classic human endothelial nitric oxide synthase human heme domain Na HH044 "[""H44""]" 1 Ki Ki = = 6735 nM 6735.0 [] unit_conversion 5.171662399940995 success True biochemical_inhibition NO hemoglobin-capture enzyme inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists HH044 human eNOS Ki = 6735 nM; page 7 states biochemical enzymatic assays used the NO hemoglobin capture assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWN\9MWN_metadata.json point structures/9MWN/9mwn_protein.pdb structures/9MWN/9mwn_pocket.pdb structures/9MWN/9mwn_ligand.sdf structures/9MWN/9mwn_ligand.pdb structures/9MWN/9mwn_ligand.cif structures/9MWN/9mwn_complex.pdb structures/9MWN/9mwn_complex.cif 9MWO classic human endothelial nitric oxide synthase human heme domain Na compound 1 "[""A1BTY""]" 1 Ki Ki = = 3712 nM 3712.0 [] unit_conversion 5.430392032453176 success True biochemical_inhibition NO hemoglobin-capture enzyme inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists 1·3HCl human eNOS Ki = 3712 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWO\9MWO_metadata.json point structures/9MWO/9mwo_protein.pdb structures/9MWO/9mwo_pocket.pdb structures/9MWO/9mwo_ligand.sdf structures/9MWO/9mwo_ligand.pdb structures/9MWO/9mwo_ligand.cif structures/9MWO/9mwo_complex.pdb structures/9MWO/9mwo_complex.cif 9MWP classic human endothelial nitric oxide synthase human heme domain Na compound 2 "[""A1BT1""]" 1 Ki Ki = = 4287 nM 4287.0 [] unit_conversion 5.367846516489367 success True biochemical_inhibition NO hemoglobin-capture enzyme inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists 2·3HCl human eNOS Ki = 4287 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWP\9MWP_metadata.json point structures/9MWP/9mwp_protein.pdb structures/9MWP/9mwp_pocket.pdb structures/9MWP/9mwp_ligand.sdf structures/9MWP/9mwp_ligand.pdb structures/9MWP/9mwp_ligand.cif structures/9MWP/9mwp_complex.pdb structures/9MWP/9mwp_complex.cif 9MWQ classic human endothelial nitric oxide synthase human heme domain Na compound 3; N-(4-(2-((3-(isoxazole-3-carboximidamido)benzyl)amino)ethyl)phenyl)isoxazole-3-carboximidamide "[""A1BT0""]" 1 Ki Ki = = 8524 nM 8524.0 [] unit_conversion 5.0693565589578355 success True biochemical_inhibition NO hemoglobin-capture enzymatic inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists compound 3·3HCl: human eNOS Ki = 8524 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWQ\9MWQ_metadata.json point structures/9MWQ/9mwq_protein.pdb structures/9MWQ/9mwq_pocket.pdb structures/9MWQ/9mwq_ligand.sdf structures/9MWQ/9mwq_ligand.pdb structures/9MWQ/9mwq_ligand.cif structures/9MWQ/9mwq_complex.pdb structures/9MWQ/9mwq_complex.cif 9MWR classic human endothelial nitric oxide synthase human heme domain Na compound 5; N-(4-(2-((3-(thiazole-2-carboximidamido)benzyl)amino)ethyl)phenyl)thiazole-2-carboximidamide "[""A1BTV""]" 1 Ki Ki = = 42283 nM 42283.0 [] unit_conversion 4.373834206860721 success True biochemical_inhibition NO hemoglobin-capture enzymatic inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists compound 5·3HCl: human eNOS Ki = 42,283 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWR\9MWR_metadata.json point structures/9MWR/9mwr_protein.pdb structures/9MWR/9mwr_pocket.pdb structures/9MWR/9mwr_ligand.sdf structures/9MWR/9mwr_ligand.pdb structures/9MWR/9mwr_ligand.cif structures/9MWR/9mwr_complex.pdb structures/9MWR/9mwr_complex.cif 9MWS classic human endothelial nitric oxide synthase human heme domain Na compound 7; N-(3-(2-((3-(thiazole-5-carboximidamido)benzyl)amino)ethyl)phenyl)thiazole-5-carboximidamide "[""A1BTX""]" 1 Ki Ki = = 8008 nM 8008.0 [] unit_conversion 5.096475935528738 success True biochemical_inhibition NO hemoglobin-capture enzymatic inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists compound 7·3HCl: human eNOS Ki = 8008 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWS\9MWS_metadata.json point structures/9MWS/9mws_protein.pdb structures/9MWS/9mws_pocket.pdb structures/9MWS/9mws_ligand.sdf structures/9MWS/9mws_ligand.pdb structures/9MWS/9mws_ligand.cif structures/9MWS/9mws_complex.pdb structures/9MWS/9mws_complex.cif 9MWT classic human endothelial nitric oxide synthase human heme domain Na compound 8; N-(3-(((2-(3-(aminomethyl)-[1,1'-biphenyl]-4-yl)ethyl)amino)methyl)phenyl)furan-2-carboximidamide "[""A1BT6""]" 1 Ki Ki = = 3642 nM 3642.0 [] unit_conversion 5.438660058541099 success True biochemical_inhibition NO hemoglobin-capture enzymatic inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists compound 8·3HCl: human eNOS Ki = 3642 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWT\9MWT_metadata.json point structures/9MWT/9mwt_protein.pdb structures/9MWT/9mwt_pocket.pdb structures/9MWT/9mwt_ligand.sdf structures/9MWT/9mwt_ligand.pdb structures/9MWT/9mwt_ligand.cif structures/9MWT/9mwt_complex.pdb structures/9MWT/9mwt_complex.cif 9MWU classic human endothelial nitric oxide synthase human heme domain Na compound 9; N-(3-(((2-(3-(aminomethyl)-[1,1'-biphenyl]-4-yl)ethyl)amino)methyl)phenyl)furan-2-carboximidamide "[""A1BT2""]" 1 Ki Ki = = 9612 nM 9612.0 [] unit_conversion 5.017186237868137 success True biochemical_inhibition NO hemoglobin-capture enzymatic inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists compound 9·3HCl: human eNOS Ki = 9612 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWU\9MWU_metadata.json point structures/9MWU/9mwu_protein.pdb structures/9MWU/9mwu_pocket.pdb structures/9MWU/9mwu_ligand.sdf structures/9MWU/9mwu_ligand.pdb structures/9MWU/9mwu_ligand.cif structures/9MWU/9mwu_complex.pdb structures/9MWU/9mwu_complex.cif 9MWV classic human endothelial nitric oxide synthase human heme domain Na compound 10; N-(3-(((2-(3-(aminomethyl)-[1,1'-biphenyl]-4-yl)ethyl)amino)methyl)phenyl)thiophene-2-carboximidamide "[""A1BT9""]" 1 Ki Ki = = 3215 nM 3215.0 [] unit_conversion 5.492819022739759 success True biochemical_inhibition NO hemoglobin-capture enzymatic inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists compound 10·3HCl: human eNOS Ki = 3215 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWV\9MWV_metadata.json point structures/9MWV/9mwv_protein.pdb structures/9MWV/9mwv_pocket.pdb structures/9MWV/9mwv_ligand.sdf structures/9MWV/9mwv_ligand.pdb structures/9MWV/9mwv_ligand.cif structures/9MWV/9mwv_complex.pdb structures/9MWV/9mwv_complex.cif 9MWW classic human endothelial nitric oxide synthase human heme domain Na compound 11; N-(3-(((2-(3-(aminomethyl)-[1,1'-biphenyl]-4-yl)ethyl)amino)methyl)phenyl)thiazole-5-carboximidamide "[""A1BTW""]" 1 Ki Ki = = 35044 nM 35044.0 [] unit_conversion 4.455386328337828 success True biochemical_inhibition NO hemoglobin-capture enzymatic inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists compound 11·3HCl: human eNOS Ki = 35,044 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWW\9MWW_metadata.json point structures/9MWW/9mww_protein.pdb structures/9MWW/9mww_pocket.pdb structures/9MWW/9mww_ligand.sdf structures/9MWW/9mww_ligand.pdb structures/9MWW/9mww_ligand.cif structures/9MWW/9mww_complex.pdb structures/9MWW/9mww_complex.cif 9MWX classic human endothelial nitric oxide synthase human heme domain Na compound 6; N-(4-(2-((3-(thiazole-5-carboximidamido)benzyl)amino)ethyl)phenyl)thiazole-5-carboximidamide "[""A1BT5""]" 1 Ki Ki = = 7023 nM 7023.0 [] unit_conversion 5.153477331583713 success True biochemical_inhibition NO hemoglobin-capture enzymatic inhibition assay; Table 1 reports human eNOS Ki. 6 Table 1 lists compound 6·3HCl: human eNOS Ki = 7023 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9MWX\9MWX_metadata.json point structures/9MWX/9mwx_protein.pdb structures/9MWX/9mwx_pocket.pdb structures/9MWX/9mwx_ligand.sdf structures/9MWX/9mwx_ligand.pdb structures/9MWX/9mwx_ligand.cif structures/9MWX/9mwx_complex.pdb structures/9MWX/9mwx_complex.cif 9MZ1 classic human endothelial nitric oxide synthase human heme domain Na compound 7; 7-(3-aminomethyl)phenyl-6-fluoro-4-methylquinolin-2-amine "[""A1BUD""]" 1 Ki Ki = = 51177 nM 51177.0 [] unit_conversion 4.290925176081356 success True biochemical_inhibition In vitro inhibition against purified heNOS; Ki calculated from IC50 dose-response data. 38 Table 1 reports compound 7 Ki = 51177 nM for heNOS; table note states assays used purified NOS isoforms and Ki values were calculated from IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\9MZ1\9MZ1_metadata.json point structures/9MZ1/9mz1_protein.pdb structures/9MZ1/9mz1_pocket.pdb structures/9MZ1/9mz1_ligand.sdf structures/9MZ1/9mz1_ligand.pdb structures/9MZ1/9mz1_ligand.cif structures/9MZ1/9mz1_complex.pdb structures/9MZ1/9mz1_complex.cif 9MZ2 classic human endothelial nitric oxide synthase human heme domain Na compound 10; 2-(2-amino-6-fluoro-4-methylquinolin-7-yl)-5-(aminomethyl)phenol "[""A1BUF""]" 1 Ki Ki = = 13257 nM 13257.0 [] unit_conversion 4.877554743718044 success True biochemical_inhibition In vitro inhibition against purified heNOS; Ki calculated from IC50 dose-response data. 38 Table 1 reports compound 10 Ki = 13257 nM for heNOS; table note states assays used purified NOS isoforms and Ki values were calculated from IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\9MZ2\9MZ2_metadata.json point structures/9MZ2/9mz2_protein.pdb structures/9MZ2/9mz2_pocket.pdb structures/9MZ2/9mz2_ligand.sdf structures/9MZ2/9mz2_ligand.pdb structures/9MZ2/9mz2_ligand.cif structures/9MZ2/9mz2_complex.pdb structures/9MZ2/9mz2_complex.cif 9MZ3 classic human endothelial nitric oxide synthase human heme domain Na compound 11; 2-(2-amino-6-fluoro-4-methylquinolin-7-yl)-5-(2-aminoethyl)phenol "[""A1BUH""]" 1 Ki Ki = = 17954 nM 17954.0 [] unit_conversion 4.745838779152574 success True biochemical_inhibition In vitro inhibition against purified heNOS; Ki calculated from IC50 dose-response data. 38 Table 1 reports compound 11 Ki = 17954 nM for heNOS; table note states assays used purified NOS isoforms and Ki values were calculated from IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\9MZ3\9MZ3_metadata.json point structures/9MZ3/9mz3_protein.pdb structures/9MZ3/9mz3_pocket.pdb structures/9MZ3/9mz3_ligand.sdf structures/9MZ3/9mz3_ligand.pdb structures/9MZ3/9mz3_ligand.cif structures/9MZ3/9mz3_complex.pdb structures/9MZ3/9mz3_complex.cif 9MZ4 classic human endothelial nitric oxide synthase human heme domain Na compound 15; 7-(3-(aminomethyl)-4-(cyclopropylmethoxy)phenyl)-6-fluoro-4-methylquinolin-2-amine "[""A1BU3""]" 1 Ki Ki = = 11503 nM 11503.0 [] unit_conversion 4.939188880208654 success True biochemical_inhibition In vitro inhibition against purified heNOS; Ki calculated from IC50 dose-response data. 38 Table 1 reports compound 15 Ki = 11503 nM for heNOS; table note states assays used purified NOS isoforms and Ki values were calculated from IC50 values. auto_single_measurement only accepted activity measurement [1] 1 structures\9MZ4\9MZ4_metadata.json point structures/9MZ4/9mz4_protein.pdb structures/9MZ4/9mz4_pocket.pdb structures/9MZ4/9mz4_ligand.sdf structures/9MZ4/9mz4_ligand.pdb structures/9MZ4/9mz4_ligand.cif structures/9MZ4/9mz4_complex.pdb structures/9MZ4/9mz4_complex.cif 9MZX classic RIPK1 human RIPK1 kinase domain Na Compound 1 "[""A1BU4""]" 1 IC50 IC50 = = 54 nM 54.0 [] unit_conversion 7.267606240177031 success True biochemical_inhibition RIPK1 ADP-glo enzyme assay. 1 “compound 1 had promising potency in a RIPK1 ADP-glo enzyme assay (IC50 = 54 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\9MZX\9MZX_metadata.json point structures/9MZX/9mzx_protein.pdb structures/9MZX/9mzx_pocket.pdb structures/9MZX/9mzx_ligand.sdf structures/9MZX/9mzx_ligand.pdb structures/9MZX/9mzx_ligand.cif structures/9MZX/9mzx_complex.pdb structures/9MZX/9mzx_complex.cif 9MZZ classic RIPK1 Na RIPK1 kinase domain Na Compound 36 "[""A1BU5""]" 1 IC50 IC50 = = 29 nM 29.0 [] unit_conversion 7.537602002101044 success True biochemical_inhibition RIPK1 IC50 reported in Table 3. 5 Table 3 lists Compound 36 with “RIPK1 IC50 (nM)” of 29. auto_single_measurement only accepted activity measurement [1] 1 structures\9MZZ\9MZZ_metadata.json point structures/9MZZ/9mzz_protein.pdb structures/9MZZ/9mzz_pocket.pdb structures/9MZZ/9mzz_ligand.sdf structures/9MZZ/9mzz_ligand.pdb structures/9MZZ/9mzz_ligand.cif structures/9MZZ/9mzz_complex.pdb structures/9MZZ/9mzz_complex.cif 9N1R extended XIAP-BIR3 Na BIR3 domain, residues 249-354 Na A171 (ALP2 series) "[""A1BUO""]" 1 pKd Kd = = 6.1 unitless 794.3282347242822 [] p_metric_transform 6.1 success True direct_binding SPR binding to XIAP-BIR3; heat-map value reported as pKd. 3 Fig. 1b lists A171 (ALP2) against XIAP-BIR3 as pKd 6.1; caption states SPR affinity data are plotted as pKd. auto_single_measurement only accepted activity measurement [1] 1 structures\9N1R\9N1R_metadata.json point structures/9N1R/9n1r_protein.pdb structures/9N1R/9n1r_pocket.pdb structures/9N1R/9n1r_ligand.pdb structures/9N1R/9n1r_ligand.cif structures/9N1R/9n1r_complex.pdb structures/9N1R/9n1r_complex.cif 9N21 classic XIAP-BIR3 Na BIR3 domain, residues 249-354 Na A250 (ALP1 series) "[""A1BVB""]" 1 pKd Kd = = 5.8 unitless 1584.893192461114 [] p_metric_transform 5.8 success True direct_binding SPR binding to XIAP-BIR3; heat-map value reported as pKd. 3 Fig. 1b lists A250 (ALP1) against XIAP-BIR3 as pKd 5.8; caption states SPR affinity data are plotted as pKd. auto_single_measurement only accepted activity measurement [1] 1 structures\9N21\9N21_metadata.json point structures/9N21/9n21_protein.pdb structures/9N21/9n21_pocket.pdb structures/9N21/9n21_ligand.sdf structures/9N21/9n21_ligand.pdb structures/9N21/9n21_ligand.cif structures/9N21/9n21_complex.pdb structures/9N21/9n21_complex.cif 9N23 classic cIAP1-BIR3 Na BIR3 domain, residues 260-352 Na A273 (XB2 series) "[""A1BVC""]" 1 pKd Kd = = 6.7 unitless 199.52623149688787 [] p_metric_transform 6.7 success True direct_binding SPR binding to cIAP1-BIR3; heat-map value reported as pKd. 3 Fig. 1b lists A273 (XB2) against cIAP1-BIR3 as pKd 6.7; caption states SPR affinity data are plotted as pKd. auto_single_measurement only accepted activity measurement [1] 1 structures\9N23\9N23_metadata.json point structures/9N23/9n23_protein.pdb structures/9N23/9n23_pocket.pdb structures/9N23/9n23_ligand.sdf structures/9N23/9n23_ligand.pdb structures/9N23/9n23_ligand.cif structures/9N23/9n23_complex.pdb structures/9N23/9n23_complex.cif 9N36 classic Respiratory syncytial virus polymerase (RSV L+P complex) human respiratory syncytial virus Full-length RSV L+P complex Na Compound 22 "[""A1BVR""]" 2 Kd Kd = = 0.47 μM 470.0 [] unit_conversion 6.327902142064282 success True direct_binding SPR binding assay using full-length RSV L+P; 1:1 Langmuir fit. 4 Figure 1 caption reports SPR for RSV L+P binding to 22 with KD = 0.47 μM. auto_metric_priority unique highest-priority metric family: Kd [2] 4 structures\9N36\9N36_metadata.json point structures/9N36/9n36_protein.pdb structures/9N36/9n36_pocket.pdb structures/9N36/9n36_ligand.sdf structures/9N36/9n36_ligand.pdb structures/9N36/9n36_ligand.cif structures/9N36/9n36_complex.pdb structures/9N36/9n36_complex.cif 9N3R classic PRMT5:MEP50 Na Na Na TNG462 "[""A1BV0""]" 1 Ki Ki <= <= 300 fM 0.0003 [] unit_conversion 12.522878745280337 success True biochemical_inhibition Enzyme activity-recovery assay; the MTA-containing condition was used to estimate potency because the initial apparent enzymatic rate approached background. 9 “the Ki of TNG462 can only be estimated to be ≤300 femtomolar”; the preceding text states this estimate follows addition of MTA. auto_single_measurement only accepted activity measurement [1] 1 structures\9N3R\9N3R_metadata.json point structures/9N3R/9n3r_protein.pdb structures/9N3R/9n3r_pocket.pdb structures/9N3R/9n3r_ligand.sdf structures/9N3R/9n3r_ligand.pdb structures/9N3R/9n3r_ligand.cif structures/9N3R/9n3r_complex.pdb structures/9N3R/9n3r_complex.cif 9N48 classic PAK1 Na Na Na compound C1 "[""A1BV1""]" 1 Ki Ki = = 19 nM 19.0 [] unit_conversion 7.721246399047171 success True biochemical_inhibition Table 1, Summary of Results; PAK1 R1 as computational input, target structure C1. 5 Table 1 visibly reports Ki (nM) = 19 for target structure C1 under PAK1. auto_single_measurement only accepted activity measurement [1] 1 structures\9N48\9N48_metadata.json point structures/9N48/9n48_protein.pdb structures/9N48/9n48_pocket.pdb structures/9N48/9n48_ligand.sdf structures/9N48/9n48_ligand.pdb structures/9N48/9n48_ligand.cif structures/9N48/9n48_complex.pdb structures/9N48/9n48_complex.cif 9N6P classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Mature Mpro D48Y/DeltaP168 D48Y and DeltaP168 Ensitrelvir (ESV) "[""7YY""]" 1 Kd Kd = = 0.028 ± 0.007 µM 28.0 [] unit_conversion 7.552841968657781 success True direct_binding ITC at 28 °C; 30 µM protein in cell, inhibitor at 10× protein concentration in syringe. 4 Table 1 reports 1/Ka = 0.028 ± 0.007 µM for MProD48Y/ΔP168 + ESV; the table is titled Kd and thermodynamic parameters of inhibitor binding. auto_single_measurement only accepted activity measurement [1] 1 structures\9N6P\9N6P_metadata.json point structures/9N6P/9n6p_protein.pdb structures/9N6P/9n6p_pocket.pdb structures/9N6P/9n6p_ligand.sdf structures/9N6P/9n6p_ligand.pdb structures/9N6P/9n6p_ligand.cif structures/9N6P/9n6p_complex.pdb structures/9N6P/9n6p_complex.cif 9N6R classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Mature wild-type Mpro Wild type Ensitrelvir (ESV) "[""7YY""]" 1 Kd Kd = = 0.006 ± 0.003 µM 6.0 [] unit_conversion 8.221848749616356 success True direct_binding ITC at 28 °C; 30 µM protein in cell, inhibitor at 10× protein concentration in syringe. 4 Table 1 reports 1/Ka = 0.006 ± 0.003 µM for MProWT + ESV; the table is titled Kd and thermodynamic parameters of inhibitor binding. auto_single_measurement only accepted activity measurement [1] 1 structures\9N6R\9N6R_metadata.json point structures/9N6R/9n6r_protein.pdb structures/9N6R/9n6r_pocket.pdb structures/9N6R/9n6r_ligand.sdf structures/9N6R/9n6r_ligand.pdb structures/9N6R/9n6r_ligand.cif structures/9N6R/9n6r_complex.pdb structures/9N6R/9n6r_complex.cif 9N7R classic HPK1 Na Na Na compound C6; N-(3,5-difluoro-4-{[3-(trifluoromethyl)-1H-pyrrolo[2,3-b]pyridin-4-yl]oxy}phenyl)-N'-[3-(morpholin-4-yl)propyl]urea "[""A1BWC""]" 1 Ki Ki = = 17.31 nM 17.31 [] unit_conversion 7.7617029321246065 success True biochemical_inhibition Table 1, Summary of Results; HPK1 R2 as computational input, target structure C6. 5 Table 1 visibly reports Ki (nM) = 17.31 for target structure C6 under HPK1. auto_single_measurement only accepted activity measurement [1] 1 structures\9N7R\9N7R_metadata.json point structures/9N7R/9n7r_protein.pdb structures/9N7R/9n7r_pocket.pdb structures/9N7R/9n7r_ligand.sdf structures/9N7R/9n7r_ligand.pdb structures/9N7R/9n7r_ligand.cif structures/9N7R/9n7r_complex.pdb structures/9N7R/9n7r_complex.cif 9N88 classic IRE1 human IRE1.KR (G547-L977) with VHL/EloB/EloC (VHL E55-D213, EloB M1-Q118, EloC M17-C112) Na G6374 "[""A1BWF""]" 1 IC50 IC50 = = 492 ± 21 nM 492.0 [] unit_conversion 6.308034897232639 success True direct_binding Fluorescence-polarization displacement of FAM-labelled HIF-1α peptide from VCB by G6374 with saturating IRE1.KR (2.4 µM), measuring the ternary-complex-dependent displacement. 5 With IRE1 present, G6374 displaced the VCB-bound HIF-1α peptide with IC50 = 492 ± 21 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9N88\9N88_metadata.json point structures/9N88/9n88_protein.pdb structures/9N88/9n88_pocket.pdb structures/9N88/9n88_ligand.sdf structures/9N88/9n88_ligand.pdb structures/9N88/9n88_ligand.cif structures/9N88/9n88_complex.pdb structures/9N88/9n88_complex.cif 9N9L classic RORgamma t Na RORgamma t LBD, residues 265-507 Na compound 7g "[""A1BW2""]" 1 Kd Kd = = 0.28 ± 0.11 nM 0.28 [] unit_conversion 9.55284196865778 success True direct_binding ThermoFluor binding assay (TF); Table 2. 4 Table 2 reports compound 7g hRORγt TF Kd = 0.28 ± 0.11 nM. The paper identifies the 9N9L cocrystal as RORγt LBD bound to 7g. auto_single_measurement only accepted activity measurement [1] 1 structures\9N9L\9N9L_metadata.json point structures/9N9L/9n9l_protein.pdb structures/9N9L/9n9l_pocket.pdb structures/9N9L/9n9l_ligand.sdf structures/9N9L/9n9l_ligand.pdb structures/9N9L/9n9l_ligand.cif structures/9N9L/9n9l_complex.pdb structures/9N9L/9n9l_complex.cif 9N9X classic HPK1 Na Na Na compound C5 "[""A1BWL""]" 1 Ki Ki = = 0.014 nM 0.014 [] unit_conversion 10.853871964321762 success True biochemical_inhibition Table 1, Summary of Results; HPK1 R2 as computational input, target structure C5. 5 Table 1 visibly reports Ki (nM) = 0.014 for target structure C5 under HPK1. auto_single_measurement only accepted activity measurement [1] 1 structures\9N9X\9N9X_metadata.json point structures/9N9X/9n9x_protein.pdb structures/9N9X/9n9x_pocket.pdb structures/9N9X/9n9x_ligand.sdf structures/9N9X/9n9x_ligand.pdb structures/9N9X/9n9x_ligand.cif structures/9N9X/9n9x_complex.pdb structures/9N9X/9n9x_complex.cif 9NA2 classic IRAK4 Na Na Na compound 9 "[""A1BW0""]" 1 IC50 IC50 = = 1.8 nM 1.8 [] unit_conversion 8.744727494896694 success True biochemical_inhibition IRAK4 biochemical inhibition assay (500 μM ATP). 3 Figure 2A profiles compound 9 and prints “IRAK4 IC50 (nM) 1.8”; its footnote identifies biochemical IRAK4 inhibition at 500 μM ATP. Figure 2B caption maps compound 9 to PDB 9NA2. auto_single_measurement only accepted activity measurement [1] 1 structures\9NA2\9NA2_metadata.json point structures/9NA2/9na2_protein.pdb structures/9NA2/9na2_pocket.pdb structures/9NA2/9na2_ligand.sdf structures/9NA2/9na2_ligand.pdb structures/9NA2/9na2_ligand.cif structures/9NA2/9na2_complex.pdb structures/9NA2/9na2_complex.cif 9NA3 extended IRAK4 Na Na Na compound 15 "[""A1BWX""]" 1 IC50 IC50 = = 0.8 nM 0.8 [] unit_conversion 9.096910013008056 success True biochemical_inhibition IRAK4 biochemical inhibition assay (500 μM ATP). 4 Table 2 lists compound 15 with “IRAK4 IC50 / monocyte TNFα EC50 (nM)” of “0.8 / 9.8”; the Table 2 footnote identifies biochemical IRAK4 inhibition at 500 μM ATP. Figure 4 caption maps compound 15 to PDB 9NA3. auto_single_measurement only accepted activity measurement [1] 1 structures\9NA3\9NA3_metadata.json point structures/9NA3/9na3_pocket.pdb structures/9NA3/9na3_ligand.sdf structures/9NA3/9na3_ligand.pdb structures/9NA3/9na3_ligand.cif structures/9NA3/9na3_complex.cif 9NA4 classic IRAK4 Na Na Na compound 18 "[""A1BW1""]" 1 IC50 IC50 = = 0.6 nM 0.6 [] unit_conversion 9.221848749616356 success True biochemical_inhibition IRAK4 biochemical inhibition assay (500 μM ATP). 4 Table 2 lists compound 18 with “IRAK4 IC50 / monocyte TNFα EC50 (nM)” of “0.6 / 5.9”; the Table 2 footnote identifies biochemical IRAK4 inhibition at 500 μM ATP. Figure 4 caption maps compound 18 to PDB 9NA4. auto_single_measurement only accepted activity measurement [1] 1 structures\9NA4\9NA4_metadata.json point structures/9NA4/9na4_protein.pdb structures/9NA4/9na4_pocket.pdb structures/9NA4/9na4_ligand.sdf structures/9NA4/9na4_ligand.pdb structures/9NA4/9na4_ligand.cif structures/9NA4/9na4_complex.pdb structures/9NA4/9na4_complex.cif 9NA5 classic IRAK4 Na Na Na compound 24 "[""A1BWY""]" 1 IC50 IC50 = = 0.9 nM 0.9 [] unit_conversion 9.045757490560675 success True biochemical_inhibition IRAK4 biochemical inhibition assay (500 μM ATP). 4 Table 2 lists compound 24 with “IRAK4 IC50 / monocyte TNFα EC50 (nM)” of “0.9 / 11”; the Table 2 footnote identifies biochemical IRAK4 inhibition at 500 μM ATP. Figure 4 caption maps compound 24 to PDB 9NA5. auto_single_measurement only accepted activity measurement [1] 1 structures\9NA5\9NA5_metadata.json point structures/9NA5/9na5_protein.pdb structures/9NA5/9na5_pocket.pdb structures/9NA5/9na5_ligand.sdf structures/9NA5/9na5_ligand.pdb structures/9NA5/9na5_ligand.cif structures/9NA5/9na5_complex.pdb structures/9NA5/9na5_complex.cif 9NAC classic HPK1 Na Na Na compound C4 "[""A1BWM""]" 1 Ki Ki = = 2.3 nM 2.3 [] unit_conversion 8.638272163982407 success True biochemical_inhibition Table 1, Summary of Results; HPK1 R2 as computational input, target structure C4. 5 Table 1 visibly reports Ki (nM) = 2.3 for target structure C4 under HPK1. auto_single_measurement only accepted activity measurement [1] 1 structures\9NAC\9NAC_metadata.json point structures/9NAC/9nac_protein.pdb structures/9NAC/9nac_pocket.pdb structures/9NAC/9nac_ligand.sdf structures/9NAC/9nac_ligand.pdb structures/9NAC/9nac_ligand.cif structures/9NAC/9nac_complex.pdb structures/9NAC/9nac_complex.cif 9NBX classic PAK1 Na Na Na compound C2 "[""A1BW5""]" 1 Ki Ki = = 36 nM 36.0 [] unit_conversion 7.443697499232712 success True biochemical_inhibition Table 1, Summary of Results; PAK1 R1 as computational input, target structure C2. 5 Table 1 visibly reports Ki (nM) = 36 for target structure C2 under PAK1. auto_single_measurement only accepted activity measurement [1] 1 structures\9NBX\9NBX_metadata.json point structures/9NBX/9nbx_protein.pdb structures/9NBX/9nbx_pocket.pdb structures/9NBX/9nbx_ligand.sdf structures/9NBX/9nbx_ligand.pdb structures/9NBX/9nbx_ligand.cif structures/9NBX/9nbx_complex.pdb structures/9NBX/9nbx_complex.cif 9NC2 classic HPK1 Na Na Na compound C3 "[""F97""]" 1 Ki Ki = = 10 nM 10.0 [] unit_conversion 8.0 success True biochemical_inhibition Table 1, Summary of Results; HPK1 R2 as computational input, target structure C3. 5 Table 1 visibly reports Ki (nM) = 10 for target structure C3 under HPK1. auto_single_measurement only accepted activity measurement [1] 1 structures\9NC2\9NC2_metadata.json point structures/9NC2/9nc2_protein.pdb structures/9NC2/9nc2_pocket.pdb structures/9NC2/9nc2_ligand.sdf structures/9NC2/9nc2_ligand.pdb structures/9NC2/9nc2_ligand.cif structures/9NC2/9nc2_complex.pdb structures/9NC2/9nc2_complex.cif 9NCU classic NitrOFF1 Staphylococcus carnosus EGFP-NreA fusion biosensor with NreA inserted into the EGFP beta-bulge; N-terminal linker residues 145-148 and C-terminal linker residues 297-300 E142V; Y238C; N146D; I283V; A228T; M249L; F290Y; S147N; A150V; N196D; L181P; K356E; K208E; N348D; N320S nitrate (NO3-) "[""NO3""]" 1 Kd Kd = = 8.9 ± 0.6 μM 8900.0 [] unit_conversion 5.050609993355087 success True direct_binding Purified NitrOFF fluorescence titration with sodium nitrate; reported as a 16,000-fold enhanced nitrate affinity relative to the NreA-EGFP parent. 7 “NitrOFF boasts a 16,000-fold enhanced affinity for nitrate (Kd = 8.9 ± 0.6 μM).” auto_single_measurement only accepted activity measurement [1] 1 structures\9NCU\9NCU_metadata.json point structures/9NCU/9ncu_protein.pdb structures/9NCU/9ncu_pocket.pdb structures/9NCU/9ncu_ligand.sdf structures/9NCU/9ncu_ligand.pdb structures/9NCU/9ncu_ligand.cif structures/9NCU/9ncu_complex.pdb structures/9NCU/9ncu_complex.cif 9NE0 classic HSV-1 helicase-primase (HP) complex (UL5, UL52, UL8) herpes simplex virus type 1 (HSV-1) Na Na pritelivir (PTV) "[""A1BXB""]" 1 IC50 IC50 = = 11.1 nM 11.1 [] unit_conversion 7.954677021213342 success True biochemical_inhibition Purified HSV-1 HP DNA-unwinding assay. 2 The purified complex was inhibited by PTV with an IC50 of 11.1 nM. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\9NE0\9NE0_metadata.json point structures/9NE0/9ne0_protein.pdb structures/9NE0/9ne0_pocket.pdb structures/9NE0/9ne0_ligand.sdf structures/9NE0/9ne0_ligand.pdb structures/9NE0/9ne0_ligand.cif structures/9NE0/9ne0_complex.pdb structures/9NE0/9ne0_complex.cif 9NEE classic HSV-1 helicase-primase (HP) complex (UL5, UL52, UL8) herpes simplex virus type 1 (HSV-1) Na Na pritelivir (PTV) "[""A1BXB""]" 1 IC50 IC50 = = 11.1 nM 11.1 [] unit_conversion 7.954677021213342 success True biochemical_inhibition Purified HSV-1 HP DNA-unwinding assay. 2 The purified complex was inhibited by PTV with an IC50 of 11.1 nM. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\9NEE\9NEE_metadata.json point structures/9NEE/9nee_protein.pdb structures/9NEE/9nee_pocket.pdb structures/9NEE/9nee_ligand.sdf structures/9NEE/9nee_ligand.pdb structures/9NEE/9nee_ligand.cif structures/9NEE/9nee_complex.pdb structures/9NEE/9nee_complex.cif 9NIA classic CqsR periplasmic domain (CqsRp) Vibrio cholerae O1 El Tor Residues 44-260; expressed as His6-SUMO-CqsR44-260 and processed to cleaved CqsR44-260 Na ethanolamine "[""ETA""]" 1 Kd Kd = = 1.3 ± 0.1 µM 1300.0 [] unit_conversion 5.886056647693163 success True direct_binding Microscale thermophoresis (MST) using purified CqsRp; ethanolamine titration. 8 Fig. 3A visibly reports “Kd = 1.3 ± 0.1 µM” for CqsRp binding to ethanolamine; the Results text identifies this as MST direct binding. auto_single_measurement only accepted activity measurement [1] 1 structures\9NIA\9NIA_metadata.json point structures/9NIA/9nia_protein.pdb structures/9NIA/9nia_pocket.pdb structures/9NIA/9nia_ligand.sdf structures/9NIA/9nia_ligand.pdb structures/9NIA/9nia_ligand.cif structures/9NIA/9nia_complex.pdb structures/9NIA/9nia_complex.cif 9NIH extended HLA-DRB1*04:01 human Soluble HLA-DRB1*04:01 alpha and beta extracellular domains; beta-chain N-terminal CLIP fusion and C-terminal Fos/Jun leucine-zipper tags, with tags removed before crystallization Na TNC1014,1016cit peptide "[""CHAIN:C""]" 1 IC50 IC50 = = 1.14 μM 1140.0 [] unit_conversion 5.943095148663527 success True biochemical_inhibition Fluorescence-polarization peptide competition assay measuring inhibition of fluorescent HA-peptide binding to HLA-DRB1*04:01 by TNC1014,1016cit. 11 Figure 7A tabulates the IC50 for DRB1*04:01 as 1.14 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9NIH\9NIH_metadata.json point structures/9NIH/9nih_protein.pdb structures/9NIH/9nih_pocket.pdb structures/9NIH/9nih_ligand.pdb structures/9NIH/9nih_ligand.cif structures/9NIH/9nih_complex.pdb structures/9NIH/9nih_complex.cif 9NIQ classic Candida albicans trehalose-6-phosphate synthase (CaTps1) Candida albicans 6xHis-tagged CaTps1; modeled residues 6-239 and 246-437 with a C-terminal alpha-helix Na 4456 "[""A1BYI""]" 1 Kd Kd = = 7.1 ± 1.6 µM 7100.0 [] unit_conversion 5.1487416512809245 success True direct_binding Microscale thermophoresis binding assay with recombinant 6xHis-CaTps1. 5 “MST experiments revealed that the binding affinities of 4456dh with recombinant 6xHis-CaTps1 … are 7.1 µM … respectively.” auto_single_measurement only accepted activity measurement [1] 1 structures\9NIQ\9NIQ_metadata.json point structures/9NIQ/9niq_protein.pdb structures/9NIQ/9niq_pocket.pdb structures/9NIQ/9niq_ligand.sdf structures/9NIQ/9niq_ligand.pdb structures/9NIQ/9niq_ligand.cif structures/9NIQ/9niq_complex.pdb structures/9NIQ/9niq_complex.cif 9NIT classic CqsR periplasmic domain (CqsRp) Vibrio cholerae O1 El Tor Residues 44-260; expressed as His6-SUMO-CqsR44-260 and processed to cleaved CqsR44-260 Na L-alaninol "[""2A1""]" 1 Kd Kd = = 3.2 ± 0.1 µM 3200.0 [] unit_conversion 5.494850021680094 success True direct_binding Microscale thermophoresis (MST) using purified CqsRp; L-alaninol titration. 8 Fig. 3B visibly reports “Kd = 3.2 ± 0.1 µM” for CqsRp binding to L-alaninol; the Results text identifies this as MST direct binding. auto_single_measurement only accepted activity measurement [1] 1 structures\9NIT\9NIT_metadata.json point structures/9NIT/9nit_protein.pdb structures/9NIT/9nit_pocket.pdb structures/9NIT/9nit_ligand.sdf structures/9NIT/9nit_ligand.pdb structures/9NIT/9nit_ligand.cif structures/9NIT/9nit_complex.pdb structures/9NIT/9nit_complex.cif 9NIV classic CqsR periplasmic domain (CqsRp) Vibrio cholerae O1 El Tor Residues 44-260; expressed as His6-SUMO-CqsR44-260 and processed to cleaved CqsR44-260 Na serinol "[""SEL""]" 1 Kd Kd = = 15.9 ± 0.8 µM 15900.0 [] unit_conversion 4.798602875679548 success True direct_binding Microscale thermophoresis (MST) using purified CqsRp; serinol titration. 8 Fig. 3C visibly reports “Kd = 15.9 ± 0.8 µM” for CqsRp binding to serinol; the Results text identifies this as MST direct binding. auto_single_measurement only accepted activity measurement [1] 1 structures\9NIV\9NIV_metadata.json point structures/9NIV/9niv_protein.pdb structures/9NIV/9niv_pocket.pdb structures/9NIV/9niv_ligand.sdf structures/9NIV/9niv_ligand.pdb structures/9NIV/9niv_ligand.cif structures/9NIV/9niv_complex.pdb structures/9NIV/9niv_complex.cif 9NK8 extended SAM complex (Sam50, Sam35, Sam37) Thermothelomyces thermophilus Monomeric SAM complex, Sam50:Sam35:Sam37 in 1:1:1 stoichiometry Na darobactin A "[""CHAIN:D""]" 1 Kd Kd = = 296 ± 31 nM 296.0 [] unit_conversion 6.528708288941061 success True direct_binding Microscale thermophoresis dose-response binding assay of purified T. thermophilus SAM complex to darobactin A; six independent experiments. 5 Fig. 2E prints “Darobactin A Kd = 296 ± 31 nM”; the caption identifies this as SAM-complex binding darobactin A and states n = 6. auto_single_measurement only accepted activity measurement [1] 1 structures\9NK8\9NK8_metadata.json point structures/9NK8/9nk8_protein.pdb structures/9NK8/9nk8_pocket.pdb structures/9NK8/9nk8_ligand.pdb structures/9NK8/9nk8_ligand.cif structures/9NK8/9nk8_complex.pdb structures/9NK8/9nk8_complex.cif 9NK9 extended Nb127 nanobody Na Na Na 127-tag peptide "[""CHAIN:B""]" 1 Kd Kd = = 14 nM 14.0 [] unit_conversion 7.853871964321762 success True direct_binding Surface plasmon resonance (SPR) assay measuring binding between Nb127 and 127-tag peptide. 5 “We experimentally confirmed high affinity binding (K_D = 14 nM) between Nb127 and the 127-tag peptide using surface plasmon resonance (SPR) assays.” auto_single_measurement only accepted activity measurement [1] 1 structures\9NK9\9NK9_metadata.json point structures/9NK9/9nk9_protein.pdb structures/9NK9/9nk9_pocket.pdb structures/9NK9/9nk9_ligand.pdb structures/9NK9/9nk9_ligand.cif structures/9NK9/9nk9_complex.pdb structures/9NK9/9nk9_complex.cif 9NLP classic HIV-1 Reverse Transcriptase Na HIV-1 RT containing 66 kDa and 51 kDa domains with a 10x-histidine tag inserted between the domains wild-type 12126065 "[""A1BYY""]" 1 IC50 IC50 = = 0.42 ± 0.57 µM 420.0 [] unit_conversion 6.376750709602099 success True biochemical_inhibition EnzChek Reverse Transcriptase Assay using purified reverse transcriptase; PicoGreen dsDNA-formation readout. 20 Table 1 reports RT (µM) for compound 12126065 as 0.42 ± 0.57; the table caption identifies this as the EnzChek Reverse Transcriptase Assay and states calculated IC50 values are reported. auto_single_measurement only accepted activity measurement [1] 1 structures\9NLP\9NLP_metadata.json point structures/9NLP/9nlp_protein.pdb structures/9NLP/9nlp_pocket.pdb structures/9NLP/9nlp_ligand.sdf structures/9NLP/9nlp_ligand.pdb structures/9NLP/9nlp_ligand.cif structures/9NLP/9nlp_complex.pdb structures/9NLP/9nlp_complex.cif 9NNA classic cholesterol 24-hydroxylase (CH24H; CYP46A1) human residues 28-494 with an N-terminal 6xHis tag Na compound 3k ([(1R,5S)-3-oxa-8-azabicyclo[3.2.1]octan-8-yl][(4R,8M)-8-(1,3-oxazol-5-yl)-6-(trifluoromethyl)imidazo[1,2-a]pyridin-3-yl]methanone) "[""A1BZE""]" 1 IC50 IC50 = = 4.5 nM 4.5 [] unit_conversion 8.346787486224656 success True biochemical_inhibition Human CH24H inhibition assay; Table 4 reports mean with 95% confidence interval. 8 Table 4 lists compound 3k CH24H IC50 = 4.5 nM (2.7–7.6); Figure 6 identifies the CH24H–3k co-crystal as PDB 9NNA. auto_single_measurement only accepted activity measurement [1] 1 structures\9NNA\9NNA_metadata.json point structures/9NNA/9nna_protein.pdb structures/9NNA/9nna_pocket.pdb structures/9NNA/9nna_ligand.sdf structures/9NNA/9nna_ligand.pdb structures/9NNA/9nna_ligand.cif structures/9NNA/9nna_complex.pdb structures/9NNA/9nna_complex.cif 9NNE classic cholesterol 24-hydroxylase (CH24H; CYP46A1) human residues 28-494 with an N-terminal 6xHis tag Na compound 2h ((morpholin-4-yl)[(4R,8M)-8-(1,3-oxazol-5-yl)-6-(trifluoromethyl)imidazo[1,2-a]pyridin-3-yl]methanone) "[""A1BZD""]" 1 IC50 IC50 = = 31 nM 31.0 [] unit_conversion 7.508638306165727 success True biochemical_inhibition Human CH24H inhibition assay; Table 2 reports mean with 95% confidence interval. 7 Table 2 lists compound 2h CH24H IC50 = 31 nM (19–53). Figure 5 identifies the CH24H–2h co-crystal as PDB 9NNE. auto_single_measurement only accepted activity measurement [1] 1 structures\9NNE\9NNE_metadata.json point structures/9NNE/9nne_protein.pdb structures/9NNE/9nne_pocket.pdb structures/9NNE/9nne_ligand.sdf structures/9NNE/9nne_ligand.pdb structures/9NNE/9nne_ligand.cif structures/9NNE/9nne_complex.pdb structures/9NNE/9nne_complex.cif 9NNI classic cholesterol 24-hydroxylase (CH24H; CYP46A1) human residues 28-494 with an N-terminal 6xHis tag Na compound 2b (cyclopropyl[(4M)-4-(1,3-oxazol-5-yl)-6-(trifluoromethyl)-1H-indol-1-yl]methanone) "[""A1BZC""]" 1 IC50 IC50 = = 5.6 nM 5.6 [] unit_conversion 8.2518119729938 success True biochemical_inhibition Human CH24H inhibition assay; Table 1 reports mean with 95% confidence interval. 6 Table 1 lists compound 2b CH24H IC50 = 5.6 nM (3.4–9.4); Figure 5 identifies the CH24H–2b co-crystal as PDB 9NNI. auto_single_measurement only accepted activity measurement [1] 1 structures\9NNI\9NNI_metadata.json point structures/9NNI/9nni_protein.pdb structures/9NNI/9nni_pocket.pdb structures/9NNI/9nni_ligand.sdf structures/9NNI/9nni_ligand.pdb structures/9NNI/9nni_ligand.cif structures/9NNI/9nni_complex.pdb structures/9NNI/9nni_complex.cif 9NTB classic HDAC2 human Na Na TNG260 "[""A1B1V""]" 1 IC50 IC50 = = 0.03 µmol/L 30.0 [] unit_conversion 7.522878745280337 success True biochemical_inhibition Purified recombinant HDAC2 Fluor de Lys deacetylase assay; 3-hour compound preincubation at room temperature. 7 Figure 2D visibly prints for HDAC2: “IC50: 0.03 µmol/L.” The Figure 2 caption identifies this as inhibition of indicated HDAC enzymes in a Fluor de Lys deacetylase assay; Methods state recombinant HDAC2 was assayed biochemically. auto_single_measurement only accepted activity measurement [1] 1 structures\9NTB\9NTB_metadata.json point structures/9NTB/9ntb_protein.pdb structures/9NTB/9ntb_pocket.pdb structures/9NTB/9ntb_ligand.sdf structures/9NTB/9ntb_ligand.pdb structures/9NTB/9ntb_ligand.cif structures/9NTB/9ntb_complex.pdb structures/9NTB/9ntb_complex.cif 9NU6 classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na compound 29 "[""A1B3B""]" 1 IC50 IC50 < < 12 nM 12.0 [] unit_conversion 7.920818753952375 success True biochemical_inhibition Biochemical Mpro inhibition discussed with the compound 29 crystal-structure analogue. 5 The text states that compound 29, with the F1 naphthyridine group, had “SARS-CoV-2 Mpro IC50 < 12 nM”; page 13 maps PDB 9NU6 to compound 29. auto_single_measurement only accepted activity measurement [1] 1 structures\9NU6\9NU6_metadata.json point structures/9NU6/9nu6_protein.pdb structures/9NU6/9nu6_pocket.pdb structures/9NU6/9nu6_ligand.sdf structures/9NU6/9nu6_ligand.pdb structures/9NU6/9nu6_ligand.cif structures/9NU6/9nu6_complex.pdb structures/9NU6/9nu6_complex.cif 9NVQ classic Nanchung-Inactive-Calmodulin Halyomorpha halys Na Na Afidopyropen (AP) "[""A1B32""]" 1 Kd Kd = = 0.017 nM 0.017 [] unit_conversion 10.769551078621726 success True direct_binding Equilibrium [3H]-AP direct binding assay; WT result. 8 Table 3 explicitly reports WT [3H]-AP Kd = 0.017 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9NVQ\9NVQ_metadata.json point structures/9NVQ/9nvq_protein.pdb structures/9NVQ/9nvq_pocket.pdb structures/9NVQ/9nvq_ligand.sdf structures/9NVQ/9nvq_ligand.pdb structures/9NVQ/9nvq_ligand.cif structures/9NVQ/9nvq_complex.pdb structures/9NVQ/9nvq_complex.cif 9NVR classic Nanchung-Inactive-Calmodulin Halyomorpha halys Na Na Afidopyropen (AP) "[""A1B32""]" 1 Kd Kd = = 0.017 nM 0.017 [] unit_conversion 10.769551078621726 success True direct_binding Equilibrium [3H]-AP direct binding assay; WT result. 8 Table 3 explicitly reports WT [3H]-AP Kd = 0.017 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9NVR\9NVR_metadata.json point structures/9NVR/9nvr_protein.pdb structures/9NVR/9nvr_pocket.pdb structures/9NVR/9nvr_ligand.sdf structures/9NVR/9nvr_ligand.pdb structures/9NVR/9nvr_ligand.cif structures/9NVR/9nvr_complex.pdb structures/9NVR/9nvr_complex.cif 9NVS classic Nanchung Halyomorpha halys Na Na Afidopyropen (AP) "[""A1B32""]" 1 Kd Kd = = 0.089 nM 0.089 [] unit_conversion 10.050609993355087 success True direct_binding [3H]-AP binding to WT Nan-only membranes; association constant fitted as an equilibrium dissociation constant. 11 Fig. 5d explicitly labels WT Nan Kd = 0.089 nM for [3H]-AP binding to Nan-only membranes. auto_single_measurement only accepted activity measurement [1] 1 structures\9NVS\9NVS_metadata.json point structures/9NVS/9nvs_protein.pdb structures/9NVS/9nvs_pocket.pdb structures/9NVS/9nvs_ligand.sdf structures/9NVS/9nvs_ligand.pdb structures/9NVS/9nvs_ligand.cif structures/9NVS/9nvs_complex.pdb structures/9NVS/9nvs_complex.cif 9NWY classic PRMT5-MEP50 complex human Heterotetrameric PRMT5:MEP50 complex; recombinant baculovirus-expressed N-terminal FLAG-tagged PRMT5 and N-terminal His-tagged MEP50 Na AM-9934 "[""A1B6Y""]" 1 IC50 IC50 = = 5 nM 5.0 [] unit_conversion 8.301029995663981 success True biochemical_inhibition PRMT5:MEP50 methyltransferase activity assay in the presence of MTA. 4 “AM-9934 also showed potent inhibition of PRMT5:MEP50 enzymatic affinity with an IC50 of 40 nM which was potentiated to 5 nM in the presence of MTA.” auto_single_measurement only accepted activity measurement [1] 1 structures\9NWY\9NWY_metadata.json point structures/9NWY/9nwy_protein.pdb structures/9NWY/9nwy_pocket.pdb structures/9NWY/9nwy_ligand.sdf structures/9NWY/9nwy_ligand.pdb structures/9NWY/9nwy_ligand.cif structures/9NWY/9nwy_complex.pdb structures/9NWY/9nwy_complex.cif 9NYQ classic CDK2/Cyclin E1 Na Na Na Cpd 3 "[""A1B7H""]" 1 IC50 IC50 = = 27 nM 27.0 [] unit_conversion 7.568636235841012 success True biochemical_inhibition CDK2 biochemical inhibition profile in Table 1. 3 Table 1 reports Cpd 3 CDK2 IC50 = 27 nM; page 4 identifies the Cpd 3/CDK2 crystal structure as PDB 9NYQ. auto_single_measurement only accepted activity measurement [1] 1 structures\9NYQ\9NYQ_metadata.json point structures/9NYQ/9nyq_protein.pdb structures/9NYQ/9nyq_pocket.pdb structures/9NYQ/9nyq_ligand.sdf structures/9NYQ/9nyq_ligand.pdb structures/9NYQ/9nyq_ligand.cif structures/9NYQ/9nyq_complex.pdb structures/9NYQ/9nyq_complex.cif 9NZK classic Yck2 Candida albicans Na Na LY364947 (LY) "[""PY1""]" 1 IC50 IC50 = = 0.17 µM 170.0 [] unit_conversion 6.769551078621726 success True biochemical_inhibition ADP-Glo kinase-enzyme inhibition assay using purified recombinant Yck2 kinase domain; Table 1 reports LY activity. 9 Table 1 lists LY with Yck2 IC50 0.17 µM. The paper maps the Yck2–LY crystal structure to PDB 9NZK (page 4). auto_single_measurement only accepted activity measurement [1] 1 structures\9NZK\9NZK_metadata.json point structures/9NZK/9nzk_protein.pdb structures/9NZK/9nzk_pocket.pdb structures/9NZK/9nzk_ligand.sdf structures/9NZK/9nzk_ligand.pdb structures/9NZK/9nzk_ligand.cif structures/9NZK/9nzk_complex.pdb structures/9NZK/9nzk_complex.cif 9O0J extended HtaA CR1 domain Corynebacterium diphtheriae HtaA residues 36-221, N-terminal CR1 domain Na hemin "[""HEM""]" 1 Kd Kd = = 1.1 ± 0.3 nM 1.1 [] unit_conversion 8.958607314841775 success True direct_binding Relative hemin-affinity determination by native ESI-MS equilibrium partitioning between CR domains; estimated Kd for HtaA CR1. 9 The paper reports the estimated hemin dissociation constant for HtaA CR1 as KD = 1.1 ± 0.3 nM. PDB 9O0J is mapped to the HtaA CR1:hemin structure on page 14. auto_single_measurement only accepted activity measurement [1] 1 structures\9O0J\9O0J_metadata.json point structures/9O0J/9o0j_protein.pdb structures/9O0J/9o0j_pocket.pdb structures/9O0J/9o0j_ligand.pdb structures/9O0J/9o0j_ligand.cif structures/9O0J/9o0j_complex.pdb structures/9O0J/9o0j_complex.cif 9O0K extended ChtA CR domain Corynebacterium diphtheriae ChtA residues 112-291, CR domain Na hemin "[""HEM""]" 1 Kd Kd = = 22.4 ± 5.3 nM 22.4 [] unit_conversion 7.649751981665837 success True direct_binding Isothermal titration calorimetry of hemin binding to WT ChtA CR domain at 25 °C; values are averages of three replicates. 8 Table 1 reports WT ChtA CR hemin KD = 22.4 ± 5.3 nM. PDB 9O0K is mapped to the ChtA CR:hemin structure on page 14. auto_single_measurement only accepted activity measurement [1] 1 structures\9O0K\9O0K_metadata.json point structures/9O0K/9o0k_protein.pdb structures/9O0K/9o0k_pocket.pdb structures/9O0K/9o0k_ligand.pdb structures/9O0K/9o0k_ligand.cif structures/9O0K/9o0k_complex.pdb structures/9O0K/9o0k_complex.cif 9O0O classic KRAS Na KRAS (1-169) wild type MRTX1133 "[""6IC""]" 1 Kd Kd = = 15 nM 15.0 [] unit_conversion 7.823908740944319 success True direct_binding ITC; Fig. 5a. 7 “KRAS(GMPPNP)-WT → MRTX1133, K_D = 15 nM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9O0O\9O0O_metadata.json point structures/9O0O/9o0o_protein.pdb structures/9O0O/9o0o_pocket.pdb structures/9O0O/9o0o_ligand.sdf structures/9O0O/9o0o_ligand.pdb structures/9O0O/9o0o_ligand.cif structures/9O0O/9o0o_complex.pdb structures/9O0O/9o0o_complex.cif 9O0Q classic MRASmut Na MRASmut (1-178) F74Y; R105H; F106Y; L109Q MRTX1133 "[""6IC""]" 1 Kd Kd = = 50 nM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding ITC; Fig. 7b. 9 “MRAS(GMPPNP)-mut → MRTX1133, K_D = 50 nM”. auto_single_measurement only accepted activity measurement [1] 1 structures\9O0Q\9O0Q_metadata.json point structures/9O0Q/9o0q_protein.pdb structures/9O0Q/9o0q_pocket.pdb structures/9O0Q/9o0q_ligand.sdf structures/9O0Q/9o0q_ligand.pdb structures/9O0Q/9o0q_ligand.cif structures/9O0Q/9o0q_complex.pdb structures/9O0Q/9o0q_complex.cif 9O2W classic NDM-1 Na Na Na compound 3 "[""A1B7Y""]" 1 IC50 IC50 = = 19.83 ± 3.04 µM 19830.0 [] unit_conversion 4.702677285794698 success True biochemical_inhibition Purified-enzyme inhibition; Table 1. 2 Table 1 reports NDM-1 IC50 = 19.83 ± 3.04 µM for compound 3. auto_single_measurement only accepted activity measurement [1] 1 structures\9O2W\9O2W_metadata.json point structures/9O2W/9o2w_protein.pdb structures/9O2W/9o2w_pocket.pdb structures/9O2W/9o2w_ligand.sdf structures/9O2W/9o2w_ligand.pdb structures/9O2W/9o2w_ligand.cif structures/9O2W/9o2w_complex.pdb structures/9O2W/9o2w_complex.cif 9O4Y classic GAS41 Na YEATS domain residues 1-148; pGST vector with N-terminal GST tag and TEV cleavage site Na DLG-1 "[""A1B9P""]" 1 IC50 IC50 = = 2.51 ± 0.16 μM 2510.0 [] unit_conversion 5.600326278518962 success True biochemical_inhibition Fluorescence-polarization competition assay using H3K23crK27cr-FAM probe; Table 3. 73 Table 3 reports compound 20 (DLG-1) IC50 FP = 2.51 ± 0.16 μM. The FP assay uses GST-GAS41 YEATS domain residues 1–148. auto_single_measurement only accepted activity measurement [1] 1 structures\9O4Y\9O4Y_metadata.json point structures/9O4Y/9o4y_protein.pdb structures/9O4Y/9o4y_pocket.pdb structures/9O4Y/9o4y_ligand.sdf structures/9O4Y/9o4y_ligand.pdb structures/9O4Y/9o4y_ligand.cif structures/9O4Y/9o4y_complex.pdb structures/9O4Y/9o4y_complex.cif 9O55 extended RM010 Fab and HLA-A*11 class I MHC Na RM010 Fab bound to HLA-A*11 presenting ada-p7; final model includes Fab variable domains and HLA alpha1/alpha2 domains Na ada-p7 (adagrasib-conjugated KRAS(G12C) peptide, residues 7-16) "[""A1B8E"", ""CHAIN:C""]" 1 Kd Kd = = 1.48 ± 0.01 nM 1.48 [] unit_conversion 8.829738284605043 success True direct_binding Biolayer interferometry; RM010 Fab binding to immobilized ada-p7/HLA-A*11 drug-peptide/MHC complex. 2 Fig. 1A prints “ada-p7/A11, KD = 1.48 ± 0.01 nM”; the caption identifies BLI measurement of RM010 Fab binding to the indicated drug-p/HLA complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9O55\9O55_metadata.json point structures/9O55/9o55_protein.pdb structures/9O55/9o55_pocket.pdb structures/9O55/9o55_ligand.pdb structures/9O55/9o55_ligand.cif structures/9O55/9o55_complex.pdb structures/9O55/9o55_complex.cif 9O9N extended PPARgamma ligand binding domain (LBD) Na PPARgamma LBD residues 203-477 (isoform 1 numbering) with a TEV-cleavable N-terminal hexahistidine tag Na FX-909 "[""CHAIN:D""]" 1 Kd Kd = = 0.13 µM 130.0 [] unit_conversion 6.886056647693163 success True direct_binding Fluorescence-polarization binding assay of NCoR1 peptide with PPARγ LBD in the presence of FX-909; the crystallographic complex likewise contains FX-909 and NCoR1 peptide. 3 Figure 2C legend reports “FX909 (Kd = 0.13 μM)” for the FP NCoR1 peptide assay; Figure 2 caption states FP directly measures binding affinities between PPARγ LBD and coregulator peptides in the presence of the indicated ligands. auto_single_measurement only accepted activity measurement [1] 1 structures\9O9N\9O9N_metadata.json point structures/9O9N/9o9n_protein.pdb structures/9O9N/9o9n_pocket.pdb structures/9O9N/9o9n_ligand.pdb structures/9O9N/9o9n_ligand.cif structures/9O9N/9o9n_complex.pdb structures/9O9N/9o9n_complex.cif 9O9Y classic YtrEF ABC transporter complex Bacillus subtilis YtrEF expressed from B. subtilis 168 ytrEF genes in E. coli C41 (DE3), with an N-terminal 6xHis-thrombin tag on YtrE and the ytrE start codon removed WT (wild-type) ADP; vanadate (VO4) "[""VO4""]" 1 IC50 IC50 = = 3.5 ± 0.8 µM 3500.0 [] unit_conversion 5.455931955649724 success True biochemical_inhibition Steady-state ATPase inhibition of purified YtrEF by orthovanadate; the inhibition assay used ATP-Mg2+, and the ADP-vanadate PDB state was prepared with ATP-Mg2+ plus orthovanadate. 4 “Orthovanadate inhibited the ATPase activity of purified YtrEF with an IC50 of 3.5 ± 0.8 µM”; the paper states orthovanadate traps YtrEF in a nucleotide-bound state. auto_single_measurement only accepted activity measurement [1] 1 structures\9O9Y\9O9Y_metadata.json point structures/9O9Y/9o9y_protein.pdb structures/9O9Y/9o9y_pocket.pdb structures/9O9Y/9o9y_ligand.sdf structures/9O9Y/9o9y_ligand.pdb structures/9O9Y/9o9y_ligand.cif structures/9O9Y/9o9y_complex.pdb structures/9O9Y/9o9y_complex.cif 9OBI classic HIV-1 protease HIV-1 Na Na GRL-075-24A; compound 4e "[""A1CAJ""]" 1 Ki Ki = = 0.22 nM 0.22 [] unit_conversion 9.657577319177793 success True biochemical_inhibition Spectrofluorometric HIV-1 protease inhibition assay; Table 1 reports the compound 4e value. The paper identifies the 4e-bound protease structure as PDB 9OBI. 5 Table 1, entry 5, lists inhibitor 4e with Ki = 0.22 nM. The text identifies this as an HIV-1 protease inhibition assay; the deposited 4e-bound protease complex is assigned accession 9OBI. auto_single_measurement only accepted activity measurement [1] 1 structures\9OBI\9OBI_metadata.json point structures/9OBI/9obi_protein.pdb structures/9OBI/9obi_pocket.pdb structures/9OBI/9obi_ligand.sdf structures/9OBI/9obi_ligand.pdb structures/9OBI/9obi_ligand.cif structures/9OBI/9obi_complex.pdb structures/9OBI/9obi_complex.cif 9OCK classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na Compound 1 "[""A1CAS""]" 1 IC50 IC50 = = 4.8 μM 4800.0 [] unit_conversion 5.318758762624412 success True biochemical_inhibition Biochemical RFMS peptide-cleavage assay with recombinant SARS-CoV-2 Mpro. 3 Table 1 reports compound 1 SARS-CoV-2 Mpro IC50 = 4.8 μM [2]; the footnote defines the biochemical RFMS recombinant-protein assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9OCK\9OCK_metadata.json point structures/9OCK/9ock_protein.pdb structures/9OCK/9ock_pocket.pdb structures/9OCK/9ock_ligand.sdf structures/9OCK/9ock_ligand.pdb structures/9OCK/9ock_ligand.cif structures/9OCK/9ock_complex.pdb structures/9OCK/9ock_complex.cif 9OG3 classic Werner syndrome ATP-dependent helicase (WRN) human Two-domain WRN construct, residues 526-946 Na compound 4 "[""A1CA4""]" 1 IC50 IC50 = = 0.017 ± 0.010 µM 17.0 [] unit_conversion 7.769551078621726 success True biochemical_inhibition Biochemical WRN unwinding assay (Table 1). 4 Table 1 reports compound 4 WRN unwinding IC50 = 0.017 ± 0.010 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9OG3\9OG3_metadata.json point structures/9OG3/9og3_protein.pdb structures/9OG3/9og3_pocket.pdb structures/9OG3/9og3_ligand.sdf structures/9OG3/9og3_ligand.pdb structures/9OG3/9og3_ligand.cif structures/9OG3/9og3_complex.pdb structures/9OG3/9og3_complex.cif 9OIM classic von Hippel-Lindau-ElonginB-ElonginC (VCB) complex Na Na Na fragment 9 "[""A1CBI""]" 1 Kd Kd = = 0.66 mM 660000.0 [] unit_conversion 3.1804560644581317 success True direct_binding NMR titration of uniformly 15N-labeled VCB with fragment 9. 3 Figure 4 reports fragment 9 with K_D = 0.66 mM; the text states K_D values of fragment hits were determined by NMR titrations. auto_single_measurement only accepted activity measurement [1] 1 structures\9OIM\9OIM_metadata.json point structures/9OIM/9oim_protein.pdb structures/9OIM/9oim_pocket.pdb structures/9OIM/9oim_ligand.sdf structures/9OIM/9oim_ligand.pdb structures/9OIM/9oim_ligand.cif structures/9OIM/9oim_complex.pdb structures/9OIM/9oim_complex.cif 9OIN classic von Hippel-Lindau-ElonginB-ElonginC (VCB) complex Na Na Na fragment 13 "[""A1CBJ""]" 1 Kd Kd = = 3.4 mM 3400000.0 [] unit_conversion 2.4685210829577446 success True direct_binding NMR titration of uniformly 15N-labeled VCB with fragment 13. 3 Figure 4 reports fragment 13 with K_D = 3.4 mM; the text states K_D values of fragment hits were determined by NMR titrations. auto_single_measurement only accepted activity measurement [1] 1 structures\9OIN\9OIN_metadata.json point structures/9OIN/9oin_protein.pdb structures/9OIN/9oin_pocket.pdb structures/9OIN/9oin_ligand.sdf structures/9OIN/9oin_ligand.pdb structures/9OIN/9oin_ligand.cif structures/9OIN/9oin_complex.pdb structures/9OIN/9oin_complex.cif 9OIQ classic von Hippel-Lindau-ElonginB-ElonginC (VCB) complex Na Na Na fragment 15 "[""A1CBM""]" 1 Kd Kd = = 4.0 mM 4000000.0 [] unit_conversion 2.3979400086720375 success True direct_binding NMR titration of uniformly 15N-labeled VCB with fragment 15. 3 Figure 4 reports fragment 15 with K_D = 4.0 mM; the text states K_D values of fragment hits were determined by NMR titrations. auto_single_measurement only accepted activity measurement [1] 1 structures\9OIQ\9OIQ_metadata.json point structures/9OIQ/9oiq_protein.pdb structures/9OIQ/9oiq_pocket.pdb structures/9OIQ/9oiq_ligand.sdf structures/9OIQ/9oiq_ligand.pdb structures/9OIQ/9oiq_ligand.cif structures/9OIQ/9oiq_complex.pdb structures/9OIQ/9oiq_complex.cif 9OJG classic SARS-CoV-2 main protease (Mpro) SARS-CoV-2 Na Na Compound 2 "[""A1CBY""]" 1 IC50 IC50 = = 0.036 μM 36.0 [] unit_conversion 7.443697499232712 success True biochemical_inhibition Biochemical RFMS peptide-cleavage assay with recombinant SARS-CoV-2 Mpro. 5 Table 2 reports compound 2 SARS-CoV-2 Mpro IC50 = 0.036 μM [17]; the footnote defines the biochemical RFMS recombinant-protein assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9OJG\9OJG_metadata.json point structures/9OJG/9ojg_protein.pdb structures/9OJG/9ojg_pocket.pdb structures/9OJG/9ojg_ligand.sdf structures/9OJG/9ojg_ligand.pdb structures/9OJG/9ojg_ligand.cif structures/9OJG/9ojg_complex.pdb structures/9OJG/9ojg_complex.cif 9OJO classic TNF alpha human TNF alpha residues 77-233 Na compound 1 "[""A1CB1""]" 1 IC50 IC50 = = 472 nM 472.0 [] unit_conversion 6.326058001365912 success True direct_binding Fluorescence-polarization binding assay using human TNFα trimer. 3 Table 1 reports compound 1 FP IC50 = 472 nM; the FP assay is described as TNFα binding. auto_single_measurement only accepted activity measurement [1] 1 structures\9OJO\9OJO_metadata.json point structures/9OJO/9ojo_protein.pdb structures/9OJO/9ojo_pocket.pdb structures/9OJO/9ojo_ligand.sdf structures/9OJO/9ojo_ligand.pdb structures/9OJO/9ojo_ligand.cif structures/9OJO/9ojo_complex.pdb structures/9OJO/9ojo_complex.cif 9OJS classic TNF alpha human TNF alpha residues 77-233 Na compound 4 "[""A1CB0""]" 1 IC50 IC50 = = 1750 nM 1750.0 [] unit_conversion 5.756961951313706 success True direct_binding Fluorescence-polarization binding assay using human TNFα trimer. 3 Table 1 reports compound 4 FP IC50 = 1750 nM; the FP assay is described as TNFα binding. auto_single_measurement only accepted activity measurement [1] 1 structures\9OJS\9OJS_metadata.json point structures/9OJS/9ojs_protein.pdb structures/9OJS/9ojs_pocket.pdb structures/9OJS/9ojs_ligand.sdf structures/9OJS/9ojs_ligand.pdb structures/9OJS/9ojs_ligand.cif structures/9OJS/9ojs_complex.pdb structures/9OJS/9ojs_complex.cif 9OJY classic TNF alpha human TNF alpha residues 77-233 Na compound 3 "[""A1CBZ""]" 1 IC50 IC50 = = 286 nM 286.0 [] unit_conversion 6.543633966870956 success True direct_binding Fluorescence-polarization binding assay using human TNFα trimer. 3 Table 1 reports compound 3 FP IC50 = 286 nM; the FP assay is described as TNFα binding. auto_single_measurement only accepted activity measurement [1] 1 structures\9OJY\9OJY_metadata.json point structures/9OJY/9ojy_protein.pdb structures/9OJY/9ojy_pocket.pdb structures/9OJY/9ojy_ligand.sdf structures/9OJY/9ojy_ligand.pdb structures/9OJY/9ojy_ligand.cif structures/9OJY/9ojy_complex.pdb structures/9OJY/9ojy_complex.cif 9OK6 classic TNF alpha human TNF alpha residues 77-233 Na compound 19 "[""A1CCE""]" 1 IC50 IC50 = = 62 nM 62.0 [] unit_conversion 7.207608310501746 success True direct_binding Fluorescence-polarization binding assay using human TNFα trimer. 5 Table 2 reports compound 19 FP IC50 = 62 nM; compound 19 is mapped to PDB 9OK6 in the accession codes. auto_single_measurement only accepted activity measurement [1] 1 structures\9OK6\9OK6_metadata.json point structures/9OK6/9ok6_protein.pdb structures/9OK6/9ok6_pocket.pdb structures/9OK6/9ok6_ligand.sdf structures/9OK6/9ok6_ligand.pdb structures/9OK6/9ok6_ligand.cif structures/9OK6/9ok6_complex.pdb structures/9OK6/9ok6_complex.cif 9OKG classic human SV2A human SV2A_EM construct: human SV2A residues 141-742 with N-terminal mVenus tag, 3C protease cleavage site, and MBP tag Na levetiracetam "[""UKX""]" 1 IC50 IC50 = = 9.5 µM 9500.0 [] unit_conversion 5.022276394711152 success True direct_binding Radioligand displacement/binding assay; levetiracetam IC50 reported for SV2A. 3 “UCB-J binds to SV2A_EM with high affinity in a radioligand displacement assay, exhibiting an IC50 of 4.1 ± 0.4 nM, 1000-fold lower than that of levetiracetam (IC50 = 9.5 µM).” auto_single_measurement only accepted activity measurement [1] 1 structures\9OKG\9OKG_metadata.json point structures/9OKG/9okg_protein.pdb structures/9OKG/9okg_pocket.pdb structures/9OKG/9okg_ligand.sdf structures/9OKG/9okg_ligand.pdb structures/9OKG/9okg_ligand.cif structures/9OKG/9okg_complex.pdb structures/9OKG/9okg_complex.cif 9OKH classic human SV2A human SV2A_EM construct: human SV2A residues 141-742 with N-terminal mVenus tag, 3C protease cleavage site, and MBP tag Na UCB-J "[""A1CCA""]" 2 Kd Kd = = 19.9 nM 19.9 [] unit_conversion 7.701146923590294 success True direct_binding 3H-UCB-J binding in the absence of UCB1244283; baseline condition of the allosteric-modulation experiment. 5 “We tested the effect of UCB1244283 on 3H-UCB-J binding to SV2A and observed a decrease in Kd (from 19.9 to 11.1 nM).” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9OKH\9OKH_metadata.json point structures/9OKH/9okh_protein.pdb structures/9OKH/9okh_pocket.pdb structures/9OKH/9okh_ligand.sdf structures/9OKH/9okh_ligand.pdb structures/9OKH/9okh_ligand.cif structures/9OKH/9okh_complex.pdb structures/9OKH/9okh_complex.cif 9OKI classic human SV2A human SV2A_EM construct: human SV2A residues 141-742 with N-terminal mVenus tag, 3C protease cleavage site, and MBP tag Na UCB-J; UCB1244283 "[""A1CCA""]" 1 Kd Kd = = 11.1 nM 11.1 [] unit_conversion 7.954677021213342 success True direct_binding 3H-UCB-J binding to SV2A in the presence of allosteric modulator UCB1244283. 5 “We tested the effect of UCB1244283 on 3H-UCB-J binding to SV2A and observed a decrease in Kd (from 19.9 to 11.1 nM).” auto_single_measurement only accepted activity measurement [1] 1 structures\9OKI\9OKI_metadata.json point structures/9OKI/9oki_protein.pdb structures/9OKI/9oki_pocket.pdb structures/9OKI/9oki_ligand.sdf structures/9OKI/9oki_ligand.pdb structures/9OKI/9oki_ligand.cif structures/9OKI/9oki_complex.pdb structures/9OKI/9oki_complex.cif 9OKJ classic human SV2A human SV2A_EM construct: human SV2A residues 141-742 with N-terminal mVenus tag, 3C protease cleavage site, and MBP tag Na padsevonil "[""X3U""]" 1 IC50 IC50 = = 20.9 ± 3.1 nM 20.9 [] unit_conversion 7.679853713888946 success True direct_binding Radioligand competition assay in which padsevonil competitively displaced 3H-UCB-J from SV2A. 5 “In our radioligand binding assay, padsevonil competitively displaced 3H-UCB-J from SV2A with an IC50 of 20.9 ± 3.1 nM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9OKJ\9OKJ_metadata.json point structures/9OKJ/9okj_protein.pdb structures/9OKJ/9okj_pocket.pdb structures/9OKJ/9okj_ligand.sdf structures/9OKJ/9okj_ligand.pdb structures/9OKJ/9okj_ligand.cif structures/9OKJ/9okj_complex.pdb structures/9OKJ/9okj_complex.cif 9OLR classic MelBSt Salmonella enterica serovar Typhimurium D59C MelBSt D59C alpha-methyl galactoside (aMG) "[""AMG""]" 1 Kd Kd = = 9.58 ± 0.03 mM 9580000.0 [] unit_conversion 2.018634490921456 success True direct_binding ITC with Na+ present. 4 Figure 1c prints Kd 9.58 ± 0.03 mM for α-MG binding by the D59C mutant. auto_single_measurement only accepted activity measurement [1] 1 structures\9OLR\9OLR_metadata.json point structures/9OLR/9olr_protein.pdb structures/9OLR/9olr_pocket.pdb structures/9OLR/9olr_ligand.sdf structures/9OLR/9olr_ligand.pdb structures/9OLR/9olr_ligand.cif structures/9OLR/9olr_complex.pdb structures/9OLR/9olr_complex.cif 9ONI classic dihydrofolate reductase (DHFR; WbDHFR) Wuchereria bancrofti Na Na methotrexate (MTX) "[""MTX""]" 2 Ki Ki = = 0.0016 µM 1.6 [] unit_conversion 8.795880017344075 success True biochemical_inhibition WbDHFR inhibition assay; Ki calculated using the Cheung-Prusoff equation. 2 Table 1 lists methotrexate IC50 as 0.023 ± 0.003 µM and Ki as 0.0016 µM for WbDHFR. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9ONI\9ONI_metadata.json point structures/9ONI/9oni_protein.pdb structures/9ONI/9oni_pocket.pdb structures/9ONI/9oni_ligand.sdf structures/9ONI/9oni_ligand.pdb structures/9ONI/9oni_ligand.cif structures/9ONI/9oni_complex.pdb structures/9ONI/9oni_complex.cif 9OOI classic dihydrofolate reductase (DHFR; WbDHFR) Wuchereria bancrofti Na Na TSD001 (OG7) "[""OG7""]" 2 Ki Ki = = 1 µM 1000.0 [] unit_conversion 6.0 success True biochemical_inhibition WbDHFR inhibition assay; Ki calculated using the Cheung-Prusoff equation. 2 Table 1 lists TSD001 IC50 as 18 ± 6 µM and Ki as 1 µM for WbDHFR. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9OOI\9OOI_metadata.json point structures/9OOI/9ooi_protein.pdb structures/9OOI/9ooi_pocket.pdb structures/9OOI/9ooi_ligand.sdf structures/9OOI/9ooi_ligand.pdb structures/9OOI/9ooi_ligand.cif structures/9OOI/9ooi_complex.pdb structures/9OOI/9ooi_complex.cif 9OOZ classic PqqT Na Y161W-PqqT Y161W PQQ "[""PQQ""]" 1 Kd Kd = = 13 ± 2 × 10−3 μM 13.000000000000002 [] unit_conversion 7.886056647693163 success True direct_binding ITC measurement of PQQ dissociation from the Y161W-PqqT variant. 5 Table 2 lists Y161W-PqqT: “PQQ into PqqT Kd (μM)” = 13 ± 2 × 10−3; the text states that the Y161W mutation enhances PqqT affinity for PQQ. auto_single_measurement only accepted activity measurement [1] 1 structures\9OOZ\9OOZ_metadata.json point structures/9OOZ/9ooz_protein.pdb structures/9OOZ/9ooz_pocket.pdb structures/9OOZ/9ooz_ligand.sdf structures/9OOZ/9ooz_ligand.pdb structures/9OOZ/9ooz_ligand.cif structures/9OOZ/9ooz_complex.pdb structures/9OOZ/9ooz_complex.cif 9OUM classic Native GABA-A receptor, beta2-alpha1-beta1-alpha6-gamma2 subtype rat Native receptor from rat cerebella Na PZ-II-029 "[""A1CEP""]" 1 Ki Ki = = 4.2 ± 0.4 nM 4.2 [] unit_conversion 8.3767507096021 success True direct_binding Scintillation-proximity competitive binding assay: displacement of [3H]-flunitrazepam by PZ-II-029 using purified native cerebellar GABA_A receptors reconstituted in nanodiscs. 6 “The K_i of PZ-II-029 is determined to be 4.2 ± 0.4 nM (Fig. 4C).” auto_single_measurement only accepted activity measurement [1] 1 structures\9OUM\9OUM_metadata.json point structures/9OUM/9oum_protein.pdb structures/9OUM/9oum_pocket.pdb structures/9OUM/9oum_ligand.sdf structures/9OUM/9oum_ligand.pdb structures/9OUM/9oum_ligand.cif structures/9OUM/9oum_complex.pdb structures/9OUM/9oum_complex.cif 9OUN classic Native GABA-A receptor, beta2-alpha1-beta2-alpha1-gamma2 subtype rat Native receptor from rat cerebella Na PZ-II-029 "[""A1CEP""]" 1 Ki Ki = = 4.2 ± 0.4 nM 4.2 [] unit_conversion 8.3767507096021 success True direct_binding Scintillation-proximity competitive binding assay: displacement of [3H]-flunitrazepam by PZ-II-029 using purified native cerebellar GABA_A receptors reconstituted in nanodiscs. 6 “The K_i of PZ-II-029 is determined to be 4.2 ± 0.4 nM (Fig. 4C).” auto_single_measurement only accepted activity measurement [1] 1 structures\9OUN\9OUN_metadata.json point structures/9OUN/9oun_protein.pdb structures/9OUN/9oun_pocket.pdb structures/9OUN/9oun_ligand.sdf structures/9OUN/9oun_ligand.pdb structures/9OUN/9oun_ligand.cif structures/9OUN/9oun_complex.pdb structures/9OUN/9oun_complex.cif 9OUO classic Native GABA-A receptor, beta1-alpha1-beta1-alpha1-gamma2 subtype rat Native receptor from rat cerebella Na PZ-II-029 "[""A1CEP""]" 1 Ki Ki = = 4.2 ± 0.4 nM 4.2 [] unit_conversion 8.3767507096021 success True direct_binding Scintillation-proximity competitive binding assay: displacement of [3H]-flunitrazepam by PZ-II-029 using purified native cerebellar GABA_A receptors reconstituted in nanodiscs. 6 “The K_i of PZ-II-029 is determined to be 4.2 ± 0.4 nM (Fig. 4C).” auto_single_measurement only accepted activity measurement [1] 1 structures\9OUO\9OUO_metadata.json point structures/9OUO/9ouo_protein.pdb structures/9OUO/9ouo_pocket.pdb structures/9OUO/9ouo_ligand.sdf structures/9OUO/9ouo_ligand.pdb structures/9OUO/9ouo_ligand.cif structures/9OUO/9ouo_complex.pdb structures/9OUO/9ouo_complex.cif 9OV4 classic Native GABA-A receptor, beta1-alpha1-beta2-alpha1-gamma2 subtype rat Native receptor from rat cerebella Na PZ-II-029 "[""A1CEP""]" 1 Ki Ki = = 4.2 ± 0.4 nM 4.2 [] unit_conversion 8.3767507096021 success True direct_binding Scintillation-proximity competitive binding assay: displacement of [3H]-flunitrazepam by PZ-II-029 using purified native cerebellar GABA_A receptors reconstituted in nanodiscs. 6 “The K_i of PZ-II-029 is determined to be 4.2 ± 0.4 nM (Fig. 4C).” auto_single_measurement only accepted activity measurement [1] 1 structures\9OV4\9OV4_metadata.json point structures/9OV4/9ov4_protein.pdb structures/9OV4/9ov4_pocket.pdb structures/9OV4/9ov4_ligand.sdf structures/9OV4/9ov4_ligand.pdb structures/9OV4/9ov4_ligand.cif structures/9OV4/9ov4_complex.pdb structures/9OV4/9ov4_complex.cif 9OVJ classic SHOC2 human SHOC2 80-582 Na (R)-5 "[""A1CF1""]" 1 Kd Kd = = 0.73 ± 0.19 (n=4) µM 730.0 [] unit_conversion 6.136677139879544 success True direct_binding SPR binding to SHOC2; Table 1 specifies the SHOC2 construct as amino acids 80–582. 6 Table 1 reports (R)-5 SPR Kd on SHOC2 of 0.73 ± 0.19 µM (n=4). auto_single_measurement only accepted activity measurement [1] 1 structures\9OVJ\9OVJ_metadata.json point structures/9OVJ/9ovj_protein.pdb structures/9OVJ/9ovj_pocket.pdb structures/9OVJ/9ovj_ligand.sdf structures/9OVJ/9ovj_ligand.pdb structures/9OVJ/9ovj_ligand.cif structures/9OVJ/9ovj_complex.pdb structures/9OVJ/9ovj_complex.cif 9OVQ classic PAD2 Na Na Na compound 4f "[""A1CE0""]" 1 IC50 IC50 = = 23 nM 23.0 [] unit_conversion 7.638272163982407 success True biochemical_inhibition Fluorescence-quenching enzyme assay; Table 2 reports enzyme FQ IC50 values for PAD2 and PAD4. 3 Table 2 lists compound 4f with PAD2 IC50 = 23 nM. The text states that PAD2/PAD4 potency was determined using a fluorescence-quenching enzyme assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9OVQ\9OVQ_metadata.json point structures/9OVQ/9ovq_protein.pdb structures/9OVQ/9ovq_pocket.pdb structures/9OVQ/9ovq_ligand.sdf structures/9OVQ/9ovq_ligand.pdb structures/9OVQ/9ovq_ligand.cif structures/9OVQ/9ovq_complex.pdb structures/9OVQ/9ovq_complex.cif 9OX9 classic S. mansoni p97 Schistosoma mansoni Na Na CB-5083 "[""JDP""]" 1 IC50 IC50 = = 11 ± 2.1 nM 11.0 [] unit_conversion 7.958607314841775 success True biochemical_inhibition Kinase-Glo ATP-consumption assay using recombinant S. mansoni p97. 6 Fig. 3D reports CB-5083 IC50 values for S. mansoni and H. sapiens p97; the S. mansoni value is 11 ± 2.1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9OX9\9OX9_metadata.json point structures/9OX9/9ox9_protein.pdb structures/9OX9/9ox9_pocket.pdb structures/9OX9/9ox9_ligand.sdf structures/9OX9/9ox9_ligand.pdb structures/9OX9/9ox9_ligand.cif structures/9OX9/9ox9_complex.pdb structures/9OX9/9ox9_complex.cif 9OZE classic 1-deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) Acinetobacter baumannii Na Na compound 3b (N-acyl fosmidomycin analog; R2=(4-Cl)Ph) "[""A1CFA""]" 1 IC50 IC50 = = 0.172 μM 172.0 [] unit_conversion 6.764471553092451 success True biochemical_inhibition Purified recombinant AbIspC enzyme-inhibition assay. 4 Table 1 reports compound 3b IC50 = 0.172 μM for AbIspC. auto_single_measurement only accepted activity measurement [1] 1 structures\9OZE\9OZE_metadata.json point structures/9OZE/9oze_protein.pdb structures/9OZE/9oze_pocket.pdb structures/9OZE/9oze_ligand.sdf structures/9OZE/9oze_ligand.pdb structures/9OZE/9oze_ligand.cif structures/9OZE/9oze_complex.pdb structures/9OZE/9oze_complex.cif 9OZF classic 1-deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) Acinetobacter baumannii Na Na compound 2b (N-acyl fosmidomycin analog; R2=(3-Cl)Ph) "[""A1CFB""]" 1 IC50 IC50 = = 0.154 μM 154.0 [] unit_conversion 6.8124792791635365 success True biochemical_inhibition Purified recombinant AbIspC enzyme-inhibition assay. 4 Table 1 reports compound 2b IC50 = 0.154 μM for AbIspC. auto_single_measurement only accepted activity measurement [1] 1 structures\9OZF\9OZF_metadata.json point structures/9OZF/9ozf_protein.pdb structures/9OZF/9ozf_pocket.pdb structures/9OZF/9ozf_ligand.sdf structures/9OZF/9ozf_ligand.pdb structures/9OZF/9ozf_ligand.cif structures/9OZF/9ozf_complex.pdb structures/9OZF/9ozf_complex.cif 9OZG classic 1-deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) Acinetobacter baumannii Na Na compound 4b (N-acyl fosmidomycin analog; R2=(3,5-Cl)Ph) "[""A1CE6""]" 1 IC50 IC50 = = 0.047 μM 47.0 [] unit_conversion 7.327902142064282 success True biochemical_inhibition Purified recombinant AbIspC enzyme-inhibition assay. 4 Table 1 reports compound 4b IC50 = 0.047 μM for AbIspC. auto_single_measurement only accepted activity measurement [1] 1 structures\9OZG\9OZG_metadata.json point structures/9OZG/9ozg_protein.pdb structures/9OZG/9ozg_pocket.pdb structures/9OZG/9ozg_ligand.sdf structures/9OZG/9ozg_ligand.pdb structures/9OZG/9ozg_ligand.cif structures/9OZG/9ozg_complex.pdb structures/9OZG/9ozg_complex.cif 9P4A classic Dihydropteroate synthase (EcDHPS) Escherichia coli Na Na 1532 "[""A1CG3""]" 1 Kd Kd = = 5.83 nM 5.83 [] unit_conversion 8.234331445240986 success True direct_binding SPR equilibrium dissociation constant for EcDHPS; Table 1 footnote defines Kd as k_off/k_on. 3 Table 1 lists compound 1532 with Kd 5.83 nM; its footnote states Kd values indicate binding affinity for EcDHPS. The text identifies the cocrystal of 1532 bound to EcDHPS as PDB 9P4A. auto_single_measurement only accepted activity measurement [1] 1 structures\9P4A\9P4A_metadata.json point structures/9P4A/9p4a_protein.pdb structures/9P4A/9p4a_pocket.pdb structures/9P4A/9p4a_ligand.sdf structures/9P4A/9p4a_ligand.pdb structures/9P4A/9p4a_ligand.cif structures/9P4A/9p4a_complex.pdb structures/9P4A/9p4a_complex.cif 9P4D classic glutamine-binding protein (GlnBP) Escherichia coli T72C-functionalized GlnBP covalently attached at Cys72 to Gd(DOTA-malN) T72C Gd(DOTA-malN) "[""GLN""]" 1 Kd Kd = = 1.8 ± 0.8 μM 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding ITC measurement of Gln binding after bioconjugation with Gd(DOTA-malN). 3 “Kd increasing from 0.6 ± 0.1 μM to 1.8 ± 0.8 μM on bioconjugation with Gd(DOTA-malN).” The preceding text identifies the main variant as T72C-GlnBP and states that the Kds are for Gln. auto_single_measurement only accepted activity measurement [1] 1 structures\9P4D\9P4D_metadata.json point structures/9P4D/9p4d_protein.pdb structures/9P4D/9p4d_pocket.pdb structures/9P4D/9p4d_ligand.sdf structures/9P4D/9p4d_ligand.pdb structures/9P4D/9p4d_ligand.cif structures/9P4D/9p4d_complex.pdb structures/9P4D/9p4d_complex.cif 9P5I extended Dihydropteroate synthase (EcDHPS) Escherichia coli Na Na 4366 "[""A1CG7""]" 1 Kd Kd = = 3.23 nM 3.23 [] unit_conversion 8.490797477668897 success True direct_binding SPR equilibrium dissociation constant for EcDHPS; Table 2 footnote defines Kd as k_off/k_on. 6 Table 2 lists compound 4366 with Kd 3.23 nM; its footnote states Kd values indicate binding affinity for EcDHPS. The text identifies the cocrystal of 4366 bound to EcDHPS as PDB 9P5I. auto_single_measurement only accepted activity measurement [1] 1 structures\9P5I\9P5I_metadata.json point structures/9P5I/9p5i_protein.pdb structures/9P5I/9p5i_pocket.pdb structures/9P5I/9p5i_ligand.pdb structures/9P5I/9p5i_ligand.cif structures/9P5I/9p5i_complex.pdb structures/9P5I/9p5i_complex.cif 9PCA classic Human PRMT5:MEP50 complex human Na Na compound 18 "[""A1CHO""]" 2 Kd Kd = = 11.7 ± 4.8 pM 0.0117 [] unit_conversion 10.931814138253838 success True direct_binding Surface plasmon resonance binding of compound 18 to human PRMT5:MEP50. 11 Figure 8 reports SPR characterization of compound 18 with human PRMT5:MEP50 and gives KD = 11.7 ± 4.8 pM. Figure 6 maps compound 18 in this complex to PDB 9PCA. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9PCA\9PCA_metadata.json point structures/9PCA/9pca_protein.pdb structures/9PCA/9pca_pocket.pdb structures/9PCA/9pca_ligand.sdf structures/9PCA/9pca_ligand.pdb structures/9PCA/9pca_ligand.cif structures/9PCA/9pca_complex.pdb structures/9PCA/9pca_complex.cif 9PCB classic Synaptic vesicle protein 2A (SV2A) human SV2ADelta64-mVenus with TwinStrep and 10-His tags and a 3C protease site N-terminal deletion of residues 1-64 (Delta64) UCB-J "[""A1CCA""]" 1 Kd Kd = = 5.3 ± 0.8 nM 5.3 [] unit_conversion 8.275724130399212 success True direct_binding Radioligand binding of 3H-UCB-J to SV2AΔ64-mVenus; measured in the absence of UCB1244283. 4 “SV2A displayed a similar binding affinity for UCB-J under both conditions, with a Kd of 6 ± 1 nM in the presence and 5.3 ± 0.8 nM in the absence of UCB1244283.” The radioligand assay uses SV2AΔ64-mVenus wild-type construct. auto_single_measurement only accepted activity measurement [1] 1 structures\9PCB\9PCB_metadata.json point structures/9PCB/9pcb_protein.pdb structures/9PCB/9pcb_pocket.pdb structures/9PCB/9pcb_ligand.sdf structures/9PCB/9pcb_ligand.pdb structures/9PCB/9pcb_ligand.cif structures/9PCB/9pcb_complex.pdb structures/9PCB/9pcb_complex.cif 9PE9 classic GSK3beta Na Na Na compound 6 "[""A1CIF""]" 1 Ki Ki = = 1.5 nM 1.5 [] unit_conversion 8.823908740944319 success True biochemical_inhibition Purified-protein kinase activity; Table 1. 2 Table 1 reports GSK3β Ki = 1.5 nM for compound 6. auto_single_measurement only accepted activity measurement [1] 1 structures\9PE9\9PE9_metadata.json point structures/9PE9/9pe9_protein.pdb structures/9PE9/9pe9_pocket.pdb structures/9PE9/9pe9_ligand.sdf structures/9PE9/9pe9_ligand.pdb structures/9PE9/9pe9_ligand.cif structures/9PE9/9pe9_complex.pdb structures/9PE9/9pe9_complex.cif 9PH4 classic COP9 signalosome (CSN) Homo sapiens CSN5i-1a-CSN Na CSN5i-1a "[""A1CH3""]" 1 IC50 IC50 = = 3.6 μM 3600.0 [] unit_conversion 5.443697499232712 success True biochemical_inhibition CSN iso-peptidase activity towards N8~CRL1 in vitro. 7 Fig. 4i prints IC50 3.6 μM for CSN5i-1a; substrate is N8~CRL1 and enzyme is CSN. auto_single_measurement only accepted activity measurement [1] 1 structures\9PH4\9PH4_metadata.json point structures/9PH4/9ph4_protein.pdb structures/9PH4/9ph4_pocket.pdb structures/9PH4/9ph4_ligand.sdf structures/9PH4/9ph4_ligand.pdb structures/9PH4/9ph4_ligand.cif structures/9PH4/9ph4_complex.pdb structures/9PH4/9ph4_complex.cif 9PHT extended influenza virus hemagglutinin Influenza A virus Na Na CP141085 (CP1) "[""CHAIN:G""]" 1 Kd Kd = = 1.80±0.34 µM 1800.0 [] unit_conversion 5.7447274948966935 success True direct_binding SPR kinetic binding assay 4 The SPR kinetic-data table explicitly reports CP1 Kd of 1.80±0.34 µM against H5/Viet HA. auto_single_measurement only accepted activity measurement [1] 1 structures\9PHT\9PHT_metadata.json point structures/9PHT/9pht_protein.pdb structures/9PHT/9pht_pocket.pdb structures/9PHT/9pht_ligand.pdb structures/9PHT/9pht_ligand.cif structures/9PHT/9pht_complex.pdb structures/9PHT/9pht_complex.cif 9PKR extended SARS-CoV-2 main protease SARS-CoV-2 Na Na compound 26 "[""CHAIN:E"", ""CHAIN:F""]" 1 IC50 IC50 = = 0.028 ± 0.011 µM 28.0 [] unit_conversion 7.552841968657781 success True biochemical_inhibition Purified-protein FRET protease inhibition assay. 5 Figure 2B visibly reports for compound 26: “SARS-CoV-2 Mpro IC50 = 0.028 ± 0.011 µM.” The paper identifies PDB 9PKR as SARS-CoV-2 Mpro bound to compound 26. auto_single_measurement only accepted activity measurement [1] 1 structures\9PKR\9PKR_metadata.json point structures/9PKR/9pkr_protein.pdb structures/9PKR/9pkr_pocket.pdb structures/9PKR/9pkr_ligand.pdb structures/9PKR/9pkr_ligand.cif structures/9PKR/9pkr_complex.pdb structures/9PKR/9pkr_complex.cif 9PLJ classic human CYP3A4 human Na WT (wild-type) THC "[""TCI""]" 1 Kd Kd = = 1.9 ± 0.1 µM 1900.0 [] unit_conversion 5.721246399047171 success True direct_binding Equilibrium spectral titration of WT CYP3A4 with THC; one-site binding fit. 2 The text reports a single-site THC binding fit with Kd 1.9 ± 0.1 µM; Fig. 1B labels Kd = 1.9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9PLJ\9PLJ_metadata.json point structures/9PLJ/9plj_protein.pdb structures/9PLJ/9plj_pocket.pdb structures/9PLJ/9plj_ligand.sdf structures/9PLJ/9plj_ligand.pdb structures/9PLJ/9plj_ligand.cif structures/9PLJ/9plj_complex.pdb structures/9PLJ/9plj_complex.cif 9PME extended MazF-E24A toxin Escherichia coli (E. coli), strain MG1655 MazF-E24A expressed with an N-terminal His6 tag; His6 tag removed before crystallization E24A (Glu24Ala) SamF (Ac-SHLFWAQFDEYF-NH2; N-acetylated and C-amidated peptide) "[""CHAIN:B""]" 1 Kd Kd = = 2.5 ± 0.7 μM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding ITC of synthetic SamF binding the catalytically less-active MazF_E24A mutant. 4 The ITC analysis reports ΔH = −11.8 ± 1.6 kcal/mol, TΔS = −3.9 ± 1.9 kcal/mol, and KD = 2.5 ± 0.7 μM for the peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\9PME\9PME_metadata.json point structures/9PME/9pme_protein.pdb structures/9PME/9pme_pocket.pdb structures/9PME/9pme_ligand.pdb structures/9PME/9pme_ligand.cif structures/9PME/9pme_complex.pdb structures/9PME/9pme_complex.cif 9PMP classic Influenza PA-N Endonuclease Na N-terminal PA (PA_N) endonuclease Delta52-74:Gly truncated construct from A/California/04/2009(H1N1) I38T compound 1 (3-hydroxy-6-(2-methylphenyl)-4-oxo-1,4-dihydropyridine-2-carboxylic acid) "[""HNS""]" 1 Kd Kd = = 6.84 ± 1.02 µM 6840.0 [] unit_conversion 5.164943898279883 success True direct_binding Differential scanning fluorometry thermal-shift binding assay; apparent Kd determined from ligand-concentration curves. 23 Table 4 reports I38T apparent Kd for compound 1 as 6.84 ± 1.02 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9PMP\9PMP_metadata.json point structures/9PMP/9pmp_protein.pdb structures/9PMP/9pmp_pocket.pdb structures/9PMP/9pmp_ligand.sdf structures/9PMP/9pmp_ligand.pdb structures/9PMP/9pmp_ligand.cif structures/9PMP/9pmp_complex.pdb structures/9PMP/9pmp_complex.cif 9PMR classic Influenza PA-N Endonuclease Na N-terminal PA (PA_N) endonuclease Delta52-74:Gly truncated construct from A/California/04/2009(H1N1) I38T compound 2 ((6M)-6-(2-ethylphenyl)-3,4-dihydroxypyridine-2-carboxylic acid) "[""A1CI3""]" 1 Kd Kd = = 3.06 ± 0.45 µM 3060.0 [] unit_conversion 5.514278573518419 success True direct_binding Differential scanning fluorometry thermal-shift binding assay; apparent Kd determined from ligand-concentration curves. 23 Table 4 reports I38T apparent Kd for compound 2 as 3.06 ± 0.45 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9PMR\9PMR_metadata.json point structures/9PMR/9pmr_protein.pdb structures/9PMR/9pmr_pocket.pdb structures/9PMR/9pmr_ligand.sdf structures/9PMR/9pmr_ligand.pdb structures/9PMR/9pmr_ligand.cif structures/9PMR/9pmr_complex.pdb structures/9PMR/9pmr_complex.cif 9PN3 classic Influenza PA-N Endonuclease Na N-terminal PA (PA_N) endonuclease Delta52-74:Gly truncated construct from A/California/04/2009(H1N1) I38T compound 4 ((6M)-3-hydroxy-4-oxo-6-(2-phenoxyphenyl)-1,4-dihydropyridine-2-carboxylic acid) "[""A1CI5""]" 1 Kd Kd = = 10.28 ± 1.38 µM 10280.0 [] unit_conversion 4.988006885340743 success True direct_binding Differential scanning fluorometry thermal-shift binding assay; apparent Kd determined from ligand-concentration curves. 23 Table 4 reports I38T apparent Kd for compound 4 as 10.28 ± 1.38 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9PN3\9PN3_metadata.json point structures/9PN3/9pn3_protein.pdb structures/9PN3/9pn3_pocket.pdb structures/9PN3/9pn3_ligand.sdf structures/9PN3/9pn3_ligand.pdb structures/9PN3/9pn3_ligand.cif structures/9PN3/9pn3_complex.pdb structures/9PN3/9pn3_complex.cif 9PNL classic Influenza PA-N Endonuclease Na N-terminal PA (PA_N) endonuclease Delta52-74:Gly truncated construct from A/California/04/2009(H1N1) E23K compound 4 ((6M)-3-hydroxy-4-oxo-6-(2-phenoxyphenyl)-1,4-dihydropyridine-2-carboxylic acid) "[""A1CI5""]" 1 Kd Kd = = 9.31 ± 2.86 µM 9310.0 [] unit_conversion 5.031050319018657 success True direct_binding Differential scanning fluorometry thermal-shift binding assay; apparent Kd determined from ligand-concentration curves. 23 Table 4 reports E23K apparent Kd for compound 4 as 9.31 ± 2.86 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9PNL\9PNL_metadata.json point structures/9PNL/9pnl_protein.pdb structures/9PNL/9pnl_pocket.pdb structures/9PNL/9pnl_ligand.sdf structures/9PNL/9pnl_ligand.pdb structures/9PNL/9pnl_ligand.cif structures/9PNL/9pnl_complex.pdb structures/9PNL/9pnl_complex.cif 9PO6 classic Influenza PA-N Endonuclease Na N-terminal PA (PA_N) endonuclease Delta52-74:Gly truncated construct from A/California/04/2009(H1N1) WT compound 4 ((6M)-3-hydroxy-4-oxo-6-(2-phenoxyphenyl)-1,4-dihydropyridine-2-carboxylic acid) "[""A1CI5""]" 1 Kd Kd = = 12.34 ± 4.19 µM 12340.0 [] unit_conversion 4.908684840302777 success True direct_binding Differential scanning fluorometry thermal-shift binding assay; apparent Kd determined from ligand-concentration curves. 23 Table 4 reports WT apparent Kd for compound 4 as 12.34 ± 4.19 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9PO6\9PO6_metadata.json point structures/9PO6/9po6_protein.pdb structures/9PO6/9po6_pocket.pdb structures/9PO6/9po6_ligand.sdf structures/9PO6/9po6_ligand.pdb structures/9PO6/9po6_ligand.cif structures/9PO6/9po6_complex.pdb structures/9PO6/9po6_complex.cif 9PPP extended AP-2 alpha appendage Mus musculus AP-2 alpha appendage residues 695-938 bound to a CCDC32 residues 17-44 extended FxDxF peptide Na CCDC32 extended FxDxF peptide, residues 17-44, sequence DLWAEICSLPSPAQEDVSDNAFSDSFM "[""CHAIN:P"", ""CHAIN:Q""]" 1 Kd Kd = = 287 nM 287.0 [] unit_conversion 6.542118103266008 success True direct_binding Fluorescence-polarization binding isotherm of a 28-residue CCDC32 peptide spanning the DLW and FxDxF sequence motifs with AP-2 alpha appendage. 25 Supplementary Figure 4C visibly reports the fitted value “Kd = 287 nM” for the “DLW + FxDxF” CCDC32 peptide; the page-3 text identifies this as the 28-amino-acid extended motif used with the alpha appendage, and Table 1 assigns the extended FxDxF alpha-appendage complex to PDB 9PPP. auto_single_measurement only accepted activity measurement [1] 1 structures\9PPP\9PPP_metadata.json point structures/9PPP/9ppp_protein.pdb structures/9PPP/9ppp_pocket.pdb structures/9PPP/9ppp_ligand.pdb structures/9PPP/9ppp_ligand.cif structures/9PPP/9ppp_complex.pdb structures/9PPP/9ppp_complex.cif 9PQ5 classic MCL-1-MBP Na MCL-1 maltose-binding protein chimera Na (S_a)-8 (ligand 8) "[""A1CMI""]" 1 Ki Ki = = 0.019 nM 0.019 [] unit_conversion 10.721246399047171 success True direct_binding Tb-MCL-1 homogeneous time-resolved fluorescence (HTRF) competitive binding assay using a Cy5-tagged BIM BH3 peptide. 3 Figure 2 reports “(S_a)-8 MCL-1 K_i 0.019 nM”; its caption identifies these compounds as MCL-1 inhibitors. Figure 3 assigns the (S_a)-8 co-crystal to printed PDB 9PQS, uniquely reconciled to requested 9PQ5. auto_single_measurement only accepted activity measurement [1] 1 structures\9PQ5\9PQ5_metadata.json point structures/9PQ5/9pq5_protein.pdb structures/9PQ5/9pq5_pocket.pdb structures/9PQ5/9pq5_ligand.sdf structures/9PQ5/9pq5_ligand.pdb structures/9PQ5/9pq5_ligand.cif structures/9PQ5/9pq5_complex.pdb structures/9PQ5/9pq5_complex.cif 9PQ6 classic MCL-1-MBP Na MCL-1 maltose-binding protein chimera Na (S_a)-12 (ligand 12) "[""A1CMH""]" 1 Ki Ki = = 0.023 nM 0.023 [] unit_conversion 10.638272163982407 success True direct_binding Tb-MCL-1 homogeneous time-resolved fluorescence (HTRF) competitive binding assay using a Cy5-tagged BIM BH3 peptide; Table 3 reports n=47 determinations. 6 Table 3 reports for (S_a)-12: K_i = 0.023 nM (n=47), with the footnote specifying the Tb-MCL-1 HTRF assay. Figure 3D identifies the (S_a)-12 MCL-1-MBP co-crystal as PDB 9PQ6. auto_single_measurement only accepted activity measurement [1] 1 structures\9PQ6\9PQ6_metadata.json point structures/9PQ6/9pq6_protein.pdb structures/9PQ6/9pq6_pocket.pdb structures/9PQ6/9pq6_ligand.sdf structures/9PQ6/9pq6_ligand.pdb structures/9PQ6/9pq6_ligand.cif structures/9PQ6/9pq6_complex.pdb structures/9PQ6/9pq6_complex.cif 9PQ7 classic MCL-1-MBP Na MCL-1 maltose-binding protein chimera Na (S_a)-21b (ligand 21b) "[""A1CMG""]" 1 Ki Ki = = 0.015 nM 0.015 [] unit_conversion 10.823908740944319 success True direct_binding Tb-MCL-1 homogeneous time-resolved fluorescence (HTRF) competitive binding assay using a Cy5-tagged BIM BH3 peptide; Table 4 reports n=36 determinations. 7 Table 4 reports for (S_a)-21b: K_i = 0.015 nM (n=36), and its footnote specifies the Tb-MCL-1 HTRF assay. Figure 3E identifies the (S_a)-21b MCL-1-MBP co-crystal as PDB 9PQ7. auto_single_measurement only accepted activity measurement [1] 1 structures\9PQ7\9PQ7_metadata.json point structures/9PQ7/9pq7_protein.pdb structures/9PQ7/9pq7_pocket.pdb structures/9PQ7/9pq7_ligand.sdf structures/9PQ7/9pq7_ligand.pdb structures/9PQ7/9pq7_ligand.cif structures/9PQ7/9pq7_complex.pdb structures/9PQ7/9pq7_complex.cif 9PQH extended Calmodulin (CaM) and NMDA receptor GluN1 subunit Na Ca2+-CaM bound to GluN1-C0 peptide, residues 841-865 Na GluN1-C0 peptide "[""CHAIN:B""]" 1 Kd Kd = = 0.06 ± 0.01 μM 60.0 [] unit_conversion 7.221848749616356 success True direct_binding ITC; Ca2+-CaM titrated with GluN1-C0 peptide; one-site model. 3 Table 1 reports Ca2+-CaM/GluN1-C0 KD = 0.06 ± 0.01 μM; page 11 maps PDB 9PQH to Ca2+-CaM/GluN1-C0. auto_single_measurement only accepted activity measurement [1] 1 structures\9PQH\9PQH_metadata.json point structures/9PQH/9pqh_protein.pdb structures/9PQH/9pqh_pocket.pdb structures/9PQH/9pqh_ligand.pdb structures/9PQH/9pqh_ligand.cif structures/9PQH/9pqh_complex.pdb structures/9PQH/9pqh_complex.cif 9PQI extended Calmodulin C-lobe and NMDA receptor GluN2A subunit Na Ca2+-CaM C-lobe bound to GluN2A-C0 peptide, residues 1004-1023 Na GluN2A-C0 peptide "[""CHAIN:B""]" 1 Kd Kd = = 0.05 ± 0.01 μM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding ITC using Ca2+-CaM C-lobe and GluN2A-C0 peptide; one-site model. 3 Table 1 reports Ca2+-CaM C-lobe/GluN2A-C0 KD = 0.05 ± 0.01 μM; page 11 maps PDB 9PQI to this complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9PQI\9PQI_metadata.json point structures/9PQI/9pqi_protein.pdb structures/9PQI/9pqi_pocket.pdb structures/9PQI/9pqi_ligand.pdb structures/9PQI/9pqi_ligand.cif structures/9PQI/9pqi_complex.pdb structures/9PQI/9pqi_complex.cif 9PRE classic Escherichia coli DsbA Escherichia coli Na Na propiolic acid 5 "[""A1CJH""]" 1 Kd Kd = = 1160 ± 70 µM 1160000.0 [] unit_conversion 2.935542010773082 success True direct_binding SPR affinity; steady-state binding-model fit (n = 3). 3 Table 1 reports propiolic acid 5 SPR affinity KD = 1160 ± 70 µM; Figure 2 assigns propiolic acid 5 to PDB 9PRE. auto_single_measurement only accepted activity measurement [1] 1 structures\9PRE\9PRE_metadata.json point structures/9PRE/9pre_protein.pdb structures/9PRE/9pre_pocket.pdb structures/9PRE/9pre_ligand.sdf structures/9PRE/9pre_ligand.pdb structures/9PRE/9pre_ligand.cif structures/9PRE/9pre_complex.pdb structures/9PRE/9pre_complex.cif 9PRG classic Escherichia coli DsbA Escherichia coli Na Na analogue 7 "[""A1CJK""]" 1 Kd Kd = = 1320 ± 230 µM 1320000.0 [] unit_conversion 2.8794260687941504 success True direct_binding SPR affinity; steady-state binding-model fit (n = 3). 4 Figure 3 reports analogue 7 SPR KD = 1320 ± 230 µM and assigns analogue 7 to PDB 9PRG. auto_single_measurement only accepted activity measurement [1] 1 structures\9PRG\9PRG_metadata.json point structures/9PRG/9prg_protein.pdb structures/9PRG/9prg_pocket.pdb structures/9PRG/9prg_ligand.sdf structures/9PRG/9prg_ligand.pdb structures/9PRG/9prg_ligand.cif structures/9PRG/9prg_complex.pdb structures/9PRG/9prg_complex.cif 9PRH classic Escherichia coli DsbA Escherichia coli Na Na analogue 8 "[""A1CJL""]" 1 Kd Kd = = 266 ± 1 µM 266000.0 [] unit_conversion 3.575118363368933 success True direct_binding SPR affinity; steady-state binding-model fit (n = 3). 4 Figure 3 reports analogue 8 SPR KD = 266 ± 1 µM and assigns analogue 8 to PDB 9PRH. auto_single_measurement only accepted activity measurement [1] 1 structures\9PRH\9PRH_metadata.json point structures/9PRH/9prh_protein.pdb structures/9PRH/9prh_pocket.pdb structures/9PRH/9prh_ligand.sdf structures/9PRH/9prh_ligand.pdb structures/9PRH/9prh_ligand.cif structures/9PRH/9prh_complex.pdb structures/9PRH/9prh_complex.cif 9PSS classic IRAK4 Na Na Na Compound 3 "[""A1CKP""]" 1 IC50 IC50 = = 0.96 nM 0.96 [] unit_conversion 9.017728766960431 success True biochemical_inhibition Biochemical IRAK4 inhibition assay (500 μM ATP). 2 Figure 2 identifies compound 3 as X-ray bound to IRAK4 (PDB ID: 9PSS) and prints “IRAK4 IC50: 0.96 nM”; its caption defines biochemical IRAK4 inhibition at 500 μM ATP. auto_single_measurement only accepted activity measurement [1] 1 structures\9PSS\9PSS_metadata.json point structures/9PSS/9pss_protein.pdb structures/9PSS/9pss_pocket.pdb structures/9PSS/9pss_ligand.sdf structures/9PSS/9pss_ligand.pdb structures/9PSS/9pss_ligand.cif structures/9PSS/9pss_complex.pdb structures/9PSS/9pss_complex.cif 9PST classic IRAK4 Na Na Na Compound 5 "[""A1CKQ""]" 1 IC50 IC50 = = 0.78 nM 0.78 [] unit_conversion 9.10790539730952 success True biochemical_inhibition Biochemical IRAK4 inhibition assay (500 μM ATP). 2 Figure 3 identifies compound 5 as bound to IRAK4 (PDB ID: 9PST) and prints “IRAK4 IC50: 0.78 nM”; its caption defines biochemical IRAK4 inhibition at 500 μM ATP. auto_single_measurement only accepted activity measurement [1] 1 structures\9PST\9PST_metadata.json point structures/9PST/9pst_protein.pdb structures/9PST/9pst_pocket.pdb structures/9PST/9pst_ligand.sdf structures/9PST/9pst_ligand.pdb structures/9PST/9pst_ligand.cif structures/9PST/9pst_complex.pdb structures/9PST/9pst_complex.cif 9PSU classic IRAK4 Na Na Na Compound 12 "[""A1CKS""]" 1 IC50 IC50 = = 0.84 nM 0.84 [] unit_conversion 9.075720713938118 success True biochemical_inhibition Biochemical IRAK4 inhibition assay (500 μM ATP). 3 Figure 4 identifies compound 12 as bound to IRAK4 (PDB ID: 9PSU). Table 2 prints compound 12 IRAK4 IC50 as 0.84 nM, with the footnote defining biochemical IRAK4 inhibition at 500 μM ATP. auto_single_measurement only accepted activity measurement [1] 1 structures\9PSU\9PSU_metadata.json point structures/9PSU/9psu_protein.pdb structures/9PSU/9psu_pocket.pdb structures/9PSU/9psu_ligand.sdf structures/9PSU/9psu_ligand.pdb structures/9PSU/9psu_ligand.cif structures/9PSU/9psu_complex.pdb structures/9PSU/9psu_complex.cif 9PUA classic recombinant streptavidin (SA) Na recombinant streptavidin (SA) Na L-(-)-biotin "[""A1CK6""]" 1 Kd Kd = = 8.0 ± 0.32 × 10^-6 M 8000.0 [] unit_conversion 5.096910013008056 success True direct_binding Isothermal titration calorimetry (ITC), mismatched recombinant SA/(−)-biotin interaction. 5 Table 1 reports the mismatched interaction of (−)-biotin with Rec SA: KD = 8.0 ± 0.32 × 10^-6 M. The text identifies the measurement as ITC, and the page maps PDB 9PUA to recombinant SA with (−)-biotin. auto_single_measurement only accepted activity measurement [1] 1 structures\9PUA\9PUA_metadata.json point structures/9PUA/9pua_protein.pdb structures/9PUA/9pua_pocket.pdb structures/9PUA/9pua_ligand.sdf structures/9PUA/9pua_ligand.pdb structures/9PUA/9pua_ligand.cif structures/9PUA/9pua_complex.pdb structures/9PUA/9pua_complex.cif 9PW7 classic Mcl-1 Na Na Na compound 13 "[""A1CL6""]" 1 Ki Ki = = 0.08 ± 0.02 nM 0.08 [] unit_conversion 10.096910013008056 success True direct_binding TR-FRET Mcl-1 binding assay; Ki measured in the presence of 1% fetal bovine serum. 4 Figure 3 prints for compound 13: “TRFRET: 0.08 ± 0.02 nM”; its caption identifies this as TR-FRET binding affinity to Mcl-1, Ki measured in 1% fetal bovine serum. auto_single_measurement only accepted activity measurement [1] 1 structures\9PW7\9PW7_metadata.json point structures/9PW7/9pw7_protein.pdb structures/9PW7/9pw7_pocket.pdb structures/9PW7/9pw7_ligand.sdf structures/9PW7/9pw7_ligand.pdb structures/9PW7/9pw7_ligand.cif structures/9PW7/9pw7_complex.pdb structures/9PW7/9pw7_complex.cif 9Q1F classic SmSTING Salpingoeca macrocollata C-terminal cyclic dinucleotide-binding domain fused to N-terminal T4 lysozyme Na 2'3'-cGAMP "[""1SY""]" 1 Kd Kd = = 2.5 μM 2500.0 [] unit_conversion 5.6020599913279625 success True direct_binding Electrophoretic mobility shift assay of purified SmSTING cyclic dinucleotide-binding domain binding 2'3'-cGAMP; nonlinear regression of the binding curve. 4 The text reports that SmSTING forms a stable complex with 2'3'-cGAMP with low-micromolar binding affinity of ~2.5 μM; Fig. 2c prints K_D = 2.5 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9Q1F\9Q1F_metadata.json point structures/9Q1F/9q1f_protein.pdb structures/9Q1F/9q1f_pocket.pdb structures/9Q1F/9q1f_ligand.sdf structures/9Q1F/9q1f_ligand.pdb structures/9Q1F/9q1f_ligand.cif structures/9Q1F/9q1f_complex.pdb structures/9Q1F/9q1f_complex.cif 9Q1G extended BLIMP-1 Na Na Na compound 5 "[""A1CNQ""]" 1 Kd Kd = = 6.6 µM 6600.0 [] unit_conversion 5.180456064458131 success True direct_binding SPR on Biacore T200; KD globally fitted with a 1:1 binding model. 2 Table 1 reports compound 5, BLIMP-1 Kd 6.6 µM. The text identifies the SPR assay as determining PR-domain binding affinity and identifies compound 5 as the crystallographic ligand. auto_single_measurement only accepted activity measurement [1] 1 structures\9Q1G\9Q1G_metadata.json point structures/9Q1G/9q1g_protein.pdb structures/9Q1G/9q1g_pocket.pdb structures/9Q1G/9q1g_ligand.pdb structures/9Q1G/9q1g_ligand.cif structures/9Q1G/9q1g_complex.pdb structures/9Q1G/9q1g_complex.cif 9Q5X classic human prolyl endopeptidase (PREP) human Na Na KT-2-74 (compound 1) "[""A1CQT""]" 1 IC50 IC50 = = 6 µM 6000.0 [] unit_conversion 5.221848749616356 success True biochemical_inhibition Fluorogenic Z-GP-AMC cleavage after 30 min preincubation. 3 Figure 2 reports compound 1 IC50 = 6 µM; the caption specifies recombinant human PREP activity. auto_single_measurement only accepted activity measurement [1] 1 structures\9Q5X\9Q5X_metadata.json point structures/9Q5X/9q5x_protein.pdb structures/9Q5X/9q5x_pocket.pdb structures/9Q5X/9q5x_ligand.sdf structures/9Q5X/9q5x_ligand.pdb structures/9Q5X/9q5x_ligand.cif structures/9Q5X/9q5x_complex.pdb structures/9Q5X/9q5x_complex.cif 9Q5Y classic human prolyl endopeptidase (PREP) human Na Na YX45 (CPzP-11) "[""A1CQR""]" 1 IC50 IC50 = = 2.3 µM 2300.0 [] unit_conversion 5.638272163982407 success True biochemical_inhibition PREP inhibition; noncovalent CPzP-11 complex. 2 Figure 1 labels CPzP-11 as noncovalent and reports IC50 = 2.3 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9Q5Y\9Q5Y_metadata.json point structures/9Q5Y/9q5y_protein.pdb structures/9Q5Y/9q5y_pocket.pdb structures/9Q5Y/9q5y_ligand.sdf structures/9Q5Y/9q5y_ligand.pdb structures/9Q5Y/9q5y_ligand.cif structures/9Q5Y/9q5y_complex.pdb structures/9Q5Y/9q5y_complex.cif 9Q5Z classic human prolyl endopeptidase (PREP) human Na Na KT-1-147 (CPzP-15) "[""A1CQS""]" 2 Ki Ki = = 18 µM 18000.0 [] unit_conversion 4.7447274948966935 success True biochemical_inhibition PREP inhibition kinetic characterization of covalent CPzP-15. 2 Figure 1 reports CPzP-15 Ki = 18 µM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9Q5Z\9Q5Z_metadata.json point structures/9Q5Z/9q5z_protein.pdb structures/9Q5Z/9q5z_pocket.pdb structures/9Q5Z/9q5z_ligand.sdf structures/9Q5Z/9q5z_ligand.pdb structures/9Q5Z/9q5z_ligand.cif structures/9Q5Z/9q5z_complex.pdb structures/9Q5Z/9q5z_complex.cif 9QA0 extended Drosophila melanogaster angiotensin converting enzyme homologue, AnCE Drosophila melanogaster Na Na IW dipeptide "[""CHAIN:B"", ""CHAIN:D""]" 2 Ki Ki = = 0.08 mM 80000.0 [] unit_conversion 4.096910013008056 success True biochemical_inhibition Purified AnCE fluorogenic substrate inhibition assay; Ki obtained using the Cheng–Prusoff equation. 4 Table 1 reports IW Ki = 0.08 mM for AnCE; Table 2 maps AnCE_IW to PDB 9QA0. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9QA0\9QA0_metadata.json point structures/9QA0/9qa0_protein.pdb structures/9QA0/9qa0_pocket.pdb structures/9QA0/9qa0_ligand.pdb structures/9QA0/9qa0_ligand.cif structures/9QA0/9qa0_complex.pdb structures/9QA0/9qa0_complex.cif 9QA1 extended Drosophila melanogaster angiotensin converting enzyme homologue, AnCE Drosophila melanogaster Na Na VW dipeptide "[""CHAIN:B"", ""CHAIN:D""]" 2 Ki Ki = = 0.17 mM 170000.0 [] unit_conversion 3.769551078621726 success True biochemical_inhibition Purified AnCE fluorogenic substrate inhibition assay; Ki obtained using the Cheng–Prusoff equation. 4 Table 1 reports VW Ki = 0.17 mM for AnCE; Table 2 maps AnCE_VW to PDB 9QA1. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9QA1\9QA1_metadata.json point structures/9QA1/9qa1_protein.pdb structures/9QA1/9qa1_pocket.pdb structures/9QA1/9qa1_ligand.pdb structures/9QA1/9qa1_ligand.cif structures/9QA1/9qa1_complex.pdb structures/9QA1/9qa1_complex.cif 9QA2 extended Drosophila melanogaster angiotensin converting enzyme homologue, AnCE Drosophila melanogaster Na Na RW dipeptide "[""POLYMER_ENTITY:1""]" 2 Ki Ki = = 0.20 mM 200000.0 [] unit_conversion 3.6989700043360187 success True biochemical_inhibition Purified AnCE fluorogenic substrate inhibition assay; Ki obtained using the Cheng–Prusoff equation. 4 Table 1 reports RW Ki = 0.20 mM for AnCE; Table 2 maps AnCE_RW to PDB 9QA2. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9QA2\9QA2_metadata.json point structures/9QA2/9qa2_protein.pdb structures/9QA2/9qa2_pocket.pdb structures/9QA2/9qa2_ligand.pdb structures/9QA2/9qa2_ligand.cif structures/9QA2/9qa2_complex.pdb structures/9QA2/9qa2_complex.cif 9QA3 extended Drosophila melanogaster angiotensin converting enzyme homologue, AnCE Drosophila melanogaster Na Na YW dipeptide "[""CHAIN:B"", ""CHAIN:D""]" 2 Ki Ki = = 0.75 mM 750000.0 [] unit_conversion 3.1249387366083 success True biochemical_inhibition Purified AnCE fluorogenic substrate inhibition assay; Ki obtained using the Cheng–Prusoff equation. 4 Table 1 reports YW Ki = 0.75 mM for AnCE; Table 2 maps AnCE_YW to PDB 9QA3. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9QA3\9QA3_metadata.json point structures/9QA3/9qa3_protein.pdb structures/9QA3/9qa3_pocket.pdb structures/9QA3/9qa3_ligand.pdb structures/9QA3/9qa3_ligand.cif structures/9QA3/9qa3_complex.pdb structures/9QA3/9qa3_complex.cif 9QA4 extended Drosophila melanogaster angiotensin converting enzyme homologue, AnCE Drosophila melanogaster Na Na WR dipeptide "[""CHAIN:B"", ""CHAIN:C""]" 2 Ki Ki = = 0.84 mM 840000.0 [] unit_conversion 3.075720713938118 success True biochemical_inhibition Purified AnCE fluorogenic substrate inhibition assay; Ki obtained using the Cheng–Prusoff equation. 4 Table 1 reports WR Ki = 0.84 mM for AnCE; Table 2 maps AnCE_WR to PDB 9QA4. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9QA4\9QA4_metadata.json point structures/9QA4/9qa4_protein.pdb structures/9QA4/9qa4_pocket.pdb structures/9QA4/9qa4_ligand.pdb structures/9QA4/9qa4_ligand.cif structures/9QA4/9qa4_complex.pdb structures/9QA4/9qa4_complex.cif 9QAC extended SMARCA2 Na Na Na compound 5 "[""A1I5P""]" 1 Kd Kd = = 31.7 µM 31700.0 [] unit_conversion 4.498940737782249 success True direct_binding SPR measurement of compound 5 binding to SMARCA2. 2 Compound 5 was confirmed as a validated hit with an SPR K_D of 31.7 µM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9QAC\9QAC_metadata.json point structures/9QAC/9qac_protein.pdb structures/9QAC/9qac_pocket.pdb structures/9QAC/9qac_ligand.pdb structures/9QAC/9qac_ligand.cif structures/9QAC/9qac_complex.pdb structures/9QAC/9qac_complex.cif 9QAD extended SMARCA2 Na Na Na compound 17 "[""A1I45""]" 1 IC50 IC50 = = 0.083 µM 83.0 [] unit_conversion 7.080921907623926 success True biochemical_inhibition TR-FRET binding assay. 3 Table 2 reports S2 TRF IC50 of 0.083 µM for compound 17; the footnote identifies S2 as SMARCA2. auto_single_measurement only accepted activity measurement [1] 1 structures\9QAD\9QAD_metadata.json point structures/9QAD/9qad_protein.pdb structures/9QAD/9qad_pocket.pdb structures/9QAD/9qad_ligand.pdb structures/9QAD/9qad_ligand.cif structures/9QAD/9qad_complex.pdb structures/9QAD/9qad_complex.cif 9QAM classic human angiotensin I-converting enzyme (ACE) Human cACE Ser-1 to Pro-633 Na ciprofloxacin (Cip1); ciprofloxacin (Cip2) "[""CPF""]" 2 Ki Ki = = 33.8 μM 33800.0 [] unit_conversion 4.471083299722345 success True biochemical_inhibition Purified soluble cACE Z-FHL peptide-cleavage inhibition assay; Ki calculated from the measured IC50 using the Cheng–Prusoff equation. 3 “inhibition was observed for cACE, with an IC50 of 202.7 μM and a Ki of 33.8 μM.” auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9QAM\9QAM_metadata.json point structures/9QAM/9qam_protein.pdb structures/9QAM/9qam_pocket.pdb structures/9QAM/9qam_ligand.sdf structures/9QAM/9qam_ligand.pdb structures/9QAM/9qam_ligand.cif structures/9QAM/9qam_complex.pdb structures/9QAM/9qam_complex.cif 9QB4 extended Yeast 20S proteasome Saccharomyces cerevisiae yCP beta5-T3M:carfilzomib beta5 T3M Carfilzomib "[""POLYMER_ENTITY:15""]" 1 IC50 IC50 = = 0.411 ± 0.079 µM 411.0 [] unit_conversion 6.386158178123931 success True biochemical_inhibition Purified mutant yeast core particles; β5 chymotrypsin-like activity inhibited with carfilzomib; IC50 fitted from residual-activity curve. 5 Figure 2C prints yCP-β5-T3M carfilzomib IC50 0.411 ± 0.079 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QB4\9QB4_metadata.json point structures/9QB4/9qb4_protein.pdb structures/9QB4/9qb4_pocket.pdb structures/9QB4/9qb4_ligand.pdb structures/9QB4/9qb4_ligand.cif structures/9QB4/9qb4_complex.pdb structures/9QB4/9qb4_complex.cif 9QBR classic lysyl-tRNA synthetase (LysRS) Mycobacterium tuberculosis Na Na compound 27 / DDD01991231 "[""A1I5H""]" 1 IC50 IC50 = = 0.4 μM 400.0 [] unit_conversion 6.3979400086720375 success True biochemical_inhibition LysRS enzymatic inhibition assay; Table 3. 6 Table 3 reports compound 27 LysRS IC50 = 0.4 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QBR\9QBR_metadata.json point structures/9QBR/9qbr_protein.pdb structures/9QBR/9qbr_pocket.pdb structures/9QBR/9qbr_ligand.sdf structures/9QBR/9qbr_ligand.pdb structures/9QBR/9qbr_ligand.cif structures/9QBR/9qbr_complex.pdb structures/9QBR/9qbr_complex.cif 9QC3 classic lysyl-tRNA synthetase (LysRS) Mycobacterium tuberculosis Na Na compound 37 / DDD01993593 "[""A1I50""]" 1 IC50 IC50 = = 0.1 μM 100.0 [] unit_conversion 7.0 success True biochemical_inhibition LysRS enzymatic inhibition assay; Table 3. 6 Table 3 reports compound 37 LysRS IC50 = 0.1 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QC3\9QC3_metadata.json point structures/9QC3/9qc3_protein.pdb structures/9QC3/9qc3_pocket.pdb structures/9QC3/9qc3_ligand.sdf structures/9QC3/9qc3_ligand.pdb structures/9QC3/9qc3_ligand.cif structures/9QC3/9qc3_complex.pdb structures/9QC3/9qc3_complex.cif 9QC4 classic lysyl-tRNA synthetase (LysRS) Mycobacterium tuberculosis Na Na compound 42 / DDD01869767 "[""A1I5Z""]" 1 IC50 IC50 = = 1.5 μM 1500.0 [] unit_conversion 5.823908740944319 success True biochemical_inhibition LysRS enzymatic inhibition assay; Table 4. 8 Table 4 reports compound 42 LysRS IC50 = 1.5 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QC4\9QC4_metadata.json point structures/9QC4/9qc4_protein.pdb structures/9QC4/9qc4_pocket.pdb structures/9QC4/9qc4_ligand.sdf structures/9QC4/9qc4_ligand.pdb structures/9QC4/9qc4_ligand.cif structures/9QC4/9qc4_complex.pdb structures/9QC4/9qc4_complex.cif 9QCD extended SHP2 Na N-SH2-C-SH2 tandem domain, residues 1-222, in complex with bis-phosphorylated pY627-pY659-Gab1 peptide Na bis-phosphorylated pY627-pY659-Gab1 peptide (title: 613-694; paper structure/model: 617-684) "[""CHAIN:C""]" 1 Kd Kd = = 37 ± 13 nM 37.0 [] unit_conversion 7.431798275933005 success True direct_binding ITC of tandem SH2 domain with bis-phosphorylated Gab1 peptide. 4 Figure 2 reports Kd = 37 ± 13 nM for SHP2(1-222):Gab1(613-694); the Figure 2 legend identifies this as the bis-phosphorylated pY627pY659-Gab1 peptide. auto_single_measurement only accepted activity measurement [1] 1 structures\9QCD\9QCD_metadata.json point structures/9QCD/9qcd_protein.pdb structures/9QCD/9qcd_pocket.pdb structures/9QCD/9qcd_ligand.pdb structures/9QCD/9qcd_ligand.cif structures/9QCD/9qcd_complex.pdb structures/9QCD/9qcd_complex.cif 9QD7 classic FKBP51 Na Na Na 15a "[""A1I5X""]" 1 Kd Kd = = 0.51 ± 0.03 μM 510.0 [] unit_conversion 6.292429823902063 success True direct_binding Competitive fluorescence-polarization (FP) binding assay. 3 Table 1 reports FKBP51 K_D = 0.51 ± 0.03 μM for para-series compound 15a; Figure 2 maps 15a to PDB 9QD7. auto_single_measurement only accepted activity measurement [1] 1 structures\9QD7\9QD7_metadata.json point structures/9QD7/9qd7_protein.pdb structures/9QD7/9qd7_pocket.pdb structures/9QD7/9qd7_ligand.sdf structures/9QD7/9qd7_ligand.pdb structures/9QD7/9qd7_ligand.cif structures/9QD7/9qd7_complex.pdb structures/9QD7/9qd7_complex.cif 9QD8 classic FKBP51 Na Na Na 29a "[""A1I53""]" 1 Kd Kd = = 50 ± 5 nM 50.0 [] unit_conversion 7.301029995663981 success True direct_binding Competitive fluorescence-polarization (FP) binding assay. 3 Figure 2 labels compound 29a K_D = 50 ± 5 nM; its caption maps 29a to PDB 9QD8, and the page states final compounds were measured by competitive FP. auto_single_measurement only accepted activity measurement [1] 1 structures\9QD8\9QD8_metadata.json point structures/9QD8/9qd8_protein.pdb structures/9QD8/9qd8_pocket.pdb structures/9QD8/9qd8_ligand.sdf structures/9QD8/9qd8_ligand.pdb structures/9QD8/9qd8_ligand.cif structures/9QD8/9qd8_complex.pdb structures/9QD8/9qd8_complex.cif 9QD9 classic FKBP51 Na Na Na 29c "[""A1I54""]" 1 Kd Kd = = 191 ± 16 nM 191.0 [] unit_conversion 6.718966632752272 success True direct_binding Competitive fluorescence-polarization (FP) binding assay. 3 Figure 2 labels compound 29c K_D = 191 ± 16 nM; its caption maps 29c to PDB 9QD9, and the page states final compounds were measured by competitive FP. auto_single_measurement only accepted activity measurement [1] 1 structures\9QD9\9QD9_metadata.json point structures/9QD9/9qd9_protein.pdb structures/9QD9/9qd9_pocket.pdb structures/9QD9/9qd9_ligand.sdf structures/9QD9/9qd9_ligand.pdb structures/9QD9/9qd9_ligand.cif structures/9QD9/9qd9_complex.pdb structures/9QD9/9qd9_complex.cif 9QDA classic FKBP51 Na Na Na 29b "[""A1I55""]" 1 Kd Kd = = 567 ± 64 nM 567.0 [] unit_conversion 6.246416941107094 success True direct_binding Competitive fluorescence-polarization (FP) binding assay. 3 Figure 2 labels compound 29b K_D = 567 ± 64 nM; its caption maps 29b to PDB 9QDA, and the page states final compounds were measured by competitive FP. auto_single_measurement only accepted activity measurement [1] 1 structures\9QDA\9QDA_metadata.json point structures/9QDA/9qda_protein.pdb structures/9QDA/9qda_pocket.pdb structures/9QDA/9qda_ligand.sdf structures/9QDA/9qda_ligand.pdb structures/9QDA/9qda_ligand.cif structures/9QDA/9qda_complex.pdb structures/9QDA/9qda_complex.cif 9QDB classic FKBP51 Na Na Na 29d "[""A1I5Y""]" 1 Kd Kd = = 605 ± 77 nM 605.0 [] unit_conversion 6.2182446253475305 success True direct_binding Competitive fluorescence-polarization (FP) binding assay. 3 Figure 2 labels compound 29d K_D = 605 ± 77 nM; its caption maps 29d to PDB 9QDB, and the page states final compounds were measured by competitive FP. auto_single_measurement only accepted activity measurement [1] 1 structures\9QDB\9QDB_metadata.json point structures/9QDB/9qdb_protein.pdb structures/9QDB/9qdb_pocket.pdb structures/9QDB/9qdb_ligand.sdf structures/9QDB/9qdb_ligand.pdb structures/9QDB/9qdb_ligand.cif structures/9QDB/9qdb_complex.pdb structures/9QDB/9qdb_complex.cif 9QDJ classic lysyl-tRNA synthetase (LysRS) Mycobacterium tuberculosis Na Na compound 32 / DDD018870911 "[""A1I60""]" 1 IC50 IC50 = = 0.2 μM 200.0 [] unit_conversion 6.698970004336019 success True biochemical_inhibition LysRS enzymatic inhibition assay; Table 3. 6 Table 3 reports compound 32 LysRS IC50 = 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QDJ\9QDJ_metadata.json point structures/9QDJ/9qdj_protein.pdb structures/9QDJ/9qdj_pocket.pdb structures/9QDJ/9qdj_ligand.sdf structures/9QDJ/9qdj_ligand.pdb structures/9QDJ/9qdj_ligand.cif structures/9QDJ/9qdj_complex.pdb structures/9QDJ/9qdj_complex.cif 9QDM classic Saccharomyces cerevisiae respiratory complex II (succinate dehydrogenase) Saccharomyces cerevisiae W303-1B-derived yeast strain with a C-terminal 10-histidine tag on Sdh4 preceded by a GARGS linker Na Bixafen (A116X) "[""A1I6X""]" 1 IC50 IC50 < < 0.5 µM 500.0 [] unit_conversion 6.301029995663981 success True biochemical_inhibition Purified CII assayed by DCPIP electron-transfer activity with 5 mM succinate; bixafen targeting the quinone-binding site produced complete inhibition. The IC50 was estimated to be slightly below 0.5 µM. 2 “The IC50 of bixafen on the purified CII preparation was estimated to be slightly below 0.5 µM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9QDM\9QDM_metadata.json point structures/9QDM/9qdm_protein.pdb structures/9QDM/9qdm_pocket.pdb structures/9QDM/9qdm_ligand.sdf structures/9QDM/9qdm_ligand.pdb structures/9QDM/9qdm_ligand.cif structures/9QDM/9qdm_complex.pdb structures/9QDM/9qdm_complex.cif 9QE4 classic VCB (VHL-Elongin B-Elongin C complex) Na VHL residues 54-213 with an N-terminal TEV-cleavable TwinStrep-tag; Elongin B residues 1-104; Elongin C residues 17-112 Na VHL-binding compound 114 "[""A1I57""]" 1 Kd Kd = = 59 ± 5 nM 59.0 [] unit_conversion 7.229147988357855 success True direct_binding Spectral-shift determination of the dissociation constant of VHL ligand 114 with the VCB complex. 5 Figure 2 identifies VCB complexed with 114 as PDB 9QE4 and prints K_D = 59 ± 5 nM for compound 114. auto_single_measurement only accepted activity measurement [1] 1 structures\9QE4\9QE4_metadata.json point structures/9QE4/9qe4_protein.pdb structures/9QE4/9qe4_pocket.pdb structures/9QE4/9qe4_ligand.sdf structures/9QE4/9qe4_ligand.pdb structures/9QE4/9qe4_ligand.cif structures/9QE4/9qe4_complex.pdb structures/9QE4/9qe4_complex.cif 9QE5 classic VCB (VHL-Elongin B-Elongin C complex) Na VHL residues 54-213 with an N-terminal TEV-cleavable TwinStrep-tag; Elongin B residues 1-104; Elongin C residues 17-112 Na VHL-binding compound 82 "[""A1I58""]" 1 Kd Kd = = 70 ± 2 nM 70.0 [] unit_conversion 7.154901959985743 success True direct_binding Spectral-shift determination of the dissociation constant of VHL ligand 82 with the VCB complex. 5 Figure 2 identifies VCB complexed with 82 as PDB 9QE5 and prints K_D = 70 ± 2 nM for compound 82. auto_single_measurement only accepted activity measurement [1] 1 structures\9QE5\9QE5_metadata.json point structures/9QE5/9qe5_protein.pdb structures/9QE5/9qe5_pocket.pdb structures/9QE5/9qe5_ligand.sdf structures/9QE5/9qe5_ligand.pdb structures/9QE5/9qe5_ligand.cif structures/9QE5/9qe5_complex.pdb structures/9QE5/9qe5_complex.cif 9QEA classic lysyl-tRNA synthetase (LysRS) Mycobacterium tuberculosis Na Na compound 10 / DDD01839469 "[""A1I61""]" 1 IC50 IC50 = = 0.2 μM 200.0 [] unit_conversion 6.698970004336019 success True biochemical_inhibition LysRS enzymatic inhibition assay; Table 2. 4 Table 2 reports compound 10 LysRS IC50 = 0.2 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QEA\9QEA_metadata.json point structures/9QEA/9qea_protein.pdb structures/9QEA/9qea_pocket.pdb structures/9QEA/9qea_ligand.sdf structures/9QEA/9qea_ligand.pdb structures/9QEA/9qea_ligand.cif structures/9QEA/9qea_complex.pdb structures/9QEA/9qea_complex.cif 9QEI classic lysyl-tRNA synthetase (LysRS) Mycobacterium tuberculosis Na Na compound 25 / DDD01866774 "[""A1I62""]" 1 IC50 IC50 = = 0.3 μM 300.0 [] unit_conversion 6.522878745280337 success True biochemical_inhibition LysRS enzymatic inhibition assay; Table 3. 6 Table 3 reports compound 25 LysRS IC50 = 0.3 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QEI\9QEI_metadata.json point structures/9QEI/9qei_protein.pdb structures/9QEI/9qei_pocket.pdb structures/9QEI/9qei_ligand.sdf structures/9QEI/9qei_ligand.pdb structures/9QEI/9qei_ligand.cif structures/9QEI/9qei_complex.pdb structures/9QEI/9qei_complex.cif 9QEL classic YTHDF2 Na Na Na compound 4 (AI-DF2-13) "[""S76""]" 1 IC50 IC50 = = 250 µM 250000.0 [] unit_conversion 3.6020599913279625 success True biochemical_inhibition HTRF-based competitive binding assay; DF2 reader-domain IC50 determined by dose-response. 3 Table 1 maps compound 4 to PDB 9QEL and reports DF2 IC50 250 µM; the table notes define the IC50 determination for the DF2 reader domain. auto_single_measurement only accepted activity measurement [1] 1 structures\9QEL\9QEL_metadata.json point structures/9QEL/9qel_protein.pdb structures/9QEL/9qel_pocket.pdb structures/9QEL/9qel_ligand.sdf structures/9QEL/9qel_ligand.pdb structures/9QEL/9qel_ligand.cif structures/9QEL/9qel_complex.pdb structures/9QEL/9qel_complex.cif 9QF1 extended CHIP E3 ubiquitin ligase TPR domain Na Na Na compound 2 "[""A1I5T""]" 2 Kd Kd = = 60 µM 60000.0 [] unit_conversion 4.221848749616356 success True direct_binding 2D NMR binding measurement. 2 Figure 1 reports “CHIP NMR Kd = 60 µM” for compound 2. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\9QF1\9QF1_metadata.json point structures/9QF1/9qf1_protein.pdb structures/9QF1/9qf1_pocket.pdb structures/9QF1/9qf1_ligand.pdb structures/9QF1/9qf1_ligand.cif structures/9QF1/9qf1_complex.pdb structures/9QF1/9qf1_complex.cif 9QFL extended YTHDF2 Na Na Na compound 15 (AI-DF2-68) "[""A1I5U""]" 1 IC50 IC50 = = 86 µM 86000.0 [] unit_conversion 4.0655015487564325 success True biochemical_inhibition HTRF-based competitive binding assay; DF2 reader-domain IC50 determined by dose-response. 3 Table 1 maps compound 15 to PDB 9QFL and reports DF2 IC50 86 µM; the table notes define the IC50 determination for the DF2 reader domain. auto_single_measurement only accepted activity measurement [1] 1 structures\9QFL\9QFL_metadata.json point structures/9QFL/9qfl_protein.pdb structures/9QFL/9qfl_pocket.pdb structures/9QFL/9qfl_ligand.pdb structures/9QFL/9qfl_ligand.cif structures/9QFL/9qfl_complex.pdb structures/9QFL/9qfl_complex.cif 9QIU classic YTHDF2 Na Na Na compound 13 (AI-DF2-56) "[""A1IR4""]" 1 IC50 IC50 = = 53 µM 53000.0 [] unit_conversion 4.275724130399211 success True biochemical_inhibition HTRF-based competitive binding assay; DF2 reader-domain IC50 determined by dose-response. 3 Table 1 maps compound 13 to PDB 9QIU and reports DF2 IC50 53 µM; the table notes define the IC50 determination for the DF2 reader domain. auto_single_measurement only accepted activity measurement [1] 1 structures\9QIU\9QIU_metadata.json point structures/9QIU/9qiu_protein.pdb structures/9QIU/9qiu_pocket.pdb structures/9QIU/9qiu_ligand.sdf structures/9QIU/9qiu_ligand.pdb structures/9QIU/9qiu_ligand.cif structures/9QIU/9qiu_complex.pdb structures/9QIU/9qiu_complex.cif 9QK3 classic SlPYL1 Solanum lycopersicum Na Na Coumaric acid (COU) "[""HC4""]" 1 Kd Kd = = 0.93 mM 930000.0 [] unit_conversion 3.031517051446065 success True direct_binding Fluorescence spectral-shift binding assay using Monolith X; binary SlPYL1–COU binding; performed in duplicates. Printed confidence interval: 0.54–1.61 mM. 6 Fig. 2B reports CsPYL1 Kd (mM): ABA 0.12, COU 0.93, CAF 2.75, FER 0.59; page 5 states these Kd values were measured by spectral-shift analysis. Page 9 maps COU to PDB 9QK3. auto_single_measurement only accepted activity measurement [1] 1 structures\9QK3\9QK3_metadata.json point structures/9QK3/9qk3_protein.pdb structures/9QK3/9qk3_pocket.pdb structures/9QK3/9qk3_ligand.sdf structures/9QK3/9qk3_ligand.pdb structures/9QK3/9qk3_ligand.cif structures/9QK3/9qk3_complex.pdb structures/9QK3/9qk3_complex.cif 9QK4 classic SlPYL1 Solanum lycopersicum Na Na Ferulic acid (FER) "[""FER""]" 1 Kd Kd = = 0.59 mM 590000.0 [] unit_conversion 3.229147988357856 success True direct_binding Fluorescence spectral-shift binding assay using Monolith X; binary SlPYL1–FER binding; performed in duplicates. Printed confidence interval: 0.26–1.17 mM. 6 Fig. 2B reports CsPYL1 Kd (mM): ABA 0.12, COU 0.93, CAF 2.75, FER 0.59; page 5 states these Kd values were measured by spectral-shift analysis. Page 9 maps FER to PDB 9QK4. auto_single_measurement only accepted activity measurement [1] 1 structures\9QK4\9QK4_metadata.json point structures/9QK4/9qk4_protein.pdb structures/9QK4/9qk4_pocket.pdb structures/9QK4/9qk4_ligand.sdf structures/9QK4/9qk4_ligand.pdb structures/9QK4/9qk4_ligand.cif structures/9QK4/9qk4_complex.pdb structures/9QK4/9qk4_complex.cif 9QK5 classic SlPYL1 Solanum lycopersicum Na Na Caffeic acid (CAF) "[""DHC""]" 1 Kd Kd = = 2.75 mM 2750000.0 [] unit_conversion 2.560667306169737 success True direct_binding Fluorescence spectral-shift binding assay using Monolith X; binary SlPYL1–CAF binding; performed in duplicates. Printed confidence interval: 1.48–5.10 mM. 6 Fig. 2B reports CsPYL1 Kd (mM): ABA 0.12, COU 0.93, CAF 2.75, FER 0.59; page 5 states these Kd values were measured by spectral-shift analysis. Page 9 maps CAF to PDB 9QK5. auto_single_measurement only accepted activity measurement [1] 1 structures\9QK5\9QK5_metadata.json point structures/9QK5/9qk5_protein.pdb structures/9QK5/9qk5_pocket.pdb structures/9QK5/9qk5_ligand.sdf structures/9QK5/9qk5_ligand.pdb structures/9QK5/9qk5_ligand.cif structures/9QK5/9qk5_complex.pdb structures/9QK5/9qk5_complex.cif 9QK6 classic SlPYL1 Solanum lycopersicum Na Na Feruloylphenylalanine (FER-Phe) "[""A1I70""]" 1 Kd Kd = = 0.063 mM 63000.0 [] unit_conversion 4.200659450546418 success True direct_binding Fluorescence spectral-shift binding assay using Monolith X; binary SlPYL1–FER-Phe binding; performed in duplicates. Printed confidence interval: 0.025–0.158 mM. 7 Fig. 3B reports CsPYL1 Kd for FER-Phe as 0.063 mM; Fig. 3 caption states these values were determined by fluorescence spectral shift using Monolith X and performed in duplicates. Page 9 maps FER-Phe to PDB 9QK6. auto_single_measurement only accepted activity measurement [1] 1 structures\9QK6\9QK6_metadata.json point structures/9QK6/9qk6_protein.pdb structures/9QK6/9qk6_pocket.pdb structures/9QK6/9qk6_ligand.sdf structures/9QK6/9qk6_ligand.pdb structures/9QK6/9qk6_ligand.cif structures/9QK6/9qk6_complex.pdb structures/9QK6/9qk6_complex.cif 9QOD extended APH(2'')-IVa Enterococcus casseliflavus Na Na 83 "[""A1I8B""]" 3 Kd Kd = = 1.06 ± 0.17 µM 1060.0 [] unit_conversion 5.97469413473523 success True direct_binding Isothermal titration calorimetry; n = 3. 8 “Kd values of 1.06 ± 0.17 µM (n = 3) for APH(2'')-IVa”. auto_metric_priority unique highest-priority metric family: Kd [3] 3 structures\9QOD\9QOD_metadata.json point structures/9QOD/9qod_protein.pdb structures/9QOD/9qod_pocket.pdb structures/9QOD/9qod_ligand.pdb structures/9QOD/9qod_ligand.cif structures/9QOD/9qod_complex.pdb structures/9QOD/9qod_complex.cif 9QOR classic APH(2'')-IVa Na Na Na compound 19 "[""A1I8H""]" 1 Ki Ki = = 20000 ± 2100 nM 20000.0 [] unit_conversion 4.698970004336019 success True biochemical_inhibition APH(2'')-IVa enzyme-kinetic inhibition assay. 4 The deposited ligand structure uniquely matches compound 19 in Table 1, which reports Ki 20000 ± 2100 nM and the matching 2.44 Å crystal resolution. auto_single_measurement only accepted activity measurement [1] 1 structures\9QOR\9QOR_metadata.json point structures/9QOR/9qor_protein.pdb structures/9QOR/9qor_pocket.pdb structures/9QOR/9qor_ligand.sdf structures/9QOR/9qor_ligand.pdb structures/9QOR/9qor_ligand.cif structures/9QOR/9qor_complex.pdb structures/9QOR/9qor_complex.cif 9QOS classic APH(3')-IIb Pseudomonas aeruginosa Na Na 83 "[""A1I8B""]" 2 Kd Kd = = 0.27 ± 0.05 µM 270.0 [] unit_conversion 6.568636235841012 success True direct_binding Isothermal titration calorimetry; n = 2. 8 “Kd values of ... 0.27 ± 0.05 µM (n = 2) for APH(3')-IIb.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9QOS\9QOS_metadata.json point structures/9QOS/9qos_protein.pdb structures/9QOS/9qos_pocket.pdb structures/9QOS/9qos_ligand.sdf structures/9QOS/9qos_ligand.pdb structures/9QOS/9qos_ligand.cif structures/9QOS/9qos_complex.pdb structures/9QOS/9qos_complex.cif 9QOU classic APH(2'')-IVa Na Na Na 14k "[""A1I8O""]" 1 Ki Ki = = 6,500 ± 400 nM 6500.0 [] unit_conversion 5.187086643357144 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 2. 6 Table 2 reports Ki = 6,500 ± 400 nM for 14k. auto_single_measurement only accepted activity measurement [1] 1 structures\9QOU\9QOU_metadata.json point structures/9QOU/9qou_protein.pdb structures/9QOU/9qou_pocket.pdb structures/9QOU/9qou_ligand.sdf structures/9QOU/9qou_ligand.pdb structures/9QOU/9qou_ligand.cif structures/9QOU/9qou_complex.pdb structures/9QOU/9qou_complex.cif 9QOW classic APH(2'')-IVa Na Na Na 14b "[""A1I8X""]" 1 Ki Ki = = 2,400 ± 320 nM 2400.0 [] unit_conversion 5.619788758288394 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 2. 6 Table 2 reports Ki = 2,400 ± 320 nM for 14b. auto_single_measurement only accepted activity measurement [1] 1 structures\9QOW\9QOW_metadata.json point structures/9QOW/9qow_protein.pdb structures/9QOW/9qow_pocket.pdb structures/9QOW/9qow_ligand.sdf structures/9QOW/9qow_ligand.pdb structures/9QOW/9qow_ligand.cif structures/9QOW/9qow_complex.pdb structures/9QOW/9qow_complex.cif 9QOX classic APH(2'')-IVa Na Na Na 14a "[""A1I8S""]" 1 Ki Ki = = 1,300 ± 55 nM 1300.0 [] unit_conversion 5.886056647693163 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 1. 4 Table 1 reports Ki = 1,300 ± 55 nM for 14a. auto_single_measurement only accepted activity measurement [1] 1 structures\9QOX\9QOX_metadata.json point structures/9QOX/9qox_protein.pdb structures/9QOX/9qox_pocket.pdb structures/9QOX/9qox_ligand.sdf structures/9QOX/9qox_ligand.pdb structures/9QOX/9qox_ligand.cif structures/9QOX/9qox_complex.pdb structures/9QOX/9qox_complex.cif 9QOZ classic APH(2'')-IVa Na Na Na 14f "[""A1I8T""]" 1 Ki Ki = = 916 ± 78 nM 916.0 [] unit_conversion 6.03810452633215 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 2. 6 Table 2 reports Ki = 916 ± 78 nM for 14f. auto_single_measurement only accepted activity measurement [1] 1 structures\9QOZ\9QOZ_metadata.json point structures/9QOZ/9qoz_protein.pdb structures/9QOZ/9qoz_pocket.pdb structures/9QOZ/9qoz_ligand.sdf structures/9QOZ/9qoz_ligand.pdb structures/9QOZ/9qoz_ligand.cif structures/9QOZ/9qoz_complex.pdb structures/9QOZ/9qoz_complex.cif 9QP0 extended APH(2'')-IVa Na Na Na 14c1 "[""A1I8U""]" 1 Ki Ki = = 325 ± 25 nM 325.0 [] unit_conversion 6.488116639021126 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 4. 9 Table 4 reports Ki = 325 ± 25 nM for 14c1. auto_single_measurement only accepted activity measurement [1] 1 structures\9QP0\9QP0_metadata.json point structures/9QP0/9qp0_protein.pdb structures/9QP0/9qp0_pocket.pdb structures/9QP0/9qp0_ligand.pdb structures/9QP0/9qp0_ligand.cif structures/9QP0/9qp0_complex.pdb structures/9QP0/9qp0_complex.cif 9QP1 extended APH(2'')-IVa Na Na Na 14c3 "[""A1I8V""]" 1 Ki Ki = = 375 ± 25 nM 375.0 [] unit_conversion 6.425968732272281 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 4. 9 Table 4 reports Ki = 375 ± 25 nM for 14c3. auto_single_measurement only accepted activity measurement [1] 1 structures\9QP1\9QP1_metadata.json point structures/9QP1/9qp1_protein.pdb structures/9QP1/9qp1_pocket.pdb structures/9QP1/9qp1_ligand.pdb structures/9QP1/9qp1_ligand.cif structures/9QP1/9qp1_complex.pdb structures/9QP1/9qp1_complex.cif 9QP2 extended APH(2'')-IVa Na Na Na 14c4 "[""A1I8W""]" 1 Ki Ki = = 367 ± 21 nM 367.0 [] unit_conversion 6.435333935747911 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 4. 9 Table 4 reports Ki = 367 ± 21 nM for 14c4. auto_single_measurement only accepted activity measurement [1] 1 structures\9QP2\9QP2_metadata.json point structures/9QP2/9qp2_protein.pdb structures/9QP2/9qp2_pocket.pdb structures/9QP2/9qp2_ligand.pdb structures/9QP2/9qp2_ligand.cif structures/9QP2/9qp2_complex.pdb structures/9QP2/9qp2_complex.cif 9QP3 classic APH(2'')-IVa Na Na Na 14c5 "[""A1I8Y""]" 1 Ki Ki = = 482 ± 36 nM 482.0 [] unit_conversion 6.31695296176115 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 4. 9 Table 4 reports Ki = 482 ± 36 nM for 14c5. auto_single_measurement only accepted activity measurement [1] 1 structures\9QP3\9QP3_metadata.json point structures/9QP3/9qp3_protein.pdb structures/9QP3/9qp3_pocket.pdb structures/9QP3/9qp3_ligand.sdf structures/9QP3/9qp3_ligand.pdb structures/9QP3/9qp3_ligand.cif structures/9QP3/9qp3_complex.pdb structures/9QP3/9qp3_complex.cif 9QP5 classic APH(2'')-IVa Na Na Na 14c6 "[""A1I8Z""]" 1 Ki Ki = = 348 ± 27 nM 348.0 [] unit_conversion 6.458420756053419 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 4. 9 Table 4 reports Ki = 348 ± 27 nM for 14c6. auto_single_measurement only accepted activity measurement [1] 1 structures\9QP5\9QP5_metadata.json point structures/9QP5/9qp5_protein.pdb structures/9QP5/9qp5_pocket.pdb structures/9QP5/9qp5_ligand.sdf structures/9QP5/9qp5_ligand.pdb structures/9QP5/9qp5_ligand.cif structures/9QP5/9qp5_complex.pdb structures/9QP5/9qp5_complex.cif 9QP6 extended APH(2'')-IVa Na Na Na 14b1 "[""A1I80""]" 1 Ki Ki = = 613 ± 76 nM 613.0 [] unit_conversion 6.212539525481585 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 4. 9 Table 4 reports Ki = 613 ± 76 nM for 14b1. auto_single_measurement only accepted activity measurement [1] 1 structures\9QP6\9QP6_metadata.json point structures/9QP6/9qp6_protein.pdb structures/9QP6/9qp6_pocket.pdb structures/9QP6/9qp6_ligand.pdb structures/9QP6/9qp6_ligand.cif structures/9QP6/9qp6_complex.pdb structures/9QP6/9qp6_complex.cif 9QP7 extended APH(2'')-IVa Na Na Na 14m "[""A1I81""]" 1 Ki Ki = = 479 ± 45 nM 479.0 [] unit_conversion 6.319664486585436 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 4. 9 Table 4 reports Ki = 479 ± 45 nM for 14m. auto_single_measurement only accepted activity measurement [1] 1 structures\9QP7\9QP7_metadata.json point structures/9QP7/9qp7_protein.pdb structures/9QP7/9qp7_pocket.pdb structures/9QP7/9qp7_ligand.pdb structures/9QP7/9qp7_ligand.cif structures/9QP7/9qp7_complex.pdb structures/9QP7/9qp7_complex.cif 9QPA extended APH(2'')-IVa Na Na Na 14n "[""A1I82""]" 1 Ki Ki = = 404 ± 35 nM 404.0 [] unit_conversion 6.393618634889394 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 4. 9 Table 4 reports Ki = 404 ± 35 nM for 14n. auto_single_measurement only accepted activity measurement [1] 1 structures\9QPA\9QPA_metadata.json point structures/9QPA/9qpa_protein.pdb structures/9QPA/9qpa_pocket.pdb structures/9QPA/9qpa_ligand.pdb structures/9QPA/9qpa_ligand.cif structures/9QPA/9qpa_complex.pdb structures/9QPA/9qpa_complex.cif 9QPC classic DNA polymerase PolC Enterococcus faecium full-length, exonuclease-inactivated PolC D431A+E433A ACX-801 "[""A1I88""]" 1 IC50 IC50 = = 5.8 ± 0.8 µM 5800.0 [] unit_conversion 5.236572006437063 success True biochemical_inhibition Real-time DNA primer-extension assay using purified exonuclease-inactivated E. faecium PolC; DNA substrate present; n=3. 2 Fig. 1e legend reports inhibition of exonuclease-inactivated E. faecium PolC by ACX-801, with derived IC50 values; the plotted value for ACX-801 is 5.8 ± 0.8 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QPC\9QPC_metadata.json point structures/9QPC/9qpc_protein.pdb structures/9QPC/9qpc_pocket.pdb structures/9QPC/9qpc_ligand.sdf structures/9QPC/9qpc_ligand.pdb structures/9QPC/9qpc_ligand.cif structures/9QPC/9qpc_complex.pdb structures/9QPC/9qpc_complex.cif 9QPX extended BRCA1 Na BRCA1 BRCT tandem repeat Na RNA polymerase II pSer5-CTD peptide (pS5 CTD peptide) "[""CHAIN:E"", ""CHAIN:F"", ""CHAIN:G""]" 1 Kd Kd = = 79.7 ± 2.7 µM 79700.0 [] unit_conversion 4.098541678603888 success True direct_binding Fluorescence anisotropy binding assay; BRCA1 BRCT domain titrated against pS5 CTD peptide at 25 °C. 7 Figure 3 identifies PDB 9QPX as BRCA1 BRCT bound to the pS5 CTD peptide; panel E reports BRCA1 BRCT w.t. with pS5, K_D 79.7 ± 2.7 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QPX\9QPX_metadata.json point structures/9QPX/9qpx_protein.pdb structures/9QPX/9qpx_pocket.pdb structures/9QPX/9qpx_ligand.pdb structures/9QPX/9qpx_ligand.cif structures/9QPX/9qpx_complex.pdb structures/9QPX/9qpx_complex.cif 9QRH classic CK2alpha human CK2alpha1A residues 1-337 wild-type Biv1 "[""A1I9M""]" 1 IC50 IC50 = = 180 ± 23 pM 0.18 [] unit_conversion 9.744727494896694 success True biochemical_inhibition ADP-Glo enzymatic assay with recombinant CK2α. 3 Table 1 reports Biv1 enzymology IC50 = 180 ± 23 pM; Fig. 2 maps Biv1 to PDB 9QRH. auto_single_measurement only accepted activity measurement [1] 1 structures\9QRH\9QRH_metadata.json point structures/9QRH/9qrh_protein.pdb structures/9QRH/9qrh_pocket.pdb structures/9QRH/9qrh_ligand.sdf structures/9QRH/9qrh_ligand.pdb structures/9QRH/9qrh_ligand.cif structures/9QRH/9qrh_complex.pdb structures/9QRH/9qrh_complex.cif 9QRI classic CK2alpha human CK2alpha1A residues 1-337 wild-type Biv2 "[""A1I9N""]" 1 IC50 IC50 = = 89 ± 9 pM 0.089 [] unit_conversion 10.050609993355087 success True biochemical_inhibition ADP-Glo enzymatic assay with recombinant CK2α. 3 Table 1 reports Biv2 enzymology IC50 = 89 ± 9 pM; Fig. 2 maps Biv2 to PDB 9QRI. auto_single_measurement only accepted activity measurement [1] 1 structures\9QRI\9QRI_metadata.json point structures/9QRI/9qri_protein.pdb structures/9QRI/9qri_pocket.pdb structures/9QRI/9qri_ligand.sdf structures/9QRI/9qri_ligand.pdb structures/9QRI/9qri_ligand.cif structures/9QRI/9qri_complex.pdb structures/9QRI/9qri_complex.cif 9QRJ classic CK2alpha human CK2alpha1A residues 1-337 wild-type Biv3 "[""A1I9O""]" 1 IC50 IC50 = = 46 ± 4 pM 0.046 [] unit_conversion 10.337242168318426 success True biochemical_inhibition ADP-Glo enzymatic assay with recombinant CK2α. 3 Table 1 reports Biv3 enzymology IC50 = 46 ± 4 pM; Fig. 3 maps Biv3 to PDB 9QRJ. auto_single_measurement only accepted activity measurement [1] 1 structures\9QRJ\9QRJ_metadata.json point structures/9QRJ/9qrj_protein.pdb structures/9QRJ/9qrj_pocket.pdb structures/9QRJ/9qrj_ligand.sdf structures/9QRJ/9qrj_ligand.pdb structures/9QRJ/9qrj_ligand.cif structures/9QRJ/9qrj_complex.pdb structures/9QRJ/9qrj_complex.cif 9QRL classic DNA polymerase PolC Enterococcus faecium full-length, exonuclease-inactivated PolC D431A+E433A ibezapolstat (IBZ) "[""A1I9T""]" 1 IC50 IC50 = = 12.3 ± 3.9 µM 12300.0 [] unit_conversion 4.910094888560602 success True biochemical_inhibition Real-time DNA primer-extension assay using purified exonuclease-inactivated E. faecium PolC; DNA substrate present; n=3. 2 Fig. 1e legend reports inhibition of exonuclease-inactivated E. faecium PolC by IBZ, with derived IC50 values; the plotted value for IBZ is 12.3 ± 3.9 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9QRL\9QRL_metadata.json point structures/9QRL/9qrl_protein.pdb structures/9QRL/9qrl_pocket.pdb structures/9QRL/9qrl_ligand.sdf structures/9QRL/9qrl_ligand.pdb structures/9QRL/9qrl_ligand.cif structures/9QRL/9qrl_complex.pdb structures/9QRL/9qrl_complex.cif 9QSR classic CK2alpha human CK2alpha1A residues 1-337 wild-type Biv4 "[""A1I90""]" 1 IC50 IC50 = = 65 ± 7 pM 0.065 [] unit_conversion 10.187086643357144 success True biochemical_inhibition ADP-Glo enzymatic assay with recombinant CK2α. 3 Table 1 reports Biv4 enzymology IC50 = 65 ± 7 pM; Fig. 3 maps Biv4 to PDB 9QSR. auto_single_measurement only accepted activity measurement [1] 1 structures\9QSR\9QSR_metadata.json point structures/9QSR/9qsr_protein.pdb structures/9QSR/9qsr_pocket.pdb structures/9QSR/9qsr_ligand.sdf structures/9QSR/9qsr_ligand.pdb structures/9QSR/9qsr_ligand.cif structures/9QSR/9qsr_complex.pdb structures/9QSR/9qsr_complex.cif 9QSU classic CK2alpha human CK2alpha1A residues 1-337 wild-type Biv7 "[""A1I92""]" 1 IC50 IC50 = = 221 ± 20 pM 0.221 [] unit_conversion 9.655607726314889 success True biochemical_inhibition ADP-Glo enzymatic assay with recombinant CK2α. 3 Table 1 reports Biv7 enzymology IC50 = 221 ± 20 pM; Fig. 3 maps Biv7 to PDB 9QSU. auto_single_measurement only accepted activity measurement [1] 1 structures\9QSU\9QSU_metadata.json point structures/9QSU/9qsu_protein.pdb structures/9QSU/9qsu_pocket.pdb structures/9QSU/9qsu_ligand.sdf structures/9QSU/9qsu_ligand.pdb structures/9QSU/9qsu_ligand.cif structures/9QSU/9qsu_complex.pdb structures/9QSU/9qsu_complex.cif 9QSV classic CK2alpha human CK2alpha1A residues 1-337 wild-type compound 5 "[""A1I93""]" 1 IC50 IC50 = = 5520 ± 700 pM 5.5200000000000005 [] unit_conversion 8.2580609222708 success True biochemical_inhibition ADP-Glo enzymatic assay with recombinant CK2α. 3 Table 1 reports compound 5 enzymology IC50 = 5520 ± 700 pM; Fig. 1 maps compound 5 to PDB 9QSV. auto_single_measurement only accepted activity measurement [1] 1 structures\9QSV\9QSV_metadata.json point structures/9QSV/9qsv_protein.pdb structures/9QSV/9qsv_pocket.pdb structures/9QSV/9qsv_ligand.sdf structures/9QSV/9qsv_ligand.pdb structures/9QSV/9qsv_ligand.cif structures/9QSV/9qsv_complex.pdb structures/9QSV/9qsv_complex.cif 9QUP classic de novo protein scaffold TFD-EE MPNN Na symmetric homodimeric TFD-EE MPNN scaffold Na Tb(III) "[""TB""]" 1 Kd Kd = = 62 ± 14 nM 62.0 [] unit_conversion 7.207608310501746 success True direct_binding Tb(III) binding affinity measured by tryptophan-enhanced Tb(III) luminescence titration at 1.375 µM dimeric protein. 9 Figure 5C labels “TFD-EE MPNN* (KD = 62 ± 14 nM)” under “TbIII binding affinity” and states that titration curves were fit using 1.375 µM protein dimer. auto_single_measurement only accepted activity measurement [1] 1 structures\9QUP\9QUP_metadata.json point structures/9QUP/9qup_protein.pdb structures/9QUP/9qup_pocket.pdb structures/9QUP/9qup_ligand.sdf structures/9QUP/9qup_ligand.pdb structures/9QUP/9qup_ligand.cif structures/9QUP/9qup_complex.pdb structures/9QUP/9qup_complex.cif 9QVT classic STING (stimulator of interferon genes) human (Homo sapiens) 8xHis-tagged R232-STING residues 138-379 wild-type D5 "[""A1JA0""]" 1 Kd Kd = = 32 nM 32.0 [] unit_conversion 7.494850021680094 success True direct_binding Binding constant to purified hSTINGwt measured by isothermal titration calorimetry. 5 Fig. 3e table reports for dimer D5: Kd hSTINGwt = 32 nM; the caption identifies these as binding constants with hSTINGwt. auto_single_measurement only accepted activity measurement [1] 1 structures\9QVT\9QVT_metadata.json point structures/9QVT/9qvt_protein.pdb structures/9QVT/9qvt_pocket.pdb structures/9QVT/9qvt_ligand.sdf structures/9QVT/9qvt_ligand.pdb structures/9QVT/9qvt_ligand.cif structures/9QVT/9qvt_complex.pdb structures/9QVT/9qvt_complex.cif 9QWB extended furin (PCSK3) Na Na Na compound 26 (MI-2456) "[""A1JA6""]" 1 Ki Ki = = 6.80±2.5 nM 6.8 [] unit_conversion 8.167491087293763 success True biochemical_inhibition Purified furin enzyme kinetic measurement; Table 1. 4 Table 1 reports Ki furin = 6.80±2.5 nM for compound 26. auto_single_measurement only accepted activity measurement [1] 1 structures\9QWB\9QWB_metadata.json point structures/9QWB/9qwb_protein.pdb structures/9QWB/9qwb_pocket.pdb structures/9QWB/9qwb_ligand.pdb structures/9QWB/9qwb_ligand.cif structures/9QWB/9qwb_complex.pdb structures/9QWB/9qwb_complex.cif 9QWD extended furin (PCSK3) Na Na Na compound 34 (MI-2470) "[""A1JA2""]" 1 Ki Ki = = 76.6±4.5 nM 76.6 [] unit_conversion 7.115771230367396 success True biochemical_inhibition Purified furin enzyme kinetic measurement; Table 1. 4 Table 1 reports Ki furin = 76.6±4.5 nM for compound 34. auto_single_measurement only accepted activity measurement [1] 1 structures\9QWD\9QWD_metadata.json point structures/9QWD/9qwd_protein.pdb structures/9QWD/9qwd_pocket.pdb structures/9QWD/9qwd_ligand.pdb structures/9QWD/9qwd_ligand.cif structures/9QWD/9qwd_complex.pdb structures/9QWD/9qwd_complex.cif 9QWF extended furin (PCSK3) Na Na Na compound 13 (MI-3102) "[""A1JA5""]" 1 Ki Ki = = 31.9±3.0 nM 31.9 [] unit_conversion 7.496209316942819 success True biochemical_inhibition Purified furin enzyme kinetic measurement; Table 1. 3 Table 1 reports Ki furin = 31.9±3.0 nM for compound 13. auto_single_measurement only accepted activity measurement [1] 1 structures\9QWF\9QWF_metadata.json point structures/9QWF/9qwf_protein.pdb structures/9QWF/9qwf_pocket.pdb structures/9QWF/9qwf_ligand.pdb structures/9QWF/9qwf_ligand.cif structures/9QWF/9qwf_complex.pdb structures/9QWF/9qwf_complex.cif 9QWG extended furin (PCSK3) Na Na Na compound 24 (MI-3140) "[""A1JA4""]" 1 Ki Ki = = 168±2.1 nM 168.0 [] unit_conversion 6.774690718274137 success True biochemical_inhibition Purified furin enzyme kinetic measurement; Table 1. 3 Table 1 reports Ki furin = 168±2.1 nM for compound 24. auto_single_measurement only accepted activity measurement [1] 1 structures\9QWG\9QWG_metadata.json point structures/9QWG/9qwg_protein.pdb structures/9QWG/9qwg_pocket.pdb structures/9QWG/9qwg_ligand.pdb structures/9QWG/9qwg_ligand.cif structures/9QWG/9qwg_complex.pdb structures/9QWG/9qwg_complex.cif 9QXN extended EGFR Na Na wild-type (WT) Sevabertinib (BAY 2927088) "[""A1JBI""]" 1 IC50 IC50 < < 0.5 nmol/L 0.5 [] unit_conversion 9.301029995663981 success True biochemical_inhibition TF-FRET biochemical kinase activity assay; ATP 2 mmol/L. 4 Figure 1B visibly reports sevabertinib IC50 for EGFR WT as <0.5 nmol/L in a TF-FRET assay at 2 mmol/L ATP. The Methods identify recombinant fragments of human EGFR/HER2, and page 12 maps the EGFR–sevabertinib crystal structure to PDB 9QXN. auto_single_measurement only accepted activity measurement [1] 1 structures\9QXN\9QXN_metadata.json point structures/9QXN/9qxn_ligand.cif structures/9QXN/9qxn_complex.cif 9QZE classic ALDH1A3 human ALDH1A3 residues 2-513 with an N-terminal His6 tag and cloning-vector tail Na NAD+ "[""NAD""]" 1 Kd Kd = = 0.033 μM 33.0 [] unit_conversion 7.481486060122112 success True direct_binding SPR steady-state affinity assay using purified His-tagged ALDH1A3 immobilised on an NTA sensor chip. 3 Table 4 reports NAD+–ALDH1A3 Kd = 0.033 μM; the accompanying SPR methods begin on this page. auto_single_measurement only accepted activity measurement [1] 1 structures\9QZE\9QZE_metadata.json point structures/9QZE/9qze_protein.pdb structures/9QZE/9qze_pocket.pdb structures/9QZE/9qze_ligand.sdf structures/9QZE/9qze_ligand.pdb structures/9QZE/9qze_ligand.cif structures/9QZE/9qze_complex.pdb structures/9QZE/9qze_complex.cif 9R0D classic Human CD73 (ecto 5'-nucleotidase) human Na Na compound 7 "[""A1JCF""]" 1 IC50 IC50 = = 1.3 nM 1.3 [] unit_conversion 8.886056647693163 success True biochemical_inhibition hCD73 biochemical phosphate-detection inhibition assay 3 Figure 3 identifies the cocrystal of compound 7 with CD73 as PDB 9R0D and prints “hCD73 IC50: 1.3 nM” for compound 7; the caption specifies biochemical phosphate detection by Malachite Green. auto_single_measurement only accepted activity measurement [1] 1 structures\9R0D\9R0D_metadata.json point structures/9R0D/9r0d_protein.pdb structures/9R0D/9r0d_pocket.pdb structures/9R0D/9r0d_ligand.sdf structures/9R0D/9r0d_ligand.pdb structures/9R0D/9r0d_ligand.cif structures/9R0D/9r0d_complex.pdb structures/9R0D/9r0d_complex.cif 9R0G extended Human CD73 (ecto 5'-nucleotidase) human Na Na compound 21 "[""A1JCG""]" 1 IC50 IC50 = = 0.13 nM 0.13 [] unit_conversion 9.886056647693163 success True biochemical_inhibition hCD73 biochemical inhibition assay; Table 2 characterization of individual diastereomers 5 Figure 5 maps compound 21 bound to hCD73 to PDB 9R0G. Table 2 prints hCD73 IC50 = 0.13 nM for compound 21. auto_single_measurement only accepted activity measurement [1] 1 structures\9R0G\9R0G_metadata.json point structures/9R0G/9r0g_protein.pdb structures/9R0G/9r0g_pocket.pdb structures/9R0G/9r0g_ligand.pdb structures/9R0G/9r0g_ligand.cif structures/9R0G/9r0g_complex.pdb structures/9R0G/9r0g_complex.cif 9R0H extended Human CD73 (ecto 5'-nucleotidase) human Na Na compound 6 (ORIC-533) "[""A1JCH""]" 2 Kd Kd = = 30 pM 0.03 [] unit_conversion 10.522878745280337 success True direct_binding surface plasmon resonance affinity measurement 8 The text reports SPR binding kinetics for compound 6 with CD73 and explicitly states a 30 pM KD. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9R0H\9R0H_metadata.json point structures/9R0H/9r0h_protein.pdb structures/9R0H/9r0h_pocket.pdb structures/9R0H/9r0h_ligand.pdb structures/9R0H/9r0h_ligand.cif structures/9R0H/9r0h_complex.pdb structures/9R0H/9r0h_complex.cif 9R0L classic carbonic anhydrase XII human Na Na compound 10 (3-(cyclooctylamino)-2,6-difluoro-4-((3-hydroxypropyl)sulfonyl)-5-(piperidin-1-yl)benzenesulfonamide) "[""A1H9A""]" 1 Kd Kd = = 36 nM 36.0 [] unit_conversion 7.443697499232712 success True direct_binding FTSA, 37 °C, pH 7.0; human recombinant CA isozymes. 4 Table 1 reports compound 10 Kd,obs = 36 nM for CA XII. The text maps CA XII–10 structures to PDB IDs 9F2N and 9R0L. auto_single_measurement only accepted activity measurement [1] 1 structures\9R0L\9R0L_metadata.json point structures/9R0L/9r0l_protein.pdb structures/9R0L/9r0l_pocket.pdb structures/9R0L/9r0l_ligand.sdf structures/9R0L/9r0l_ligand.pdb structures/9R0L/9r0l_ligand.cif structures/9R0L/9r0l_complex.pdb structures/9R0L/9r0l_complex.cif 9R0U classic carbonic anhydrase XII human Na Na compound 14 (3-(cyclooctylamino)-5-ethoxy-2,6-difluoro-4-((3-hydroxypropyl)sulfonyl)benzenesulfonamide) "[""A1H92""]" 1 Kd Kd = = 0.11 nM 0.11 [] unit_conversion 9.958607314841775 success True direct_binding FTSA, 37 °C, pH 7.0; human recombinant CA isozymes. 4 Table 1 reports compound 14 Kd,obs = 0.11 nM for CA XII (95% confidence interval [0.096; 0.17]). The text identifies CA XII–14 structures as PDB IDs 9F30 and 9R0U. auto_single_measurement only accepted activity measurement [1] 1 structures\9R0U\9R0U_metadata.json point structures/9R0U/9r0u_protein.pdb structures/9R0U/9r0u_pocket.pdb structures/9R0U/9r0u_ligand.sdf structures/9R0U/9r0u_ligand.pdb structures/9R0U/9r0u_ligand.cif structures/9R0U/9r0u_complex.pdb structures/9R0U/9r0u_complex.cif 9R0V classic TMA Lyase (CutC) Na Na Na compound 14 "[""A1JCI""]" 1 Kd Kd = = 0.37 μM 370.0 [] unit_conversion 6.431798275933005 success True direct_binding DSF-derived binding affinity; Table 1. 3 Table 1 reports compound 14 DSF Kd = 0.37 μM; Figure 2 maps compound 14 to PDB 9R0V. auto_single_measurement only accepted activity measurement [1] 1 structures\9R0V\9R0V_metadata.json point structures/9R0V/9r0v_protein.pdb structures/9R0V/9r0v_pocket.pdb structures/9R0V/9r0v_ligand.sdf structures/9R0V/9r0v_ligand.pdb structures/9R0V/9r0v_ligand.cif structures/9R0V/9r0v_complex.pdb structures/9R0V/9r0v_complex.cif 9R0Y classic NDM-1 metallo-beta-lactamase Na Na Na thiol compound 22b "[""A1JCK""]" 1 IC50 IC50 = = 14.09 μM 14090.0 [] unit_conversion 4.851089006890644 success True biochemical_inhibition Fluorogenic purified-enzyme NDM-1 inhibition assay; Table 2 determination. 7 Table 2 reports compound 22b with IC50 = 14.09 μM against NDM-1. auto_single_measurement only accepted activity measurement [1] 1 structures\9R0Y\9R0Y_metadata.json point structures/9R0Y/9r0y_protein.pdb structures/9R0Y/9r0y_pocket.pdb structures/9R0Y/9r0y_ligand.sdf structures/9R0Y/9r0y_ligand.pdb structures/9R0Y/9r0y_ligand.cif structures/9R0Y/9r0y_complex.pdb structures/9R0Y/9r0y_complex.cif 9R1P classic STUB1 Na N-terminal STUB1 (residues 16-153) Na SKPer1 (XMU-MP-8) "[""A1JBJ""]" 1 Kd Kd = = 3.06E-07 M 306.0 [] unit_conversion 6.514278573518419 success True direct_binding Microscale thermophoresis (MST) binding-affinity determination. 26 Supplementary Table 3 lists STUB1–SKPer1 with Kd (M) = 3.06E-07; Supplementary Table 2 maps PDB 9R1P to N-terminal STUB1 (16–153 aa) and SKPer1. auto_single_measurement only accepted activity measurement [1] 1 structures\9R1P\9R1P_metadata.json point structures/9R1P/9r1p_protein.pdb structures/9R1P/9r1p_pocket.pdb structures/9R1P/9r1p_ligand.sdf structures/9R1P/9r1p_ligand.pdb structures/9R1P/9r1p_ligand.cif structures/9R1P/9r1p_complex.pdb structures/9R1P/9r1p_complex.cif 9R2J extended human MAO B human human recombinant MAO-B over-expressed in Pichia pastoris Na 4a; (E)-3-(4-nitrophenyl)-1-(3-(trifluoromethyl)phenyl)prop-2-en-1-one "[""A1JCO""]" 1 Ki Ki = = 245 ± 50 nM 245.0 [] unit_conversion 6.610833915635467 success True biochemical_inhibition Continuous HRP-coupled spectrophotometric enzymatic assay; Ki determined by varying benzylamine with inhibitor, competitive-inhibition model. 4 Table 1 reports compound 4a Ki = 245 ± 50 nM; the text identifies 4a as co-crystallized with human MAO-B, and the accession list maps 4a to 9R2J. auto_single_measurement only accepted activity measurement [1] 1 structures\9R2J\9R2J_metadata.json point structures/9R2J/9r2j_ligand.sdf structures/9R2J/9r2j_ligand.cif structures/9R2J/9r2j_complex.cif 9R30 classic carbonic anhydrase IX human Na Na compound 26 (2,6-difluoro-3,5-bis(((1r,4r)-4-hydroxycyclohexyl)amino)-4-(methylsulfonyl)benzenesulfonamide) "[""A1JC2""]" 1 Kd Kd = = 56 nM 56.0 [] unit_conversion 7.251811972993799 success True direct_binding FTSA, 37 °C, pH 7.0; human recombinant CA isozymes. 4 Table 1 reports compound 26 Kd,obs = 56 nM for CA IX. The paper identifies the CA IX–compound 26 complex as PDB ID 9R30. auto_single_measurement only accepted activity measurement [1] 1 structures\9R30\9R30_metadata.json point structures/9R30/9r30_protein.pdb structures/9R30/9r30_pocket.pdb structures/9R30/9r30_ligand.sdf structures/9R30/9r30_ligand.pdb structures/9R30/9r30_ligand.cif structures/9R30/9r30_complex.pdb structures/9R30/9r30_complex.cif 9R31 classic carbonic anhydrase XII human Na Na compound 13 (3-(cyclooctylamino)-2,6-difluoro-4-((3-hydroxypropyl)sulfonyl)-5-methoxybenzenesulfonamide) "[""A1H89""]" 1 Kd Kd = = 0.050 nM 0.05 [] unit_conversion 10.301029995663981 success True direct_binding FTSA, 37 °C, pH 7.0; human recombinant CA isozymes. 4 Table 1 reports compound 13 Kd,obs = 0.050 nM for CA XII (95% confidence interval [0.031; 0.071]). The text maps CA XII–13 structures to PDB IDs 9F2O and 9R31. auto_single_measurement only accepted activity measurement [1] 1 structures\9R31\9R31_metadata.json point structures/9R31/9r31_protein.pdb structures/9R31/9r31_pocket.pdb structures/9R31/9r31_ligand.sdf structures/9R31/9r31_ligand.pdb structures/9R31/9r31_ligand.cif structures/9R31/9r31_complex.pdb structures/9R31/9r31_complex.cif 9R3B classic Recombinant human butyrylcholinesterase human Na Na N-([(3R)-1-benzylpiperidin-3-yl]methyl)-N-(2-methoxyethyl)naphthalene-2-sulfonamide; (R)-(-)-2 "[""A1JC3""]" 1 IC50 IC50 = = 13.60 ± 1.81 nM 13.6 [] unit_conversion 7.866461091629782 success True biochemical_inhibition In vitro Ellman cholinesterase-inhibition assay; recombinant hBChE. 5 Table 1 reports hBChE IC50 = 13.60 ± 1.81 nM for (R)-(-)-2. auto_single_measurement only accepted activity measurement [1] 1 structures\9R3B\9R3B_metadata.json point structures/9R3B/9r3b_protein.pdb structures/9R3B/9r3b_pocket.pdb structures/9R3B/9r3b_ligand.sdf structures/9R3B/9r3b_ligand.pdb structures/9R3B/9r3b_ligand.cif structures/9R3B/9r3b_complex.pdb structures/9R3B/9r3b_complex.cif 9R3C classic Recombinant human butyrylcholinesterase human Na Na N-([(3S)-1-benzylpiperidin-3-yl]methyl)-N-(2-methoxyethyl)naphthalene-2-sulfonamide; (S)-(+)-2 "[""5HF""]" 1 IC50 IC50 = = 31.09 ± 7.40 nM 31.09 [] unit_conversion 7.507379277956808 success True biochemical_inhibition In vitro Ellman cholinesterase-inhibition assay; recombinant hBChE. 5 Table 1 reports hBChE IC50 = 31.09 ± 7.40 nM for (S)-(+)-2. auto_single_measurement only accepted activity measurement [1] 1 structures\9R3C\9R3C_metadata.json point structures/9R3C/9r3c_protein.pdb structures/9R3C/9r3c_pocket.pdb structures/9R3C/9r3c_ligand.sdf structures/9R3C/9r3c_ligand.pdb structures/9R3C/9r3c_ligand.cif structures/9R3C/9r3c_complex.pdb structures/9R3C/9r3c_complex.cif 9R3J extended human MAO B human human recombinant MAO-B over-expressed in Pichia pastoris Na 4e; (E)-3-(benzo[d][1,3]dioxol-5-yl)-1-(3-(trifluoromethyl)phenyl)prop-2-en-1-one "[""A1JC8""]" 1 Ki Ki = = 210 ± 40 nM 210.0 [] unit_conversion 6.6777807052660805 success True biochemical_inhibition Continuous HRP-coupled spectrophotometric enzymatic assay; Ki determined by varying benzylamine with inhibitor, competitive-inhibition model. 4 Table 1 reports compound 4e Ki = 210 ± 40 nM; the text identifies 4e as co-crystallized with human MAO-B, and the accession list maps 4e to 9R3J. auto_single_measurement only accepted activity measurement [1] 1 structures\9R3J\9R3J_metadata.json point structures/9R3J/9r3j_ligand.cif structures/9R3J/9r3j_complex.cif 9R3K extended human MAO B human human recombinant MAO-B over-expressed in Pichia pastoris Na 4b; (E)-3-(3-nitrophenyl)-1-(3-(trifluoromethyl)phenyl)prop-2-en-1-one "[""A1JC6""]" 1 Ki Ki = = 152 ± 20 nM 152.0 [] unit_conversion 6.818156412055227 success True biochemical_inhibition Continuous HRP-coupled spectrophotometric enzymatic assay; Ki determined by varying benzylamine with inhibitor, competitive-inhibition model. 4 Table 1 reports compound 4b Ki = 152 ± 20 nM; the text identifies 4b as co-crystallized with human MAO-B, and the accession list maps 4b to 9R3K. auto_single_measurement only accepted activity measurement [1] 1 structures\9R3K\9R3K_metadata.json point structures/9R3K/9r3k_ligand.sdf structures/9R3K/9r3k_ligand.cif structures/9R3K/9r3k_complex.cif 9R3O classic liver pyruvate kinase Na Na Na 4a "[""A1JBW""]" 2 Kd Kd = = 19.3 µM 19300.0 [] unit_conversion 4.714442690992226 success True direct_binding Fluorescence titration/indicator-displacement analysis of PKL with 4a; reported as the calculated lower limit under stated PEP conditions. 8 “the lower limit of KD for 4a is calculated to be 19.3 µM.” auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\9R3O\9R3O_metadata.json point structures/9R3O/9r3o_protein.pdb structures/9R3O/9r3o_pocket.pdb structures/9R3O/9r3o_ligand.sdf structures/9R3O/9r3o_ligand.pdb structures/9R3O/9r3o_ligand.cif structures/9R3O/9r3o_complex.pdb structures/9R3O/9r3o_complex.cif 9R3Y extended N-WASP GBD Na N-WASP GBD2 (residues 207-275); EspFu R5 (residues 268-314) Na EspFu R5 "[""CHAIN:B""]" 1 Kd Kd = = 2.8 nM 2.8 [] unit_conversion 8.55284196865778 success True direct_binding Isothermal titration calorimetry (ITC); GBD2–EspFu R5 interaction. 8 Fig. 5B lists GBD2+EspFu R5 with Kd 2.8 nM; the caption states affinities were determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\9R3Y\9R3Y_metadata.json point structures/9R3Y/9r3y_protein.pdb structures/9R3Y/9r3y_pocket.pdb structures/9R3Y/9r3y_ligand.pdb structures/9R3Y/9r3y_ligand.cif structures/9R3Y/9r3y_complex.pdb structures/9R3Y/9r3y_complex.cif 9R4V extended N-WASP GBD Na N-WASP GBD2 (residues 207-275); EspF R2' (residues 115-161) Na EspF R2' "[""CHAIN:B""]" 1 Kd Kd = = 23.5 nM 23.5 [] unit_conversion 7.628932137728263 success True direct_binding Isothermal titration calorimetry (ITC); GBD2–EspF R2' interaction. 8 Fig. 5B lists GBD2+EspF R2' with Kd 23.5 nM; the caption states affinities were determined by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\9R4V\9R4V_metadata.json point structures/9R4V/9r4v_protein.pdb structures/9R4V/9r4v_pocket.pdb structures/9R4V/9r4v_ligand.pdb structures/9R4V/9r4v_ligand.cif structures/9R4V/9r4v_complex.pdb structures/9R4V/9r4v_complex.cif 9R4W extended SNX9 SH3 Na SNX9 SH3 (A2-S62); EspF R2' Na EspF R2' "[""CHAIN:B""]" 1 Kd Kd = = 0.7 µM 700.0 [] unit_conversion 6.154901959985743 success True direct_binding Isothermal titration calorimetry (ITC); SNX9 SH3–EspF R2' interaction. 6 Fig. 4A lists EspF R2' binding to SNX9 SH3 with Kd 0.7 µM; the caption states the affinities were probed by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\9R4W\9R4W_metadata.json point structures/9R4W/9r4w_protein.pdb structures/9R4W/9r4w_pocket.pdb structures/9R4W/9r4w_ligand.pdb structures/9R4W/9r4w_ligand.cif structures/9R4W/9r4w_complex.pdb structures/9R4W/9r4w_complex.cif 9R9D classic recombinant human butyrylcholinesterase human recombinant hBChE Na compound 4; N-(2-methoxyethyl)-N-{[1-(prop-2-yn-1-yl)pyrrolidin-3-yl]methyl}naphthalene-2-carboxamide "[""A1JDP""]" 1 IC50 IC50 = = 3.89 ± 0.54 μM 3890.0 [] unit_conversion 5.410050398674292 success True biochemical_inhibition Ellman cholinesterase inhibition assay; IC50 determined after 5 min preincubation. 4 Table 1 reports compound 4 hBChE IC50 = 3.89 ± 0.54 μM; footnote a specifies 5 min inhibitor–enzyme preincubation. auto_single_measurement only accepted activity measurement [1] 1 structures\9R9D\9R9D_metadata.json point structures/9R9D/9r9d_protein.pdb structures/9R9D/9r9d_pocket.pdb structures/9R9D/9r9d_ligand.sdf structures/9R9D/9r9d_ligand.pdb structures/9R9D/9r9d_ligand.cif structures/9R9D/9r9d_complex.pdb structures/9R9D/9r9d_complex.cif 9R9E classic recombinant human butyrylcholinesterase human recombinant hBChE Na compound 10; N-(3-methoxypropyl)-N-{[1-(prop-2-yn-1-yl)pyrrolidin-3-yl]methyl}naphthalene-2-sulfonamide "[""A1JDO""]" 1 IC50 IC50 = = 0.203 ± 0.005 μM 203.0 [] unit_conversion 6.692503962086787 success True biochemical_inhibition Ellman cholinesterase inhibition assay; IC50 determined after 5 min preincubation. 4 Table 1 reports compound 10 hBChE IC50 = 0.203 ± 0.005 μM; footnote a specifies 5 min inhibitor–enzyme preincubation. auto_single_measurement only accepted activity measurement [1] 1 structures\9R9E\9R9E_metadata.json point structures/9R9E/9r9e_protein.pdb structures/9R9E/9r9e_pocket.pdb structures/9R9E/9r9e_ligand.sdf structures/9R9E/9r9e_ligand.pdb structures/9R9E/9r9e_ligand.cif structures/9R9E/9r9e_complex.pdb structures/9R9E/9r9e_complex.cif 9R9G classic IRAK4 Na Na Na BAY1830839 (4) "[""Y9T""]" 1 IC50 IC50 = = 0.0018 µM 1.8 [] unit_conversion 8.744727494896694 success True biochemical_inhibition IRAK4 biochemical assay; Table 4 reports 0.0018 µM for compound 4. 7 Table 4 lists compound 4 with “IRAK4 biochem. [µM]” of 0.0018; the table describes experimental data for the IRAK4 inhibitor series. auto_single_measurement only accepted activity measurement [1] 1 structures\9R9G\9R9G_metadata.json point structures/9R9G/9r9g_protein.pdb structures/9R9G/9r9g_pocket.pdb structures/9R9G/9r9g_ligand.sdf structures/9R9G/9r9g_ligand.pdb structures/9R9G/9r9g_ligand.cif structures/9R9G/9r9g_complex.pdb structures/9R9G/9r9g_complex.cif 9R9J classic IRAK4 Na Na Na compound 5e "[""A1JDR""]" 1 IC50 IC50 = = 0.0008 µM 0.8 [] unit_conversion 9.096910013008056 success True biochemical_inhibition IRAK4 biochemical assay; the secondary-pharmacology table gives the IRAK4 IC50 for 5e. 9 Figure 8 table lists IRAK4 with “5e, IC50 [µM]” = 0.0008. auto_single_measurement only accepted activity measurement [1] 1 structures\9R9J\9R9J_metadata.json point structures/9R9J/9r9j_protein.pdb structures/9R9J/9r9j_pocket.pdb structures/9R9J/9r9j_ligand.sdf structures/9R9J/9r9j_ligand.pdb structures/9R9J/9r9j_ligand.cif structures/9R9J/9r9j_complex.pdb structures/9R9J/9r9j_complex.cif 9R9K classic IRAK4 human Na Na AS2444697 (1a) "[""A1JDQ""]" 1 IC50 IC50 = = 0.017 µM 17.0 [] unit_conversion 7.769551078621726 success True biochemical_inhibition IRAK4 biochemical assay; secondary-pharmacology table. 9 Figure 8 table lists IRAK4 with “1a, IC50 [µM]” = 0.017. auto_single_measurement only accepted activity measurement [1] 1 structures\9R9K\9R9K_metadata.json point structures/9R9K/9r9k_protein.pdb structures/9R9K/9r9k_pocket.pdb structures/9R9K/9r9k_ligand.sdf structures/9R9K/9r9k_ligand.pdb structures/9R9K/9r9k_ligand.cif structures/9R9K/9r9k_complex.pdb structures/9R9K/9r9k_complex.cif 9RCI classic Flap endonuclease 1 (FEN1) Na FEN1 residues 1-336 Na Compound 28 "[""A1JD4""]" 1 IC50 IC50 = = 22 nM 22.0 [] unit_conversion 7.657577319177793 success True biochemical_inhibition FEN1 biochemical inhibition assay; Table 4, n ≥ 2. 8 Table 4 reports Compound 28 FEN1 IC50 = 22 nM. The text identifies Compound 28 as crystallized with FEN1, and the data-availability statement maps FEN1–Compound 28 to PDB 9RCI. auto_single_measurement only accepted activity measurement [1] 1 structures\9RCI\9RCI_metadata.json point structures/9RCI/9rci_protein.pdb structures/9RCI/9rci_pocket.pdb structures/9RCI/9rci_ligand.sdf structures/9RCI/9rci_ligand.pdb structures/9RCI/9rci_ligand.cif structures/9RCI/9rci_complex.pdb structures/9RCI/9rci_complex.cif 9RD1 classic OppA Escherichia coli Na Na G-SisoK (GSisoK) "[""A1JHR""]" 1 Kd Kd = = 50 ± 5 µM 50000.0 [] unit_conversion 4.301029995663981 success True direct_binding Microscale thermophoresis of wild-type OppA binding G-SisoK; mean Kd ± s.e.m. from three biologically independent experiments. 6 Fig. 4d reports a Kd of 50 ± 5 µM for G-SisoK binding to wt-OppA. auto_single_measurement only accepted activity measurement [1] 1 structures\9RD1\9RD1_metadata.json point structures/9RD1/9rd1_protein.pdb structures/9RD1/9rd1_pocket.pdb structures/9RD1/9rd1_ligand.sdf structures/9RD1/9rd1_ligand.pdb structures/9RD1/9rd1_ligand.cif structures/9RD1/9rd1_complex.pdb structures/9RD1/9rd1_complex.cif 9RDI classic Flap endonuclease 1 (FEN1) human Na Na Compound 5 "[""A1JED""]" 2 Kd Kd = = 275 nM 275.0 [] unit_conversion 6.560667306169737 success True direct_binding SPR direct-binding assay; Figure 2A table. 2 Figure 2A reports Compound 5 FEN1 SPR KD = 275 nM. Figure 2 caption identifies 5 as bound to FEN1, and the data-availability statement maps FEN1–Compound 5 to PDB 9RDI. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9RDI\9RDI_metadata.json point structures/9RDI/9rdi_protein.pdb structures/9RDI/9rdi_pocket.pdb structures/9RDI/9rdi_ligand.sdf structures/9RDI/9rdi_ligand.pdb structures/9RDI/9rdi_ligand.cif structures/9RDI/9rdi_complex.pdb structures/9RDI/9rdi_complex.cif 9RFT classic liver pyruvate kinase (PKL) Na Na Na fluorescent probe II (compound II) "[""A1JFT""]" 1 Kd Kd = = 36.2 ± 0.289 μM 36200.0 [] unit_conversion 4.441291429466834 success True direct_binding SPR (PKL), 20 °C. 5 Table 2 reports compound II binding to PKL by SPR: K_D = 36.2 ± 0.289 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9RFT\9RFT_metadata.json point structures/9RFT/9rft_protein.pdb structures/9RFT/9rft_pocket.pdb structures/9RFT/9rft_ligand.sdf structures/9RFT/9rft_ligand.pdb structures/9RFT/9rft_ligand.cif structures/9RFT/9rft_complex.pdb structures/9RFT/9rft_complex.cif 9RG8 extended DNPH1 Na Na Na compound 1 "[""A1JFX""]" 2 Kd Kd = = 9.1 μM 9100.0 [] unit_conversion 5.040958607678906 success True direct_binding Surface plasmon resonance measurement of compound 1 binding to DNPH1; binding was reversed by 100 μM N6-benzyl AMP. 3 The text states that compound 1 showed a binding constant Kd of 9.1 μM by SPR. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9RG8\9RG8_metadata.json point structures/9RG8/9rg8_protein.pdb structures/9RG8/9rg8_pocket.pdb structures/9RG8/9rg8_ligand.pdb structures/9RG8/9rg8_ligand.cif structures/9RG8/9rg8_complex.pdb structures/9RG8/9rg8_complex.cif 9RJ1 classic S-methylcysteine synthase (BSAS4;1; PvBSAS4;1) Phaseolus vulgaris (common bean) Na Na BEZ (benzoic acid) "[""BEZ""]" 1 IC50 IC50 ~ ~ 0.6 mM 600000.0 [] unit_conversion 3.221848749616356 success True biochemical_inhibition Recombinant PvBSAS4;1 enzymatic assay with O-acetylserine and sodium sulfide substrates; benzoic acid was tested as inhibitor. 4 “The IC50 value of benzoic acid was equal to approximately 0.6 mM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9RJ1\9RJ1_metadata.json point structures/9RJ1/9rj1_protein.pdb structures/9RJ1/9rj1_pocket.pdb structures/9RJ1/9rj1_ligand.sdf structures/9RJ1/9rj1_ligand.pdb structures/9RJ1/9rj1_ligand.cif structures/9RJ1/9rj1_complex.pdb structures/9RJ1/9rj1_complex.cif 9RL1 classic APH(2'')-IVa Na Na Na 24 "[""A1JG8""]" 1 Ki Ki = = 799 ± 81 nM 799.0 [] unit_conversion 6.097453220686009 success True biochemical_inhibition Enzymatic-coupled inhibition assay; Table 2. 6 Table 2 reports Ki = 799 ± 81 nM for 24. auto_single_measurement only accepted activity measurement [1] 1 structures\9RL1\9RL1_metadata.json point structures/9RL1/9rl1_protein.pdb structures/9RL1/9rl1_pocket.pdb structures/9RL1/9rl1_ligand.sdf structures/9RL1/9rl1_ligand.pdb structures/9RL1/9rl1_ligand.cif structures/9RL1/9rl1_complex.pdb structures/9RL1/9rl1_complex.cif 9RM3 classic human CD22 human CD22_d1-d3, residues 20-330; deglycosylated with EndoH Na 17 "[""A1JJP""]" 1 Kd Kd = = 3.29 ± 0.72 µM 3290.0 [] unit_conversion 5.482804102050025 success True direct_binding Isothermal titration calorimetry (ITC), CD22_d1-d3 with compound 17. 5 Figure 3A explicitly prints KD = 3.29 ± 0.72 µM for compound 17; its caption identifies ITC binding to CD22. auto_single_measurement only accepted activity measurement [1] 1 structures\9RM3\9RM3_metadata.json point structures/9RM3/9rm3_protein.pdb structures/9RM3/9rm3_pocket.pdb structures/9RM3/9rm3_ligand.sdf structures/9RM3/9rm3_ligand.pdb structures/9RM3/9rm3_ligand.cif structures/9RM3/9rm3_complex.pdb structures/9RM3/9rm3_complex.cif 9RME extended SARS-CoV-2 Nsp3b SARS-CoV-2 Na Na compound 3; sulfamoyl derivative of GS-441524 "[""A1JHT""]" 1 Kd Kd = = 0.86 ± 0.04 µM 860.0 [] unit_conversion 6.065501548756432 success True direct_binding Isothermal titration calorimetry (ITC) measurement of compound 3 binding to Nsp3b. 8 Table 1 reports the Nsp3b–compound 3 interaction with KD = 0.86 ± 0.04 µM; page 10 states that the spatial structure of Nsp3b in complex with compound 3 is deposited as PDB 9RME. auto_single_measurement only accepted activity measurement [1] 1 structures\9RME\9RME_metadata.json point structures/9RME/9rme_protein.pdb structures/9RME/9rme_pocket.pdb structures/9RME/9rme_ligand.pdb structures/9RME/9rme_ligand.cif structures/9RME/9rme_complex.pdb structures/9RME/9rme_complex.cif 9RO7 classic human CD22 human CD22_d1-d3, residues 20-330; deglycosylated with EndoH Na 7-012 "[""A1JJO""]" 1 Kd Kd = = 7.55 ± 0.66 µM 7550.0 [] unit_conversion 5.1220530483708115 success True direct_binding Isothermal titration calorimetry (ITC), CD22_d1-d3 with compound 7-012. 5 Figure 3A explicitly prints KD = 7.55 ± 0.66 µM for compound 7-012; its caption identifies ITC binding to CD22. auto_single_measurement only accepted activity measurement [1] 1 structures\9RO7\9RO7_metadata.json point structures/9RO7/9ro7_protein.pdb structures/9RO7/9ro7_pocket.pdb structures/9RO7/9ro7_ligand.sdf structures/9RO7/9ro7_ligand.pdb structures/9RO7/9ro7_ligand.cif structures/9RO7/9ro7_complex.pdb structures/9RO7/9ro7_complex.cif 9ROB classic human CD22 human CD22_d1-d3, residues 20-330; deglycosylated with EndoH Na 1B "[""A1JJN""]" 1 Kd Kd = = 0.63 ± 0.08 µM 630.0 [] unit_conversion 6.200659450546418 success True direct_binding Isothermal titration calorimetry (ITC), CD22_d1-d3 with compound 1B. 5 Figure 3A explicitly prints KD = 0.63 ± 0.08 µM for compound 1B; its caption identifies ITC binding to CD22. auto_single_measurement only accepted activity measurement [1] 1 structures\9ROB\9ROB_metadata.json point structures/9ROB/9rob_protein.pdb structures/9ROB/9rob_pocket.pdb structures/9ROB/9rob_ligand.sdf structures/9ROB/9rob_ligand.pdb structures/9ROB/9rob_ligand.cif structures/9ROB/9rob_complex.pdb structures/9ROB/9rob_complex.cif 9RPO classic DNPH1 Na Na Na compound 3 "[""A1JH5""]" 2 Kd Kd = = 6.7 μM 6700.0 [] unit_conversion 5.173925197299173 success True direct_binding SPR direct-binding assay 3 Table 1 lists compound 3 with SPR Kd = 6.7 μM; Figure 3 maps compound 3 to PDB 9RPO. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9RPO\9RPO_metadata.json point structures/9RPO/9rpo_protein.pdb structures/9RPO/9rpo_pocket.pdb structures/9RPO/9rpo_ligand.sdf structures/9RPO/9rpo_ligand.pdb structures/9RPO/9rpo_ligand.cif structures/9RPO/9rpo_complex.pdb structures/9RPO/9rpo_complex.cif 9RZZ classic human pyrroline-5-carboxylate reductase 1 (PYCR1) human PYCR1 residues 1-273 of the 319-residue full-length variant, with N-terminal MHHHHHHSSGVDLGTENLYFQS sequence Na P1S; pyrrolidine-1-sulfonic acid (pyrrolidine-1-sulfonate) "[""A1JKN""]" 1 IC50 IC50 = = 1.88 ± 0.159 mM 1880000.0 [] unit_conversion 2.7258421507363204 success True biochemical_inhibition PYCR1 P5C-reduction assay under saturating substrate concentrations (2.5 mM P5C and 500 μM NADH). 7 “P1S exhibited an IC50 of 1.88 ± 0.159 mM, indicating weak inhibitory activity.” auto_single_measurement only accepted activity measurement [1] 1 structures\9RZZ\9RZZ_metadata.json point structures/9RZZ/9rzz_protein.pdb structures/9RZZ/9rzz_pocket.pdb structures/9RZZ/9rzz_ligand.sdf structures/9RZZ/9rzz_ligand.pdb structures/9RZZ/9rzz_ligand.cif structures/9RZZ/9rzz_complex.pdb structures/9RZZ/9rzz_complex.cif 9S02 classic human pyrroline-5-carboxylate reductase 1 (PYCR1) human PYCR1 residues 1-273 of the 319-residue full-length variant, with N-terminal MHHHHHHSSGVDLGTENLYFQS sequence Na D11; 3-(2-thiazolyl)propionic acid "[""R9M""]" 1 IC50 IC50 = = 2.74 ± 0.14 mM 2740000.0 [] unit_conversion 2.562249437179612 success True biochemical_inhibition PYCR1 P5C-reduction assay under saturating concentrations of both P5C and NADH. 4 “The resulting IC50 value of 2.74 ± 0.14 mM classifies D11 as a weak inhibitor.” auto_single_measurement only accepted activity measurement [1] 1 structures\9S02\9S02_metadata.json point structures/9S02/9s02_protein.pdb structures/9S02/9s02_pocket.pdb structures/9S02/9s02_ligand.sdf structures/9S02/9s02_ligand.pdb structures/9S02/9s02_ligand.cif structures/9S02/9s02_complex.pdb structures/9S02/9s02_complex.cif 9S0O classic DNPH1 Na Na Na compound 6 "[""A1JKT""]" 1 IC50 IC50 = = 7.3 μM 7300.0 [] unit_conversion 5.136677139879544 success True biochemical_inhibition TR-FRET DNPH1 binding assay 4 Table 2 lists compound 6 (THIQs) with TR-FRET IC50 = 7.3 μM; Figure 3 and Figure 7 map compound 6 to PDB 9S0O. auto_single_measurement only accepted activity measurement [1] 1 structures\9S0O\9S0O_metadata.json point structures/9S0O/9s0o_protein.pdb structures/9S0O/9s0o_pocket.pdb structures/9S0O/9s0o_ligand.sdf structures/9S0O/9s0o_ligand.pdb structures/9S0O/9s0o_ligand.cif structures/9S0O/9s0o_complex.pdb structures/9S0O/9s0o_complex.cif 9S1N classic DNPH1 Na Na Na compound 19 "[""A1JKZ""]" 1 IC50 IC50 = = 37 μM 37000.0 [] unit_conversion 4.431798275933005 success True biochemical_inhibition TR-FRET DNPH1 binding assay 4 Table 2 lists compound 19 (THIQs) with TR-FRET IC50 = 37 μM; Figure 8 maps compound 19 to PDB 9S1N. auto_single_measurement only accepted activity measurement [1] 1 structures\9S1N\9S1N_metadata.json point structures/9S1N/9s1n_protein.pdb structures/9S1N/9s1n_pocket.pdb structures/9S1N/9s1n_ligand.sdf structures/9S1N/9s1n_ligand.pdb structures/9S1N/9s1n_ligand.cif structures/9S1N/9s1n_complex.pdb structures/9S1N/9s1n_complex.cif 9S1O classic DNPH1 Na Na Na compound 18 "[""A1JK6""]" 1 IC50 IC50 = = 74 μM 74000.0 [] unit_conversion 4.130768280269024 success True biochemical_inhibition TR-FRET DNPH1 binding assay 4 Table 2 lists compound 18 (THIQs) with TR-FRET IC50 = 74 μM; Figure 7 maps compound 18 to PDB 9S1O. auto_single_measurement only accepted activity measurement [1] 1 structures\9S1O\9S1O_metadata.json point structures/9S1O/9s1o_protein.pdb structures/9S1O/9s1o_pocket.pdb structures/9S1O/9s1o_ligand.sdf structures/9S1O/9s1o_ligand.pdb structures/9S1O/9s1o_ligand.cif structures/9S1O/9s1o_complex.pdb structures/9S1O/9s1o_complex.cif 9S1W classic IDO1 human Na Na iDeg-7 "[""A1JLB""]" 1 Kd Kd = = 0.12 ± 0.02 µM 120.0 [] unit_conversion 6.920818753952375 success True direct_binding Isothermal titration calorimetry (ITC) measurement of iDeg binding to IDO1 at 25 °C. 12 Figure 5e reports “Kd = 0.12 ± 0.02 µM” for iDeg-7. auto_single_measurement only accepted activity measurement [1] 1 structures\9S1W\9S1W_metadata.json point structures/9S1W/9s1w_protein.pdb structures/9S1W/9s1w_pocket.pdb structures/9S1W/9s1w_ligand.sdf structures/9S1W/9s1w_ligand.pdb structures/9S1W/9s1w_ligand.cif structures/9S1W/9s1w_complex.pdb structures/9S1W/9s1w_complex.cif 9S1X classic IDO1 human Na Na iDeg-9 "[""A1JLA""]" 1 Kd Kd = = 0.22 ± 0.02 µM 220.0 [] unit_conversion 6.657577319177793 success True direct_binding Isothermal titration calorimetry (ITC) measurement of iDeg binding to IDO1 at 25 °C. 12 Figure 5f reports “Kd = 0.22 ± 0.02 µM” for iDeg-9. auto_single_measurement only accepted activity measurement [1] 1 structures\9S1X\9S1X_metadata.json point structures/9S1X/9s1x_protein.pdb structures/9S1X/9s1x_pocket.pdb structures/9S1X/9s1x_ligand.sdf structures/9S1X/9s1x_ligand.pdb structures/9S1X/9s1x_ligand.cif structures/9S1X/9s1x_complex.pdb structures/9S1X/9s1x_complex.cif 9S21 extended SIRT2 human Na Na LG023 (compound 7) "[""A1JK1""]" 1 IC50 IC50 = = 7.8 ± 2.1 µM 7800.0 [] unit_conversion 5.107905397309519 success True biochemical_inhibition Fluorescence-based SIRT2 deacetylation (ZMAL assay, 37 °C). 5 Table 1 reports LG023/compound 7 SIRT2 deacetylation IC50 = 7.8 ± 2.1 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9S21\9S21_metadata.json point structures/9S21/9s21_protein.pdb structures/9S21/9s21_pocket.pdb structures/9S21/9s21_ligand.pdb structures/9S21/9s21_ligand.cif structures/9S21/9s21_complex.pdb structures/9S21/9s21_complex.cif 9S46 classic SIRT2 human SIRT2 residues 56-356 with an N-terminal His6-SUMO fusion Na compound 29; RW-78 "[""A1JLK""]" 1 IC50 IC50 = = 26 ± 2 nM 26.0 [] unit_conversion 7.585026652029182 success True biochemical_inhibition Fluorescence-based in vitro SIRT2 inhibition assay; Table 1 reports mean ± standard deviation (n = 3). 7 Table 1 lists compound 29 with SIRT2 IC50 = 26 ± 2 nM. The text identifies 29 as RW-78 and maps the SIRT2:RW-78 structure to PDB ID 9S46. auto_single_measurement only accepted activity measurement [1] 1 structures\9S46\9S46_metadata.json point structures/9S46/9s46_protein.pdb structures/9S46/9s46_pocket.pdb structures/9S46/9s46_ligand.sdf structures/9S46/9s46_ligand.pdb structures/9S46/9s46_ligand.cif structures/9S46/9s46_complex.pdb structures/9S46/9s46_complex.cif 9S48 classic SIRT2 human SIRT2 residues 56-356 with an N-terminal His6-SUMO fusion Na compound 31; RW-80 "[""A1JLL""]" 1 IC50 IC50 = = 29 ± 2 nM 29.0 [] unit_conversion 7.537602002101044 success True biochemical_inhibition Fluorescence-based in vitro SIRT2 inhibition assay; Table 1 reports mean ± standard deviation (n = 3). 7 Table 1 lists compound 31 with SIRT2 IC50 = 29 ± 2 nM. The text maps the SIRT2:RW-80 structure to PDB ID 9S48. auto_single_measurement only accepted activity measurement [1] 1 structures\9S48\9S48_metadata.json point structures/9S48/9s48_protein.pdb structures/9S48/9s48_pocket.pdb structures/9S48/9s48_ligand.sdf structures/9S48/9s48_ligand.pdb structures/9S48/9s48_ligand.cif structures/9S48/9s48_complex.pdb structures/9S48/9s48_complex.cif 9S4H classic Fatty Acid Thioesterase A Arabidopsis thaliana Na Na x1816-FU1 "[""A1JLP""]" 1 Kd Kd = = 0.092 µM 92.0 [] unit_conversion 7.036212172654444 success True direct_binding Surface plasmon resonance (SPR) binding measurement. 12 Figure 8A reports x1816-FU1 K_D = 0.092 µM; the Figure 8 caption states that the K_D data were obtained by Surface Plasmon Resonance. The preceding text maps the FatA–x1816-FU1 structure to PDB 9S4H. auto_single_measurement only accepted activity measurement [1] 1 structures\9S4H\9S4H_metadata.json point structures/9S4H/9s4h_protein.pdb structures/9S4H/9s4h_pocket.pdb structures/9S4H/9s4h_ligand.sdf structures/9S4H/9s4h_ligand.pdb structures/9S4H/9s4h_ligand.cif structures/9S4H/9s4h_complex.pdb structures/9S4H/9s4h_complex.cif 9S5X classic Neisseria gonorrhoeae FabI Neisseria gonorrhoeae Na Na Debio 1453; (E)-3-((2R,3S)-3-hydroxy-2-methyl-4-oxo-2,3,4,5-tetrahydro-1H-pyrido[2,3-b][1,4]diazepin-8-yl)-N-methyl-N-((3-methylbenzofuran-2-yl)methyl)acrylamide "[""A1H1H""]" 1 IC50 IC50 = = 0.6 nM 0.6 [] unit_conversion 9.221848749616356 success True biochemical_inhibition Recombinant NgFabI NADH-consumption inhibition assay; NADH was added to initiate the reaction. 2 Fig. 1b explicitly reports NgFabI IC50 values of 6 nM, 2.4 nM, and 0.6 nM for Compound 1, Compound 2, and Debio 1453, respectively; the text also states Debio 1453 IC50 0.6 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9S5X\9S5X_metadata.json point structures/9S5X/9s5x_protein.pdb structures/9S5X/9s5x_pocket.pdb structures/9S5X/9s5x_ligand.sdf structures/9S5X/9s5x_ligand.pdb structures/9S5X/9s5x_ligand.cif structures/9S5X/9s5x_complex.pdb structures/9S5X/9s5x_complex.cif 9S9M classic human p53 Homo sapiens p53 DNA-binding domain residues 94-312 with stabilizing mutations M133L, V203A, N239Y, and N268D Y220C; M133L; V203A; N239Y; N268D rezatapopt analog 7, compound 7 "[""A1JMO""]" 1 Kd Kd = = 119 ± 10 nM 119.0 [] unit_conversion 6.924453038607469 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 reports Y220C with compound 7. 4 Table 2: Y220C, compound 7, Kd 119 ± 10 nM (3). auto_single_measurement only accepted activity measurement [1] 1 structures\9S9M\9S9M_metadata.json point structures/9S9M/9s9m_protein.pdb structures/9S9M/9s9m_pocket.pdb structures/9S9M/9s9m_ligand.sdf structures/9S9M/9s9m_ligand.pdb structures/9S9M/9s9m_ligand.cif structures/9S9M/9s9m_complex.pdb structures/9S9M/9s9m_complex.cif 9S9N classic human p53 Homo sapiens p53 DNA-binding domain residues 94-312 with stabilizing mutations M133L, V203A, N239Y, and N268D Y220C; M133L; V203A; N239Y; N268D rezatapopt analog 8, compound 8 "[""A1JMP""]" 1 Kd Kd = = 64.7 ± 18.4 nM 64.7 [] unit_conversion 7.189095719331299 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 reports Y220C with compound 8. 4 Table 2: Y220C, compound 8, Kd 64.7 ± 18.4 nM (2). auto_single_measurement only accepted activity measurement [1] 1 structures\9S9N\9S9N_metadata.json point structures/9S9N/9s9n_protein.pdb structures/9S9N/9s9n_pocket.pdb structures/9S9N/9s9n_ligand.sdf structures/9S9N/9s9n_ligand.pdb structures/9S9N/9s9n_ligand.cif structures/9S9N/9s9n_complex.pdb structures/9S9N/9s9n_complex.cif 9S9O classic human p53 Homo sapiens p53 DNA-binding domain residues 94-312 with stabilizing mutations M133L, V203A, N239Y, and N268D Y220C; M133L; V203A; N239Y; N268D rezatapopt "[""A1JMR""]" 1 Kd Kd = = 22.3 ± 4.2 nM 22.3 [] unit_conversion 7.651695136951839 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 reports Y220C with rezatapopt. 4 Table 2: Y220C, rezatapopt, Kd 22.3 ± 4.2 nM (6). auto_single_measurement only accepted activity measurement [1] 1 structures\9S9O\9S9O_metadata.json point structures/9S9O/9s9o_protein.pdb structures/9S9O/9s9o_pocket.pdb structures/9S9O/9s9o_ligand.sdf structures/9S9O/9s9o_ligand.pdb structures/9S9O/9s9o_ligand.cif structures/9S9O/9s9o_complex.pdb structures/9S9O/9s9o_complex.cif 9S9P classic human p53 Homo sapiens p53 DNA-binding domain residues 94-312 with stabilizing mutations M133L, V203A, N239Y, and N268D Y220S; M133L; V203A; N239Y; N268D rezatapopt "[""A1JMR""]" 1 Kd Kd = = 96.6 ± 7.5 nM 96.6 [] unit_conversion 7.015022873584506 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 reports Y220S with rezatapopt. 4 Table 2: Y220S, rezatapopt, Kd 96.6 ± 7.5 nM (2). auto_single_measurement only accepted activity measurement [1] 1 structures\9S9P\9S9P_metadata.json point structures/9S9P/9s9p_protein.pdb structures/9S9P/9s9p_pocket.pdb structures/9S9P/9s9p_ligand.sdf structures/9S9P/9s9p_ligand.pdb structures/9S9P/9s9p_ligand.cif structures/9S9P/9s9p_complex.pdb structures/9S9P/9s9p_complex.cif 9S9Q classic human p53 Homo sapiens p53 DNA-binding domain residues 94-312 with stabilizing mutations M133L, V203A, N239Y, and N268D Y220N; M133L; V203A; N239Y; N268D rezatapopt "[""A1JMR""]" 1 Kd Kd = = 526 ± 56 nM 526.0 [] unit_conversion 6.279014255846261 success True direct_binding Isothermal titration calorimetry (ITC); Table 2 reports Y220N with rezatapopt. 4 Table 2: Y220N, rezatapopt, Kd 526 ± 56 nM (6). auto_single_measurement only accepted activity measurement [1] 1 structures\9S9Q\9S9Q_metadata.json point structures/9S9Q/9s9q_protein.pdb structures/9S9Q/9s9q_pocket.pdb structures/9S9Q/9s9q_ligand.sdf structures/9S9Q/9s9q_ligand.pdb structures/9S9Q/9s9q_ligand.cif structures/9S9Q/9s9q_complex.pdb structures/9S9Q/9s9q_complex.cif 9SAJ classic SARS-CoV-2 NSP14 SARS-CoV-2 Na Na compound 5 "[""A1JMY""]" 1 IC50 IC50 = = 1.9 ± 0.30 μM 1900.0 [] unit_conversion 5.721246399047171 success True biochemical_inhibition Enzymatic inhibition, Table 1 4 Table 1 reports SARS-CoV-2 nsp14 IC50 = 1.9 ± 0.30 μM for compound 5. auto_single_measurement only accepted activity measurement [1] 1 structures\9SAJ\9SAJ_metadata.json point structures/9SAJ/9saj_protein.pdb structures/9SAJ/9saj_pocket.pdb structures/9SAJ/9saj_ligand.sdf structures/9SAJ/9saj_ligand.pdb structures/9SAJ/9saj_ligand.cif structures/9SAJ/9saj_complex.pdb structures/9SAJ/9saj_complex.cif 9SAK classic SARS-CoV-2 NSP14 SARS-CoV-2 Na Na compound 6 "[""A1JMZ""]" 1 IC50 IC50 = = 0.31 ± 0.12 μM 310.0 [] unit_conversion 6.508638306165727 success True biochemical_inhibition Enzymatic inhibition, Table 1 4 Table 1 reports SARS-CoV-2 nsp14 IC50 = 0.31 ± 0.12 μM for compound 6. auto_single_measurement only accepted activity measurement [1] 1 structures\9SAK\9SAK_metadata.json point structures/9SAK/9sak_protein.pdb structures/9SAK/9sak_pocket.pdb structures/9SAK/9sak_ligand.sdf structures/9SAK/9sak_ligand.pdb structures/9SAK/9sak_ligand.cif structures/9SAK/9sak_complex.pdb structures/9SAK/9sak_complex.cif 9SAL classic SARS-CoV-2 NSP14 SARS-CoV-2 Na Na compound 18 "[""A1JM0""]" 1 IC50 IC50 = = 2.1 ± 0.2 μM 2100.0 [] unit_conversion 5.6777807052660805 success True biochemical_inhibition Enzymatic inhibition, Table 2 5 Table 2 reports SARS-CoV-2 nsp14 IC50 = 2.1 ± 0.2 μM for compound 18. auto_single_measurement only accepted activity measurement [1] 1 structures\9SAL\9SAL_metadata.json point structures/9SAL/9sal_protein.pdb structures/9SAL/9sal_pocket.pdb structures/9SAL/9sal_ligand.sdf structures/9SAL/9sal_ligand.pdb structures/9SAL/9sal_ligand.cif structures/9SAL/9sal_complex.pdb structures/9SAL/9sal_complex.cif 9SDI classic Focal adhesion kinase (FAK) human kinase domain, residues 410-689 Na Fragment 6; 6-(1H-Pyrazol-4-yl)-nicotinic acid "[""A1JNJ""]" 1 Kd Kd = = 1.3 mM 1300000.0 [] unit_conversion 2.886056647693163 success True direct_binding SPR-derived binding affinity; FAK kinase-domain fragment-binding experiment. 3 Table 1 lists Fragment 6 versus FAK with K_D 1.3 mM and PDB ID 9SDI; the table note states binding affinities were determined by SPR. auto_single_measurement only accepted activity measurement [1] 1 structures\9SDI\9SDI_metadata.json point structures/9SDI/9sdi_protein.pdb structures/9SDI/9sdi_pocket.pdb structures/9SDI/9sdi_ligand.sdf structures/9SDI/9sdi_ligand.pdb structures/9SDI/9sdi_ligand.cif structures/9SDI/9sdi_complex.pdb structures/9SDI/9sdi_complex.cif 9SI4 classic human neutrophil elastase human Na Na compound 15 "[""A1JN2""]" 3 Kd Kd = = 0.16 nM 0.16 [] unit_conversion 9.795880017344075 success True direct_binding Surface-plasmon-resonance binding affinity reported in Table 5. 9 Table 5 reports K_D = 0.16 nM for compound 15; its footnote identifies binding kinetics and affinity to NE as measured by SPR (Biacore). auto_metric_priority unique highest-priority metric family: Kd [3] 5 structures\9SI4\9SI4_metadata.json point structures/9SI4/9si4_protein.pdb structures/9SI4/9si4_pocket.pdb structures/9SI4/9si4_ligand.sdf structures/9SI4/9si4_ligand.pdb structures/9SI4/9si4_ligand.cif structures/9SI4/9si4_complex.pdb structures/9SI4/9si4_complex.cif 9SL8 classic recombinant human butyrylcholinesterase human recombinant, secreted, low-glycosylation hBChE produced in Chinese hamster ovary cells Na 6b; naphthalen-2-yl methyl((2S,3R)-2-(pyridin-3-ylmethyl)quinuclidin-3-yl)carbamate "[""A1JOH""]" 1 IC50 IC50 = = 0.35 ± 0.12 µM 350.0 [] unit_conversion 6.455931955649724 success True biochemical_inhibition Modified Ellman's assay; recombinant human hBChE; 5 min preincubation. 4 Table 1 reports hBChE IC50 after 5 min preincubation for the (2S,3R)-enantiomer of 6b as 0.35 ± 0.12 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9SL8\9SL8_metadata.json point structures/9SL8/9sl8_protein.pdb structures/9SL8/9sl8_pocket.pdb structures/9SL8/9sl8_ligand.sdf structures/9SL8/9sl8_ligand.pdb structures/9SL8/9sl8_ligand.cif structures/9SL8/9sl8_complex.pdb structures/9SL8/9sl8_complex.cif 9SL9 classic recombinant human butyrylcholinesterase human recombinant, secreted, low-glycosylation hBChE produced in Chinese hamster ovary cells Na 7a; (2S,3R)-2-(pyridin-3-ylmethyl)quinuclidin-3-yl phenylcarbamate "[""A1JOI""]" 1 IC50 IC50 = = 2.18 ± 0.84 µM 2180.0 [] unit_conversion 5.661543506395395 success True biochemical_inhibition Modified Ellman's assay; recombinant human hBChE; 5 min preincubation. 4 Table 1 reports hBChE IC50 after 5 min preincubation for the (2S,3R)-enantiomer of 7a as 2.18 ± 0.84 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9SL9\9SL9_metadata.json point structures/9SL9/9sl9_protein.pdb structures/9SL9/9sl9_pocket.pdb structures/9SL9/9sl9_ligand.sdf structures/9SL9/9sl9_ligand.pdb structures/9SL9/9sl9_ligand.cif structures/9SL9/9sl9_complex.pdb structures/9SL9/9sl9_complex.cif 9SMZ classic SaMhqR (MhqR) Staphylococcus aureus C-terminal hexahistidine-tagged SaMhqR; tag not depicted in the main structural figures WT (wild type) 2-methylbenzoquinone (MBQ) "[""YMR""]" 1 Kd Kd = = 3.12 ± 0.61 µM 3120.0 [] unit_conversion 5.505845405981557 success True direct_binding Isothermal titration calorimetry (ITC) of purified SaMhqR binding MBQ; representative experiment shown, with assays performed in two replicates. 6 Figure 3B visibly reports “MBQ K_D(M) = 3.12 ± 0.61 µM”; the figure caption identifies the MBQ-bound SaMhqR crystal structure and MBQ-binding pocket. auto_single_measurement only accepted activity measurement [1] 1 structures\9SMZ\9SMZ_metadata.json point structures/9SMZ/9smz_protein.pdb structures/9SMZ/9smz_pocket.pdb structures/9SMZ/9smz_ligand.sdf structures/9SMZ/9smz_ligand.pdb structures/9SMZ/9smz_ligand.cif structures/9SMZ/9smz_complex.pdb structures/9SMZ/9smz_complex.cif 9SRG classic Prenylated FMN oxidative maturase PhdC Mycolicibacterium fortuitum C-terminal His-tagged PhdC Na FMN "[""FMN""]" 1 Kd Kd = = 17.75 ± 0.26 μM 17750.0 [] unit_conversion 4.750801642608887 success True direct_binding Isothermal titration calorimetry of FMN binding to purified C-terminal His-tagged PhdC at 25°C. 5 “The FMN binding affinity (Kd) for FMN was determined using isothermal titration calorimetry… FMN displayed a Kd of 17.75 ± 0.26 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9SRG\9SRG_metadata.json point structures/9SRG/9srg_protein.pdb structures/9SRG/9srg_pocket.pdb structures/9SRG/9srg_ligand.sdf structures/9SRG/9srg_ligand.pdb structures/9SRG/9srg_ligand.cif structures/9SRG/9srg_complex.pdb structures/9SRG/9srg_complex.cif 9T9W extended beta-TrCP Na 8xHis-ZZ-TEV-beta-TrCP residues 186-548 L188E,L192E diphosphorylated I-kappa-B-alpha degron peptide (DRHDpSGLDpSMKD) "[""CHAIN:C""]" 1 Ki Ki = = 26.26 ± 6.24 nM 26.26 [] unit_conversion 7.58070527824654 success True direct_binding Biochemical FRET-based probe displacement binding assay; Ki reported in Table 1. 2 Table 1 maps IκBα peptide to PDB 9T9W and reports Ki vs beta-TrCP of 26.26 ± 6.24 nM; table footnote states Ki values were determined using a FRET-based probe displacement assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9T9W\9T9W_metadata.json point structures/9T9W/9t9w_protein.pdb structures/9T9W/9t9w_pocket.pdb structures/9T9W/9t9w_ligand.pdb structures/9T9W/9t9w_ligand.cif structures/9T9W/9t9w_complex.pdb structures/9T9W/9t9w_complex.cif 9TCB classic human PARP15 human TEV-cleaved PARP15 catalytic domain (PARP15CAT) WT (wild type) BAD (benzamide adenine dinucleotide) "[""DQV""]" 1 Kd Kd = = 29 ± 2 μM 29000.0 [] unit_conversion 4.5376020021010435 success True direct_binding Native-MS titration series of PARP15CAT WT dimer with BAD; n=3. 15 The reported titration series for PARP15CAT WT dimer yielded Kd = (29 ± 2) μM for BAD. auto_single_measurement only accepted activity measurement [1] 1 structures\9TCB\9TCB_metadata.json point structures/9TCB/9tcb_protein.pdb structures/9TCB/9tcb_pocket.pdb structures/9TCB/9tcb_ligand.sdf structures/9TCB/9tcb_ligand.pdb structures/9TCB/9tcb_ligand.cif structures/9TCB/9tcb_complex.pdb structures/9TCB/9tcb_complex.cif 9TDA classic ERAP1 Na Na Na 1-[2-(5-bromo-7-fluoro-2-oxo-2,3-dihydro-1,3-benzothiazol-3-yl)acetamido]-4,4-difluorocyclohexane-1-carboxylic acid "[""A1JVE""]" 1 pIC50 IC50 = = 7.9 12.589254117941662 [] p_metric_transform 7.9 success True biochemical_inhibition ERAP1 enzymatic inhibition. The experimental section specifies ERAP1 allotype 2 enzymatic activity using YTAFTIPSI substrate; Table 6 reports compound 40. 14 Table 6 visibly reports compound 40 with ERAP1 pIC50 = 7.9. The compound 40 chemical name printed on page 22 matches the supplied 9TDA ligand title by notation-only benzothiazolone naming. auto_single_measurement only accepted activity measurement [1] 1 structures\9TDA\9TDA_metadata.json point structures/9TDA/9tda_protein.pdb structures/9TDA/9tda_pocket.pdb structures/9TDA/9tda_ligand.sdf structures/9TDA/9tda_ligand.pdb structures/9TDA/9tda_ligand.cif structures/9TDA/9tda_complex.pdb structures/9TDA/9tda_complex.cif 9TDZ extended beta-TrCP Na 8xHis-ZZ-TEV-beta-TrCP residues 186-548 L188E,L192E diphosphorylated Claspin degron peptide (SPSDpSGGXpSYET) "[""CHAIN:B""]" 1 Ki Ki = = 97.35 ± 26.75 nM 97.35 [] unit_conversion 7.0116640441439495 success True direct_binding Biochemical FRET-based probe displacement binding assay; Ki reported in Table 1. 2 Table 1 maps Claspin peptide to PDB 9TDZ and reports Ki vs beta-TrCP of 97.35 ± 26.75 nM; table footnote states Ki values were determined using a FRET-based probe displacement assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9TDZ\9TDZ_metadata.json point structures/9TDZ/9tdz_protein.pdb structures/9TDZ/9tdz_pocket.pdb structures/9TDZ/9tdz_ligand.pdb structures/9TDZ/9tdz_ligand.cif structures/9TDZ/9tdz_complex.pdb structures/9TDZ/9tdz_complex.cif 9TES extended beta-TrCP Na 8xHis-ZZ-TEV-beta-TrCP residues 186-548 L188E,L192E diphosphorylated PDCD4 degron peptide (SSRDpSGRDpSVSD) "[""CHAIN:B""]" 1 Ki Ki = = 6.10 ± 1.07 nM 6.1 [] unit_conversion 8.214670164989233 success True direct_binding Biochemical FRET-based probe displacement binding assay; Ki reported in Table 1. 2 Table 1 maps PDCD4 peptide to PDB 9TES and reports Ki vs beta-TrCP of 6.10 ± 1.07 nM; table footnote states Ki values were determined using a FRET-based probe displacement assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9TES\9TES_metadata.json point structures/9TES/9tes_protein.pdb structures/9TES/9tes_pocket.pdb structures/9TES/9tes_ligand.pdb structures/9TES/9tes_ligand.cif structures/9TES/9tes_complex.pdb structures/9TES/9tes_complex.cif 9TFU extended beta-TrCP Na 8xHis-ZZ-TEV-beta-TrCP residues 186-548 L188E,L192E monophosphorylated ATF4 degron peptide (SDNDpSGICMSPES) "[""CHAIN:B""]" 1 Ki Ki = = 3.62 ± 1.14 nM 3.62 [] unit_conversion 8.441291429466835 success True direct_binding Biochemical FRET-based probe displacement binding assay; Ki reported in Table 1. 2 Table 1 maps ATF4 peptide to PDB 9TFU and reports Ki vs beta-TrCP of 3.62 ± 1.14 nM; table footnote states Ki values were determined using a FRET-based probe displacement assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9TFU\9TFU_metadata.json point structures/9TFU/9tfu_protein.pdb structures/9TFU/9tfu_pocket.pdb structures/9TFU/9tfu_ligand.pdb structures/9TFU/9tfu_ligand.cif structures/9TFU/9tfu_complex.pdb structures/9TFU/9tfu_complex.cif 9TG7 extended beta-TrCP Na 8xHis-ZZ-TEV-beta-TrCP residues 186-548 L188E,L192E monophosphorylated WEE1 degron peptide (TGEDpSAFQEPDS) "[""CHAIN:B""]" 1 Ki Ki = = 566.53 ± 116.48 nM 566.53 [] unit_conversion 6.246777087584367 success True direct_binding Biochemical FRET-based probe displacement binding assay; Ki reported in Table 1. 2 Table 1 maps WEE1 peptide to PDB 9TG7 and reports Ki vs beta-TrCP of 566.53 ± 116.48 nM; table footnote states Ki values were determined using a FRET-based probe displacement assay. auto_single_measurement only accepted activity measurement [1] 1 structures\9TG7\9TG7_metadata.json point structures/9TG7/9tg7_protein.pdb structures/9TG7/9tg7_pocket.pdb structures/9TG7/9tg7_ligand.pdb structures/9TG7/9tg7_ligand.cif structures/9TG7/9tg7_complex.pdb structures/9TG7/9tg7_complex.cif 9TPG classic Zika virus NS2B-NS3 protease Zika virus (ZIKV) NS2B residues 45-96 linked via a flexible GGGGSGGG linker to NS3 residues 1-177; N-terminal hexahistidine tag with thrombin cleavage site Na R-(+)-IRBM-Z-1 (compound 1) "[""A1H2Z""]" 1 IC50 IC50 = = 0.8 ± 0.2 μM 800.0 [] unit_conversion 6.096910013008056 success True biochemical_inhibition Purified ZIKV NS2B-NS3 protease biochemical assay; Table 1 values are IC50 values in μM. 4 Table 1 lists R-IRBM-Z-1 against “ZIKV NS2B-NS3” as 0.8 ± 0.2; the table note specifies biochemical data are IC50 values in μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9TPG\9TPG_metadata.json point structures/9TPG/9tpg_protein.pdb structures/9TPG/9tpg_pocket.pdb structures/9TPG/9tpg_ligand.sdf structures/9TPG/9tpg_ligand.pdb structures/9TPG/9tpg_ligand.cif structures/9TPG/9tpg_complex.pdb structures/9TPG/9tpg_complex.cif 9U3B classic Monomeric sarcosine oxidase (SoxB) Bacillus sp. SoxB with a C-terminal His-tag wild-type L-Thioproline "[""PRS""]" 1 Ki Ki = = 4.2 ± 1.5 mM 4200000.0 [] unit_conversion 2.376750709602099 success True biochemical_inhibition Purified wild-type SoxB kinetic activity assay; L-thioproline substrate inhibition was fitted using the substrate-inhibition equation. 4 Table 1 reports for L-thioproline with wild-type SoxB: Ki = 4.2 ± 1.5 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\9U3B\9U3B_metadata.json point structures/9U3B/9u3b_protein.pdb structures/9U3B/9u3b_pocket.pdb structures/9U3B/9u3b_ligand.sdf structures/9U3B/9u3b_ligand.pdb structures/9U3B/9u3b_ligand.cif structures/9U3B/9u3b_complex.pdb structures/9U3B/9u3b_complex.cif 9U50 classic KRAS Na Na G12V MCB-294 "[""A1EN3""]" 1 IC50 IC50 = = 25.7 nM 25.7 [] unit_conversion 7.590066876668706 success True biochemical_inhibition HTRF binding assay measuring MCB-294 inhibition of GDP-loaded KRAS–SOS^cat binding (inactive state). 4 Figure 1E lists the inactive-state IC50 for G12V as 25.7 nM; the legend defines this as an HTRF binding assay using GDP-loaded KRAS–SOS^cat. auto_single_measurement only accepted activity measurement [1] 1 structures\9U50\9U50_metadata.json point structures/9U50/9u50_protein.pdb structures/9U50/9u50_pocket.pdb structures/9U50/9u50_ligand.sdf structures/9U50/9u50_ligand.pdb structures/9U50/9u50_ligand.cif structures/9U50/9u50_complex.pdb structures/9U50/9u50_complex.cif 9U5T classic KRAS Na Na G12D MCB-294 "[""A1EN3""]" 1 IC50 IC50 = = 6.6 nM 6.6 [] unit_conversion 8.18045606445813 success True biochemical_inhibition HTRF binding assay measuring MCB-294 inhibition of GDP-loaded KRAS–SOS^cat binding (inactive state). 4 Figure 1E lists the inactive-state IC50 for G12D as 6.6 nM; the legend defines this as an HTRF binding assay using GDP-loaded KRAS–SOS^cat. auto_single_measurement only accepted activity measurement [1] 1 structures\9U5T\9U5T_metadata.json point structures/9U5T/9u5t_protein.pdb structures/9U5T/9u5t_pocket.pdb structures/9U5T/9u5t_ligand.sdf structures/9U5T/9u5t_ligand.pdb structures/9U5T/9u5t_ligand.cif structures/9U5T/9u5t_complex.pdb structures/9U5T/9u5t_complex.cif 9U7E classic FGFR2 human FGFR2 residues 465-765 wild-type compound 8g "[""A1EOH""]" 1 IC50 IC50 = = 0.13 μM 130.0 [] unit_conversion 6.886056647693163 success True biochemical_inhibition Biochemical kinase inhibition assay (Table 1); 5 μM ATP for FGFR2. 3 Table 1 prints compound 8g IC50 = 0.13 μM against FGFR2; page 4 states that 8g has an FGFR2 cocrystal structure, PDB 9U7E. auto_single_measurement only accepted activity measurement [1] 1 structures\9U7E\9U7E_metadata.json point structures/9U7E/9u7e_protein.pdb structures/9U7E/9u7e_pocket.pdb structures/9U7E/9u7e_ligand.sdf structures/9U7E/9u7e_ligand.pdb structures/9U7E/9u7e_ligand.cif structures/9U7E/9u7e_complex.pdb structures/9U7E/9u7e_complex.cif 9U7S classic FGFR2 human FGFR2 residues 465-765 wild-type compound 8r "[""A1EOJ""]" 1 IC50 IC50 = = 6.9 nM 6.9 [] unit_conversion 8.161150909262744 success True biochemical_inhibition Biochemical kinase inhibition assay (Table 3); 5 μM ATP for FGFR2. 4 Table 3 prints compound 8r IC50 = 6.9 nM against FGFR2. Figure 4 on page 5 identifies the wild-type FGFR2/8r cocrystal as PDB 9U7S. auto_single_measurement only accepted activity measurement [1] 1 structures\9U7S\9U7S_metadata.json point structures/9U7S/9u7s_protein.pdb structures/9U7S/9u7s_pocket.pdb structures/9U7S/9u7s_ligand.sdf structures/9U7S/9u7s_ligand.pdb structures/9U7S/9u7s_ligand.cif structures/9U7S/9u7s_complex.pdb structures/9U7S/9u7s_complex.cif 9UBI classic FERONIA receptor kinase (FER) Arabidopsis thaliana FER kinase domain, residues 518-820, N-terminally His-tagged recombinant protein Na Ferovicin (FRV; OTSSP167) "[""OT5""]" 1 Kd Kd = = 0.4 µM 400.0 [] unit_conversion 6.3979400086720375 success True direct_binding Surface plasmon resonance (SPR) binding assay of FRV to recombinant FER-KD. 2 “the equilibrium dissociation constant (K_D) of FRV binding to FER was determined to be 0.4 μM (Fig. 1E).” FER-KD is defined as residues 518–820 immediately above. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9UBI\9UBI_metadata.json point structures/9UBI/9ubi_protein.pdb structures/9UBI/9ubi_pocket.pdb structures/9UBI/9ubi_ligand.sdf structures/9UBI/9ubi_ligand.pdb structures/9UBI/9ubi_ligand.cif structures/9UBI/9ubi_complex.pdb structures/9UBI/9ubi_complex.cif 9UO8 classic mouse Keap1 mouse Keap1-DC domain, residues 321-609, with an N-terminal His6 tag followed by a TEV protease recognition sequence Na compound 5i; N,N'-(2-(2-oxo-2-(pyrrolidin-1-yl)ethyl)naphthalene-1,4-diyl)bis(4-ethoxybenzenesulfonamide) "[""A1L9D""]" 1 IC50 IC50 = = 1.07 ± 0.04 µM 1070.0 [] unit_conversion 5.97061622231479 success True biochemical_inhibition Fluorescence-polarization Keap1-Nrf2 PPI inhibition assay; Table 1 reports inhibition of Keap1-DC interaction with an Nrf2 ETGE-motif fragment peptide. 4 Table 1 visibly reports compound 5i Keap1-Nrf2 PPI inhibitory activity (FP, IC50) of 1.07 ± 0.04 µM. The paper maps the Keap1-DC/5i crystal complex to PDB 9UO8 on page 5. auto_single_measurement only accepted activity measurement [1] 1 structures\9UO8\9UO8_metadata.json point structures/9UO8/9uo8_protein.pdb structures/9UO8/9uo8_pocket.pdb structures/9UO8/9uo8_ligand.sdf structures/9UO8/9uo8_ligand.pdb structures/9UO8/9uo8_ligand.cif structures/9UO8/9uo8_complex.pdb structures/9UO8/9uo8_complex.cif 9USB classic KRAS Na Na G12D MCB-294 "[""A1EN3""]" 1 IC50 IC50 = = 30.4 nM 30.4 [] unit_conversion 7.517126416391246 success True biochemical_inhibition HTRF binding assay measuring MCB-294 inhibition of GppNHp-loaded KRAS–RBD binding (active state). 4 Figure 1E lists the active-state IC50 for G12D as 30.4 nM; the legend defines this as an HTRF binding assay using GppNHp-loaded KRAS–RBD. auto_single_measurement only accepted activity measurement [1] 1 structures\9USB\9USB_metadata.json point structures/9USB/9usb_protein.pdb structures/9USB/9usb_pocket.pdb structures/9USB/9usb_ligand.sdf structures/9USB/9usb_ligand.pdb structures/9USB/9usb_ligand.cif structures/9USB/9usb_complex.pdb structures/9USB/9usb_complex.cif 9UYY classic human indoleamine 2,3-dioxygenase 2 (IDO2) human N-terminal MBP-tagged human IDO2, residues 11-420 wild-type L-Trp "[""TRP""]" 1 Kd Kd = = 66.6 ± 5.4 μM 66600.0 [] unit_conversion 4.176525770829699 success True direct_binding Purified MBP-ID02 absorption-titration measurement; Table 1 reports its L-Trp binding affinity. 4 The text states MBP-ID02 had Kd for L-Trp of 66.6 μM; Table 1 prints 66.6 ± 5.4 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9UYY\9UYY_metadata.json point structures/9UYY/9uyy_protein.pdb structures/9UYY/9uyy_pocket.pdb structures/9UYY/9uyy_ligand.sdf structures/9UYY/9uyy_ligand.pdb structures/9UYY/9uyy_ligand.cif structures/9UYY/9uyy_complex.pdb structures/9UYY/9uyy_complex.cif 9UYZ classic human indoleamine 2,3-dioxygenase 2 (IDO2) human N-terminal MBP-tagged human IDO2, residues 11-420 wild-type 5-HT (serotonin) "[""SRO""]" 1 Kd Kd = = 260 ± 38 μM 260000.0 [] unit_conversion 3.585026652029182 success True direct_binding Absorption-titration binding assay of purified IDO2 WT with tryptophan analogs. 10 Table 4 prints IDO2 Kd = 260 ± 38 μM for 5HT. auto_single_measurement only accepted activity measurement [1] 1 structures\9UYZ\9UYZ_metadata.json point structures/9UYZ/9uyz_protein.pdb structures/9UYZ/9uyz_pocket.pdb structures/9UYZ/9uyz_ligand.sdf structures/9UYZ/9uyz_ligand.pdb structures/9UYZ/9uyz_ligand.cif structures/9UYZ/9uyz_complex.pdb structures/9UYZ/9uyz_complex.cif 9UZ1 classic human indoleamine 2,3-dioxygenase 2 (IDO2) human N-terminal MBP-tagged human IDO2, residues 11-420 H143Y L-Trp "[""TRP""]" 1 Kd Kd = = 37.5 ± 5.4 μM 37500.0 [] unit_conversion 4.425968732272281 success True direct_binding Absorption-titration binding assay of purified IDO2 H143Y with L-Trp. 9 Table 3 prints Kd = 37.5 ± 5.4 μM for the IDO2 H143Y mutant with L-Trp. auto_single_measurement only accepted activity measurement [1] 1 structures\9UZ1\9UZ1_metadata.json point structures/9UZ1/9uz1_protein.pdb structures/9UZ1/9uz1_pocket.pdb structures/9UZ1/9uz1_ligand.sdf structures/9UZ1/9uz1_ligand.pdb structures/9UZ1/9uz1_ligand.cif structures/9UZ1/9uz1_complex.pdb structures/9UZ1/9uz1_complex.cif 9UZ3 classic human indoleamine 2,3-dioxygenase 2 (IDO2) human N-terminal MBP-tagged human IDO2, residues 11-420 wild-type D-Trp (D-tryptophan) "[""DTR""]" 1 Kd Kd = = 517 ± 24 μM 517000.0 [] unit_conversion 3.2865094569060576 success True direct_binding Absorption-titration binding assay of purified IDO2 WT with tryptophan analogs. 10 Table 4 reports IDO2 WT Kd 517 ± 24 μM for D-Trp. auto_single_measurement only accepted activity measurement [1] 1 structures\9UZ3\9UZ3_metadata.json point structures/9UZ3/9uz3_protein.pdb structures/9UZ3/9uz3_pocket.pdb structures/9UZ3/9uz3_ligand.sdf structures/9UZ3/9uz3_ligand.pdb structures/9UZ3/9uz3_ligand.cif structures/9UZ3/9uz3_complex.pdb structures/9UZ3/9uz3_complex.cif 9UZ5 classic human indoleamine 2,3-dioxygenase 2 (IDO2) human N-terminal MBP-tagged human IDO2, residues 11-420 wild-type 5-methyl-L-Trp (L-5MT) "[""D0Q""]" 1 Kd Kd = = 66.0 ± 4.5 μM 66000.0 [] unit_conversion 4.180456064458132 success True direct_binding Absorption-titration binding assay of purified IDO2 WT with tryptophan analogs. 10 Table 4 prints IDO2 Kd = 66.0 ± 4.5 μM for L-5MT. auto_single_measurement only accepted activity measurement [1] 1 structures\9UZ5\9UZ5_metadata.json point structures/9UZ5/9uz5_protein.pdb structures/9UZ5/9uz5_pocket.pdb structures/9UZ5/9uz5_ligand.sdf structures/9UZ5/9uz5_ligand.pdb structures/9UZ5/9uz5_ligand.cif structures/9UZ5/9uz5_complex.pdb structures/9UZ5/9uz5_complex.cif 9UZG classic Kasokero virus cap-snatching endonuclease Kasokero virus KASV L protein residues 610-904 Na DPBA (2,4-dioxo-4-phenylbutanoic acid) "[""XI7""]" 1 Kd Kd = = 70.7 ± 23.2 µM 70700.0 [] unit_conversion 4.150580586203101 success True direct_binding Microscale thermophoresis binding assay of KASV EN with DPBA; assay buffer contained 2 mM MnCl2. 11 Figure 5B prints “Kd = 70.7 ± 23.2 µM” for DPBA in MST binding assays of KASV EN. auto_single_measurement only accepted activity measurement [1] 1 structures\9UZG\9UZG_metadata.json point structures/9UZG/9uzg_protein.pdb structures/9UZG/9uzg_pocket.pdb structures/9UZG/9uzg_ligand.sdf structures/9UZG/9uzg_ligand.pdb structures/9UZG/9uzg_ligand.cif structures/9UZG/9uzg_complex.pdb structures/9UZG/9uzg_complex.cif 9UZH extended Kasokero virus cap-snatching endonuclease Kasokero virus KASV L protein residues 610-904 Na L-742,001 "[""0N8""]" 1 Kd Kd = = 140.1 ± 35.0 µM 140100.0 [] unit_conversion 3.8535618647142256 success True direct_binding Microscale thermophoresis binding assay of KASV EN with L-742,001; assay buffer contained 2 mM MnCl2. 11 Figure 5B prints “Kd = 140.1 ± 35.0 µM” for L-742,001 in MST binding assays of KASV EN. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9UZH\9UZH_metadata.json point structures/9UZH/9uzh_protein.pdb structures/9UZH/9uzh_pocket.pdb structures/9UZH/9uzh_ligand.pdb structures/9UZH/9uzh_ligand.cif structures/9UZH/9uzh_complex.pdb structures/9UZH/9uzh_complex.cif 9UZI classic Kasokero virus cap-snatching endonuclease Kasokero virus KASV L protein residues 610-904 Na BXA (baloxavir acid) "[""E4Z""]" 1 Kd Kd = = 4.5 ± 1.5 µM 4500.0 [] unit_conversion 5.346787486224656 success True direct_binding Microscale thermophoresis binding assay of KASV EN with BXA; assay buffer contained 2 mM MnCl2. 11 Figure 5B prints “Kd = 4.5 ± 1.5 µM” for BXA in MST binding assays of KASV EN. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9UZI\9UZI_metadata.json point structures/9UZI/9uzi_protein.pdb structures/9UZI/9uzi_pocket.pdb structures/9UZI/9uzi_ligand.sdf structures/9UZI/9uzi_ligand.pdb structures/9UZI/9uzi_ligand.cif structures/9UZI/9uzi_complex.pdb structures/9UZI/9uzi_complex.cif 9UZT extended human PTPN2 human PTPN2 gene fragment expressed from pGEX-6P-1 with N-terminal 6xHis and GST tags; tags cleaved before crystallization Na K-38 "[""A1EQR""]" 1 IC50 IC50 = = 7.05 nM 7.05 [] unit_conversion 8.1518108830086 success True biochemical_inhibition In vitro enzymatic inhibition assay using human PTPN2; Table 3 reports the PTPN2 IC50 for K-38. 9 Table 3 lists K-38 with PTPN2 IC50 = 7.05 nM. The enzymatic-assay methods specify human PTPN2. auto_single_measurement only accepted activity measurement [1] 1 structures\9UZT\9UZT_metadata.json point structures/9UZT/9uzt_protein.pdb structures/9UZT/9uzt_pocket.pdb structures/9UZT/9uzt_ligand.pdb structures/9UZT/9uzt_ligand.cif structures/9UZT/9uzt_complex.pdb structures/9UZT/9uzt_complex.cif 9V8D extended PPARgamma Na Na Na PG08 "[""CHAIN:B""]" 1 Kd Kd = = 9.4 nM 9.4 [] unit_conversion 8.0268721464003 success True direct_binding Surface plasmon resonance; PPARγ was immobilized on a Biacore 8K in the absence of rosiglitazone. 5 Table 1 reports PG08 K_D = 9.4 nM; the text states that PPARγ was immobilized for SPR in the absence of rosiglitazone. auto_single_measurement only accepted activity measurement [1] 1 structures\9V8D\9V8D_metadata.json point structures/9V8D/9v8d_protein.pdb structures/9V8D/9v8d_pocket.pdb structures/9V8D/9v8d_ligand.pdb structures/9V8D/9v8d_ligand.cif structures/9V8D/9v8d_complex.pdb structures/9V8D/9v8d_complex.cif 9V8E extended PPARgamma Na Na Na PG11 "[""CHAIN:B""]" 1 Kd Kd = = 0.14 nM 0.14 [] unit_conversion 9.853871964321762 success True direct_binding Surface plasmon resonance; PPARγ was immobilized on a Biacore 8K in the absence of rosiglitazone. 5 Table 1 reports PG11 K_D = 0.14 nM; the text states that PPARγ was immobilized for SPR in the absence of rosiglitazone. auto_single_measurement only accepted activity measurement [1] 1 structures\9V8E\9V8E_metadata.json point structures/9V8E/9v8e_protein.pdb structures/9V8E/9v8e_pocket.pdb structures/9V8E/9v8e_ligand.pdb structures/9V8E/9v8e_ligand.cif structures/9V8E/9v8e_complex.pdb structures/9V8E/9v8e_complex.cif 9V8F extended PPARgamma Na Na Na PG14 "[""CHAIN:B""]" 1 Kd Kd = = 2.7 nM 2.7 [] unit_conversion 8.568636235841012 success True direct_binding Surface plasmon resonance; PPARγ was immobilized on a Biacore 8K in the absence of rosiglitazone. 5 Table 1 reports PG14 K_D = 2.7 nM; the text states that PPARγ was immobilized for SPR in the absence of rosiglitazone. auto_single_measurement only accepted activity measurement [1] 1 structures\9V8F\9V8F_metadata.json point structures/9V8F/9v8f_protein.pdb structures/9V8F/9v8f_pocket.pdb structures/9V8F/9v8f_ligand.pdb structures/9V8F/9v8f_ligand.cif structures/9V8F/9v8f_complex.pdb structures/9V8F/9v8f_complex.cif 9V8W classic human creatine transporter (hCRT; SLC6A8) human full-length SLC6A8 with a C-terminal tandem Strep tag Na RGX202 (title: RGX) "[""A1D9S""]" 1 Kd Kd = = 3.39 μM 3390.0 [] unit_conversion 5.4698003017969175 success True direct_binding SPR analysis of purified hCRT binding RGX202. 6 “SPR assays revealed that RGX202 binds hCRT with an affinity of 3.39 μM.” auto_single_measurement only accepted activity measurement [1] 1 structures\9V8W\9V8W_metadata.json point structures/9V8W/9v8w_protein.pdb structures/9V8W/9v8w_pocket.pdb structures/9V8W/9v8w_ligand.sdf structures/9V8W/9v8w_ligand.pdb structures/9V8W/9v8w_ligand.cif structures/9V8W/9v8w_complex.pdb structures/9V8W/9v8w_complex.cif 9V8X classic human creatine transporter (hCRT; SLC6A8) human full-length SLC6A8 with a C-terminal tandem Strep tag Na creatine (title: Crea) "[""CRN""]" 1 Kd Kd = = 3.2 μM 3200.0 [] unit_conversion 5.494850021680094 success True direct_binding SPR analysis of purified hCRT binding creatine. 2 “Surface Plasmon Resonance (SPR) analysis yielded an affinity of 3.2 μM for creatine.” auto_single_measurement only accepted activity measurement [1] 1 structures\9V8X\9V8X_metadata.json point structures/9V8X/9v8x_protein.pdb structures/9V8X/9v8x_pocket.pdb structures/9V8X/9v8x_ligand.sdf structures/9V8X/9v8x_ligand.pdb structures/9V8X/9v8x_ligand.cif structures/9V8X/9v8x_complex.pdb structures/9V8X/9v8x_complex.cif 9VAK extended Carbohydrate-binding module 32 of LnbB Bifidobacterium bifidum LnbB-CBM32, residues 775-938 Na LNB "[""BRANCHED_ENTITY:2""]" 1 Kd Kd = = 98.0 µM 98000.0 [] unit_conversion 4.008773924307505 success True direct_binding ITC at 25 °C; one-site binding model. 5 Table 1 reports Kd = 98.0 µM for LNB binding to LnbB-CBM32 at 25 °C measured by ITC. auto_single_measurement only accepted activity measurement [1] 1 structures\9VAK\9VAK_metadata.json point structures/9VAK/9vak_protein.pdb structures/9VAK/9vak_pocket.pdb structures/9VAK/9vak_ligand.pdb structures/9VAK/9vak_ligand.cif structures/9VAK/9vak_complex.pdb structures/9VAK/9vak_complex.cif 9VPT classic Trypanosoma brucei DHODH Trypanosoma brucei E. coli pET47b-based expression construct for the C131A DHODH variant C131A dihydroorotate "[""DOR""]" 1 Kd Kd = = 1.1 ± 0.7 mM 1100000.0 [] unit_conversion 2.9586073148417746 success True direct_binding WaterLOGSY direct-binding experiment; C131A mutant in the FMN-oxidized state. 6 Table 1 reports a dissociation constant for dihydroorotate of 1.1 ± 0.7 mM in the oxidized state. auto_single_measurement only accepted activity measurement [1] 1 structures\9VPT\9VPT_metadata.json point structures/9VPT/9vpt_protein.pdb structures/9VPT/9vpt_pocket.pdb structures/9VPT/9vpt_ligand.sdf structures/9VPT/9vpt_ligand.pdb structures/9VPT/9vpt_ligand.cif structures/9VPT/9vpt_complex.pdb structures/9VPT/9vpt_complex.cif 9VPU classic Trypanosoma brucei DHODH Trypanosoma brucei E. coli pET47b-based expression construct for the C131A DHODH variant C131A dihydroorotate "[""DOR""]" 1 Kd Kd = = 9.0 ± 0.7 mM 9000000.0 [] unit_conversion 2.045757490560675 success True direct_binding WaterLOGSY direct-binding experiment; C131A mutant in the FMN-reduced state. 6 Table 1 reports a dissociation constant for dihydroorotate of 9.0 ± 0.7 mM in the reduced state. auto_single_measurement only accepted activity measurement [1] 1 structures\9VPU\9VPU_metadata.json point structures/9VPU/9vpu_protein.pdb structures/9VPU/9vpu_pocket.pdb structures/9VPU/9vpu_ligand.sdf structures/9VPU/9vpu_ligand.pdb structures/9VPU/9vpu_ligand.cif structures/9VPU/9vpu_complex.pdb structures/9VPU/9vpu_complex.cif 9VPV classic Trypanosoma brucei DHODH Trypanosoma brucei E. coli pET47b-based expression construct for the C131A DHODH variant C131A orotate "[""ORO""]" 1 Kd Kd = = 0.34 ± 0.08 mM 340000.0 [] unit_conversion 3.4685210829577446 success True direct_binding WaterLOGSY direct-binding experiment; C131A mutant in the FMN-oxidized state. 6 Table 1 reports a dissociation constant for orotate of 0.34 ± 0.08 mM in the oxidized state. auto_single_measurement only accepted activity measurement [1] 1 structures\9VPV\9VPV_metadata.json point structures/9VPV/9vpv_protein.pdb structures/9VPV/9vpv_pocket.pdb structures/9VPV/9vpv_ligand.sdf structures/9VPV/9vpv_ligand.pdb structures/9VPV/9vpv_ligand.cif structures/9VPV/9vpv_complex.pdb structures/9VPV/9vpv_complex.cif 9VPW classic Trypanosoma brucei DHODH Trypanosoma brucei E. coli pET47b-based expression construct for the C131A DHODH variant C131A orotate "[""ORO""]" 1 Kd Kd = = 1.03 ± 0.09 mM 1030000.0 [] unit_conversion 2.987162775294828 success True direct_binding WaterLOGSY direct-binding experiment; C131A mutant in the FMN-reduced state. 6 Table 1 reports a dissociation constant for orotate of 1.03 ± 0.09 mM in the reduced state. auto_single_measurement only accepted activity measurement [1] 1 structures\9VPW\9VPW_metadata.json point structures/9VPW/9vpw_protein.pdb structures/9VPW/9vpw_pocket.pdb structures/9VPW/9vpw_ligand.sdf structures/9VPW/9vpw_ligand.pdb structures/9VPW/9vpw_ligand.cif structures/9VPW/9vpw_complex.pdb structures/9VPW/9vpw_complex.cif 9VPX classic Trypanosoma brucei DHODH Trypanosoma brucei E. coli pET47b-based expression construct for the C131A DHODH variant C131A fumarate "[""FUM""]" 1 Kd Kd = = 22 ± 5 mM 22000000.0 [] unit_conversion 1.6575773191777934 success True direct_binding WaterLOGSY direct-binding experiment; C131A mutant in the FMN-oxidized state. 6 Table 1 reports a dissociation constant for fumarate of 22 ± 5 mM in the oxidized state. auto_single_measurement only accepted activity measurement [1] 1 structures\9VPX\9VPX_metadata.json point structures/9VPX/9vpx_protein.pdb structures/9VPX/9vpx_pocket.pdb structures/9VPX/9vpx_ligand.sdf structures/9VPX/9vpx_ligand.pdb structures/9VPX/9vpx_ligand.cif structures/9VPX/9vpx_complex.pdb structures/9VPX/9vpx_complex.cif 9VPY classic Trypanosoma brucei DHODH Trypanosoma brucei E. coli pET47b-based expression construct for the C131A DHODH variant C131A fumarate "[""FUM""]" 1 Kd Kd = = 3.3 ± 1.0 mM 3300000.0 [] unit_conversion 2.481486060122113 success True direct_binding WaterLOGSY direct-binding experiment; C131A mutant in the FMN-reduced state. 6 Table 1 reports a dissociation constant for fumarate of 3.3 ± 1.0 mM in the reduced state. auto_single_measurement only accepted activity measurement [1] 1 structures\9VPY\9VPY_metadata.json point structures/9VPY/9vpy_protein.pdb structures/9VPY/9vpy_pocket.pdb structures/9VPY/9vpy_ligand.sdf structures/9VPY/9vpy_ligand.pdb structures/9VPY/9vpy_ligand.cif structures/9VPY/9vpy_complex.pdb structures/9VPY/9vpy_complex.cif 9VQ0 classic Trypanosoma brucei DHODH Trypanosoma brucei E. coli pET47b-based expression construct for the A115V DHODH variant A115V (designated wild type in the paper) orotate "[""ORO""]" 1 Kd Kd = = 0.29 mM 290000.0 [] unit_conversion 3.5376020021010435 success True direct_binding WaterLOGSY direct-binding experiment; protein designated wild type in the paper, FMN-oxidized state. 4 The text states that fitting the orotate WaterLOGSY peak-intensity dependence for wild-type TbDHODH in the oxidized state gave a dissociation constant of 0.29 mM. auto_single_measurement only accepted activity measurement [1] 1 structures\9VQ0\9VQ0_metadata.json point structures/9VQ0/9vq0_protein.pdb structures/9VQ0/9vq0_pocket.pdb structures/9VQ0/9vq0_ligand.sdf structures/9VQ0/9vq0_ligand.pdb structures/9VQ0/9vq0_ligand.cif structures/9VQ0/9vq0_complex.pdb structures/9VQ0/9vq0_complex.cif 9VQ3 classic human phosphodiesterase 10A human Na Na QC-3; (6-fluoro-2-(1-(4-methylquinazolin-2-yl)azetidin-3-yl)imidazo[1,2-a]pyridin-3-yl)(4,7-diazaspiro[2.5]octan-7-yl)methanone "[""A1ETB""]" 1 IC50 IC50 = = 6.2 ± 0.1 nM 6.2 [] unit_conversion 8.207608310501746 success True biochemical_inhibition Table 1, PDE10A inhibitory activity; the paper maps QC-3 to the PDE10A–QC-3 crystal structure (PDB 9VQ3). 3 Table 1 reports QC-3 PDE10A IC50 = 6.2 ± 0.1 nM. auto_equivalent_value_dedup top candidates normalize to one identical metric/qualifier/value [1, 2] 2 structures\9VQ3\9VQ3_metadata.json point structures/9VQ3/9vq3_protein.pdb structures/9VQ3/9vq3_pocket.pdb structures/9VQ3/9vq3_ligand.sdf structures/9VQ3/9vq3_ligand.pdb structures/9VQ3/9vq3_ligand.cif structures/9VQ3/9vq3_complex.pdb structures/9VQ3/9vq3_complex.cif 9VRR classic PTPN2 human PTPN2 residues 5-296 with an N-terminal 6x His-GST tag and PreScission Protease recognition site Na WS3 "[""A1ETL""]" 1 IC50 IC50 = = 114.3 nM 114.3 [] unit_conversion 6.941953769604718 success True biochemical_inhibition Fluorescence-intensity phosphatase assay using DiFMUP substrate; human PTPN2 enzymatic activity. 5 Table 1 reports WS3: PTPN2 114.3 nM; its footnote specifies human PTPN2/N1 enzymatic activities tested using a fluorescence-intensity phosphatase assay with DiFMUP. auto_single_measurement only accepted activity measurement [1] 1 structures\9VRR\9VRR_metadata.json point structures/9VRR/9vrr_protein.pdb structures/9VRR/9vrr_pocket.pdb structures/9VRR/9vrr_ligand.sdf structures/9VRR/9vrr_ligand.pdb structures/9VRR/9vrr_ligand.cif structures/9VRR/9vrr_complex.pdb structures/9VRR/9vrr_complex.cif 9VRS classic PTPN2 human PTPN2 residues 5-296 with an N-terminal 6x His-GST tag and PreScission Protease recognition site Na WS19 "[""A1ETK""]" 1 IC50 IC50 = = 23.9 nM 23.9 [] unit_conversion 7.621602099051862 success True biochemical_inhibition Fluorescence-intensity phosphatase assay using DiFMUP substrate; human PTPN2 enzymatic activity. 7 Table 2 reports WS19: PTPN2 23.9 nM; its footnote specifies human PTPN2/N1 enzymatic activities tested using a fluorescence-intensity phosphatase assay with DiFMUP. auto_single_measurement only accepted activity measurement [1] 1 structures\9VRS\9VRS_metadata.json point structures/9VRS/9vrs_protein.pdb structures/9VRS/9vrs_pocket.pdb structures/9VRS/9vrs_ligand.sdf structures/9VRS/9vrs_ligand.pdb structures/9VRS/9vrs_ligand.cif structures/9VRS/9vrs_complex.pdb structures/9VRS/9vrs_complex.cif 9VSP extended TMEM175 human Full-length human TMEM175 residues 1-1512 with C-terminal HRV-3C site, 2x MBP, 1x Flag, and His tags Na DCY1020 "[""A1ETD""]" 1 Kd Kd = = 8.3 μM 8300.0 [] unit_conversion 5.080921907623926 success True direct_binding Surface plasmon resonance (SPR) direct binding of DCY1020 to TMEM175. 3 “The SPR results demonstrated a direct binding between DCY1020 and the TMEM175 (KD = 8.3 μM; Figures S1H, Figures S1I).” auto_single_measurement only accepted activity measurement [1] 1 structures\9VSP\9VSP_metadata.json point structures/9VSP/9vsp_protein.pdb structures/9VSP/9vsp_pocket.pdb structures/9VSP/9vsp_ligand.pdb structures/9VSP/9vsp_ligand.cif structures/9VSP/9vsp_complex.pdb structures/9VSP/9vsp_complex.cif 9VSQ classic TMEM175 human Full-length human TMEM175 residues 1-1512 with C-terminal HRV-3C site, 2x MBP, 1x Flag, and His tags Na TUG-891 "[""YN9""]" 1 Kd Kd = = 22.1 μM 22100.0 [] unit_conversion 4.655607726314889 success True direct_binding Surface plasmon resonance (SPR) direct binding of TUG-891 to TMEM175. 5 “The SPR results exhibited that TUG-891 directly binds to TMEM175 as well (KD = 22.1 μM; Figures S8A and S8B).” auto_single_measurement only accepted activity measurement [1] 1 structures\9VSQ\9VSQ_metadata.json point structures/9VSQ/9vsq_protein.pdb structures/9VSQ/9vsq_pocket.pdb structures/9VSQ/9vsq_ligand.sdf structures/9VSQ/9vsq_ligand.pdb structures/9VSQ/9vsq_ligand.cif structures/9VSQ/9vsq_complex.pdb structures/9VSQ/9vsq_complex.cif 9VVS classic IRED-68 (NAD(P)-dependent oxidoreductase) Kutzneria albida Na V123Q/S233G/V232H/A122T NADPH "[""NDP""]" 1 Kd Kd = = 4.1 ± 0.6 µM 4100.0 [] unit_conversion 5.3872161432802645 success True direct_binding Isothermal titration calorimetry (ITC), cofactor-binding affinity. 6 Figure 4C reports K_D (NADPH) of 4.1 ± 0.6 µM for IRED-68-M4; the text identifies 9VVS as the IRED-68-M4–NADPH complex. auto_single_measurement only accepted activity measurement [1] 1 structures\9VVS\9VVS_metadata.json point structures/9VVS/9vvs_protein.pdb structures/9VVS/9vvs_pocket.pdb structures/9VVS/9vvs_ligand.sdf structures/9VVS/9vvs_ligand.pdb structures/9VVS/9vvs_ligand.cif structures/9VVS/9vvs_complex.pdb structures/9VVS/9vvs_complex.cif 9WGW extended human Haspin human Na Na LJ-4827 "[""A1MBI""]" 1 Ki Ki = = 0.4648 nM 0.4648 [] unit_conversion 9.332733880617726 success True direct_binding KINOMEscan profiling/binding-constant determination for HASPIN. 3 The text reports that LJ4827's Ki value for HASPIN was 0.46 nM; Figure 2B prints Ki = 0.4648 nM for HASPIN. auto_metric_priority unique highest-priority metric family: Ki [1] 2 structures\9WGW\9WGW_metadata.json point structures/9WGW/9wgw_protein.pdb structures/9WGW/9wgw_pocket.pdb structures/9WGW/9wgw_ligand.pdb structures/9WGW/9wgw_ligand.cif structures/9WGW/9wgw_complex.pdb structures/9WGW/9wgw_complex.cif 9X2Q extended GSK3beta Na Na Na BiS-1 (BiS1) "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.86 ± 0.07 nM 0.86 [] unit_conversion 9.065501548756432 success True direct_binding Surface plasmon resonance binding-affinity measurement. 5 Figure 4a lists BiS1 with K_D = 0.86 ± 0.07 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9X2Q\9X2Q_metadata.json point structures/9X2Q/9x2q_protein.pdb structures/9X2Q/9x2q_pocket.pdb structures/9X2Q/9x2q_ligand.pdb structures/9X2Q/9x2q_ligand.cif structures/9X2Q/9x2q_complex.pdb structures/9X2Q/9x2q_complex.cif 9X2U extended GSK3beta Na Na Na BiS-2 (BiS2) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 1.02 ± 0.06 nM 1.02 [] unit_conversion 8.991399828238082 success True direct_binding Surface plasmon resonance binding-affinity measurement. 5 Figure 4a lists BiS2 with K_D = 1.02 ± 0.06 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9X2U\9X2U_metadata.json point structures/9X2U/9x2u_protein.pdb structures/9X2U/9x2u_pocket.pdb structures/9X2U/9x2u_ligand.pdb structures/9X2U/9x2u_ligand.cif structures/9X2U/9x2u_complex.pdb structures/9X2U/9x2u_complex.cif 9X2V extended GSK3beta Na Na Na BiS-3 (BiS3) "[""CHAIN:B""]" 1 Kd Kd = = 0.28 ± 0.07 nM 0.28 [] unit_conversion 9.55284196865778 success True direct_binding Surface plasmon resonance binding-affinity measurement. 5 Figure 4a lists BiS3 with K_D = 0.28 ± 0.07 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9X2V\9X2V_metadata.json point structures/9X2V/9x2v_protein.pdb structures/9X2V/9x2v_pocket.pdb structures/9X2V/9x2v_ligand.pdb structures/9X2V/9x2v_ligand.cif structures/9X2V/9x2v_complex.pdb structures/9X2V/9x2v_complex.cif 9X2W extended GSK3beta Na Na Na BiS-4 (BiS4) "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 1.6 ± 0.7 nM 1.6 [] unit_conversion 8.795880017344075 success True direct_binding Surface plasmon resonance binding-affinity measurement. 5 Figure 4a lists BiS4 with K_D = 1.6 ± 0.7 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9X2W\9X2W_metadata.json point structures/9X2W/9x2w_protein.pdb structures/9X2W/9x2w_pocket.pdb structures/9X2W/9x2w_ligand.pdb structures/9X2W/9x2w_ligand.cif structures/9X2W/9x2w_complex.pdb structures/9X2W/9x2w_complex.cif 9X2X extended GSK3beta Na Na Na BiS-5 (BiS5) "[""CHAIN:B"", ""CHAIN:D""]" 1 Kd Kd = = 0.35 ± 0.1 nM 0.35 [] unit_conversion 9.455931955649724 success True direct_binding Surface plasmon resonance binding-affinity measurement. 5 Figure 4a lists BiS5 with K_D = 0.35 ± 0.1 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9X2X\9X2X_metadata.json point structures/9X2X/9x2x_protein.pdb structures/9X2X/9x2x_pocket.pdb structures/9X2X/9x2x_ligand.pdb structures/9X2X/9x2x_ligand.cif structures/9X2X/9x2x_complex.pdb structures/9X2X/9x2x_complex.cif 9X2Y extended GSK3beta Na Na Na BiS-8 (BiS8) "[""CHAIN:C"", ""CHAIN:D""]" 1 Kd Kd = = 0.84 ± 0.08 nM 0.84 [] unit_conversion 9.075720713938118 success True direct_binding Surface plasmon resonance binding-affinity measurement. 5 Figure 4a lists BiS8 with K_D = 0.84 ± 0.08 nM. auto_metric_priority unique highest-priority metric family: Kd [1] 2 structures\9X2Y\9X2Y_metadata.json point structures/9X2Y/9x2y_protein.pdb structures/9X2Y/9x2y_pocket.pdb structures/9X2Y/9x2y_ligand.pdb structures/9X2Y/9x2y_ligand.cif structures/9X2Y/9x2y_complex.pdb structures/9X2Y/9x2y_complex.cif 9X55 classic RhoGDI2 Na Na Na 3054a "[""A1EY4""]" 1 Kd Kd = = 54 ± 5 μM 54000.0 [] unit_conversion 4.267606240177032 success True direct_binding Steady-state SPR. 3 Figure 2B and its caption report the steady-state SPR affinity of 3054a, annotated Kd = 54 ± 5 μM. auto_single_measurement only accepted activity measurement [1] 1 structures\9X55\9X55_metadata.json point structures/9X55/9x55_protein.pdb structures/9X55/9x55_pocket.pdb structures/9X55/9x55_ligand.sdf structures/9X55/9x55_ligand.pdb structures/9X55/9x55_ligand.cif structures/9X55/9x55_complex.pdb structures/9X55/9x55_complex.cif 9XAX classic L-threonate 3-dehydrogenase (Ltn3D; GL300_RS07945) Paracoccus litorisediminis N-terminal His6-tagged recombinant protein with the additional sequence MRGSHHHHHHGS Na tartronate "[""TTN""]" 1 Ki Ki = = 55.5 µM 55500.0 [] unit_conversion 4.255707016877324 success True biochemical_inhibition Competitive inhibition of L-threonate oxidation by tartronate; Michaelis–Menten and Lineweaver–Burk analyses. 6 Figure 4B explicitly reports competitive inhibition by tartronate and gives Ki = 55.5 µM. Table 2 and the deposition statement map 9XAX to the NADP+- and tartronate-bound PlLtn3D structure. auto_single_measurement only accepted activity measurement [1] 1 structures\9XAX\9XAX_metadata.json point structures/9XAX/9xax_protein.pdb structures/9XAX/9xax_pocket.pdb structures/9XAX/9xax_ligand.sdf structures/9XAX/9xax_ligand.pdb structures/9XAX/9xax_ligand.cif structures/9XAX/9xax_complex.pdb structures/9XAX/9xax_complex.cif 9XMM extended integrin alpha v beta6 Na alpha v beta6 headpiece Na 10-Mansa "[""CHAIN:E""]" 2 Kd Kd = = 8.23 ± 0.84 nM 8.23 [] unit_conversion 8.08460016478773 success True direct_binding Biolayer interferometry (BLI) binding of 10-Mansa to αvβ6. 5 The text reports BLI affinities for the αvβ6 integrin: 10-Mansa, KD = 8.23 ± 0.84 nM; Figure 2f is captioned as BLI binding of 10-Mansa to αvβ6. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9XMM\9XMM_metadata.json point structures/9XMM/9xmm_protein.pdb structures/9XMM/9xmm_pocket.pdb structures/9XMM/9xmm_ligand.pdb structures/9XMM/9xmm_ligand.cif structures/9XMM/9xmm_complex.pdb structures/9XMM/9xmm_complex.cif 9XYL classic human prolyl endopeptidase (PREP) human Na Na S17092 "[""A1CRK""]" 2 Ki Ki = = 0.378 nM 0.378 [] unit_conversion 9.422508200162774 success True biochemical_inhibition PREP covalent-inhibition kinetic analysis. 9 The text reports S17092 KI = 0.378 nM. auto_metric_priority unique highest-priority metric family: Ki [2] 2 structures\9XYL\9XYL_metadata.json point structures/9XYL/9xyl_protein.pdb structures/9XYL/9xyl_pocket.pdb structures/9XYL/9xyl_ligand.sdf structures/9XYL/9xyl_ligand.pdb structures/9XYL/9xyl_ligand.cif structures/9XYL/9xyl_complex.pdb structures/9XYL/9xyl_complex.cif 9Y65 classic Plasmodium falciparum M1 aminopeptidase (PfA-M1) Plasmodium falciparum Na Na 3k (MIPS3415) "[""A1CTH""]" 1 Ki Ki = = 27 ± 1 nM 27.0 [] unit_conversion 7.568636235841012 success True biochemical_inhibition Purified-enzyme aminopeptidase inhibition; Table 1. 5 Table 1 reports compound 3k PfA-M1 Ki(app) = 27 ± 1 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y65\9Y65_metadata.json point structures/9Y65/9y65_protein.pdb structures/9Y65/9y65_pocket.pdb structures/9Y65/9y65_ligand.sdf structures/9Y65/9y65_ligand.pdb structures/9Y65/9y65_ligand.cif structures/9Y65/9y65_complex.pdb structures/9Y65/9y65_complex.cif 9Y8J classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 1 "[""A1CTS""]" 1 Kd Kd = = 150 µM 150000.0 [] unit_conversion 3.8239087409443187 success True direct_binding Protein-observed SOFAST-HMQC NMR titration; NMR-derived affinity. 3 Figure 2 labels compound 1 as 150 µM, and the text states that benzimidazole 1 had an NMR-determined affinity of 150 µM. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8J\9Y8J_metadata.json point structures/9Y8J/9y8j_protein.pdb structures/9Y8J/9y8j_pocket.pdb structures/9Y8J/9y8j_ligand.sdf structures/9Y8J/9y8j_ligand.pdb structures/9Y8J/9y8j_ligand.cif structures/9Y8J/9y8j_complex.pdb structures/9Y8J/9y8j_complex.cif 9Y8K classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 7k "[""A1CTR""]" 1 Ki Ki = = 0.33 µM 330.0 [] unit_conversion 6.481486060122112 success True direct_binding Competition fluorescence-polarization anisotropy (FPA) binding assay with a labeled peptide-derived probe. 4 Table 1 reports FPA Ki = 0.33 µM for 7k; Figure 4 maps 7k to PDB 9Y8K. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8K\9Y8K_metadata.json point structures/9Y8K/9y8k_protein.pdb structures/9Y8K/9y8k_pocket.pdb structures/9Y8K/9y8k_ligand.sdf structures/9Y8K/9y8k_ligand.pdb structures/9Y8K/9y8k_ligand.cif structures/9Y8K/9y8k_complex.pdb structures/9Y8K/9y8k_complex.cif 9Y8L classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 8e "[""A1CTQ""]" 1 Ki Ki = = 0.9 µM 900.0 [] unit_conversion 6.045757490560675 success True direct_binding Competition FPA binding assay with a labeled peptide-derived probe. 5 Table 2 reports FPA Ki = 0.9 µM for 8e; Figure 4 maps 8e to PDB 9Y8L. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8L\9Y8L_metadata.json point structures/9Y8L/9y8l_protein.pdb structures/9Y8L/9y8l_pocket.pdb structures/9Y8L/9y8l_ligand.sdf structures/9Y8L/9y8l_ligand.pdb structures/9Y8L/9y8l_ligand.cif structures/9Y8L/9y8l_complex.pdb structures/9Y8L/9y8l_complex.cif 9Y8M classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 8i "[""A1CTE""]" 1 Ki Ki = = 38.4 µM 38400.0 [] unit_conversion 4.4156687756324695 success True direct_binding Competition FPA binding assay with a labeled peptide-derived probe. 5 Table 2 reports FPA Ki = 38.4 µM for 8i; Figure 4 maps 8i to PDB 9Y8M. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8M\9Y8M_metadata.json point structures/9Y8M/9y8m_protein.pdb structures/9Y8M/9y8m_pocket.pdb structures/9Y8M/9y8m_ligand.sdf structures/9Y8M/9y8m_ligand.pdb structures/9Y8M/9y8m_ligand.cif structures/9Y8M/9y8m_complex.pdb structures/9Y8M/9y8m_complex.cif 9Y8N classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 8m "[""A1CTL""]" 1 Ki Ki = = 5.2 µM 5200.0 [] unit_conversion 5.2839966563652006 success True direct_binding Competition FPA binding assay with a labeled peptide-derived probe. 5 Table 2 reports FPA Ki = 5.2 µM for 8m; Figure 4 maps 8m to PDB 9Y8N. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8N\9Y8N_metadata.json point structures/9Y8N/9y8n_protein.pdb structures/9Y8N/9y8n_pocket.pdb structures/9Y8N/9y8n_ligand.sdf structures/9Y8N/9y8n_ligand.pdb structures/9Y8N/9y8n_ligand.cif structures/9Y8N/9y8n_complex.pdb structures/9Y8N/9y8n_complex.cif 9Y8O classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 9c "[""A1CTM""]" 1 Ki Ki = = 11.4 µM 11400.0 [] unit_conversion 4.943095148663527 success True direct_binding Competition FPA binding assay with a labeled peptide-derived probe. 6 Table 3 reports FPA Ki = 11.4 µM for 9c; Figure 5 maps 9c to PDB 9Y8O. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8O\9Y8O_metadata.json point structures/9Y8O/9y8o_protein.pdb structures/9Y8O/9y8o_pocket.pdb structures/9Y8O/9y8o_ligand.sdf structures/9Y8O/9y8o_ligand.pdb structures/9Y8O/9y8o_ligand.cif structures/9Y8O/9y8o_complex.pdb structures/9Y8O/9y8o_complex.cif 9Y8Q classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 9e "[""A1CTO""]" 1 Ki Ki = = 4.2 µM 4200.0 [] unit_conversion 5.376750709602099 success True direct_binding Competition FPA binding assay with a labeled peptide-derived probe. 6 Table 3 reports FPA Ki = 4.2 µM for 9e; Figure 5 maps 9e to PDB 9Y8Q. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8Q\9Y8Q_metadata.json point structures/9Y8Q/9y8q_protein.pdb structures/9Y8Q/9y8q_pocket.pdb structures/9Y8Q/9y8q_ligand.sdf structures/9Y8Q/9y8q_ligand.pdb structures/9Y8Q/9y8q_ligand.cif structures/9Y8Q/9y8q_complex.pdb structures/9Y8Q/9y8q_complex.cif 9Y8R classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 9h "[""A1CTP""]" 1 Ki Ki = = 2.2 µM 2200.0 [] unit_conversion 5.657577319177793 success True direct_binding Competition FPA binding assay with a labeled peptide-derived probe. 6 Table 3 reports FPA Ki = 2.2 µM for 9h; Figure 5 maps 9h to PDB 9Y8R. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8R\9Y8R_metadata.json point structures/9Y8R/9y8r_protein.pdb structures/9Y8R/9y8r_pocket.pdb structures/9Y8R/9y8r_ligand.sdf structures/9Y8R/9y8r_ligand.pdb structures/9Y8R/9y8r_ligand.cif structures/9Y8R/9y8r_complex.pdb structures/9Y8R/9y8r_complex.cif 9Y8S classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 9k "[""A1CTN""]" 1 Ki Ki = = 3.7 µM 3700.0 [] unit_conversion 5.431798275933005 success True direct_binding Competition FPA binding assay with a labeled peptide-derived probe. 6 Table 3 reports FPA Ki = 3.7 µM for 9k; Figure 5 maps 9k to PDB 9Y8S. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8S\9Y8S_metadata.json point structures/9Y8S/9y8s_protein.pdb structures/9Y8S/9y8s_pocket.pdb structures/9Y8S/9y8s_ligand.sdf structures/9Y8S/9y8s_ligand.pdb structures/9Y8S/9y8s_ligand.cif structures/9Y8S/9y8s_complex.pdb structures/9Y8S/9y8s_complex.cif 9Y8T classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 10b "[""A1CTJ""]" 1 Ki Ki = = 4.7 µM 4700.0 [] unit_conversion 5.327902142064282 success True direct_binding Competition FPA binding assay with a labeled small-molecule probe. 8 Table 4 reports FPA Ki = 4.7 µM for 10b; Figure 6 maps 10b to PDB 9Y8T. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8T\9Y8T_metadata.json point structures/9Y8T/9y8t_protein.pdb structures/9Y8T/9y8t_pocket.pdb structures/9Y8T/9y8t_ligand.sdf structures/9Y8T/9y8t_ligand.pdb structures/9Y8T/9y8t_ligand.cif structures/9Y8T/9y8t_complex.pdb structures/9Y8T/9y8t_complex.cif 9Y8U classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 10j "[""A1CTK""]" 1 Ki Ki = = 10.4 µM 10400.0 [] unit_conversion 4.982966660701219 success True direct_binding Competition FPA binding assay with a labeled small-molecule probe. 8 Table 4 reports FPA Ki = 10.4 µM for 10j; Figure 6 maps 10j to PDB 9Y8U. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8U\9Y8U_metadata.json point structures/9Y8U/9y8u_protein.pdb structures/9Y8U/9y8u_pocket.pdb structures/9Y8U/9y8u_ligand.sdf structures/9Y8U/9y8u_ligand.pdb structures/9Y8U/9y8u_ligand.cif structures/9Y8U/9y8u_complex.pdb structures/9Y8U/9y8u_complex.cif 9Y8V classic human KLHL12 human KLHL12 Kelch domain residues 279-567, expressed from pET28a(+) with cleavable His-tag Na compound 10q "[""A1CTF""]" 1 Ki Ki = = 2.1 µM 2100.0 [] unit_conversion 5.6777807052660805 success True direct_binding Competition FPA binding assay with a labeled small-molecule probe. 8 Table 4 reports FPA Ki = 2.1 µM for 10q; Figure 6 maps 10q to PDB 9Y8V. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y8V\9Y8V_metadata.json point structures/9Y8V/9y8v_protein.pdb structures/9Y8V/9y8v_pocket.pdb structures/9Y8V/9y8v_ligand.sdf structures/9Y8V/9y8v_ligand.pdb structures/9Y8V/9y8v_ligand.cif structures/9Y8V/9y8v_complex.pdb structures/9Y8V/9y8v_complex.cif 9Y9N extended PLK4 Na Na Na Compound 25; (R)-7-hydroxy-N-(3-(1-(2,2,2-trifluoroethyl)-1H-pyrazolo[4,3-c]pyridin-6-yl)-1H-pyrazol-4-yl)-7-(trifluoromethyl)-4-azaspiro[2.5]octane-4-carboxamide "[""A1CTV""]" 1 IC50 IC50 = = 7.9 ± 4.0 nM 7.9 [] unit_conversion 8.102372908709558 success True biochemical_inhibition PLK4 ADPGlo biochemical assay; Table 4 aminopyrazole PLK4 inhibitor data. 5 Table 4 explicitly reports compound 25 PLK4 ADPGlo IC50 = 7.9 ± 4.0 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9Y9N\9Y9N_metadata.json point structures/9Y9N/9y9n_protein.pdb structures/9Y9N/9y9n_pocket.pdb structures/9Y9N/9y9n_ligand.pdb structures/9Y9N/9y9n_ligand.cif structures/9Y9N/9y9n_complex.pdb structures/9Y9N/9y9n_complex.cif 9Y9W extended FrhA Vibrio cholerae FrhA_split-PBD construct spanning S1127-F1439 with N-terminal 6xHis tag Na AGWTD "[""CHAIN:M"", ""CHAIN:N"", ""CHAIN:O"", ""CHAIN:P"", ""CHAIN:Q"", ""CHAIN:R""]" 2 Kd Kd = = 0.381 µM 381.0 [] unit_conversion 6.41907502432438 success True direct_binding MST summary table; three independent MST experiments. 9 Table 1 lists AGWTD binding to FrhA-PBD as Kd 0.381 µM. auto_qualifier_priority unique best qualifier within highest-priority metric family [2] 2 structures\9Y9W\9Y9W_metadata.json point structures/9Y9W/9y9w_protein.pdb structures/9Y9W/9y9w_pocket.pdb structures/9Y9W/9y9w_ligand.pdb structures/9Y9W/9y9w_ligand.cif structures/9Y9W/9y9w_complex.pdb structures/9Y9W/9y9w_complex.cif 9YC7 classic Plasmodium falciparum M17 aminopeptidase (PfA-M17) Plasmodium falciparum Na Na 3k (MIPS3415) "[""A1CTH""]" 1 Ki Ki = = 81 ± 8 nM 81.0 [] unit_conversion 7.0915149811213505 success True biochemical_inhibition Purified-enzyme aminopeptidase inhibition; Table 1. 5 Table 1 reports compound 3k PfA-M17 Ki(app) = 81 ± 8 nM. auto_single_measurement only accepted activity measurement [1] 1 structures\9YC7\9YC7_metadata.json point structures/9YC7/9yc7_protein.pdb structures/9YC7/9yc7_pocket.pdb structures/9YC7/9yc7_ligand.sdf structures/9YC7/9yc7_ligand.pdb structures/9YC7/9yc7_ligand.cif structures/9YC7/9yc7_complex.pdb structures/9YC7/9yc7_complex.cif 9YIC classic IL-17A human Na Na Compound 1 "[""A1CXF""]" 2 Kd Kd = = 92 ± 22 nM 92.0 [] unit_conversion 7.036212172654444 success True direct_binding SPR titration of Compound 1 binding to the IL-17A homodimer. 2 “SPR was used to characterize the binding of 1 to the IL-17A homodimer… characterized by an apparent KD of 92 ± 22 nM.” auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9YIC\9YIC_metadata.json point structures/9YIC/9yic_protein.pdb structures/9YIC/9yic_pocket.pdb structures/9YIC/9yic_ligand.sdf structures/9YIC/9yic_ligand.pdb structures/9YIC/9yic_ligand.cif structures/9YIC/9yic_complex.pdb structures/9YIC/9yic_complex.cif 9YMT classic Staphylococcus aureus serine/threonine kinase Stk1 Staphylococcus aureus strain Mu50 (ATCC 700699) Stk1 kinase domain, residues 1-291, with thrombin-cleaved N-terminal 10X His-tag Na GW779439X (GWX) "[""A1CYJ""]" 2 Kd Kd = = 21.1 ± 11.1 nM 21.1 [] unit_conversion 7.675717544702307 success True direct_binding Isothermal titration calorimetry of purified Stk1 kinase domain with GWX; one-binding-site model. 21 ITC determined binding of GWX to Stk1(1-291), with a calculated Kd of 21.1 nM ± 11.1 nM. auto_metric_priority unique highest-priority metric family: Kd [2] 2 structures\9YMT\9YMT_metadata.json point structures/9YMT/9ymt_protein.pdb structures/9YMT/9ymt_pocket.pdb structures/9YMT/9ymt_ligand.sdf structures/9YMT/9ymt_ligand.pdb structures/9YMT/9ymt_ligand.cif structures/9YMT/9ymt_complex.pdb structures/9YMT/9ymt_complex.cif 9YQ4 classic Chlorella virus hyaluronan synthase (CvHAS) Chlorella virus D302N CvHAS-Nb complex reconstituted into MSP1E3D1 lipid nanodiscs D302N (Asp302Asn) UDP-GlcA "[""UGA""]" 1 Kd Kd = = 69 µM 69000.0 [] unit_conversion 4.161150909262744 success True direct_binding Isothermal titration calorimetry; UDP-GlcA titrated into 45 µM catalytically inactive D302N CvHAS with MnCl2, without a GlcNAc primer. 6 ITC gave an apparent UDP-GlcA dissociation constant of 69 µM in the absence of a GlcNAc primer. auto_single_measurement only accepted activity measurement [1] 1 structures\9YQ4\9YQ4_metadata.json point structures/9YQ4/9yq4_protein.pdb structures/9YQ4/9yq4_pocket.pdb structures/9YQ4/9yq4_ligand.sdf structures/9YQ4/9yq4_ligand.pdb structures/9YQ4/9yq4_ligand.cif structures/9YQ4/9yq4_complex.pdb structures/9YQ4/9yq4_complex.cif 9YQ5 classic Chlorella virus hyaluronan synthase (CvHAS) Chlorella virus D302N CvHAS-Nb complex reconstituted into MSP1E3D1 lipid nanodiscs D302N (Asp302Asn) UDP-GlcA "[""UGA""]" 1 Kd Kd = = 69 µM 69000.0 [] unit_conversion 4.161150909262744 success True direct_binding Isothermal titration calorimetry; UDP-GlcA titrated into 45 µM catalytically inactive D302N CvHAS with MnCl2, without a GlcNAc primer. 6 ITC gave an apparent UDP-GlcA dissociation constant of 69 µM in the absence of a GlcNAc primer. auto_single_measurement only accepted activity measurement [1] 1 structures\9YQ5\9YQ5_metadata.json point structures/9YQ5/9yq5_protein.pdb structures/9YQ5/9yq5_pocket.pdb structures/9YQ5/9yq5_ligand.sdf structures/9YQ5/9yq5_ligand.pdb structures/9YQ5/9yq5_ligand.cif structures/9YQ5/9yq5_complex.pdb structures/9YQ5/9yq5_complex.cif 9Z2C classic KHK-C Na Na Na Compound 22; GS-1291269 "[""A1C0H""]" 1 IC50 IC50 = = 0.38 nM 0.38 [] unit_conversion 9.42021640338319 success True biochemical_inhibition KHK-C ADP-Glo biochemical assay, with fructose as substrate. 7 Table 8 reports GS-1291269 (compound 22) KHK-C IC50 = 0.38 nM. Figure 6 identifies the KHK-C/compound 22 structure as PDB 9Z2C. auto_single_measurement only accepted activity measurement [1] 1 structures\9Z2C\9Z2C_metadata.json point structures/9Z2C/9z2c_protein.pdb structures/9Z2C/9z2c_pocket.pdb structures/9Z2C/9z2c_ligand.sdf structures/9Z2C/9z2c_ligand.pdb structures/9Z2C/9z2c_ligand.cif structures/9Z2C/9z2c_complex.pdb structures/9Z2C/9z2c_complex.cif 9ZXM classic DDB1 (DNA damage-binding protein 1) Na DDB1-deltaB comprising beta-propeller A and beta-propeller C connected by a short linker Na compound 6 "[""A1C4E""]" 1 Kd Kd = = 2.8 µM 2800.0 [] unit_conversion 5.552841968657781 success True direct_binding SPR direct ligand-binding assay; Fig. 3D reports the geometric mean of replicate SPR Kd determinations. 4 Figure 3D lists compound 6 with an SPR Kd of 2.8 µM. The text identifies Avi-DDB1ΔB as the construct used for SPR, comprising β-propeller A and β-propeller C connected by a short linker. auto_single_measurement only accepted activity measurement [1] 1 structures\9ZXM\9ZXM_metadata.json point structures/9ZXM/9zxm_protein.pdb structures/9ZXM/9zxm_pocket.pdb structures/9ZXM/9zxm_ligand.sdf structures/9ZXM/9zxm_ligand.pdb structures/9ZXM/9zxm_ligand.cif structures/9ZXM/9zxm_complex.pdb structures/9ZXM/9zxm_complex.cif