reactant_set_id int64 7.11k 51.6M | pmid int64 42.8k 39.4M | protein stringlengths 4 182 | ligand dict | affinity_data dict | DESCRIPTION stringlengths 29 1.83k | search_path listlengths 0 7 | supplementary_source listlengths 0 2 | references_previous stringlengths 4 3.72k | original_paragraph stringlengths 2 88.8k | structured_description stringlengths 529 2.87k ⌀ | assay_type stringclasses 4
values | source_filename stringlengths 10 13 | source_record_key stringlengths 4 8 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
380,914 | 24,257,746 | APC family lysine-specific permease | {
"smiles": "NCCCC[C@@H](N)C(O)=O"
} | {
"type": "Kd",
"value": 1800000,
"relation": "=",
"unit": "nM"
} | ITC measurements were carried out at 20 °C with a VP-ITC calorimeter (GE Healthcare, MicroCal, Inc.) consisting of a 1.45-ml reaction cell. STM2200 in 20 mM MES-NaOH, 150 mM NaCl, 0.025% (w/v) β-DDM, pH 5.9 at concentrations ranging between 15 and 30 μM was titrated with ligands under conditions where the sum... | [
"main"
] | [] | none | {"Figure 3 Caption": "FIGURE 3. Titration calorimetry of STM2200 at 20 °C. A, L-lysine titration of 30 uM STM2200 in 20 mM MES-NaOH, 0.025% (w/v) β-DDM (buffer B) containing 150 mM NaCl, pH 5.9 with 1 × 4 ul and 22 × 5.0 ul of 5 mM L-lysine in buffer B containing 145 mM NaCl, pH 5.9 and corresponding reference titratio... | {"assay_conditions": {"buffer_composition": "20 mM MES-NaOH, 150 mM NaCl, 0.025% (w/v) β-DDM", "control_method": "Titration of ligand into buffer (heats of dilution subtracted)", "injection_parameters": {"duration": null, "first_volume": "4", "spacing": "240-300", "subsequent_volume": "5", "total_count": "23"}, "pH": 5... | itc | 24257746.json | 380914 |
51,070,506 | 24,294,411 | Hexokinase-4 | {
"smiles": "CC(C)Oc1cc(OCCc2ccsc2)cc(c1)C(=O)Nc1ccc(cn1)C(O)=O"
} | {
"type": "Kd",
"value": 170,
"relation": "=",
"unit": "nM"
} | Binding affinity to recombinant wild-type human pancreatic glucokinase expressed in Escherichia coli K-12 at 100 uM by isothermal titration calorimetry in presence of 200 mM glucose | [] | [] | none | {} | null | itc | 24294411.json | 51070506 |
51,070,505 | 24,294,411 | Hexokinase-4 | {
"smiles": "Cc1csc(NC(=O)c2cc(Sc3nncn3C)ccc2N)n1"
} | {
"type": "Kd",
"value": 440,
"relation": "=",
"unit": "nM"
} | Binding affinity to recombinant wild-type human pancreatic glucokinase expressed in Escherichia coli K-12 at 11 uM by isothermal titration calorimetry in presence of 200 mM glucose | [] | [] | none | {} | null | itc | 24294411.json | 51070505 |
51,070,507 | 24,294,411 | Hexokinase-4 | {
"smiles": "CS(=O)(=O)c1ccc(cc1)[C@@H](CC1CCCC1)C(=O)Nc1nccs1"
} | {
"type": "Kd",
"value": 500,
"relation": "=",
"unit": "nM"
} | Binding affinity to recombinant wild-type human pancreatic glucokinase expressed in Escherichia coli K-12 by isothermal titration calorimetry in presence of 200 mM glucose | [] | [] | none | {} | null | itc | 24294411.json | 51070507 |
397,408 | 24,356,970 | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial | {
"smiles": "C[C@@H]1C[C@H]2O[C@@H]2\\C=C/C=C/C(=O)Cc2c(Cl)c(O)cc(O)c2C(=O)O1"
} | {
"type": "Kd",
"value": 18600,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397408 |
397,409 | 24,356,970 | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial | {
"smiles": "Oc1ccc(-c2n[nH]c(=S)n2-c2cccc3ccccc23)c(O)c1"
} | {
"type": "Kd",
"value": 6760,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397409 |
397,410 | 24,356,970 | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial | {
"smiles": "Oc1cc(O)c(cc1Br)C(=O)N1Cc2ccccc2C1"
} | {
"type": "Kd",
"value": 3570,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397410 |
397,411 | 24,356,970 | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial | {
"smiles": "Oc1ccc(C(=O)N2Cc3ccccc3C2)c(O)c1"
} | {
"type": "Kd",
"value": 1827,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397411 |
397,412 | 24,356,970 | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial | {
"smiles": "Oc1ccc(c(O)c1)S(=O)(=O)N1Cc2ccccc2C1"
} | {
"type": "Kd",
"value": 711,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397412 |
397,413 | 24,356,970 | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial | {
"smiles": "Oc1ccc2CN(Cc2c1)S(=O)(=O)c1ccc(O)cc1O"
} | {
"type": "Kd",
"value": 426,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397413 |
397,414 | 24,356,970 | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial | {
"smiles": "Oc1ccc(c(O)c1)S(=O)(=O)N1Cc2cc(O)cc(O)c2C1"
} | {
"type": "Kd",
"value": 239,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397414 |
397,415 | 24,356,970 | Heat shock protein HSP 90-alpha [1-236] | {
"smiles": "C[C@@H]1C[C@H]2O[C@@H]2\\C=C/C=C/C(=O)Cc2c(Cl)c(O)cc(O)c2C(=O)O1"
} | {
"type": "Kd",
"value": 46.3,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397415 |
397,416 | 24,356,970 | Heat shock protein HSP 90-alpha [1-236] | {
"smiles": "Oc1ccc(-c2n[nH]c(=S)n2-c2cccc3ccccc23)c(O)c1"
} | {
"type": "Kd",
"value": 25,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397416 |
397,417 | 24,356,970 | Heat shock protein HSP 90-alpha [1-236] | {
"smiles": "Oc1cc(O)c(cc1Br)C(=O)N1Cc2ccccc2C1"
} | {
"type": "Kd",
"value": 6,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397417 |
397,418 | 24,356,970 | Heat shock protein HSP 90-alpha [1-236] | {
"smiles": "Oc1ccc(C(=O)N2Cc3ccccc3C2)c(O)c1"
} | {
"type": "Kd",
"value": 27.3,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397418 |
397,419 | 24,356,970 | Heat shock protein HSP 90-alpha [1-236] | {
"smiles": "Oc1ccc(c(O)c1)S(=O)(=O)N1Cc2ccccc2C1"
} | {
"type": "Kd",
"value": 50900,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397419 |
397,420 | 24,356,970 | Heat shock protein HSP 90-alpha [1-236] | {
"smiles": "Oc1ccc2CN(Cc2c1)S(=O)(=O)c1ccc(O)cc1O"
} | {
"type": "Kd",
"value": 60100,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397420 |
397,421 | 24,356,970 | Heat shock protein HSP 90-alpha [1-236] | {
"smiles": "Oc1ccc(c(O)c1)S(=O)(=O)N1Cc2cc(O)cc(O)c2C1"
} | {
"type": "Kd",
"value": 47000,
"relation": "=",
"unit": "nM"
} | The PDK2 or Hsp90 N-terminal domain protein was dialyzed against 1 liter of thedialysis buffer containing 50 mM Tris-Cl, pH 7.5, 50 mM KCl, 1 mM MgCl2, and 0.5 mM β-mercaptoethanol. Known or novel PDK inhibitor solutions (150-1500 μM) were placed in the titration syringe and injected in 8-μl increments i... | [
"main"
] | [] | 32. Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C. A., and Schuck, P. (2012) High precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066–5073 | {"Figure 4 Caption": "FIGURE 4. Thermodynamic analysis of inhibitor binding to PDK2 and Hsp90. A, thermograms of PS10 binding to PDK2 and Hsp90 obtained by ITC. B, thermodynamic signatures of inhibitor bindings to PDK2 (left panel) and Hsp90 (right panel); ΔG, Gibbs binding energy; ΔH, binding enthalpy; ΔS, binding ent... | {"assay_conditions": {"buffer_composition": "50 mM Tris-Cl, 50 mM KCl, 1 mM MgCl2, 0.5 mM β-mercaptoethanol", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": "8", "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_spe... | itc | 24356970.json | 397421 |
51,087,552 | 24,363,833 | Biotin--[biotin carboxyl-carrier protein] ligase | {
"smiles": "CC(C)(C)C#Cc1nc(N)c2ncn([C@@H]3O[C@H](COS(=O)(=O)[N-]C(=O)CCCC[C@@H]4SC[C@@H]5NC(=O)N[C@H]45)[C@@H](O)[C@H]3O)c2n1"
} | {
"type": "Kd",
"value": 11,
"relation": "=",
"unit": "nM"
} | Inhibition of biotin binding to Mycobacterium tuberculosis BirA by isothermal titration calorimetry | [
"main"
] | [] | none | {"Associated Content": "Supporting Information All synthetic procedures, ITC experimental methods, and Mtb whole-cell assays. This material is available free of charge via the Internet at http://pubs.acs.org.", "Results Section": "As a result of the tight-binding nature of Bio-AMS 9 and analogues 10−13 and our inabilit... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24363833.json | 51087552 |
51,087,553 | 24,363,833 | Biotin--[biotin carboxyl-carrier protein] ligase | {
"smiles": "Nc1nc2ccccc2c2n(cnc12)[C@@H]1O[C@H](COS(=O)(=O)[N-]C(=O)CCCC[C@@H]2SC[C@@H]3NC(=O)N[C@H]23)[C@@H](O)[C@H]1O"
} | {
"type": "Kd",
"value": 0.23,
"relation": "=",
"unit": "nM"
} | Inhibition of biotin binding to Mycobacterium tuberculosis BirA by isothermal titration calorimetry | [
"main"
] | [] | none | {"Associated Content": "Supporting Information All synthetic procedures, ITC experimental methods, and Mtb whole-cell assays. This material is available free of charge via the Internet at http://pubs.acs.org.", "Results Section": "As a result of the tight-binding nature of Bio-AMS 9 and analogues 10−13 and our inabilit... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24363833.json | 51087553 |
51,087,554 | 24,363,833 | Biotin--[biotin carboxyl-carrier protein] ligase | {
"smiles": "Nc1nccc2n(cnc12)[C@@H]1O[C@H](COS(=O)(=O)[N-]C(=O)CCCC[C@@H]2SC[C@@H]3NC(=O)N[C@H]23)[C@@H](O)[C@H]1O"
} | {
"type": "Kd",
"value": 0.04,
"relation": "=",
"unit": "nM"
} | Inhibition of biotin binding to Mycobacterium tuberculosis BirA by isothermal titration calorimetry | [
"main"
] | [] | none | {"Associated Content": "Supporting Information All synthetic procedures, ITC experimental methods, and Mtb whole-cell assays. This material is available free of charge via the Internet at http://pubs.acs.org.", "Results Section": "As a result of the tight-binding nature of Bio-AMS 9 and analogues 10−13 and our inabilit... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24363833.json | 51087554 |
51,087,555 | 24,363,833 | Biotin--[biotin carboxyl-carrier protein] ligase | {
"smiles": "Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CCS(=O)(=O)[N-]C(=O)CCCC[C@@H]2SC[C@@H]3NC(=O)N[C@H]23)[C@@H](O)[C@H]1O"
} | {
"type": "Kd",
"value": 0.1,
"relation": "=",
"unit": "nM"
} | Inhibition of biotin binding to Mycobacterium tuberculosis BirA by isothermal titration calorimetry | [
"main"
] | [] | none | {"Associated Content": "Supporting Information All synthetic procedures, ITC experimental methods, and Mtb whole-cell assays. This material is available free of charge via the Internet at http://pubs.acs.org.", "Results Section": "As a result of the tight-binding nature of Bio-AMS 9 and analogues 10−13 and our inabilit... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24363833.json | 51087555 |
51,089,375 | 24,436,777 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(C)NC(=O)Cc1cc(C)no1"
} | {
"type": "Kd",
"value": 4300000,
"relation": "=",
"unit": "nM"
} | Displacement of 19-mer HIF-1alpha peptide from VHL (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Results Section": "To assess binding affinity for the displaced compounds, competitive ITC experiments were carried out using inhibitor 2 as the titrant in the presence of fragments 8 and 11, yielding apparent Kd of 2.7 and 4.3 mM for 8 and 11, respectively (Table 1 and Figure S8 and S11, panel g, Supporting Informat... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24436777.json | 51089375 |
51,089,376 | 24,436,777 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)NCc1ccc(cc1)-c1scnc1C"
} | {
"type": "Kd",
"value": 2700000,
"relation": "=",
"unit": "nM"
} | Displacement of 19-mer HIF-1alpha peptide from VHL (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Results Section": "To assess binding affinity for the displaced compounds, competitive ITC experiments were carried out using inhibitor 2 as the titrant in the presence of fragments 8 and 11, yielding apparent Kd of 2.7 and 4.3 mM for 8 and 11, respectively (Table 1 and Figure S8 and S11, panel g, Supporting Informat... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24436777.json | 51089376 |
51,089,377 | 24,436,777 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CNC(=O)[C@@H]1C[C@@H](O)CN1C(C)=O"
} | {
"type": "Kd",
"value": 4900000,
"relation": "=",
"unit": "nM"
} | Displacement of 19-mer HIF-1alpha peptide from VHL (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Results Section": "To assess binding affinity for the displaced compounds, competitive ITC experiments were carried out using inhibitor 2 as the titrant in the presence of fragments 8 and 11, yielding apparent Kd of 2.7 and 4.3 mM for 8 and 11, respectively (Table 1 and Figure S8 and S11, panel g, Supporting Informat... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24436777.json | 51089377 |
51,089,378 | 24,436,777 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CNC(=O)[C@@H]1C[C@@H](O)CN1C(=O)Cc1cc(C)no1"
} | {
"type": "Kd",
"value": 240000,
"relation": "=",
"unit": "nM"
} | Displacement of 19-mer HIF-1alpha peptide from VHL (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Results Section": "To assess binding affinity for the displaced compounds, competitive ITC experiments were carried out using inhibitor 2 as the titrant in the presence of fragments 8 and 11, yielding apparent Kd of 2.7 and 4.3 mM for 8 and 11, respectively (Table 1 and Figure S8 and S11, panel g, Supporting Informat... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24436777.json | 51089378 |
51,089,379 | 24,436,777 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1cnco1"
} | {
"type": "Kd",
"value": 150000,
"relation": "=",
"unit": "nM"
} | Displacement of 19-mer HIF-1alpha peptide from VHL (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Results Section": "To assess binding affinity for the displaced compounds, competitive ITC experiments were carried out using inhibitor 2 as the titrant in the presence of fragments 8 and 11, yielding apparent Kd of 2.7 and 4.3 mM for 8 and 11, respectively (Table 1 and Figure S8 and S11, panel g, Supporting Informat... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24436777.json | 51089379 |
51,089,380 | 24,436,777 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C"
} | {
"type": "Kd",
"value": 36000,
"relation": "=",
"unit": "nM"
} | Displacement of 19-mer HIF-1alpha peptide from VHL (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Results Section": "To assess binding affinity for the displaced compounds, competitive ITC experiments were carried out using inhibitor 2 as the titrant in the presence of fragments 8 and 11, yielding apparent Kd of 2.7 and 4.3 mM for 8 and 11, respectively (Table 1 and Figure S8 and S11, panel g, Supporting Informat... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24436777.json | 51089380 |
51,089,381 | 24,436,777 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "Cc1cc(CC(=O)N2C[C@H](O)C[C@H]2C(=O)NCc2ccc(cc2)-c2cnco2)on1"
} | {
"type": "Kd",
"value": 5500,
"relation": "=",
"unit": "nM"
} | Displacement of 19-mer HIF-1alpha peptide from VHL (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Results Section": "To assess binding affinity for the displaced compounds, competitive ITC experiments were carried out using inhibitor 2 as the titrant in the presence of fragments 8 and 11, yielding apparent Kd of 2.7 and 4.3 mM for 8 and 11, respectively (Table 1 and Figure S8 and S11, panel g, Supporting Informat... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24436777.json | 51089381 |
51,089,382 | 24,436,777 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "Cc1cc(CC(=O)N2C[C@H](O)C[C@H]2C(=O)NCc2ccc(cc2)-c2scnc2C)on1"
} | {
"type": "Kd",
"value": 1500,
"relation": "=",
"unit": "nM"
} | Displacement of 19-mer HIF-1alpha peptide from VHL (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Results Section": "To assess binding affinity for the displaced compounds, competitive ITC experiments were carried out using inhibitor 2 as the titrant in the presence of fragments 8 and 11, yielding apparent Kd of 2.7 and 4.3 mM for 8 and 11, respectively (Table 1 and Figure S8 and S11, panel g, Supporting Informat... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": null}, "data_analysis": {"bind... | itc | 24436777.json | 51089382 |
51,095,203 | 24,476,493 | Type 1 fimbrin D-mannose specific adhesin | {
"smiles": "CCCCCCCOC1OC(CO)C(O)C(O)C1O"
} | {
"type": "Kd",
"value": 17,
"relation": "=",
"unit": "nM"
} | Binding affinity to Escherichia coli J96 wild type FimH lectin domain expressed in Escherichia coli C43 (DE3) by direct ITC analysis | [
"main"
] | [] | none | {"Experimental Section - Isothermal Titration Calorimetry": "Isothermal Titration Calorimetry. Experiments were performed at 25 °C in an ITC200 calorimeter (GE Healthcare, USA). All the protein and sugar solutions were prepared in 20 mM sodium phosphate/100 mM NaCl pH 6.0 and degassed before use. For the direct titrati... | {"assay_conditions": {"buffer_composition": "20 mM sodium phosphate, 100 mM NaCl", "control_method": "integrated data corrected for the heat of dilution of the ligand", "injection_parameters": {"duration": null, "first_volume": null, "spacing": "140", "subsequent_volume": "1.5", "total_count": "26"}, "pH": 6.0, "refere... | itc | 24476493.json | 51095203 |
51,095,204 | 24,476,493 | Type 1 fimbrin D-mannose specific adhesin | {
"smiles": "CCCCCCCOC1OC(CO)C(O)C(O)C1O"
} | {
"type": "Kd",
"value": 19,
"relation": "=",
"unit": "nM"
} | Binding affinity to Escherichia coli J96 wild type FimH lectin domain expressed in Escherichia coli C43 (DE3) by reverse ITC analysis | [
"main"
] | [] | none | {"Experimental Section - Isothermal Titration Calorimetry": "Isothermal Titration Calorimetry. Experiments were performed at 25 °C in an ITC200 calorimeter (GE Healthcare, USA). All the protein and sugar solutions were prepared in 20 mM sodium phosphate/100 mM NaCl pH 6.0 and degassed before use. For the direct titrati... | {"assay_conditions": {"buffer_composition": "20 mM sodium phosphate, 100 mM NaCl", "control_method": "integrated data corrected for the heat of dilution of the ligand", "injection_parameters": {"duration": null, "first_volume": null, "spacing": "140", "subsequent_volume": "1.5", "total_count": "26"}, "pH": 6.0, "refere... | itc | 24476493.json | 51095204 |
50,086,033 | 24,571,165 | Gamma-butyrobetaine dioxygenase | {
"smiles": "CC(CCC([O-])=O)[N+](C)(C)C"
} | {
"type": "Kd",
"value": 4100,
"relation": "=",
"unit": "nM"
} | Binding affinity to purified human BBOX by isothermal titration calorimetry analysis | [
"main"
] | [] | (52) Turnbull, W. B.; Darnaus, A. H. On the value of c: Can low affinity systems be studied by isothermal titration calorimetry? J. Am. Soc. 2003, 125, 14859−14866. | {"Isothermal Calorimetric Experiments": "Isothermal Calorimetric Experiments. All experiments were performed with purified human BBOX in 50 mM N-(2-hydroxyethyl)piperazine-N′-ethanesulfonic acid (HEPES) buffer (pH = 7.4) with 100 mM KCl added for protein stabilization. All protein portions were dialyzed; the same dialy... | {"assay_conditions": {"buffer_composition": "50 mM HEPES, 100 mM KCl", "control_method": "Heats of dilution arising from ligand titration into the buffer were subtracted from the data", "injection_parameters": {"duration": null, "first_volume": "0.2", "spacing": null, "subsequent_volume": "2", "total_count": "20"}, "pH... | itc | 24571165.json | 50086033 |
50,086,034 | 24,571,165 | Gamma-butyrobetaine dioxygenase | {
"smiles": "CN(CCC([O-])=O)[N+](C)(C)C"
} | {
"type": "Kd",
"value": 9300,
"relation": "=",
"unit": "nM"
} | Binding affinity to purified human BBOX by isothermal titration calorimetry analysis | [
"main"
] | [] | (52) Turnbull, W. B.; Darnaus, A. H. On the value of c: Can low affinity systems be studied by isothermal titration calorimetry? J. Am. Soc. 2003, 125, 14859−14866. | {"Isothermal Calorimetric Experiments": "Isothermal Calorimetric Experiments. All experiments were performed with purified human BBOX in 50 mM N-(2-hydroxyethyl)piperazine-N′-ethanesulfonic acid (HEPES) buffer (pH = 7.4) with 100 mM KCl added for protein stabilization. All protein portions were dialyzed; the same dialy... | {"assay_conditions": {"buffer_composition": "50 mM HEPES, 100 mM KCl", "control_method": "Heats of dilution arising from ligand titration into the buffer were subtracted from the data", "injection_parameters": {"duration": null, "first_volume": "0.2", "spacing": null, "subsequent_volume": "2", "total_count": "20"}, "pH... | itc | 24571165.json | 50086034 |
50,088,835 | 24,625,057 | Chromobox protein homolog 1 | {
"smiles": "CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(C)=O)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 43000,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX1 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088835 |
50,088,836 | 24,625,057 | Chromobox protein homolog 1 | {
"smiles": "COC(=O)c1ccc(cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)NC(CO)CO"
} | {
"type": "Kd",
"value": 500000,
"relation": ">",
"unit": "nM"
} | Binding affinity to CBX1 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088836 |
50,088,833 | 24,625,057 | E3 SUMO-protein ligase CBX4 | {
"smiles": "CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(C)=O)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 3700,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX4 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088833 |
50,088,834 | 24,625,057 | E3 SUMO-protein ligase CBX4 | {
"smiles": "COC(=O)c1ccc(cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)NC(CO)CO"
} | {
"type": "Kd",
"value": 290,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX4 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088834 |
50,088,817 | 24,625,057 | Chromobox protein homolog 7 | {
"smiles": "CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(C)=O)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 2000,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX7 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088817 |
50,088,818 | 24,625,057 | Chromobox protein homolog 7 | {
"smiles": "C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(C)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 1770,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX7 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088818 |
50,088,819 | 24,625,057 | Chromobox protein homolog 7 | {
"smiles": "CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(C)=O)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 5400,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX7 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088819 |
50,088,820 | 24,625,057 | Chromobox protein homolog 7 | {
"smiles": "CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(=O)c1ccc(Br)cc1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 280,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX7 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088820 |
50,088,821 | 24,625,057 | Chromobox protein homolog 7 | {
"smiles": "C[C@H](NC(=O)Cc1ccccc1)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)NC(CO)CO"
} | {
"type": "Kd",
"value": 4100,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX7 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088821 |
50,088,822 | 24,625,057 | Chromobox protein homolog 7 | {
"smiles": "C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)c1ccc(Br)cc1)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)NCC[NH3+]"
} | {
"type": "Kd",
"value": 220,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX7 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088822 |
50,088,823 | 24,625,057 | Chromobox protein homolog 7 | {
"smiles": "COC(=O)c1ccc(cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 200,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX7 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088823 |
50,088,824 | 24,625,057 | Chromobox protein homolog 7 | {
"smiles": "COC(=O)c1ccc(cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)NC(CO)CO"
} | {
"type": "Kd",
"value": 200,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX7 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088824 |
50,088,825 | 24,625,057 | Chromobox protein homolog 8 | {
"smiles": "CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(C)=O)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 14200,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX8 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088825 |
50,088,826 | 24,625,057 | Chromobox protein homolog 8 | {
"smiles": "C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(C)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 12300,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX8 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088826 |
50,088,827 | 24,625,057 | Chromobox protein homolog 8 | {
"smiles": "CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(C)=O)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 15000,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX8 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088827 |
50,088,828 | 24,625,057 | Chromobox protein homolog 8 | {
"smiles": "CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(=O)c1ccc(Br)cc1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 1500,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX8 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088828 |
50,088,829 | 24,625,057 | Chromobox protein homolog 8 | {
"smiles": "C[C@H](NC(=O)Cc1ccccc1)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)NC(CO)CO"
} | {
"type": "Kd",
"value": 15000,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX8 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088829 |
50,088,830 | 24,625,057 | Chromobox protein homolog 8 | {
"smiles": "C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)c1ccc(Br)cc1)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)NCC[NH3+]"
} | {
"type": "Kd",
"value": 480,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX8 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088830 |
50,088,831 | 24,625,057 | Chromobox protein homolog 8 | {
"smiles": "COC(=O)c1ccc(cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)N[C@H](CO)C(N)=O"
} | {
"type": "Kd",
"value": 1780,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX8 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088831 |
50,088,832 | 24,625,057 | Chromobox protein homolog 8 | {
"smiles": "COC(=O)c1ccc(cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@@H](C1CCCC1)C(=O)N[C@@H](CCCC[N+](C)(C)C)C(=O)NC(CO)CO"
} | {
"type": "Kd",
"value": 1890,
"relation": "=",
"unit": "nM"
} | Binding affinity to CBX8 (unknown origin) by isothermal titration calorimetry assay | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry Section": "Isothermal Titration Calorimetry. Isothermal titration calorimetry was carried out on a VP-ITC (Microcal, Inc.) at 298 K in Tris-buffered water (20 mM Tris, 250 mM NaCl, 1 mM DTT, pH 8). Inhibitor concentration in the syringe was 0.75−1.0 mM, which was titrated into a sampl... | {"assay_conditions": {"buffer_composition": "20 mM Tris, 250 mM NaCl, 1 mM DTT", "control_method": "subtraction of background heats of dilution", "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 8.0, "reference_cell_content": null, ... | itc | 24625057.json | 50088832 |
50,082,509 | 24,702,184 | cGMP-specific 3',5'-cyclic phosphodiesterase | {
"smiles": "CCCOc1ccc(cc1-c1nc(CC)cc(=O)[nH]1)S(=O)(=O)N1CCN(C)CC1"
} | {
"type": "Kd",
"value": 1500,
"relation": "=",
"unit": "nM"
} | Binding affinity to recombinant PDE5 catalytic domain (unknown origin) by ITC analysis | [
"main"
] | [] | none | {"Figure 2 Caption": "Figure 2. The binding free energy (ΔG), enthalpy (ΔH), and entropy term (−TΔS) of five inhibitors binding to the catalytic domain of PDE5 in solution (A) and ΔΔG, ΔΔH, and Δ(−TΔS) between 1 and the other four inhibitors (B).", "Isothermal Titration Calorimetry (ITC) Section": "Isothermal Titration... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "25"}, "data_analysis": {"bind... | itc | 24702184.json | 50082509 |
50,082,510 | 24,702,184 | cGMP-specific 3',5'-cyclic phosphodiesterase | {
"smiles": "CCCOc1ccc(cc1-c1nc(CC)c(F)c(=O)[nH]1)S(=O)(=O)N1CCN(C)CC1"
} | {
"type": "Kd",
"value": 1700,
"relation": "=",
"unit": "nM"
} | Binding affinity to recombinant PDE5 catalytic domain (unknown origin) by ITC analysis | [
"main"
] | [] | none | {"Figure 2 Caption": "Figure 2. The binding free energy (ΔG), enthalpy (ΔH), and entropy term (−TΔS) of five inhibitors binding to the catalytic domain of PDE5 in solution (A) and ΔΔG, ΔΔH, and Δ(−TΔS) between 1 and the other four inhibitors (B).", "Isothermal Titration Calorimetry (ITC) Section": "Isothermal Titration... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "25"}, "data_analysis": {"bind... | itc | 24702184.json | 50082510 |
50,082,511 | 24,702,184 | cGMP-specific 3',5'-cyclic phosphodiesterase | {
"smiles": "CCCOc1ccc(cc1-c1nc(CC)c(Cl)c(=O)[nH]1)S(=O)(=O)N1CCN(C)CC1"
} | {
"type": "Kd",
"value": 770,
"relation": "=",
"unit": "nM"
} | Binding affinity to recombinant PDE5 catalytic domain (unknown origin) by ITC analysis | [
"main"
] | [] | none | {"Figure 2 Caption": "Figure 2. The binding free energy (ΔG), enthalpy (ΔH), and entropy term (−TΔS) of five inhibitors binding to the catalytic domain of PDE5 in solution (A) and ΔΔG, ΔΔH, and Δ(−TΔS) between 1 and the other four inhibitors (B).", "Isothermal Titration Calorimetry (ITC) Section": "Isothermal Titration... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "25"}, "data_analysis": {"bind... | itc | 24702184.json | 50082511 |
50,082,512 | 24,702,184 | cGMP-specific 3',5'-cyclic phosphodiesterase | {
"smiles": "CCCOc1ccc(cc1-c1nc(CC)c(Br)c(=O)[nH]1)S(=O)(=O)N1CCN(C)CC1"
} | {
"type": "Kd",
"value": 420,
"relation": "=",
"unit": "nM"
} | Binding affinity to recombinant PDE5 catalytic domain (unknown origin) by ITC analysis | [
"main"
] | [] | none | {"Figure 2 Caption": "Figure 2. The binding free energy (ΔG), enthalpy (ΔH), and entropy term (−TΔS) of five inhibitors binding to the catalytic domain of PDE5 in solution (A) and ΔΔG, ΔΔH, and Δ(−TΔS) between 1 and the other four inhibitors (B).", "Isothermal Titration Calorimetry (ITC) Section": "Isothermal Titration... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "25"}, "data_analysis": {"bind... | itc | 24702184.json | 50082512 |
50,082,513 | 24,702,184 | cGMP-specific 3',5'-cyclic phosphodiesterase | {
"smiles": "CCCOc1ccc(cc1-c1nc(CC)c(I)c(=O)[nH]1)S(=O)(=O)N1CCN(C)CC1"
} | {
"type": "Kd",
"value": 150,
"relation": "=",
"unit": "nM"
} | Binding affinity to recombinant PDE5 catalytic domain (unknown origin) by ITC analysis | [
"main"
] | [] | none | {"Figure 2 Caption": "Figure 2. The binding free energy (ΔG), enthalpy (ΔH), and entropy term (−TΔS) of five inhibitors binding to the catalytic domain of PDE5 in solution (A) and ΔΔG, ΔΔH, and Δ(−TΔS) between 1 and the other four inhibitors (B).", "Isothermal Titration Calorimetry (ITC) Section": "Isothermal Titration... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "25"}, "data_analysis": {"bind... | itc | 24702184.json | 50082513 |
50,093,751 | 24,709,560 | Menin | {
"smiles": "NCC1O[C@@H](O[C@@H]2[C@@H](CO)O[C@@H](O[C@H]3[C@H](O)[C@@H](N)C[C@@H](N)[C@@H]3O[C@H]3O[C@H](CN)[C@@H](O)[C@H](O)[C@H]3N)[C@@H]2O)[C@@H](N)[C@H](O)[C@H]1O"
} | {
"type": "Kd",
"value": 15600,
"relation": "=",
"unit": "nM"
} | Binding affinity to menin (unknown origin) by isothermal titration calorimetry analysis | [
"main"
] | [] | none | {"Figure 2 Caption": "Figure 2. Isothermal titration calorimetry experiment confirms the interaction between neomycin and menin with 1:1 stoichiometry.", "Figure 2 Data Labels": "Kd=15.6uM, N=0.871, ΔH=-2.6kcals/mol, TΔS=3.95kcals/mol", "Results Section": "To precisely validate our conclusion, we performed isothermal t... | {"assay_conditions": {"buffer_composition": "50 mM Tris–HCl, 150 mM NaCl", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": 7.5, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "25"},... | itc | 24709560.json | 50093751 |
404,283 | 24,755,226 | Eyes absent homolog 2 [253-538] | {
"smiles": "Fc1cccc(c1)C(=O)N\\N=C\\c1ccc(Sc2ccccn2)o1"
} | {
"type": "Kd",
"value": 2000,
"relation": "=",
"unit": "nM"
} | Eya proteins were purified via S200 in isothermal titration calorimetry (ITC) buffer (50mM NaPO4 buffer, pH 6.5, 50 mM NaCl). Inhibitor solutions were prepared by diluting from a DMSO stock into ITC buffer. DMSO was added to the protein solution to the same concentration as the inhibitor solution (0.2%), and all soluti... | [
"main"
] | [] | none | {"Figure 10 Caption": "FIGURE 10. MLS000544460 likely binds to an allosteric site. A, the proposed allosteric compound binding site is on the opposite face of the active site. Compound is shown as a green ball-and-stick model, and the Mg2+ ion in the active site is represented by a green sphere. B, a docking model demo... | {"assay_conditions": {"buffer_composition": "50 mM NaPO4, 50 mM NaCl, 0.2% DMSO", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "2", "spacing": "300", "subsequent_volume": "10", "total_count": null}, "pH": 6.5, "reference_cell_content": "ITC buffer", "stirring_speed": null, "tempera... | itc | 24755226.json | 404283 |
404,284 | 24,755,226 | Eyes absent homolog 2 [253-538] | {
"smiles": "Fc1cccc(c1)C(=O)N\\N=C\\c1ccc(Sc2ccccn2)o1"
} | {
"type": "Kd",
"value": 6100,
"relation": "=",
"unit": "nM"
} | Eya proteins were purified via S200 in isothermal titration calorimetry (ITC) buffer (50mM NaPO4 buffer, pH 6.5, 50 mM NaCl). Inhibitor solutions were prepared by diluting from a DMSO stock into ITC buffer. DMSO was added to the protein solution to the same concentration as the inhibitor solution (0.2%), and all soluti... | [
"main"
] | [] | none | {"Figure 10 Caption": "FIGURE 10. MLS000544460 likely binds to an allosteric site. A, the proposed allosteric compound binding site is on the opposite face of the active site. Compound is shown as a green ball-and-stick model, and the Mg2+ ion in the active site is represented by a green sphere. B, a docking model demo... | {"assay_conditions": {"buffer_composition": "50 mM NaPO4, 50 mM NaCl, 0.2% DMSO", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "2", "spacing": "300", "subsequent_volume": "10", "total_count": null}, "pH": 6.5, "reference_cell_content": "ITC buffer", "stirring_speed": null, "tempera... | itc | 24755226.json | 404284 |
404,285 | 24,755,226 | Eyes absent homolog 2 [253-538] | {
"smiles": "Fc1cccc(c1)C(=O)N\\N=C\\c1ccc(Sc2ccccn2)o1"
} | {
"type": "Kd",
"value": 800,
"relation": "=",
"unit": "nM"
} | Eya proteins were purified via S200 in isothermal titration calorimetry (ITC) buffer (50mM NaPO4 buffer, pH 6.5, 50 mM NaCl). Inhibitor solutions were prepared by diluting from a DMSO stock into ITC buffer. DMSO was added to the protein solution to the same concentration as the inhibitor solution (0.2%), and all soluti... | [
"main"
] | [] | none | {"Figure 10 Caption": "FIGURE 10. MLS000544460 likely binds to an allosteric site. A, the proposed allosteric compound binding site is on the opposite face of the active site. Compound is shown as a green ball-and-stick model, and the Mg2+ ion in the active site is represented by a green sphere. B, a docking model demo... | {"assay_conditions": {"buffer_composition": "50 mM NaPO4, 50 mM NaCl, 0.2% DMSO", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "2", "spacing": "300", "subsequent_volume": "10", "total_count": null}, "pH": 6.5, "reference_cell_content": "ITC buffer", "stirring_speed": null, "tempera... | itc | 24755226.json | 404285 |
50,101,863 | 24,801,499 | Retinoic acid receptor RXR-alpha | {
"smiles": "CC1CC\\C(=C/C(/C)=C\\C=C\\C(\\C)=C\\C(O)=O)c2ccccc12"
} | {
"type": "Kd",
"value": 1550,
"relation": "=",
"unit": "nM"
} | Agonist activity at human RXR-alpha-ligand binding domain homodimers assessed as coactivator recruitment by measuring GRIP1 binding to receptor by isothermal titration calorimetry | [
"main"
] | [] | (7) Xia, G.; Boerma, L. J.; Cox, B. D.; Qiu, C.; Kang, S.; Smith, C. D.; Renfrow, M. B.; Muccio, D. D. Dynamics, energetics, and dynamics of binding coactivator peptide to the human retinoid X receptor alpha ligand binding domain complex with 9-cis-retinoic acid. Biochemistry 2011, 50, 93−105. (24) Otwinowski, Z.; Mino... | {"Experimental Section 4.5": "4.5. Protein Purification, Crystallization, and X-ray Crystallography. The hRXRα-LBD (T223−L462) was overexpressed in Escherichia coli and purified using AKTA purifier system.7 The hRXRα-LBD homodimers were isolated from a gel filtration chromatography. The protein was mixed with a 4-fold ... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "37"}, "data_analysis": {"bind... | itc | 24801499.json | 50101863 |
50,101,864 | 24,801,499 | Retinoic acid receptor RXR-alpha | {
"smiles": "C\\C(\\C=C\\C1=C(C)CCCC1(C)C)=C\\C=C\\C(\\C)=C\\C(O)=O"
} | {
"type": "Kd",
"value": 1560,
"relation": "=",
"unit": "nM"
} | Agonist activity at human RXR-alpha-ligand binding domain homodimers assessed as coactivator recruitment by measuring GRIP1 binding to receptor by isothermal titration calorimetry | [
"main"
] | [] | (7) Xia, G.; Boerma, L. J.; Cox, B. D.; Qiu, C.; Kang, S.; Smith, C. D.; Renfrow, M. B.; Muccio, D. D. Dynamics, energetics, and dynamics of binding coactivator peptide to the human retinoid X receptor alpha ligand binding domain complex with 9-cis-retinoic acid. Biochemistry 2011, 50, 93−105. (24) Otwinowski, Z.; Mino... | {"Experimental Section 4.5": "4.5. Protein Purification, Crystallization, and X-ray Crystallography. The hRXRα-LBD (T223−L462) was overexpressed in Escherichia coli and purified using AKTA purifier system.7 The hRXRα-LBD homodimers were isolated from a gel filtration chromatography. The protein was mixed with a 4-fold ... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "37"}, "data_analysis": {"bind... | itc | 24801499.json | 50101864 |
50,101,867 | 24,801,499 | Retinoic acid receptor RXR-alpha | {
"smiles": "C/C(/C=C/C=C(/C)\\C=C1/CCCc2cc(C)ccc12)=C\\C(O)=O"
} | {
"type": "Kd",
"value": 1750,
"relation": "=",
"unit": "nM"
} | Agonist activity at human RXR-alpha-ligand binding domain homodimers assessed as coactivator recruitment by measuring GRIP1 binding to receptor by isothermal titration calorimetry | [
"main"
] | [] | (7) Xia, G.; Boerma, L. J.; Cox, B. D.; Qiu, C.; Kang, S.; Smith, C. D.; Renfrow, M. B.; Muccio, D. D. Dynamics, energetics, and dynamics of binding coactivator peptide to the human retinoid X receptor alpha ligand binding domain complex with 9-cis-retinoic acid. Biochemistry 2011, 50, 93−105. (24) Otwinowski, Z.; Mino... | {"Experimental Section 4.5": "4.5. Protein Purification, Crystallization, and X-ray Crystallography. The hRXRα-LBD (T223−L462) was overexpressed in Escherichia coli and purified using AKTA purifier system.7 The hRXRα-LBD homodimers were isolated from a gel filtration chromatography. The protein was mixed with a 4-fold ... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "37"}, "data_analysis": {"bind... | itc | 24801499.json | 50101867 |
50,101,872 | 24,801,499 | Retinoic acid receptor RXR-alpha | {
"smiles": "C/C(/C=C/C=C(/C)\\C=C1/CCCc2ccc(C)cc12)=C\\C(O)=O"
} | {
"type": "Kd",
"value": 1860,
"relation": "=",
"unit": "nM"
} | Agonist activity at human RXR-alpha-ligand binding domain homodimers assessed as coactivator recruitment by measuring GRIP1 binding to receptor by isothermal titration calorimetry | [
"main"
] | [] | (7) Xia, G.; Boerma, L. J.; Cox, B. D.; Qiu, C.; Kang, S.; Smith, C. D.; Renfrow, M. B.; Muccio, D. D. Dynamics, energetics, and dynamics of binding coactivator peptide to the human retinoid X receptor alpha ligand binding domain complex with 9-cis-retinoic acid. Biochemistry 2011, 50, 93−105. (24) Otwinowski, Z.; Mino... | {"Experimental Section 4.5": "4.5. Protein Purification, Crystallization, and X-ray Crystallography. The hRXRα-LBD (T223−L462) was overexpressed in Escherichia coli and purified using AKTA purifier system.7 The hRXRα-LBD homodimers were isolated from a gel filtration chromatography. The protein was mixed with a 4-fold ... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "37"}, "data_analysis": {"bind... | itc | 24801499.json | 50101872 |
50,101,875 | 24,801,499 | Retinoic acid receptor RXR-alpha | {
"smiles": "C/C(/C=C/C=C(/C)\\C=C1/CCCc2ccccc12)=C\\C(O)=O"
} | {
"type": "Kd",
"value": 1880,
"relation": "=",
"unit": "nM"
} | Agonist activity at human RXR-alpha-ligand binding domain homodimers assessed as coactivator recruitment by measuring GRIP1 binding to receptor by isothermal titration calorimetry | [
"main"
] | [] | (7) Xia, G.; Boerma, L. J.; Cox, B. D.; Qiu, C.; Kang, S.; Smith, C. D.; Renfrow, M. B.; Muccio, D. D. Dynamics, energetics, and dynamics of binding coactivator peptide to the human retinoid X receptor alpha ligand binding domain complex with 9-cis-retinoic acid. Biochemistry 2011, 50, 93−105. (24) Otwinowski, Z.; Mino... | {"Experimental Section 4.5": "4.5. Protein Purification, Crystallization, and X-ray Crystallography. The hRXRα-LBD (T223−L462) was overexpressed in Escherichia coli and purified using AKTA purifier system.7 The hRXRα-LBD homodimers were isolated from a gel filtration chromatography. The protein was mixed with a 4-fold ... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "37"}, "data_analysis": {"bind... | itc | 24801499.json | 50101875 |
50,101,878 | 24,801,499 | Retinoic acid receptor RXR-alpha | {
"smiles": "Cc1cc2c(cc1C(=C)c1ccc(cc1)C(O)=O)C(C)(C)CCC2(C)C"
} | {
"type": "Kd",
"value": 1890,
"relation": "=",
"unit": "nM"
} | Agonist activity at human RXR-alpha-ligand binding domain homodimers assessed as coactivator recruitment by measuring GRIP1 binding to receptor by isothermal titration calorimetry | [
"main"
] | [] | (7) Xia, G.; Boerma, L. J.; Cox, B. D.; Qiu, C.; Kang, S.; Smith, C. D.; Renfrow, M. B.; Muccio, D. D. Dynamics, energetics, and dynamics of binding coactivator peptide to the human retinoid X receptor alpha ligand binding domain complex with 9-cis-retinoic acid. Biochemistry 2011, 50, 93−105. (24) Otwinowski, Z.; Mino... | {"Experimental Section 4.5": "4.5. Protein Purification, Crystallization, and X-ray Crystallography. The hRXRα-LBD (T223−L462) was overexpressed in Escherichia coli and purified using AKTA purifier system.7 The hRXRα-LBD homodimers were isolated from a gel filtration chromatography. The protein was mixed with a 4-fold ... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "37"}, "data_analysis": {"bind... | itc | 24801499.json | 50101878 |
50,101,880 | 24,801,499 | Retinoic acid receptor RXR-alpha | {
"smiles": "C/C(/C=C/C=C(/C)\\C=C1/CCCc2c(C)cccc12)=C\\C(O)=O"
} | {
"type": "Kd",
"value": 2240,
"relation": "=",
"unit": "nM"
} | Agonist activity at human RXR-alpha-ligand binding domain homodimers assessed as coactivator recruitment by measuring GRIP1 binding to receptor by isothermal titration calorimetry | [
"main"
] | [] | (7) Xia, G.; Boerma, L. J.; Cox, B. D.; Qiu, C.; Kang, S.; Smith, C. D.; Renfrow, M. B.; Muccio, D. D. Dynamics, energetics, and dynamics of binding coactivator peptide to the human retinoid X receptor alpha ligand binding domain complex with 9-cis-retinoic acid. Biochemistry 2011, 50, 93−105. (24) Otwinowski, Z.; Mino... | {"Experimental Section 4.5": "4.5. Protein Purification, Crystallization, and X-ray Crystallography. The hRXRα-LBD (T223−L462) was overexpressed in Escherichia coli and purified using AKTA purifier system.7 The hRXRα-LBD homodimers were isolated from a gel filtration chromatography. The protein was mixed with a 4-fold ... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "37"}, "data_analysis": {"bind... | itc | 24801499.json | 50101880 |
50,101,881 | 24,801,499 | Retinoic acid receptor RXR-alpha | {
"smiles": "C/C(/C=C/C=C(/C)\\C=C1/CCCc2cccc(C)c12)=C\\C(O)=O"
} | {
"type": "Kd",
"value": 2330,
"relation": "=",
"unit": "nM"
} | Agonist activity at human RXR-alpha-ligand binding domain homodimers assessed as coactivator recruitment by measuring GRIP1 binding to receptor by isothermal titration calorimetry | [
"main"
] | [] | (7) Xia, G.; Boerma, L. J.; Cox, B. D.; Qiu, C.; Kang, S.; Smith, C. D.; Renfrow, M. B.; Muccio, D. D. Dynamics, energetics, and dynamics of binding coactivator peptide to the human retinoid X receptor alpha ligand binding domain complex with 9-cis-retinoic acid. Biochemistry 2011, 50, 93−105. (24) Otwinowski, Z.; Mino... | {"Experimental Section 4.5": "4.5. Protein Purification, Crystallization, and X-ray Crystallography. The hRXRα-LBD (T223−L462) was overexpressed in Escherichia coli and purified using AKTA purifier system.7 The hRXRα-LBD homodimers were isolated from a gel filtration chromatography. The protein was mixed with a 4-fold ... | {"assay_conditions": {"buffer_composition": null, "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": null, "subsequent_volume": null, "total_count": null}, "pH": null, "reference_cell_content": null, "stirring_speed": null, "temperature_c": "37"}, "data_analysis": {"bind... | itc | 24801499.json | 50101881 |
50,101,976 | 24,801,997 | Dihydroorotate dehydrogenase (quinone), mitochondrial | {
"smiles": "Cc1cc(Nc2cc(F)c(c(F)c2)C(F)(F)F)n2nc(nc2n1)C(C)(F)F"
} | {
"type": "Kd",
"value": 48,
"relation": "=",
"unit": "nM"
} | Binding affinity to rat DHODH by isothermal titration calorimetry | [] | [] | none | {"error": "CUDA out of memory. Tried to allocate 2.49 GiB. GPU 0 has a total capacity of 79.22 GiB of which 542.06 MiB is free. Process 3774929 has 6.98 GiB memory in use. Including non-PyTorch memory, this process has 71.69 GiB memory in use. Of the allocated memory 60.82 GiB is allocated by PyTorch, and 10.19 GiB is ... | null | itc | 24801997.json | 50101976 |
404,318 | 24,860,094 | Thiol:disulfide interchange protein [27-205] | {
"smiles": "CC[C@H](C)[C@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](C)N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O"
} | {
"type": "Kd",
"value": 146,
"relation": "=",
"unit": "nM"
} | Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The isothermal titration experiments were performed using either a MicrocalTm ITC200 or an autoITC200 (GE ... | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry (ITC) - Experimental Procedures": "Isothermal Titration Calorimetry (ITC)—Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The iso... | {"assay_conditions": {"buffer_composition": "25 mM HEPES, 100 mM NaCl", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "0.5", "spacing": "180", "subsequent_volume": "2", "total_count": "19"}, "pH": 7.4, "reference_cell_content": null, "stirring_speed": "1000", "temperature_c": "25"},... | itc | 24860094.json | 404318 |
404,319 | 24,860,094 | Thiol:disulfide interchange protein [27-205] | {
"smiles": "CC[C@H](C)[C@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](C)N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O"
} | {
"type": "Kd",
"value": 74,
"relation": "=",
"unit": "nM"
} | Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The isothermal titration experiments were performed using either a MicrocalTm ITC200 or an autoITC200 (GE ... | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry (ITC) - Experimental Procedures": "Isothermal Titration Calorimetry (ITC)—Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The iso... | {"assay_conditions": {"buffer_composition": "25 mM HEPES, 100 mM NaCl", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "0.5", "spacing": "180", "subsequent_volume": "2", "total_count": "19"}, "pH": 7.4, "reference_cell_content": null, "stirring_speed": "1000", "temperature_c": "25"},... | itc | 24860094.json | 404319 |
404,320 | 24,860,094 | Thiol:disulfide interchange protein [27-205] | {
"smiles": "CC[C@H](C)[C@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](C)N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O"
} | {
"type": "Kd",
"value": 162,
"relation": "=",
"unit": "nM"
} | Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The isothermal titration experiments were performed using either a MicrocalTm ITC200 or an autoITC200 (GE ... | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry (ITC) - Experimental Procedures": "Isothermal Titration Calorimetry (ITC)—Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The iso... | {"assay_conditions": {"buffer_composition": "25 mM HEPES, 100 mM NaCl", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "0.5", "spacing": "180", "subsequent_volume": "2", "total_count": "19"}, "pH": 7.4, "reference_cell_content": null, "stirring_speed": "1000", "temperature_c": "25"},... | itc | 24860094.json | 404320 |
404,321 | 24,860,094 | Thiol:disulfide interchange protein [27-205] | {
"smiles": "CC[C@H](C)[C@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](N)CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O"
} | {
"type": "Kd",
"value": 476,
"relation": "=",
"unit": "nM"
} | Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The isothermal titration experiments were performed using either a MicrocalTm ITC200 or an autoITC200 (GE ... | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry (ITC) - Experimental Procedures": "Isothermal Titration Calorimetry (ITC)—Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The iso... | {"assay_conditions": {"buffer_composition": "25 mM HEPES, 100 mM NaCl", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "0.5", "spacing": "180", "subsequent_volume": "2", "total_count": "19"}, "pH": 7.4, "reference_cell_content": null, "stirring_speed": "1000", "temperature_c": "25"},... | itc | 24860094.json | 404321 |
404,322 | 24,860,094 | Thiol:disulfide interchange protein [27-205] | {
"smiles": "CC[C@H](C)[C@H](NC(=O)[C@@H](N)CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O"
} | {
"type": "Kd",
"value": 1675,
"relation": "=",
"unit": "nM"
} | Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The isothermal titration experiments were performed using either a MicrocalTm ITC200 or an autoITC200 (GE ... | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry (ITC) - Experimental Procedures": "Isothermal Titration Calorimetry (ITC)—Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The iso... | {"assay_conditions": {"buffer_composition": "25 mM HEPES, 100 mM NaCl", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "0.5", "spacing": "180", "subsequent_volume": "2", "total_count": "19"}, "pH": 7.4, "reference_cell_content": null, "stirring_speed": "1000", "temperature_c": "25"},... | itc | 24860094.json | 404322 |
404,323 | 24,860,094 | Thiol:disulfide interchange protein [27-205] | {
"smiles": "CC(C)C[C@H](NC(=O)CNC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1)C(O)=O"
} | {
"type": "Kd",
"value": 7.9,
"relation": "=",
"unit": "nM"
} | Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The isothermal titration experiments were performed using either a MicrocalTm ITC200 or an autoITC200 (GE ... | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry (ITC) - Experimental Procedures": "Isothermal Titration Calorimetry (ITC)—Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The iso... | {"assay_conditions": {"buffer_composition": "25 mM HEPES, 100 mM NaCl", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "0.5", "spacing": "180", "subsequent_volume": "2", "total_count": "19"}, "pH": 7.4, "reference_cell_content": null, "stirring_speed": "1000", "temperature_c": "25"},... | itc | 24860094.json | 404323 |
404,324 | 24,860,094 | Thiol:disulfide interchange protein [27-205]/AFDQIDNAPEE | {
"smiles": "CC(C)C[C@H](NC(=O)CNC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1)C(O)=O"
} | {
"type": "Kd",
"value": 9.4,
"relation": "=",
"unit": "nM"
} | Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The isothermal titration experiments were performed using either a MicrocalTm ITC200 or an autoITC200 (GE ... | [
"main"
] | [] | none | {"Isothermal Titration Calorimetry (ITC) - Experimental Procedures": "Isothermal Titration Calorimetry (ITC)—Synthetic peptides were purchased from Genicbio Ltd. Peptides were dissolved in 25 mM HEPES, pH 7.4, 100 mM NaCl (ITC buffer) to obtain 4 mM stock solutions, which were flash-frozen and stored at −80 °C. The iso... | {"assay_conditions": {"buffer_composition": "25 mM HEPES, 100 mM NaCl", "control_method": null, "injection_parameters": {"duration": null, "first_volume": "0.5", "spacing": "180", "subsequent_volume": "2", "total_count": "19"}, "pH": 7.4, "reference_cell_content": null, "stirring_speed": "1000", "temperature_c": "25"},... | itc | 24860094.json | 404324 |
51,086,409 | 24,900,632 | DNA ligase | {
"smiles": "Clc1cncc(n1)-c1nnc[nH]1"
} | {
"type": "Kd",
"value": 38000,
"relation": "=",
"unit": "nM"
} | Binding affinity to C-terminal 6xHis-tagged Staphylococcus aureus DNA ligase (1 to 312) expressed in Escherichia coli BL21 (DE3) by ITC assay | [] | [] | none | {} | null | itc | 24900632.json | 51086409 |
51,086,413 | 24,900,632 | DNA ligase | {
"smiles": "Clc1cccc(n1)-c1nnc[nH]1"
} | {
"type": "Kd",
"value": 10000,
"relation": "=",
"unit": "nM"
} | Binding affinity to C-terminal 6xHis-tagged Staphylococcus aureus DNA ligase (1 to 312) expressed in Escherichia coli BL21 (DE3) by ITC assay | [] | [] | none | {} | null | itc | 24900632.json | 51086413 |
51,086,416 | 24,900,632 | DNA ligase | {
"smiles": "OCCNc1cc(nc(n1)-c1n[nH]c2cnccc12)C(F)(F)F"
} | {
"type": "Kd",
"value": 25,
"relation": "=",
"unit": "nM"
} | Binding affinity to C-terminal 6xHis-tagged Staphylococcus aureus DNA ligase (1 to 312) expressed in Escherichia coli BL21 (DE3) by ITC assay | [] | [] | none | {} | null | itc | 24900632.json | 51086416 |
50,279,917 | 25,032,507 | N-lysine methyltransferase KMT5A | {
"smiles": "COc1cc2nc(nc(NCCCCCN3CCCC3)c2cc1OC)N1CCCC1"
} | {
"type": "Kd",
"value": 18300,
"relation": "=",
"unit": "nM"
} | Inhibition of SETD8 (unknown origin) catalytic domain expressed in Escherichia coli by ITC assay | [
"main"
] | [] | none | {"Figure 3 Caption": "Figure 3. Compound 1 binds SETD8 with a KD of 18.3 ± 3.2 uM (n = 3) in ITC studies.", "ITC and SPR Studies (Results Section)": "ITC and SPR Studies. We next characterized compound 1 in biophysical assays. In ITC studies, compound 1 bound SETD8 with a KD of 18.3 ± 3.2 uM (n = 3) (Figure 3).", "Isot... | {"assay_conditions": {"buffer_composition": "150 mM NaCl", "control_method": "Titration of compound 1 into buffer under identical settings to determine the heat signals that arose from compound dilution; these were subtracted from the heat signals of protein−compound interaction", "injection_parameters": {"duration": n... | itc | 25032507.json | 50279917 |
294,330 | 25,144,524 | Fatty acid-binding protein, intestinal | {
"smiles": "CN(C)c1cccc2c1cccc2S(=O)(=O)NCCCCCCCCCCC(=O)O"
} | {
"type": "Kd",
"value": 360,
"relation": "=",
"unit": "nM"
} | ITC experiments were carried out using an iTC200 microcalorimeter (MicroCal) with coin shaped sample cell (200 μL) at 37 C with stirring at 1000 rpm. Depending on the solubility of the samples, protein was placed in the cell or the syringe for the titration. Compounds that were readily solubilized (ANS, ketorolac ... | [
"main"
] | [] | none | {"Figure 3 Caption": "Figure 3. ITC data of compound titrations with hIFABP. The upper panels show the raw data from individual ITC experiments, and the lower panels show the binding isotherm generated from the corresponding data fitted to the one-site binding site model. (A) Titration of hIFABP (50 uM) with ANS (800 u... | {"assay_conditions": {"buffer_composition": "20 mM HEPES, 50 mM NaCl, 0.5 mM EDTA", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": "220", "subsequent_volume": null, "total_count": "16"}, "pH": 8.0, "reference_cell_content": null, "stirring_speed": "1000", "temperatur... | itc | 25144524.json | 294330 |
294,331 | 25,144,524 | Fatty acid-binding protein, intestinal | {
"smiles": "c1ccc(cc1)Nc2cccc3c2c(ccc3)S(=O)(=O)O"
} | {
"type": "Kd",
"value": 13300,
"relation": "=",
"unit": "nM"
} | ITC experiments were carried out using an iTC200 microcalorimeter (MicroCal) with coin shaped sample cell (200 μL) at 37 C with stirring at 1000 rpm. Depending on the solubility of the samples, protein was placed in the cell or the syringe for the titration. Compounds that were readily solubilized (ANS, ketorolac ... | [
"main"
] | [] | none | {"Figure 3 Caption": "Figure 3. ITC data of compound titrations with hIFABP. The upper panels show the raw data from individual ITC experiments, and the lower panels show the binding isotherm generated from the corresponding data fitted to the one-site binding site model. (A) Titration of hIFABP (50 uM) with ANS (800 u... | {"assay_conditions": {"buffer_composition": "20 mM HEPES, 50 mM NaCl, 0.5 mM EDTA", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": "220", "subsequent_volume": null, "total_count": "16"}, "pH": 8.0, "reference_cell_content": null, "stirring_speed": "1000", "temperatur... | itc | 25144524.json | 294331 |
294,332 | 25,144,524 | Fatty acid-binding protein, intestinal | {
"smiles": "OC(=O)C1CCn2c1ccc2C(=O)c1ccccc1"
} | {
"type": "Kd",
"value": 56700,
"relation": "=",
"unit": "nM"
} | ITC experiments were carried out using an iTC200 microcalorimeter (MicroCal) with coin shaped sample cell (200 μL) at 37 C with stirring at 1000 rpm. Depending on the solubility of the samples, protein was placed in the cell or the syringe for the titration. Compounds that were readily solubilized (ANS, ketorolac ... | [
"main"
] | [] | none | {"Figure 3 Caption": "Figure 3. ITC data of compound titrations with hIFABP. The upper panels show the raw data from individual ITC experiments, and the lower panels show the binding isotherm generated from the corresponding data fitted to the one-site binding site model. (A) Titration of hIFABP (50 uM) with ANS (800 u... | {"assay_conditions": {"buffer_composition": "20 mM HEPES, 50 mM NaCl, 0.5 mM EDTA", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": "220", "subsequent_volume": null, "total_count": "16"}, "pH": 8.0, "reference_cell_content": null, "stirring_speed": "1000", "temperatur... | itc | 25144524.json | 294332 |
294,333 | 25,144,524 | Fatty acid-binding protein, intestinal | {
"smiles": "CC(C)OC(=O)C(C)(C)Oc1ccc(cc1)C(=O)c2ccc(cc2)Cl"
} | {
"type": "Kd",
"value": 4410,
"relation": "=",
"unit": "nM"
} | ITC experiments were carried out using an iTC200 microcalorimeter (MicroCal) with coin shaped sample cell (200 μL) at 37 C with stirring at 1000 rpm. Depending on the solubility of the samples, protein was placed in the cell or the syringe for the titration. Compounds that were readily solubilized (ANS, ketorolac ... | [
"main"
] | [] | none | {"Figure 3 Caption": "Figure 3. ITC data of compound titrations with hIFABP. The upper panels show the raw data from individual ITC experiments, and the lower panels show the binding isotherm generated from the corresponding data fitted to the one-site binding site model. (A) Titration of hIFABP (50 uM) with ANS (800 u... | {"assay_conditions": {"buffer_composition": "20 mM HEPES, 50 mM NaCl, 0.5 mM EDTA", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": "220", "subsequent_volume": null, "total_count": "16"}, "pH": 8.0, "reference_cell_content": null, "stirring_speed": "1000", "temperatur... | itc | 25144524.json | 294333 |
294,334 | 25,144,524 | Fatty acid-binding protein, intestinal | {
"smiles": "CC(C)(C(=O)O)Sc1ccc(cc1)CCN(CCCCC2CCCCC2)C(=O)NC3CCCCC3"
} | {
"type": "Kd",
"value": 1300,
"relation": "=",
"unit": "nM"
} | ITC experiments were carried out using an iTC200 microcalorimeter (MicroCal) with coin shaped sample cell (200 μL) at 37 C with stirring at 1000 rpm. Depending on the solubility of the samples, protein was placed in the cell or the syringe for the titration. Compounds that were readily solubilized (ANS, ketorolac ... | [
"main"
] | [] | none | {"Figure 3 Caption": "Figure 3. ITC data of compound titrations with hIFABP. The upper panels show the raw data from individual ITC experiments, and the lower panels show the binding isotherm generated from the corresponding data fitted to the one-site binding site model. (A) Titration of hIFABP (50 uM) with ANS (800 u... | {"assay_conditions": {"buffer_composition": "20 mM HEPES, 50 mM NaCl, 0.5 mM EDTA", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": "220", "subsequent_volume": null, "total_count": "16"}, "pH": 8.0, "reference_cell_content": null, "stirring_speed": "1000", "temperatur... | itc | 25144524.json | 294334 |
294,335 | 25,144,524 | Fatty acid-binding protein, intestinal | {
"smiles": "CCCc1c(ccc(c1O)C(=O)C)OCCCOc2ccc(cc2)OCC(=O)O"
} | {
"type": "Kd",
"value": 7200,
"relation": "=",
"unit": "nM"
} | ITC experiments were carried out using an iTC200 microcalorimeter (MicroCal) with coin shaped sample cell (200 μL) at 37 C with stirring at 1000 rpm. Depending on the solubility of the samples, protein was placed in the cell or the syringe for the titration. Compounds that were readily solubilized (ANS, ketorolac ... | [
"main"
] | [] | none | {"Figure 3 Caption": "Figure 3. ITC data of compound titrations with hIFABP. The upper panels show the raw data from individual ITC experiments, and the lower panels show the binding isotherm generated from the corresponding data fitted to the one-site binding site model. (A) Titration of hIFABP (50 uM) with ANS (800 u... | {"assay_conditions": {"buffer_composition": "20 mM HEPES, 50 mM NaCl, 0.5 mM EDTA", "control_method": null, "injection_parameters": {"duration": null, "first_volume": null, "spacing": "220", "subsequent_volume": null, "total_count": "16"}, "pH": 8.0, "reference_cell_content": null, "stirring_speed": "1000", "temperatur... | itc | 25144524.json | 294335 |
50,367,080 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N1Cc2ccccc2C[C@H]1C(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C"
} | {
"type": "Kd",
"value": 2320,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367080 |
50,367,081 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N[C@H](C(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C)c1ccccc1"
} | {
"type": "Kd",
"value": 2040,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367081 |
50,367,082 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N[C@H](C(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C)C(C)(C)C"
} | {
"type": "Kd",
"value": 9520,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367082 |
50,367,083 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C"
} | {
"type": "Kd",
"value": 291,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367083 |
50,367,084 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(C)C[C@H](NC(C)=O)C(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C"
} | {
"type": "Kd",
"value": 588,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367084 |
50,367,085 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "C[C@H](NC(C)=O)C(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C"
} | {
"type": "Kd",
"value": 943,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367085 |
50,367,086 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N1CCCC[C@H]1C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C"
} | {
"type": "Kd",
"value": 384,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367086 |
50,367,087 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N1C[C@H](O)C[C@H]1C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C"
} | {
"type": "Kd",
"value": 1100,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367087 |
50,367,088 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N1CCC[C@H]1C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C"
} | {
"type": "Kd",
"value": 714,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367088 |
50,367,089 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)c1ccccc1"
} | {
"type": "Kd",
"value": 826,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367089 |
50,367,090 | 25,166,285 | von Hippel-Lindau disease tumor suppressor | {
"smiles": "CC(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C"
} | {
"type": "Kd",
"value": 185,
"relation": "=",
"unit": "nM"
} | Binding affinity to N-terminal His6-tagged pVHL (54 to 213 amino acids) (unknown origin) expressed in Escherichia coli BL21 (DE3) by isothermal titration calorimetry | [] | [] | none | {} | null | itc | 25166285.json | 50367090 |
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