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Yorodumi- PDB-1ejm: CRYSTAL STRUCTURE OF THE BPTI ALA16LEU MUTANT IN COMPLEX WITH BOV... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ejm | ||||||
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Title | CRYSTAL STRUCTURE OF THE BPTI ALA16LEU MUTANT IN COMPLEX WITH BOVINE TRYPSIN | ||||||
Components |
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Keywords | HYDROLASE/INHIBITOR / Complex / HYDROLASE-INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / potassium channel inhibitor activity / negative regulation of platelet aggregation / zymogen binding / serine protease inhibitor complex / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / cap snatching ...trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / potassium channel inhibitor activity / negative regulation of platelet aggregation / zymogen binding / serine protease inhibitor complex / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / cap snatching / virion component / serine-type endopeptidase inhibitor activity / protease binding / hydrolase activity / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / nucleotide binding / calcium ion binding / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.85 Å | ||||||
Authors | Otlewski, J. / Smalas, A. / Helland, R. / Grzesiak, A. / Krowarsch, D. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases. Authors: Grzesiak, A. / Helland, R. / Smalas, A.O. / Krowarsch, D. / Dadlez, M. / Otlewski, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ejm.cif.gz | 176.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ejm.ent.gz | 146 KB | Display | PDB format |
PDBx/mmJSON format | 1ejm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ejm_validation.pdf.gz | 482 KB | Display | wwPDB validaton report |
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Full document | 1ejm_full_validation.pdf.gz | 493.5 KB | Display | |
Data in XML | 1ejm_validation.xml.gz | 38.8 KB | Display | |
Data in CIF | 1ejm_validation.cif.gz | 55.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ej/1ejm ftp://data.pdbj.org/pub/pdb/validation_reports/ej/1ejm | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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Details | There are 3 complex molecules in the asymmetric unit. |
-Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Details: PURCHASED FROM SIGMA / Source: (natural) Bos taurus (cattle) / Organ: PANCREAS / References: UniProt: P00760, trypsin #2: Protein | Mass: 6579.624 Da / Num. of mol.: 3 / Mutation: K15R, A16L, M52L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Production host: Escherichia coli (E. coli) / References: UniProt: P00974 #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.88 Å3/Da / Density % sol: 68.34 % | ||||||||||||||||||||
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Crystal grow | Temperature: 310 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 48% saturated ammonium sulphate, 0.1 M Hepes buffer, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 37K | ||||||||||||||||||||
Crystal grow | *PLUS Details: Helland, R., (1999) J. Mol. Biol., 287, 923. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Type: ESRF / Wavelength: 0.93 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 18, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→15 Å / Num. all: 1193911 / Num. obs: 119391 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.4 % / Biso Wilson estimate: 30.3 Å2 / Rmerge(I) obs: 0.071 / Net I/σ(I): 5.4 |
Reflection shell | Resolution: 1.85→1.95 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.412 / % possible all: 99.3 |
Reflection | *PLUS Num. measured all: 1360301 |
-Processing
Software |
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Refinement | Resolution: 1.85→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Eng & Huber
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Refinement step | Cycle: LAST / Resolution: 1.85→15 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 15 Å / σ(F): 0 / Rfactor obs: 0.211 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 30.3 Å2 | ||||||||||||||||||||
Refine LS restraints | *PLUS
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