[English] 日本語
![](img/lk-miru.gif)
- PDB-1ejm: CRYSTAL STRUCTURE OF THE BPTI ALA16LEU MUTANT IN COMPLEX WITH BOV... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1ejm | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF THE BPTI ALA16LEU MUTANT IN COMPLEX WITH BOVINE TRYPSIN | ||||||
![]() |
| ||||||
![]() | HYDROLASE/INHIBITOR / Complex / HYDROLASE-INHIBITOR COMPLEX | ||||||
Function / homology | ![]() trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / trypsin / serpin family protein binding ...trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / protease binding / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Otlewski, J. / Smalas, A. / Helland, R. / Grzesiak, A. / Krowarsch, D. | ||||||
![]() | ![]() 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 176.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 146 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 482 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 493.5 KB | Display | |
Data in XML | ![]() | 38.8 KB | Display | |
Data in CIF | ![]() | 55.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
Unit cell |
| ||||||||
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) ![]() ![]() #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.) ![]() ![]() ![]() ![]() #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.88 Å3/Da / Density % sol: 68.34 % | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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
|
-Data collection
Diffraction | Mean temperature: 120 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() ![]() ![]() |
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 |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.85→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Eng & Huber
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.85→15 Å
| ||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||
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
|