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- PDB-2btc: BOVINE TRYPSIN IN COMPLEX WITH SQUASH SEED INHIBITOR (CUCURBITA P... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2btc | ||||||
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Title | BOVINE TRYPSIN IN COMPLEX WITH SQUASH SEED INHIBITOR (CUCURBITA PEPO TRYPSIN INHIBITOR II) | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEINASE / TRYPSIN INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Helland, R. / Berglund, G.I. / Otlewski, J. / Apostoluk, W. / Andersen, O.A. / Willassen, N.P. / Smalas, A.O. | ||||||
![]() | ![]() Title: High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes. Authors: Helland, R. / Berglund, G.I. / Otlewski, J. / Apostoluk, W. / Andersen, O.A. / Willassen, N.P. / Smalas, A.O. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.6 KB | Display | ![]() |
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PDB format | ![]() | 45.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 418.6 KB | Display | ![]() |
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Full document | ![]() | 421 KB | Display | |
Data in XML | ![]() | 13.2 KB | Display | |
Data in CIF | ![]() | 18.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2staC ![]() 2stbC ![]() 1ppeS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein/peptide | Mass: 3265.932 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 46.92 % | |||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | |||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / PH range low: 5 / PH range high: 4 | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→20 Å / Num. obs: 60871 / % possible obs: 89.8 % / Redundancy: 3.2 % / Biso Wilson estimate: 15.1 Å2 / Rmerge(I) obs: 0.084 |
Reflection | *PLUS Num. measured all: 266925 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1PPE Resolution: 1.5→6 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 18.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.1 Å / Luzzati d res low obs: 6 Å / Luzzati sigma a obs: 0.18 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→6 Å
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Refine LS restraints |
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