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Yorodumi- PDB-1f2s: CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1f2s | |||||||||
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Title | CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY AT 1.8 A RESOLUTION | |||||||||
Components |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / PROTEINASE-INHIBITOR COMPLEX / TRYPSIN / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | |||||||||
Function / homology | Function and homology information trypsin / serpin family protein binding / digestion / serine protease inhibitor complex / serine-type endopeptidase inhibitor activity / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | |||||||||
Biological species | Bos taurus (cattle) Momordica charantia (bitter melon) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.79 Å | |||||||||
Authors | Zhu, Y. / Huang, Q. / Qian, M. / Jia, Y. / Tang, Y. | |||||||||
Citation | Journal: J.Protein Chem. / Year: 1999 Title: Crystal structure of the complex formed between bovine beta-trypsin and MCTI-A, a trypsin inhibitor of squash family, at 1.8-A resolution. Authors: Zhu, Y. / Huang, Q. / Qian, M. / Jia, Y. / Tang, Y. #1: Journal: J.Mol.Biol. / Year: 1993 Title: REFINED 1.6A RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN PORCINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF THE SQUASH FAMILY Authors: Huang, Q. / Liu, S. / Tang, Y. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f2s.cif.gz | 65 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f2s.ent.gz | 45.8 KB | Display | PDB format |
PDBx/mmJSON format | 1f2s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f2/1f2s ftp://data.pdbj.org/pub/pdb/validation_reports/f2/1f2s | HTTPS FTP |
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-Related structure data
Related structure data | 1ppeS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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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 / Details: PANCREATIC / Source: (natural) Bos taurus (cattle) / Organ: PANCREATICPancreas / References: UniProt: P00760, trypsin |
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#2: Protein/peptide | Mass: 3251.958 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SEED / Source: (natural) Momordica charantia (bitter melon) / References: UniProt: P10295 |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.09 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 5.1 Details: PEG6000, soduim phosphate buffer, pH 5.10, VAPOR DIFFUSION, HANGING DROP, temperature 295K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 5 Details: drop consists of equal volume of protein and precipitant solutions | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 297 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54178 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Oct 26, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.79→75 Å / Num. all: 23032 / Num. obs: 20741 / % possible obs: 86.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 5.7 % / Biso Wilson estimate: 20.9 Å2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 8.7 |
Reflection shell | Resolution: 1.79→1.86 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.213 / Num. unique all: 1607 / % possible all: 63.4 |
Reflection shell | *PLUS % possible obs: 63.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1PPE Resolution: 1.79→7 Å / σ(F): 2 / σ(I): 1 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.79→7 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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