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Yorodumi- PDB-1smf: Studies on an artificial trypsin inhibitor peptide derived from t... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1smf | ||||||
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Title | Studies on an artificial trypsin inhibitor peptide derived from the mung bean inhibitor | ||||||
Components |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information 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 | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.1 Å | ||||||
Authors | Huang, Q. / Li, Y. / Zhang, S. / Liu, S. / Tang, Y. / Qi, C. | ||||||
Citation | Journal: J.Biochem.(Tokyo) / Year: 1994 Title: Studies on an artificial trypsin inhibitor peptide derived from the mung bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin. Authors: Li, Y. / Huang, Q. / Zhang, S. / Liu, S. / Chi, C. / Tang, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1smf.cif.gz | 64 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1smf.ent.gz | 50.7 KB | Display | PDB format |
PDBx/mmJSON format | 1smf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sm/1smf ftp://data.pdbj.org/pub/pdb/validation_reports/sm/1smf | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO I 14 |
-Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Tissue: PANCREAS / References: UniProt: P00760, trypsin | ||||
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#2: Protein/peptide | Mass: 2412.808 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P01062 | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | BOWMAN-BIRK INHIBITOR IS A SYNTHESIZED PEPTIDE BASED ON MIMIC MUNG BEAN TRYPSIN INHIBITOR LYSINE ...BOWMAN-BIRK INHIBITOR IS A SYNTHESIZE | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.71 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 24 ℃ / pH: 6.4 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.2 Å / Num. obs: 12563 / % possible obs: 82.8 % / Num. measured all: 42768 / Rmerge(I) obs: 0.0768 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.19 / Rfactor obs: 0.19 / Highest resolution: 2.1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.1 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.193 / Rfactor Rwork: 0.193 / Highest resolution: 2.2 Å / Lowest resolution: 7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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