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- PDB-1smf: Studies on an artificial trypsin inhibitor peptide derived from t... -
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Open data
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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 | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / PROTEINASE / 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 | ![]() | ||||||
![]() | Huang, Q. / Li, Y. / Zhang, S. / Liu, S. / Tang, Y. / Qi, C. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64 KB | Display | ![]() |
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PDB format | ![]() | 50.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.4 KB | Display | ![]() |
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Full document | ![]() | 428.1 KB | Display | |
Data in XML | ![]() | 11.6 KB | Display | |
Data in CIF | ![]() | 15.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: CIS PROLINE - PRO I 14 |
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Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||||
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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: ![]() |
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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 |
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Processing
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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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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