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Yorodumi- PDB-2sic: REFINED CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILISIN BPN' AND S... -
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-Basic information
Entry | Database: PDB / ID: 2sic | |||||||||
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Title | REFINED CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILISIN BPN' AND STREPTOMYCES SUBTILISIN INHIBITOR AT 1.8 ANGSTROMS RESOLUTION | |||||||||
Components |
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Keywords | COMPLEX (PROTEINASE/INHIBITOR) / COMPLEX (PROTEINASE-INHIBITOR) / COMPLEX (PROTEINASE-INHIBITOR) complex | |||||||||
Function / homology | Function and homology information subtilisin / sporulation resulting in formation of a cellular spore / fibrinolysis / serine-type endopeptidase inhibitor activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | |||||||||
Biological species | Bacillus amyloliquefaciens (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | |||||||||
Authors | Mitsui, Y. / Takeuchi, Y. / Hirono, S. / Akagawa, H. / Nakamura, K.T. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1991 Title: Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution. Authors: Takeuchi, Y. / Satow, Y. / Nakamura, K.T. / Mitsui, Y. #1: Journal: J.Mol.Biol. / Year: 1984 Title: Crystal Structure at 2.6 Angstroms Resolution of the Complex of Subtilisin with Bpn' with Streptomyces Subtilisin Inhibitor Authors: Hirono, S. / Akagawa, H. / Mitsui, Y. / Iitaka, Y. #2: Journal: J.Mol.Biol. / Year: 1979 Title: Crystal Structure of the Complex of Subtilisin Bpn' with its Protein Inhibitor Streptomyces Subtilisin Inhibitor Authors: Hirono, S. / Nakamura, K.T. / Iitaka, Y. / Mitsui, Y. #3: Journal: Nature / Year: 1979 Title: Crystal Structures of Streptomyces Subtilisin Inhibitor and its Complex with Subtilisin Bpn' Authors: Mitsui, Y. / Satow, Y. / Watanabe, Y. / Hirono, S. / Iitaka, Y. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2sic.cif.gz | 83.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2sic.ent.gz | 65.6 KB | Display | PDB format |
PDBx/mmJSON format | 2sic.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2sic_validation.pdf.gz | 373.2 KB | Display | wwPDB validaton report |
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Full document | 2sic_full_validation.pdf.gz | 388.2 KB | Display | |
Data in XML | 2sic_validation.xml.gz | 11 KB | Display | |
Data in CIF | 2sic_validation.cif.gz | 17.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/si/2sic ftp://data.pdbj.org/pub/pdb/validation_reports/si/2sic | HTTPS FTP |
-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: RESIDUES PRO E 168 AND PRO I 37 ARE CIS PROLINES. |
-Components
#1: Protein | Mass: 27552.525 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / References: UniProt: P00782, 3.4.21.14 | ||
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#2: Protein | Mass: 10940.334 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P01006 | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.24 Å3/Da / Density % sol: 62.02 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: unknownDetails: used seeding, Hirono, S., (1979) J.Mol.Biol., 131, 855. | ||||||||||||||||||||||||
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: 1.8 Å / Num. obs: 28118 / Observed criterion σ(F): 2 / Num. measured all: 97766 / Rmerge(I) obs: 0.0472 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→6 Å /
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Refinement step | Cycle: LAST / Resolution: 1.8→6 Å
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Refine LS restraints |
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