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Yorodumi- PDB-1s02: EFFECTS OF ENGINEERED SALT BRIDGES ON THE STABILITY OF SUBTILISIN BPN' -
+Open data
-Basic information
Entry | Database: PDB / ID: 1s02 | ||||||
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Title | EFFECTS OF ENGINEERED SALT BRIDGES ON THE STABILITY OF SUBTILISIN BPN' | ||||||
Components | SUBTILISIN BPN' | ||||||
Keywords | HYDROLASE (SERINE PROTEINASE) | ||||||
Function / homology | Function and homology information subtilisin / sporulation resulting in formation of a cellular spore / fibrinolysis / serine-type endopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Bacillus amyloliquefaciens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Erwin, C.R. / Barnett, B.L. / Oliver, J.D. / Sullivan, J.F. | ||||||
Citation | Journal: Protein Eng. / Year: 1990 Title: Effects of engineered salt bridges on the stability of subtilisin BPN'. Authors: Erwin, C.R. / Barnett, B.L. / Oliver, J.D. / Sullivan, J.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1s02.cif.gz | 63.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1s02.ent.gz | 46.2 KB | Display | PDB format |
PDBx/mmJSON format | 1s02.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s0/1s02 ftp://data.pdbj.org/pub/pdb/validation_reports/s0/1s02 | 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: RESIDUE 168 IS A CIS PROLINE. |
-Components
#1: Protein | Mass: 27554.494 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: Chemical | #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | Nonpolymer details | THE SULFATE ION HAS AN INTRAMOLECULAR INTERACTION WITH ND1 HIS 238 AND HAS INTERMOLECULAR ...THE SULFATE ION HAS AN INTRAMOLEC | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37.21 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 9999 / % possible obs: 56.3 % / Num. measured all: 59579 / Rmerge(I) obs: 0.085 |
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-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.169 / Highest resolution: 1.9 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.9 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.9 Å / Rfactor obs: 0.169 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |