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Yorodumi- PDB-1bsb: CRYSTAL STRUCTURAL ANALYSIS OF MUTATIONS IN THE HYDROPHOBIC CORES... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bsb | ||||||
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Title | CRYSTAL STRUCTURAL ANALYSIS OF MUTATIONS IN THE HYDROPHOBIC CORES OF BARNASE | ||||||
Components | BARNASE | ||||||
Keywords | ENDONUCLEASE | ||||||
Function / homology | Function and homology information Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA endonuclease activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | Bacillus amyloliquefaciens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Buckle, A.M. / Henrick, K. / Fersht, A.R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1993 Title: Crystal structural analysis of mutations in the hydrophobic cores of barnase. Authors: Buckle, A.M. / Henrick, K. / Fersht, A.R. #1: Journal: J.Mol.Biol. / Year: 1992 Title: The Folding of an Enzyme. II. Substructure of Barnase and the Contribution of Different Interactions to Protein Stability Authors: Serrano, L. / Kellis Junior, J.T. / Cann, P. / Matouschek, A. / Fersht, A.R. #2: Journal: Nature / Year: 1982 Title: Molecular Structures of a New Family of Ribonucleases Authors: Mauguen, Y. / Hartley, R.W. / Dodson, E.J. / Dodson, G.G. / Bricogne, G. / Chothia, C. / Jack, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bsb.cif.gz | 78.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bsb.ent.gz | 60.7 KB | Display | PDB format |
PDBx/mmJSON format | 1bsb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bs/1bsb ftp://data.pdbj.org/pub/pdb/validation_reports/bs/1bsb | HTTPS FTP |
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-Related structure data
Related structure data | 1bniC 1bnjC 1bsaC 1bscC 1bsdC 1bseC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 12384.694 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) References: UniProt: P00648, Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.73 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 23 ℃ / pH: 7.5 / 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 Å / % possible obs: 90.5 % / Observed criterion σ(F): 27.7 / Rmerge(I) obs: 0.065 |
-Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.166 / Highest resolution: 2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 6 Å / σ(F): 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 16.4 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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