+Open data
-Basic information
Entry | Database: PDB / ID: 1bni | ||||||
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Title | BARNASE WILDTYPE STRUCTURE AT PH 6.0 | ||||||
Components | BARNASE | ||||||
Keywords | MICROBIAL RIBONUCLEASE / ALPHA/BETA PROTEIN | ||||||
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 / SYNCHROTRON / Resolution: 2.1 Å | ||||||
Authors | Cameron, A. / Henrick, K. / Fersht, A.R. / Dodson, G. / Buckle, A.M. | ||||||
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: Nature / Year: 1982 Title: Molecular Structure 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 | 1bni.cif.gz | 78.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bni.ent.gz | 59.9 KB | Display | PDB format |
PDBx/mmJSON format | 1bni.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bni_validation.pdf.gz | 382.1 KB | Display | wwPDB validaton report |
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Full document | 1bni_full_validation.pdf.gz | 407.1 KB | Display | |
Data in XML | 1bni_validation.xml.gz | 10.8 KB | Display | |
Data in CIF | 1bni_validation.cif.gz | 16.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bn/1bni ftp://data.pdbj.org/pub/pdb/validation_reports/bn/1bni | HTTPS FTP |
-Related structure data
Related structure data | 1bnjC 1bsaC 1bsbC 1bscC 1bsdC 1bseC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 12398.721 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Plasmid: PUC19 / Production host: Escherichia coli (E. coli) 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: 2.26 Å3/Da / Density % sol: 45.58 % | |||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 23 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX7.2 / Wavelength: 1.488 |
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Detector | Detector: FILM |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→10 Å / Num. obs: 16312 / % possible obs: 80 % / Observed criterion σ(I): 3 / Redundancy: 2.2 % / Rmerge(I) obs: 0.089 |
Reflection | *PLUS Rmerge(I) obs: 0.089 |
-Processing
Software |
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Refinement | Resolution: 2.1→10 Å / σ(F): 0 /
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Displacement parameters | Biso mean: 15.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→10 Å
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Refine LS restraints |
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