+Open data
-Basic information
Entry | Database: PDB / ID: 1bnf | ||||||
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Title | BARNASE T70C/S92C DISULFIDE MUTANT | ||||||
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 / SYNCHROTRON / Resolution: 2 Å | ||||||
Authors | Clarke, J. / Henrick, K. / Fersht, A.R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Disulfide mutants of barnase. I: Changes in stability and structure assessed by biophysical methods and X-ray crystallography. Authors: Clarke, J. / Henrick, K. / Fersht, A.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bnf.cif.gz | 74.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bnf.ent.gz | 60.5 KB | Display | PDB format |
PDBx/mmJSON format | 1bnf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bn/1bnf ftp://data.pdbj.org/pub/pdb/validation_reports/bn/1bnf | HTTPS FTP |
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-Related 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: 12416.825 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Gene: BARNASE / Plasmid: PTZ18 DERIVED / Gene (production host): BARNASE / 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: 2.22 Å3/Da / Density % sol: 44.5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 37.3 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: SRS / Type: SRS |
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Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: 1993 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 20982 / % possible obs: 97.2 % / Observed criterion σ(I): 3 / Redundancy: 2.41 % / Rmerge(I) obs: 0.122 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 10.3 Å / Num. measured all: 50660 / Rmerge(I) obs: 0.122 |
-Processing
Software |
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Refinement | Resolution: 2→6 Å / σ(F): 0 Details: SSBOND THERE IS TWO-FOLD DISORDER IN THE ENGINEERED DISULFIDE BOND IN ALL THREE CHAINS, A, B, AND C.
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Displacement parameters | Biso mean: 13.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 20982 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |