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Open data
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Basic information
Entry | Database: PDB / ID: 1bni | ||||||
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Title | BARNASE WILDTYPE STRUCTURE AT PH 6.0 | ||||||
![]() | BARNASE | ||||||
![]() | MICROBIAL RIBONUCLEASE / ALPHA/BETA PROTEIN | ||||||
Function / homology | ![]() Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA endonuclease activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Cameron, A. / Henrick, K. / Fersht, A.R. / Dodson, G. / Buckle, A.M. | ||||||
![]() | ![]() Title: Crystal structural analysis of mutations in the hydrophobic cores of barnase. Authors: Buckle, A.M. / Henrick, K. / Fersht, A.R. #1: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.6 KB | Display | ![]() |
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PDB format | ![]() | 59.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 382.1 KB | Display | ![]() |
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Full document | ![]() | 407.1 KB | Display | |
Data in XML | ![]() | 10.8 KB | Display | |
Data in CIF | ![]() | 16.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bnjC ![]() 1bsaC ![]() 1bsbC ![]() 1bscC ![]() 1bsdC ![]() 1bseC C: citing same article ( |
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Similar structure data |
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Links
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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: 12398.721 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() 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: ![]() |
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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: ![]() ![]() ![]() |
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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 |
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Processing
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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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