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Open data
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Basic information
Entry | Database: PDB / ID: 1bns | ||||||
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Title | STRUCTURAL STUDIES OF BARNASE MUTANTS | ||||||
![]() | BARNASE | ||||||
![]() | ENDONUCLEASE | ||||||
Function / homology | ![]() Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA endonuclease activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Chen, Y.W. | ||||||
![]() | ![]() Title: Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants. Authors: Chen, Y.W. / Fersht, A.R. / Henrick, K. #1: ![]() Title: Capping and Alpha-Helix Stability Authors: Serrano, L. / Fersht, A.R. #2: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.1 KB | Display | ![]() |
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PDB format | ![]() | 59.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 427.8 KB | Display | ![]() |
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Full document | ![]() | 442.8 KB | Display | |
Data in XML | ![]() | 18.2 KB | Display | |
Data in CIF | ![]() | 25.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Atom site foot note | 1: RESIDUE HIS B 102 HAS ALTERNATE CONFORMATIONS FOR ITS SIDE CHAINS. |
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Components
#1: Protein | Mass: 12368.694 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: 2.25 Å3/Da / Density % sol: 45.4 % |
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Num. obs: 41566 / % possible obs: 75 % / Num. measured all: 93923 / Rmerge(I) obs: 0.039 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.05→6 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 2.05→6 Å
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Refine LS restraints |
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