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- PDB-1ban: THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: T... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ban | ||||||
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Title | THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: THE CRYSTAL STRUCTURES OF TWO 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. / Fersht, A.R. / Henrick, K. | ||||||
![]() | ![]() 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: 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: ![]() 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 | ![]() | 80 KB | Display | ![]() |
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PDB format | ![]() | 60.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 429.9 KB | Display | ![]() |
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Full document | ![]() | 449.2 KB | Display | |
Data in XML | ![]() | 19.2 KB | Display | |
Data in CIF | ![]() | 26.9 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: WATERS A 6, A 11, A 19, A 21, A 41, A 64, A 69, B 60 AND C 92 ARE DISORDERED. |
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Components
#1: Protein | Mass: 12382.721 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: 2.28 Å3/Da / Density % sol: 45.94 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS 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: 2.2 Å / Lowest resolution: 6 Å / Num. obs: 16276 / % possible obs: 97.8 % / Num. measured all: 39235 / Rmerge(I) obs: 0.139 |
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Processing
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Refinement | Resolution: 2.2→6 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 2.2→6 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection all: 15464 / Rfactor obs: 0.176 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |