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Open data
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Basic information
Entry | Database: PDB / ID: 1b3s | ||||||
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Title | STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / RNASE-INHIBITOR COMPLEX / INTERFACIAL DOUBLE MUTANT / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Vaughan, C.K. / Buckle, A.M. / Fersht, A.R. | ||||||
![]() | ![]() Title: Structural response to mutation at a protein-protein interface. Authors: Vaughan, C.K. / Buckle, A.M. / Fersht, A.R. #1: ![]() Title: Protein-Protein Recognition: Crystal Structural Analysis of a Barnase-Barstar Complex at 2.0-A Resolution Authors: Buckle, A.M. / Schreiber, G. / Fersht, A.R. #2: ![]() Title: Stability and Function: Two Constraints in the Evolution of Barstar and Other Proteins Authors: Schreiber, G. / Buckle, A.M. / Fersht, A.R. #3: ![]() Title: Recognition between a Bacterial Ribonuclease, Barnase, and its Natural Inhibitor, Barstar Authors: Guillet, V. / Lapthorn, A. / Hartley, R.W. / Mauguen, Y. #4: ![]() Title: Interaction of Barnase with its Polypeptide Inhibitor Barstar Studied by Protein Engineering Authors: Schreiber, G. / Fersht, A.R. #5: ![]() 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 | ![]() | 129.5 KB | Display | ![]() |
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PDB format | ![]() | 101.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1b27C ![]() 1b2sC ![]() 1b2uC ![]() 1brsS S: Starting model for refinement 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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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 12331.651 Da / Num. of mol.: 3 / Mutation: H102A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() #2: Protein | Mass: 10336.739 Da / Num. of mol.: 3 / Mutation: Y30F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() #3: Water | ChemComp-HOH / | ![]() Sequence details | TER SER: THE ORIGINAL SEQUENCE OF BARSTAR OMITTED AN N-TERMINAL METHIONINE, WHICH WAS VISIBLE IN ...TER SER: THE ORIGINAL SEQUENCE OF BARSTAR OMITTED AN N-TERMINAL METHIONINE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 53 % Description: RIGID-BODY REFINEMENT OF 1BRS WAS USED TO SOLVE THE STRUCTURE | |||||||||||||||||||||||||
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Crystal grow![]() | pH: 8 / Details: 0.2M (NH4)2SO4; 0.1M TRIS/HCL PH 8.0: 22% PEG-8000 | |||||||||||||||||||||||||
Components of the solutions |
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 1, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.391→38.925 Å / Num. obs: 26773 / % possible obs: 96.2 % / Redundancy: 3.2 % / Biso Wilson estimate: 45.7 Å2 / Rmerge(I) obs: 0.098 / Net I/σ(I): 9.42 |
Reflection shell | Resolution: 2.39→2.52 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.242 / Mean I/σ(I) obs: 2.51 / % possible all: 90 |
Reflection shell | *PLUS % possible obs: 90 % |
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Processing
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Refinement | Method to determine structure![]() Starting model: PDB ENTRY 1BRS Resolution: 2.39→25 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 34 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.39→25 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 25 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.247 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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