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Open data
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Basic information
Entry | Database: PDB / ID: 1b2u | ||||||
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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 | ![]() Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA endonuclease activity / RNA binding / extracellular region / cytoplasm 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 | ![]() | 137 KB | Display | ![]() |
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PDB format | ![]() | 107.3 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 ![]() 1b3sC ![]() 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: 12340.618 Da / Num. of mol.: 3 / Mutation: K27A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 10308.729 Da / Num. of mol.: 3 / Mutation: D36A 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: 2.49 Å3/Da / Density % sol: 51 % Description: THE STRUCTURE WAS SOLVED BY RIGID BODY REFINEMENT OF PDB ENTRY 1BRS IN THE ASYMMETRIC UNIT | ||||||||||||||||||||
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Crystal grow | pH: 6.5 Details: 21% PEG-8K 0.2 M AMMONIUM SULPHATE 0.1 M NA CACODYLATE PH6.5 | ||||||||||||||||||||
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: Jan 1, 1996 / Details: SUPER DOUBLE MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→22.3 Å / Num. obs: 32841 / % possible obs: 98.9 % / Redundancy: 3.6 % / Biso Wilson estimate: 24.56 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 14.45 |
Reflection shell | Resolution: 2.1→2.15 Å / Redundancy: 3 % / Rmerge(I) obs: 0.298 / Mean I/σ(I) obs: 4 / % possible all: 98.9 |
Reflection | *PLUS Rmerge(I) obs: 0.065 |
Reflection shell | *PLUS % possible obs: 99.7 % |
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Processing
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Refinement | Method to determine structure: OTHER Starting model: PDB ENTRY 1BRS Resolution: 2.1→21.3 Å / SU B: 5.9 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 29.17 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→21.3 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 21.3 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.214 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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