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- PDB-1bgs: RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bgs | ||||||
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Title | RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR | ||||||
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Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Guillet, V. / Lapthorn, A. / Mauguen, Y. | ||||||
![]() | ![]() Title: Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar. Authors: Guillet, V. / Lapthorn, A. / Hartley, R.W. / Mauguen, Y. #1: ![]() Title: Crystallization and Preliminary X-Ray Investigation of Barstar, the Intracellular Inhibitor of Barnase Authors: Guillet, V. / Lapthorn, A. / Fourniat, J. / Benoit, J.P. / Hartley, R.W. / Mauguen, Y. #2: ![]() Title: Three-Dimensional Structure of Barnase-3'Gmp Complex at 2.2 Angstroms Resolution Authors: Guillet, V. / Lapthorn, A. / Mauguen, Y. #3: ![]() Title: Crystal Structure of a Barnase-D(Gpc) Complex at 1.9 Angstroms Resolution Authors: Baudet, S. / Janin, J. #4: ![]() 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 | ![]() | 129.1 KB | Display | ![]() |
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PDB format | ![]() | 102.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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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Atom site foot note | 1: CIS PROLINE - PRO E 48 / 2: CIS PROLINE - PRO F 48 / 3: CIS PROLINE - PRO G 48 |
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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, ![]() #2: Protein | ![]() Mass: 10157.412 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 53.76 % | |||||||||||||||
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Crystal grow![]() | *PLUS Method: other | |||||||||||||||
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: 2.6 Å / Num. obs: 22051 / % possible obs: 98.8 % / Num. measured all: 77876 / Rmerge(I) obs: 0.072 |
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Processing
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Refinement | Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å / Rfactor obs: 0.17 / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 2.71 Å / Rfactor Rfree: 0.32 / Total num. of bins used: 8 / Rfactor obs: 0.206 |