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Yorodumi- 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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Keywords | ENDONUCLEASE | ||||||
| Function / homology | Function and homology informationHydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA endonuclease activity / RNA binding / extracellular region / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 2.6 Å | ||||||
Authors | Guillet, V. / Lapthorn, A. / Mauguen, Y. | ||||||
Citation | Journal: Structure / Year: 1993Title: Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar. Authors: Guillet, V. / Lapthorn, A. / Hartley, R.W. / Mauguen, Y. #1: Journal: Proteins / Year: 1993Title: 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: Journal: FEBS Lett. / Year: 1993Title: Three-Dimensional Structure of Barnase-3'Gmp Complex at 2.2 Angstroms Resolution Authors: Guillet, V. / Lapthorn, A. / Mauguen, Y. #3: Journal: J.Mol.Biol. / Year: 1991Title: Crystal Structure of a Barnase-D(Gpc) Complex at 1.9 Angstroms Resolution Authors: Baudet, S. / Janin, J. #4: Journal: Nature / Year: 1982Title: 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. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1bgs.cif.gz | 129.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1bgs.ent.gz | 102.3 KB | Display | PDB format |
| PDBx/mmJSON format | 1bgs.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1bgs_validation.pdf.gz | 401.3 KB | Display | wwPDB validaton report |
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| Full document | 1bgs_full_validation.pdf.gz | 418.1 KB | Display | |
| Data in XML | 1bgs_validation.xml.gz | 13.3 KB | Display | |
| Data in CIF | 1bgs_validation.cif.gz | 22.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bg/1bgs ftp://data.pdbj.org/pub/pdb/validation_reports/bg/1bgs | HTTPS FTP |
-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, Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters #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: X-RAY DIFFRACTION |
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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: 0.17 / Rfactor obs: 0.17 / Highest resolution: 2.6 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Highest resolution: 2.6 Å
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| Refine LS restraints |
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| Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement | *PLUS Lowest resolution: 8 Å / Rfactor obs: 0.17 / Rfactor Rwork: 0.17 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 |
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