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Yorodumi- PDB-1rnv: REFINEMENT OF THE CRYSTAL STRUCTURE OF RIBONUCLEASE S. COMPARISON... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1rnv | ||||||
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| Title | REFINEMENT OF THE CRYSTAL STRUCTURE OF RIBONUCLEASE S. COMPARISON WITH AND BETWEEN THE VARIOUS RIBONUCLEASE A STRUCTURES | ||||||
Components | RIBONUCLEASE S | ||||||
Keywords | HYDROLASE(PHOSPHORIC DIESTER / RNA) | ||||||
| Function / homology | Function and homology informationpancreatic ribonuclease / ribonuclease A activity / RNA nuclease activity / nucleic acid binding / defense response to Gram-positive bacterium / lyase activity / extracellular region Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 1.6 Å | ||||||
Authors | Kim, E.E. / Varadarajan, R. / Wyckoff, H.W. / Richards, F.M. | ||||||
Citation | Journal: Biochemistry / Year: 1992Title: Refinement of the crystal structure of ribonuclease S. Comparison with and between the various ribonuclease A structures. Authors: Kim, E.E. / Varadarajan, R. / Wyckoff, H.W. / Richards, F.M. | ||||||
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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 | 1rnv.cif.gz | 36.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1rnv.ent.gz | 25 KB | Display | PDB format |
| PDBx/mmJSON format | 1rnv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1rnv_validation.pdf.gz | 374.8 KB | Display | wwPDB validaton report |
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| Full document | 1rnv_full_validation.pdf.gz | 375.1 KB | Display | |
| Data in XML | 1rnv_validation.xml.gz | 3.8 KB | Display | |
| Data in CIF | 1rnv_validation.cif.gz | 5.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rn/1rnv ftp://data.pdbj.org/pub/pdb/validation_reports/rn/1rnv | 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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| Unit cell |
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| Atom site foot note | 1: RESIDUES PRO 93 AND PRO 114 ARE CIS PROLINES. |
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Components
| #1: Protein | Mass: 13708.326 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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| #2: Chemical | ChemComp-SO4 / |
| #3: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.4 % | ||||||||||||||||||||||||||||||||||||
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| Crystal grow | *PLUS pH: 4.75 / Method: unknown | ||||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Reflection | *PLUS Highest resolution: 1.6 Å / Num. all: 15364 / Num. obs: 14562 / Num. measured all: 93541 / Rmerge(I) obs: 0.057 |
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Processing
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| Refinement | Resolution: 1.6→8 Å / σ(F): 4 /
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| Refinement step | Cycle: LAST / Resolution: 1.6→8 Å
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| Refine LS restraints |
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| Refinement | *PLUS Num. reflection obs: 14163 / Rfactor obs: 0.186 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.79 |
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