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Yorodumi- PDB-1rnu: REFINEMENT OF THE CRYSTAL STRUCTURE OF RIBONUCLEASE S. COMPARISON... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rnu | ||||||
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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 information pancreatic ribonuclease / ribonuclease A activity / RNA nuclease activity / nucleic acid binding / lyase activity / defense response to Gram-positive bacterium / extracellular region Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.6 Å | ||||||
Authors | Kim, E.E. / Varadarajan, R. / Wyckoff, H.W. / Richards, F.M. | ||||||
Citation | Journal: Biochemistry / Year: 1992 Title: 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rnu.cif.gz | 33.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rnu.ent.gz | 25.8 KB | Display | PDB format |
PDBx/mmJSON format | 1rnu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1rnu_validation.pdf.gz | 373.1 KB | Display | wwPDB validaton report |
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Full document | 1rnu_full_validation.pdf.gz | 373.7 KB | Display | |
Data in XML | 1rnu_validation.xml.gz | 3.9 KB | Display | |
Data in CIF | 1rnu_validation.cif.gz | 6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rn/1rnu ftp://data.pdbj.org/pub/pdb/validation_reports/rn/1rnu | HTTPS FTP |
-Related structure data
-Links
-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. |
-Components
#1: Protein | Mass: 13708.326 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P61823, EC: 3.1.27.5 |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.67 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.5 / Method: unknown | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.6 Å / Num. all: 15437 / Num. obs: 15104 / Num. measured all: 76450 / Rmerge(I) obs: 0.054 |
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-Processing
Software |
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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 Highest resolution: 1.6 Å / Lowest resolution: 8 Å / Num. reflection obs: 14924 / σ(F): 4 / Rfactor obs: 0.176 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.75 |