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Yorodumi- PDB-5rnt: X-RAY ANALYSIS OF CUBIC CRYSTALS OF THE COMPLEX FORMED BETWEEN RI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5rnt | ||||||
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Title | X-RAY ANALYSIS OF CUBIC CRYSTALS OF THE COMPLEX FORMED BETWEEN RIBONUCLEASE T1 AND GUANOSINE-3',5'-BISPHOSPHATE | ||||||
Components | RIBONUCLEASE T1 | ||||||
Keywords | HYDROLASE(ENDORIBONUCLEASE) | ||||||
Function / homology | Function and homology information hyphal tip / ribonuclease T1 / ribonuclease T1 activity / cell septum / RNA endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | Aspergillus oryzae (mold) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3.2 Å | ||||||
Authors | Saenger, W. / Heinemann, U. / Lenz, A. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.B / Year: 1991 Title: X-ray analysis of cubic crystals of the complex formed between ribonuclease T1 and guanosine-3',5'-bisphosphate. Authors: Lenz, A. / Heinemann, U. / Maslowska, M. / Saenger, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5rnt.cif.gz | 26.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5rnt.ent.gz | 20.5 KB | Display | PDB format |
PDBx/mmJSON format | 5rnt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5rnt_validation.pdf.gz | 816.3 KB | Display | wwPDB validaton report |
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Full document | 5rnt_full_validation.pdf.gz | 822.7 KB | Display | |
Data in XML | 5rnt_validation.xml.gz | 8.2 KB | Display | |
Data in CIF | 5rnt_validation.cif.gz | 10.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rn/5rnt ftp://data.pdbj.org/pub/pdb/validation_reports/rn/5rnt | HTTPS FTP |
-Related structure data
Similar structure data |
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-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 39 AND PRO 55 ARE CIS PROLINES. | ||||||||
Components on special symmetry positions |
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-Components
#1: Protein | Mass: 11094.694 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus oryzae (mold) / References: UniProt: P00651, EC: 3.1.27.3 |
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#2: Chemical | ChemComp-PGP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.43 Å3/Da / Density % sol: 49.32 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.5 / Method: microdialysisDetails: enzyme was dissoloved sodium acetate buffer, containing protein and calcium acetate. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 3.2 Å / Num. obs: 1408 / Observed criterion σ(I): 1 / Num. measured all: 4274 / Rmerge(I) obs: 0.043 |
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-Processing
Software | Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 3.2→10 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 3.2→10 Å
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Refine LS restraints |
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