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Yorodumi- PDB-4rnt: HIS 92 ALA MUTATION IN RIBONUCLEASE T1 INDUCES SEGMENTAL FLEXIBIL... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 4rnt | ||||||
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| Title | HIS 92 ALA MUTATION IN RIBONUCLEASE T1 INDUCES SEGMENTAL FLEXIBILITY. AN X-RAY STUDY | ||||||
Components | RIBONUCLEASE T1 | ||||||
Keywords | HYDROLASE(ENDORIBONUCLEASE) | ||||||
| Function / homology | Function and homology informationhyphal tip / ribonuclease T1 / ribonuclease T1 activity / cell septum / RNA endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | ||||||
Authors | Saenger, W. / Koellner, G. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992Title: His92Ala mutation in ribonuclease T1 induces segmental flexibility. An X-ray study. Authors: Koellner, G. / Choe, H.W. / Heinemann, U. / Grunert, H.P. / Zouni, A. / Hahn, U. / Saenger, W. | ||||||
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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 | 4rnt.cif.gz | 32.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb4rnt.ent.gz | 20.6 KB | Display | PDB format |
| PDBx/mmJSON format | 4rnt.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4rnt_validation.pdf.gz | 368.4 KB | Display | wwPDB validaton report |
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| Full document | 4rnt_full_validation.pdf.gz | 379.8 KB | Display | |
| Data in XML | 4rnt_validation.xml.gz | 5.2 KB | Display | |
| Data in CIF | 4rnt_validation.cif.gz | 7.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rn/4rnt ftp://data.pdbj.org/pub/pdb/validation_reports/rn/4rnt | 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 39 AND 55 ARE CIS PROLINES. |
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Components
| #1: Protein | Mass: 11027.625 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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| #2: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 1.92 Å3/Da / Density % sol: 35.78 % | |||||||||||||||||||||||||
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| Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Reflection | *PLUS Num. obs: 982 / Observed criterion σ(F): 1 / Num. measured all: 6189 / Rmerge(I) obs: 0.072 |
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| Reflection shell | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 2.4 Å / % possible obs: 69 % |
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Processing
| Software | Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Refinement | Resolution: 2.2→10 Å / σ(I): 0 /
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| Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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| Refine LS restraints |
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| Refinement | *PLUS Rfactor obs: 0.158 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS |
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