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Yorodumi- PDB-1trp: X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1trp | ||||||
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| Title | X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF THE MUTATION TRP 59 TYR IN RIBONUCLEASE T1 | ||||||
Components | RIBONUCLEASE T1 ISOZYME | ||||||
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: 2.4 Å | ||||||
Authors | Schluckebier, G. / Saenger, W. | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 1994Title: X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1. Authors: Schubert, W.D. / Schluckebier, G. / Backmann, J. / Granzin, J. / Kisker, C. / Choe, H.W. / Hahn, U. / Pfeil, W. / 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 | 1trp.cif.gz | 54.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1trp.ent.gz | 39.3 KB | Display | PDB format |
| PDBx/mmJSON format | 1trp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1trp_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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| Full document | 1trp_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 1trp_validation.xml.gz | 13 KB | Display | |
| Data in CIF | 1trp_validation.cif.gz | 16.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tr/1trp ftp://data.pdbj.org/pub/pdb/validation_reports/tr/1trp | 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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| 2 | ![]()
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| Unit cell |
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| Atom site foot note | 1: CIS PROLINE - PRO A 39 / 2: CIS PROLINE - PRO A 55 / 3: CIS PROLINE - PRO B 239 / 4: CIS PROLINE - PRO B 255 |
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Components
| #1: Protein | Mass: 11094.694 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.53 % | |||||||||||||||||||||||||||||||||||
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| Crystal grow | *PLUS Method: vapor diffusion, sitting drop / pH: 4.2 | |||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 6347 / % possible obs: 84 % / Observed criterion σ(F): 1 / Num. measured all: 10071 / Rmerge F obs: 0.054 |
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Processing
| Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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| Refinement | Resolution: 2.4→10 Å / σ(F): 1 /
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| Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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| Refine LS restraints |
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| Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
| Refinement | *PLUS Rfactor obs: 0.16 | ||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS Type: t_angle_d / Dev ideal: 1.24 |
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