[English] 日本語
Yorodumi- PDB-1rat: EFFECTS OF TEMPERATURE ON PROTEIN STRUCTURE AND DYNAMICS: X-RAY C... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rat | ||||||
---|---|---|---|---|---|---|---|
Title | EFFECTS OF TEMPERATURE ON PROTEIN STRUCTURE AND DYNAMICS: X-RAY CRYSTALLOGRAPHIC STUDIES OF THE PROTEIN RIBONUCLEASE-A AT NINE DIFFERENT TEMPERATURES FROM 98 TO 320 K | ||||||
Components | RIBONUCLEASE A | ||||||
Keywords | HYDROLASE (NUCLEIC ACID / 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: 1.5 Å | ||||||
Authors | Tiltonjunior, R.F. / Dewan, J.C. / Petsko, G.A. | ||||||
Citation | Journal: Biochemistry / Year: 1992 Title: Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K. Authors: Tilton Jr., R.F. / Dewan, J.C. / Petsko, G.A. #1: Journal: J.Appl.Crystallogr. / Year: 1987 Title: Greatly Reduced Radiation Damage in Ribonuclease Crystals Mounted on Glass Fibers Authors: Dewan, J.C. / Tilton, R.F. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1rat.cif.gz | 33.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1rat.ent.gz | 22.6 KB | Display | PDB format |
PDBx/mmJSON format | 1rat.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1rat_validation.pdf.gz | 367.1 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1rat_full_validation.pdf.gz | 372.7 KB | Display | |
Data in XML | 1rat_validation.xml.gz | 4.6 KB | Display | |
Data in CIF | 1rat_validation.cif.gz | 6.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ra/1rat ftp://data.pdbj.org/pub/pdb/validation_reports/ra/1rat | HTTPS FTP |
-Related structure data
Related structure data | 2ratC 3ratC 4ratC 5ratC 6ratC 7ratC 8ratC 9ratC C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
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) / Organ: PANCREAS / References: UniProt: P61823, EC: 3.1.27.5 |
---|---|
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 40.96 % | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 5.5 / Method: batch method / Details: Tilton Jr., R.F., (1992) Biochemistry, 31, 2469. | ||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.5 Å / Num. obs: 11214 / Observed criterion σ(I): 2 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Highest resolution: 1.5 Å / σ(I): 2 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.5 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.5 Å / Rfactor obs: 0.171 / Num. reflection obs: 11214 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |