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- PDB-5rat: Effects of temperature on protein structure and dynamics: X-ray c... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5rat | ||||||
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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 | ||||||
![]() | RIBONUCLEASE A | ||||||
![]() | HYDROLASE (NUCLEIC ACID / RNA) | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Tiltonjunior, R.F. / Dewan, J.C. / Petsko, G.A. | ||||||
![]() | ![]() 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: ![]() Title: Greatly Reduced Radiation Damage in Ribonuclease Crystals Mounted on Glass Fibers Authors: Dewan, J.C. / Tilton, R.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 33 KB | Display | ![]() |
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PDB format | ![]() | 22.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 367.2 KB | Display | ![]() |
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Full document | ![]() | 369.4 KB | Display | |
Data in XML | ![]() | 4.3 KB | Display | |
Data in CIF | ![]() | 5.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ratC ![]() 2ratC ![]() 3ratC ![]() 4ratC ![]() 6ratC ![]() 7ratC ![]() 8ratC ![]() 9ratC C: citing same article ( |
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Similar 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 PRO 93 AND PRO 114 ARE CIS-PROLINES. |
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Components
#1: Protein | Mass: 13708.326 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.43 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 5.5 / Method: batch methodDetails: taken from Gilbert, W.A. et al. (1982) J. Raman. Spectrosc., 12, 173-179. | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 220 K |
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Radiation | Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.5 Å / Num. obs: 10235 / Observed criterion σ(I): 2 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Highest resolution: 1.5 Å / σ(I): 2 /
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Refinement step | Cycle: LAST / Highest resolution: 1.5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.5 Å / Num. reflection obs: 10235 / Rfactor obs: 0.151 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |