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Open data
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Basic information
Entry | Database: PDB / ID: 1rra | ||||||
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Title | RIBONUCLEASE A FROM RATTUS NORVEGICUS (COMMON RAT) | ||||||
![]() | PROTEIN (RIBONUCLEASE) | ||||||
![]() | HYDROLASE / HYDROLASE(PHOSPHORIC DIESTER) / RIBONUCLEASE | ||||||
Function / homology | ![]() : / pancreatic ribonuclease / ribonuclease A activity / RNA nuclease activity / nucleic acid binding / lyase activity / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Gupta, V. / Muyldermans, S. / Wyns, L. / Salunke, D. | ||||||
![]() | ![]() Title: The crystal structure of recombinant rat pancreatic RNase A. Authors: Gupta, V. / Muyldermans, S. / Wyns, L. / Salunke, D.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 38.7 KB | Display | ![]() |
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PDB format | ![]() | 26.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 373.8 KB | Display | ![]() |
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Full document | ![]() | 376.1 KB | Display | |
Data in XML | ![]() | 4.3 KB | Display | |
Data in CIF | ![]() | 6.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7rsaS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 13756.479 Da / Num. of mol.: 1 Mutation: FOUR N-TERMINAL AMINO ACIDS SUBSTITUTED TO ONE SINGLE ALA Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-PO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.07 Å3/Da / Density % sol: 59.9 % | |||||||||||||||||||||||||
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Crystal grow | pH: 5.5 Details: 35% PEG-8K IN 10MM ACETATE BUFFER PH 5.5 CONTAINING 1MM DISODIUM HYDROGEN PHOSPHATE AND 10 MG/ML PROTEIN | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 1, 1993 / Details: DUEL SLITS |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→8 Å / Num. obs: 4534 / % possible obs: 77 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Rsym value: 0.106 |
Reflection | *PLUS Rmerge(I) obs: 0.106 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.75 Å / % possible obs: 60 % / Rmerge(I) obs: 0.156 / Mean I/σ(I) obs: 1.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 7RSA Resolution: 2.5→8 Å / Data cutoff high absF: 0 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PARAM19X.PRO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 8 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.186 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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