+Open data
-Basic information
Entry | Database: PDB / ID: 1c0c | ||||||
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Title | BOVINE PANCREATIC RIBONUCLEASE A DESICCATED FOR 4.0 DAYS | ||||||
Components | RIBONUCLEASE A | ||||||
Keywords | HYDROLASE / HYDROLASE (PHOSPHORIC DIESTER / RNA) / DESICCATED / DRY / DEHYDRATED | ||||||
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: 2 Å | ||||||
Authors | Bell, J.A. | ||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: X-ray crystal structures of a severely desiccated protein Authors: Bell, J.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1c0c.cif.gz | 32.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c0c.ent.gz | 24.9 KB | Display | PDB format |
PDBx/mmJSON format | 1c0c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1c0c_validation.pdf.gz | 431.2 KB | Display | wwPDB validaton report |
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Full document | 1c0c_full_validation.pdf.gz | 443.9 KB | Display | |
Data in XML | 1c0c_validation.xml.gz | 8.9 KB | Display | |
Data in CIF | 1c0c_validation.cif.gz | 10.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c0/1c0c ftp://data.pdbj.org/pub/pdb/validation_reports/c0/1c0c | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14062.729 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Organ: PANCREAS / References: UniProt: P61823, EC: 3.1.27.5 | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal grow | Temperature: 295 K / Method: small tubes / pH: 4.5 Details: 58% methanol (v/v), pH 4.5, SMALL TUBES, temperature 295K |
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Sep 14, 1995 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→99 Å / Num. obs: 4742 / % possible obs: 84.5 % / Observed criterion σ(I): 1 / Redundancy: 3 % / Biso Wilson estimate: 41 Å2 / Rmerge(I) obs: 0.045 / Net I/σ(I): 17.3 |
Reflection shell | Resolution: 2→2.2 Å / Rmerge(I) obs: 0.19 / % possible all: 64 |
Reflection | *PLUS Lowest resolution: 9999 Å / Num. measured all: 14417 |
-Processing
Software |
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Refinement | Resolution: 2→10 Å / Cross valid method: THROUGHOUT / σ(I): 1 / Stereochemistry target values: protgeo Details: Final five cycles of refinement included all observed data
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5E / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / % reflection Rfree: 10 % / Rfactor obs: 0.19 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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