+Open data
-Basic information
Entry | Database: PDB / ID: 1fs3 | ||||||
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Title | CRYSTAL STRUCTURE OF WILD-TYPE BOVINE PANCREATIC RIBONUCLEASE A | ||||||
Components | Ribonuclease A | ||||||
Keywords | HYDROLASE / ribonuclease / RNase A / Bovine pancreas | ||||||
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 / SYNCHROTRON / Resolution: 1.4 Å | ||||||
Authors | Chatani, E. / Hayashi, R. / Moriyama, H. / Ueki, T. | ||||||
Citation | Journal: Protein Sci. / Year: 2002 Title: Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 A resolution. Authors: Chatani, E. / Hayashi, R. / Moriyama, H. / Ueki, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fs3.cif.gz | 33.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fs3.ent.gz | 26.3 KB | Display | PDB format |
PDBx/mmJSON format | 1fs3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fs3_validation.pdf.gz | 413.7 KB | Display | wwPDB validaton report |
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Full document | 1fs3_full_validation.pdf.gz | 418 KB | Display | |
Data in XML | 1fs3_validation.xml.gz | 8.5 KB | Display | |
Data in CIF | 1fs3_validation.cif.gz | 11.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fs/1fs3 ftp://data.pdbj.org/pub/pdb/validation_reports/fs/1fs3 | HTTPS FTP |
-Related structure data
Related structure data | 1eicC 1eidC 1eieC 1dp1 C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a monomer. |
-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) / Tissue: PANCREAS / Production host: Escherichia coli (E. coli) / References: UniProt: P61823, EC: 3.1.27.5 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.74 Å3/Da / Density % sol: 55.03 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: ammonium sulfate, sodium chloride, sodium acetate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL40B2 / Wavelength: 0.968641 |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Oct 31, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.968641 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→6 Å / Num. all: 33877 / Num. obs: 33471 / % possible obs: 98.8 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Biso Wilson estimate: 11.6 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 14.3 |
Reflection shell | Resolution: 1.35→1.4 Å / Redundancy: 3 % / Rmerge(I) obs: 0.19 / Num. unique all: 3202 / % possible all: 97.4 |
-Processing
Software |
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Refinement | Resolution: 1.4→6 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 108825.38 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 15.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.4→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.4→1.45 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 10
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Xplor file |
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