+Open data
-Basic information
Entry | Database: PDB / ID: 1z3p | ||||||
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Title | X-Ray crystal structure of a mutant Ribonuclease S (M13Nva) | ||||||
Components |
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Keywords | HYDROLASE / RNase S mutant (M13Nva) / S-Peptide / S-Protein / cavity | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Das, M. / Rao, B.V. / Ghosh, S. / Varadarajan, R. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Attempts to delineate the relative contributions of changes in hydrophobicity and packing to changes in stability of ribonuclease S mutants. Authors: Das, M. / Rao, B.V. / Ghosh, S. / Varadarajan, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1z3p.cif.gz | 37.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1z3p.ent.gz | 25.1 KB | Display | PDB format |
PDBx/mmJSON format | 1z3p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1z3p_validation.pdf.gz | 451.7 KB | Display | wwPDB validaton report |
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Full document | 1z3p_full_validation.pdf.gz | 452.4 KB | Display | |
Data in XML | 1z3p_validation.xml.gz | 7.6 KB | Display | |
Data in CIF | 1z3p_validation.cif.gz | 9.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z3/1z3p ftp://data.pdbj.org/pub/pdb/validation_reports/z3/1z3p | HTTPS FTP |
-Related structure data
Related structure data | 1z3lC 1z3mC 2rlnS C: citing same article (ref.) S: Starting model for refinement |
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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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-Components
#1: Protein/peptide | Mass: 1720.879 Da / Num. of mol.: 1 / Mutation: M13NVA / Source method: obtained synthetically Details: S-Peptide synthesized by solid phase peptide synthesis References: UniProt: P61823, EC: 3.1.27.5 | ||
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#2: Protein | Mass: 11555.981 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P61823, EC: 3.1.27.5 | ||
#3: Chemical | #4: 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: 2.09 Å3/Da / Density % sol: 41.04 % |
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Crystal grow | Temperature: 293 K / Method: batch method / pH: 5.2 Details: ammonium sulfate, cesium chloride, sodium acetate, pH 5.2, Batch method, temperature 293K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 10, 2003 |
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→20 Å / Num. all: 8125 / Num. obs: 7872 / % possible obs: 97.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.4 % / Biso Wilson estimate: 24.4 Å2 / Rmerge(I) obs: 0.067 |
Reflection shell | Resolution: 2→2.07 Å / Rmerge(I) obs: 0.195 / % possible all: 91.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB Entry 2RLN Resolution: 2→14.96 Å / Rfactor Rfree error: 0.012 / Data cutoff high absF: 1158259.84 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 43.6085 Å2 / ksol: 0.371117 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27 Å2 | ||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→14.96 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.11 Å / Rfactor Rfree error: 0.044 / Total num. of bins used: 7
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Xplor file |
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