+Open data
-Basic information
Entry | Database: PDB / ID: 1fys | ||||||
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Title | Ribonuclease T1 V16C mutant | ||||||
Components | GUANYL-SPECIFIC RIBONUCLEASE T1 | ||||||
Keywords | HYDROLASE / ribonuclease | ||||||
Function / homology | Function and homology information hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | Aspergillus oryzae (mold) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | De Vos, S. / Loris, R. / Steyaert, J. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Hydrophobic core manipulations in ribonuclease T1. Authors: De Vos, S. / Backmann, J. / Prevost, M. / Steyaert, J. / Loris, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fys.cif.gz | 30.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fys.ent.gz | 22.2 KB | Display | PDB format |
PDBx/mmJSON format | 1fys.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fy/1fys ftp://data.pdbj.org/pub/pdb/validation_reports/fy/1fys | HTTPS FTP |
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-Related structure data
Related structure data | 1fzuC 1g02C 1i2eC 1i2fC 1i2gC 1i3fC 1i3iC 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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-Components
#1: Protein | Mass: 11098.707 Da / Num. of mol.: 1 / Mutation: V16C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus oryzae (mold) / Production host: Escherichia coli (E. coli) / References: UniProt: P00651, EC: 3.1.27.3 | ||||
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#2: Chemical | #3: Chemical | ChemComp-2GP / | #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: 2.2 Å3/Da / Density % sol: 44.16 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: MPD, Na-acetate, calcium chloride, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 4.2 / Method: vapor diffusion, hanging drop / Details: Zegers, I., (1998) Nat.Struct.Biol., 5, 280. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 3, 1999 |
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: 6601 / Num. obs: 6601 / % possible obs: 94.3 % / Observed criterion σ(F): -6 / Observed criterion σ(I): -3 / Redundancy: 4.07 % / Biso Wilson estimate: 13.4 Å2 / Rmerge(I) obs: 0.127 / Net I/σ(I): 9.22 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.349 / Num. unique all: 587 / % possible all: 85.9 |
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 6623 / Num. measured all: 26858 |
-Processing
Software |
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Refinement | Resolution: 2→2.09 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→2.09 Å
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Refine LS restraints |
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