+Open data
-Basic information
Entry | Database: PDB / ID: 1t2i | ||||||
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Title | T76W mutant of RNase Sa from Streptomyces aureofaciens | ||||||
Components | Guanyl-specific ribonuclease Sa | ||||||
Keywords | HYDROLASE / mutant / ribonuclease | ||||||
Function / homology | Function and homology information ribonuclease T1 activity / ribonuclease T1 / RNA endonuclease activity / lyase activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | Streptomyces aureofaciens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.1 Å | ||||||
Authors | Urbanikova, L. / Sevcik, J. | ||||||
Citation | Journal: Biophys.J. / Year: 2004 Title: Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease sa. Authors: Alston, R.W. / Urbanikova, L. / Sevcik, J. / Lasagna, M. / Reinhart, G.D. / Scholtz, J.M. / Pace, C.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t2i.cif.gz | 62 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t2i.ent.gz | 45.8 KB | Display | PDB format |
PDBx/mmJSON format | 1t2i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t2/1t2i ftp://data.pdbj.org/pub/pdb/validation_reports/t2/1t2i | HTTPS FTP |
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-Related structure data
Related structure data | 1t2hC 1rggS S: Starting model for refinement 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: 10667.598 Da / Num. of mol.: 1 / Mutation: T76W Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces aureofaciens (bacteria) / Strain: BMK / Gene: U39467 / Plasmid: PUC19 / Production host: Escherichia coli (E. coli) / Strain (production host): NOVABLUE / References: UniProt: P05798, EC: 3.1.27.3 |
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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: 1.8 Å3/Da / Density % sol: 32 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: ammonium sulfate, disodium phosphate, monosodium phosphate, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 1.096 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 1, 2003 |
Radiation | Monochromator: Si(111) channel-cut Xtal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.096 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→29 Å / Num. obs: 29254 / % possible obs: 95.3 % / Redundancy: 6.4 % / Biso Wilson estimate: 10 Å2 / Rmerge(I) obs: 0.03 / Net I/σ(I): 53.3 |
Reflection shell | Resolution: 1.1→1.11 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 8.7 / Num. unique all: 705 / % possible all: 90.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1rgg Resolution: 1.1→29 Å / Cor.coef. Fo:Fc: 0.979 / Cor.coef. Fo:Fc free: 0.96 / SU B: 0.375 / SU ML: 0.019 / Cross valid method: THROUGHOUT / ESU R: 0.034 / ESU R Free: 0.036 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 8.383 Å2
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Refinement step | Cycle: LAST / Resolution: 1.1→29 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.1→1.11 Å / Total num. of bins used: 20
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