+Open data
-Basic information
Entry | Database: PDB / ID: 1w53 | ||||||
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Title | Kinase recruitment domain of the stress phosphatase RsbU | ||||||
Components | PHOSPHOSERINE PHOSPHATASE RSBU | ||||||
Keywords | HYDROLASE / PHOSPHATASE / STRESS / BACILLUS / KINASE | ||||||
Function / homology | Function and homology information phosphoserine phosphatase / L-phosphoserine phosphatase activity / phosphatase activity / phosphoprotein phosphatase activity Similarity search - Function | ||||||
Biological species | BACILLUS SUBTILIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.6 Å | ||||||
Authors | Delumeau, O. / Dutta, S. / Brigulla, M. / Kuhnke, G. / Hardwick, S.W. / Voelker, U. / Yudkin, M.D. / Lewis, R.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Functional and Structural Characterization of Rsbu, a Stress Signaling Protein Phosphatase 2C Authors: Delumeau, O. / Dutta, S. / Brigulla, M. / Kuhnke, G. / Hardwicku, S.W. / Voelker, U. / Yudkin, M.D. / Lewis, R.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1w53.cif.gz | 46.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1w53.ent.gz | 37.4 KB | Display | PDB format |
PDBx/mmJSON format | 1w53.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w5/1w53 ftp://data.pdbj.org/pub/pdb/validation_reports/w5/1w53 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 10086.598 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1-84 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACILLUS SUBTILIS (bacteria) / Plasmid: PET22B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P40399 | ||||||
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#2: Chemical | #3: Chemical | ChemComp-XE / | #4: Water | ChemComp-HOH / | Compound details | CATALYTIC ACTIVITY: PHOSPHOSER | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.7 % |
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Crystal grow | pH: 6.5 / Details: 12% PEG 6000 100 MM MES.NAOH, PH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 13, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→31.01 Å / Num. obs: 9645 / % possible obs: 100 % / Observed criterion σ(I): 1 / Redundancy: 4.86 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 4.14 |
Reflection shell | Resolution: 1.6→1.69 Å / Redundancy: 4.08 % / Rmerge(I) obs: 0.16 / Mean I/σ(I) obs: 3.99 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.6→28.87 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.943 / SU B: 1.784 / SU ML: 0.065 / Cross valid method: THROUGHOUT / ESU R: 0.178 / ESU R Free: 0.106 / 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: 20.68 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→28.87 Å
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Refine LS restraints |
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