+Open data
-Basic information
Entry | Database: PDB / ID: 5iwh | ||||||
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Title | Structure of P. vulgaris HigB toxin delta H92 | ||||||
Components | Endoribonuclease HigB | ||||||
Keywords | HYDROLASE / bacterial toxins / biofilms / cell metabolism / energy metabolism / microbial pathogenesis / stress response / stringent response / translation control | ||||||
Function / homology | Function and homology information plasmid maintenance / RNA catabolic process / translation repressor activity / RNA endonuclease activity / negative regulation of cell growth / ribosome binding / Hydrolases; Acting on ester bonds / negative regulation of translation / negative regulation of cell population proliferation / mRNA binding Similarity search - Function | ||||||
Biological species | Proteus vulgaris (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.101 Å | ||||||
Authors | Schureck, M.A. / Repack, A.A. / Miles, S.J. / Marquez, J. / Dunham, C.M. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2016 Title: Mechanism of endonuclease cleavage by the HigB toxin. Authors: Schureck, M.A. / Repack, A. / Miles, S.J. / Marquez, J. / Dunham, C.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5iwh.cif.gz | 63.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5iwh.ent.gz | 46.1 KB | Display | PDB format |
PDBx/mmJSON format | 5iwh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iw/5iwh ftp://data.pdbj.org/pub/pdb/validation_reports/iw/5iwh | HTTPS FTP |
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-Related structure data
Related structure data | 4zsnC 5ixlC 4px8S 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 13575.263 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Proteus vulgaris (bacteria) / Gene: higB / Variant: delta H92 / Production host: Escherichia coli BW25113 (bacteria) References: UniProt: Q7A225, Hydrolases; Acting on ester bonds | ||
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#2: Chemical | #3: 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: 1.58 Å3/Da / Density % sol: 22.32 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 30-40% w/v polyethylene glycol monomethylether 2,000 and 0.15 M KBr |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jul 7, 2012 |
Radiation | Monochromator: Cryogenically-cooled Si-220 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→15 Å / Num. obs: 32761 / % possible obs: 94.7 % / Redundancy: 2 % / Net I/σ(I): 20.7 |
Reflection shell | Resolution: 1.1→1.14 Å / Redundancy: 2 % / Mean I/σ(I) obs: 9.3 / % possible all: 96.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4px8 Resolution: 1.101→14.974 Å / SU ML: 0.08 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 14.59
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.101→14.974 Å
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Refine LS restraints |
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LS refinement shell |
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