+Open data
-Basic information
Entry | Database: PDB / ID: 9jxc | ||||||
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Title | Crystal Structure of AbOhr-R15C | ||||||
Components | Organic hydroperoxide resistance protein | ||||||
Keywords | OXIDOREDUCTASE / organic hydroperoxide resistance / R15C mutation | ||||||
Function / homology | Organic hydroperoxide resistance protein famiy / OsmC/Ohr family / OsmC/Ohr superfamily / OsmC-like protein / K homology domain-like, alpha/beta / response to oxidative stress / Organic hydroperoxide resistance protein Function and homology information | ||||||
Biological species | Acinetobacter baumannii (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Huang, W. / Hu, C.X. | ||||||
Funding support | China, 1items
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Citation | Journal: To Be Published Title: Crystal Structure of 6D1-Ab-ohrB complex Authors: Huang, W. / Hu, C.X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 9jxc.cif.gz | 117.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb9jxc.ent.gz | 91.6 KB | Display | PDB format |
PDBx/mmJSON format | 9jxc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 9jxc_validation.pdf.gz | 451.5 KB | Display | wwPDB validaton report |
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Full document | 9jxc_full_validation.pdf.gz | 463.9 KB | Display | |
Data in XML | 9jxc_validation.xml.gz | 27.4 KB | Display | |
Data in CIF | 9jxc_validation.cif.gz | 36.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jx/9jxc ftp://data.pdbj.org/pub/pdb/validation_reports/jx/9jxc | HTTPS FTP |
-Related structure data
Related structure data | 9jx6C 9k1jC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 15003.864 Da / Num. of mol.: 4 / Mutation: R15C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter baumannii (bacteria) / Gene: ohr / Production host: Escherichia coli (E. coli) / References: UniProt: Q5DQT1 #2: Water | ChemComp-HOH / | Has protein modification | N | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.7 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 0.2 M AMMONIUM SULFATE, 18 % w/v Polyethylene glycol 3350, 0.1 M MES pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.9795 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jun 25, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→39.88 Å / Num. obs: 33504 / % possible obs: 96 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.085 / Rpim(I) all: 0.035 / Net I/σ(I): 14.8 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 7.1 % / Rmerge(I) obs: 0.239 / Mean I/σ(I) obs: 6.2 / Num. unique obs: 3328 / Rpim(I) all: 0.096 / % possible all: 96.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→43.21 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.914 / SU B: 4.972 / SU ML: 0.134 / Cross valid method: THROUGHOUT / ESU R: 0.24 / ESU R Free: 0.205 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.266 Å2
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Refinement step | Cycle: 1 / Resolution: 2.1→43.21 Å
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