+Open data
-Basic information
Entry | Database: PDB / ID: 5b3k | ||||||
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Title | C101A mutant of Flavodoxin from Pseudomonas aeruginosa | ||||||
Components | Uncharacterized protein PA3435 | ||||||
Keywords | ELECTRON TRANSPORT | ||||||
Function / homology | Function and homology information oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / FMN binding Similarity search - Function | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Okada, D. / Nakanishi, T. / Kitamura, M. | ||||||
Citation | Journal: To Be Published Title: C101A mutant of Flavodoxin from Pseudomonas aeruginosa Authors: Okada, D. / Nakanishi, T. / Kitamura, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5b3k.cif.gz | 44.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5b3k.ent.gz | 29.9 KB | Display | PDB format |
PDBx/mmJSON format | 5b3k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5b3k_validation.pdf.gz | 433 KB | Display | wwPDB validaton report |
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Full document | 5b3k_full_validation.pdf.gz | 433.7 KB | Display | |
Data in XML | 5b3k_validation.xml.gz | 9.1 KB | Display | |
Data in CIF | 5b3k_validation.cif.gz | 12.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b3/5b3k ftp://data.pdbj.org/pub/pdb/validation_reports/b3/5b3k | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 15851.837 Da / Num. of mol.: 1 / Mutation: C101A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) (bacteria) Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 / Gene: PA3435 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9HYH1 |
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#2: Chemical | ChemComp-SO4 / |
#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: 2.82 Å3/Da / Density % sol: 56.36 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.6 Details: 1.9M Ammonium sulfate, 0.1M HEPES sodium, 2% PEG 400 |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NE3A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Nov 30, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. obs: 19685 / % possible obs: 99.5 % / Redundancy: 20.2 % / Net I/σ(I): 33.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→20 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.931 / SU B: 1.61 / SU ML: 0.056 / Cross valid method: THROUGHOUT / ESU R: 0.101 / ESU R Free: 0.099 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.399 Å2
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Refinement step | Cycle: 1 / Resolution: 1.7→20 Å
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Refine LS restraints |
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