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Yorodumi- PDB-4c5o: Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H19... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4c5o | ||||||
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Title | Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant | ||||||
Components | FLAVIN MONOOXYGENASE | ||||||
Keywords | OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information | ||||||
Biological species | STENOTROPHOMONAS MALTOPHILIA (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Jensen, C.N. / Ali, S.T. / Allen, M.J. / Grogan, G. | ||||||
Citation | Journal: FEBS Open Bio / Year: 2013 Title: Mutations of an Nad(P)H-Dependent Flavoprotein Monooxygenase that Influence Cofactor Promiscuity and Enantioselectivity. Authors: Jensen, C.N. / Ali, S.T. / Allen, M.J. / Grogan, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4c5o.cif.gz | 508.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4c5o.ent.gz | 415.6 KB | Display | PDB format |
PDBx/mmJSON format | 4c5o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c5/4c5o ftp://data.pdbj.org/pub/pdb/validation_reports/c5/4c5o | HTTPS FTP |
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-Related structure data
Related structure data | 4a9wS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 38587.469 Da / Num. of mol.: 8 / Fragment: RESIDUES 9-365 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) STENOTROPHOMONAS MALTOPHILIA (bacteria) Description: ENVIRONMENTAL ISOLATE / Plasmid: PETYSBLIC-3C / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) References: UniProt: B2FRL2, flavin-containing monooxygenase #2: Chemical | ChemComp-FAD / #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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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: 2.8 Å3/Da / Density % sol: 56 % / Description: NONE |
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Crystal grow | pH: 5.6 Details: THE RESERVOIR CONTAINED 0.9 M LITHIUM SULPHATE IN 100 MM BIS-TRIS PROPANE BUFFER (PH 5.6). THE PROTEIN CONCENTRATION USED WAS 3 MG ML-1. |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 7, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→59.78 Å / Num. obs: 102301 / % possible obs: 97.8 % / Observed criterion σ(I): 2 / Redundancy: 4.8 % / Rmerge(I) obs: 0.15 / Net I/σ(I): 4.6 |
Reflection shell | Resolution: 2.6→2.65 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 2.1 / % possible all: 99.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4A9W Resolution: 2.6→147.69 Å / Cor.coef. Fo:Fc: 0.93 / Cor.coef. Fo:Fc free: 0.899 / SU B: 17.307 / SU ML: 0.357 / Cross valid method: THROUGHOUT / ESU R: 0.869 / ESU R Free: 0.367 / 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: 52.483 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→147.69 Å
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Refine LS restraints |
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