+Open data
-Basic information
Entry | Database: PDB / ID: 2r14 | ||||||
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Title | Structure of morphinone reductase in complex with tetrahydroNAD | ||||||
Components | Morphinone reductase | ||||||
Keywords | FLAVOPROTEIN / H-tunnelling / NADH / morphinone reductase / hydride transfer / OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Pseudomonas putida (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.4 Å | ||||||
Authors | Costello, C.L. / Scrutton, N.S. / Leys, D. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2007 Title: Mutagenesis of morphinone reductase induces multiple reactive configurations and identifies potential ambiguity in kinetic analysis of enzyme tunneling mechanisms. Authors: Pudney, C.R. / Hay, S. / Pang, J. / Costello, C. / Leys, D. / Sutcliffe, M.J. / Scrutton, N.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2r14.cif.gz | 185.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2r14.ent.gz | 144.7 KB | Display | PDB format |
PDBx/mmJSON format | 2r14.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2r14_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 2r14_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 2r14_validation.xml.gz | 23.5 KB | Display | |
Data in CIF | 2r14_validation.cif.gz | 37.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r1/2r14 ftp://data.pdbj.org/pub/pdb/validation_reports/r1/2r14 | 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 41290.891 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas putida (bacteria) / Gene: morB / Production host: Escherichia coli (E. coli) / References: UniProt: Q51990 |
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#2: Chemical | ChemComp-FMN / |
#3: Chemical | ChemComp-TXD / |
#4: 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: 3.27 Å3/Da / Density % sol: 62.38 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 2.5M ammonium sulphate, 0.1M Hepes, saturating tetrahydroNAD, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Feb 1, 2004 |
Radiation | Monochromator: diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.3→20 Å / Num. all: 123781 / Num. obs: 123781 / % possible obs: 89.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 18 Å2 / Rmerge(I) obs: 0.097 / Net I/σ(I): 12.1 |
Reflection shell | Resolution: 1.3→1.34 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.493 / Mean I/σ(I) obs: 2.3 / % possible all: 85.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.4→12 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.968 / SU B: 2.996 / SU ML: 0.048 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.053 / ESU R Free: 0.05 / 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: 16.72 Å2
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Refinement step | Cycle: LAST / Resolution: 1.4→12 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.4→1.436 Å / Total num. of bins used: 20
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