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Yorodumi- PDB-3rmz: Crystal Structure of the W199F-MauG/pre-Methylamine Dehydrogenase... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3rmz | ||||||
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Title | Crystal Structure of the W199F-MauG/pre-Methylamine Dehydrogenase Complex | ||||||
Components |
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Keywords | Oxidoreductase/electron transport / MauG / methylamine dehydrogenase / c-heme / quinone cofactor / ELECTRON TRANSPORT / Oxidoreductase-electron transport complex | ||||||
Function / homology | Function and homology information methylamine dehydrogenase (amicyanin) / methylamine dehydrogenase (amicyanin) activity / methylamine metabolic process / aliphatic amine dehydrogenase activity / amine metabolic process / Oxidoreductases / cytochrome-c peroxidase activity / outer membrane-bounded periplasmic space / periplasmic space / electron transfer activity ...methylamine dehydrogenase (amicyanin) / methylamine dehydrogenase (amicyanin) activity / methylamine metabolic process / aliphatic amine dehydrogenase activity / amine metabolic process / Oxidoreductases / cytochrome-c peroxidase activity / outer membrane-bounded periplasmic space / periplasmic space / electron transfer activity / heme binding / metal ion binding Similarity search - Function | ||||||
Biological species | Paracoccus denitrificans (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.72 Å | ||||||
Authors | Jensen, L.M.R. / Wilmot, C.M. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2011 Title: Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis. Authors: Tarboush, N.A. / Jensen, L.M. / Yukl, E.T. / Geng, J. / Liu, A. / Wilmot, C.M. / Davidson, V.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3rmz.cif.gz | 716.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3rmz.ent.gz | 583.9 KB | Display | PDB format |
PDBx/mmJSON format | 3rmz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3rmz_validation.pdf.gz | 2.2 MB | Display | wwPDB validaton report |
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Full document | 3rmz_full_validation.pdf.gz | 2.2 MB | Display | |
Data in XML | 3rmz_validation.xml.gz | 84.7 KB | Display | |
Data in CIF | 3rmz_validation.cif.gz | 125.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rm/3rmz ftp://data.pdbj.org/pub/pdb/validation_reports/rm/3rmz | HTTPS FTP |
-Related structure data
Related structure data | 3rlmC 3rn0C 3l4mS 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
-Protein / Antibody / Methylamine dehydrogenase ... , 3 types, 6 molecules ABCEDF
#1: Protein | Mass: 41107.594 Da / Num. of mol.: 2 / Mutation: W199F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Paracoccus denitrificans (bacteria) / Strain: Pd 1222 / Gene: mauG, Pden_4736 / Production host: Paracoccus denitrificans (bacteria) / References: UniProt: Q51658, Oxidoreductases #2: Antibody | Mass: 15025.595 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Paracoccus denitrificans (bacteria) / Strain: Pd 1222 / Gene: Pden_4733 / Production host: Rhodobacter sphaeroides (bacteria) References: UniProt: A1BBA0, UniProt: P22619*PLUS, EC: 1.4.99.3 #3: Protein | Mass: 42449.277 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Paracoccus denitrificans (bacteria) / Strain: Pd 1222 / Gene: Pden_4730 / Production host: Rhodobacter sphaeroides (bacteria) / References: UniProt: A1BB97, EC: 1.4.99.3 |
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-Non-polymers , 10 types, 1893 molecules
#4: Chemical | #5: Chemical | ChemComp-NA / #6: Chemical | ChemComp-HEC / #7: Chemical | #8: Chemical | ChemComp-PEG / | #9: Chemical | ChemComp-ACT / | #10: Chemical | ChemComp-PG4 / | #11: Chemical | ChemComp-P6G / | #12: Chemical | ChemComp-MES / | #13: 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: 2.27 Å3/Da / Density % sol: 45.89 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: Drops contained 1uL protein with 3uL reservoir solution. Protein solution: 100uM W199F-MauG and 50uM preMADH in 10mM potassium phosphate, pH 7.5. Reservoir solution contained: 22% w/v PEG ...Details: Drops contained 1uL protein with 3uL reservoir solution. Protein solution: 100uM W199F-MauG and 50uM preMADH in 10mM potassium phosphate, pH 7.5. Reservoir solution contained: 22% w/v PEG 8000, 0.1M sodium acetate, 0.1M MES pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.03315 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 8, 2010 / Details: Biomorph mirrors (Kirkpatrick-Baez configuration) |
Radiation | Monochromator: Si(111) double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.03315 Å / Relative weight: 1 |
Reflection | Resolution: 1.72→50 Å / Num. all: 180384 / Num. obs: 173890 / % possible obs: 96.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Rsym value: 0.064 / Net I/σ(I): 18.3 |
Reflection shell | Resolution: 1.72→1.77 Å / Redundancy: 2.8 % / Mean I/σ(I) obs: 2.8 / Num. unique all: 8981 / Rsym value: 0.355 / % possible all: 82.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 3L4M Resolution: 1.72→39.58 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.958 / SU B: 4.133 / SU ML: 0.061 / Cross valid method: THROUGHOUT / ESU R Free: 0.099 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.264 Å2
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Refinement step | Cycle: LAST / Resolution: 1.72→39.58 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.72→1.768 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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