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Yorodumi- PDB-1tvc: FAD and NADH binding domain of methane monooxygenase reductase fr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tvc | ||||||
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Title | FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath) | ||||||
Components | METHANE MONOOXYGENASE COMPONENT C | ||||||
Keywords | OXIDOREDUCTASE / FAD-BINDING / NADH-BINDING | ||||||
Function / homology | Function and homology information methane monooxygenase (soluble) / : / : / 2 iron, 2 sulfur cluster binding / one-carbon metabolic process / flavin adenine dinucleotide binding / metal ion binding Similarity search - Function | ||||||
Biological species | Methylococcus capsulatus (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Chatwood, L.L. / Mueller, J. / Gross, J.D. / Wagner, G. / Lippard, S.J. | ||||||
Citation | Journal: Biochemistry / Year: 2004 Title: NMR Structure of the Flavin Domain from Soluble Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath) Authors: Chatwood, L.L. / Gross, J.D. / Wagner, G. / Lippard, S.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tvc.cif.gz | 776 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tvc.ent.gz | 640.3 KB | Display | PDB format |
PDBx/mmJSON format | 1tvc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tvc_validation.pdf.gz | 466 KB | Display | wwPDB validaton report |
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Full document | 1tvc_full_validation.pdf.gz | 793.6 KB | Display | |
Data in XML | 1tvc_validation.xml.gz | 122.3 KB | Display | |
Data in CIF | 1tvc_validation.cif.gz | 156.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tv/1tvc ftp://data.pdbj.org/pub/pdb/validation_reports/tv/1tvc | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 27654.258 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methylococcus capsulatus (bacteria) / Gene: mmoC / Plasmid: pFAD21 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: P22868, methane monooxygenase (soluble) |
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#2: Chemical | ChemComp-FDA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: A standard set of NMR experiments required for high-resolution structure; TROSY |
-Sample preparation
Details | Contents: 0.6-1mM Protein; 50mM phosphate buffer; 1mM DTT, 2mM protease inhibitor; 0.1% NaN3; 3mM NADH; 30mM dithionite Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50mM Na phosphate / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 10 |