BMRB Entry 6295
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6295
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Chatwood, Lisa; Mueller, Jens; Gross, John; Wagner, Gerhard; Lippard, Stephen. "NMR structure of the flavin domain from soluble methane monooxygenase reductase
from Methylococcus capsulatus (Bath)" Biochemistry 43, 11983-11991 (2004).
PubMed: 15379538
Assembly members:
Flavin domain of methane monooxygenase reductase, polymer, 252 residues, Formula weight is not available
Natural source: Common Name: Methylococcus capsulatus Taxonomy ID: 414 Superkingdom: Eubacteria Kingdom: not available Genus/species: Methylococcus capsulatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pFAD21
Entity Sequences (FASTA):
Flavin domain of methane monooxygenase reductase: MCRISFGEVGSFEAEVVGLN
WVSSNTVQFLLQKRPDECGN
RGVKFEPGQFMDLTIPGTDV
SRSYSPANLPNPEGRLEFLI
RVLPEGRFSDYLRNDARVGQ
VLSVKGPLGVFGLKERGMAP
RYFVAGGTGLAPVVSMVRQM
QEWTAPNETRIYFGVNTEPE
LFYIDELKSLERSMRNLTVK
ACVWHPSGDWEGEQGSPIDA
LREDLESSDANPDIYLCGPP
GMIDAACELVRSRGIPGEQV
FFEKFLPSGAAX
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 1120 |
| 15N chemical shifts | 247 |
| 13C chemical shifts | 935 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MMOR-FAD | 1 |
Entities:
Entity 1, MMOR-FAD 252 residues - Formula weight is not available
| 1 | MET | CYS | ARG | ILE | SER | PHE | GLY | GLU | VAL | GLY | ||||
| 2 | SER | PHE | GLU | ALA | GLU | VAL | VAL | GLY | LEU | ASN | ||||
| 3 | TRP | VAL | SER | SER | ASN | THR | VAL | GLN | PHE | LEU | ||||
| 4 | LEU | GLN | LYS | ARG | PRO | ASP | GLU | CYS | GLY | ASN | ||||
| 5 | ARG | GLY | VAL | LYS | PHE | GLU | PRO | GLY | GLN | PHE | ||||
| 6 | MET | ASP | LEU | THR | ILE | PRO | GLY | THR | ASP | VAL | ||||
| 7 | SER | ARG | SER | TYR | SER | PRO | ALA | ASN | LEU | PRO | ||||
| 8 | ASN | PRO | GLU | GLY | ARG | LEU | GLU | PHE | LEU | ILE | ||||
| 9 | ARG | VAL | LEU | PRO | GLU | GLY | ARG | PHE | SER | ASP | ||||
| 10 | TYR | LEU | ARG | ASN | ASP | ALA | ARG | VAL | GLY | GLN | ||||
| 11 | VAL | LEU | SER | VAL | LYS | GLY | PRO | LEU | GLY | VAL | ||||
| 12 | PHE | GLY | LEU | LYS | GLU | ARG | GLY | MET | ALA | PRO | ||||
| 13 | ARG | TYR | PHE | VAL | ALA | GLY | GLY | THR | GLY | LEU | ||||
| 14 | ALA | PRO | VAL | VAL | SER | MET | VAL | ARG | GLN | MET | ||||
| 15 | GLN | GLU | TRP | THR | ALA | PRO | ASN | GLU | THR | ARG | ||||
| 16 | ILE | TYR | PHE | GLY | VAL | ASN | THR | GLU | PRO | GLU | ||||
| 17 | LEU | PHE | TYR | ILE | ASP | GLU | LEU | LYS | SER | LEU | ||||
| 18 | GLU | ARG | SER | MET | ARG | ASN | LEU | THR | VAL | LYS | ||||
| 19 | ALA | CYS | VAL | TRP | HIS | PRO | SER | GLY | ASP | TRP | ||||
| 20 | GLU | GLY | GLU | GLN | GLY | SER | PRO | ILE | ASP | ALA | ||||
| 21 | LEU | ARG | GLU | ASP | LEU | GLU | SER | SER | ASP | ALA | ||||
| 22 | ASN | PRO | ASP | ILE | TYR | LEU | CYS | GLY | PRO | PRO | ||||
| 23 | GLY | MET | ILE | ASP | ALA | ALA | CYS | GLU | LEU | VAL | ||||
| 24 | ARG | SER | ARG | GLY | ILE | PRO | GLY | GLU | GLN | VAL | ||||
| 25 | PHE | PHE | GLU | LYS | PHE | LEU | PRO | SER | GLY | ALA | ||||
| 26 | ALA | FDA |
Samples:
Sample_1: Flavin domain of methane monooxygenase reductase, [U-13C; U-15N; U-2H], 0.6 – 1.0 mM; phosphate buffer 50 mM; DTT 1 mM; NaN3 0.1%; Pefabloc protease inhibitor 2 mM; NADH 3 mM; Na2S2O4 30 mM
cond_1: pH: 7.0; temperature: 298 K; ionic strength: 50 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | Sample_1 | not available | cond_1 |
| 13C HMQC-NOESY | Sample_1 | not available | cond_1 |
| 13C NOESY-HSQC | Sample_1 | not available | cond_1 |
| 15N NOESY-HSQC | Sample_1 | not available | cond_1 |
| 15N TOCSY-HSQC | Sample_1 | not available | cond_1 |
| HC(CO)NH-TOCSY | Sample_1 | not available | cond_1 |
| H(CCO)NH-TOCSY | Sample_1 | not available | cond_1 |
| HN(COCA)CB-TROSY | Sample_1 | not available | cond_1 |
| HN(CA)CB-TROSY | Sample_1 | not available | cond_1 |
| HN(CA)CO-TROSY | Sample_1 | not available | cond_1 |
| HNCO-TROSY | Sample_1 | not available | cond_1 |
| HN(CO)CA-TROSY | Sample_1 | not available | cond_1 |
| HNCA-TROSY | Sample_1 | not available | cond_1 |
Software:
FELIX v97.0 - processing
XEASY v1.3.13 - data analysis
PROSA v6.0 - processing
DYANA v1.5 - structure solution
XPLOR v3.84 - refinement
XWINNMR v2.5 - collection
VNMR v5.1a - collection
NMR spectrometers:
- Varian UNITY-INOVA 750 MHz
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
- Varian INOVA 500 MHz
Related Database Links:
| PDB | |
| GB | AAB62391 AAU92722 |
| REF | WP_010960487 YP_113665 |
| SP | P22868 |
| AlphaFold | P22868 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks