BMRB Entry 11172
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11172
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Citation: Todokoro, Yasuto; Kobayashi, Masatoshi; Sato, Takeshi; Kawakami, Toru; Yumen, Ikuko; Aimoto, Saburo; Fujiwara, Toshimichi; Akutsu, Hideo. "Structural analysis of the membrane-reconstituted subunit c-ring of E. coli
H+-ATP synthase by solid-state NMR" J. Biomol. NMR 48, 1-11 (2010).
PubMed: 20596883
Assembly members:
FoF1 ATP synthase subunit c (EFoc), polymer, 79 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pCP35
Entity Sequences (FASTA):
FoF1 ATP synthase subunit c (EFoc): MENLNMDLLYMAAAVMMGLA
AIGAAIGIGILGGKFLEGAA
RQPDLIPLLRTQFFIVMGLV
DAIPMIAVGLGLYVMFAVA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 127 |
| 15N chemical shifts | 35 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FoF1 ATP synthase subunit c (EFoc) | 1 |
Entities:
Entity 1, FoF1 ATP synthase subunit c (EFoc) 79 residues - Formula weight is not available
| 1 | MET | GLU | ASN | LEU | ASN | MET | ASP | LEU | LEU | TYR | ||||
| 2 | MET | ALA | ALA | ALA | VAL | MET | MET | GLY | LEU | ALA | ||||
| 3 | ALA | ILE | GLY | ALA | ALA | ILE | GLY | ILE | GLY | ILE | ||||
| 4 | LEU | GLY | GLY | LYS | PHE | LEU | GLU | GLY | ALA | ALA | ||||
| 5 | ARG | GLN | PRO | ASP | LEU | ILE | PRO | LEU | LEU | ARG | ||||
| 6 | THR | GLN | PHE | PHE | ILE | VAL | MET | GLY | LEU | VAL | ||||
| 7 | ASP | ALA | ILE | PRO | MET | ILE | ALA | VAL | GLY | LEU | ||||
| 8 | GLY | LEU | TYR | VAL | MET | PHE | ALA | VAL | ALA |