BMRB Entry 50166
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50166
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Citation: Orriss, George; To, Vu; Moya-Torres, Aniel; Seabrook, Genevieve; O'Neil, Joe; Stetefeld, Jorg. "Solution Structure of the Cytoplasmic Domain of NhaP2 a K +/H + Antiporter From Vibrio Cholera" Biochim. Biophys. Acta Biomembr. 1862, 183225-183225 (2020).
PubMed: 32126231
Assembly members:
Cytoplasmic tail of NhaP2 a K+/H+ antiporter from Vibrio cholera, polymer, 165 residues, Formula weight is not available
Natural source: Common Name: Vibrio cholera Taxonomy ID: 666 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio cholera
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21a(+)
Entity Sequences (FASTA):
Cytoplasmic tail of NhaP2 a K+/H+ antiporter from Vibrio cholera: MTSEWELFIYKLKADKWCIG
EPLRNLFMPEGTRIAAVFRD
NQLLHPSGSTELCEGDTLCV
MAQERDLESLSRLFSEAPEK
ASLARFFGDFFLDIEAKLQD
VALLYGLDLGELEADAKLKD
LVLEHLGETPVLGDYFEWHG
LQWVVADVVDWKVTKIGLRE
NLYFQ
- assigned_chemical_shifts
- spectral_peak_list
- theoretical_heteronucl_NOEs
- theoretical_heteronucl_T1_relaxation
- theoretical_heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 502 |
| 15N chemical shifts | 137 |
| 1H chemical shifts | 751 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | P2MIN | 1 |
Entities:
Entity 1, P2MIN 165 residues - Formula weight is not available
Sequence corresponds to the 158 amino acid fragment consisting of T397 to R555 (the full length NhaP2 protein is 581 amino acid residues) plus an additional 6 residues (ENLYFQ) at the C-terminal end of the molecule which are the remnants of the TEV protease cleavage site after TEV treatment to remove the His6-tag. The 165th and final residue is the initiating Methionine that is required for the bacterial over-expression of the protein and which preceeds the first residue T2 observed in the NMR structure. The 158 amino acid fragment corresponds to the predicted RCK and TrkA-like domains found in the cytoplasmic tail of the NhaP2 K+/H+ antiporter.
| 1 | MET | THR | SER | GLU | TRP | GLU | LEU | PHE | ILE | TYR | ||||
| 2 | LYS | LEU | LYS | ALA | ASP | LYS | TRP | CYS | ILE | GLY | ||||
| 3 | GLU | PRO | LEU | ARG | ASN | LEU | PHE | MET | PRO | GLU | ||||
| 4 | GLY | THR | ARG | ILE | ALA | ALA | VAL | PHE | ARG | ASP | ||||
| 5 | ASN | GLN | LEU | LEU | HIS | PRO | SER | GLY | SER | THR | ||||
| 6 | GLU | LEU | CYS | GLU | GLY | ASP | THR | LEU | CYS | VAL | ||||
| 7 | MET | ALA | GLN | GLU | ARG | ASP | LEU | GLU | SER | LEU | ||||
| 8 | SER | ARG | LEU | PHE | SER | GLU | ALA | PRO | GLU | LYS | ||||
| 9 | ALA | SER | LEU | ALA | ARG | PHE | PHE | GLY | ASP | PHE | ||||
| 10 | PHE | LEU | ASP | ILE | GLU | ALA | LYS | LEU | GLN | ASP | ||||
| 11 | VAL | ALA | LEU | LEU | TYR | GLY | LEU | ASP | LEU | GLY | ||||
| 12 | GLU | LEU | GLU | ALA | ASP | ALA | LYS | LEU | LYS | ASP | ||||
| 13 | LEU | VAL | LEU | GLU | HIS | LEU | GLY | GLU | THR | PRO | ||||
| 14 | VAL | LEU | GLY | ASP | TYR | PHE | GLU | TRP | HIS | GLY | ||||
| 15 | LEU | GLN | TRP | VAL | VAL | ALA | ASP | VAL | VAL | ASP | ||||
| 16 | TRP | LYS | VAL | THR | LYS | ILE | GLY | LEU | ARG | GLU | ||||
| 17 | ASN | LEU | TYR | PHE | GLN |
Related Database Links:
| EXPASY | A5F4U3 |
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