Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18721
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Citation: Letourneau, Danny; Lorin, Aurelien; Lefebvre, Andree; Cabana, Jerome; Lavigne, Pierre; LeHoux, Jean-Guy. "Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5." Biochim. Biophys. Acta 1831, 1589-1599 (2013).
PubMed: 23872533
Assembly members:
Molecule_1, polymer, 213 residues, 23797.1169 Da.
HisTag, polymer, 6 residues, 846.9074 Da.
Natural source: Common Name: Escherichia coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3A
Data type | Count |
13C chemical shifts | 557 |
15N chemical shifts | 186 |
1H chemical shifts | 186 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | StarD5 | 1 |
2 | HisTag | 2 |
Entity 1, StarD5 213 residues - 23797.1169 Da.
1 | MET | ASP | PRO | ALA | LEU | ALA | ALA | GLN | MET | SER | ||||
2 | GLU | ALA | VAL | ALA | GLU | LYS | MET | LEU | GLN | TYR | ||||
3 | ARG | ARG | ASP | THR | ALA | GLY | TRP | LYS | ILE | CYS | ||||
4 | ARG | GLU | GLY | ASN | GLY | VAL | SER | VAL | SER | TRP | ||||
5 | ARG | PRO | SER | VAL | GLU | PHE | PRO | GLY | ASN | LEU | ||||
6 | TYR | ARG | GLY | GLU | GLY | ILE | VAL | TYR | GLY | THR | ||||
7 | LEU | GLU | GLU | VAL | TRP | ASP | CYS | VAL | LYS | PRO | ||||
8 | ALA | VAL | GLY | GLY | LEU | ARG | VAL | LYS | TRP | ASP | ||||
9 | GLU | ASN | VAL | THR | GLY | PHE | GLU | ILE | ILE | GLN | ||||
10 | SER | ILE | THR | ASP | THR | LEU | CYS | VAL | SER | ARG | ||||
11 | THR | SER | THR | PRO | SER | ALA | ALA | MET | LYS | LEU | ||||
12 | ILE | SER | PRO | ARG | ASP | PHE | VAL | ASP | LEU | VAL | ||||
13 | LEU | VAL | LYS | ARG | TYR | GLU | ASP | GLY | THR | ILE | ||||
14 | SER | SER | ASN | ALA | THR | HIS | VAL | GLU | HIS | PRO | ||||
15 | LEU | CYS | PRO | PRO | LYS | PRO | GLY | PHE | VAL | ARG | ||||
16 | GLY | PHE | ASN | HIS | PRO | CYS | GLY | CYS | PHE | CYS | ||||
17 | GLU | PRO | LEU | PRO | GLY | GLU | PRO | THR | LYS | THR | ||||
18 | ASN | LEU | VAL | THR | PHE | PHE | HIS | THR | ASP | LEU | ||||
19 | SER | GLY | TYR | LEU | PRO | GLN | ASN | VAL | VAL | ASP | ||||
20 | SER | PHE | PHE | PRO | ARG | SER | MET | THR | ARG | PHE | ||||
21 | TYR | ALA | ASN | LEU | GLN | LYS | ALA | VAL | LYS | GLN | ||||
22 | PHE | HIS | GLU |
Entity 2, HisTag 6 residues - 846.9074 Da.
1 | HIS | HIS | HIS | HIS | HIS | HIS |
BMRB | 17909 |
PDB | 2R55 |
EMBL | CAH91861 |
GB | AAH04365 AAL89654 AIC52409 EAW99097 EHH27540 |
REF | NP_001126078 NP_001247845 NP_871629 XP_003281060 XP_003810787 |
SP | Q5R8P9 Q9NSY2 |
AlphaFold | Q5R8P9 Q9NSY2 |
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