Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17640
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Citation: Nash, Abigail; McNulty, Reginald; Shillito, Mary Elizabeth; Swartz, Trevor; Bogomolni, Roberto; Luecke, Hartmut; Gardner, Kevin. "Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein." Proc. Natl. Acad. Sci. U.S.A. 108, 9449-9454 (2011).
PubMed: 21606338
Assembly members:
EL222(14-222), polymer, 212 residues, Formula weight is not available
FMN, non-polymer, 456.344 Da.
Natural source: Common Name: Erythrobacter litoralis Taxonomy ID: 314225 Superkingdom: Bacteria Kingdom: not available Genus/species: Erythrobacter litoralis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: His6-GB1 parallel
Data type | Count |
13C chemical shifts | 437 |
15N chemical shifts | 167 |
1H chemical shifts | 655 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EL222(14-222) protein | 1 |
2 | FMN | 2 |
Entity 1, EL222(14-222) protein 212 residues - Formula weight is not available
EL222 = Erythrobactor litoralis HTCC2594 protein, 222aa total. GB incorrectly annotated to function and start Met aa. first three residues (GEF) are vector-derived; remainder of sequence are residues 14-222 of protein
1 | GLY | GLU | PHE | GLY | ALA | ASP | ASP | THR | ARG | VAL | ||||
2 | GLU | VAL | GLN | PRO | PRO | ALA | GLN | TRP | VAL | LEU | ||||
3 | ASP | LEU | ILE | GLU | ALA | SER | PRO | ILE | ALA | SER | ||||
4 | VAL | VAL | SER | ASP | PRO | ARG | LEU | ALA | ASP | ASN | ||||
5 | PRO | LEU | ILE | ALA | ILE | ASN | GLN | ALA | PHE | THR | ||||
6 | ASP | LEU | THR | GLY | TYR | SER | GLU | GLU | GLU | CYS | ||||
7 | VAL | GLY | ARG | ASN | CYS | ARG | PHE | LEU | ALA | GLY | ||||
8 | SER | GLY | THR | GLU | PRO | TRP | LEU | THR | ASP | LYS | ||||
9 | ILE | ARG | GLN | GLY | VAL | ARG | GLU | HIS | LYS | PRO | ||||
10 | VAL | LEU | VAL | GLU | ILE | LEU | ASN | TYR | LYS | LYS | ||||
11 | ASP | GLY | THR | PRO | PHE | ARG | ASN | ALA | VAL | LEU | ||||
12 | VAL | ALA | PRO | ILE | TYR | ASP | ASP | ASP | ASP | GLU | ||||
13 | LEU | LEU | TYR | PHE | LEU | GLY | SER | GLN | VAL | GLU | ||||
14 | VAL | ASP | ASP | ASP | GLN | PRO | ASN | MET | GLY | MET | ||||
15 | ALA | ARG | ARG | GLU | ARG | ALA | ALA | GLU | MET | LEU | ||||
16 | LYS | THR | LEU | SER | PRO | ARG | GLN | LEU | GLU | VAL | ||||
17 | THR | THR | LEU | VAL | ALA | SER | GLY | LEU | ARG | ASN | ||||
18 | LYS | GLU | VAL | ALA | ALA | ARG | LEU | GLY | LEU | SER | ||||
19 | GLU | LYS | THR | VAL | LYS | MET | HIS | ARG | GLY | LEU | ||||
20 | VAL | MET | GLU | LYS | LEU | ASN | LEU | LYS | THR | SER | ||||
21 | ALA | ASP | LEU | VAL | ARG | ILE | ALA | VAL | GLU | ALA | ||||
22 | GLY | ILE |
Entity 2, FMN - C17 H21 N4 O9 P - 456.344 Da.
1 | FMN |
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