Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50626
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Citation: Grasso, Emily; Majumdar, Ananya; Wrabl, James; Frueh, Dominique; Hilser, Vincent. "Conserved allosteric ensembles in a disordered protein using TROSY/Anti-TROSY R 2-filtered spectroscopy" Biophys. J. 120, 2498-2510 (2021).
PubMed: 33901472
Assembly members:
entity_1, polymer, 193 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pj411
Data type | Count |
13C chemical shifts | 495 |
15N chemical shifts | 166 |
1H chemical shifts | 164 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | protein | 1 |
2 | zinc 1 | 2 |
3 | zinc 2 | 2 |
Entity 1, protein 193 residues - Formula weight is not available
The initial 3 amino acids remain after cleavage of N-terminal his tag; residue 336 is the initial M in the sequence.
1 | GLY | SER | HIS | MET | ASN | THR | ALA | SER | LEU | SER | ||||
2 | GLN | GLN | GLN | ASP | GLN | LYS | PRO | ILE | PHE | ASN | ||||
3 | VAL | ILE | PRO | PRO | ILE | PRO | VAL | GLY | SER | GLU | ||||
4 | ASN | TRP | ASN | ARG | CYS | GLN | GLY | SER | GLY | ASP | ||||
5 | ASP | ASN | LEU | THR | SER | LEU | GLY | THR | LEU | ASN | ||||
6 | PHE | PRO | GLY | ARG | THR | VAL | PHE | SER | ASN | GLY | ||||
7 | TYR | SER | SER | PRO | SER | MET | ARG | PRO | ASP | VAL | ||||
8 | SER | SER | PRO | PRO | SER | SER | SER | SER | THR | ALA | ||||
9 | THR | THR | GLY | PRO | PRO | PRO | LYS | LEU | CYS | LEU | ||||
10 | VAL | CYS | SER | ASP | GLU | ALA | SER | GLY | CYS | HIS | ||||
11 | TYR | GLY | VAL | LEU | THR | CYS | GLY | SER | CYS | LYS | ||||
12 | VAL | PHE | PHE | LYS | ARG | ALA | VAL | GLU | GLY | GLN | ||||
13 | HIS | ASN | TYR | LEU | CYS | ALA | GLY | ARG | ASN | ASP | ||||
14 | CYS | ILE | ILE | ASP | LYS | ILE | ARG | ARG | LYS | ASN | ||||
15 | CYS | PRO | ALA | CYS | ARG | TYR | ARG | LYS | CYS | LEU | ||||
16 | GLN | ALA | GLY | MET | ASN | LEU | GLU | ALA | ARG | LYS | ||||
17 | THR | LYS | LYS | LYS | ILE | LYS | GLY | ILE | GLN | GLN | ||||
18 | ALA | THR | THR | GLY | VAL | SER | GLN | GLU | THR | SER | ||||
19 | GLU | ASN | PRO | GLY | ASN | LYS | THR | ILE | VAL | PRO | ||||
20 | ALA | THR | LEU |
Entity 2, zinc 1 - Zn - 65.409 Da.
1 | ZN |
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