BMRB Entry 50781
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50781
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Citation: Vos, Margaret; Piraino, Benjamin; LaBreck, Christopher; Rahmani, Negar; Trebino, Catherine; Schoenle, Marta; Peti, Wolfgang; Camberg, Jodi; Page, Rebecca. "Degradation of the E. coli antitoxin MqsA by the proteolytic complex ClpXP is regulated by zinc occupancy and oxidation" J. Biol. Chem. 298, 101557-101557 (2022).
PubMed: 34974059
Assembly members:
entity_1, polymer, 57 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: RP1B
Entity Sequences (FASTA):
entity_1: GHMTDKRKDGSGKLLYCSFC
GKSQHEVRKLIAGPSVYICD
ECVDLCNDIIREEIKEV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 111 |
| 15N chemical shifts | 53 |
| 1H chemical shifts | 53 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ClpX Residues 1-55 Dimer, Chain 1 | 1 |
| 2 | ClpX Residues 1-55 Dimer, Chain 2 | 1 |
| 3 | Zinc Ion, 1 | 2 |
| 4 | Zinc Ion, 2 | 2 |
Entities:
Entity 1, ClpX Residues 1-55 Dimer, Chain 1 57 residues - Formula weight is not available
GH are a cloning artifacts; ClpX sequence starts with MTD
| 1 | GLY | HIS | MET | THR | ASP | LYS | ARG | LYS | ASP | GLY | ||||
| 2 | SER | GLY | LYS | LEU | LEU | TYR | CYS | SER | PHE | CYS | ||||
| 3 | GLY | LYS | SER | GLN | HIS | GLU | VAL | ARG | LYS | LEU | ||||
| 4 | ILE | ALA | GLY | PRO | SER | VAL | TYR | ILE | CYS | ASP | ||||
| 5 | GLU | CYS | VAL | ASP | LEU | CYS | ASN | ASP | ILE | ILE | ||||
| 6 | ARG | GLU | GLU | ILE | LYS | GLU | VAL |
Entity 2, Zinc Ion, 1 - Zn - 65.409 Da.
| 1 | ZN |
Related Database Links:
| NCBI | P0A6H1 |
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