BMRB Entry 16327
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16327
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Citation: Sperling, Lindsay; Berthold, Deborah; Sasser, Terry; Jeisy-Scott, Victoria; Rienstra, Chad. "Assignment Strategies for Large Proteins by Magic-Angle Spinning NMR: The 21-kDa Disulfide-Bond-Forming Enzyme DsbA" J. Mol. Biol. 399, 268-282 (2010).
PubMed: 20394752
Assembly members:
DsbA, polymer, 189 residues, 21000 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: purified from the natural source Host organism: Escherichia coli
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 694 |
| 15N chemical shifts | 172 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DsbA | 1 |
Entities:
Entity 1, DsbA 189 residues - 21000 Da.
| 1 | ALA | GLN | TYR | GLU | ASP | GLY | LYS | GLN | TYR | THR | ||||
| 2 | THR | LEU | GLU | LYS | PRO | VAL | ALA | GLY | ALA | PRO | ||||
| 3 | GLN | VAL | LEU | GLU | PHE | PHE | SER | PHE | PHE | CYS | ||||
| 4 | PRO | HIS | CYS | TYR | GLN | PHE | GLU | GLU | VAL | LEU | ||||
| 5 | HIS | ILE | SER | ASP | ASN | VAL | LYS | LYS | LYS | LEU | ||||
| 6 | PRO | GLU | GLY | VAL | LYS | MET | THR | LYS | TYR | HIS | ||||
| 7 | VAL | ASN | PHE | MET | GLY | GLY | ASP | LEU | GLY | LYS | ||||
| 8 | ASP | LEU | THR | GLN | ALA | TRP | ALA | VAL | ALA | MET | ||||
| 9 | ALA | LEU | GLY | VAL | GLU | ASP | LYS | VAL | THR | VAL | ||||
| 10 | PRO | LEU | PHE | GLU | GLY | VAL | GLN | LYS | THR | GLN | ||||
| 11 | THR | ILE | ARG | SER | ALA | SER | ASP | ILE | ARG | ASP | ||||
| 12 | VAL | PHE | ILE | ASN | ALA | GLY | ILE | LYS | GLY | GLU | ||||
| 13 | GLU | TYR | ASP | ALA | ALA | TRP | ASN | SER | PHE | VAL | ||||
| 14 | VAL | LYS | SER | LEU | VAL | ALA | GLN | GLN | GLU | LYS | ||||
| 15 | ALA | ALA | ALA | ASP | VAL | GLN | LEU | ARG | GLY | VAL | ||||
| 16 | PRO | ALA | MET | PHE | VAL | ASN | GLY | LYS | TYR | GLN | ||||
| 17 | LEU | ASN | PRO | GLN | GLY | MET | ASP | THR | SER | ASN | ||||
| 18 | MET | ASP | VAL | PHE | VAL | GLN | GLN | TYR | ALA | ASP | ||||
| 19 | THR | VAL | LYS | TYR | LEU | SER | GLU | LYS | LYS |
Related Database Links:
| BMRB | 17710 18396 18543 18544 |
| PDB | 1A23 1A24 1A2J 1A2L 1A2M 1AC1 1ACV 1BQ7 1DSB 1FVJ 1FVK 1TI1 1U3A 2B3S 2B6M 2HI7 2LEG 2ZUP 3DKS 3E9J 4TKY 4WET 4WEY 4WF4 4WF5 |
| DBJ | BAB38206 BAE77448 BAG79665 BAI27892 BAI33015 |
| EMBL | CAA44868 CAA56736 CAA90910 CAP78318 CAQ34212 |
| GB | AAA23715 AAB02995 AAC43519 AAC43520 AAC43521 |
| REF | NP_312810 NP_418297 NP_709659 WP_000725331 WP_000725332 |
| SP | P0A4L5 P0A4L6 P0AEG4 P0AEG5 P52235 |
| AlphaFold | P0A4L5 P0A4L6 P0AEG4 P0AEG5 P52235 |