BMRB Entry 15207
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15207
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Citation: Boudet, Julien; Chouquet, Anne; Chahboune, Aicha; Giustini, Cecile; Joris, Bernard; Simorre, Jean-Pierre; Bougault, Catherine. "1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function" Biomol. NMR Assignments 1, 89-91 (2007).
PubMed: 19636835
Assembly members:
yajg, polymer, 182 residues, 19990 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: Escherichia Genus/species: coli coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET26b
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 750 |
| 15N chemical shifts | 184 |
| 1H chemical shifts | 1167 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | yajg | 1 |
Entities:
Entity 1, yajg 182 residues - 19990 Da.
Residues 175-182 represent a non-native C-terminal histidine tag Signal sequence at the N-terminus of yajg from E. coli (first 18 residues of Swiss-Prot entry P0ADA6) have been deleted.
| 1 | ALA | LYS | PRO | PRO | THR | THR | ILE | GLU | VAL | SER | ||||
| 2 | PRO | THR | ILE | THR | LEU | PRO | GLN | GLN | ASP | PRO | ||||
| 3 | SER | LEU | MET | GLY | VAL | THR | VAL | SER | ILE | ASN | ||||
| 4 | GLY | ALA | ASP | GLN | ARG | THR | ASP | GLN | ALA | LEU | ||||
| 5 | ALA | LYS | VAL | THR | ARG | ASP | ASN | GLN | ILE | VAL | ||||
| 6 | THR | LEU | THR | ALA | SER | ARG | ASP | LEU | ARG | PHE | ||||
| 7 | LEU | LEU | GLN | GLU | VAL | LEU | GLU | LYS | GLN | MET | ||||
| 8 | THR | ALA | ARG | GLY | TYR | MET | VAL | GLY | PRO | ASN | ||||
| 9 | GLY | PRO | VAL | ASN | LEU | GLN | ILE | ILE | VAL | SER | ||||
| 10 | GLN | LEU | TYR | ALA | ASP | VAL | SER | GLN | GLY | ASN | ||||
| 11 | VAL | ARG | TYR | ASN | ILE | ALA | THR | LYS | ALA | ASP | ||||
| 12 | ILE | ALA | ILE | ILE | ALA | THR | ALA | GLN | ASN | GLY | ||||
| 13 | ASN | LYS | MET | THR | LYS | ASN | TYR | ARG | ALA | SER | ||||
| 14 | TYR | ASN | VAL | GLU | GLY | ALA | PHE | GLN | ALA | SER | ||||
| 15 | ASN | LYS | ASN | ILE | ALA | ASP | ALA | VAL | ASN | SER | ||||
| 16 | VAL | LEU | THR | ASP | THR | ILE | ALA | ASP | MET | SER | ||||
| 17 | GLN | ASP | THR | SER | ILE | HIS | GLU | PHE | ILE | LYS | ||||
| 18 | GLN | ASN | ALA | ARG | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 19 | HIS | HIS |
Related Database Links:
| DBJ | BAB33911 BAE76214 BAG75983 BAI23808 BAI29279 |
| EMBL | CAP74968 CAQ30906 CAQ97309 CAR01777 CAR06667 |
| GB | AAB28883 AAB40190 AAC73537 AAG54784 AAN42034 |
| REF | NP_308515 NP_414968 NP_706327 WP_000473497 WP_000473498 |
| SP | P0ADA5 P0ADA6 |
| AlphaFold | P0ADA5 P0ADA6 |
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