BMRB Entry 15546
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15546
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Citation: Li, Ying; Berthold, Deborah; Gennis, Robert; Rienstra, Chad. "Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy" Protein Sci. 17, 199-204 (2008).
PubMed: 18227427
Assembly members:
DsbB, polymer, 186 residues, Formula weight is not available
UQ8, non-polymer, 250.290 Da.
Natural source: Common Name: not available Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: dsbB(Cys41Ser)-pQE70
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 201 |
| 15N chemical shifts | 57 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DsbB ploypeptide | 1 |
| 2 | substrate | 2 |
Entities:
Entity 1, DsbB ploypeptide 186 residues - Formula weight is not available
| 1 | MET | LEU | ARG | PHE | LEU | ASN | GLN | ALA | SER | GLN | ||||
| 2 | GLY | ARG | GLY | ALA | TRP | LEU | LEU | MET | ALA | PHE | ||||
| 3 | THR | ALA | LEU | ALA | LEU | GLU | LEU | THR | ALA | LEU | ||||
| 4 | TRP | PHE | GLN | HIS | VAL | MET | LEU | LEU | LYS | PRO | ||||
| 5 | SER | VAL | LEU | CYS | ILE | TYR | GLU | ARG | VAL | ALA | ||||
| 6 | LEU | PHE | GLY | VAL | LEU | GLY | ALA | ALA | LEU | ILE | ||||
| 7 | GLY | ALA | ILE | ALA | PRO | LYS | THR | PRO | LEU | ARG | ||||
| 8 | TYR | VAL | ALA | MET | VAL | ILE | TRP | LEU | TYR | SER | ||||
| 9 | ALA | PHE | ARG | GLY | VAL | GLN | LEU | THR | TYR | GLU | ||||
| 10 | HIS | THR | MET | LEU | GLN | LEU | TYR | PRO | SER | PRO | ||||
| 11 | PHE | ALA | THR | CYS | ASP | PHE | MET | VAL | ARG | PHE | ||||
| 12 | PRO | GLU | TRP | LEU | PRO | LEU | ASP | LYS | TRP | VAL | ||||
| 13 | PRO | GLN | VAL | PHE | VAL | ALA | SER | GLY | ASP | CYS | ||||
| 14 | ALA | GLU | ARG | GLN | TRP | ASP | PHE | LEU | GLY | LEU | ||||
| 15 | GLU | MET | PRO | GLN | TRP | LEU | LEU | GLY | ILE | PHE | ||||
| 16 | ILE | ALA | TYR | LEU | ILE | VAL | ALA | VAL | LEU | VAL | ||||
| 17 | VAL | ILE | SER | GLN | PRO | PHE | LYS | ALA | LYS | LYS | ||||
| 18 | ARG | ASP | LEU | PHE | GLY | ARG | GLY | SER | ARG | SER | ||||
| 19 | HIS | HIS | HIS | HIS | HIS | HIS |
Entity 2, substrate - C14 H18 O4 - 250.290 Da.
| 1 | UQ8 |
Samples:
sample_1: DsbB, [U-100% 13C; U-100% 15N], 20 mg
sample_conditions_1: ionic strength: 25 mM; pH: 7.5; pressure: 1 atm; temperature controller setting: 223 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D CC DARR mixing | sample_1 | solid | sample_conditions_1 |
| 3D NCACX | sample_1 | solid | sample_conditions_1 |
| 3D NCOCX | sample_1 | solid | sample_conditions_1 |
| 3D CAN(CO)CX | sample_1 | solid | sample_conditions_1 |
| 3D CON(CA)CX | sample_1 | solid | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Varian INOVA 750 MHz
Related Database Links:
| BMRB | 18395 18493 |
| PDB | |
| DBJ | BAA36032 BAB35103 BAG76757 BAI24997 BAI30121 |
| EMBL | CAP75720 CAQ31687 CAQ98064 CAR02574 CAR12682 |
| GB | AAA23711 AAB25233 AAC74269 AAG56036 AAN42789 |
| PIR | H85696 |
| REF | NP_309707 NP_415703 NP_707082 WP_000652474 WP_000943442 |
| SP | A1AAA8 P0A6M2 P0A6M3 P59343 Q0T5L6 |
| AlphaFold | A1AAA8 P0A6M2 P0A6M3 P59343 Q0T5L6 |