BMRB Entry 17361
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17361
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Higman, Victoria; Varga, Krisztina; Aslimovska, Lubica; Judge, Peter; Sperling, Lindsay; Rienstra, Chad; Watts, Anthony. "The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy." Angew. Chem. Int. Ed. Engl. 50, 8432-8435 (2011).
PubMed: 21770003
Assembly members:
bR, polymer, 249 residues, Formula weight is not available
Natural source: Common Name: Halobacterium salinarum Taxonomy ID: 2242 Superkingdom: Archaea Kingdom: not available Genus/species: Halobacterium salinarum
Experimental source: Production method: purified from the natural source
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 204 |
| 15N chemical shifts | 51 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | bR | 1 |
Entities:
Entity 1, bR 249 residues - Formula weight is not available
| 1 | GLN | ALA | GLN | ILE | THR | GLY | ARG | PRO | GLU | TRP | ||||
| 2 | ILE | TRP | LEU | ALA | LEU | GLY | THR | ALA | LEU | MET | ||||
| 3 | GLY | LEU | GLY | THR | LEU | TYR | PHE | LEU | VAL | LYS | ||||
| 4 | GLY | MET | GLY | VAL | SER | ASP | PRO | ASP | ALA | LYS | ||||
| 5 | LYS | PHE | TYR | ALA | ILE | THR | THR | LEU | VAL | PRO | ||||
| 6 | ALA | ILE | ALA | PHE | THR | MET | TYR | LEU | SER | MET | ||||
| 7 | LEU | LEU | GLY | TYR | GLY | LEU | THR | MET | VAL | PRO | ||||
| 8 | PHE | GLY | GLY | GLU | GLN | ASN | PRO | ILE | TYR | TRP | ||||
| 9 | ALA | ARG | TYR | ALA | ASP | TRP | LEU | PHE | THR | THR | ||||
| 10 | PRO | LEU | LEU | LEU | LEU | ASP | LEU | ALA | LEU | LEU | ||||
| 11 | VAL | ASP | ALA | ASP | GLN | GLY | THR | ILE | LEU | ALA | ||||
| 12 | LEU | VAL | GLY | ALA | ASP | GLY | ILE | MET | ILE | GLY | ||||
| 13 | THR | GLY | LEU | VAL | GLY | ALA | LEU | THR | LYS | VAL | ||||
| 14 | TYR | SER | TYR | ARG | PHE | VAL | TRP | TRP | ALA | ILE | ||||
| 15 | SER | THR | ALA | ALA | MET | LEU | TYR | ILE | LEU | TYR | ||||
| 16 | VAL | LEU | PHE | PHE | GLY | PHE | THR | SER | LYS | ALA | ||||
| 17 | GLU | SER | MET | ARG | PRO | GLU | VAL | ALA | SER | THR | ||||
| 18 | PHE | LYS | VAL | LEU | ARG | ASN | VAL | THR | VAL | VAL | ||||
| 19 | LEU | TRP | SER | ALA | TYR | PRO | VAL | VAL | TRP | LEU | ||||
| 20 | ILE | GLY | SER | GLU | GLY | ALA | GLY | ILE | VAL | PRO | ||||
| 21 | LEU | ASN | ILE | GLU | THR | LEU | LEU | PHE | MET | VAL | ||||
| 22 | LEU | ASP | VAL | SER | ALA | LYS | VAL | GLY | PHE | GLY | ||||
| 23 | LEU | ILE | LEU | LEU | ARG | SER | ARG | ALA | ILE | PHE | ||||
| 24 | GLY | GLU | ALA | GLU | ALA | PRO | GLU | PRO | SER | ALA | ||||
| 25 | GLY | ASP | GLY | ALA | ALA | ALA | THR | SER | ASP |
Samples:
sample_1: bR, [U-100% 13C; U-100% 15N], 18 mg; sodium citrate 20 mM; sodium azide 0.01%; H2O 95%; D2O 5%; purple membrane lipids, [U-100% 13C; U-100% 15N], 6 mg
sample_conditions_1: ionic strength: 0.2 mM; pH: 6.0; pressure: 1 atm; temperature: 278 K
sample_conditions_2: ionic strength: 0.2 mM; pH: 6.0; pressure: 1 atm; temperature: 263 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| DARR | sample_1 | solid | sample_conditions_1 |
| NCACX | sample_1 | isotropic | sample_conditions_1 |
| NCOCX | sample_1 | isotropic | sample_conditions_1 |
| CANCO | sample_1 | isotropic | sample_conditions_2 |
| CANCOCX | sample_1 | isotropic | sample_conditions_2 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Analysis v2.1.15, CCPN - chemical shift assignment, peak picking
Spinsight, Chemagnetics/Varian - collection
NMR spectrometers:
- Varian Infinity Plus 800 MHz
- Varian Infinity Plus 500 MHz