BMRB Entry 16678
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16678
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Title: 1H, 13C and 15N Chemical Shift Assignments for Sensory Rhodopsin II PubMed: 20512150
Deposition date: 2010-01-14 Original release date: 2010-06-01
Authors: Gautier, Antoine; Mott, Helen; Bostock, Mark; Kirkpatrick, John; Nietlispach, Daniel
Citation: Gautier, Antoine; Mott, Helen; Bostock, Mark; Kirkpatrick, John; Nietlispach, Daniel. "Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy." Nat. Struct. Mol. Biol. 17, 768-774 (2010).
Assembly members:
Sensory Rhodopsin II, polymer, 247 residues, 26723.572 Da.
Natural source: Common Name: Natronomonas pharaonis Taxonomy ID: 2257 Superkingdom: Archaea Kingdom: not available Genus/species: Natronomonas pharaonis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Sensory Rhodopsin II: MVGLTTLFWLGAIGMLVGTL
AFAWAGRDAGSGERRYYVTL
VGISGIAAVAYAVMALGVGW
VPVAERTVFVPRYIDWILTT
PLIVYFLGLLAGLDSREFGI
VITLNTVVMLAGFAGAMVPG
IERYALFGMGAVAFIGLVYY
LVGPMTESASQRSSGIKSLY
VRLRNLTVVLWAIYPFIWLL
GPPGVALLTPTVDVALIVYL
DLVTXVGFGFIALDAAATLR
AEHGESLAGVDTDTPAVADL
EHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 1004 |
| 15N chemical shifts | 239 |
| 1H chemical shifts | 1530 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Sensory Rhodopsin II | 1 |
Entities:
Entity 1, Sensory Rhodopsin II 247 residues - 26723.572 Da.
| 1 | MET | VAL | GLY | LEU | THR | THR | LEU | PHE | TRP | LEU | ||||
| 2 | GLY | ALA | ILE | GLY | MET | LEU | VAL | GLY | THR | LEU | ||||
| 3 | ALA | PHE | ALA | TRP | ALA | GLY | ARG | ASP | ALA | GLY | ||||
| 4 | SER | GLY | GLU | ARG | ARG | TYR | TYR | VAL | THR | LEU | ||||
| 5 | VAL | GLY | ILE | SER | GLY | ILE | ALA | ALA | VAL | ALA | ||||
| 6 | TYR | ALA | VAL | MET | ALA | LEU | GLY | VAL | GLY | TRP | ||||
| 7 | VAL | PRO | VAL | ALA | GLU | ARG | THR | VAL | PHE | VAL | ||||
| 8 | PRO | ARG | TYR | ILE | ASP | TRP | ILE | LEU | THR | THR | ||||
| 9 | PRO | LEU | ILE | VAL | TYR | PHE | LEU | GLY | LEU | LEU | ||||
| 10 | ALA | GLY | LEU | ASP | SER | ARG | GLU | PHE | GLY | ILE | ||||
| 11 | VAL | ILE | THR | LEU | ASN | THR | VAL | VAL | MET | LEU | ||||
| 12 | ALA | GLY | PHE | ALA | GLY | ALA | MET | VAL | PRO | GLY | ||||
| 13 | ILE | GLU | ARG | TYR | ALA | LEU | PHE | GLY | MET | GLY | ||||
| 14 | ALA | VAL | ALA | PHE | ILE | GLY | LEU | VAL | TYR | TYR | ||||
| 15 | LEU | VAL | GLY | PRO | MET | THR | GLU | SER | ALA | SER | ||||
| 16 | GLN | ARG | SER | SER | GLY | ILE | LYS | SER | LEU | TYR | ||||
| 17 | VAL | ARG | LEU | ARG | ASN | LEU | THR | VAL | VAL | LEU | ||||
| 18 | TRP | ALA | ILE | TYR | PRO | PHE | ILE | TRP | LEU | LEU | ||||
| 19 | GLY | PRO | PRO | GLY | VAL | ALA | LEU | LEU | THR | PRO | ||||
| 20 | THR | VAL | ASP | VAL | ALA | LEU | ILE | VAL | TYR | LEU | ||||
| 21 | ASP | LEU | VAL | THR | LYR | VAL | GLY | PHE | GLY | PHE | ||||
| 22 | ILE | ALA | LEU | ASP | ALA | ALA | ALA | THR | LEU | ARG | ||||
| 23 | ALA | GLU | HIS | GLY | GLU | SER | LEU | ALA | GLY | VAL | ||||
| 24 | ASP | THR | ASP | THR | PRO | ALA | VAL | ALA | ASP | LEU | ||||
| 25 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SENSORY RHODOPSIN II, [U-100% 15N], 0.5 mM; sodium chloride 50 mM; sodium phosphate 50 mM; sodium azide 0.05%
sample_2: SENSORY RHODOPSIN II, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 50 mM; sodium phosphate 50 mM; sodium azide 0.05%
sample_3: SENSORY RHODOPSIN II, [U-13C; U-15N; U-2H], 0.5 mM; sodium chloride 50 mM; sodium phosphate 50 mM; sodium azide 0.05%
sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CA)CB | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O, . - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
ANALYSIS, CCPN - chemical shift assignment, chemical shift calculation, peak picking
AZARA, Boucher - processing
TALOS, Cornilescu, Delaglio and Bax - Torsion angle prediction
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts