BMRB Entry 30077
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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/BMR30077
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Title: Structural model of a apo G-protein alpha subunit determined with NMR residual dipolar couplings and SAXS PubMed: 27298341
Deposition date: 2016-05-07 Original release date: 2016-06-24
Authors: Goricanec, D.; Stehle, R.; Grigoriu, S.; Wagner, G.; Hagn, F.
Citation: Goricanec, D.; Stehle, R.; Egloff, P.; Grigori, S.; Plueckthun, A.; Wagner, G.; Hagn, F.. "Conformational dynamics of a G-protein alpha subunit is tightly regulated by nucleotide binding" Proc. Natl. Acad. Sci. U. S. A. 113, E3629-E3638 (2016).
Assembly members:
Guanine nucleotide-binding protein G(i) subunit alpha-1, polymer, 326 residues, 37247.414 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
Entity Sequences (FASTA):
Guanine nucleotide-binding protein G(i) subunit alpha-1: GASREVKLLLLGAGESGKST
IVKQMKIIHEAGYSEEECKQ
YKAVVYSNTIQSIIAIIRAM
GRLKIDFGDSARADDARQLF
VLAGAAEEGFMTAELAGVIK
RLWKDSGVQACFNRSREYQL
NDSAAYYLNDLDRIAQPNYI
PTQQDVLRTRVKTTGIVETH
FTFKDLHFKMFDVGGQRSER
KKWIHCFEGVAAIIFCVALS
DYDLVLAEDEEMNRMHESMK
LFDSICNNKWFTDTSIILFL
NKKDLFEEKIKKSPLTICYQ
EYAGSNTYEEAAAYIQCQFE
DLNKRKDTKEIYTHFTCATD
TKNVQFVFDAVTDVIIKNNL
KDCGLF
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 244 |
| 1H chemical shifts | 244 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 326 residues - 37247.414 Da.
| 1 | GLY | ALA | SER | ARG | GLU | VAL | LYS | LEU | LEU | LEU | ||||
| 2 | LEU | GLY | ALA | GLY | GLU | SER | GLY | LYS | SER | THR | ||||
| 3 | ILE | VAL | LYS | GLN | MET | LYS | ILE | ILE | HIS | GLU | ||||
| 4 | ALA | GLY | TYR | SER | GLU | GLU | GLU | CYS | LYS | GLN | ||||
| 5 | TYR | LYS | ALA | VAL | VAL | TYR | SER | ASN | THR | ILE | ||||
| 6 | GLN | SER | ILE | ILE | ALA | ILE | ILE | ARG | ALA | MET | ||||
| 7 | GLY | ARG | LEU | LYS | ILE | ASP | PHE | GLY | ASP | SER | ||||
| 8 | ALA | ARG | ALA | ASP | ASP | ALA | ARG | GLN | LEU | PHE | ||||
| 9 | VAL | LEU | ALA | GLY | ALA | ALA | GLU | GLU | GLY | PHE | ||||
| 10 | MET | THR | ALA | GLU | LEU | ALA | GLY | VAL | ILE | LYS | ||||
| 11 | ARG | LEU | TRP | LYS | ASP | SER | GLY | VAL | GLN | ALA | ||||
| 12 | CYS | PHE | ASN | ARG | SER | ARG | GLU | TYR | GLN | LEU | ||||
| 13 | ASN | ASP | SER | ALA | ALA | TYR | TYR | LEU | ASN | ASP | ||||
| 14 | LEU | ASP | ARG | ILE | ALA | GLN | PRO | ASN | TYR | ILE | ||||
| 15 | PRO | THR | GLN | GLN | ASP | VAL | LEU | ARG | THR | ARG | ||||
| 16 | VAL | LYS | THR | THR | GLY | ILE | VAL | GLU | THR | HIS | ||||
| 17 | PHE | THR | PHE | LYS | ASP | LEU | HIS | PHE | LYS | MET | ||||
| 18 | PHE | ASP | VAL | GLY | GLY | GLN | ARG | SER | GLU | ARG | ||||
| 19 | LYS | LYS | TRP | ILE | HIS | CYS | PHE | GLU | GLY | VAL | ||||
| 20 | ALA | ALA | ILE | ILE | PHE | CYS | VAL | ALA | LEU | SER | ||||
| 21 | ASP | TYR | ASP | LEU | VAL | LEU | ALA | GLU | ASP | GLU | ||||
| 22 | GLU | MET | ASN | ARG | MET | HIS | GLU | SER | MET | LYS | ||||
| 23 | LEU | PHE | ASP | SER | ILE | CYS | ASN | ASN | LYS | TRP | ||||
| 24 | PHE | THR | ASP | THR | SER | ILE | ILE | LEU | PHE | LEU | ||||
| 25 | ASN | LYS | LYS | ASP | LEU | PHE | GLU | GLU | LYS | ILE | ||||
| 26 | LYS | LYS | SER | PRO | LEU | THR | ILE | CYS | TYR | GLN | ||||
| 27 | GLU | TYR | ALA | GLY | SER | ASN | THR | TYR | GLU | GLU | ||||
| 28 | ALA | ALA | ALA | TYR | ILE | GLN | CYS | GLN | PHE | GLU | ||||
| 29 | ASP | LEU | ASN | LYS | ARG | LYS | ASP | THR | LYS | GLU | ||||
| 30 | ILE | TYR | THR | HIS | PHE | THR | CYS | ALA | THR | ASP | ||||
| 31 | THR | LYS | ASN | VAL | GLN | PHE | VAL | PHE | ASP | ALA | ||||
| 32 | VAL | THR | ASP | VAL | ILE | ILE | LYS | ASN | ASN | LEU | ||||
| 33 | LYS | ASP | CYS | GLY | LEU | PHE |
Samples:
sample_1: G protein alpha subunit subtype i1, GNAI1, [U-98% 2H; U-99% 13C; U-99% 15N], 400 uM; H2O 95%; D2O 5%; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; magnesium chloride 5 mM
sample_2: G protein alpha subunit subtype i1, GNAI1, [U-98% 15N; U-90% 2H], 250 uM; H2O 95%; D2O 5%; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; magnesium chloride 5 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K
sample_conditions_2: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
TOPSPIN, Bruker Biospin - collection
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts