BMRB Entry 51316
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51316
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Title: b2-adrenergic receptor C-terminal domain PubMed: 35625550
Deposition date: 2022-02-09 Original release date: 2022-06-08
Authors: Guillien, Myriam; Sibille, Nathalie
Citation: Guillien, Myriam; Mouhand, Assia; Fournet, Aurelie; Gontier, Amandine; Marti Navia, Aleix; Cordeiro, Tiago; Allemand, Frederic; Thureau, Aurelien; Baneres, Jean-Louis; Bernado, Pau; Sibille, Nathalie. "Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction" Biomolecules 12, 617-617 (2022).
Assembly members:
entity_1, polymer, 76 residues, Formula weight is not available
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 Vector: pET1a
Entity Sequences (FASTA):
entity_1: GAMALRRSSLKAYGNGYSSN
GNTGEQSGYHVEQEKENKLL
CEDLPGTEDFVGHQGTVPSD
NIDSQGRNCSTNDSLL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 216 |
| 15N chemical shifts | 72 |
| 1H chemical shifts | 72 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | b2AR-Cter GPCR | 1 |
Entities:
Entity 1, b2AR-Cter GPCR 76 residues - Formula weight is not available
| 1 | GLY | ALA | MET | ALA | LEU | ARG | ARG | SER | SER | LEU | ||||
| 2 | LYS | ALA | TYR | GLY | ASN | GLY | TYR | SER | SER | ASN | ||||
| 3 | GLY | ASN | THR | GLY | GLU | GLN | SER | GLY | TYR | HIS | ||||
| 4 | VAL | GLU | GLN | GLU | LYS | GLU | ASN | LYS | LEU | LEU | ||||
| 5 | CYS | GLU | ASP | LEU | PRO | GLY | THR | GLU | ASP | PHE | ||||
| 6 | VAL | GLY | HIS | GLN | GLY | THR | VAL | PRO | SER | ASP | ||||
| 7 | ASN | ILE | ASP | SER | GLN | GLY | ARG | ASN | CYS | SER | ||||
| 8 | THR | ASN | ASP | SER | LEU | LEU |
Samples:
sample_1: wt-b2AR-Cter, [U-13C; U-15N], 255 uM; Bis-Tris 50 mM; NaCl 150 mM; EDTA 1 mM; TCEP 0.5 mM; DSS-d6 5 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.7; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts