BMRB Entry 15178
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15178
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone, C' and CB 13C, 15N and 1H chemical shift assignments for the RGS domain of the human Regulator of G-protein Signalling 3(RGS3)protein PubMed: 18434541
Deposition date: 2007-03-16 Original release date: 2007-03-30
Authors: Higman, Victoria; Leidert, Martina; Schmieder, Peter; Bray, James; Elkins, Jon; Phillips, Claire; Fedorov, Oleg; Johannson, Catrine; Smee, Carol; Burgess, Nicola; Doyle, Declan; Yang, Xiaowen; Berridge, Georgine; Diehl, Annette; Sundstrom, Michael; Arrowsmith, Cheryl; Weigelt, Johan; Edwards, Aled; Oschkinat, Hartmut; Ball, Linda
Citation: Soundararajan, Meera; Willard, Francis; Kimple, Adam; Turnbull, Andrew; Ball, Linda; Schoch, Guillaume; Gileadi, Carina; Fedorov, Oleg; Dowler, Elizabeth; Higman, Victoria; Hutsell, Stephanie; Sundstrom, Michael; Doyle, Declan; Siderovski, David. "Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits" Proc. Natl. Acad. Sci. USA 105, 6457-6462 (2008).
Assembly members:
RGS3, polymer, 144 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: BL21 (DE3) - Rosetta (Novagen)
Entity Sequences (FASTA):
RGS3: SMDLSWLDLEKPTSEEALKW
GESLEKLLVHKYGLAVFQAF
LRTEFSEENLEFWLACEDFK
KVKSQSKMASKAKKIFAEYI
AIQACKEVNLDSYTREHTKD
NLQSVTRGCFDLAQKRIFGL
MEKDSYPRFLRSDLYLDLIN
QKKM
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 418 |
15N chemical shifts | 140 |
1H chemical shifts | 325 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RGS3 | 1 |
Entities:
Entity 1, RGS3 144 residues - Formula weight is not available
The N terminal SM residues are an artefact from the vector. The next 8 residues 'DLSWLDLE' are a non-natural, inserted sequence, engineered into the construct as an interaction site for 14-3-3 proteins (included for use in later studies).
1 | SER | MET | ASP | LEU | SER | TRP | LEU | ASP | LEU | GLU | ||||
2 | LYS | PRO | THR | SER | GLU | GLU | ALA | LEU | LYS | TRP | ||||
3 | GLY | GLU | SER | LEU | GLU | LYS | LEU | LEU | VAL | HIS | ||||
4 | LYS | TYR | GLY | LEU | ALA | VAL | PHE | GLN | ALA | PHE | ||||
5 | LEU | ARG | THR | GLU | PHE | SER | GLU | GLU | ASN | LEU | ||||
6 | GLU | PHE | TRP | LEU | ALA | CYS | GLU | ASP | PHE | LYS | ||||
7 | LYS | VAL | LYS | SER | GLN | SER | LYS | MET | ALA | SER | ||||
8 | LYS | ALA | LYS | LYS | ILE | PHE | ALA | GLU | TYR | ILE | ||||
9 | ALA | ILE | GLN | ALA | CYS | LYS | GLU | VAL | ASN | LEU | ||||
10 | ASP | SER | TYR | THR | ARG | GLU | HIS | THR | LYS | ASP | ||||
11 | ASN | LEU | GLN | SER | VAL | THR | ARG | GLY | CYS | PHE | ||||
12 | ASP | LEU | ALA | GLN | LYS | ARG | ILE | PHE | GLY | LEU | ||||
13 | MET | GLU | LYS | ASP | SER | TYR | PRO | ARG | PHE | LEU | ||||
14 | ARG | SER | ASP | LEU | TYR | LEU | ASP | LEU | ILE | ASN | ||||
15 | GLN | LYS | LYS | MET |
Samples:
sample_1: RGS3, [U-98% 13C; U-98% 15N], 0.2 ± 0.05 mM; H2O 90%; D2O 10%; potassium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02%
sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 300 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - processing
ANALYSIS v1.0.13, CCPNMR - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
PDB | |
DBJ | BAB70766 BAC87285 BAE90824 BAF82355 BAG53374 |
GB | AAC50394 AAH18072 AAH19039 AAH42555 AAI23616 |
PRF | 2206475A |
REF | NP_001071441 NP_001263189 NP_001263190 NP_001263191 NP_001269851 |
SP | P49796 |
TPG | DAA26468 |
AlphaFold | P49796 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts