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PDB ID: 2jnu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15128
MolProbity Validation Chart
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NMR-STAR v3 text file.
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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).
PubMed: 18434541
Assembly members:
RGS14, polymer, 154 residues, 17728.135 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 Vector: Home-made vector pLIC-SGC1
Data type | Count |
13C chemical shifts | 567 |
15N chemical shifts | 151 |
1H chemical shifts | 1011 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RGS domain | 1 |
Entity 1, RGS domain 154 residues - 17728.135 Da.
The two residues at the extreme N-terminus (SM) are from the vector following TEV cleavage of the N-terminus hexahistidine purification tag.
1 | SER | MET | THR | GLU | GLU | GLN | PRO | VAL | ALA | SER | ||||
2 | TRP | ALA | LEU | SER | PHE | GLU | ARG | LEU | LEU | GLN | ||||
3 | ASP | PRO | LEU | GLY | LEU | ALA | TYR | PHE | THR | GLU | ||||
4 | PHE | LEU | LYS | LYS | GLU | PHE | SER | ALA | GLU | ASN | ||||
5 | VAL | THR | PHE | TRP | LYS | ALA | CYS | GLU | ARG | PHE | ||||
6 | GLN | GLN | ILE | PRO | ALA | SER | ASP | THR | GLN | GLN | ||||
7 | LEU | ALA | GLN | GLU | ALA | ARG | ASN | ILE | TYR | GLN | ||||
8 | GLU | PHE | LEU | SER | SER | GLN | ALA | LEU | SER | PRO | ||||
9 | VAL | ASN | ILE | ASP | ARG | GLN | ALA | TRP | LEU | GLY | ||||
10 | GLU | GLU | VAL | LEU | ALA | GLU | PRO | ARG | PRO | ASP | ||||
11 | MET | PHE | ARG | ALA | GLN | GLN | LEU | GLN | ILE | PHE | ||||
12 | ASN | LEU | MET | LYS | PHE | ASP | SER | TYR | ALA | ARG | ||||
13 | PHE | VAL | LYS | SER | PRO | LEU | TYR | ARG | GLU | CYS | ||||
14 | LEU | LEU | ALA | GLU | ALA | GLU | GLY | ARG | PRO | LEU | ||||
15 | ARG | GLU | PRO | GLY | SER | SER | ARG | LEU | GLY | SER | ||||
16 | PRO | ASP | ALA | THR |
PDB | 2JNU |
DBJ | BAJ20688 |
GB | AAH14094 ADZ15921 EAW85011 EAW85012 EAW85013 |
REF | NP_001179660 NP_006471 XP_001089197 XP_002744538 XP_003280558 |
SP | O43566 |
TPG | DAA27643 |
AlphaFold | O43566 |
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