Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19451
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Citation: Choy, Meng; Hieke, Martina; Kumar, Ganesan Senthil; Lewis, Greyson; Gonzalez-Dewhitt, Kristofer; Kessler, Rene; Stein, Benjamin; Hessenberger, Manuel; Nairn, Angus; Peti, Wolfgang; Page, Rebecca. "Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code." Proc. Natl. Acad. Sci. U.S.A. 111, 4097-4102 (2014).
PubMed: 24591642
Assembly members:
PNUTS, polymer, 84 residues, Formula weight is not available
Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-M30-GST
Entity Sequences (FASTA):
PNUTS: GAMGASDAKPVESPGDPNQL
TRKGRKRKTVTWPEEGKLRE
YFYFELDETERVNVNKIKDF
GEAAKREILSDRHAFETARR
LSHD
Data type | Count |
13C chemical shifts | 114 |
15N chemical shifts | 64 |
1H chemical shifts | 64 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PNUTS:PP1 Holoenzyme | 1 |
Entity 1, PNUTS:PP1 Holoenzyme 84 residues - Formula weight is not available
residues GAMGAS are cloning artifacts
1 | GLY | ALA | MET | GLY | ALA | SER | ASP | ALA | LYS | PRO | ||||
2 | VAL | GLU | SER | PRO | GLY | ASP | PRO | ASN | GLN | LEU | ||||
3 | THR | ARG | LYS | GLY | ARG | LYS | ARG | LYS | THR | VAL | ||||
4 | THR | TRP | PRO | GLU | GLU | GLY | LYS | LEU | ARG | GLU | ||||
5 | TYR | PHE | TYR | PHE | GLU | LEU | ASP | GLU | THR | GLU | ||||
6 | ARG | VAL | ASN | VAL | ASN | LYS | ILE | LYS | ASP | PHE | ||||
7 | GLY | GLU | ALA | ALA | LYS | ARG | GLU | ILE | LEU | SER | ||||
8 | ASP | ARG | HIS | ALA | PHE | GLU | THR | ALA | ARG | ARG | ||||
9 | LEU | SER | HIS | ASP |
sample_1: PNUTS:PP1 Holoenzyme, [U-99% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM; H2O 90%; D2O 10%
sample_2: PNUTS:PP1 Holoenzyme, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
TOPSPIN v3.1, Bruker Biospin, Keller and Wuthrich - collection, processing
XEASY vCARA 1.8.2, Keller and Wuthrich - chemical shift assignment
DBJ | BAB63324 BAC54929 BAC78178 BAD08440 BAD69765 |
EMBL | CAA73697 CAD44294 CAD67521 CAE84038 |
GB | AAB96775 AAH29765 AAH52059 AAI34806 AAI36295 |
REF | NP_001038965 NP_001108416 NP_001116637 NP_001157290 NP_002705 |
SP | O55000 Q5TM61 Q767K9 Q7YR38 Q80W00 |
AlphaFold | O55000 Q5TM61 Q767K9 Q7YR38 Q80W00 |
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