BMRB Entry 19451

Title:
Chemical Shift Assignment of the PNUTS PP1 Binding Domain
Deposition date:
2013-08-24
Original release date:
2014-04-14
Authors:
Choy, Meng Shyan; Hieke, Martina; Peti, Wolfgang
Citation:

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:

Assembly members:
PNUTS, polymer, 84 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-M30-GST

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts114
15N chemical shifts64
1H chemical shifts64

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PNUTS:PP1 Holoenzyme1

Entities:

Entity 1, PNUTS:PP1 Holoenzyme 84 residues - Formula weight is not available

residues GAMGAS are cloning artifacts

1   GLYALAMETGLYALASERASPALALYSPRO
2   VALGLUSERPROGLYASPPROASNGLNLEU
3   THRARGLYSGLYARGLYSARGLYSTHRVAL
4   THRTRPPROGLUGLUGLYLYSLEUARGGLU
5   TYRPHETYRPHEGLULEUASPGLUTHRGLU
6   ARGVALASNVALASNLYSILELYSASPPHE
7   GLYGLUALAALALYSARGGLUILELEUSER
8   ASPARGHISALAPHEGLUTHRALAARGARG
9   LEUSERHISASP

Samples:

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin, Keller and Wuthrich - collection, processing

XEASY vCARA 1.8.2, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks