BMRB Entry 30722

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30722
MolProbity Validation Chart

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Title:
Solution NMR structure of the N-terminal domain of the Serine/threonine-protein phosphatase 1 regulatory subunit 10, PPP1R10
Deposition date:
2020-02-12
Original release date:
2020-02-21
Authors:
Lemak, A.; Wei, Y.; Duan, S.; Houliston, S.; Penn, L.; Arrowsmith, C.
Citation:

Citation: Wei, Yong; Redel, Cornelia; Ahlner, Alexandra; Lemak, Alexander; Johansson-Akhe, Isak; Houliston, Scott; Kenney, Tristan; Tamachi, Aaliya; Morad, Vivian; Duan, Shili; Andrews, David; Wallner, Bjorn; Sunnerhagen, Maria; Arrowsmith, Cheryl; Penn, Linda. "The MYC oncoprotein directly interacts with its chromatin cofactor PNUTS to recruit PP1 phosphatase"  Nucleic Acids Res. 50, 3505-3522 (2022).
PubMed: 35244724

Assembly members:

Assembly members:
entity_1, polymer, 148 residues, 16648.477 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSGPIDPKELLKGLDSFLT RDGEVKSVDGIAKIFSLMKE ARKMVSRCTYLNIILQTRAP EVLVKFIDVGGYKLLNSWLT YSKTTNNIPLLQQILLTLQH LPLTVDHLKQNNTAKLVKQL SKSSEDEELRKLASVLVSDW MAVIRSQS

Data sets:
Data typeCount
13C chemical shifts629
15N chemical shifts153
1H chemical shifts1070

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 148 residues - 16648.477 Da.

1   METGLYSERGLYPROILEASPPROLYSGLU
2   LEULEULYSGLYLEUASPSERPHELEUTHR
3   ARGASPGLYGLUVALLYSSERVALASPGLY
4   ILEALALYSILEPHESERLEUMETLYSGLU
5   ALAARGLYSMETVALSERARGCYSTHRTYR
6   LEUASNILEILELEUGLNTHRARGALAPRO
7   GLUVALLEUVALLYSPHEILEASPVALGLY
8   GLYTYRLYSLEULEUASNSERTRPLEUTHR
9   TYRSERLYSTHRTHRASNASNILEPROLEU
10   LEUGLNGLNILELEULEUTHRLEUGLNHIS
11   LEUPROLEUTHRVALASPHISLEULYSGLN
12   ASNASNTHRALALYSLEUVALLYSGLNLEU
13   SERLYSSERSERGLUASPGLUGLULEUARG
14   LYSLEUALASERVALLEUVALSERASPTRP
15   METALAVALILEARGSERGLNSER

Samples:

sample_1: PPP1R10 N-terminal domain, [U-13C; U-15N], 450 ± 50 uM; glycerol 2.5%; NaCl 200 mM; HEPES 20 mM; DTT 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.9; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

  • Bruker AVANCE II 800 MHz
  • Bruker AVANCE III 600 MHz

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