BMRB Entry 27649

Title:
hnRNPA2 low complexity domain 266-341 backbone and Cbeta chemical shifts
Deposition date:
2018-10-12
Original release date:
2018-11-05
Authors:
Ryan, Veronica; Fawzi, Nicolas
Citation:

Citation: Amaya, Joshua; Ryan, Veronica; Fawzi, Nicolas. "The SH3 domain of Fyn kinase interacts with and induces liquid-liquid phase separation of the low-complexity domain of hnRNPA2"  J. Biol. Chem. 293, 19522-19531 (2018).
PubMed: 30397184

Assembly members:

Assembly members:
hnRNPA2_266-341, polymer, 79 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: hnRNPA2_266-341_pJ411

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts196
15N chemical shifts72
1H chemical shifts72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hnRNPA2_266-3411

Entities:

Entity 1, hnRNPA2_266-341 79 residues - Formula weight is not available

1   GLYHISMETASNGLNGLYGLYGLYTYRGLY
2   GLYGLYTYRASPASNTYRGLYGLYGLYASN
3   TYRGLYSERGLYASNTYRASNASPPHEGLY
4   ASNTYRASNGLNGLNPROSERASNTYRGLY
5   PROMETLYSSERGLYASNPHEGLYGLYSER
6   ARGASNMETGLYGLYPROTYRGLYGLYGLY
7   ASNTYRGLYPROGLYGLYSERGLYGLYSER
8   GLYGLYTYRGLYGLYARGSERARGTYR

Samples:

sample_1: H2O 90%; D2O, [U-2H], 10%; MES 20 mM; Bis-Tris 1 mM; hnRNPA2 266-341, [U-99% 13C; U-99% 15N], 125 uM

sample_conditions_1: ionic strength: 0 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz

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