BMRB Entry 27649

Name: hnRNPA2 low complexity domain 266-341 backbone and Cbeta chemical shifts
Published: 2018-11-05

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27649

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: hnRNPA2 low complexity domain 266-341 backbone and Cbeta chemical shifts PubMed: 30397184

Deposition date: 2018-10-12 Original release date: 2018-11-05

Authors: Ryan, Veronica; Fawzi, Nicolas

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).

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

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: hnRNPA2_266-341_pJ411

Entity Sequences (FASTA):
hnRNPA2_266-341: GHMNQGGGYGGGYDNYGGGN YGSGNYNDFGNYNQQPSNYG PMKSGNFGGSRNMGGPYGGG NYGPGGSGGSGGYGGRSRY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	196
15N chemical shifts	72
1H chemical shifts	72

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hnRNPA2_266-341	1

Entities:

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

1

GLY

HIS

MET

ASN

GLN

GLY

TYR

GLY

2

GLY

TYR

ASP

ASN

TYR

GLY

ASN

3

TYR

GLY

SER

GLY

ASN

TYR

ASN

ASP

PHE

GLY

4

ASN

TYR

ASN

GLN

PRO

SER

ASN

TYR

GLY

5

PRO

MET

LYS

SER

GLY

ASN

PHE

GLY

SER

6

ARG

ASN

MET

GLY

PRO

TYR

GLY

7

ASN

TYR

GLY

PRO

GLY

SER

GLY

SER

8

GLY

TYR

GLY

ARG

SER

ARG

TYR

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_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 shifts
SPARKY: Backbone or all simulated shifts