BMRB Entry 27299

Name: hnRNPA2 P298L low complexity domain 190-341 backbone and Cbeta chemical shifts
Published: 2018-01-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27299

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

hnRNPA2 P298L low complexity domain 190-341 backbone and Cbeta chemical shifts

Deposition date:

2017-11-02

Original release date:

2018-01-11

Authors:

Ryan, Veronica; Fawzi, Nicolas; Burke, Kathleen; Silva, Rute

Citation:

Citation: Ryan, Veronica; Dignon, Gregory; Zerze, Gul; Chabata, Charlene; Silva, Rute; Conicella, Alexander; Amaya, Joshua; Burke, Kathleen; Mittal, Jeetain; Fawzi, Nicolas. "Disease mutation, protein interactions, and posttranslational modifications modulate hnRNPA2 liquid-liquid phase separation" Mol. Cell 69, 465-479 (2018).
PubMed: 29358076

Assembly members:

Assembly members:
hnRNPA2_LC_P298L_disordered_monomer, polymer, 155 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_LC_P298L_pJ411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hnRNPA2_LC_P298L_disordered_monomer: GHMGRGGNFGFGDSRGGGGN FGPGPGSNFRGGSDGYGSGR GFGDGYNGYGGGPGGGNFGG SPGYGGGRGGYGGGGPGYGN QGGGYGGGYDNYGGGNYGSG NYNDFGNYNQQLSNYGPMKS GNFGGSRNMGGPYGGGNYGP GGSGGSGGYGGRSRY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	360
15N chemical shifts	144
1H chemical shifts	144

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hnRNPA2 LC P298L disordered monomer	1

Entities:

Entity 1, hnRNPA2 LC P298L disordered monomer 155 residues - Formula weight is not available

1

GLY

HIS

MET

GLY

ARG

GLY

ASN

PHE

GLY

2

PHE

GLY

ASP

SER

ARG

GLY

ASN

3

PHE

GLY

PRO

GLY

PRO

GLY

SER

ASN

PHE

ARG

4

GLY

SER

ASP

GLY

TYR

GLY

SER

GLY

ARG

5

GLY

PHE

GLY

ASP

GLY

TYR

ASN

GLY

TYR

GLY

6

GLY

PRO

GLY

ASN

PHE

GLY

7

SER

PRO

GLY

TYR

GLY

ARG

GLY

8

TYR

GLY

PRO

GLY

TYR

GLY

ASN

9

GLN

GLY

TYR

GLY

TYR

ASP

10

ASN

TYR

GLY

ASN

TYR

GLY

SER

GLY

11

ASN

TYR

ASN

ASP

PHE

GLY

ASN

TYR

ASN

GLN

12

GLN

LEU

SER

ASN

TYR

GLY

PRO

MET

LYS

SER

13

GLY

ASN

PHE

GLY

SER

ARG

ASN

MET

GLY

14

GLY

PRO

TYR

GLY

ASN

TYR

GLY

PRO

15

GLY

SER

GLY

SER

GLY

TYR

GLY

16

GLY

ARG

SER

ARG

TYR

Samples:

sample_1: hnRNPA2 LC P298L, [U-99% 13C; U-99% 15N], 50 uM; D2O, [U-2H], 10%; MES 20 mM; Bis-Tris 1 mM; H2O 90%

sample_conditions_1: 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:

CARA, Wuthrich - chemical shift assignment

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

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