BMRB Entry 50257

Name: hnRNPA2 1-189 bound to rA2RE11
Published: 2020-08-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50257

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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 1-189 bound to rA2RE11

Deposition date:

2020-05-01

Original release date:

2020-08-20

Authors:

Ryan, Veronica; Watters, Scott; Naik, Mandar; Fawzi, Nicolas

Citation:

Citation: Ryan, Veronica; Watters, Scott; Amaya, Joshua; Khatiwada, Balabhadra; Vendetti, Vincenzo; Naik, Mandar; Fawzi, Nicolas. "Weak binding to the A2RE RNA rigidifies hnRNPA2 RRMs and reduces liquid-liquid phase separation and aggregation" Nucleic Acids Res. 48, 10542-10554 (2020).
PubMed: 32870271

Assembly members:

Assembly members:
entity_1, polymer, 189 residues, Formula weight is not available
entity_2, polymer, 11 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: pJ411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEREKEQFRKLFIGGLSFET TEESLRNYYEQWGKLTDCVV MRDPASKRSRGFGFVTFSSM AEVDAAMAARPHSIDGRVVE PKRAVAREESGKPGAHVTVK KLFVGGIKEDTEEHHLRDYF EEYGKIDTIEIITDRQSGKK RGFGFVTFDDHDPVDKIVLQ KYHTINGHNAEVRKALSRQE MQEVQSSRS
entity_2: GCCAAGGAGCC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	88
1H chemical shifts	88

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hnRNPA2 1-189	1
2	rA2RE11	2

Entities:

Entity 1, hnRNPA2 1-189 189 residues - Formula weight is not available

1

MET

GLU

ARG

GLU

LYS

GLU

GLN

PHE

ARG

LYS

2

LEU

PHE

ILE

GLY

LEU

SER

PHE

GLU

THR

3

THR

GLU

SER

LEU

ARG

ASN

TYR

GLU

4

GLN

TRP

GLY

LYS

LEU

THR

ASP

CYS

VAL

5

MET

ARG

ASP

PRO

ALA

SER

LYS

ARG

SER

ARG

6

GLY

PHE

GLY

PHE

VAL

THR

PHE

SER

MET

7

ALA

GLU

VAL

ASP

ALA

MET

ALA

ARG

8

PRO

HIS

SER

ILE

ASP

GLY

ARG

VAL

GLU

9

PRO

LYS

ARG

ALA

VAL

ALA

ARG

GLU

SER

10

GLY

LYS

PRO

GLY

ALA

HIS

VAL

THR

VAL

LYS

11

LYS

LEU

PHE

VAL

GLY

ILE

LYS

GLU

ASP

12

THR

GLU

HIS

LEU

ARG

ASP

TYR

PHE

13

GLU

TYR

GLY

LYS

ILE

ASP

THR

ILE

GLU

14

ILE

THR

ASP

ARG

GLN

SER

GLY

LYS

15

ARG

GLY

PHE

GLY

PHE

VAL

THR

PHE

ASP

16

HIS

ASP

PRO

VAL

ASP

LYS

ILE

VAL

LEU

GLN

17

LYS

TYR

HIS

THR

ILE

ASN

GLY

HIS

ASN

ALA

18

GLU

VAL

ARG

LYS

ALA

LEU

SER

ARG

GLN

GLU

19

MET

GLN

GLU

VAL

GLN

SER

ARG

SER

Entity 2, rA2RE11 11 residues - Formula weight is not available

1

G

C

A

G

A

G

C

2

C

Samples:

sample_1: hnRNPA2 1-189, [U-99% 15N], 200 uM; rA2RE11 600 uM; D2O, [U-99% 2H], 10%; NaCl 150 mM; NaPi 20 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - data analysis

NMRFAM-SPARKY - 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