BMRB Entry 51741

Name: EWS RRM-RG2-ZnF
Published: 2023-05-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51741

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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:

EWS RRM-RG2-ZnF

Deposition date:

2022-12-15

Original release date:

2023-05-24

Authors:

Selig, Emily; Xu, Xiaoping; Libich, David

Citation:

Citation: Selig, Emily; Bhura, Roohi; White, Matthew; Akula, Shivani; Hoffman, Renee; Tovar, Carmel; Xu, Xiaoping; Booth, Rachell; Libich, David. "Biochemical and biophysical characterization of the nucleic acid binding properties of the RNA/DNA binding protein EWS" Biopolymers 114, e23536-e23536 (2023).
PubMed: 36929870

Assembly members:

Assembly members:
entity_1, polymer, 193 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GADNSAIYVQGLNDSVTLDD LADFFKQCGVVKMNKRTGQP MIHIYLDKETGKPKGDATVS YEDPPTAKAAVEWFDGKDFQ GSKLKVSLARKKPPMNSMRG GLPPREGRGMPPPLRGGPGG PGGPGGPMGRMGGRGGDRGG FPPRGPRGSRGNPSGGGNVQ HRAGDWQCPNPGCGNQNFAW RTECNQCKAPKPE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	382
15N chemical shifts	132
1H chemical shifts	132

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM-RG2-ZnF	1
2	zinc ion	2

Entities:

Entity 1, RRM-RG2-ZnF 193 residues - Formula weight is not available

1

GLY

ALA

ASP

ASN

SER

ALA

ILE

TYR

VAL

GLN

2

GLY

LEU

ASN

ASP

SER

VAL

THR

LEU

ASP

3

LEU

ALA

ASP

PHE

LYS

GLN

CYS

GLY

VAL

4

VAL

LYS

MET

ASN

LYS

ARG

THR

GLY

GLN

PRO

5

MET

ILE

HIS

ILE

TYR

LEU

ASP

LYS

GLU

THR

6

GLY

LYS

PRO

LYS

GLY

ASP

ALA

THR

VAL

SER

7

TYR

GLU

ASP

PRO

THR

ALA

LYS

ALA

8

VAL

GLU

TRP

PHE

ASP

GLY

LYS

ASP

PHE

GLN

9

GLY

SER

LYS

LEU

LYS

VAL

SER

LEU

ALA

ARG

10

LYS

PRO

MET

ASN

SER

MET

ARG

GLY

11

GLY

LEU

PRO

ARG

GLU

GLY

ARG

GLY

MET

12

PRO

LEU

ARG

GLY

PRO

GLY

13

PRO

GLY

PRO

GLY

PRO

MET

GLY

ARG

14

MET

GLY

ARG

GLY

ASP

ARG

GLY

15

PHE

PRO

ARG

GLY

PRO

ARG

GLY

SER

ARG

16

GLY

ASN

PRO

SER

GLY

ASN

VAL

GLN

17

HIS

ARG

ALA

GLY

ASP

TRP

GLN

CYS

PRO

ASN

18

PRO

GLY

CYS

GLY

ASN

GLN

ASN

PHE

ALA

TRP

19

ARG

THR

GLU

CYS

ASN

GLN

CYS

LYS

ALA

PRO

20

LYS

PRO

GLU

Entity 2, zinc ion - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: EWS RRM-RG2-ZnF monomer, [U-99% 15N], 400 uM; potassium phosphate 20 mM; potassium chloride 150 mM; zinc chloride 0.5 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v3.1 - chemical shift assignment

NMRPipe - processing

SMILE - processing

NMRDraw - processing

TOPSPIN v4.1.1 - collection, processing

NMR spectrometers:

Bruker Avance 700 MHz

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