BMRB Entry 51111

Name: The 1H, 15N, and 13C resonance assignments of the low-complexity domain from the oncogenic fusion protein EWS-FLI1
Published: 2022-02-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51111

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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: The 1H, 15N, and 13C resonance assignments of the low-complexity domain from the oncogenic fusion protein EWS-FLI1 PubMed: 34994941

Deposition date: 2021-09-29 Original release date: 2022-02-18

Authors: Johnson, Courtney; Xu, Xiaoping; Holloway, Stephen; Libich, David

Citation: Johnson, Courtney; Xu, Xiaoping; Holloway, Stephen; Libich, David. "The 1H, 15N and 13C resonance assignments of the low-complexity domain from the oncogenic fusion protein EWS-FLI1" Biomol. NMR Assignments 16, 67-73 (2022).

Assembly members:
entity_1, polymer, 121 residues, Formula weight is not available

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pAG8H-GFP

Entity Sequences (FASTA):
entity_1: GAASTDYSTYSQAAAQQGYS AYTAQPTQGYAQTTQAYGQQ SYGTYGQPTDVSYTQAQTTA TYGQTAYATSYGQPPTGYTT PTAPQAYSQPVQGYGTGAYD TTTATVTTTQASYAAQSAYG T

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	341
15N chemical shifts	109
1H chemical shifts	110

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EWSR1 1-120	1

Entities:

Entity 1, EWSR1 1-120 121 residues - Formula weight is not available

Numbering starts at 0

1

GLY

ALA

SER

THR

ASP

TYR

SER

THR

TYR

2

SER

GLN

ALA

GLN

GLY

TYR

SER

3

ALA

TYR

THR

ALA

GLN

PRO

THR

GLN

GLY

TYR

4

ALA

GLN

THR

GLN

ALA

TYR

GLY

GLN

5

SER

TYR

GLY

THR

TYR

GLY

GLN

PRO

THR

ASP

6

VAL

SER

TYR

THR

GLN

ALA

GLN

THR

ALA

7

THR

TYR

GLY

GLN

THR

ALA

TYR

ALA

THR

SER

8

TYR

GLY

GLN

PRO

THR

GLY

TYR

THR

9

PRO

THR

ALA

PRO

GLN

ALA

TYR

SER

GLN

PRO

10

VAL

GLN

GLY

TYR

GLY

THR

GLY

ALA

TYR

ASP

11

THR

ALA

THR

VAL

THR

GLN

12

ALA

SER

TYR

ALA

GLN

SER

ALA

TYR

GLY

13

THR

Samples:

sample_1: EWSR1 1-120, [U-100% 13C; U-100% 15N], 100 mM; MES 20 mM; PMSF 0.1 mM; EDTA 1 mM

sample_conditions_1: pH: 6.2; 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 HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

ANALYSIS - chemical shift assignment

TOPSPIN - collection

NMRPipe - processing

NMRDraw - processing

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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