BMRB Entry 51113

Title:
The 1H, 15N, and 13C resonance assignments of the low-complexity domain from the oncogenic fusion protein EWS-FLI1
Deposition date:
2021-09-29
Original release date:
2022-02-18
Authors:
Johnson, Courtney; Xu, Xiaoping; Holloway, Stephen; Libich, David
Citation:

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).
PubMed: 34994941

Assembly members:

Assembly members:
entity_1, polymer, 94 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pAG8H-GB1

Data sets:
Data typeCount
13C chemical shifts262
15N chemical shifts78
1H chemical shifts78

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1EWSR1 171-2641

Entities:

Entity 1, EWSR1 171-264 94 residues - Formula weight is not available

1   THRTYRPROGLNVALPROGLYSERTYRPRO
2   METGLNPROVALTHRALAPROPROSERTYR
3   PROPROTHRSERTYRSERSERTHRGLNPRO
4   THRSERTYRASPGLNSERSERTYRSERGLN
5   GLNASNTHRTYRGLYGLNPROSERSERTYR
6   GLYGLNGLNSERSERTYRGLYGLNGLNSER
7   SERTYRGLYGLNGLNPROPROTHRSERTYR
8   PROPROGLNTHRGLYSERTYRSERGLNALA
9   PROSERGLNTYRSERGLNGLNSERSERSER
10   TYRGLYGLNGLN

Samples:

sample_1: EWSR1 171-264, [U-100% 13C; U-100% 15N], 100 uM; MES 20 mM; PMSF 0.1 mM; EDTA 1 mM

sample_conditions_1: pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_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 peaks
SPARKY: Backbone or all simulated peaks