BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 51113

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, 94 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-GB1

Entity Sequences (FASTA):
entity_1: TYPQVPGSYPMQPVTAPPSY PPTSYSSTQPTSYDQSSYSQ QNTYGQPSSYGQQSSYGQQS SYGQQPPTSYPPQTGSYSQA PSQYSQQSSSYGQQ

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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 shifts
SPARKY: Backbone or all simulated shifts