BMRB Entry 51112

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51112

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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, 110 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-Sumo

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AQGYGTGAYDTTTATVTTTQ ASYAAQSAYGTQPAYPAYGQ QPAATAPTRPQDGNKPTETS QPQSSTGGYNQPSLGYGQSN YSYPQVPGSYPMQPVTAPPS YPPTSYSSTQ

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts92
1H chemical shifts92

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EWSR1 91-1991

Entities:

Entity 1, EWSR1 91-199 110 residues - Formula weight is not available

1   ALAGLNGLYTYRGLYTHRGLYALATYRASP
2   THRTHRTHRALATHRVALTHRTHRTHRGLN
3   ALASERTYRALAALAGLNSERALATYRGLY
4   THRGLNPROALATYRPROALATYRGLYGLN
5   GLNPROALAALATHRALAPROTHRARGPRO
6   GLNASPGLYASNLYSPROTHRGLUTHRSER
7   GLNPROGLNSERSERTHRGLYGLYTYRASN
8   GLNPROSERLEUGLYTYRGLYGLNSERASN
9   TYRSERTYRPROGLNVALPROGLYSERTYR
10   PROMETGLNPROVALTHRALAPROPROSER
11   TYRPROPROTHRSERTYRSERSERTHRGLN

Samples:

sample_1: EWSR1 91-199, [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