BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51114

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51114

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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, 265 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-His

Entity Sequences (FASTA):
entity_1: GAASTDYSTYSQAAAQQGYS AYTAQPTQGYAQTTQAYGQQ SYGTYGQPTDVSYTQAQTTA TYGQTAYATSYGQPPTGYTT PTAPQAYSQPVQGYGTGAYD TTTATVTTTQASYAAQSAYG TQPAYPAYGQQPAATAPTRP QDGNKPTETSQPQSSTGGYN QPSLGYGQSNYSYPQVPGSY PMQPVTAPPSYPPTSYSSTQ PTSYDQSSYSQQNTYGQPSS YGQQSSYGQQSSYGQQPPTS YPPQTGSYSQAPSQYSQQSS SYGQQ

Data sets:
Data typeCount
13C chemical shifts839
15N chemical shifts244
1H chemical shifts440

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EWSR1 1-2641

Entities:

Entity 1, EWSR1 1-264 265 residues - Formula weight is not available

Numbering starts at 0

1   GLYALAALASERTHRASPTYRSERTHRTYR
2   SERGLNALAALAALAGLNGLNGLYTYRSER
3   ALATYRTHRALAGLNPROTHRGLNGLYTYR
4   ALAGLNTHRTHRGLNALATYRGLYGLNGLN
5   SERTYRGLYTHRTYRGLYGLNPROTHRASP
6   VALSERTYRTHRGLNALAGLNTHRTHRALA
7   THRTYRGLYGLNTHRALATYRALATHRSER
8   TYRGLYGLNPROPROTHRGLYTYRTHRTHR
9   PROTHRALAPROGLNALATYRSERGLNPRO
10   VALGLNGLYTYRGLYTHRGLYALATYRASP
11   THRTHRTHRALATHRVALTHRTHRTHRGLN
12   ALASERTYRALAALAGLNSERALATYRGLY
13   THRGLNPROALATYRPROALATYRGLYGLN
14   GLNPROALAALATHRALAPROTHRARGPRO
15   GLNASPGLYASNLYSPROTHRGLUTHRSER
16   GLNPROGLNSERSERTHRGLYGLYTYRASN
17   GLNPROSERLEUGLYTYRGLYGLNSERASN
18   TYRSERTYRPROGLNVALPROGLYSERTYR
19   PROMETGLNPROVALTHRALAPROPROSER
20   TYRPROPROTHRSERTYRSERSERTHRGLN
21   PROTHRSERTYRASPGLNSERSERTYRSER
22   GLNGLNASNTHRTYRGLYGLNPROSERSER
23   TYRGLYGLNGLNSERSERTYRGLYGLNGLN
24   SERSERTYRGLYGLNGLNPROPROTHRSER
25   TYRPROPROGLNTHRGLYSERTYRSERGLN
26   ALAPROSERGLNTYRSERGLNGLNSERSER
27   SERTYRGLYGLNGLN

Samples:

sample_1: EWSR1 1-264, [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