BMRB Entry 26672

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26672

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Title:
Backbone 1H, 13C (C, CA, CB), and 15N Chemical Shift Assignments for the low complexity prion-like domain of Fused in Sarcoma (FUS 1-163)
Deposition date:
2015-09-23
Original release date:
2015-10-09
Authors:
Burke, Kathleen; Fawzi, Nicolas
Citation:

Citation: Burke, Kathleen; Janke, Abigail; Rhine, Christy; Fawzi, Nicolas. "Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II"  Mol. Cell 60, 231-241 (2015).
PubMed: 26455390

Assembly members:

Assembly members:
Fused_in_Sarcoma_Low_Complesity_Domain, polymer, 163 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fused_in_Sarcoma_Low_Complesity_Domain: MASNDYTQQATQSYGAYPTQ PGQGYSQQSSQPYGQQSYSG YSQSTDTSGYGQSSYSSYGQ SQNTGYGTQSTPQGYGSTGG YGSSQSSQSSYGQQSSYPGY GQQPAPSSTSGSYGSSSQSS SYGQPQSGSYSQQPSYGGQQ QSYGQQQSYNPPQGYGQQNQ YNS

Data sets:
Data typeCount
13C chemical shifts408
15N chemical shifts145
1H chemical shifts145

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FUS LC monomer1

Entities:

Entity 1, FUS LC monomer 163 residues - Formula weight is not available

This is the N-terminal low complexity domain of FUS known as SYGQ-rich, QGSY-rich, or prion-like domain

1   METALASERASNASPTYRTHRGLNGLNALA
2   THRGLNSERTYRGLYALATYRPROTHRGLN
3   PROGLYGLNGLYTYRSERGLNGLNSERSER
4   GLNPROTYRGLYGLNGLNSERTYRSERGLY
5   TYRSERGLNSERTHRASPTHRSERGLYTYR
6   GLYGLNSERSERTYRSERSERTYRGLYGLN
7   SERGLNASNTHRGLYTYRGLYTHRGLNSER
8   THRPROGLNGLYTYRGLYSERTHRGLYGLY
9   TYRGLYSERSERGLNSERSERGLNSERSER
10   TYRGLYGLNGLNSERSERTYRPROGLYTYR
11   GLYGLNGLNPROALAPROSERSERTHRSER
12   GLYSERTYRGLYSERSERSERGLNSERSER
13   SERTYRGLYGLNPROGLNSERGLYSERTYR
14   SERGLNGLNPROSERTYRGLYGLYGLNGLN
15   GLNSERTYRGLYGLNGLNGLNSERTYRASN
16   PROPROGLNGLYTYRGLYGLNGLNASNGLN
17   TYRASNSER

Samples:

sample_1: Fused in Sarcoma Low Complesity Domain, [U-99% 13C; U-99% 15N], 50 uM; D2O, [U-99% 2H], 10%; H2O 90%; MES 20 mM; CAPS 0.2 mM

sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D (H)N(CA)NNHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v3.2, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III HD 850 MHz

Related Database Links:

UNP P35637
AlphaFold Q9H4A8

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