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 27887

Title: Backbone (1H and 15N) Chemical Shift Assignments and Relaxation Parameters for the low complexity domain of FUS in the condensed phase   PubMed: 31270472

Authors: Murthy, Anastasia; Burke, Kathleen; Fawzi, Nicolas

Citation: Murthy, Anastasia; Dignon, Gregory; Kan, Yelena; Zerze, Gul; Parekh, Sapun; Mittal, Jeetain; Fawzi, Nicolas. "Molecular interactions underlying liquid-liquid phase separation of the FUS low complexity domain"  Nat. Struct. Mol. Biol. 26, 637-648 (2019).

Assembly members:
FUS_1-163, polymer, 163 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
FUS_1-163: MASNDYTQQATQSYGAYPTQ PGQGYSQQSSQPYGQQSYSG YSQSTDTSGYGQSSYSSYGQ SQNTGYGTQSTPQGYGSTGG YGSSQSSQSSYGQQSSYPGY GQQPAPSSTSGSYGSSSQSS SYGQPQSGSYSQQPSYGGQQ QSYGQQQSYNPPQGYGQQNQ YNS

Data sets:
Data typeCount
15N chemical shifts145
T1 relaxation values35
T2 relaxation values43
heteronuclear NOE values35

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1FUS 1-1631

Entities:

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

The protein sequence starts from alanine 2 due to cleavage of the n-terminal methionine.

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: Condensed FUS 1-163, [U-99% 15N], 27.8 mM; MES 50 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
hsqct2etf3gpsitc3dsample_1isotropicsample_conditions_1
hsqct1etf3gpsitc3dsample_1isotropicsample_conditions_1
hsqcnoef3gpsisample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links: