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 27125

Title: FUS low complexity domain with 12 phosphomimetic S/T to E mutations   PubMed: 28790177

Deposition date: 2017-06-05 Original release date: 2017-08-02

Authors: Ryan, Veronica; Fawzi, Nicolas; Burke, Kathleen

Citation: Monahan, Zachary; Ryan, Veronica; Janke, Abigail; Burke, Kathleen; Rhoads, Shannon; Zerze, Gul; O'Meally, Robert; Dignon, Gregory; Conicella, Alexander; Zheng, Wenwei; Best, Robert; Cole, Robert; Mittal, Jeetain; Shewmaker, Frank; Fawzi, Nicolas. "Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity"  EMBO J. 36, 2951-2967 (2017).

Assembly members:
FUS_12E_LC, polymer, 164 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   Vector: MBP-FUS_LC_12E_pTHMT

Entity Sequences (FASTA):
FUS_12E_LC: GMASNDYEQQAEQSYGAYPE QPGQGYEQQSEQPYGQQSYS GYEQSTDTSGYGQSSYSSYG QEQNTGYGEQSTPQGYGSTG GYGSEQSEQSSYGQQSSYPG YGQQPAPSSTSGSYGSSEQS SSYGQPQSGSYEQQPSYGGQ QQSYGQQQSYNPPQGYGQQN QYNS

Data sets:
Data typeCount
13C chemical shifts423
15N chemical shifts151
1H chemical shifts151

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FUS 12E LC1

Entities:

Entity 1, FUS 12E LC 164 residues - Formula weight is not available

Residue 1 is cleavage artifact, reside 2 is residue 1 in FUS

1   GLYMETALASERASNASPTYRGLUGLNGLN
2   ALAGLUGLNSERTYRGLYALATYRPROGLU
3   GLNPROGLYGLNGLYTYRGLUGLNGLNSER
4   GLUGLNPROTYRGLYGLNGLNSERTYRSER
5   GLYTYRGLUGLNSERTHRASPTHRSERGLY
6   TYRGLYGLNSERSERTYRSERSERTYRGLY
7   GLNGLUGLNASNTHRGLYTYRGLYGLUGLN
8   SERTHRPROGLNGLYTYRGLYSERTHRGLY
9   GLYTYRGLYSERGLUGLNSERGLUGLNSER
10   SERTYRGLYGLNGLNSERSERTYRPROGLY
11   TYRGLYGLNGLNPROALAPROSERSERTHR
12   SERGLYSERTYRGLYSERSERGLUGLNSER
13   SERSERTYRGLYGLNPROGLNSERGLYSER
14   TYRGLUGLNGLNPROSERTYRGLYGLYGLN
15   GLNGLNSERTYRGLYGLNGLNGLNSERTYR
16   ASNPROPROGLNGLYTYRGLYGLNGLNASN
17   GLNTYRASNSER

Samples:

sample_1: FUS 12E LC, [U-99% 13C; U-99% 15N], 100 uM; D2O, [U-2H], 10%; MES 50 mM; Bis Tris 1 mM; H2O 90%

sample_conditions_1: ionic strength: 0 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HN(CAN)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

CARA, Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts