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 50026

Title: 2H,15N,13C-labeled FUS-LC fibrils   PubMed: 31895552

Deposition date: 2019-10-01 Original release date: 2020-09-21

Authors: Murray, Dylan; Tycko, Robert

Citation: Murray, Dylan; Tycko, Robert. "Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy"  Biochemistry 59, 364-378 (2020).

Assembly members:
entity_1, polymer, 243 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: pHis

Entity Sequences (FASTA):
entity_1: MSYYHHHHHHDYDIPTTENL YFQGAMDPASNDYTQQATQS YGAYPTQPGQGYSQQSSQPY GQQSYSGYSQSTDTSGYGQS SYSSYGQSTSQNTGYGTQST PQGYGSTGGYGSSQSSQSSY GQQSSYPGYGQQPAPSSTSG SYGSSSQSSSYGQPQSGSYS QQPSYGGQQQSYGQQQSYNP PQGYGQQNQYNSSSGGGGGG GGGGNYGQDQSSMSSGGGSG GGYGNQDQSGGGGSGGYGQQ DRG

Data sets:
Data typeCount
13C chemical shifts136
15N chemical shifts53
1H chemical shifts52

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FUS-LC fibril1

Entities:

Entity 1, FUS-LC fibril 243 residues - Formula weight is not available

1   METSERTYRTYRHISHISHISHISHISHIS
2   ASPTYRASPILEPROTHRTHRGLUASNLEU
3   TYRPHEGLNGLYALAMETASPPROALASER
4   ASNASPTYRTHRGLNGLNALATHRGLNSER
5   TYRGLYALATYRPROTHRGLNPROGLYGLN
6   GLYTYRSERGLNGLNSERSERGLNPROTYR
7   GLYGLNGLNSERTYRSERGLYTYRSERGLN
8   SERTHRASPTHRSERGLYTYRGLYGLNSER
9   SERTYRSERSERTYRGLYGLNSERTHRSER
10   GLNASNTHRGLYTYRGLYTHRGLNSERTHR
11   PROGLNGLYTYRGLYSERTHRGLYGLYTYR
12   GLYSERSERGLNSERSERGLNSERSERTYR
13   GLYGLNGLNSERSERTYRPROGLYTYRGLY
14   GLNGLNPROALAPROSERSERTHRSERGLY
15   SERTYRGLYSERSERSERGLNSERSERSER
16   TYRGLYGLNPROGLNSERGLYSERTYRSER
17   GLNGLNPROSERTYRGLYGLYGLNGLNGLN
18   SERTYRGLYGLNGLNGLNSERTYRASNPRO
19   PROGLNGLYTYRGLYGLNGLNASNGLNTYR
20   ASNSERSERSERGLYGLYGLYGLYGLYGLY
21   GLYGLYGLYGLYASNTYRGLYGLNASPGLN
22   SERSERMETSERSERGLYGLYGLYSERGLY
23   GLYGLYTYRGLYASNGLNASPGLNSERGLY
24   GLYGLYGLYSERGLYGLYTYRGLYGLNGLN
25   ASPARGGLY

Samples:

sample_1: FUS-LC, [U-13C; U-15N; U-2H], 50 ± 10 %

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 301 K

Experiments:

NameSampleSample stateSample conditions
3D NCCsample_1fibrilssample_conditions_1
3D CANHsample_1fibrilssample_conditions_1
3D CONHsample_1fibrilssample_conditions_1
3D NHHsample_1fibrilssample_conditions_1
3D HN(CO)CXsample_1fibrilssample_conditions_1
3D CAN(H)Hsample_1fibrilssample_conditions_1
3D CON(H)Hsample_1fibrilssample_conditions_1
3D NHHsample_1fibrilssample_conditions_1
3D CANHsample_1fibrilssample_conditions_1

Software:

SPARKY, T. D. Goddard and D. G. Kneller - peak picking

NMR spectrometers:

  • Varian InfinityPlus 600 MHz
  • Varian InfinityPlus 750 MHz

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