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 30304

Title: Molecular structure of FUS low sequence complexity domain protein fibrils   PubMed: 28942918

Deposition date: 2017-06-08 Original release date: 2017-09-15

Authors: Murray, D.; Kato, M.; Lin, Y.; Thurber, K.; Hung, I.; McKnight, S.; Tycko, R.

Citation: Murray, D.; Kato, M.; Lin, Y.; Thurber, K.; Hung, I.; McKnight, S.; Tycko, R.. "Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains"  Cell 171, 615-627 (2017).

Assembly members:
RNA-binding protein FUS, polymer, 61 residues, 6290.144 Da.

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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
RNA-binding protein FUS: SYSGYSQSTDTSGYGQSSYS SYGQSQNTGYGTQSTPQGYG STGGYGSSQSSQSSYGQQSS Y

Data sets:
Data typeCount
13C chemical shifts173
15N chemical shifts45

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, chain 11
2entity_1, chain 21
3entity_1, chain 31
4entity_1, chain 41
5entity_1, chain 51
6entity_1, chain 61
7entity_1, chain 71
8entity_1, chain 81
9entity_1, chain 91

Entities:

Entity 1, entity_1, chain 1 61 residues - 6290.144 Da.

1   SERTYRSERGLYTYRSERGLNSERTHRASP
2   THRSERGLYTYRGLYGLNSERSERTYRSER
3   SERTYRGLYGLNSERGLNASNTHRGLYTYR
4   GLYTHRGLNSERTHRPROGLNGLYTYRGLY
5   SERTHRGLYGLYTYRGLYSERSERGLNSER
6   SERGLNSERSERTYRGLYGLNGLNSERSER
7   TYR

Samples:

sample_1: FUS-LC Fibril, [U-99% 13C; U-99% 15N], 0.28 ± 0.03 mg/uL; soduim phosphate 20 mM

sample_2: FUS-LC Fibril, 99% 15N, 99% 2-13C Glycerol, 0.28 ± 0.03 mg/uL; soduim phosphate 20 mM

sample_3: FUS-LC Fibril, 99% 15N, 99% 1,3-13C Glycerol, 0.28 ± 0.03 mg/uL; soduim phosphate 20 mM

sample_4: FUS-LC Fibril, 99% 1-13C Tyrosine, 0.23 ± 0.03 mg/uL; soduim phosphate 20 mM

sample_5: FUS-LC Fibril, 99% 1-13C Threonine, 0.23 ± 0.03 mg/uL; soduim phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D NCACXsample_1isotropicsample_conditions_1
3D NCOCXsample_1isotropicsample_conditions_1
3D CONCAsample_1isotropicsample_conditions_1
3D CANCXsample_1isotropicsample_conditions_1
13C-13C PITHIRDS-CTsample_4isotropicsample_conditions_1
13C-13C PITHIRDS-CTsample_5isotropicsample_conditions_1
15N-15N BAREsample_1isotropicsample_conditions_1
15N-15N BAREsample_2isotropicsample_conditions_1
13C-13C DARRsample_2isotropicsample_conditions_1
13C-13C DARRsample_3isotropicsample_conditions_1
3D NCACXsample_2isotropicsample_conditions_1
3D NCOCXsample_3isotropicsample_conditions_1

Software:

MCASSIGN v2B, Kan-Nian Hu, Wei Qiang, and Robert Tycko - chemical shift assignment

NMRPipe v8.9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

X-PLOR NIH v2.45, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker AvanceIII 895.1 MHz
  • Varian Infinity 746.1 MHz
  • Varian InfinityPlus 599.2 MHz
  • Bruker AvanceIII 400.6 MHz