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 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
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