BMRB Entry 30304
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30304
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 173 |
| 15N chemical shifts | 45 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1, chain 1 | 1 |
| 2 | entity_1, chain 2 | 1 |
| 3 | entity_1, chain 3 | 1 |
| 4 | entity_1, chain 4 | 1 |
| 5 | entity_1, chain 5 | 1 |
| 6 | entity_1, chain 6 | 1 |
| 7 | entity_1, chain 7 | 1 |
| 8 | entity_1, chain 8 | 1 |
| 9 | entity_1, chain 9 | 1 |
Entities:
Entity 1, entity_1, chain 1 61 residues - 6290.144 Da.
| 1 | SER | TYR | SER | GLY | TYR | SER | GLN | SER | THR | ASP | ||||
| 2 | THR | SER | GLY | TYR | GLY | GLN | SER | SER | TYR | SER | ||||
| 3 | SER | TYR | GLY | GLN | SER | GLN | ASN | THR | GLY | TYR | ||||
| 4 | GLY | THR | GLN | SER | THR | PRO | GLN | GLY | TYR | GLY | ||||
| 5 | SER | THR | GLY | GLY | TYR | GLY | SER | SER | GLN | SER | ||||
| 6 | SER | GLN | SER | SER | TYR | GLY | GLN | GLN | SER | SER | ||||
| 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D NCACX | sample_1 | isotropic | sample_conditions_1 |
| 3D NCOCX | sample_1 | isotropic | sample_conditions_1 |
| 3D CONCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CANCX | sample_1 | isotropic | sample_conditions_1 |
| 13C-13C PITHIRDS-CT | sample_4 | isotropic | sample_conditions_1 |
| 13C-13C PITHIRDS-CT | sample_5 | isotropic | sample_conditions_1 |
| 15N-15N BARE | sample_1 | isotropic | sample_conditions_1 |
| 15N-15N BARE | sample_2 | isotropic | sample_conditions_1 |
| 13C-13C DARR | sample_2 | isotropic | sample_conditions_1 |
| 13C-13C DARR | sample_3 | isotropic | sample_conditions_1 |
| 3D NCACX | sample_2 | isotropic | sample_conditions_1 |
| 3D NCOCX | sample_3 | isotropic | sample_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