BMRB Entry 26672
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26672
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: Backbone 1H, 13C (C, CA, CB), and 15N Chemical Shift Assignments for the low complexity prion-like domain of Fused in Sarcoma (FUS 1-163) PubMed: 26455390
Deposition date: 2015-09-23 Original release date: 2015-10-09
Authors: Burke, Kathleen; Fawzi, Nicolas
Citation: Burke, Kathleen; Janke, Abigail; Rhine, Christy; Fawzi, Nicolas. "Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II" Mol. Cell 60, 231-241 (2015).
Assembly members:
Fused_in_Sarcoma_Low_Complesity_Domain, polymer, 163 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
Entity Sequences (FASTA):
Fused_in_Sarcoma_Low_Complesity_Domain: MASNDYTQQATQSYGAYPTQ
PGQGYSQQSSQPYGQQSYSG
YSQSTDTSGYGQSSYSSYGQ
SQNTGYGTQSTPQGYGSTGG
YGSSQSSQSSYGQQSSYPGY
GQQPAPSSTSGSYGSSSQSS
SYGQPQSGSYSQQPSYGGQQ
QSYGQQQSYNPPQGYGQQNQ
YNS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 408 |
15N chemical shifts | 145 |
1H chemical shifts | 145 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | FUS LC monomer | 1 |
Entities:
Entity 1, FUS LC monomer 163 residues - Formula weight is not available
This is the N-terminal low complexity domain of FUS known as SYGQ-rich, QGSY-rich, or prion-like domain
1 | MET | ALA | SER | ASN | ASP | TYR | THR | GLN | GLN | ALA | ||||
2 | THR | GLN | SER | TYR | GLY | ALA | TYR | PRO | THR | GLN | ||||
3 | PRO | GLY | GLN | GLY | TYR | SER | GLN | GLN | SER | SER | ||||
4 | GLN | PRO | TYR | GLY | GLN | GLN | SER | TYR | SER | GLY | ||||
5 | TYR | SER | GLN | SER | THR | ASP | THR | SER | GLY | TYR | ||||
6 | GLY | GLN | SER | SER | TYR | SER | SER | TYR | GLY | GLN | ||||
7 | SER | GLN | ASN | THR | GLY | TYR | GLY | THR | GLN | SER | ||||
8 | THR | PRO | GLN | GLY | TYR | GLY | SER | THR | GLY | GLY | ||||
9 | TYR | GLY | SER | SER | GLN | SER | SER | GLN | SER | SER | ||||
10 | TYR | GLY | GLN | GLN | SER | SER | TYR | PRO | GLY | TYR | ||||
11 | GLY | GLN | GLN | PRO | ALA | PRO | SER | SER | THR | SER | ||||
12 | GLY | SER | TYR | GLY | SER | SER | SER | GLN | SER | SER | ||||
13 | SER | TYR | GLY | GLN | PRO | GLN | SER | GLY | SER | TYR | ||||
14 | SER | GLN | GLN | PRO | SER | TYR | GLY | GLY | GLN | GLN | ||||
15 | GLN | SER | TYR | GLY | GLN | GLN | GLN | SER | TYR | ASN | ||||
16 | PRO | PRO | GLN | GLY | TYR | GLY | GLN | GLN | ASN | GLN | ||||
17 | TYR | ASN | SER |
Samples:
sample_1: Fused in Sarcoma Low Complesity Domain, [U-99% 13C; U-99% 15N], 50 uM; D2O, [U-99% 2H], 10%; H2O 90%; MES 20 mM; CAPS 0.2 mM
sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D (H)N(CA)NNH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN v3.2, Bruker Biospin - collection
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance III HD 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts