BMRB Entry 27931
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27931
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Title: Unfolded ZnF in FUS (371-526) prion-like domain PubMed: 31188823
Deposition date: 2019-05-29 Original release date: 2020-09-28
Authors: Song, Jianxing; Lim, Liang Zhong
Citation: Kang, Jian; Lim, Liangzhong; Lu, Yimei; Song, Jianxing. "A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acids" PLoS Biol. 17, e3000327-e3000327 (2019).
Assembly members:
Unfolded_FUS_(371-526), polymer, 164 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
Unfolded_FUS_(371-526): RRADFNRGGGNGRGGRGRGG
PMGRGGYGGGGSGGGGRGGF
PSGGGGGGGQQRAGDWKCPN
PTCENMNFSWRNECNQCKAP
KPDGPGGGPGGSHMGGNYGD
DRRGGRGGYDRGGYRGRGGD
RGGFRGGRGGGDRGGFGPGK
MDSRGEHRQDRRERPYLEHH
HHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 223 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 268 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FUS (371-526) | 1 |
Entities:
Entity 1, FUS (371-526) 164 residues - Formula weight is not available
| 1 | ARG | ARG | ALA | ASP | PHE | ASN | ARG | GLY | GLY | GLY | ||||
| 2 | ASN | GLY | ARG | GLY | GLY | ARG | GLY | ARG | GLY | GLY | ||||
| 3 | PRO | MET | GLY | ARG | GLY | GLY | TYR | GLY | GLY | GLY | ||||
| 4 | GLY | SER | GLY | GLY | GLY | GLY | ARG | GLY | GLY | PHE | ||||
| 5 | PRO | SER | GLY | GLY | GLY | GLY | GLY | GLY | GLY | GLN | ||||
| 6 | GLN | ARG | ALA | GLY | ASP | TRP | LYS | CYS | PRO | ASN | ||||
| 7 | PRO | THR | CYS | GLU | ASN | MET | ASN | PHE | SER | TRP | ||||
| 8 | ARG | ASN | GLU | CYS | ASN | GLN | CYS | LYS | ALA | PRO | ||||
| 9 | LYS | PRO | ASP | GLY | PRO | GLY | GLY | GLY | PRO | GLY | ||||
| 10 | GLY | SER | HIS | MET | GLY | GLY | ASN | TYR | GLY | ASP | ||||
| 11 | ASP | ARG | ARG | GLY | GLY | ARG | GLY | GLY | TYR | ASP | ||||
| 12 | ARG | GLY | GLY | TYR | ARG | GLY | ARG | GLY | GLY | ASP | ||||
| 13 | ARG | GLY | GLY | PHE | ARG | GLY | GLY | ARG | GLY | GLY | ||||
| 14 | GLY | ASP | ARG | GLY | GLY | PHE | GLY | PRO | GLY | LYS | ||||
| 15 | MET | ASP | SER | ARG | GLY | GLU | HIS | ARG | GLN | ASP | ||||
| 16 | ARG | ARG | GLU | ARG | PRO | TYR | LEU | GLU | HIS | HIS | ||||
| 17 | HIS | HIS | HIS | HIS |
Samples:
sample_1: Unfolded FUS (371-526), [U-100% 13C; U-100% 15N], 500 uM; sodium phosphate 5 mM
sample_conditions_1: ionic strength: 10 mM; pH: 6; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, CCPN - chemical shift assignment, processing
NMR spectrometers:
- Bruker AMX 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts