BMRB Entry 27398
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27398
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NMR-STAR v3 text file.
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Citation: Stowell, James; Wagstaff, Jane; Hill, Chris; Yu, Minmin; McLaughlin, Stephen; Freund, Stefan; Passmore, Lori. "A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding." J. Biol. Chem. 293, 9210-9222 (2018).
PubMed: 29695507
Assembly members:
USR+YTH_domain, polymer, 207 residues, Formula weight is not available
Natural source: Common Name: fission yeast Taxonomy ID: 4896 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizosaccharomyces pombe
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 393 |
| 15N chemical shifts | 123 |
| 1H chemical shifts | 123 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | USR+YTH domain | 1 |
Entities:
Entity 1, USR+YTH domain 207 residues - Formula weight is not available
| 1 | GLY | ALA | TYR | PRO | GLU | LYS | SER | SER | TYR | LEU | ||||
| 2 | LEU | SER | ASN | SER | SER | ASN | ASP | SER | ALA | SER | ||||
| 3 | ARG | LYS | GLU | LYS | PRO | LYS | ALA | ARG | ALA | SER | ||||
| 4 | THR | PRO | PRO | PRO | LEU | ASN | PHE | SER | ARG | ALA | ||||
| 5 | SER | GLU | HIS | ARG | ASN | GLU | LYS | GLY | GLU | ARG | ||||
| 6 | ILE | SER | MET | ILE | ASN | PRO | ARG | VAL | VAL | LEU | ||||
| 7 | ASP | GLU | ASN | GLY | ILE | SER | HIS | ARG | SER | ARG | ||||
| 8 | TYR | PHE | ILE | MET | LEU | CYS | ASP | ASN | GLU | THR | ||||
| 9 | ALA | ILE | ALA | HIS | ALA | LYS | LYS | THR | SER | ILE | ||||
| 10 | TRP | ALA | VAL | LYS | LYS | ASP | SER | SER | LYS | ARG | ||||
| 11 | ILE | SER | ASP | ALA | TYR | LYS | LYS | ALA | SER | VAL | ||||
| 12 | TYR | PHE | ILE | PHE | VAL | ALA | GLN | GLN | THR | TYR | ||||
| 13 | ASN | ALA | LEU | GLY | TYR | ALA | GLN | VAL | VAL | SER | ||||
| 14 | ASP | LEU | ASN | SER | THR | GLU | LEU | PRO | PHE | TRP | ||||
| 15 | SER | ASP | SER | SER | HIS | ALA | GLY | GLY | VAL | ARG | ||||
| 16 | ILE | LYS | TRP | ILE | LYS | THR | CYS | ASN | LEU | PHE | ||||
| 17 | SER | ALA | GLU | ILE | SER | GLU | ILE | VAL | SER | HIS | ||||
| 18 | MET | ASP | HIS | GLY | SER | GLU | ALA | ARG | ASP | GLY | ||||
| 19 | MET | GLU | MET | MET | TYR | ASP | GLU | GLY | SER | ARG | ||||
| 20 | LEU | CYS | THR | LEU | ILE | ASN | TYR | ALA | ILE | MET | ||||
| 21 | LYS | ARG | ILE | GLY | ARG | ASP | ARG |
Samples:
sample_1: USR+YTH domain (APO), [U-100% 13C; U-100% 15N; U-80% 2H], 200 uM; D2O, [U-100% 2H], 5%; sodium chloride 150 mM; PIPES 20 mM
sample_conditions_1: ionic strength: 170 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 15N-1H BEST_TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D trHNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D trHNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D trHNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D trHNCOCA | sample_1 | isotropic | sample_conditions_1 |
| 3D trHNCOCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D trHNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D trHNCANNH | sample_1 | isotropic | sample_conditions_1 |
| 3D trHNCOCANNH | sample_1 | isotropic | sample_conditions_1 |
Software:
Topspin_3.1, Bruker Biospin - collection
qMDD, Kazimierczuk and Orekhov - processing
nmrPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Sparky, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks