BMRB Entry 50325
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50325
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Title: Backbone chemical shift assignment of the FRB domain of mTOR PubMed: 34519269
Deposition date: 2020-06-12 Original release date: 2021-08-20
Authors: Heimhalt, Maren; Berndt, Alex; Wagstaff, Jane; Perisic, Olga; Maslen, Sarah; Yu, Conny Wing-Heng; Anandapadamanaban, Madhangopal; Masson, Glenn; Boland, Andreas; Johnson, Christopher; McLaughlin, Stephen; Skehel, Mark; Freund, Stefan; Williams, Roger
Citation: Heimhalt, Maren; Berndt, Alex; Wagstaff, Jane; Anandapadamanaban, Madhangopal; Perisic, Olga; Maslen, Sarah; McLaughlin, Stephen; Yu, Conny Wing-Heng; Masson, Glenn; Boland, Andreas; Ni, Xiaodan; Yamashita, Keitaro; Murshudov, Garib; Skehel, Mark; Freund, Stefan; Williams, Roger. "Bipartite binding and partial inhibition links DEPTOR and mTOR in a mutually antagonistic embrace" Elife 10, e68799-e68799 (2021).
Assembly members:
entity_1, polymer, 104 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 Vector: pOPTG
Entity Sequences (FASTA):
entity_1: GSHMELIRVAILWHEMWHEG
LEEASRLYFGERNVKGMFEV
LEPLHAMMERGPQTLKETSF
NQAYGRDLMEAQEWCRKYMK
SGNVKDLTQAWDLYYHVFRR
ISKQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 294 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mTOR-FRB | 1 |
Entities:
Entity 1, mTOR-FRB 104 residues - Formula weight is not available
This construct contains a cloning scar at the N-terminus (GSHM) the construct covers residues 2015 to 2114 of the published DEPTOR sequence.
| 1 | GLY | SER | HIS | MET | GLU | LEU | ILE | ARG | VAL | ALA | ||||
| 2 | ILE | LEU | TRP | HIS | GLU | MET | TRP | HIS | GLU | GLY | ||||
| 3 | LEU | GLU | GLU | ALA | SER | ARG | LEU | TYR | PHE | GLY | ||||
| 4 | GLU | ARG | ASN | VAL | LYS | GLY | MET | PHE | GLU | VAL | ||||
| 5 | LEU | GLU | PRO | LEU | HIS | ALA | MET | MET | GLU | ARG | ||||
| 6 | GLY | PRO | GLN | THR | LEU | LYS | GLU | THR | SER | PHE | ||||
| 7 | ASN | GLN | ALA | TYR | GLY | ARG | ASP | LEU | MET | GLU | ||||
| 8 | ALA | GLN | GLU | TRP | CYS | ARG | LYS | TYR | MET | LYS | ||||
| 9 | SER | GLY | ASN | VAL | LYS | ASP | LEU | THR | GLN | ALA | ||||
| 10 | TRP | ASP | LEU | TYR | TYR | HIS | VAL | PHE | ARG | ARG | ||||
| 11 | ILE | SER | LYS | GLN |
Samples:
sample_1: FRB domain of mTOR, [U-98% 13C; U-98% 15N], 70 uM; D2O 5% v/v; HEPES 50 mM; NaCl 200 mM
sample_conditions_1: pH: 8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 115N-1H BEST-TROSY | 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 |
Software:
TOPSPIN v3.6.0 - collection, processing
qMDD v3.2 - processing NUS data by compressed sensing
NMRFAM-SPARKY - chemical shift assignment, data analysis
MARS - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts