BMRB Entry 50326
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50326
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Title: Backbone chemical shift assignment of the linker region of DEPTOR 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, 99 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: pOPTH
Entity Sequences (FASTA):
entity_1: GSHMELLNEKSPSSQETHDS
PFCLRKQSHDNRKSTSFMSV
SPSKEIKIVSAVRRSSMSSC
GSSGYFSSSPTLSSSPPVLC
NPKSVLKRPVTSEELLTPG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 285 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 84 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DEPTOR Linker | 1 |
Entities:
Entity 1, DEPTOR Linker 99 residues - Formula weight is not available
This construct contains a cloning scar at the N-terminus (GSH) the construct covers residues 228 to 323 of the published DEPTOR sequence.
| 1 | GLY | SER | HIS | MET | GLU | LEU | LEU | ASN | GLU | LYS | ||||
| 2 | SER | PRO | SER | SER | GLN | GLU | THR | HIS | ASP | SER | ||||
| 3 | PRO | PHE | CYS | LEU | ARG | LYS | GLN | SER | HIS | ASP | ||||
| 4 | ASN | ARG | LYS | SER | THR | SER | PHE | MET | SER | VAL | ||||
| 5 | SER | PRO | SER | LYS | GLU | ILE | LYS | ILE | VAL | SER | ||||
| 6 | ALA | VAL | ARG | ARG | SER | SER | MET | SER | SER | CYS | ||||
| 7 | GLY | SER | SER | GLY | TYR | PHE | SER | SER | SER | PRO | ||||
| 8 | THR | LEU | SER | SER | SER | PRO | PRO | VAL | LEU | CYS | ||||
| 9 | ASN | PRO | LYS | SER | VAL | LEU | LYS | ARG | PRO | VAL | ||||
| 10 | THR | SER | GLU | GLU | LEU | LEU | THR | PRO | GLY |
Samples:
sample_1: DEPTOR Linker, [U-98% 13C; U-98% 15N], 140 uM; D2O 5% v/v; HEPES 50 mM; NaCl 200 mM
sample_conditions_1: pH: 8; pressure: 1 atm; temperature: 278 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 |
| 3D HNCOCANNH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCANNH | sample_1 | isotropic | sample_conditions_1 |
| 3D c_hcacon | sample_1 | isotropic | sample_conditions_1 |
| 3D c_hcanco | sample_1 | isotropic | sample_conditions_1 |
| 3D c_cbcacon | sample_1 | isotropic | sample_conditions_1 |
| 3D cbcanco | 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 II+ 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts