BMRB Entry 50324
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50324
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Title: Assigned backbone chemical shifts of DEPTOR-PDZ 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, 90 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: pOPTL
Entity Sequences (FASTA):
entity_1: GSHMAPYARKTFTIVGDAVG
WGFVVRGSKPCHIQAVDPSG
PAAAAGMKVCQFVVSVNGLN
VLHVDYRTVNNLILTGPRTI
VMEVMEELEC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 251 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 80 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DEPTOR-PDZ | 1 |
Entities:
Entity 1, DEPTOR-PDZ 90 residues - Formula weight is not available
This construct contains a cloning scar at the N-terminus (GSHM) the construct covers residues 324 to 409 of the published DEPTOR sequence.
| 1 | GLY | SER | HIS | MET | ALA | PRO | TYR | ALA | ARG | LYS | |
| 2 | THR | PHE | THR | ILE | VAL | GLY | ASP | ALA | VAL | GLY | |
| 3 | TRP | GLY | PHE | VAL | VAL | ARG | GLY | SER | LYS | PRO | |
| 4 | CYS | HIS | ILE | GLN | ALA | VAL | ASP | PRO | SER | GLY | |
| 5 | PRO | ALA | ALA | ALA | ALA | GLY | MET | LYS | VAL | CYS | |
| 6 | GLN | PHE | VAL | VAL | SER | VAL | ASN | GLY | LEU | ASN | |
| 7 | VAL | LEU | HIS | VAL | ASP | TYR | ARG | THR | VAL | ASN | |
| 8 | ASN | LEU | ILE | LEU | THR | GLY | PRO | ARG | THR | ILE | |
| 9 | VAL | MET | GLU | VAL | MET | GLU | GLU | LEU | GLU | CYS |
Samples:
sample_1: DEPTOR-PDZ, [U-98% 13C; U-98% 15N], 190 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 |
Software:
TOPSPIN v3.6.0 - collection, processing
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