BMRB Entry 50326

Title:
Backbone chemical shift assignment of the linker region of DEPTOR
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:

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).
PubMed: 34519269

Assembly members:

Assembly members:
entity_1, polymer, 99 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pOPTH

Data sets:
Data typeCount
13C chemical shifts285
15N chemical shifts94
1H chemical shifts84

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1DEPTOR Linker1

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   GLYSERHISMETGLULEULEUASNGLULYS
2   SERPROSERSERGLNGLUTHRHISASPSER
3   PROPHECYSLEUARGLYSGLNSERHISASP
4   ASNARGLYSSERTHRSERPHEMETSERVAL
5   SERPROSERLYSGLUILELYSILEVALSER
6   ALAVALARGARGSERSERMETSERSERCYS
7   GLYSERSERGLYTYRPHESERSERSERPRO
8   THRLEUSERSERSERPROPROVALLEUCYS
9   ASNPROLYSSERVALLEULYSARGPROVAL
10   THRSERGLUGLULEULEUTHRPROGLY

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:

NameSampleSample stateSample conditions
115N-1H BEST-TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOCANNHsample_1isotropicsample_conditions_1
3D HNCANNHsample_1isotropicsample_conditions_1
3D c_hcaconsample_1isotropicsample_conditions_1
3D c_hcancosample_1isotropicsample_conditions_1
3D c_cbcaconsample_1isotropicsample_conditions_1
3D cbcancosample_1isotropicsample_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

Related Database Links:

UniprotKB Q8TB45

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks