BMRB Entry 50326

Name: Backbone chemical shift assignment of the linker region of DEPTOR
Published: 2021-08-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50326

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMELLNEKSPSSQETHDS PFCLRKQSHDNRKSTSFMSV SPSKEIKIVSAVRRSSMSSC GSSGYFSSSPTLSSSPPVLC NPKSVLKRPVTSEELLTPG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	285
15N chemical shifts	94
1H chemical shifts	84

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

ASN

GLU

LYS

2

SER

PRO

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

SER

MET

SER

CYS

7

GLY

SER

GLY

TYR

PHE

SER

PRO

8

THR

LEU

SER

PRO

VAL

LEU

CYS

9

ASN

PRO

LYS

SER

VAL

LEU

LYS

ARG

PRO

VAL

10

THR

SER

GLU

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