BMRB Entry 50325

Name: Backbone chemical shift assignment of the FRB domain of mTOR
Published: 2021-08-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50325

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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 FRB domain of mTOR

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, 104 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: pOPTG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMELIRVAILWHEMWHEG LEEASRLYFGERNVKGMFEV LEPLHAMMERGPQTLKETSF NQAYGRDLMEAQEWCRKYMK SGNVKDLTQAWDLYYHVFRR ISKQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	294
15N chemical shifts	93
1H chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

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

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

HIS

VAL

PHE

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