BMRB Entry 52063

Name: A conformational switch in the c-MYC transactivation domain
Published: 2024-09-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52063

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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:

A conformational switch in the c-MYC transactivation domain

Deposition date:

2023-07-30

Original release date:

2024-09-10

Authors:

Lama, Dilraj; Vosselman, Thilbault; Sahin, Carla; Liano-Pons, Judit; Cerrato, Carmine; Nilsson, Lennart; Teilum, Kaare; Lane, David P.; Landreh, Michael; Arsenian-Henriksson, Marie

Citation:

Citation: Lama, Dilraj; Vosselman, Thilbault; Sahin, Carla; Liano-Pons, Judit; Cerrato, Carmine; Nilsson, Lennart; Teilum, Kaare; Lane, David P.; Landreh, Michael; Arsenian-Henriksson, Marie. "A druggable conformational switch in the c-MYC transactivation domain" Nat. Commun. 15, 1865-1865 (2024).
PubMed: 38424045

Assembly members:

Assembly members:
entity_1, polymer, 58 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: pET-26b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGHHHHHHMVTELLGGDMVN QSFICDPDDETFIKNIIIQD CMWSGFSAAAKLVSEKLA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	144
15N chemical shifts	50
1H chemical shifts	50

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cMYC	1

Entities:

Entity 1, cMYC 58 residues - Formula weight is not available

1

MET

GLY

HIS

MET

VAL

2

THR

GLU

LEU

GLY

ASP

MET

VAL

ASN

3

GLN

SER

PHE

ILE

CYS

ASP

PRO

ASP

GLU

4

THR

PHE

ILE

LYS

ASN

ILE

GLN

ASP

5

CYS

MET

TRP

SER

GLY

PHE

SER

ALA

6

LYS

LEU

VAL

SER

GLU

LYS

LEU

ALA

Samples:

sample_1: cMYC, [U-100% 13C; U-100% 15N], 85 uM; HEPES 10 mM; TCEP 2 mM; D2O 5%; sodium azide 0.01%; DSS 0.25 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.5; pressure: 1 atm; temperature: 280 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

qMDD - processing

NMRPipe - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE IIIHD 750 MHz

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