BMRB Entry 12033

Name: c-MYC 353-437
Published: 2019-07-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR12033

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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:

c-MYC 353-437

Deposition date:

2019-02-27

Original release date:

2019-07-23

Authors:

Zinzalla, Giovanna

Citation:

Citation: Sammak, Susan; Hamdani, Najoua; Gorrec, Fabrice; Allen, Mark D; Freund, Stefan M V; Bycroft, Mark; Zinzalla, Giovanna. "Crystal Structures and Nuclear Magnetic Resonance Studies of the Apo Form of the c-MYC:MAX bHLHZip Complex Reveal a Helical Basic Region in the Absence of DNA." Biochemistry ., .-. (2019).
PubMed: 31260268

Assembly members:

Assembly members:
c-MYC, polymer, 106 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: pRSETA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
c-MYC: MGSSHHHHHHSSGLVPRGSH MNVKRRTHNVLERQRRNELK RSFFALRDQIPELENNEKAP KVVILKKATAYILSVQAEEQ KLISEEDLLRKRREQLKHKL EQLRNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	175
15N chemical shifts	54
1H chemical shifts	54

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	c-MYC	1

Entities:

Entity 1, c-MYC 106 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ASN

VAL

LYS

ARG

THR

HIS

ASN

VAL

4

LEU

GLU

ARG

GLN

ARG

ASN

GLU

LEU

LYS

5

ARG

SER

PHE

ALA

LEU

ARG

ASP

GLN

ILE

6

PRO

GLU

LEU

GLU

ASN

GLU

LYS

ALA

PRO

7

LYS

VAL

ILE

LEU

LYS

ALA

THR

ALA

8

TYR

ILE

LEU

SER

VAL

GLN

ALA

GLU

GLN

9

LYS

LEU

ILE

SER

GLU

ASP

LEU

ARG

10

LYS

ARG

GLU

GLN

LEU

LYS

HIS

LYS

LEU

11

GLU

GLN

LEU

ARG

ASN

SER

Samples:

sample_1: c-MYC, [U-99% 13C; U-99% 15N], 80 uM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 278 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker ARX 800 MHz

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