BMRB Entry 27571

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the bHLHZip c-MYC:MAX complex.
Published: 2018-09-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27571

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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 1H, 13C, and 15N Chemical Shift Assignments for the bHLHZip c-MYC:MAX complex.

Deposition date:

2018-08-06

Original release date:

2018-09-18

Authors:

Bycroft, Mark; Zinzalla, Giovanna

Citation:

Citation: Sammak, Susan; Hamdani, Najoua; Gorrec, Fabrice; Allen, Mark; Freund, Stefan; 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, 105 residues, Formula weight is not available
MAX, polymer, 82 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: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
c-MYC: GSSHHHHHHSSGLVPRGSHM NVKRRTHNVLERQRRNELKR SFFALRDQIPELENNEKAPK VVILKKATAYILSVQAEEQK LISEEDLLRKRREQLKHKLE QLRNS
MAX: ADKRAHHNALERKRRDHIKD SFHSLRDSVPSLQGEKASRA QILDKATEYIQYMRRKNHTH QQDIDDLKRQNALLEQQVRA LE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	466
15N chemical shifts	149
1H chemical shifts	149

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	c-MYC	1
2	MAX	2

Entities:

Entity 1, c-MYC 105 residues - Formula weight is not available

Residues 1-20 represent a non-native affinity tag, residues 20-105 are residues 352-437 of the human Myc proto-oncogene protein.

1

GLY

SER

HIS

SER

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

MET

3

ASN

VAL

LYS

ARG

THR

HIS

ASN

VAL

LEU

4

GLU

ARG

GLN

ARG

ASN

GLU

LEU

LYS

ARG

5

SER

PHE

ALA

LEU

ARG

ASP

GLN

ILE

PRO

6

GLU

LEU

GLU

ASN

GLU

LYS

ALA

PRO

LYS

7

VAL

ILE

LEU

LYS

ALA

THR

ALA

TYR

8

ILE

LEU

SER

VAL

GLN

ALA

GLU

GLN

LYS

9

LEU

ILE

SER

GLU

ASP

LEU

ARG

LYS

10

ARG

GLU

GLN

LEU

LYS

HIS

LYS

LEU

GLU

11

GLN

LEU

ARG

ASN

SER

Entity 2, MAX 82 residues - Formula weight is not available

Residues 22-103 of human MAX protein.

1

ALA

ASP

LYS

ARG

ALA

HIS

ASN

ALA

LEU

2

GLU

ARG

LYS

ARG

ASP

HIS

ILE

LYS

ASP

3

SER

PHE

HIS

SER

LEU

ARG

ASP

SER

VAL

PRO

4

SER

LEU

GLN

GLY

GLU

LYS

ALA

SER

ARG

ALA

5

GLN

ILE

LEU

ASP

LYS

ALA

THR

GLU

TYR

ILE

6

GLN

TYR

MET

ARG

LYS

ASN

HIS

THR

HIS

7

GLN

ASP

ILE

ASP

LEU

LYS

ARG

GLN

8

ASN

ALA

LEU

GLU

GLN

VAL

ARG

ALA

9

LEU

GLU

Samples:

sample_1: c-MYC, [U-100% 13C; U-100% 15N; U-80% 2H], 250 uM; MAX, [U-100% 13C; U-100% 15N; U-80% 2H], 250 uM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	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 HNCO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker ARX 800 MHz

SP	P01106 P61244
AlphaFold	Q14026 Q96CY8