BMRB Entry 6163

Name: Backbone 1H, 13C, 15N assignment of the bHLHZip domain of the oncogenic transcription factor v-myc in complex with its authentic binding partner max
Published: 2004-12-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6163

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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, 15N assignment of the bHLHZip domain of the oncogenic transcription factor v-myc in complex with its authentic binding partner max

Deposition date:

2004-04-02

Original release date:

2004-12-16

Authors:

Baminger, Bettina; Ludwiczek, Martin; Hoffmann, Bernd; Kontaxis, Georg; Bister, Klaus; Konrat, Robert

Citation:

Citation: Baminger, Bettina; Ludwiczek, Martin; Hoffmann, Bernd; Kontaxis, Georg; Bister, Klaus; Konrat, Robert. "Letter to the editor: Backbone assignment of the dimerization and DNA-binding domain of the oncogenic transcription factor v-Myc in complex with its authentic binding partner Max" J. Biomol. NMR 30, 361-362 (2004).

Assembly members:

Assembly members:
v-myc, polymer, 103 residues, 12357 Da.
max, polymer, 93 residues, 10927 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
v-myc: SNNRKCSSPRTLDSEENDKR RTHNVLERQRRNELKLRFFA LRDQIPEVANNEKAPKVVIL KKATEYVLSLQSDEHKLIAE KEQLRRRREQLKHNLEQLRN SRA
max: MADKRAHHNALERKRRDHIK DSFHSLRDSVFSLQGEKASR AQILDKATEYIQYMRRKNHT HQQDIDDLKRQNALLEQQVR ALEKARSSAQLQA

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
1H chemical shifts	88
13C chemical shifts	95
15N chemical shifts	88

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	v-myc	1
2	max	2

Entities:

Entity 1, v-myc 103 residues - 12357 Da.

1

SER

ASN

ARG

LYS

CYS

SER

PRO

ARG

2

THR

LEU

ASP

SER

GLU

ASN

ASP

LYS

ARG

3

ARG

THR

HIS

ASN

VAL

LEU

GLU

ARG

GLN

ARG

4

ARG

ASN

GLU

LEU

LYS

LEU

ARG

PHE

ALA

5

LEU

ARG

ASP

GLN

ILE

PRO

GLU

VAL

ALA

ASN

6

ASN

GLU

LYS

ALA

PRO

LYS

VAL

ILE

LEU

7

LYS

ALA

THR

GLU

TYR

VAL

LEU

SER

LEU

8

GLN

SER

ASP

GLU

HIS

LYS

LEU

ILE

ALA

GLU

9

LYS

GLU

GLN

LEU

ARG

GLU

GLN

10

LEU

LYS

HIS

ASN

LEU

GLU

GLN

LEU

ARG

ASN

11

SER

ARG

ALA

Entity 2, max 93 residues - 10927 Da.

1

MET

ALA

ASP

LYS

ARG

ALA

HIS

ASN

ALA

2

LEU

GLU

ARG

LYS

ARG

ASP

HIS

ILE

LYS

3

ASP

SER

PHE

HIS

SER

LEU

ARG

ASP

SER

VAL

4

PHE

SER

LEU

GLN

GLY

GLU

LYS

ALA

SER

ARG

5

ALA

GLN

ILE

LEU

ASP

LYS

ALA

THR

GLU

TYR

6

ILE

GLN

TYR

MET

ARG

LYS

ASN

HIS

THR

7

HIS

GLN

ASP

ILE

ASP

LEU

LYS

ARG

8

GLN

ASN

ALA

LEU

GLU

GLN

VAL

ARG

9

ALA

LEU

GLU

LYS

ALA

ARG

SER

ALA

GLN

10

LEU

GLN

ALA

Samples:

sample_1: v-myc, [U-2H; U-15N; U-13C], 1.1 mM; max 1.1 mM

cond_v-Myc_1: pH: 6.5; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
HNCA	sample_1	not available	cond_v-Myc_1
HNCACB	sample_1	not available	cond_v-Myc_1
HNCO	sample_1	not available	cond_v-Myc_1
1H-15N NOESY	sample_1	not available	cond_v-Myc_1

Software:

NMRView v5.0.4 - analysis of NMR datasets

NMR spectrometers:

Varian Unity_Inova 800 MHz

PDB	1AN2 1HLO 1NKP 1NLW 1NLW 1NKP 1HLO 1AN2
DBJ	BAA03337 BAA03338 BAA07038 BAC37914 BAE00858 BAF85319 BAF83618
EMBL	CAA42827 CAA47337 CAA47338 CAA47339 CAG46988 CAG46988 CAA47339 CAA47338 CAA42827
GB	AAA16834 AAA36200 AAA36201 AAB35748 AAH03525
REF	NP_001009866 NP_001139648 NP_001248298 NP_001272145 NP_002373 XP_001514941 XP_001369712 XP_001103369 NP_660092 NP_660088
SP	P52162 P52164 P61244 P61245
SWISS-PROT	P52162
GenBank	EAW80899 AAQ57210 AAH36092 AAB35748 AAA16834
AlphaFold	P52162 P52164 P61244 P61245