BMRB: 4200

NMR Solution Structure of the c-Myc-Max Heterodimeric Leucine Zipper

Authors

Lavigne, P., Crump, M.P., Gagne, S.M., Hodges, R.S., Kay, C.M., Sykes, B.D.

Assembly

c-Myc-Max Heterodimeric Leucine Zipper

Entity

1. Leucine Zipper domain of c-Myc (polymer, Thiol state: not present), 34 monomers, 3829.365 Da Detail

XCGGVQAEEQ KLISEEDLLR KRREQLKHKL EQLX

2. Max Leucine Zipper Domain (polymer, Thiol state: not present), 34 monomers, 3775.220 Da Detail

XCGGMRRKND THQQDIDDLK RQNALLEQQV RALX

Total weight

7604.585 Da

Max. entity weight

3829.365 Da

Source organism

Homo sapiens , Mus musculus

Exptl. method

NMR

Refine. method

SIMULATED ANNEALING

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 42.6 %, Completeness: 38.4 %, Completeness (bb): 41.7 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	38.4 % (161 of 419)	38.4 % (161 of 419)
Backbone	41.7 % (55 of 132)	41.7 % (55 of 132)
Sidechain	36.9 % (106 of 287)	36.9 % (106 of 287)
Aromatic	50.0 % (2 of 4)	50.0 % (2 of 4)
Methyl	46.9 % (15 of 32)	46.9 % (15 of 32)

1. Leucine Zipper domain of c-Myc

XCGGVQAEEQ KLISEEDLLR KRREQLKHKL EQLX

2. Max Leucine Zipper Domain

XCGGMRRKND THQQDIDDLK RQNALLEQQV RALX

Show sample condition

Sample

Temperature 298.15 (±0.2) K, pH 4.8 (±0.3), Details The sample is a heterodimer consisting of disulfide-linked Leucine Zipper domains of c-Myc (chain A) and Max (chain B)

#	Name	Isotope labeling	Type	Concentration
1	Leucine Zipper domain of c-Myc			1.0 mM
2	potassium phosphate			50 mM
3	H2O			90 %
4	D2O			10 %
5	KCl			50 mM
6	DSS			1 mM

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Chem. Shift Complete2

Sequence coverage: 42.6 %, Completeness: 38.1 %, Completeness (bb): 41.3 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	38.1 % (319 of 838)	38.1 % (319 of 838)
Backbone	41.3 % (109 of 264)	41.3 % (109 of 264)
Sidechain	36.6 % (210 of 574)	36.6 % (210 of 574)
Aromatic	50.0 % (4 of 8)	50.0 % (4 of 8)
Methyl	46.9 % (30 of 64)	46.9 % (30 of 64)

1. Leucine Zipper domain of c-Myc

XCGGVQAEEQ KLISEEDLLR KRREQLKHKL EQLX

2. Max Leucine Zipper Domain

XCGGMRRKND THQQDIDDLK RQNALLEQQV RALX

Show sample condition

Sample

Temperature 298.15 (±0.2) K, pH 4.8 (±0.3), Details The sample is a heterodimer consisting of disulfide-linked Leucine Zipper domains of c-Myc (chain A) and Max (chain B)

#	Name	Isotope labeling	Type	Concentration
1	Leucine Zipper domain of c-Myc			1.0 mM
2	potassium phosphate			50 mM
3	H2O			90 %
4	D2O			10 %
5	KCl			50 mM
6	DSS			1 mM

Hide sample codition

Protein Blocks Logo

Calculated from 1 models in PDB: 1A93, Strand ID: A, B Detail

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Release date

2006-09-21

Citation 1

Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper
Lavigne, P., Crump, M.P., Gagne, S.M., Hodges, R.S., Kay, C.M., Sykes, B.D.
J. Mol. Biol. (1998), 281, 165-181, PubMed 9680483 , DOI 10.1006/jmbi.1998.1914 , Abstract

Show more 1 citaion

Citation 2

No title is available
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140

Hide non-primary 1 citaion

Related entities 1. Leucine Zipper domain of c-Myc, : 1 : 9 : 55 entities Detail

Related entities 2. Max Leucine Zipper Domain, : 1 : 11 : 9 entities Detail

Interaction partners 1. Leucine Zipper domain of c-Myc, : 205 : 1 interactors Detail

Experiments performed 1 experiments Detail