BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27571

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the bHLHZip c-MYC:MAX complex.   PubMed: 31260268

Deposition date: 2018-08-06 Original release date: 2018-09-18

Authors: Bycroft, Mark; Zinzalla, Giovanna

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).

Assembly members:
c-MYC, polymer, 105 residues, Formula weight is not available
MAX, polymer, 82 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24a

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

Data sets:
Data typeCount
13C chemical shifts466
15N chemical shifts149
1H chemical shifts149

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1c-MYC1
2MAX2

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   GLYSERSERHISHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERHISMET
3   ASNVALLYSARGARGTHRHISASNVALLEU
4   GLUARGGLNARGARGASNGLULEULYSARG
5   SERPHEPHEALALEUARGASPGLNILEPRO
6   GLULEUGLUASNASNGLULYSALAPROLYS
7   VALVALILELEULYSLYSALATHRALATYR
8   ILELEUSERVALGLNALAGLUGLUGLNLYS
9   LEUILESERGLUGLUASPLEULEUARGLYS
10   ARGARGGLUGLNLEULYSHISLYSLEUGLU
11   GLNLEUARGASNSER

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

Residues 22-103 of human MAX protein.

1   ALAASPLYSARGALAHISHISASNALALEU
2   GLUARGLYSARGARGASPHISILELYSASP
3   SERPHEHISSERLEUARGASPSERVALPRO
4   SERLEUGLNGLYGLULYSALASERARGALA
5   GLNILELEUASPLYSALATHRGLUTYRILE
6   GLNTYRMETARGARGLYSASNHISTHRHIS
7   GLNGLNASPILEASPASPLEULYSARGGLN
8   ASNALALEULEUGLUGLNGLNVALARGALA
9   LEUGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker ARX 800 MHz

Related Database Links:

SP P01106 P61244

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts