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 27416

Title: Backbone 1H, 15N, 13C assignment of Human Myc S373D/T400D, N353 to A399.   PubMed: 29695509

Deposition date: 2018-03-06 Original release date: 2018-04-11

Authors: Macek, Pavel

Citation: Macek, Pavel; Cliff, Matthew; Embrey, Kevin; Holdgate, Geoffrey; Nissink, J Willem; Panova, Stanislava; Waltho, Jonathan; Davies, Rick. "Myc phosphorylation in its basic helix-loop-helix region destabilizes transient alpha-helical structures, disrupting Max and DNA binding"  J. Biol. Chem. 293, 9301-9310 (2018).

Assembly members:
cMyc_S373D-T400D, polymer, 87 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: pET

Entity Sequences (FASTA):
cMyc_S373D-T400D: GSNVKRRTHNVLERQRRNEL KRDFFALRDQIPELENNEKA PKVVILKKADAYILSVQAEE QKLISEEDLLRKRREQLKHK LEQLRNS

Data sets:
Data typeCount
13C chemical shifts94
15N chemical shifts45
1H chemical shifts45

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1cMyc S373D/T400D1

Entities:

Entity 1, cMyc S373D/T400D 87 residues - Formula weight is not available

1   GLYSERASNVALLYSARGARGTHRHISASN
2   VALLEUGLUARGGLNARGARGASNGLULEU
3   LYSARGASPPHEPHEALALEUARGASPGLN
4   ILEPROGLULEUGLUASNASNGLULYSALA
5   PROLYSVALVALILELEULYSLYSALAASP
6   ALATYRILELEUSERVALGLNALAGLUGLU
7   GLNLYSLEUILESERGLUGLUASPLEULEU
8   ARGLYSARGARGGLUGLNLEULYSHISLYS
9   LEUGLUGLNLEUARGASNSER

Samples:

sample_1: cMyc S373D/T400D, [U-100% 13C; U-100% 15N], 0.15 mM; potassium phosphate 50 mM; ammonium chloride 500 mM; DTT 1 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 550 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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