BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26662

Title: Backbone 1H, 13C and 15N Chemical Shift Assignments for c-Myc-1-88   PubMed: 26655473

Deposition date: 2015-09-17 Original release date: 2015-12-17

Authors: Helander, Sara; Montecchio, Meri; Sunnerhagen, Maria

Citation: Helander, Sara; Montecchio, Meri; Pilstal, Robert; Su, Yulong; Kuruvilla, Jacob; Elven, Malin; Ziauddin, Javed; Anandapadamanaban, Madhanagopal; Cristobal, Susana; Lundstrom, Patrik; Sears, Rosalie; Wallner, Bjorn; Sunnerhagen, Maria. "Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity"  Structure 23, 2267-2279 (2015).

Assembly members:
c-Myc, polymer, 94 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: pETMCSIII

Entity Sequences (FASTA):
c-Myc: HHHHHHMPLNVSFTNRNYDL DYDSVQPYFYCDEEENFYQQ QQQSELQPPAPSEDIWKKFE LLPTPPLSPSRRSGLCSPSY VAVTPFSLRGDNDG

Data sets:
Data typeCount
13C chemical shifts235
15N chemical shifts76
1H chemical shifts71

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1c-Myc1

Entities:

Entity 1, c-Myc 94 residues - Formula weight is not available

1   HISHISHISHISHISHISMETPROLEUASN
2   VALSERPHETHRASNARGASNTYRASPLEU
3   ASPTYRASPSERVALGLNPROTYRPHETYR
4   CYSASPGLUGLUGLUASNPHETYRGLNGLN
5   GLNGLNGLNSERGLULEUGLNPROPROALA
6   PROSERGLUASPILETRPLYSLYSPHEGLU
7   LEULEUPROTHRPROPROLEUSERPROSER
8   ARGARGSERGLYLEUCYSSERPROSERTYR
9   VALALAVALTHRPROPHESERLEUARGGLY
10   ASPASNASPGLY

Samples:

sample_1: c-Myc, [U-99% 13C; U-99% 15N], 80 – 250 uM; DTT 5 mM; glycerol 5%; H2O 90%; D2O 10%; HEPES 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HACANsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Analysis of data processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

UNP P01106
AlphaFold Q14026

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