BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 6163

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

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

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

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

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

Data sets:
Data typeCount
1H chemical shifts88
13C chemical shifts95
15N chemical shifts88

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1v-myc1
2max2

Entities:

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

1   SERASNASNARGLYSCYSSERSERPROARG
2   THRLEUASPSERGLUGLUASNASPLYSARG
3   ARGTHRHISASNVALLEUGLUARGGLNARG
4   ARGASNGLULEULYSLEUARGPHEPHEALA
5   LEUARGASPGLNILEPROGLUVALALAASN
6   ASNGLULYSALAPROLYSVALVALILELEU
7   LYSLYSALATHRGLUTYRVALLEUSERLEU
8   GLNSERASPGLUHISLYSLEUILEALAGLU
9   LYSGLUGLNLEUARGARGARGARGGLUGLN
10   LEULYSHISASNLEUGLUGLNLEUARGASN
11   SERARGALA

Entity 2, max 93 residues - 10927 Da.

1   METALAASPLYSARGALAHISHISASNALA
2   LEUGLUARGLYSARGARGASPHISILELYS
3   ASPSERPHEHISSERLEUARGASPSERVAL
4   PHESERLEUGLNGLYGLULYSALASERARG
5   ALAGLNILELEUASPLYSALATHRGLUTYR
6   ILEGLNTYRMETARGARGLYSASNHISTHR
7   HISGLNGLNASPILEASPASPLEULYSARG
8   GLNASNALALEULEUGLUGLNGLNVALARG
9   ALALEUGLULYSALAARGSERSERALAGLN
10   LEUGLNALA

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:

NameSampleSample stateSample conditions
HNCAsample_1not availablecond_v-Myc_1
HNCACBsample_1not availablecond_v-Myc_1
HNCOsample_1not availablecond_v-Myc_1
1H-15N NOESYsample_1not availablecond_v-Myc_1

Software:

NMRView v5.0.4 - analysis of NMR datasets

NMR spectrometers:

  • Varian Unity_Inova 800 MHz

Related Database Links:

PDB
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 P61244 P61245 P52162 P52164

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