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 11585

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for c-Myb R2R3 V103L/C130I

Deposition date: 2014-11-28 Original release date: 2015-12-09

Authors: Inaba, Satomi; Ikegami, Takahisa; Oda, Masayuki

Citation: Inaba, Satomi; Maeno, Akihiro; Sakurai, Kazumasa; Puthenpurackal, Sunilkumar; Ikegami, Takahisa; Akasaka, Kazuyuki; Oda, Masayuki. "Molecular strategy of c-Myb DNA-binding domain for function: Low-populated unfolding species revealed from temperature-dependent (NMR) studies"  Biophys. J. ., .-..

Assembly members:
c-Myb R2R3 V103L/C130I, polymer, 104 residues, Formula weight is not available

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
c-Myb R2R3 V103L/C130I: LIKGPWTKEEDQRLIKLVQK YGPKRWSVIAKHLKGRIGKQ IRERWHNHLNPEVKKTSWTE EEDRIIYQAHKRLGNRWAEI AKLLPGRTDNAIKNHWNSTM RRKV

Data sets:
Data typeCount
13C chemical shifts70
15N chemical shifts84
1H chemical shifts84

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1c-Myb R2R3 V103L/C130I1

Entities:

Entity 1, c-Myb R2R3 V103L/C130I 104 residues - Formula weight is not available

1   LEUILELYSGLYPROTRPTHRLYSGLUGLU
2   ASPGLNARGLEUILELYSLEUVALGLNLYS
3   TYRGLYPROLYSARGTRPSERVALILEALA
4   LYSHISLEULYSGLYARGILEGLYLYSGLN
5   ILEARGGLUARGTRPHISASNHISLEUASN
6   PROGLUVALLYSLYSTHRSERTRPTHRGLU
7   GLUGLUASPARGILEILETYRGLNALAHIS
8   LYSARGLEUGLYASNARGTRPALAGLUILE
9   ALALYSLEULEUPROGLYARGTHRASPASN
10   ALAILELYSASNHISTRPASNSERTHRMET
11   ARGARGLYSVAL

Samples:

sample_1: c-Myb R2R3 V103L/C130I, [U-99% 15N], 1.0 mM; TRIS 25 mM; potassium chloride 20 mM; H2O 90%; D2O, U-2H, 10%

sample_conditions_1: ionic strength: 45 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 950 MHz

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