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 51427

Title: B-Myb association with DNA is mediated by its negative regulatory domain and Cdk phosphorylation   PubMed: 35926712

Deposition date: 2022-05-04 Original release date: 2022-10-19

Authors: Wijeratne, Tilini; Guiley, Keelan; Lee, Hsiau-Wei; Muller, Gerd; Rubin, Seth

Citation: Wijeratne, Tilini; Guiley, Keelan; Lee, Hsiau-Wei; Muller, Gerd; Rubin, Seth. "Cyclin-dependent kinase-mediated phosphorylation and the negative regulatory domain of transcription factor B-Myb modulate its DNA binding"  J. Biol. Chem. 298, 102319-102319 (2022).

Assembly members:
entity_1, polymer, 93 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: pGEX

Entity Sequences (FASTA):
entity_1: KYSMDNTPHTPTPFKNALEK YGPLKPLPQTPHLEEDLKEV LRSEAGIELIIEDDIRPEKQ KRKPGLRRSPIKKVRKSLAL DIVDEDVKLMMST

Data sets:
Data typeCount
13C chemical shifts257
15N chemical shifts81
1H chemical shifts78

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1NRD1

Entities:

Entity 1, NRD 93 residues - Formula weight is not available

1   LYSTYRSERMETASPASNTHRPROHISTHR
2   PROTHRPROPHELYSASNALALEUGLULYS
3   TYRGLYPROLEULYSPROLEUPROGLNTHR
4   PROHISLEUGLUGLUASPLEULYSGLUVAL
5   LEUARGSERGLUALAGLYILEGLULEUILE
6   ILEGLUASPASPILEARGPROGLULYSGLN
7   LYSARGLYSPROGLYLEUARGARGSERPRO
8   ILELYSLYSVALARGLYSSERLEUALALEU
9   ASPILEVALASPGLUASPVALLYSLEUMET
10   METSERTHR

Samples:

sample_1: NRD, B-Myb, [U-100% 13C; U-100% 15N], 300 uM; sodium phosphate 20 mM; DTT 1 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CCONHsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

TOPSPIN - collection

VNMRj - collection

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz
  • Varian INOVA 600 MHz

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