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 19074

Title: 1H, 13C, 15N chemical shift assignments of Dido PHD domain in complex with peptide H3K4me3   PubMed: 23579637

Deposition date: 2013-03-05 Original release date: 2013-05-30

Authors: Santiveri, Clara; Perez-Canadillas, Jose; Jimenez, M Angeles

Citation: Santiveri, Clara; Garcia-Mayoral, M. Flor; Perez-Canadillas, Jose; Jimenez, M. Angeles. "NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3."  J. Biomol. NMR 56, 183-190 (2013).

Assembly members:
Dido_PHD, polymer, 61 residues, 7048.059 Da.
Dido_PHD, polymer, 61 residues, 7048.059 Da.
ZINC ION, non-polymer, 65.409 Da.

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

Entity Sequences (FASTA):
Dido_PHD: GSMDPNALYCICRQPHNNRF MICCDRCEEWFHGDCVGISE ARGRLLERNGEDYICPNCTI L
Dido_PHD: GSMDPNALYCICRQPHNNRF MICCDRCEEWFHGDCVGISE ARGRLLERNGEDYICPNCTI L

Data sets:
Data typeCount
13C chemical shifts267
15N chemical shifts66
1H chemical shifts383

Additional metadata:

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