1H, 13C, 15N chemical shift assignments of Dido PHD domain

NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3.

Residues 1-3, GSM, are the cloning tag.
Residues 4-61 correspond to residues 265-322 from human Dido or to residues 262-319 from mouse Dido.

Solution Structure Of Phd Domain In Death Inducer- Obliterator 1(Dio-1)

Crystal Structure Of The Dido Phd Finger In Complex With H3k4me3

unnamed protein product [Macaca fascicularis]

death inducer-obliterator-1 [Mus musculus]

hypothetical protein RCJMB04_5h22 [Gallus gallus]

Death inducer-obliterator 1 [Homo sapiens]

death-inducer obliterator 1 [Pongo abelii]

death-inducer obliterator 1 isoform c [Homo sapiens]

death-inducer obliterator 1 isoform b [Homo sapiens]

death-inducer obliterator 1 Dido1 [Mus musculus]

death-inducer obliterator 1 Dido2 [Mus musculus]

RecName: Full=Death-inducer obliterator 1; Short=DIO-1; AltName: Full=Death-associated transcription factor 1; Short=DATF-1

RecName: Full=Death-inducer obliterator 1; Short=DIO-1; Short=hDido1; AltName: Full=Death-associated transcription factor 1; Sh