Chromatin-remodeling proteins have a pivotal role in normal cell function and 
development, catalyzing conformational changes in DNA that ultimately result in 
changes in gene expression patterns. Chromodomain helicase DNA-binding protein 4 
(CHD4), the defining subunit of the nucleosome remodeling and deacetylase (NuRD) 
complex, is a nucleosome-remodeling protein of the SNF2/ISWI2 family, members of 
which contain two chromo domains and an ATP-dependent helicase module. CHD3, 
CHD4 and CHD5 also contain two contiguous PHD domains and have an extended 
N-terminal region that has not previously been characterized. We have identified 
a stable domain in the N-terminal region of CHD4 and report here the backbone 
and side chain resonance assignments for this domain at pH 7.5 and 25 °C (BMRB 
No. 18906).