NMR data of human linker histone H1x N-terminal domain and globular domain in the presence and absence of perchlorate.

Human linker histone H1 is an important role player in the packaging of DNA. H1 has a tripartite structure: an evolutionarily conserved central globular domain that adopts a winged-helix fold, flanked by the highly variable and intrinsically unstructured N- and C-terminal domains. This dataset consists of raw 2D and 3D BEST-TROSY NMR data recorded on a Bruker 950 MHz NMR instrument. Data were recorded for NGH1x (residues 1 – 120 of human H1x; UniProtKB: Q92522(H1X_HUMAN) consisting of the N-terminal and globular domains) in 20 mM sodium phosphate (‘low salt’) or 20 mM sodium phosphate + 1 M sodium perchlorate (‘high salt’). Data can be analyzed using NMR spectra analysis software such as Sparky, CCPNMR, etc.