Linker histone H1 plays a vital role in the packaging of DNA. H1 has a tripartite structure: a conserved central globular domain that adopts a winged-helix fold, flanked by highly variable and intrinsically unstructured N- and C-terminal domains. The datasets presented in this article include raw 2D and 3D BEST-TROSY NMR data [1H-15 N HSQC; 15 N and 13C HNCO, HN(CO)CACB, HNCACB, HN(CA)CO] recorded for NGH1x, a truncated version of H1x containing the N-terminal and globular domains, but lacking the C-terminal domain. Experiments were conducted on double-labelled (15 N and 13C) NGH1x in 'low' and 'high salt,' to investigate the secondary structure content of the N-terminal domain of H1x under these conditions. We provide modelled structures of NGH1x (in low and high salt) based on the assigned chemical shifts in PDB format. The high salt structure of NGH1x (globular domain of H1x [GH1x; PDB: 2LSO] with the H1x NTD) was docked to the nucleosome to generate NGH1x- and GH1x-chromatosomes. The GH1x-chromatosome was generated for comparative purposes to elucidate the role of the N-terminal domain. We present raw data trajectories of molecular dynamics simulations of these chromatosomes in this article. The MD dataset provides nanosecond resolution data on the dynamics of GH1x- vs NGH1x-chromatosomes, which is useful to elucidate the DNA binding properties of the N-terminal domain of H1x in chromatin, as well as the dynamic behaviour of linker DNA in these chromatosomes.
Keywords: BEST-TROSY; Core histone; Intrinsically unstructured protein; Linker DNA; Linker histone; Molecular dynamics; NMR; Nucleosome.
© 2020 The Authors.