Raw nuclear magnetic resonance data of human linker histone H1x lacking the C-terminal domain (NGH1x) and trajectory data of nanosecond molecular dynamics simulations of GH1x- and NGH1x-chromatosomes (NMR data).

Published: 14 May 2020| Version 3 | DOI: 10.17632/7rjd6r2x76.3
Herna de Wit,


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 Bruker Avance III HD spectrometers, operating at 700 or 950 MHz 1H frequency, and equipped with cryogenically cooled triple-resonance (HCN) probes and pulsed z-field gradients at 5'C (278 K). 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. A description of the data folders is given in the file "NMR Description of data folders.pdf".



Institut de Biologie Structurale, University of Johannesburg


Nuclear Magnetic Resonance, Histone, Intrinsically Disordered Protein, NMR Pulse, Human, 13C NMR Studies, Biomolecular NMR Assignment, Protein Structure