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
Contributors:
Herna de Wit,
Alicia Vallet,
Bernhard Brutscher,
Gerrit Koorsen

Description

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".

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Institutions

Institut de Biologie Structurale, University of Johannesburg

Categories

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

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