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).

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".

人源连接蛋白组蛋白H1在DNA的包装过程中扮演着至关重要的角色。H1蛋白具有三分子的结构：一个进化上保守的中央球形结构域，该结构域采用翅膀螺旋折叠，两侧被高度可变且内源无结构的N端和C端结构域所包围。

本数据集包含Bruker Avance III HD核磁共振光谱仪上记录的原始2D和3D BEST-TROSY NMR数据，该光谱仪在700或950 MHz的1H频率下运行，并配备了液氮冷却的三共振（HCN）探头和5°C（278 K）的脉冲z场梯度。

数据记录了NGH1x（人源H1x的第1至120个氨基酸残基；UniProtKB：Q92522(H1X_HUMAN)，包括N端和球形结构域）在20 mM磷酸钠（低盐）或20 mM磷酸钠+1 M高氯酸钠（高盐）溶液中。

数据可使用Sparky、CCPNMR等NMR光谱分析软件进行分析。

数据文件夹的描述详见文件“NMR Description of data folders.pdf”。