Data for: Fast ultra-selective 1H-15N 1D NMR spectroscopy unlocks atom-resolved dynamics of low-complexity protein regions

Insight into the conformational dynamics of proteins is essential towards understanding their function at a molecular level. The motions experienced by individual atoms in the protein can be precisely quantified through NMR relaxation rates, but their measurement requires well-resolved spectral responses. Two-dimensional 1H‑15N correlation spectra are the standard approach to resolve amide signals in protein NMR, but come with an excessive cost in experimental time when spectra are heavily congested due to limited 15N chemical shift dispersions. This limitation often thwarts complete characterization of dynamics for intrinsically disordered proteins, especially when they feature low-complexity or homopolymer amino acid sequences. Here, we introduce an ultra-selective 1H-15N NMR method that allows high-quality measurement of individual 15N spin-relaxation constants using fast 1D NMR spectra, even when 15N resonances are merely 6-8 Hz apart. We demonstrate the new experiment by characterizing, for the first time, pico- to nanosecond dynamics along a 16‑residue polyglutamine stretch within the protein huntingtin, the causal agent of Huntington’s disease, as well as millisecond conformational exchange in the SH3GL3 protein. The new experiment will find wide application in the study of conformational dynamics of intrinsically disordered proteins or any other biomacromolecule that features highly dense 1H-15N 2D spectra. This deposit contains Bruker pulse sequences of the SNIPER 15N R1, SNIPER 15N R1rho, SNIPER 1H-15N nOe and SNIPER zz-exchange experiments, pulse shapes used, and the NMR experimental data (Bruker format). See the Data_overview.pdf file for a more detailed description. Version 2 : Additional data has been added concerning part 3 of the Supplementary Information.深入解析蛋白质的构象动态，是在分子层面理解其功能的核心前提。蛋白质中单个原子的运动可通过核磁共振（Nuclear Magnetic Resonance, NMR）弛豫速率进行精准定量，但该测量需要获得高分辨的光谱响应。二维1H-15N相关谱是蛋白质核磁共振中解析酰胺信号的标准方法，但当15N化学位移分散度有限导致谱峰严重重叠时，该方法会耗费极长的实验时间。这一局限往往阻碍了对内在无序蛋白（intrinsically disordered proteins）动态特性的完整表征，尤其是当这类蛋白具有低复杂度或均聚氨基酸序列时。本研究提出一种超高选择性的1H-15N核磁共振方法，即便15N共振峰间距仅为6~8 Hz，也可通过快速一维核磁共振谱高质量测定单个15N自旋弛豫常数。我们通过两项首次报道的表征验证了该新实验方法：一是对亨廷顿舞蹈症致病蛋白亨廷顿中16个氨基酸残基组成的聚谷氨酰胺肽段的皮秒至纳秒级动态特性进行解析，二是对SH3GL3蛋白的毫秒级构象交换过程进行分析。该新实验方法将在内在无序蛋白或其他具有高密1H-15N二维谱的生物大分子的构象动态研究中拥有广阔应用前景。 本数据集包含SNIPER 15N R1、SNIPER 15N R1rho、SNIPER 1H-15N核奥弗豪泽效应（nuclear Overhauser effect, nOe）以及SNIPER zz-exchange实验的布鲁克（Bruker）脉冲序列、所用脉冲波形，以及核磁共振实验数据（布鲁克格式）。详细说明请参阅Data_overview.pdf文件。 版本2：补充了关于补充材料第3部分的额外数据。