Data repository: Complete NMR assignment for 275 of the most common dipeptides in intrinsically disordered proteins

In addition, we report side-chain protonation-dependent chemical shifts for dipeptides containing aspartic or glutamic acid. The dataset contains all NMR-accessible backbone and side-chain nuclei, in total 11 571 rigorously validated data points, as well as the 1D (1H, 13C) and 2D (15N HSQC, 13C HSQC, TOCSY, NOESY, HMBC) spectra used for the assignment, making it a rich resource for the training, testing, and benchmarking of tools for data-driven protein assignment, peak picking, and synthetic spectrum generation.

To facilitate such machine learning applications, all data are delivered in standardized, machine-readable formats. REMARK: For better overview, you can switch to "Tree view" in the "Files section": Files > Change View > Tree DATA: The following NMR experiments are included: 1D 1H (zgesgppe; gradient-enhanced, with water suppression) 1D 1H (1D NOESY ) 1D 1H (q-NMR; quantitative NMR) 1D 13C (C13CPD; composite pulse decoupling) 2D 1H-15N HSQC (heteronuclear single quantum coherence) 2D 1H-13C HSQC (heteronuclear single quantum coherence) 2D 1H-1H TOCSY (total correlation spectroscopy) 2D 1H-1H NOESY (nuclear overhauser effect spectroscopy) 2D 1H-13C HMBC (heteronuclear multiple-bond correlation)