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Updated: Jun 13, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Complete NMR assignment for 275 of the most common dipeptides in intrinsically disordered proteins
Tobias Rindfleisch1,2,3, Emilie Fjeldberg Taule4, Markus S Miettinen5,6
1Computational Biology Unit, Department of Informatics, University of Bergen, 5008, Bergen, Norway. tobias.rindfleisch@uib.no.
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Accurate NMR chemical shift assignments are essential for atomic-resolution characterization of proteins. Especially for intrinsically disordered proteins (IDPs) and regions (IDRs), however, the assignment remains a labor-intensive task due to spectral overlap and conformational heterogeneity. Consequently, complete side-chain assignments are rare. Here, we present a comprehensive reference dataset, comprising the complete NMR chemical shift assignments for 275 of the most prevalent dipeptides in the IDPome, covering 93% of it. 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 validated data points, as well as the 1D (1H, 13C) and 2D (1H-15N HSQC, 1H-13C HSQC, TOCSY, NOESY, 1H-13C 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.
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