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. 2021 Feb 19;11:4284. doi: 10.1038/s41598-021-83198-w

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© Crown 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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NMR signal perturbations of the ¹⁵N-labelled Ubi-ID protein by VHH-IR5. Weighted deviations are calculated as the square root of the weighted frequency shifts along both the ¹H and ¹⁵N dimensions of the HSQC spectra of the free Ubi-ID as compared to a 1:1 complex of Ubi-ID with unlabelled VHH-IR5 (Fig. S3a) and plotted according to residue-specific assignments achieved for Ubi-ID (Fig. S4). The ubiquitin moiety from 1 to 76 exhibits relatively small differences between the free protein and its complex with VHH-IR5. Some residues of the IGF1R ID 694-742 moiety show pronounced perturbations, especially for T675-E687 (or residues 84-96 of Ubi-ID). Bars with an arrow indicate those residues whose HSQC signals disappeared in the complex of ¹⁵N-labelled Ubi-ID with VHH-IR5. Hatched boxes indicate that no HSQC signals were found for this region of Ubi-ID (R689-R709), except for R704. HSQC signals of the ID segment re-emerge from residue 119 to 151 (R710-E742), with essentially no responses to VHH-IR5 binding.