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. 2022 Aug 25;18(10):1152–1160. doi: 10.1038/s41589-022-01111-6

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© The Author(s) 2022

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 2 — Overlay of methyl TROSY NMR spectra of the Xrn2 enzyme with (black, WT) and without (purple, Delta ZnF) the ZnF. Removal of the ZnF does not perturb the structure of the Xrn2 enzyme, as can be concluded from the limited number of residues that experience CSPs. The observed CSPs upon deletion of the ZnF can be explained by the proximity of these residues to the (deleted) ZnF (for example I235) and by a transient interactions between the ZnF and a region of the enzyme that is located around the active site (I89, I59, I166, I314 and I850). In summary, these data thus show that the ZnF is loosely associated with Xrn2 and transiently interacts with the region of the enzyme that also contains the active site.