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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. 1 — The ¹H-¹⁵N TROSY NMR spectrum of Xrn2 (black; residues 1-875) displays only ¹H-¹⁵N correlations from highly flexible parts of the protein; the ¹H-¹⁵N resonances in the protein core are broadened beyond detection due to the high molecular weight of the enzyme. The ¹H-¹⁵N spectrum from the isolated Xrn2 linker region (yellow; residues 265-293) largely overlaps with the spectrum from Xrn2 (1-875), proving that the CR1-CR2 linker region is flexible and disordered in the context of the full length protein.