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. 2020 Jan 16;11:303. doi: 10.1038/s41467-019-14220-z

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© The Author(s) 2020

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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Fig. 5 — a Enzymatic activity of sFKRP with CDP-Rbo and the RboP-(phospho-)core M3 peptide. The products were analyzed by HPLC. Upper, without sFKRP; lower, with sFKRP. S1, acceptor substrate [RboP-(phospho-)core M3 peptide]; P1, product of the reaction of sFKRP with CDP-Rbo. b No enzymatic activity was observed for sFKRP with CDP-Rbo and the RboP-core M3 peptide. The products were analyzed by HPLC. Upper, without sFKRP; lower, with sFKRP. S2, acceptor substrate (RboP-core M3 peptide). Eluates with the retention times indicated by dotted lines were subjected to MS analysis (Supplementary Fig. 6).