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. 2017 Sep 5;7:10418. doi: 10.1038/s41598-017-10741-z

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© The Author(s) 2017

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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Lipid substrate dependence of ATPase activity of R898 mutants. The ATPase activity of the wild type bATP8A2 (WT) and the indicated mutants was determined at the indicated concentrations of PS (a, b) or PE (c, d). The data for R898E and E897R are repeated in (b and d) for direct comparison with E897R_R898E. Further information as in the legend to Fig. 3.