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. 2019 Mar 6;9:3717. doi: 10.1038/s41598-019-40170-z

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© The Author(s) 2019

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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LolA binding site conforms to the shape of BLP lipid. (A) Structural comparison of LolA at the end of a simulation with zero MAC (cyan) to the crystal structure (grey). The tilt of the β-sheet is highlighted by the red arrow and the binding cavity is marked “X”. (B) Contact analysis with a distance cut-off of 4 A performed for each residue of LolA with BLP lipid averaged over three simulations. A score of 1 indicates contact made throughout the entire simulations. Residues that show more contact in simulations with zero MAC compared to that with three MACs are labelled. (C,D) Same analyses as (A,B), respectively, performed for simulations with 3 MACs.