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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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BLP binds to LolA even when two or three inhibitor molecules are present. (A) The chemical structure of MAC13243 inhibitor. (B) Snapshots at different time points during a simulation of LolA and BLP with three MAC molecules (red, pink, magenta) bound in the hydrophobic cavity. Residue F90 is labelled. (C) Minimum distance between the BLP lipids and F90 from simulations with two (left) and three (right) MAC inhibitors. Results are from three independent simulations. The insert illustrates hydrophobic entanglement of BLP lipids and three MAC molecules from one of the simulations.