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. 2018 Mar 13;8:4446. doi: 10.1038/s41598-018-22476-6

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© The Author(s) 2018

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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Energy profiles for different depths and tilt angles inside and outside the membrane. The native position at (0, 0) is the protein embedding from PDBTM with the topology from the OPM database. Note that at this position, the protein can already be tilted with respect to the membrane normal. The protein tilt angles at the native position are the following: Glycophorin A = 11.7°, Bacteriorhodopsin = 0°, Chloride channel = 10.7°, Cox2 = NA, PagP = 29.0°, WALP23 = 1.6°. Low energy conformations are shown in the pictures with membrane planes in red being the outer leaflet and blue being the inner leaflet. z-axis and tilt angles are shown for the low energy conformations; the lowest energy embedding parameters for the predicted topologies are highlighted in bold. Correct predictions are highlighted in green, the incorrect one (Cox2) in red.