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. 2019 May 30;10:2370. doi: 10.1038/s41467-019-10345-3

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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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Fig. 2 — 3D structural model of FAM134B-RHD from MD simulations. a, b Transmembrane fragments fold into helical hairpins (red and blue helices in (a) TM12 and (b) TM34. Flanking charged and polar residues and luminal loop residues anchor the two hairpins within the ER membrane (labeled side chains). c, d Linker and C-terminal fragments form amphipathic helices (c) AH_L and (d) AH_C (yellow cartoon). Polar (colored labels) and apolar residues (yellow labels) on opposite sides position the helices at the water–bilayer interface. e Overlapping, individually refined fragment structures were used to assemble the FAM134B-RHD (80–260) structural model. The model was first equilibrated using coarse-grained simulations and then refined with all-atom MD simulations. f Time-averaged local membrane profile (gray mesh; top, side, and 3D views) around FAM134B-RHD (colored) computed from all-atom MD simulations displays perturbations of the bilayer structure