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. 2017 Sep 12;7:11255. doi: 10.1038/s41598-017-11483-8

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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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Structural superposition between representative conformations of the most probable kinetic macrostates of intermediate regions I and II of the morphine-bound and TRV-130-bound MOR systems with inactive and activated MOR crystal structures. Cytoplasmic views of overlaps of the active (gray) and inactive (white) crystal structures of MOR with representative structures of: (a,c) the most probable kinetic macrostates #14 and #1 found in the intermediate region I and II, respectively, sampled by morphine-bound MOR, and (b,d) the most probable kinetic macrostates #13 and #10 located in the intermediate region I and II, respectively, sampled by TRV-130-bound MOR. Residues Y252^5.58 and Y336^7.53 are shown as sticks. Cα atoms of residues R165^3.50 and T279^6.34 are shown as spheres, and are connected by dotted line. TM1, TM4, helix 8 and intracellular loops are not shown for clarity.