10.1371/journal.pcbi.1005673.g002 Siri Camee van Keulen Siri Camee van Keulen Ursula Rothlisberger Ursula Rothlisberger Gα<sub>i1</sub><sup>myr</sup>’s interactions with AC5 are stable over the course of the classical MD trajectory. Public Library of Science 2017 adenylyl cyclase type 5 n-terminal myristoylated G α i 1 Adenylyl cyclase apo adenylyl cyclase type 5 G-protein-coupled-receptor signal transduction pathways G protein function AC regulation 2017-09-11 17:26:18 Figure https://plos.figshare.com/articles/figure/G_sub_i1_sub_sup_myr_sup_s_interactions_with_AC5_are_stable_over_the_course_of_the_classical_MD_trajectory_/5395720 <p>(A) Aligned structures of the docked model (cyan) and the Gα<sub>i1</sub><sup>myr</sup>:AC5 complex after ∼ 1.7 μs (orange and red). The structures were aligned on the C1 domain, residues 456 to 644, as this domain’s RMSD is low over the course of the simulation (<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1005673#pcbi.1005673.g003" target="_blank">Fig 3C</a>). (B) Aligned structures of the docked model (cyan) and the Gα<sub>i1</sub><sup>myr</sup>:AC5 complex after ∼ 1.7 μs (orange and red). The structures were aligned on the Gα<sub>i1</sub><sup>myr</sup> subunit (residues 34 to 334) in order to show the change in the conformation of Gα<sub>i1</sub><sup>myr</sup>. (C) Number of hydrogen bonds between Gα<sub>i1</sub><sup>myr</sup> and C1 and Gα<sub>i1</sub><sup>myr</sup> and C2 that are present during the classical MD trajectory.</p>