i1myr’s interactions with AC5 are stable over the course of the classical MD trajectory.

(A) Aligned structures of the docked model (cyan) and the Gαi1myr: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 (Fig 3C). (B) Aligned structures of the docked model (cyan) and the Gαi1myr:AC5 complex after ∼ 1.7 μs (orange and red). The structures were aligned on the Gαi1myr subunit (residues 34 to 334) in order to show the change in the conformation of Gαi1myr. (C) Number of hydrogen bonds between Gαi1myr and C1 and Gαi1myr and C2 that are present during the classical MD trajectory.