Phosphorylation site topology governs the functional dynamics of arrestin recruitment to GPCRs

Molecular Dynamics Data for "Phosphorylation site topology governs the functional dynamics of arrestin recruitment to GPCRs" 

Authors: Timo Müller^#, Woojin Lee^#, Asat Baischew, Yasmin Aydin, Jordy Homing Lam, Falko Nagel, Andrea Sinz, Carsten Hoffmann, Stefan Schultz, Vsevolod Katritch*, Irene Coin*

This data contains the molecular dynamics (MD) simulation data for the muscarinic acetylcholine receptor M2 (M2R) in complex with beta-arrestin-1 (arr2), produced as part of the study “Phosphorylation site topology governs the functional dynamics of arrestin recruitment to GPCRs.” The simulations were initiated from three crosslinking-guided atomistic complex models (m134, m162, and m181) and propagated as unbiased MD in a lipid bilayer without applying crosslinking restraints. For each starting model, ten independent 1.2-µs replicas were run (12 µs per model; 36 µs total). The dataset includes the production trajectories in .xtc format, with frames recorded every 50 steps (1 step = 2 fs). The corresponding input and topology files are also included. Periodic boundary conditions can be restored using standard VMD commands. Due to Zenodo storage limitations, this dataset provides a subset of the full data set, containing the m134 and m162 trajectories.