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.《磷酸化位点拓扑结构调控抑制蛋白招募至G蛋白偶联受体（G protein-coupled receptors, GPCRs）的功能动态》相关分子动力学数据集 作者：蒂莫·米勒（Timo Müller）#、禹真李（Woojin Lee）#、阿萨特·巴伊切夫（Asat Baischew）、亚斯明·艾丁（Yasmin Aydin）、乔迪·洪·拉姆（Jordy Homing Lam）、法尔科·纳格尔（Falko Nagel）、安德里亚·辛茨（Andrea Sinz）、卡斯滕·霍夫曼（Carsten Hoffmann）、斯特凡·舒尔茨（Stefan Schultz）、弗谢沃洛德·卡特里奇（Vsevolod Katritch）*、艾琳·库安（Irene Coin）* 本数据集包含上述研究论文中，针对毒蕈碱型乙酰胆碱受体M2（M2R）与β抑制蛋白-1（arr2）复合物开展的分子动力学（molecular dynamics, MD）模拟数据。模拟从三种基于交联指导构建的原子级复合物模型（m134、m162及m181）启动，在脂质双分子层环境中开展无交联约束的非偏倚分子动力学模拟。每个初始模型均运行10组独立的1.2微秒重复模拟，单模型总模拟时长为12微秒，整体总模拟时长达36微秒。数据集包含.xtc格式的生产模拟轨迹，每50步记录一帧（1步=2飞秒），同时附带对应的输入文件与拓扑文件。可通过标准VMD命令恢复周期性边界条件。受限于Zenodo存储限制，本数据集仅提供完整数据集的子集，包含m134与m162的模拟轨迹。