FR is a close analog of YM: The atomic coordinates of YM were retrieved from the crystal structure of Gαq in the inactive state [Protein Data Bank (PDB) ID, 3ah8 (19)] and transformed to the structure of active Gαq in complex with PLC-β3 [PDB ID, 3ohm (23)] by superimposition of the backbone atoms of the two proteins using a mean square distance optimization method, as previously described (50). To model FR, the ligand was modified by adding and removing the appropriate atoms and locally minimized using MOE (Molecular Operating Environment, version 2016) using the AMBER 10 force field (51).

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