Structural model of MT7-dimeric hM1 complex based on experimental double mutant cycle data. A, restraint energy as a function of r.m.s.d. from the MT7-hM1 dimer for about 30,000 calculated complexes obtained by five independent docking simulations (supplemental Table 1). The reference structure was the lowest energy structure. The r.m.s.d. was calculated using the Cα atoms of MT7 and hM1 dimer excluding the extracellular loops. B, histogram of the averaged minimum distances between residue pairs with ΔΔGint >0.7 kcal/mol and involved in ambiguous distance restraints (a) and with ΔΔGint <0.7 kcal/mol and not used in the docking calculations (b). C and D, two perpendicular views of a superimposed ribbon representation of the 10 best structures. E and F, two perpendicular views of a schematic of the lowest restraint energy model. hM1A, hM1B, and MT7 are in red, blue, and green, respectively. hM1 loops are in cyan except E2, which is in magenta.