Table 1.

Summary of interface composition and binding free energy calculations of the most stable complex models.

Complex (Subject-Partner)	Model	Interface composition		Binding free energy (kcal/mol)
		Subject (left)	Partner (right)
ADORA1-ADORA1	Noncry	TM3 (E)	Identical	9.15 ± 0.24
ADORA1-Iso_3TM	CP-6	TM4, TM2 (E), TM3 (E)	TM2, TM1, TM3 (E)	-133.94 ± 0.25
ADORA1-Iso_4TM	AF-1	TM1, TM3 (E), TM4 (I)	TM4	-111.64 ± 0.18
	AF-3	TM1, TM2	TM4	-115.60 ± 0.39
mGlu2-mGlu2	Inactive	TM4, TM3(E)	Identical	-61.06 ± 0.35
	Active	TM6, TM7 (E)	Identical	-43.55 ± 0.13
mGlu2-Iso_2TM	LD-15	TM4, TM2, TM3 (E)	TM7, TM6	-163.79 ± 0.26
	CP-H10	TM7, TM6, TM1	TM6, TM7	-192.07 ± 0.32
SMO-SMO		TM4, TM5	Identical	-69.66 ± 0.13
SMO-Iso_3TM	LD-34	TM4, TM5	TM4, TM5	-95.90 ± 0.34

Note: The content of “Interface composition” is ordered by the contribution to the interface formation and only TM helices are shown. For example, “TM7, TM1, TM6” indicates TM7 > TM1 > TM6 in terms of contact contribution. E, the extracellular side-facing part of the helix; M, the middle part of the helix; I, the intracellular side-facing part of the helix. No parenthesis indicates that the majority of this helix is involved in the interface composition. “AF-1” denotes the Rank 1 model generated by AlphaFold-Multimer; “LD-12” denotes the No.12 model generated by LightDock; “CP-12” denotes the No.12 model generated by ClusPro with the default Balanced mode, and “CP-H12” denotes the No.12 model generated by ClusPro with the Hydrophobic-favored mode. Isoforms are displayed in the abbreviated forms without the prefix. For example, “mGlu2-Iso_2TM” denotes the complex formed by mGlu2 and its truncated isoform with two transmembrane helices. The numbering of transmembrane helices in truncated isoforms corresponds to their numbering in the full-length counterparts. Binding free energy values are shown as mean ± standard error of the mean (SEM).