Fig. 3.

All-atom MD simulations of the active-state human β₂AR–G_s with NE(+) bound based on Anton runs. (A) run 1 with the Top Inset. (B) run 2 with the Bottom Inset  Final structures are captured from the 5-μs–long unbiased MD simulation runs. Individual protein chains/subunits are labeled and shown in the ribbon representation using different colors. G_sα α5 helix and β₂AR intracellular loop 3 (ICL3) are colored in yellow and dark gray, respectively. C_α atoms of residues A161 on G_sαAH domain and E299 on G_sαRas domain are shown as blue and green balls, and distances between them are shown by light-blue dashed arrows. The quantification of the interactions between ICL3 and α5 helix can be found in SI Appendix, Table S3. The geometric centers were used for the distance measurements. The common Gα numbering (CGN) numbers (D381^G.H5.13, D378^G.H5.10, N377^G.H5.9, R374^G.H5.6, R385^G.H5.17) for residues in G_sα α5 as well as A161^H.HD.5 and E299^G.HG.6 are omitted in the figure for clarity.