Extended Data Fig. 7. β₁AR_6P–βarr1 and formoterol–β₁AR_6P contacts, and comparison with other complexes.

a, interactions between amino acid residues in β₁AR_6P and βarr1. The size of the circle depicting the residue is proportional to the number of van der Waals interactions (grey lines) and hydrogen bonds (red lines) made, with residues in circles outlined in black making potential hydrogen bonds. Secondary structure elements are shown with the total number of interactions they make. The thickness of lines making contacts is proportional to the number of contacts made. b, Residues are depicted in β₁AR_6P that make contact (≤3.9 Å) with βarr1 (red) and residues in β₂AR (PDB ID: 3SN6) that make contact to G_s (blue); purple residues make contacts in both structures. The sequence of turkey β₁AR is depicted. c, Residues in human rhodopsin that make contact with either visual arrestin or transducin (G_t). Plots were made using GPCRdb. d, The number of atomic contacts between the ligand formoterol and secondary structure elements in β₁AR is depicted; grey bars, β₁AR–Nb80 complex; blue bars, β₁AR_6P–βarr1 complex. Light regions correspond to the number of van der Waals interactions and dark regions correspond to the number of hydrogen bonds. Data for chain A and chain B in the crystal unit cell of the β₁AR–Nb80 complex are shown separately (A and B).