(A) The modeled structures of almost full-length FcγRIIB (232I and 232T, residues A46-I310, shown in gray cartoon) are complexed with IgG Fc (using the complex structure of IgG Fc and FcγRIIB ectodomain, PDB ID: 3WJJ as a reference, shown in color shaded surface) and imbedded in an asymmetric lipid bilayer (lines with atoms colored by element type: P, tan; O, red; N, blue; C, cyan). The helical structures in the vicinity of residue 232 for 232I (green) and 232T (blue) are shown in the insets. (B) Probability distributions of the distance between T232 Oγ atom and its nearest backbone O atom from residue V228 (left), and of the tilting angles between TM helix and lipid bilayer (right). The inclination of TM for 232T can be observed clearly. Blue dashed line in the upper inset of the left panel indicates H-bond. (C) The representative snapshot comparison of 232I and 232T at the stalk and TM region by superposing the lipid bilayers (left), and the length distribution of S218-P221 backbone in normal direction of lipid bilayer (right). (D) Conformational comparison of I212-S220 regions by aligning residues S218 to S220 (left), and the time courses of the dihedral angles (ψ, φ) of residue P217 (right). (E) Representative snapshots of 232I and 232T with the inclination angles and C1(Ig-like C2-Type one domain)/bilayer distances, probability distributions of the inclination angle between FcγRIIB ectodomain and lipid bilayer (left), and the distances between C1 domain and lipid bilayer (right).