Fig. 6. MD simulations highlight residues that stabilize N_LRS oligomers.

Shown are snapshots from the MD simulations for the trimer (A) and tetramer (B). The cores of the oligomers are formed by five nonpolar residues in a well-packed configuration (left column of each panel). More specific interactions stabilizing the complex surfaces are (right column of each panel): a hydrophobic surface cluster formed by four leucine residues, two salt bridges (R226-E231 and K233-E231), and an H-bond interaction between polar (N228) and charged (R226) residues. Helix backbones drawn as gold ribbons; interacting residues rendered as atom-based Van der Waals spheres (nonpolar residues in gray; polar and charged residues in color: white, H; red, O; gray, C; blue, N). G215 is shown in green for reference.