Design for the UUKV-N protein mutations based on multiple alignments and 2D- and 3D-structure predictions.(A) Jpred alignment shows the N- and C-termini of N proteins among five members in the genus Phlebovirus. α-helix-forming aa residues are shadowed. Point mutations for the UUKV-N protein were targeted to the aromatic and hydrophobic aa residues. (B) Robetta server's ab initio model for the UUKV-N protein: the first two predicted α-helices in N-terminus are shown in blue, and the C-terminus is shown in green. (C) The N-terminal part of the Robetta model (Fig. 3B) showing the residues presumably involved in the oligomerization (except Y33 facing outside of the α-helices).