Fig. 3

AA’s appearing in the most significant rules marked on the 3D structures of different proteins. AA residues appearing in the rules are shown as spheres. Positions from the high pathogenicity rules are shown in blue, positions from the low pathogenicity rules are in magenta and mutations associated with the shift of pathogenicity from low to high as defined by the rules are shown in red. a Mapping of amino acid positions associated with pathogenicity from the rules onto 3D structure of the HA protein of Influenza A virus (A/Hubei/1/2010 (H5N1)) (PDB: 4KTH). Chain A (HA1 residues) and chain B (HA2 residues) are presented in green, while the rest of the trimer is shown in gray. b A cartoon representation of chains A, B, C and D of the NA protein with AA positions from the rules (PDBID: 2HU4). Chain A, the one marked with rule positions, is shown in green and the others in gray. Residue R-371, shown as a sphere in orange, is a part of the catalytic site of the protein. Cyan spheres constitute Oseltamivir 2, a substrate bound to the protein. c A cartoon representation of the NP protein trimer (PDBID: 2IQH) with positions from the rules. Chain A is shown in green and the others are in gray. d AA’s from the rules marked on a cartoon representation of NS1 (PDBID: 3FST). e A cartoon representation of the PB2 protein cap-binding domain (PDBID: 4CB4) with AA’s from the rules