The structural basis of peptide binding to mammalian major histocompatibility complex (MHC) class I molecules is well understood [8] . The peptide-binding groove is formed by the a1 and a2 domains. Each domain contributes four strands to an eight -stranded anti-parallel b-sheet. Two long interrupted helices, one from each domain, pack against the side of this sheet in an orientation directed away from the cell membrane. There is a series of pockets (A-F) along the peptide-binding groove where highly polymorphic amino acids mediate recognition via haplotype-specific associations with antigens and T cell receptors. However, highly conserved residues are found at both ends of the peptide-binding groove that form a network of hydrogen bonds, which directly interact with hydrogen bonds at the peptide's Nterminus and C-terminus [9] [10] [11] . Peptides that bind to MHC class I molecules are usually octamers or nonamers, where only one or a few residues can interact with polymorphic residues in the groove. These residues are known as anchor residues when they are found in an anchoring position [12] [13] [14] [15] . Several public databases and prediction services are available for MHC molecular ligands and peptide motifs, including SYFPEITHI and RANKPEP [16, 17] .