FIG 5.

Divergent presentations of RLI9/MVM9 peptides presented by Anpl-UAA*01. (A and B) Electron densities and overall conformations of the structurally defined peptides RLI9 and MVM9. Simulated annealing omit maps (CNS) calculated for the two peptides are shown in blue at a contour of 1.5, and the coloration of the two peptides is according to the isotropic B factors. (C) General side chain orientations and the different interfacing areas of RLI9/MVM9 presented by Anpl-UAA*01 PBG, as viewed in profile from the peptide N terminus toward the C terminus. Black arrows indicate the directions in which the residues point: up is toward the T cell receptor, down is toward the floor of the peptide binding groove, left is toward the α1 helix domain, and right is toward the α2 helix domain. Pockets accommodating each residue are listed under the corresponding anchors within the peptide binding groove. ASA, accessible surface area of each residue; BSA, buried surface areas of the residues.