TRACeR-I modeling involved global docking, high-resolution RifDock, and Rosetta sequence design. Combinatorial libraries were constructed, yeast-displayed, and screened. Binder proteins were expressed, purified, and characterized. CD, BLI, and peptide library methods were used. Recombinant MHC proteins were expressed, refolded, and biotinylated. Tetramer libraries were prepared, and peptide exchange validated. SSM scanning and sequence-based selection identified cross-reactive peptides. Immunogenicity assays, IFNγ ELISpot, flow cytometry, and bispecific-induced cytotoxicity assays were performed. X-ray crystallography determined the TRACeR–pMHC I complex structure. Sequence conservation analysis and structural modeling were conducted. Ethical approvals and reporting summary are included.