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In both structures the 14.C6 and J809.B5 CDR3α loops make similar types of contacts with the peptide. Despite the 14.C6 CDR3α loop being one amino acid longer, the J809.B5 CDR3α loop extends 2.5Å further towards the peptide, relative to the 14.C6 CDR3α loop. Because of the different CDR3α loop conformations, a steric clash would occur between the J809.B5 CDR3α loop and the peptide if this TCR bound IAb-3K with the same geometry as that of the 14.C6 TCR. Thus, the differences in CDR3α loop conformation likely underlie why the J809.B5 and 14.C6 TCRs bind IAb-3K with different tilts. The most prominent differences in how the J809.B5 and 14.C6 TCRα chains engage IAb-3K involve CDR1α and CDR2α residues.
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