Fig. 6: Structure of the pMHC-TCR ternary complex.

a Kinetics of soluble TCR-47BE7 binding to immobilised H2-D^b/Hsf2 p.K72N as determined by biolayer interferometry. The dissociation constant (K_D) was determined by curve fitting in Octet® 9.1 System Data Analysis software. b Structural superimposition of TCR-47BE7/H2-D^b/Hsf2 p.K72N_68-76 (7NA5) and H2-D^b/Hsf2 p.K72N_68-76 (7N9J) structures. (Inset) Superposition of the corresponding Hsf2 p.K72N_68-76 peptides. c Residue-specific solvent-accessible surface area (SASA) in unbound/binary (grey) and bound/ternary (blue) structures were calculated using NACCES⁸⁹. d TCR footprint on pMHC (inter-atomic distance cutoff 4 Å). En face view of H2-D^b/Hsf2 p.K72N_68-76 with superimposed TCR-47BE7 CDR loops with residues as sticks. H2-D^b interface is coloured according to observed CDR1ɑ-CDR3ɑ (orange), CDR1β-CDR3β (red), or no TCR contact (white). Peptide interface is coloured blue. e TCR-pMHC interface distribution between components. f Distribution of inter-atomic interface contacts between TCR and pMHC, distance cutoff 8 Å. Computed by NACCESS, as described in Methods. g Interface H2-D^b (green) and peptide (blue) residues, stick models. Inter-atom distance cutoff 4 Å. h The interface between bound neoepitope and TCR-47BE7 in the pMHC-TCR structure in cartoon model. The polar bonds are depicted as dotted lines. Only the TCR residues that are in direct contact (<4 Å distance) with epitope atoms are shown as sticks. i Interface between Hsf2 p.K72N_68-76 (atoms presented as VDW spheres) and TCR-47BE7 (the protein surface was coloured according to the TCR chains). One alternate conformation for pR₄ was excluded for clarity. Source data are provided as a Source Data file.