Fig. 7: Predicted complexes between four additional kinetochore subunits in Arabidopsis thaliana.

Each panel shows the predicted complex and its Predicted Alignment Error (PAE) heatmap which reports the confidence in the relative positions of residue pairs (blue = high to yellow = low confidence/flexible). Blue off-diagonal blocks indicate confident inter-domain positioning (i.e. a well-defined interface). A AtESD4 (orange)-AtCSM1 (lilac). A disordered region of ESD4 (residues 91–116) is suggested to mediate the interaction. The PAE indicates medium overall confidence (ipTM = 0.35, score often underestimated with coiled-coils). B AtBUB3 (purple)-AtKNL1 (pink). Two disordered KNL1 segments (260–275 and 403–421) are predicted to contact BUB3 (ipTM = 0.76). The location of the MELT-binding site described in yeast is indicated for comparison. No interaction is predicted with AtBUB3/AtBMF1 (aquamarine). C AtBMF1/MAD3 (aquamarine)-AtCENP-C (brown). The TPR domain of MAD3 (residues 1–150) is predicted to bind a disordered N-terminal region of CENP-C (residues 15–74) (ipTM = 0.65) consistent with the PAE signal. D AtCENP-E (green)-BUB3 (purple). A coiled-coil region of CENP-E (residues 1200–1225) is predicted to interact with BUB3 (ipTM = 0.70) with a coherent high confidence in the PAE.