This PDF file includes:

• table S1. X-ray data collection and refinement statistics for TPR2-TPD + D53 EAR-2 peptide complex structures.
• table S2. D53 EAR-2 peptide increases the average hydrodynamic radius of the TPR2 TPD.
• fig. S1. Sequence alignment of the EAR motifs of D53 homologs from monocots and dicots.
• fig. S2. Sequence alignment of the TPD from monocots and dicots.
• fig. S3. Interaction of D53 EAR-2 peptide with the TPDs of TPL, TPR1, and TPR2.
• fig. S4. Expression and protein loading controls.
• fig. S5. M2H interaction between EAR-3–containing D53 fragments and TPL proteins.
• fig. S6. Fo-Fc omit map of the bound EAR peptide contoured at 2σ in the binding pocket of the TPR2 TPD.
• fig. S7. Mutations in TPR2 TPD site 1 do not abolish binding of the D53 EAR motif.
• fig. S8. D53 EAR-2 peptide binds site 1 in TPR2 TPD site 2 mutation L179A/L195A.
• fig. S9. TPR2 TPD L111A/L130A/L179A/I195A fails to bind the D53 EAR-2 motif.
• fig. S10. Relative binding strength of wild-type and mutant D53 EAR-2 motif peptides.
• fig. S11. The D53 EAR-2 peptide does not change the stability of the TPR2 TPD.
• fig. S12. The EAR peptides of SMXL6, SMXL7, and SMXL8 do not induce TPR2 TPD tetramer-tetramer interaction.
• fig. S13. Analysis of GFP-D53 and GFP-D53/TPD complexes by fluorescencedetection SEC.
• fig. S14. D53 homology model.

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