Supplemental Material Figure legends
S1: Initial characterization of A1LS and  JR2LS. A) 1H-15N HSQC of A1LS before and after redox buffer.   Magenta contours show purified A1LS in PBS buffer.  The blue contours show A1LS following incubation with reduced and oxidized glutathione (2 and 0.5 mM respectively).  New peaks following treatment are labeled. B) TALOS secondary structure prediction for A1LS based on backbone and side-chain chemical shifts. The two helical regions of the predicted α-hairpin fold are clearly identifiable. C) 1H-15N-NMR spectrum of FL JR2 LS displaying numerous well-dispersed peaks consistent with an alpha-helical protein. D) Circular dichroism spectra of indicated hairpinin and the table below showing the percentage of a-helices, b-sheets and random coils within each.
S2: Additional NMR characterization of J2LS fragments.Predicted secondary structure of JR2 VBPs as calculated based on the backbone and side chain NMR chemical shifts using the TALOS algorithm.
S3: Additional NMR data . A) Data table showing various parameters relating to the NMR structure determination and validation of A1pro and JR2 LS fragments. B) Cysteine CB chemical shift values for all four constructs. Values indicate that all cystines are involved in disulfide bonds.
S4:  Surface comparison with distant VBP’s. A) NMR structure of VBP-8; and B) BWI-2C VBP’s from tomato and buckwheat respectively. Spade surface-similarity comparison with immunodominant A1LS and JR2.1. shown below, revealing areas of high surface similarity despite the lack of known tomato-nut and buckwheat-nut cross-reactivity . PDB ID: 6O3S, 2LQX