Science Advances

This PDF file includes:

• Fig. S1. Concentration-response relationship of HmK blockade of KcsA-Shaker.
• Fig. S2. Effect of mutation KcsA-Shaker–Y82V on block by TEA and HmK.
• Fig. S3. Hui1-Arg²³ mediates the voltage-dependent block of KcsA-Shaker.
• Fig. S4. Structures of HmK, ShK, and Hui1 toxins noting some important, conserved residues.
• Table S1. Single-particle counting and calculation of effective T-HmK surface concentration.
• Table S2. Single-particle counting and calculation of effective T-HmK surface concentration with coexpression of KcsA-Shaker channels.
• Table S3. Blocking parameters of hKv1.3 by T-HmK, T-ShK, and the analogous free peptide variants.
• Table S4. ¹H chemical shifts of HmK.
• Table S5. Heteronuclear chemical shifts of HmK.
• Table S6. Statistics for HmK structure calculation.

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