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In both peptides, the N-terminal histidine sits in an enclosed pocket-forming hydrophobic and hydrogen bond interactions with E364 6.53 , E387 7.42 , R310 5.40 , Y241 3.44 , W306 5.36 , I313 5.43 and Q234 3.37 however, these interactions are more persistent with GLP-1, and this is likely linked to the stability of interactions of Glu9 and with residues at the base of the binding cavity (Supplementary Table 3, Supplementary Movie 1)

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