Superposition of 3hvp and 2hvp Helix present in 3hvp but missing from 2hvp N-terminal residues 1-5 ordered in 3hvp Loop is different in the 2 structures.

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Superposition of 3hvp and 2hvp Helix present in 3hvp but missing from 2hvp N-terminal residues 1-5 ordered in 3hvp Loop is different in the 2 structures 2hvp: Nevia et al., hvp: Wlodawer et al., 1989

Outliers in 2hvp Outliers in 2hvp: 8 ARG (-17.0, 125.9) 20 LYS (160.8, 176.9) 39 PRO (-55.8, ) 40 GLY (-25.4, ) 44 PRO (-104.0, 121.1) 49 GLY (160.8, 93.8) 50 ILE (44.7, 93.4) 52 GLY (138.7, -96.2) 8 Arg 20 Lys

Conformational changes due to inhibitor binding 1 Flap movement upon inhibitor binding Inhibitor binding asymmetry introduced

Protease bound to inhibitor inhibitor Flap-like loops PDB ID 4hvp, Miller et al., 1989

Conformational changes due to inhibitor binding 2 Asymmetry introduced in loop (residues 77-82) due to asymmetric inhibitor N-acetyl-Thr-Ile-Nle-T[CH2-NH]-Nle-Gln-Arg.amide Nle-R-Nle Asymmetric regions of inhibitor Val82