Fig. 1

3D structure diagram of protease PB92 （PDB∶1AH2）"

Fig. 2

The 3D structure diagram of protease PB92 before and after binding to the substrate after simulation （a means no substrate binding; b means substrate binding）"

Fig. 3

RMSD of protease PB92 binding substrate before and after simulation"

Fig. 4

Distribution of α-helix secondary structure before and after protease PB92 binding to substrate （1 indicates the distribution of α-helix secondary structure before protease PB92 binding substrate, 2 indicates the distribution of α-helix secondary structure after protease PB92 binding substrate）"

Fig. 5

Changes in α-helix content before and after the binding of protease PB92 to substrate （a. Amino acid No. 1 to 25; b. Amino acid No. 60 to 75; c. Amino acid No. 100 to 150; d. Amino acid No. 210 to 270; 1 indicates the change in α-helix content before protease PB92 binds to the substrate, 2 indicates the change in α-helix content after protease PB92 binds to the substrate）"

Tab. 1

Amino acids with significant changes in α-helix before and after protease PB92 substrate binding"

Fig. 6

The distribution of β-sheet secondary structure before and after protease PB92 binds to the substrate （1 represents the β-sheet secondary structure distribution before protease PB92 binds to the substrate, 2 represents the β-sheet secondary structure distribution after protease PB92 binds to the substrate）"

Fig. 7

The content of β-sheet before and after the binding of protease PB92 to the substrate （a. Amino acids No. 1 to 70; b. Amino acids No. 70 to 140; c. Amino acids No. 140 to 210; d. Amino acids No. 210 to 269; 1 represents the change in β-sheet content before protease PB92 binds to the substrate, 2 represents the change in β-sheet content after protease PB92 binds to the substrate）"

Tab. 2

Amino acids with significant changes in β-sheet before and after protease PB92 substrate binding"

Fig. 8

Local contact map of protease PB92 before and after binding substrate"