2LPR
structural basis for broad specificity in alpha-lytic protease mutants
Total interactions analyzed 1
Total true interactions 1
Strongest Interaction Chains A-P
Int. Res. 37
Norm. En. per Res. -2.3058
Hub Node A(1)
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Weak Strong
Width of edge <-> No. of inter. res.
All Interactions
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Chains Hydro. Bond Ener. (kJ/mol) Elec. Ener. (kJ/mol) VDW. Ener. (kJ/mol) Tot. Stab. Ener. (kJ/mol) #int. res. # Short cont. #Hydr. int. #VDW pairs #salt bridges #Pot. fav. elec. int #Pot. unfav. elec. int int. res.
A-P -21.2389 0.0 -64.0751 -85.314 37 2 5 2282 0 0 0