3GJS
caspase-3 binds diverse p4 residues in peptides
Total interactions analyzed 15
Total true interactions 10
Strongest Interaction Chains C-D
Int. Res. 165
Norm. En. per Res. -5.076
Hub Node A(4)
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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-B -171.2901 -22.3166 -649.709 -843.3158 170 31 14 23576 3 42 37
A-C -12.9359 -12.4807 -62.3991 -87.8157 40 1 0 2678 0 23 13
A-D -57.5997 4.3852 -97.4227 -150.6371 39 10 2 3333 0 9 11
A-E 0.0 0.0 -3.8252 -3.8252 18 0 0 359 0 0 0
B-C -56.112 10.2647 -101.192 -147.0394 40 9 2 3517 0 6 10
B-D -65.2365 -68.007 -411.301 -544.5445 110 11 8 15860 4 42 32
B-E -23.1627 0.0 -86.5506 -109.7133 26 3 3 2906 0 0 0
C-D -163.7874 -16.8027 -656.958 -837.5481 165 39 13 24347 2 38 29
C-F 0.0 0.0 -3.532 -3.532 18 0 0 313 0 0 0
D-F -20.3021 0.0 -81.2505 -101.5526 28 6 3 2852 0 0 0