3LDI
crystal structure of aprotinin in complex with sucrose octasulfate: unusual interactions and implication for heparin binding
Total interactions analyzed 10
Total true interactions 6
Strongest Interaction Chains C-D
Int. Res. 35
Norm. En. per Res. -1.7739
Hub Node A(2)
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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 0.0 15.6869 -67.1693 -51.4824 39 2 3 3380 0 2 11
A-E 0.0 9.081 -66.9192 -57.8382 37 3 3 3234 0 2 11
B-C 0.0 16.0562 -73.3801 -57.3239 35 4 3 3428 0 2 11
B-D 0.0 0.0 -0.0004 -0.0004 2 0 0 1 0 0 2
C-D -12.8825 14.5859 -63.7897 -62.0863 35 4 3 3314 0 2 11
D-E 0.0 13.9454 -72.3331 -58.3877 33 3 3 3352 0 2 12