3FOA
crystal structure of the bacteriophage t4 tail sheath protein, deletion mutant gp18m
Total interactions analyzed 6
Total true interactions 5
Strongest Interaction Chains B-C
Int. Res. 80
Norm. En. per Res. -1.3726
Hub Node A(2)
Click on the Nodes or Edges in the network to see the details
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 0.0 -20.7238 -20.7238 33 7 2 1019 0 7 7
A-C 0.0 0.0 -1.2737 -1.2737 17 0 0 240 0 7 10
B-C -7.4257 0.3049 -102.687 -109.8078 80 19 0 5388 1 34 38
B-D 0.0 6.0281 -25.4685 -19.4404 45 0 2 1807 0 17 19
C-D 0.0 0.0 -0.0166 -0.0166 3 0 0 2 0 0 0