3TDZ
n-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: structure of a human cul1whb- dcn1p-stapled acetylated ubc12n complex
Total interactions analyzed 15
Total true interactions 7
Strongest Interaction Chains A-C
Int. Res. 66
Norm. En. per Res. -4.8879
Hub Node A(3)
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-C -79.2889 -79.4872 -163.825 -322.6011 66 12 0 6120 6 53 28
A-D -2.2986 2.1004 -28.0445 -28.2427 33 3 0 1298 0 9 5
A-E -34.7072 -73.2806 -98.1696 -206.1575 49 20 7 4737 3 14 1
C-B 0.0 0.0 -0.0606 -0.0606 3 0 0 9 0 2 3
C-D 0.0 0.0 -14.03 -14.03 18 0 0 709 0 4 6
B-D -60.1133 -83.2582 -142.004 -285.3754 60 6 0 5820 6 52 27
B-F -25.9541 -25.5323 -108.743 -160.2293 51 7 6 4562 2 14 2