3BEF
crystal structure of thrombin bound to the extracellular fragment of par1
Total interactions analyzed 15
Total true interactions 9
Strongest Interaction Chains A-C
Int. Res. 16
Norm. En. per Res. -3.2989
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-B -126.0143 -67.8885 215.2 21.2972 119 41 4 20428 8 47 39
A-C -20.1998 0.0 -32.5832 -52.783 16 2 0 1325 0 3 4
A-E 0.0 -11.4335 -11.9154 -23.3489 19 0 0 769 0 26 28
B-C -16.0105 36.7056 -77.3816 -56.6865 36 12 0 3147 0 8 6
B-E 0.0 -23.5471 -39.3724 -62.9196 26 7 0 1576 1 12 16
C-E 0.0 0.0 -0.0406 -0.0406 2 0 0 16 0 1 1
D-E -118.0207 -56.3584 235.356 60.9768 119 40 4 19964 11 45 37
D-F -7.4145 0.0 -28.8244 -36.2389 11 1 0 1094 0 3 4
E-F -4.8762 0.0 -64.9422 -69.8184 28 6 0 2267 0 6 4