1SPS
binding of a high affinity phosphotyrosyl peptide to the src sh2 domain: crystal structures of the complexed and peptide-free forms
Total interactions analyzed 15
Total true interactions 5
Strongest Interaction Chains A-F
Int. Res. 15
Norm. En. per Res. -3.9863
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-D -11.6224 -5.5719 -84.3249 -101.5193 39 5 2 3215 0 15 6
A-C -6.9908 -11.0853 -27.1362 -45.2123 22 0 0 1327 0 9 11
A-F -16.4132 0.0 -43.3814 -59.7946 15 3 2 1574 0 0 1
B-E -13.5422 -6.0949 -68.2239 -87.861 38 8 2 2992 1 14 6
C-F -10.7907 -11.885 -78.9713 -101.6469 40 7 2 3082 2 15 6