1LK2
1.35a crystal structure of h-2kb complexed with the gnysfyal peptide
Total interactions analyzed 3
Total true interactions 2
Strongest Interaction Chains A-P
Int. Res. 83
Norm. En. per Res. -3.7465
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 -66.2286 -15.3515 -395.448 -477.0281 132 14 2 13235 1 41 38
A-P -43.4163 0.0 -267.543 -310.9593 83 12 4 8882 0 0 0