3S1A
crystal structure of the phosphorylation-site double mutant s431e/t432e of the kaic circadian clock protein
Total interactions analyzed 15
Total true interactions 11
Strongest Interaction Chains C-D
Int. Res. 315
Norm. En. per Res. -3.4595
Hub Node B(4)
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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 -115.7468 -126.2549 -767.021 -1009.0227 330 84 4 34005 17 143 133
A-E 0.0 0.0 -0.0322 -0.0322 2 0 0 15 0 0 0
A-F -145.8342 -184.1286 -790.618 -1120.5808 332 76 4 33820 20 143 133
B-C -112.029 -154.7935 -812.604 -1079.4265 318 60 4 34053 15 133 123
B-D 0.0 0.0 -0.0296 -0.0296 2 0 0 16 0 0 0
B-E 0.0 0.0 -0.0027 -0.0027 2 0 0 3 0 0 0
B-F 0.0 0.0 -0.003 -0.003 2 0 0 4 0 0 0
C-D -125.1596 -144.1963 -820.397 -1089.7529 315 66 5 34504 17 138 124
C-E 0.0 0.0 -0.0108 -0.0108 2 0 0 6 0 0 0
D-E -153.1447 -112.704 -815.147 -1080.9957 317 65 5 34017 13 135 122
E-F -123.0696 -121.4197 -794.16 -1038.6493 315 64 4 33254 14 132 122