3K0F
crystal structure of the phosphorylation-site double mutant t426a/t432a of the kaic circadian clock protein
Total interactions analyzed 15
Total true interactions 11
Strongest Interaction Chains A-F
Int. Res. 325
Norm. En. per Res. -3.6714
Hub Node B(4)
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 -127.6062 -174.2002 -821.131 -1122.9374 328 62 8 34533 18 138 122
A-E 0.0 0.0 -0.0253 -0.0253 2 0 0 14 0 0 0
A-F -144.3845 -179.3391 -869.492 -1193.2156 325 55 6 34583 21 144 121
B-C -122.8706 -198.9922 -796.104 -1117.9668 315 62 5 33338 15 137 116
B-D 0.0 0.0 -0.0405 -0.0405 2 0 0 18 0 0 0
B-E 0.0 0.0 -0.0031 -0.0031 2 0 0 4 0 0 0
B-F 0.0 0.0 -0.0048 -0.0048 2 0 0 5 0 0 0
C-D -142.1021 -176.8043 -795.594 -1114.5003 309 70 5 33635 15 136 116
C-E 0.0 0.0 -0.0106 -0.0106 2 0 0 6 0 0 0
D-E -136.3102 -164.9394 -797.113 -1098.3626 312 53 5 32943 16 130 109
E-F -133.8267 -170.1581 -737.411 -1041.3957 306 55 5 31928 16 130 107