3DPQ
crystal structure of the substrate binding domain of e. coli dnak in complex with a long pyrrhocoricin-derived inhibitor peptide (form b)
Total interactions analyzed 28
Total true interactions 11
Strongest Interaction Chains A-D
Int. Res. 59
Norm. En. per Res. -3.4112
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 -9.6093 -38.41 -48.5587 -96.5781 68 0 1 2757 3 48 50
A-C 0.0 7.1364 -22.0288 -14.8924 16 0 0 950 0 3 4
A-D -27.5522 0.0 -173.707 -201.2592 59 8 6 6641 0 8 6
B-F -10.6705 0.0 -65.9289 -76.5994 56 8 1 3236 1 7 12
B-C -11.5437 -10.9865 -159.152 -181.6822 58 8 6 6661 0 8 5
B-D 0.0 0.0 -4.0623 -4.0623 9 0 0 222 0 3 1
E-F -23.3958 7.8163 -57.1766 -72.7561 67 8 0 2848 3 48 51
E-G 0.0 -2.8357 -12.4994 -15.3351 15 1 0 934 0 3 4
E-H -12.1945 -11.2801 -166.758 -190.2326 58 6 5 6914 0 9 5
F-G -25.0468 0.0 -127.69 -152.7368 54 7 6 6264 0 7 4
F-H 0.0 0.0 -2.741 -2.741 8 0 0 134 0 2 1