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Association Energy Data for 5a7a



Click on the data column titles for details on the calculated properties(Caution*)

Interface Symmetry Association Energy (kcal/mol)Buried Surface Area2)Solvation Energy (kcal/mol)Relative Strength (Percentage of strongest association energy)
A1-A54I-21-86.64097.0-16.9100%
A1-A53I-21-86.64099.3-16.9100%
A1-A33I-105-24.21313.1-1.8 28%
A1-R1Q-0-10.2826.6-3.7 12%
A1-R32Q-0-4.6450.11.5 5%
A75-R1Q-0-4.6449.91.5 5%
A74-R1Q-0-2.9452.5-3.3 3%
A1-R33Q-0-2.9452.3-3.3 3%
A1-A75I-27-0.4354.90.9 0%
A1-A32I-27-0.4355.00.9 0%


*Word of caution: The association and solvation energies shown in the table above were calculated based the buried surface areas and atomic solvation parameters (See References below). They may not match (quantitatively) the experimental values. However, we strongly believe that the relative energies, i.e., strengths of the interfaces is reflected in these numbers. So use them with caution especially while comparing with the experimental values.

Eisenberg, D., and McLachlan, A. D. (1986). Solvation energy in protein folding and binding. Nature 319(6050), 199-203.
Horton, N., and Lewis, M. (1992). Calculation of the free energy of association for protein complexes 1(1), 169-181.
Reddy, V. S., Giesing, H. A., Morton, R. T., Kumar, A., Post, C. B., Brooks, C. L., 3rd, and Johnson, J. E. (1998). Energetics of quasiequivalence: computational analysis of protein-protein interactions in icosahedral viruses. Biophys J 74(1), 546-58.



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