Table 3 |
||||||||||
| Pair energies in peptide binding pocket 1 | ||||||||||
| DP chain | position | aa | peptide position | aa | Etotal | Eatr | Erep | Esol | Ehbnd | Epair |
| A | 9 | Tyr | 1 | Phe | 0.02 | −0.4 | 0 | 0.41 | 0 | 0 |
| A | 24 | Phe | 1 | Phe | −0.46 | −0.45 | 0 | −0.01 | 0 | 0 |
| A | 32 | Phe | 1 | Phe | −1.69 | −1.64 | 0 | −0.05 | 0 | 0 |
| A | 43 | Trp | 1 | Phe | −0.01 | −0.13 | 0 | 0.12 | 0 | 0 |
| A | 52 | Phe | 1 | Phe | −0.39 | −0.42 | 0 | 0.04 | 0 | 0 |
| A | 53 | Ser | 1 | Phe | −0.88 | −0.50 | 0 | 0.33 | −0.71 | 0 |
| A | 54 | Phe | 1 | Phe | −0.75 | −1.50 | 0.41 | 0.34 | 0 | 0 |
| A | 55 | Glu | 1 | Phe | 0.01 | −0.01 | 0 | 0.02 | 0 | 0 |
| B | 80 | Asn | 1 | Phe | −0.12 | −1.52 | 0.03 | 1.38 | 0 | 0 |
| B | 83 | Leu | 1 | Phe | −0.11 | −0.15 | 0 | 0.04 | 0 | 0 |
| B | 84 | Gly | 1 | Phe | −0.17 | −0.21 | 0 | 0.04 | 0 | 0 |
| sum | −4.55 | −6.93 | 0.44 | 2.66 | −0.71 | 0 | ||||
Polymorphic residues are given in bold. Etot corresponds to the sum of all energies between the pair residues; Eatr and Erep are the Lennard – Jones attractive and repulsive energies, respectively; Esol – the solvatation energy; Ehbnd – energy of hydrogen bonding per residue; Epair – statistics-based pair term.
Patronov et al. BMC Structural Biology 2012 12:20 doi:10.1186/1472-6807-12-20
