Table 2. HIS0 Interaction Scores for Fab (SFabα) and Fc (SFc) Fragmentsa.
| interaction type (α) | Eintα | HP | (SAA)Fc,avgi | (SAA)Fab,avgi | (SAA)exposedi | (SFcα)i | (SFabα)i |
|---|---|---|---|---|---|---|---|
| cation–π: | |||||||
| Arg | –8.193 | 12.9 | 12.5 | 2.22 | 47.7 | 46.1 | |
| Lys | –9.268 | 34.5 | 28.3 | 1.93 | 165.3 | 135.5 | |
| total (Sα) | 213 | 181.6 | |||||
| π–π stacking: | |||||||
| Phe | –0.093 | 4.7 | 2.5 | 1.9 | 0.2 | 0.1 | |
| Tyr | –0.098 | 9.4 | 9.5 | 2.0 | 0.5 | 0.5 | |
| Trp | –0.535 | 0.7 | 0.3 | 2.3 | 0.2 | 0.1 | |
| Arg | –2.402 | 12.9 | 12.3 | 2.2 | 14.0 | 13.3 | |
| total (Sα) | 15 | 14 | |||||
| h–π: | |||||||
| Phe | –2.735 | 4.7 | 2.5 | 1.9 | 6.8 | 3.6 | |
| Tyr | –2.599 | 9.4 | 9.5 | 2.0 | 12.3 | 12.4 | |
| Trp | –3.679 | 0.7 | 0.3 | 2.3 | 1.1 | 0.5 | |
| total (Sα) | 20.2 | 16.5 | |||||
| h-bonding: | |||||||
| Arg | –0.50 | 12.9 | 12.5 | 2.2 | 2.9 | 2.8 | |
| Asn | –0.27 | 17.7 | 8.4 | 1.4 | 3.5 | 1.7 | |
| Asp | –0.47 | 9.9 | 8.2 | 1.2 | 3.9 | 3.3 | |
| Gln | –0.25 | 17.6 | 11.2 | 1.6 | 2.7 | 1.7 | |
| Glu | –0.46 | 20.2 | 9.7 | 1.5 | 6.1 | 2.9 | |
| Lys | –0.22 | 34.5 | 28.3 | 1.9 | 3.9 | 3.2 | |
| Ser | –0.14 | 13.9 | 34.9 | 1.0 | 2.0 | 5 | |
| Thr | –0.05 | 9.7 | 19.3 | 1.2 | 0.4 | 0.8 | |
| His | –0.34 | 9.7 | 2.1 | 1.6 | 2 | 0.4 | |
| total (Sα) | 27.4 | 21.8 |
a
The interaction energies, Eintα (in kcal/mol), are taken from ref (41). α is the interaction type, and i refers to the amino acid type. HP is the residue hydrophobicity taken from the Black and Mold scale.42 (SAA)Fab,avg and (SAA)Fc,avg are the average solvent-accessible surface areas of different residue types in the Fab and Fc domain, respectively. (SAA)exposed is the solvent-accessible area for different residue types (i), calculated using the Ala–i–Ala tripeptide in pure water.