Table 3.
AP33 residues in close proximity to E2 peptide 8741
| AP33 residue | No. of contacts with peptide 8741a | Buried surface area (%)b |
|---|---|---|
| H chain | ||
| YH33 | 26 | 95.2 |
| YH50 | 16 | 73.5 |
| YH53 | 3 | 25.0 |
| YH58 | 24 | 40.7 |
| IH95 | 2 | 38.0 |
| TH97 | 8 | 46.1 |
| YH100 | 31 | 49.4 |
| L chain | ||
| YL28 | 39 | 46.3 |
| NL30 | 1 | 18.3 |
| FL32 | 18 | 58.1 |
| NL91 | 13 | 40.1 |
| NL92 | 30 | 78.0 |
| VL93 | 1 | 0 |
| DL94 | 2 | 20.8 |
| WL96 | 18 | 26.0 |
a
Atomic intermolecular contacts between AP33 Fab residues and the E2 epitope peptide 8741 were determined using the software program CONTACT, as implemented in the CCP4 suite (54). Atoms within 4.5 Å of each other were considered to be in contact.
b
Percent surface area of the AP33 residue that becomes buried upon complex formation with the peptide. Buried surface areas were calculated by the software program PISA (33).