Table 4.
Structural positions of replacement mutations in mouse monoclonal 5S
| Position | Mutational motif | Mutability index | Probability of R | |
|---|---|---|---|---|
| Light chain | ||||
| Binding site | ||||
| Asn L28 to Tyr | CDR1 | 1·98 | 0·88 | |
| Asn L30 to Asp | CDR1 | 1·28 | 0·88 | |
| VH/VL interface | ||||
| Tyr L36 to His | FR2 | TAC | 1·78 | 0·85 |
| Leu L55 to Phe | CDR2 | 0·86 | 0·88 | |
| Solvent exposed, away from binding site | ||||
| Asp L70 to Glu | FR3 | 0·88 | 0·89 | |
| Tyr L87 to Phe | FR3 | 1·92 | 0·88 | |
| Solvent inaccessible, away from binding site | ||||
| Ser L25 to Ala | CDR1 | 1·22 | 0·66 | |
| Heavy chain | ||||
| Binding site | ||||
| Glu H50 to Thr | CDR2 | RGYW | 2·10 | 0·66 |
| Asn H54 to Ile | CDR2 | 0·89 | 0·88 | |
| Solvent exposed, away from binding site | ||||
| Val H12 to Ala | FR1 | 0·36 | 0·66 | |
| Lys H13 to Thr | FR1 | AANB | 1·52 | 0·87 |
| Thr H28 to Ser | FR1 | 0·93 | 0·66 | |
| Thr H30 to Ser | FR1 | WDCH | 1·40 | 0·66 |
| Ser H31 to Thr | CDR1 | RGYW | 1·39 | 0·88 |
| Gln H43 to Arg | FR2 | 0·78 | 0·87 | |
| Gln H81 to His | FR3 | DGHD | 0·91 | 0·87 |
| Ser H82a to Asn | FR3 | RGYW | 0·94 | 0·88 |
| Solvent inaccessible, away from binding site | ||||
| Val H18 to Leu | FR1 | DGHD | 0·94 | 0·66 |
| Met H34 to Ile | CDR1 | DGHD | 0·91 | 1·00 |
| Met H80 to Leu | FR3 | 1·34 | 1·00 | |
Residues up to FR3 are shown here.