TABLE 1.
%ASA of candidate residues for mutagenesis
ΔASA = %ASA(monomer) − %ASA(dimer). % of ASA was calculated with the program MOE (Chemical Computing Group).
Interface residues | %ASA (dimer) | %ASA (monomer) | ΔASA |
---|---|---|---|
Gln347a | 26.5 | 41.8 | 15.4 |
Tyr349 | 5.1 | 41.4 | 36.3 |
Leu351 | 3.8 | 41.9 | 38.0 |
Ser354 | 13.6 | 60.2 | 46.6 |
Asp356 | 47.9 | 74.4 | 26.5 |
Glu357 | 2.8 | 26.9 | 24.1 |
Lys360 | 42.7 | 62.9 | 20.2 |
Ser364a | 3.8 | 18.5 | 14.8 |
Thr366a | 0.7 | 21.2 | 20.5 |
Leu368a | 1.4 | 15.2 | 13.8 |
Lys370 | 17.1 | 37.3 | 20.0 |
Asn390a | 39.9 | 55.6 | 15.7 |
Lys392 | 42.8 | 77.6 | 34.9 |
Thr394 | 2.5 | 42.7 | 40.2 |
Val397 | 13.6 | 42.3 | 28.7 |
Ser400 | 56.7 | 89.2 | 32.5 |
Asp401a | 14.0 | 32.4 | 18.5 |
Phe405a | 0 | 24.2 | 24.2 |
Tyr407a | 0 | 37.3 | 37.3 |
Lys409a | 1.5 | 50.5 | 48.9 |
Lys439 | 27.9 | 41.3 | 13.4 |
Ser444 | 56.8 | 68.8 | 12.0 |
a The positions selected for N-glycosylation engineering.