Table 3. Binding affinities of LysM alanine mutants determined by SPR.
| LysM | KD (μM) | Residual binding (%) |
|---|---|---|
| WT | 11.7±1.7 | 100 |
| D12A | 72.0±15.2 | 16.2 |
| T13A | 730.2±83.1 | 1.6 (17.1) |
| L14A | 927.9±151.1 | 1.3 |
| N15A | 21.5±3.9 | 64.1 (50.0) |
| K16A | 13.1±1.2 | 89.3 |
| N32A | 15.8±2.3 | 74.0 |
| D37A | 138.3±14.2 | 10.0 |
| L38A | 145.5±27.7 | 12.4 (28.9) |
| I39A | 1,021±224.2 | 1.3 (1.6) |
| F40A | 54.0±12.0 | 25.5 (29.7) |
| V41A | 11.7±2.1 | 100.0 (50.1) |
GlcNAc5 was used as the analyte. Residual activity is the ratio of the apparent affinity to that of wild-type, obtained from surface plasmon resonance (SPR) or NMR (NMR values in brackets).