Table 2. Kd values for DNA binding with mutant proteins were calculated using one-site saturation model from the binding data.
| Kd (M) | R2 | |
|---|---|---|
| Interaction with DNA in the absence of ATP | ||
| ADAAD* | (19.9 ± 4.9) × 10−9 | 0.96 |
| F507A | (19.0 ± 4.5) × 10−9 | 0.98 |
| F507W | (44.8 ± 9.0) × 10−9 | 0.96 |
| S558A | (11.0 ± 2.7) × 10−9 | 0.99 |
| T560A | (6.8 ± 0.6) × 10−9 | 0.96 |
| R592A | (31.5 ± 1.3) × 10−9 | 0.98 |
| H594A | (10.9 ± 2.6) × 10−9 | 0.99 |
| R595A | (24.0 ± 0.6) × 10−9 | 0.96 |
| R595K | (25.1 ± 7.4) × 10−9 | 0.91 |
| D591H | (21.3 ± 7.0) X 10−9 | 0.96 |
| H329D/D591H | (16.1 ± 5.7) × 10−9 | 0.96 |
| F507A/R592A | (27.8 ± 3.6) × 10−9 | 0.95 |
| R595H | (24.3 ± 6.1) × 10−9 | 0.94 |
| Interaction with DNA in the presence of ATP | ||
| ADAAD* | (3.4 ± 0.2) × 10−9 | 0.97 |
| F507A | (32.8 ± 6.0) X 10−9 | 0.98 |
| F507W | (14.0 ± 2.2) × 10−9 | 0.98 |
| S558A | (13.8 ± 2.2) × 10−9 | 0.92 |
| T560A | (1.4 ± 0.3) × 10−9 | 0.97 |
| R592A | (6.4 ± 1.1) × 10−9 | 0.92 |
| H594A | (6.6 ± 0.9) × 10−9 | 0.95 |
| R595A | (7.5 ± 1.5) × 10−9 | 0.96 |
| R595K | (7.9 ± 2.1) × 10−9 | 0.87 |
| D591H | (6.9 ± 1.4) × 10−9 | 0.90 |
| H329D/D591H | (9.9 ± 2.2) X 10−9 | 0.90 |
| F507A/R592A | (9.4 ± 0.9) × 10−9 | 0.92 |
| R595H | (10.1 ± 0.3) × 10−9 | 0.93 |
Data are presented as an average ± s.d. of three binding curves.
*
Reported in [24].