Table 3. Kd values for ATP binding with mutant proteins were calculated using one-site saturation model from the binding data.
Kd (M) | R2 | |
---|---|---|
Interaction with ATP in the absence of DNA | ||
ADAAD* | (1.6 ± 0.5) × 10−6 | 0.98 |
F507A | (1.6 ± 0.4) × 10−6 | 0.98 |
F507W | (1.0 ± 0.3) × 10−6 | 0.98 |
S558A | (1.9 ± 0.4) × 10-6 | 0.95 |
T560A | (1.0 ± 0.3) × 10−6 | 0.99 |
R592A | (1.6 ± 0.6) × 10−6 | 0.98 |
H594A | (1.6 ± 0.2) × 10−6 | 0.98 |
R595A | (1.2 ± 0.2) × 10−6 | 0.96 |
R595K | (1.2 ± 0.2) × 10−6 | 0.97 |
D591H | (3.2 ± 0.3) × 10−6 | 0.97 |
H329D/D591H | (2.8 ± 0.1) × 10−6 | 0.98 |
F507A/R592A | (1.7 ± 0.1) × 10−6 | 0.99 |
R595H | (1.3 ± 0.2) × 10−6 | 0.98 |
Interaction with ATP in the presence of DNA | ||
ADAAD* | (0.14 ± 0.03) × 10−6 | 0.98 |
F507A | (0.45 ± 0.02) × 10−6 | 0.99 |
F507W | (0.22 ± 0.03) × 10−6 | 0.99 |
S558A | (0.36 ± 0.005) × 10−6 | 0.98 |
T560A | (0.22 ± 0.03) × 10−6 | 0.99 |
R592A | (0.24 ± 0.02) × 10−6 | 0.97 |
H594A | (0.09 ± 0.01) × 10−6 | 0.99 |
R595A | (0.11 ± 0.02) × 10−6 | 0.97 |
R595K | (0.11 ± 0.04) × 10−6 | 0.98 |
D591H | (0.21 ± 0.06) × 10−6 | 0.99 |
H329D/D591H | (0.24 ± 0.02) × 10−6 | 0.96 |
F507A/R592A | (0.24 ± 0.04) × 10−6 | 0.98 |
R595H | (0.23 ± 0.07) × 10−6 | 0.95 |
Data are presented as an average ± s.d. of three binding curves.
Reported in [24].