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. 2018 Jun 27;38(3):BSR20180568. doi: 10.1042/BSR20180568

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].