Table 3 Predicted experimental values and comparative binding free energies for wild-type and alanine mutants.

From: Alanine mutation of the catalytic sites of Pantothenate Synthetase causes distinct conformational changes in the ATP binding region

Systems

Isothermal titration microcalorimetry results

MM-GBSA

Ka(x104 M−1)

−∆G (kcal mol−1)

−∆H (kcal mol−1)

−T∆S (kcal mol−1)

Pre-MD (kcal mol−1)

Post-MD (kcal mol−1)

Wild-type

22.4 ± 1.6

7.3

14.2 ± 0.2

6.9

−29.71

−26.61

H44A

—

—

—

—

−29.97

−21.70

H47A

2.46 ± 0.11

6.0

7.2 ± 0.2

1.2

−28.56

−20.76

N69A

9.1 ± 0.4

6.8

13.0 ± 0.23

6.1

−30.39

−22.33

Q72A

13.2 ± 0.29

7.0

13.1 ± 0.46

6.2

−32.00

−27.28

K160A

0.45 ± 0.02

5.0

8.4 ± 0.3

3.4

−25.24

−17.93

Q164A

13.2 ± 0.29

7.0

17.3 ± 0.1

10.3

−30.49

−26.47

  1. “—”: not predicted.
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