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Table 3 Barnase (BN) – Barstar (BS) interaction: thermodynamic and kinetic data and ZD scores from docking simulations with interfacial water molecules

From: In silico screening of mutational effects on enzyme-proteic inhibitor affinity: a docking-based approach

BS

BN

log k d a

log k a

ΔG° (kcal/mol)

ΔΔG (kcal/mol)

Nsol

Best Rank

ZDbest

ZD-s

ZDsc

ZDel

ZDdes

wtb

wt

-5.43

8.57

-19.00

-

50

1

65.5

55.6

41.6

12.0

2.0

wt

H102A

-0.89

8.60

-12.90

6.10

49

1

63.3

53.0

39.4

11.1

2.6

Y29A

wt

-3.00

8.46

-15.60

3.40

53

1

60.4

52.7

40.1

11.0

1.6

Y29A

H102A

-0.82

8.56

-12.70

6.30

50

1

59.5

50.7

38.1

10.6

2.0

Y29F

wt

-5.62

8.48

-19.10

-0.10

52

1

63.1

54.5

41.8

10.1

2.6

Y29F

H102A

-1.35

8.59

-13.50

5.50

48

1

61.7

51.3

38.6

10.6

2.2

D39A

H102A

1.23

8.64

-10.10

8.90

50

1

60.4

48.6

37.8

6.8

4.0

wt

K27A

-2.35

7.71

-13.60

5.40

48

1

61.5

52.6

40.2

9.7

2.7

D39A

K27A

-0.17

7.76

-10.80

8.20

48

1

59.3

48.3

38.6

5.1

4.5

D35A

wt

-2.42

8.28

-14.50

4.50

50

1

58.2

51.4

38.9

9.7

2.8

E76A

wt

-4.68

8.30

-17.70

1.30

49

1

60.6

53.1

42.2

8.5

2.4

  1. aDetails and legend concerning the quantities reported herein were explained in Table 1.
  2. bExperimental data from [8] (Table 3) and [12] (Table 1)