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Table 1 Predictions of harmful mutations: 22 mutations identified as possibly causing damage to protein function using our manual selection strategy.

From: VERMONT: Visualizing mutations and their effects on protein physicochemical and topological property conservation

Mutation

Avg. degree

Avg. betweenness

Avg. closeness (E-04)

Avg. accessibility

S19E

3.93

101.68

9.9

47.47

I20A

8.45

728.61

9.9

3.12

N28K

5.54

93.93

9.9

30.09

K56G

6.87

198.56

9.9

16.32

T60K

5.25

455.12

9.8

25.92

K69E

4.57

362.98

10.0

39.75

S71K

2.86

160.55

9.7

69.87

K89D

3.82

289.67

9.9

44.37

D111K

5.08

89.62

9.8

44.26

G118E

3.53

19.84

9.8

78.12

E152A

3.8

22.26

9.9

73.91

E153G

5.91

120.75

9.9

40.56

K155D

3.49

23.58

9.8

74.42

T158K

4.39

100.68

9.9

60.49

S194E

4.37

26.71

9.9

74.15

K195N

4.61

49.99

9.9

55.2

K199E

3.56

56.41

9.9

64.94

S202E

4.35

100.48

9.9

52.74

N213K

5.72

265.96

9.9

37.79

G214P

4.09

108.98

9.9

31.33

K221A

5.24

246.48

10.0

19.78

D222A

4.89

56.55

9.9

68.43

  1. Sequence numbering according to PDB ID 2YPI:A