Table 2A

ProMotif Summary

PDB code:1a4f

OXYGEN TRANSPORT MOL_ID: 1; MOL_ID: 1;

Chain A

Chain B

Number of residues is: 141

Number of residues is: 146

Number of strands is: 0

Number of strands is: 0

Number of alpha helices is: 7

Number of alpha helices is: 7

Number of 3,10 helices is: 1

Number of 3,10 helices is: 2

Secondary structure summary:

Secondary structure summary:

HTHGTTHTHHTHTHTT

HTHGHHTHHGHT

Helices: 8 examples

Helices: 10 examples

Beta Turns: 12 examples

Beta Turns: 4 examples

Gamma Turns: 2 examples

 

H=helix, T=turn, G=γ-turn.

Data adapted from ProMotif 

Table 2B

Chain A Secondary Structure: Summary

Topology: HTHGTTHTHHTHTHTT

Chain B Secondary Structure: Summary                                     

Topology: HTHGHHTHHGHT

Helices

  

B-Turns

    

G-Turns

  

Helices

  

B-Turns

    

G-Turns

  

Location

Type

Location

Seq

Type

Location

Type

Location

Type

Location

Seq

Type

Location

Type

4—17

H

17-20

LSGH

I

116-118

INV

5—15

H

77--80

NLDN

I

121-123

INV

21—35

H

18-21

SGHA

IV

138-140

INV

20-34

H

78--81

LDNI

IV

    

37-42

G

43-46

FPHF

I

    

36-42

G

142--145

ARKY

I

    

57-30

H

49-52

QHGS

II

    

43-45

G

143--146

RKYH

IV

    

76-79

H

70-73

VNHI

IV

    

51-55

H

          

81-88

H

72-75

HIDD

I

    

58-76

H

          

96-112

H

73-76

IDDI

IV

    

81-94

H

          

119-135

H

113-116

HPSA

I

    

101-118

H

          
   

114-117

PSAL

I

    

119-121

G

          
   

115-118

SALT

IV

    

124-141

H

          
   

137-140

TAKY

IV

                  
   

138-141

AKYR

IV

                  

H=helix, G=310-helix

Table 2C
Chain A Secondary Structure: Details

Helices

Helix No.

Start

End

Type

Residues

Length

Rise

Res/Turn

Pitch

Deviation

Sequ

1

4

17

H

14

21.13

1.51

3.56

5.39

10.2

AADKTNVKGVFSKI

2

21

35

H

15

22.27

1.45

3.75

5.45

6.3

AEEYGAETLERMFTA

3

37

42

G

6

11.5

1.91

3.15

6

6.9

PQTKTY

4

53

70

H

18

27.74

1.51

3.62

5.46

8.1

AQIKAHGKKVVAALVEAV

5

76

79

H

4

6.26

1.46

3.75

5.48

38.5

IAGA

6

81

88

H

8

12.33

1.5

3.75

5.64

14

SKLSDLHA

7

96

112

H

17

26.64

1.56

3.59

5.58

4.4

VNFKFLGHCFLVVVAIH

8

119

135

H

17

25.86

1.5

3.58

5.37

10

AEVHASLDKFLCAVGTV

H=helix, G=310-helix

B-turns

         

Residue I +1

  

Residue I +1

    

Start

End

Sequ

Turn Type

Phi

Psi

Chi1

Phi

Psi

Chi1

Cadist

Hbond

17

20

ISGH

I

-58.3

-22.6

-131.4

-82.8

-15.4

-

5.6

YES

18

21

SGHA

IV

-82.8

-15.4

-

-129

43.4

-35.7

6.1

NO

43

46

FPHF

I

-58.9

-30.4

33.5

-84.5

5.4

56.4

5.4

YES

49

52

QHGS

II

-47.4

134.4

172.7

69.2

13.9

-

5.2

YES

70

73

VNHI

IV

-61.6

-19.1

-66.8

-133.7

34

-74.2

4.9

YES

72

75

HIDD

I

-51.1

-19

-153.1

-78.5

-23.2

-70.8

5.6

YES

73

76

IDDI

IV

-78.5

-23.2

-70.8

-159.5

77.2

167.8

5.2

NO

113

116

HPSA

I

-51.6

-49.7

12.1

-70.4

-21.2

70.2

5.5

YES

114

117

PSAL

I

-70.4

-21.2

70.2

-75.3

-32

-

5.1

NO

115

118

SALT

IV

-75.3

-32

-

-84.8

66.8

-162.9

6.1

NO

137

140

TAKY

IV

-50.9

-35.1

-

-81

46.5

-87.1

6

NO

138

141

AKYR

IV

-81

46.5

-87.1

-135.3

-35

-78.4

5.6

YES

G-Turns

         

Residue I +1

    

Start

End

Sequ

Turn Type

Phi

Psi

Chi1

Cadist

Hbond

116

-

118

ALT

INVERSE

-84.8

66.8

-162.9

5.9

138

-

140

AKY

INVERSE

-81

46.5

-87.1

5.2

  
Table 2D
Chain B Secondary Structure: Details

Helices

Helix No.

Start

End

Type

residues

Length

Rise

Res/Turn

Pitch

Deviation

Sequ

9

5

15

H

11

17.19

1.51

3.69

5.56

7.9

AEEKQLITGLW

10

20

34

H

15

21.99

1.44

3.78

5.42

7.6

VADCGAEALARLLIV

11

36

42

G

7

12.19

1.75

3.39

5.95

18.2

PWTQRFF

12

43

45

G

3

-

-

-

-

-

SSF

13

51

55

H

5

7.74

1.43

3.59

5.11

21.8

PTAIL

14

58

76

H

19

29.55

1.53

3.57

5.47

9.8

PMVRAHGKKVLTSFGDAVK

15

81

94

H

14

20.51

1.43

4.22

6.05

31.7

IKNTFAQLSELHCD

16

101

118

H

18

27.61

1.52

3.62

5.51

6.2

ENFRLLGDILIIVLAAHF

17

119

121

G

3

-

-

-

-

-

AKE

18

124

141

H

18

27.18

1.49

3.63

5.42

9.4

PDCQAAWQKLVRVVAHAL

H=helix, G=310-helix

B-Turns

         

Residue I +1

  

Residue I +1

    

Start

End

Sequ

Turn Type

Phi

Psi

Chi1

Phi

Psi

Chi1

Cadist

Hbond

77

80

NLDN

I

-55.9

-10.8

-61.7

-105.5

-16.8

-61.8

5.4

YES

78

81

LDNI

IV

-105.5

-16.8

-61.8

-106.4

37

-175.5

5.9

NO

142

145

ARKY

I

-61.6

-32.3

122.3

-81.7

12.8

-115.5

5.4

YES

143

146

RKYH

IV

-81.7

12.8

-115.5

-86.9

23.1

-93.1

6.3

NO

G-Turns

         

Residue I +1

  

Start

End

Sequ

Turn Type

Phi

Psi

Chi1

Cadist

121

123

EFT

INVERSE

-87.9

84

-167.6

5.4