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Table 3 Disulfide bond prediction result of BlaR-CTD using Disulfide by Design 2.0

From: Analysis of the stability and affinity of BlaR-CTD protein to β-lactam antibiotics based on docking and mutagenesis studies

Location

Residue1

Residue2

Bond

Seq #

AA

Seq #

AA

χ3

Energy

ΣB-Factors

Ω-loop

 Flexible region of Ω-loop behind α7

135

SER

145

SER

−94.78

2.45

120

Between α helixs and β sheets

 β2 and before the flexible region of α1

19

SER

24

GLY

−68.19

3.71

113

 Between α3 and β2

28

GLY

47

SER

93.37

2.61

113

 β5 and behind the flexible region of α3

54

ALA

194

GLY

−68

8.54

120

 Between α4 and β5

56

THR

194

GLY

−106.37

8.44

113

 Between α8 and β7

153

GLN

221

ALA

−106.61

4.74

116

 Between α5 and α10

195

THR

232

GLY

−100.49

4.36

113

 Between β6 and α10

203

HIS

231

ALA

108.1

4.45

113

 Between β6 and α10

205

GLY

235

ALA

71.1

3.47

120

 Between β6 and α10

207

PHE

235

ALA

−107.6

4.95

113

 Between β7 and α10

222

VAL

239

ALA

106.21

4.13

113

Between α helixs

 Behind the flexible region of α3 and α7

50

ARG

147

GLN

−72.34

3.89

112

 α4 and behind the flexible region of α3

53

PRO

57

TYR

−103.61

3.27

106

 α4 and behind the flexible region of α7

57

TYR

141

TRP

−97.51

1.11

106

 Between α4 and α9

66

LEU

171

ASN

−96.08

2.58

109

 α5 and behind the flexible region of α4

76

SER

96

LEU

−81.41

2.69

113

 Behind the flexible region of α4

85

TYR

90

TRP

106.13

2.75

106

 α5 and behind the flexible region of α4

89

GLU

102

SER

112.89

5.87

109

 α5 and behind the flexible region of α4

95

ASP

98

SER

92.89

3.08

106

 Between α5 and α6

99

ALA

107

SER

−78.90

2.67

113

 α8 and behind the flexible region of α7

149

SER

152

GLU

121.50

3.56

109

Between β sheets

 Between β2 and β7

27

GLY

224

ILE

70.9

6.45

113

 Between β4 and β5

183

GLU

188

ILE

110.15

2.61

116

  1. Note: The boldface part indicated that the mutant AAs which selected in this study