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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