5 A GLY 0.45 0.41 0.90 0.1
   6 A LEU 0.38 0.70 0.86 0.1
   7 A PRO 0.56 0.47 0.85 0.1
   8 A PRO 0.82 0.47 0.77 0.1
  32 A ARG 0.51 0.51 0.78 0.1
  36 A LEU 0.64 0.70 0.85 0.1
  84 A ASN 0.90 0.39 0.83 0.1
  85 A ALA 0.45 0.38 0.89 0.1
  86 A LEU 0.77 0.70 0.90 0.1
  87 A GLY 0.91 0.41 0.85 0.1
 100 A TYR 0.48 0.80 0.39 1.0
 106 A PRO 0.70 0.47 0.22 0.6
 108 A HIS 0.27 0.60 0.47 0.6
 110 A LEU 0.39 0.70 0.45 1.0
 142 A GLN 0.64 0.43 0.36 1.0
 143 A TYR 0.77 0.80 0.52 1.0
 151 A TRP 0.76 0.99 0.48 1.0
 154 A ILE 0.49 0.64 0.48 0.2
 155 A PRO 0.64 0.47 0.55 0.2
 166 A PHE 0.67 1.00 0.53 0.2
 180 A ARG 0.67 0.51 0.33 1.0
 182 A ARG 0.74 0.51 0.14 1.0
 188 A GLY 0.79 0.41 0.35 0.5
 190 A GLY 0.84 0.41 0.15 1.0
 191 A TYR 0.36 0.80 0.05 1.0
 192 A TRP 0.91 0.99 0.11 1.0
 195 A TRP 0.83 0.99 0.24 1.0
 196 A SER 0.86 0.36 0.30 1.0