Protein Data Bank File : 1e0sa Title : G PROTEIN 06-APR-00 1E0S Number of Amino Acid Residues : 173 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY LYS VAL LEU SER LYS ILE PHE GLY ASN 10 LYS GLU MET ARG ILE LEU MET LEU GLY LEU 20 ASP ALA ALA GLY LYS THR THR ILE LEU TYR 30 LYS LEU LYS LEU GLY GLN SER VAL THR THR 40 ILE PRO THR VAL GLY PHE ASN VAL GLU THR 50 VAL THR TYR LYS ASN VAL LYS PHE ASN VAL 60 TRP ASP VAL GLY GLY GLN ASP LYS ILE ARG 70 PRO LEU TRP ARG HIS TYR TYR THR GLY THR 80 GLN GLY LEU ILE PHE VAL VAL ASP CYS ALA 90 ASP ARG ASP ARG ILE ASP GLU ALA ARG GLN 100 GLU LEU HIS ARG ILE ILE ASN ASP ARG GLU 110 MET ARG ASP ALA ILE ILE LEU ILE PHE ALA 120 ASN LYS GLN ASP LEU PRO ASP ALA MET LYS 130 PRO HIS GLU ILE GLN GLU LYS LEU GLY LEU 140 THR ARG ILE ARG ASP ARG ASN TRP TYR VAL 150 GLN PRO SER CYS ALA THR SER GLY ASP GLY 160 LEU TYR GLU GLY LEU THR TRP LEU THR SER 170 ASN TYR LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 -100.4 171.8 2 LYS -59.7 -41.9 169.8 -67.9 -173.0 166.9 -178.8 3 VAL -62.0 -52.0 177.2 -86.1 4 LEU -61.2 -36.5 177.9 -78.6 -169.1 5 SER -64.3 -37.3 179.2 -133.1 6 LYS -75.2 -37.7 -178.8 -162.7 170.7 -178.3 171.7 7 ILE -73.9 -52.6 180.0 -63.8 177.9 8 PHE -84.0 -40.2 -176.7 -68.5 -48.2 9 GLY 59.1 -136.2 175.6 10 ASN -104.8 22.3 -179.0 -57.4 -53.3 11 LYS -68.4 144.2 -176.9 -68.5 164.2 -144.4 -154.8 12 GLU -99.4 119.0 177.7 -52.7 173.0 -54.0 13 MET -150.5 140.5 -178.8 24.9 -170.0 -27.0 14 ARG -114.1 117.2 -167.4 -70.9 176.7 -79.4 -105.0 15 ILE -129.7 137.3 166.6 -63.7 164.2 16 LEU -102.7 135.6 172.2 -65.0 -179.2 17 MET -120.0 107.7 -175.1 175.8 163.3 84.5 18 LEU -124.5 168.8 176.0 -50.4 176.3 19 GLY 164.5 165.7 173.7 20 LEU -59.9 162.3 173.2 -59.5 174.4 21 ASP -59.2 142.1 178.8 56.0 -68.5 22 ALA 76.7 3.7 179.9 23 ALA -65.9 -30.0 178.2 24 GLY 126.4 16.8 -174.9 25 LYS -64.6 -49.7 177.2 -56.8 179.4 -64.9 -61.4 26 THR -56.7 -43.7 -179.2 -65.1 27 THR -62.0 -43.1 176.7 -50.6 28 ILE -56.5 -47.8 -179.3 -66.5 177.7 29 LEU -64.9 -43.4 175.6 -59.9 168.2 30 TYR -59.3 -36.7 179.4 -77.0 -26.5 31 LYS -68.9 -37.8 175.7 -111.4 -80.6 132.9 127.9 32 LEU -77.3 2.4 -179.1 -57.5 172.2 33 LYS 72.8 16.4 176.3 -52.9 -63.3 -157.5 -57.3 34 LEU -85.9 69.0 -172.4 -54.7 -173.4 35 GLY -76.6 -30.3 179.9 36 GLN -95.7 148.9 176.6 -66.8 -69.9 -43.9 37 SER -155.2 172.0 176.7 64.1 38 VAL -119.6 126.2 179.0 -170.6 39 THR -94.3 131.6 168.6 -48.8 40 THR -120.5 144.3 179.3 -59.7 41 ILE -124.6 86.7 -175.1 -54.7 177.7 42 PRO -68.5 -22.2 171.5 -21.9 38.1 43 THR -156.4 152.1 -178.4 -171.1 44 VAL -52.1 123.3 178.5 -176.6 45 GLY 94.1 -9.8 175.8 46 PHE -107.0 101.2 -179.1 177.1 46.4 47 ASN -101.3 125.9 179.3 -51.5 -55.7 48 VAL -113.3 128.5 173.3 177.4 49 GLU -103.8 132.5 177.3 -67.9 -66.8 -11.3 50 THR -117.1 126.7 176.5 -54.7 51 VAL -117.8 127.9 169.3 178.6 52 THR -100.5 139.1 167.6 69.5 53 TYR -137.1 104.6 -177.1 177.1 81.7 54 LYS 56.1 -114.7 179.6 -55.7 -114.6 -87.8 179.5 55 ASN -100.6 14.7 174.6 -66.7 -43.2 56 VAL -102.3 138.4 169.6 -174.5 57 LYS -129.6 125.6 171.1 -175.6 -177.6 -79.6 175.6 58 PHE -102.9 137.3 161.2 -60.6 77.4 59 ASN -112.3 136.6 -172.8 -71.0 108.7 60 VAL -134.1 134.7 174.0 -177.3 61 TRP -160.4 157.5 175.2 66.1 84.8 62 ASP -76.5 133.4 165.5 -63.3 -19.4 63 VAL -91.8 -175.4 -179.4 -61.0 64 GLY 87.2 6.9 -178.1 65 GLY -79.9 -169.6 171.7 66 GLN -58.9 137.4 177.6 -81.7 163.7 -77.1 67 ASP -49.6 -34.5 -177.7 -69.0 12.9 68 LYS -67.1 -16.0 -179.8 68.9 -179.4 -164.6 177.6 69 ILE -92.1 -8.7 -177.6 69.7 159.5 70 ARG -58.3 -36.2 176.3 -60.8 -173.8 173.2 143.1 71 PRO -58.7 -35.2 178.8 -36.3 46.2 72 LEU -67.9 -21.7 -178.9 -59.3 179.9 73 TRP -65.8 -35.5 -178.5 -68.9 -2.2 74 ARG -69.6 -7.2 171.7 69.0 -176.4 -41.3 -72.4 75 HIS -66.2 -15.8 -176.5 -64.4 -170.8 76 TYR -105.3 4.7 -173.9 -67.9 -85.2 77 TYR -86.2 -36.1 -175.8 -62.8 -12.7 78 THR -59.5 123.8 -178.8 -0.7 79 GLY 84.1 -3.8 176.2 80 THR -69.4 120.2 -178.3 -59.6 81 GLN -100.4 -21.5 -179.0 47.0 -142.3 108.8 82 GLY -141.1 132.4 169.7 83 LEU -108.9 125.4 168.6 -179.8 69.3 84 ILE -107.2 120.5 -178.0 -58.9 172.1 85 PHE -117.2 120.1 -175.5 -164.8 84.6 86 VAL -101.4 129.4 -176.4 -174.6 87 VAL -124.2 135.6 171.5 -176.3 88 ASP -83.7 110.4 -178.9 179.0 -18.3 89 CYS -75.0 -14.3 174.1 -59.4 90 ALA -83.6 -10.1 -178.0 91 ASP -101.5 80.7 -173.9 -173.3 -1.7 92 ARG -64.3 -28.1 179.5 -67.3 178.7 174.7 -91.8 93 ASP -72.7 -21.0 179.1 -71.0 -44.0 94 ARG -109.0 7.2 177.1 -69.5 -157.1 -61.5 168.7 95 ILE -62.5 -36.1 175.5 -169.1 62.4 96 ASP -69.3 -33.2 174.9 -155.8 69.5 97 GLU -70.4 -38.4 176.3 -170.2 -175.3 -2.9 98 ALA -62.8 -40.2 174.7 99 ARG -57.5 -54.5 176.2 180.0 -176.1 57.5 82.5 100 GLN -59.1 -40.8 173.6 -71.4 -179.1 31.6 101 GLU -61.6 -45.8 179.3 -64.0 -74.6 73.0 102 LEU -57.6 -47.5 -174.9 177.4 60.3 103 HIS -72.1 -32.1 170.0 -77.5 -84.9 104 ARG -57.7 -43.7 -179.0 -92.2 165.2 -141.3 162.0 105 ILE -69.1 -52.2 -176.7 -60.9 160.2 106 ILE -72.7 -12.9 174.6 63.0 -177.8 107 ASN -85.7 -13.0 170.9 -74.5 -34.0 108 ASP -58.5 140.8 177.6 -169.5 -75.4 109 ARG -44.8 -44.5 -174.9 -84.3 -175.2 -72.1 132.5 110 GLU -84.8 -2.3 179.3 -154.3 79.0 75.8 111 MET -111.0 11.9 -175.2 -71.3 -62.2 -78.2 112 ARG -60.4 -28.0 -179.5 -79.0 174.5 -80.3 166.1 113 ASP -111.7 9.3 177.4 55.4 35.3 114 ALA -76.1 135.1 169.3 115 ILE -75.6 155.6 -174.6 61.9 172.3 116 ILE -118.1 115.4 166.3 -52.2 156.1 117 LEU -94.8 123.7 167.6 174.7 59.0 118 ILE -96.9 124.7 161.4 -48.5 -58.6 119 PHE -86.1 107.2 175.2 -79.9 -58.6 120 ALA -84.2 87.2 -164.6 121 ASN -89.8 160.4 178.0 -165.5 38.4 122 LYS 69.3 37.1 175.7 -45.4 -162.4 -168.3 173.0 123 GLN -59.9 -18.8 178.6 -70.6 -66.1 -61.7 124 ASP -78.5 -15.7 -177.1 62.2 -57.1 125 LEU -82.2 150.0 -177.2 -69.8 -177.8 126 PRO -51.7 122.9 178.8 -31.8 39.2 127 ASP 55.7 37.0 172.8 -155.3 34.5 128 ALA -65.9 140.3 171.0 129 MET -63.2 135.9 -177.9 -61.1 -172.8 -85.9 130 LYS -81.2 158.7 178.8 -68.2 -70.0 173.8 162.8 131 PRO -46.4 -42.5 -175.6 -28.7 36.3 132 HIS -71.9 -33.2 171.9 -77.0 96.9 133 GLU -75.9 -31.9 172.1 54.7 -167.4 -49.3 134 ILE -59.7 -40.7 173.5 -72.0 -63.4 135 GLN -52.9 -40.8 -176.8 -70.4 177.3 -161.6 136 GLU -82.2 -42.9 -177.2 -169.9 -161.5 -10.7 137 LYS -66.7 -31.5 179.5 -93.2 138.0 -169.3 -174.9 138 LEU -89.0 4.4 178.4 -70.1 179.0 139 GLY 69.3 25.2 -175.5 140 LEU -77.1 -33.0 178.4 -56.7 178.5 141 THR -54.1 -30.0 178.7 -69.4 142 ARG -91.2 -3.1 176.8 83.5 -156.5 -177.2 -155.9 143 ILE -87.8 101.9 179.3 -64.7 173.7 144 ARG -99.7 -4.8 -171.4 -47.5 147.7 -160.7 167.3 145 ASP -91.0 -12.1 -178.2 85.7 -41.9 146 ARG -153.7 166.8 179.9 101.7 -105.2 -49.1 -94.6 147 ASN -81.6 131.9 -178.0 -165.2 -167.2 148 TRP -144.8 159.3 178.6 58.6 -96.9 149 TYR -154.9 141.5 175.8 -179.7 79.9 150 VAL -107.9 117.5 178.8 -178.0 151 GLN -106.5 115.2 170.8 176.9 63.2 61.4 152 PRO -62.3 138.4 178.1 32.1 -40.8 153 SER -146.3 159.1 170.7 61.9 154 CYS -134.0 90.9 -168.1 -68.5 155 ALA -65.3 -30.9 177.8 156 THR -62.3 -33.8 178.4 48.0 157 SER -105.6 -1.0 177.9 47.2 158 GLY 86.0 2.7 -177.1 159 ASP -72.1 136.5 175.6 -60.3 89.8 160 GLY 82.4 -10.6 -174.5 161 LEU -69.3 -53.7 176.3 -52.2 -177.6 162 TYR -61.6 -34.6 176.2 -64.8 -71.7 163 GLU -64.2 -42.8 178.1 -65.6 75.4 4.6 164 GLY -65.0 -44.3 -179.3 165 LEU -69.7 -25.0 178.2 -65.5 174.2 166 THR -73.5 -38.0 174.6 -67.0 167 TRP -60.7 -46.5 -173.2 -180.0 85.6 168 LEU -64.2 -46.8 178.6 -173.9 80.1 169 THR -66.1 -36.4 176.5 59.1 170 SER -74.0 -15.5 -173.8 -57.3 171 ASN -116.4 -9.4 -177.9 -79.5 -80.6 172 TYR -75.5 154.7 179.3 95.9 -71.3 173 LYS -130.7 -20.3 0.0 -71.1 -154.6 162.7 -58.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 3.378 -3.264 61.029 2 LYS 5.999 -5.700 62.395 3 VAL 8.676 -3.192 61.383 4 LEU 6.788 -0.189 62.922 5 SER 6.025 -2.266 65.979 6 LYS 9.714 -3.029 66.484 7 ILE 10.824 0.577 65.917 8 PHE 8.133 2.422 67.939 9 GLY 6.978 -0.318 70.345 10 ASN 4.944 1.163 73.161 11 LYS 7.130 4.318 73.299 12 GLU 5.469 7.639 73.920 13 MET 6.378 10.349 71.430 14 ARG 5.054 13.616 70.069 15 ILE 6.442 14.361 66.646 16 LEU 6.014 17.095 64.064 17 MET 6.589 16.216 60.418 18 LEU 6.897 19.409 58.357 19 GLY 8.215 20.624 55.043 20 LEU 7.201 22.681 52.012 21 ASP 4.358 21.496 49.837 22 ALA 5.407 18.690 47.526 23 ALA 8.378 17.652 49.758 24 GLY 6.938 14.116 50.056 25 LYS 5.025 14.077 53.430 26 THR 1.818 12.353 52.294 27 THR 3.905 9.681 50.396 28 ILE 5.995 8.925 53.483 29 LEU 2.831 8.245 55.489 30 TYR 1.279 6.057 52.757 31 LYS 4.457 4.022 52.480 32 LEU 4.518 3.281 56.195 33 LYS 0.818 2.134 55.815 34 LEU -0.335 5.043 58.035 35 GLY -3.316 5.497 55.779 36 GLN -5.849 7.016 58.193 37 SER -5.645 10.469 59.736 38 VAL -7.599 13.284 61.312 39 THR -7.773 16.686 59.636 40 THR -8.081 19.925 61.592 41 ILE -8.426 23.322 59.853 42 PRO -7.537 26.043 62.450 43 THR -7.966 28.750 59.770 44 VAL -8.977 28.600 56.067 45 GLY -6.170 27.180 53.977 46 PHE -4.158 25.830 56.915 47 ASN -4.662 22.045 57.015 48 VAL -3.232 19.861 59.788 49 GLU -3.159 16.070 59.637 50 THR -2.847 14.143 62.891 51 VAL -1.882 10.487 62.901 52 THR -1.912 8.274 65.992 53 TYR -0.014 5.001 66.196 54 LYS -0.276 3.454 69.681 55 ASN 1.481 5.991 72.022 56 VAL 2.916 7.970 69.093 57 LYS 1.291 11.091 67.648 58 PHE 2.320 12.913 64.454 59 ASN 1.095 16.371 63.482 60 VAL 1.807 17.226 59.834 61 TRP 1.446 20.443 57.800 62 ASP 3.019 22.348 54.933 63 VAL 5.302 25.205 55.749 64 GLY 6.001 28.039 53.283 65 GLY 2.529 29.574 53.722 66 GLN 1.448 33.173 54.392 67 ASP 3.241 34.932 57.193 68 LYS -0.038 35.615 58.992 69 ILE -0.558 31.901 59.794 70 ARG 2.834 31.577 61.534 71 PRO 1.381 32.449 65.050 72 LEU -0.965 29.484 64.725 73 TRP 1.928 27.034 64.237 74 ARG 3.140 27.351 67.791 75 HIS -0.089 25.824 69.143 76 TYR 1.534 22.520 68.122 77 TYR 4.932 23.024 69.785 78 THR 4.436 22.214 73.491 79 GLY 5.725 18.757 74.359 80 THR 7.136 18.136 70.867 81 GLN 10.216 15.975 71.176 82 GLY 11.086 15.250 67.555 83 LEU 10.972 17.301 64.413 84 ILE 11.073 15.529 61.054 85 PHE 11.731 18.016 58.302 86 VAL 11.221 16.669 54.779 87 VAL 13.089 18.359 51.926 88 ASP 12.779 17.817 48.163 89 CYS 16.436 17.569 47.123 90 ALA 15.550 18.044 43.434 91 ASP 14.019 21.479 44.068 92 ARG 17.130 23.626 44.171 93 ASP 15.225 26.890 43.869 94 ARG 13.334 26.445 47.157 95 ILE 16.195 25.113 49.355 96 ASP 16.858 28.588 50.759 97 GLU 13.155 28.986 51.667 98 ALA 13.248 25.532 53.320 99 ARG 16.340 26.730 55.324 100 GLN 14.566 29.874 56.587 101 GLU 11.401 27.911 57.500 102 LEU 13.437 25.348 59.469 103 HIS 15.350 27.928 61.502 104 ARG 12.140 29.828 62.181 105 ILE 10.661 26.639 63.748 106 ILE 13.639 25.489 65.876 107 ASN 14.292 29.055 67.154 108 ASP 10.922 29.176 68.834 109 ARG 11.140 29.155 72.608 110 GLU 9.141 25.955 72.906 111 MET 11.249 24.074 70.311 112 ARG 14.637 24.482 72.039 113 ASP 15.037 20.761 72.849 114 ALA 13.540 18.832 69.867 115 ILE 16.063 16.750 67.936 116 ILE 15.954 17.172 64.136 117 LEU 15.635 14.350 61.554 118 ILE 15.943 15.634 57.942 119 PHE 14.500 13.422 55.215 120 ALA 16.672 14.449 52.192 121 ASN 13.979 13.169 49.886 122 LYS 13.804 12.390 46.132 123 GLN 17.414 11.166 45.871 124 ASP 16.327 9.278 42.736 125 LEU 15.622 12.497 40.785 126 PRO 18.029 14.174 38.240 127 ASP 20.721 16.173 39.932 128 ALA 19.190 15.918 43.444 129 MET 21.314 17.440 46.194 130 LYS 23.143 14.867 48.254 131 PRO 22.867 14.555 52.108 132 HIS 26.199 16.329 52.604 133 GLU 25.301 19.370 50.575 134 ILE 21.881 19.491 52.307 135 GLN 23.720 19.701 55.670 136 GLU 25.442 22.850 54.468 137 LYS 22.537 24.314 52.509 138 LEU 20.106 23.998 55.436 139 GLY 22.684 25.642 57.765 140 LEU 22.886 22.528 59.995 141 THR 26.703 22.557 60.167 142 ARG 26.451 25.733 62.298 143 ILE 23.867 24.246 64.760 144 ARG 26.033 23.263 67.745 145 ASP 23.241 23.387 70.341 146 ARG 21.388 20.153 69.498 147 ASN 21.422 16.710 67.928 148 TRP 20.472 16.399 64.230 149 TYR 20.826 13.866 61.329 150 VAL 20.241 13.843 57.557 151 GLN 18.777 10.647 56.122 152 PRO 18.739 10.275 52.286 153 SER 15.399 8.892 51.179 154 CYS 13.266 7.865 48.236 155 ALA 9.789 7.907 49.696 156 THR 8.156 6.415 46.585 157 SER 10.108 3.184 46.916 158 GLY 10.436 3.297 50.722 159 ASP 14.259 3.700 50.860 160 GLY 15.744 5.359 53.975 161 LEU 12.398 5.690 55.850 162 TYR 12.813 2.936 58.467 163 GLU 16.507 3.957 58.908 164 GLY 15.501 7.569 59.588 165 LEU 12.806 6.569 62.062 166 THR 15.273 4.243 63.854 167 TRP 17.593 7.257 64.313 168 LEU 14.715 9.341 65.747 169 THR 13.476 6.735 68.213 170 SER 17.033 5.857 69.389 171 ASN 17.909 9.509 69.982 172 TYR 14.746 11.117 71.405 173 LYS 14.462 11.989 75.137 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H C S 10 S S S S S S/S S S S S 20 C C C H H H H H H H 30 H H H C S S S S S S 40 S S T T T T/S S S S S 50 S S S/T T T T/S S S S S 60 S S S S C T T T T H 70 H H H 3 3 3 3 C S S 80 S S/S S S S S S S C C 90 C C C H H H H H H H 100 H H H H H H H H/T T T 110 T S S S S/S S S S S S 120 C C C C C C C C C H 130 H H H H H H H H H/T T 140 T T C C C S S S S S 150 S S S S/T T T T/S S S S/H 160 H H H H H H H H H H 170 H H/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H H h T 10 t E E E E E E E E 20 e T t h H H H H H H 30 H h T t E E E 40 E E E T T E E E E E 50 E E E T e E E E E E 60 E E E S g G G h H 70 H H H h G G g T T t 80 e E E E E E E E e T 90 g G G h H H H H H H 100 H H H H H H h g G G 110 G g T t E E E E E E 120 E t T T t T T t h 130 H H H H H H H h g G 140 G G g S S e E E E 150 E E e B T T T T B h 160 H H H H H H H H H H 170 H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 82.7 2 LYS 0.0 0.0 88.8 3 VAL 41.0 34.5 71.5 4 LEU 144.9 98.0 36.3 5 SER 41.5 49.6 77.2 6 LYS 5.1 3.0 89.3 7 ILE 119.9 83.5 52.5 8 PHE 166.7 99.9 25.5 9 GLY 14.7 42.4 76.7 10 ASN 31.5 26.0 83.7 11 LYS 86.5 49.9 72.2 12 GLU 18.8 13.5 83.6 13 MET 159.1 99.8 29.9 14 ARG 66.9 32.0 77.6 15 ILE 143.5 100.0 33.7 16 LEU 146.1 98.8 36.2 17 MET 157.8 99.0 27.1 18 LEU 147.8 100.0 33.6 19 GLY 34.8 100.0 48.3 20 LEU 134.9 91.3 54.2 21 ASP 45.2 40.9 80.8 22 ALA 15.6 21.5 90.0 23 ALA 70.6 97.2 57.0 24 GLY 23.6 67.8 67.8 25 LYS 162.6 93.8 52.8 26 THR 24.3 22.7 72.2 27 THR 61.1 57.2 54.4 28 ILE 140.4 97.9 29.0 29 LEU 132.3 89.5 36.8 30 TYR 60.7 33.5 74.6 31 LYS 91.5 52.8 74.0 32 LEU 144.5 97.7 34.0 33 LYS 23.3 13.4 92.0 34 LEU 131.4 88.9 37.3 35 GLY 11.2 32.1 68.3 36 GLN 0.0 0.0 92.0 37 SER 58.7 70.2 60.8 38 VAL 17.4 14.6 85.2 39 THR 60.3 56.4 71.2 40 THR 42.2 39.5 69.9 41 ILE 63.7 44.4 71.8 42 PRO 98.3 79.0 55.7 43 THR 57.4 53.7 59.2 44 VAL 0.0 0.0 83.3 45 GLY 1.7 4.9 78.9 46 PHE 161.6 96.9 39.0 47 ASN 49.8 41.2 65.4 48 VAL 118.3 99.6 46.6 49 GLU 84.5 61.0 64.3 50 THR 84.4 79.0 57.5 51 VAL 114.6 96.5 42.7 52 THR 36.0 33.6 70.1 53 TYR 138.5 76.5 48.4 54 LYS 77.1 44.5 82.0 55 ASN 52.4 43.3 68.7 56 VAL 118.7 99.9 45.7 57 LYS 78.7 45.4 66.1 58 PHE 164.1 98.4 28.6 59 ASN 98.4 81.4 43.4 60 VAL 109.5 92.2 36.9 61 TRP 200.5 97.8 33.0 62 ASP 49.8 45.0 69.8 63 VAL 118.8 100.0 36.8 64 GLY 31.3 90.0 65.2 65 GLY 9.7 28.0 72.0 66 GLN 30.5 20.5 76.7 67 ASP 27.1 24.5 85.7 68 LYS 31.1 17.9 80.2 69 ILE 122.1 85.1 44.2 70 ARG 143.5 68.7 66.7 71 PRO 41.2 33.1 74.1 72 LEU 100.6 68.1 55.2 73 TRP 197.3 96.2 46.9 74 ARG 131.9 63.1 72.5 75 HIS 46.8 31.2 71.3 76 TYR 138.3 76.4 49.2 77 TYR 174.3 96.3 40.1 78 THR 29.2 27.3 85.8 79 GLY 5.3 15.4 80.6 80 THR 102.2 95.6 52.9 81 GLN 121.4 81.7 62.4 82 GLY 34.8 100.0 41.5 83 LEU 147.8 100.0 28.7 84 ILE 142.2 99.1 26.7 85 PHE 166.5 99.8 30.7 86 VAL 118.8 100.0 37.9 87 VAL 113.1 95.2 35.0 88 ASP 92.6 83.8 54.9 89 CYS 99.2 100.0 51.3 90 ALA 58.8 81.0 62.7 91 ASP 72.0 65.2 73.5 92 ARG 123.5 59.1 78.1 93 ASP 0.0 0.0 86.9 94 ARG 135.9 65.1 73.4 95 ILE 125.0 87.1 40.5 96 ASP 43.1 39.0 80.8 97 GLU 72.5 52.3 61.8 98 ALA 69.4 95.5 36.8 99 ARG 150.0 71.8 71.7 100 GLN 78.5 52.8 82.8 101 GLU 137.4 99.2 47.6 102 LEU 147.8 100.0 27.3 103 HIS 128.4 85.5 59.7 104 ARG 121.5 58.2 75.0 105 ILE 142.1 99.0 31.2 106 ILE 138.3 96.4 43.0 107 ASN 29.3 24.2 79.9 108 ASP 83.2 75.3 62.3 109 ARG 50.0 23.9 88.9 110 GLU 78.7 56.8 70.5 111 MET 159.3 99.9 41.0 112 ARG 43.0 20.6 86.1 113 ASP 7.7 7.0 87.4 114 ALA 72.6 100.0 63.0 115 ILE 125.6 87.5 52.6 116 ILE 143.5 100.0 32.5 117 LEU 147.8 100.0 33.8 118 ILE 143.5 100.0 31.2 119 PHE 166.1 99.6 33.4 120 ALA 72.6 100.0 42.3 121 ASN 117.4 97.1 51.4 122 LYS 124.9 72.0 67.7 123 GLN 126.6 85.2 48.9 124 ASP 43.4 39.3 64.1 125 LEU 76.7 51.9 63.9 126 PRO 18.4 14.8 76.7 127 ASP 12.1 11.0 88.0 128 ALA 70.3 96.8 70.7 129 MET 158.3 99.3 48.0 130 LYS 41.2 23.8 82.7 131 PRO 99.7 80.1 50.0 132 HIS 19.4 12.9 83.0 133 GLU 90.2 65.1 66.6 134 ILE 143.5 100.0 26.4 135 GLN 105.2 70.8 55.0 136 GLU 24.6 17.8 81.3 137 LYS 97.3 56.1 65.5 138 LEU 147.8 100.0 31.1 139 GLY 29.8 85.5 69.2 140 LEU 147.8 100.0 30.3 141 THR 27.9 26.1 71.7 142 ARG 92.8 44.4 71.8 143 ILE 128.8 89.8 53.3 144 ARG 12.8 6.1 90.1 145 ASP 32.6 29.5 77.3 146 ARG 184.6 88.4 60.0 147 ASN 53.9 44.6 65.6 148 TRP 161.5 78.8 56.2 149 TYR 90.7 50.1 63.4 150 VAL 118.4 99.7 37.6 151 GLN 132.4 89.1 41.4 152 PRO 73.9 59.3 63.4 153 SER 81.5 97.4 46.0 154 CYS 80.2 80.8 66.2 155 ALA 71.0 97.7 53.5 156 THR 21.8 20.4 76.2 157 SER 31.8 38.1 83.3 158 GLY 28.2 81.1 60.3 159 ASP 29.4 26.6 79.7 160 GLY 30.7 88.1 64.6 161 LEU 146.9 99.4 38.6 162 TYR 113.3 62.6 53.3 163 GLU 42.6 30.8 81.2 164 GLY 34.8 100.0 48.5 165 LEU 145.2 98.2 26.0 166 THR 39.8 37.2 74.7 167 TRP 170.7 83.3 53.1 168 LEU 147.8 100.0 29.3 169 THR 102.7 96.0 45.5 170 SER 29.6 35.4 81.1 171 ASN 78.2 64.7 65.2 172 TYR 148.3 81.9 54.8 173 LYS 0.0 0.0 85.8