Protein Data Bank File : 2pth Title : HYDROLASE 25-MAR-97 2PTH Number of Amino Acid Residues : 193 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR ILE LYS LEU ILE VAL GLY LEU ALA ASN 10 PRO GLY ALA GLU TYR ALA ALA THR ARG HIS 20 ASN ALA GLY ALA TRP PHE VAL ASP LEU LEU 30 ALA GLU ARG LEU ARG ALA PRO LEU ARG GLU 40 GLU ALA LYS PHE PHE GLY TYR THR SER ARG 50 VAL THR LEU GLY GLY GLU ASP VAL ARG LEU 60 LEU VAL PRO THR THR PHE MET ASN LEU SER 70 GLY LYS ALA VAL ALA ALA MET ALA SER PHE 80 PHE ARG ILE ASN PRO ASP GLU ILE LEU VAL 90 ALA HIS ASP GLU LEU ASP LEU PRO PRO GLY 100 VAL ALA LYS PHE LYS LEU GLY GLY GLY HIS 110 GLY GLY HIS ASN GLY LEU LYS ASP ILE ILE 120 SER LYS LEU GLY ASN ASN PRO ASN PHE HIS 130 ARG LEU ARG ILE GLY ILE GLY HIS PRO GLY 140 ASP LYS ASN LYS VAL VAL GLY PHE VAL LEU 150 GLY LYS PRO PRO VAL SER GLU GLN LYS LEU 160 ILE ASP GLU ALA ILE ASP GLU ALA ALA ARG 170 CYS THR GLU MET TRP PHE THR ASP GLY LEU 180 THR LYS ALA THR ASN ARG LEU HIS ALA PHE 190 LYS ALA GLN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 167.7 -178.6 -169.7 2 ILE -100.5 127.9 -179.7 -67.1 -60.3 3 LYS -107.7 -20.9 -178.5 -70.9 178.8 177.1 167.1 4 LEU -140.7 132.0 176.8 176.3 67.0 5 ILE -117.5 124.3 -178.4 -62.7 173.3 6 VAL -113.8 135.7 177.9 -177.4 7 GLY -118.6 114.1 -178.3 8 LEU -72.4 144.0 -178.0 -58.5 -171.7 9 ALA -172.2 174.9 173.1 10 ASN -113.2 143.0 -179.0 -81.8 -56.0 11 PRO -81.5 156.8 177.5 36.9 -40.0 12 GLY 96.0 153.4 -180.0 13 ALA -58.5 -27.5 178.9 14 GLU -56.9 -34.2 -178.1 -178.4 -178.1 -9.5 15 TYR -111.5 -2.0 -176.4 -55.6 -81.0 16 ALA -50.6 -38.9 -179.1 17 ALA -101.7 8.7 -178.9 18 THR -81.8 156.0 -179.4 63.2 19 ARG -56.5 -36.2 -179.0 -65.7 -180.0 173.6 98.4 20 HIS -65.1 -10.1 178.2 -130.1 21.0 21 ASN -99.2 12.1 -178.7 -89.0 34.2 22 ALA -53.6 -39.4 179.0 23 GLY -59.9 -42.4 178.8 24 ALA -64.5 -35.7 179.4 25 TRP -58.4 -40.8 179.4 -62.0 -13.8 26 PHE -63.0 -50.3 179.9 171.9 75.2 27 VAL -62.7 -38.2 178.4 173.3 28 ASP -60.7 -42.7 179.8 -85.1 -18.1 29 LEU -59.5 -46.7 179.4 -177.7 63.9 30 LEU -59.3 -47.2 180.0 -70.9 179.9 31 ALA -63.4 -42.0 -179.6 32 GLU -60.8 -50.2 -179.0 -163.7 -103.5 -60.8 33 ARG -61.2 -29.6 179.7 -74.5 -167.8 -175.4 158.2 34 LEU -94.9 -3.7 -177.9 -64.2 164.5 35 ARG 58.7 38.1 -179.8 -56.4 -61.6 -167.2 -95.6 36 ALA -116.2 83.9 -179.4 37 PRO -51.7 141.8 178.7 -28.7 44.9 38 LEU -87.7 137.3 -179.9 -64.3 165.5 39 ARG -130.4 134.9 -179.1 -177.7 172.7 60.5 71.7 40 GLU -72.0 129.3 177.8 -173.4 168.8 5.2 41 GLU -119.7 115.4 -179.5 -69.0 -159.9 71.7 42 ALA -49.5 -45.5 -179.3 43 LYS -53.0 -31.6 -178.5 -173.9 177.0 -171.0 167.8 44 PHE -108.1 4.6 178.5 -56.9 -53.5 45 PHE 53.3 41.5 179.4 -49.6 -76.9 46 GLY 174.8 178.3 178.2 47 TYR -78.7 136.2 179.5 -59.9 -81.4 48 THR -132.6 161.4 176.7 65.3 49 SER -161.6 164.4 179.6 -169.3 50 ARG -129.6 126.9 -179.3 -172.5 -172.5 -171.6 175.4 51 VAL -136.1 168.5 177.9 -61.9 52 THR -110.5 120.8 -179.1 -63.4 53 LEU -128.7 120.9 -179.0 -151.4 51.7 54 GLY 59.9 28.9 -179.3 55 GLY 84.8 -8.4 -178.4 56 GLU -98.4 152.1 -179.8 -61.0 -55.7 -61.4 57 ASP -82.2 116.3 -178.5 -168.7 27.7 58 VAL -131.8 139.4 177.2 -174.1 59 ARG -103.2 146.8 -179.7 -70.5 175.8 -172.1 -78.6 60 LEU -114.6 145.3 179.2 -54.7 -178.8 61 LEU -145.4 131.3 174.3 173.3 65.5 62 VAL -127.8 106.2 -179.6 173.1 63 PRO -60.4 148.5 177.0 -26.9 42.3 64 THR -119.1 23.6 -178.1 50.9 65 THR -82.8 -16.1 -171.4 51.8 66 PHE 92.6 147.5 -174.8 -89.7 76.4 67 MET -43.6 -55.8 -176.4 -169.4 61.6 77.9 68 ASN -68.5 -5.0 179.7 -60.7 9.7 69 LEU -117.6 15.6 -179.7 -61.6 161.8 70 SER -56.4 -34.6 -178.0 -63.3 71 GLY -51.5 -38.2 179.6 72 LYS -53.7 -47.5 179.9 -172.1 176.7 172.1 -176.1 73 ALA -68.3 -47.5 -179.3 74 VAL -60.5 -45.2 179.3 177.6 75 ALA -62.2 -42.5 179.6 76 ALA -61.4 -45.6 180.0 77 MET -67.2 -47.2 -179.5 -160.8 105.4 113.1 78 ALA -60.5 -37.8 -179.8 79 SER -72.4 -40.7 -179.9 -65.6 80 PHE -65.5 -44.6 -179.1 -170.8 80.8 81 PHE -91.8 0.2 179.3 -64.3 -73.0 82 ARG 54.8 61.5 -179.0 -59.7 -175.3 64.5 -139.5 83 ILE -106.4 131.7 179.5 -61.2 168.7 84 ASN -78.3 154.2 -179.7 -64.3 -20.7 85 PRO -54.0 -38.6 180.0 -32.7 44.4 86 ASP -79.1 7.0 175.6 63.9 -3.6 87 GLU -107.8 11.6 -179.9 -68.6 171.9 -34.8 88 ILE -116.0 136.9 176.7 -54.6 -178.9 89 LEU -117.8 120.2 179.2 175.1 60.9 90 VAL -109.9 117.8 178.8 179.3 91 ALA -91.0 132.1 -179.0 92 HIS -153.1 160.4 176.4 69.3 -90.1 93 ASP -72.9 142.0 -177.8 52.3 -52.5 94 GLU -127.0 113.4 179.4 175.5 60.1 82.9 95 LEU -66.8 -29.6 -177.5 -67.6 162.3 96 ASP -79.5 3.6 177.4 -70.2 -11.1 97 LEU -128.6 144.2 -179.7 -68.4 176.8 98 PRO -81.2 161.4 179.0 36.2 -42.0 99 PRO -59.3 133.2 -179.4 19.9 -37.8 100 GLY 110.2 -11.4 -178.9 101 VAL -120.6 146.6 177.6 174.2 102 ALA -145.1 149.5 180.0 103 LYS -143.7 151.8 175.8 -69.9 -171.9 175.8 -68.5 104 PHE -95.5 152.1 178.5 -73.1 -53.1 105 LYS -156.0 144.0 177.2 176.1 178.6 174.1 59.8 106 LEU -116.4 120.7 177.9 173.2 60.7 107 GLY 77.5 -162.7 -178.6 108 GLY 97.7 -175.8 -178.9 109 GLY -89.6 -158.7 178.3 110 HIS -95.1 -18.6 -179.7 52.9 -114.9 111 GLY 57.7 27.3 -179.8 112 GLY 93.6 -5.9 179.2 113 HIS -81.9 113.8 -177.4 -166.7 -67.6 114 ASN -68.2 -20.0 176.5 -70.9 -42.9 115 GLY -73.1 -46.0 179.2 116 LEU -63.2 -40.0 -179.8 -70.0 -179.5 117 LYS -56.4 -46.9 -180.0 -176.6 -179.9 168.3 177.9 118 ASP -66.3 -36.1 178.2 -161.6 57.3 119 ILE -64.2 -44.2 178.8 -66.4 167.3 120 ILE -58.7 -45.3 179.3 -65.7 168.6 121 SER -60.2 -53.6 -177.9 180.0 122 LYS -67.6 -18.1 177.3 -56.9 -55.5 -167.8 -72.8 123 LEU -89.9 13.4 179.8 -69.4 -178.8 124 GLY 85.0 43.1 -178.7 125 ASN 54.8 47.1 -179.2 -169.4 -151.6 126 ASN -120.6 108.7 -179.8 -168.9 -24.4 127 PRO -88.4 1.9 -176.6 38.1 -42.5 128 ASN -79.4 51.7 176.2 -58.8 -53.1 129 PHE -118.1 159.1 179.7 49.9 88.4 130 HIS -78.9 152.1 179.0 -70.8 93.6 131 ARG -136.5 144.5 173.8 -54.9 98.6 -178.9 -86.0 132 LEU -111.4 107.7 -178.9 168.7 61.1 133 ARG -88.7 107.6 -178.6 -52.0 167.3 59.3 -146.7 134 ILE -97.2 110.2 -177.7 -56.4 166.8 135 GLY -59.2 130.7 177.4 136 ILE -126.3 -5.1 -178.3 60.0 165.1 137 GLY 86.3 171.6 -177.9 138 HIS -130.4 137.8 -179.6 -166.4 120.3 139 PRO -74.4 -20.7 179.4 33.3 -43.7 140 GLY 135.3 -42.2 179.3 141 ASP -153.0 168.7 -178.1 53.4 76.9 142 LYS -62.7 -28.5 -179.4 -65.3 161.6 175.6 -177.0 143 ASN -66.4 -29.0 -179.0 -61.7 -54.1 144 LYS -92.3 -9.1 -177.9 -60.6 170.9 -176.0 54.7 145 VAL -59.1 -43.9 -178.7 172.7 146 VAL -55.8 -54.6 -180.0 -177.5 147 GLY -66.3 -26.7 179.8 148 PHE -71.8 -54.6 -179.2 -174.3 79.1 149 VAL -66.9 -26.7 178.3 -57.7 150 LEU -95.6 17.3 178.6 -63.0 -178.9 151 GLY -108.5 161.0 179.5 152 LYS -93.0 132.1 -179.7 -178.1 -178.8 168.0 -179.7 153 PRO -72.1 148.2 178.9 31.6 -42.9 154 PRO -63.7 158.4 -179.0 27.2 -41.7 155 VAL -48.8 -44.4 -179.2 169.7 156 SER -62.7 -39.0 178.3 71.0 157 GLU -71.2 -38.3 178.8 -78.7 -175.5 -1.2 158 GLN -58.9 -42.0 179.7 -175.5 63.3 -122.7 159 LYS -59.7 -42.9 179.6 -59.1 -75.7 179.2 -178.6 160 LEU -64.8 -43.5 179.1 -70.5 170.2 161 ILE -62.9 -42.2 178.9 -65.0 164.7 162 ASP -59.6 -39.2 178.0 -74.6 -11.3 163 GLU -63.3 -47.0 -179.3 -81.2 177.9 55.9 164 ALA -62.3 -40.8 -179.9 165 ILE -63.9 -41.5 178.2 -75.9 170.8 166 ASP -61.1 -47.7 179.2 -164.3 -16.3 167 GLU -63.3 -43.5 179.2 178.4 69.3 1.8 168 ALA -58.3 -39.7 179.1 169 ALA -63.1 -43.2 179.0 170 ARG -65.3 -40.3 179.2 -63.2 167.8 -178.7 -167.2 171 CYS -69.1 -31.8 178.4 -66.6 172 THR -67.2 -38.9 178.7 -62.3 173 GLU -65.9 -39.7 179.3 -173.6 173.4 -25.8 174 MET -61.8 -35.4 179.2 -159.4 172.9 118.1 175 TRP -54.6 -43.7 -179.5 -177.1 -19.8 176 PHE -67.1 -42.3 -179.0 -72.0 -77.4 177 THR -85.2 -41.1 -178.4 64.3 178 ASP -109.4 -10.3 179.9 -67.4 87.5 179 GLY 103.9 157.7 -178.6 180 LEU -62.1 -42.6 -179.3 176.7 57.9 181 THR -55.2 -50.7 179.6 -55.9 182 LYS -65.6 -42.5 179.1 -77.2 -174.0 169.4 177.7 183 ALA -60.6 -42.3 179.7 184 THR -65.7 -46.4 179.3 -60.4 185 ASN -57.5 -40.2 178.5 -71.0 163.1 186 ARG -70.3 -48.5 -178.4 176.2 -177.8 172.0 177.9 187 LEU -61.8 -45.0 -178.4 -173.9 58.5 188 HIS -69.9 -12.5 178.3 -68.4 20.7 189 ALA -88.1 -14.6 -179.2 190 PHE -66.5 119.5 -179.3 -167.1 66.9 191 LYS 78.4 -9.5 179.4 -56.4 -52.9 177.3 -167.2 192 ALA -94.0 -16.7 -180.0 193 GLN -143.2 -33.3 0.0 -172.5 -91.5 -33.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR 59.759 29.378 67.157 2 ILE 57.484 31.912 65.369 3 LYS 57.206 35.432 66.828 4 LEU 55.347 37.208 63.995 5 ILE 52.614 36.066 61.588 6 VAL 51.973 38.289 58.526 7 GLY 48.954 38.112 56.211 8 LEU 49.455 39.784 52.811 9 ALA 46.723 41.964 51.328 10 ASN 45.674 45.224 49.691 11 PRO 43.768 47.645 51.954 12 GLY 40.147 48.728 51.755 13 ALA 36.730 47.200 51.083 14 GLU 37.546 47.356 47.341 15 TYR 40.045 44.438 47.748 16 ALA 38.655 42.631 50.841 17 ALA 37.172 39.599 49.062 18 THR 39.800 39.239 46.348 19 ARG 42.133 36.242 46.015 20 HIS 45.259 38.360 46.616 21 ASN 44.012 38.932 50.199 22 ALA 44.053 35.205 51.110 23 GLY 46.897 35.747 53.595 24 ALA 44.849 38.362 55.461 25 TRP 41.871 35.949 55.633 26 PHE 44.129 33.578 57.560 27 VAL 45.309 36.232 60.026 28 ASP 41.716 37.485 60.477 29 LEU 40.633 33.949 61.386 30 LEU 43.323 33.671 64.089 31 ALA 42.388 37.057 65.582 32 GLU 38.646 36.282 65.463 33 ARG 38.978 32.955 67.287 34 LEU 41.060 34.513 70.025 35 ARG 38.850 37.649 70.176 36 ALA 42.010 39.782 69.718 37 PRO 41.054 42.605 67.284 38 LEU 43.549 44.034 64.814 39 ARG 44.136 47.784 65.073 40 GLU 46.056 49.875 62.542 41 GLU 49.306 51.329 63.889 42 ALA 50.937 54.005 61.692 43 LYS 54.397 53.138 63.027 44 PHE 54.138 49.606 61.569 45 PHE 52.207 50.484 58.368 46 GLY 49.445 47.983 59.047 47 TYR 46.986 46.296 61.385 48 THR 48.601 44.651 64.399 49 SER 47.569 42.506 67.359 50 ARG 49.193 40.406 70.094 51 VAL 47.899 36.936 70.917 52 THR 48.769 33.788 72.841 53 LEU 48.986 30.767 70.574 54 GLY 49.919 27.359 71.962 55 GLY 50.980 29.187 75.114 56 GLU 53.446 31.368 73.182 57 ASP 53.496 35.160 72.679 58 VAL 52.866 35.944 68.988 59 ARG 52.305 39.207 67.090 60 LEU 50.021 39.555 64.041 61 LEU 50.410 41.936 61.093 62 VAL 48.323 42.717 58.004 63 PRO 50.086 45.517 56.028 64 THR 48.067 48.504 54.757 65 THR 50.867 49.625 52.383 66 PHE 49.311 47.977 49.263 67 MET 50.774 44.615 48.148 68 ASN 53.925 45.668 46.326 69 LEU 55.053 47.823 49.269 70 SER 54.525 45.155 51.998 71 GLY 58.220 44.848 52.902 72 LYS 58.108 48.217 54.658 73 ALA 55.587 46.983 57.280 74 VAL 57.285 43.616 57.939 75 ALA 60.682 45.312 58.300 76 ALA 59.299 47.979 60.697 77 MET 57.739 45.355 62.989 78 ALA 60.725 42.992 62.840 79 SER 63.131 45.819 63.682 80 PHE 61.153 47.195 66.637 81 PHE 60.629 43.815 68.317 82 ARG 63.987 42.481 67.088 83 ILE 62.607 39.412 65.289 84 ASN 64.816 37.298 62.989 85 PRO 63.617 36.355 59.467 86 ASP 63.250 32.681 60.408 87 GLU 60.970 33.681 63.297 88 ILE 58.476 35.128 60.787 89 LEU 55.597 33.297 59.057 90 VAL 54.112 35.005 55.976 91 ALA 50.700 33.788 54.782 92 HIS 49.978 34.443 51.100 93 ASP 47.893 33.315 48.108 94 GLU 49.563 30.670 45.937 95 LEU 48.736 30.242 42.207 96 ASP 50.626 26.915 42.069 97 LEU 48.280 25.107 44.484 98 PRO 44.523 24.581 43.920 99 PRO 41.755 25.953 46.171 100 GLY 41.422 23.597 49.183 101 VAL 45.148 22.939 49.686 102 ALA 47.751 24.823 51.759 103 LYS 51.467 24.154 52.434 104 PHE 54.313 25.413 54.647 105 LYS 57.678 26.314 53.080 106 LEU 60.905 27.850 54.428 107 GLY 62.796 30.095 52.040 108 GLY 62.864 29.988 48.258 109 GLY 62.164 32.861 45.906 110 HIS 59.101 35.023 45.435 111 GLY 57.946 32.990 42.418 112 GLY 56.465 36.099 40.807 113 HIS 54.433 37.214 43.866 114 ASN 55.225 40.932 44.241 115 GLY 54.335 41.075 47.932 116 LEU 56.908 38.357 48.698 117 LYS 59.428 40.088 46.447 118 ASP 59.250 43.312 48.479 119 ILE 59.544 41.483 51.824 120 ILE 62.733 39.699 50.667 121 SER 64.147 43.057 49.583 122 LYS 63.300 44.973 52.795 123 LEU 64.653 42.260 55.115 124 GLY 68.030 42.858 53.476 125 ASN 67.634 40.511 50.503 126 ASN 66.889 37.620 52.871 127 PRO 64.319 35.039 51.651 128 ASN 64.735 32.825 54.728 129 PHE 61.388 33.351 56.378 130 HIS 58.561 30.823 56.661 131 ARG 55.519 30.901 54.367 132 LEU 51.996 29.512 54.477 133 ARG 51.051 28.979 50.801 134 ILE 47.247 29.171 50.449 135 GLY 46.099 27.622 47.167 136 ILE 43.944 29.767 44.863 137 GLY 44.441 27.991 41.522 138 HIS 45.937 29.333 38.270 139 PRO 44.025 30.859 35.306 140 GLY 46.222 29.384 32.535 141 ASP 48.774 32.025 31.536 142 LYS 50.380 35.236 32.785 143 ASN 48.040 37.535 30.846 144 LYS 45.032 36.397 32.887 145 VAL 46.770 36.537 36.277 146 VAL 46.051 40.228 37.035 147 GLY 42.271 40.003 36.717 148 PHE 42.347 36.627 38.486 149 VAL 44.194 37.610 41.696 150 LEU 42.220 40.852 41.910 151 GLY 38.998 38.907 41.380 152 LYS 36.578 37.391 43.909 153 PRO 36.381 33.540 43.892 154 PRO 33.056 31.831 43.078 155 VAL 31.220 30.444 46.166 156 SER 32.355 26.834 45.637 157 GLU 36.045 27.837 45.507 158 GLN 35.636 30.133 48.512 159 LYS 34.303 27.187 50.556 160 LEU 37.429 25.156 49.660 161 ILE 39.827 27.995 50.528 162 ASP 38.014 28.500 53.867 163 GLU 38.503 24.804 54.707 164 ALA 42.231 24.981 53.993 165 ILE 42.597 28.160 56.073 166 ASP 40.790 26.548 59.008 167 GLU 43.093 23.477 58.834 168 ALA 46.168 25.718 58.433 169 ALA 45.200 27.613 61.631 170 ARG 44.997 24.355 63.617 171 CYS 48.353 23.177 62.227 172 THR 50.019 26.528 63.048 173 GLU 48.876 26.086 66.654 174 MET 50.251 22.525 66.535 175 TRP 53.611 23.909 65.375 176 PHE 53.936 25.698 68.749 177 THR 52.999 22.736 70.968 178 ASP 54.323 19.767 68.919 179 GLY 56.891 21.187 66.486 180 LEU 57.149 22.010 62.782 181 THR 57.681 18.430 61.548 182 LYS 54.399 17.165 63.003 183 ALA 52.522 20.317 61.952 184 THR 53.825 19.987 58.352 185 ASN 52.979 16.273 58.122 186 ARG 49.386 16.973 59.139 187 LEU 48.879 19.989 56.842 188 HIS 50.434 18.387 53.757 189 ALA 48.180 15.330 54.231 190 PHE 45.066 17.518 53.976 191 LYS 43.368 16.589 50.666 192 ALA 46.248 14.245 49.797 193 GLN 44.856 11.294 51.792 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/S S S S S S S 10 C T T T T C C C C C 20 H H H H H H H H H H 30 H H H H H/S S S S S S 40 S/T T T T C S S S S S 50 S S/T T T T/S S S S S S 60 S S S S C T T T T H 70 H H H H H H H H H H 80 H H C T T T T/S S S S 90 S S S C C S S S S S 100 S S S/S S S S S/S S S S 110 C C H H H H H H H H 120 H H H H C C C S S S 130 S S S S S/S S S S S C 140 C C C H H H H H H H 150 H/S S S S/H H H H H H H 160 H H H H H H H H H H 170 H H H H H H H H H H 180 H H H H H H H H H H 190 S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E e 10 t T T T T T g G G 20 h H H H H H H H H H 30 H H H H h t E E 40 E G G G e E E E E E 50 E E E T T E E E E E 60 E E E e S g G G G h 70 H H H H H H H H H H 80 H h t g G G e E E E 90 E E E E T T t t T T 100 e E E E E E e t 110 T T h H H H H H H H 120 H H h T t e E 130 E E E E E e S 140 h H H H H H H H H h 150 t h H H H H H H 160 H H H H H H H H H H 170 H H H H H H H H h H 180 H H H H H H H H H h 190 T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 43.5 40.7 72.7 2 ILE 142.1 99.0 39.6 3 LYS 90.2 52.0 67.3 4 LEU 147.8 100.0 29.4 5 ILE 143.5 100.0 24.5 6 VAL 118.8 100.0 29.5 7 GLY 34.8 100.0 49.8 8 LEU 147.7 99.9 35.9 9 ALA 69.8 96.1 57.5 10 ASN 110.7 91.5 33.7 11 PRO 97.9 78.6 57.8 12 GLY 1.2 3.4 80.6 13 ALA 0.0 0.0 80.1 14 GLU 16.7 12.1 80.2 15 TYR 136.1 75.2 62.8 16 ALA 25.5 35.1 80.7 17 ALA 31.4 43.3 62.2 18 THR 95.0 88.9 59.1 19 ARG 189.9 90.9 43.9 20 HIS 125.4 83.5 55.6 21 ASN 110.8 91.6 63.6 22 ALA 72.6 100.0 41.4 23 GLY 34.8 100.0 52.8 24 ALA 64.9 89.4 53.3 25 TRP 168.2 82.0 57.9 26 PHE 166.8 100.0 30.7 27 VAL 118.8 100.0 39.9 28 ASP 41.2 37.3 65.9 29 LEU 112.5 76.1 63.6 30 LEU 139.7 94.5 32.5 31 ALA 67.2 92.6 52.0 32 GLU 34.9 25.2 77.6 33 ARG 120.5 57.7 70.4 34 LEU 94.4 63.8 59.6 35 ARG 43.1 20.7 88.3 36 ALA 52.9 72.8 60.9 37 PRO 22.2 17.8 82.2 38 LEU 132.6 89.7 50.6 39 ARG 45.1 21.6 85.4 40 GLU 66.8 48.2 66.8 41 GLU 87.8 63.4 70.2 42 ALA 0.0 0.0 85.0 43 LYS 51.3 29.6 66.2 44 PHE 157.0 94.1 39.3 45 PHE 95.8 57.4 66.7 46 GLY 34.8 100.0 56.3 47 TYR 101.1 55.9 59.2 48 THR 95.6 89.4 50.7 49 SER 69.9 83.6 54.6 50 ARG 82.7 39.6 84.0 51 VAL 110.8 93.3 41.0 52 THR 30.2 28.3 77.1 53 LEU 140.8 95.3 34.6 54 GLY 27.3 78.3 57.5 55 GLY 4.2 12.0 72.9 56 GLU 59.6 43.0 76.7 57 ASP 49.2 44.6 79.1 58 VAL 118.5 99.7 46.3 59 ARG 152.5 73.0 50.5 60 LEU 147.8 100.0 35.6 61 LEU 147.8 100.0 35.9 62 VAL 108.7 91.5 40.6 63 PRO 124.3 99.8 50.0 64 THR 95.6 89.4 56.3 65 THR 93.0 87.0 54.8 66 PHE 69.2 41.5 72.4 67 MET 153.8 96.5 64.1 68 ASN 42.6 35.3 69.5 69 LEU 44.5 30.1 79.1 70 SER 83.6 100.0 49.8 71 GLY 34.7 99.8 50.6 72 LYS 72.0 41.5 60.2 73 ALA 72.6 100.0 45.7 74 VAL 118.8 100.0 26.1 75 ALA 50.7 69.9 63.3 76 ALA 49.6 68.4 64.6 77 MET 157.6 98.9 30.4 78 ALA 66.5 91.5 51.4 79 SER 12.6 15.1 83.6 80 PHE 76.1 45.6 66.4 81 PHE 123.3 73.9 53.3 82 ARG 14.2 6.8 91.7 83 ILE 140.3 97.8 44.8 84 ASN 34.0 28.2 75.8 85 PRO 90.8 72.9 59.3 86 ASP 41.4 37.4 69.7 87 GLU 111.7 80.6 64.4 88 ILE 143.3 99.9 34.7 89 LEU 147.7 100.0 31.3 90 VAL 118.8 100.0 31.9 91 ALA 72.6 100.0 42.2 92 HIS 144.3 96.1 43.0 93 ASP 108.6 98.3 46.7 94 GLU 112.1 80.9 62.2 95 LEU 106.7 72.2 50.0 96 ASP 26.7 24.1 82.3 97 LEU 128.8 87.1 48.1 98 PRO 51.4 41.3 56.9 99 PRO 106.7 85.7 50.4 100 GLY 33.0 94.9 48.9 101 VAL 90.0 75.8 49.8 102 ALA 72.5 99.8 39.5 103 LYS 115.3 66.5 56.1 104 PHE 160.7 96.3 40.0 105 LYS 86.0 49.6 74.0 106 LEU 74.7 50.5 66.4 107 GLY 31.5 90.5 70.0 108 GLY 11.1 32.0 79.2 109 GLY 4.9 14.0 76.7 110 HIS 89.1 59.3 56.1 111 GLY 0.0 0.0 79.4 112 GLY 2.6 7.5 77.2 113 HIS 128.0 85.2 55.9 114 ASN 54.7 45.2 76.6 115 GLY 34.8 100.0 52.9 116 LEU 143.1 96.8 43.6 117 LYS 61.4 35.4 76.9 118 ASP 94.3 85.4 68.4 119 ILE 143.4 100.0 28.9 120 ILE 128.0 89.2 58.0 121 SER 32.8 39.2 77.0 122 LYS 90.9 52.4 76.4 123 LEU 134.3 90.9 42.7 124 GLY 0.0 0.0 83.3 125 ASN 17.5 14.5 76.5 126 ASN 75.9 62.8 60.2 127 PRO 84.2 67.6 68.8 128 ASN 41.2 34.1 67.2 129 PHE 166.8 100.0 40.1 130 HIS 132.7 88.4 35.8 131 ARG 204.6 97.9 45.3 132 LEU 147.8 100.0 27.1 133 ARG 163.2 78.1 47.1 134 ILE 143.3 99.9 37.3 135 GLY 34.8 100.0 64.0 136 ILE 143.5 100.0 40.7 137 GLY 22.0 63.1 62.2 138 HIS 90.4 60.2 60.2 139 PRO 108.5 87.2 44.8 140 GLY 3.6 10.4 73.9 141 ASP 59.8 54.1 77.4 142 LYS 0.0 0.0 85.9 143 ASN 4.3 3.5 85.0 144 LYS 58.3 33.6 82.6 145 VAL 89.6 75.4 45.6 146 VAL 16.6 14.0 74.5 147 GLY 0.0 0.0 76.8 148 PHE 131.1 78.6 59.6 149 VAL 106.3 89.5 41.5 150 LEU 90.1 61.0 58.9 151 GLY 16.3 46.7 80.4 152 LYS 42.4 24.5 76.3 153 PRO 124.5 100.0 52.2 154 PRO 50.8 40.8 83.9 155 VAL 12.9 10.9 74.0 156 SER 9.7 11.6 70.6 157 GLU 93.4 67.4 58.1 158 GLN 105.2 70.8 57.0 159 LYS 43.0 24.8 76.3 160 LEU 78.9 53.4 68.5 161 ILE 143.2 99.8 40.4 162 ASP 44.7 40.4 70.0 163 GLU 66.3 47.9 67.9 164 ALA 72.2 99.5 54.0 165 ILE 137.3 95.7 38.9 166 ASP 72.9 66.0 72.9 167 GLU 120.2 86.7 49.2 168 ALA 72.6 100.0 37.4 169 ALA 69.3 95.5 51.9 170 ARG 83.5 40.0 86.9 171 CYS 99.2 100.0 44.7 172 THR 106.8 99.9 31.2 173 GLU 56.0 40.4 66.9 174 MET 120.2 75.4 61.5 175 TRP 185.3 90.4 34.6 176 PHE 160.8 96.4 47.4 177 THR 50.2 47.0 75.3 178 ASP 53.7 48.6 71.0 179 GLY 7.3 20.8 78.9 180 LEU 89.9 60.8 60.0 181 THR 7.3 6.9 82.4 182 LYS 49.2 28.4 77.2 183 ALA 72.6 100.0 44.3 184 THR 76.0 71.1 55.1 185 ASN 30.7 25.4 72.9 186 ARG 111.1 53.2 66.3 187 LEU 147.7 99.9 42.0 188 HIS 105.2 70.1 65.3 189 ALA 31.3 43.1 73.7 190 PHE 121.9 73.1 67.1 191 LYS 99.9 57.6 65.3 192 ALA 22.7 31.3 80.5 193 GLN 5.4 3.7 88.1