Protein Data Bank File : 1aoca Title : COAGULATION FACTOR 28-NOV-96 1AOC Number of Amino Acid Residues : 175 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA ASP THR ASN ALA PRO ILE CYS LEU CYS 10 ASP GLU PRO GLY VAL LEU GLY ARG THR GLN 20 ILE VAL THR THR GLU ILE LYS ASP LYS ILE 30 GLU LYS ALA VAL GLU ALA VAL ALA GLN GLU 40 SER GLY VAL SER GLY ARG GLY PHE SER ILE 50 PHE SER HIS HIS PRO VAL PHE ARG GLU CYS 60 GLY LYS TYR GLU CYS ARG THR VAL ARG PRO 70 GLU HIS SER ARG CYS TYR ASN PHE PRO PRO 80 PHE THR HIS PHE LYS SER GLU CYS PRO VAL 90 SER THR ARG ASP CYS GLU PRO VAL PHE GLY 100 TYR THR VAL ALA GLY GLU PHE ARG VAL ILE 110 VAL GLN ALA PRO ARG ALA GLY PHE ARG GLN 120 CYS VAL TRP GLN HIS LYS CYS ARG PHE GLY 130 SER ASN SER CYS GLY TYR ASN GLY ARG CYS 140 THR GLN GLN ARG SER VAL VAL ARG LEU VAL 150 THR TYR ASN LEU GLU LYS ASP GLY PHE LEU 160 CYS GLU SER PHE ARG THR CYS CYS GLY CYS 170 PRO CYS ARG SER PHE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 108.0 -179.7 2 ASP -60.8 -76.6 178.8 -51.2 88.3 3 THR -98.2 103.9 -178.9 46.7 4 ASN -131.5 133.6 179.7 59.2 -58.4 5 ALA -169.3 125.8 179.9 6 PRO -63.0 -42.8 179.3 -29.0 43.6 7 ILE 61.6 102.6 177.7 -54.4 -176.2 8 CYS -88.2 159.9 178.8 -85.4 9 LEU -58.3 137.1 -179.5 -75.8 176.9 10 CYS 67.3 3.2 179.7 -69.2 11 ASP -56.5 136.3 179.7 -96.6 0.6 12 GLU -172.7 131.3 -179.8 -159.0 -79.9 -50.2 13 PRO -58.8 -49.1 -178.9 -31.8 44.8 14 GLY -71.1 71.6 179.4 15 VAL 65.5 21.4 179.8 -166.9 16 LEU 57.3 70.1 179.9 -69.6 68.9 17 GLY -121.1 -140.3 -179.8 18 ARG -99.1 134.3 179.1 -44.7 175.7 -169.3 -177.2 19 THR -79.7 -64.5 178.7 49.3 20 GLN -114.5 169.3 179.9 -79.5 78.8 15.3 21 ILE -112.3 110.3 -180.0 -180.0 64.8 22 VAL -63.0 138.5 -178.9 56.0 23 THR -59.0 136.1 179.0 68.2 24 THR -61.6 -29.4 178.9 80.1 25 GLU -61.2 -39.6 178.7 67.6 -172.4 -88.8 26 ILE -64.4 -49.1 178.1 -71.0 -176.1 27 LYS -54.2 -37.0 179.0 -67.7 -174.7 173.0 -63.7 28 ASP -65.1 -46.1 178.9 -70.3 -47.9 29 LYS -60.0 -42.6 -179.3 -80.6 -145.0 72.5 -148.5 30 ILE -66.9 -50.1 178.9 -59.9 -179.9 31 GLU -51.5 -46.6 -178.7 -78.1 -77.0 10.6 32 LYS -60.1 -51.2 179.3 -164.2 48.3 66.1 176.8 33 ALA -57.5 -41.4 179.4 34 VAL -68.9 -35.0 177.9 173.4 35 GLU -64.8 -42.6 179.0 -86.0 157.6 6.6 36 ALA -55.8 -41.9 179.7 37 VAL -64.7 -46.5 -179.4 175.5 38 ALA -60.5 -36.1 -179.8 39 GLN -75.0 -41.2 177.7 80.3 -179.1 -177.5 40 GLU -59.2 -7.0 178.2 -58.1 172.0 -25.6 41 SER -102.7 -74.2 -179.7 158.0 42 GLY 74.5 -65.1 -180.0 43 VAL -61.3 145.0 -179.7 -174.7 44 SER 71.8 37.3 179.7 -56.6 45 GLY -76.5 65.5 179.9 46 ARG -123.3 -20.6 -179.8 -59.8 -70.5 79.5 127.1 47 GLY -178.0 -143.9 -179.9 48 PHE -47.8 -29.1 179.3 179.2 88.3 49 SER -44.3 -29.3 179.3 -42.3 50 ILE -66.5 -21.3 179.2 62.7 177.1 51 PHE -99.3 -18.4 -177.3 -63.9 -60.9 52 SER -62.8 -0.7 -180.0 68.3 53 HIS -94.4 -25.7 -179.3 -52.0 -92.9 54 HIS -82.1 129.2 -179.9 -177.5 111.5 55 PRO -43.3 -53.2 -179.1 -35.4 43.4 56 VAL -64.7 -46.4 -179.8 174.7 57 PHE -62.1 -36.4 177.1 -67.6 78.8 58 ARG -65.2 -36.9 -178.3 -102.6 -166.1 -64.0 -161.1 59 GLU -73.5 -47.9 -176.1 -172.8 -171.0 -19.5 60 CYS -141.2 21.0 -177.7 64.0 61 GLY -100.0 17.8 -178.5 62 LYS -93.0 11.4 178.0 -67.3 163.7 -174.8 160.9 63 TYR -86.2 65.2 -178.9 -88.8 -74.0 64 GLU -65.0 119.8 178.9 -64.5 179.4 31.3 65 CYS -52.9 -33.5 179.2 -72.0 66 ARG -66.4 -26.2 -175.6 -89.2 70.4 176.5 -145.0 67 THR -113.3 -19.3 -178.0 60.8 68 VAL -74.6 117.0 178.0 -179.8 69 ARG -98.0 156.1 -179.3 -61.3 -169.4 65.1 -144.2 70 PRO -56.0 -36.9 -178.4 24.9 -39.8 71 GLU -64.3 -24.7 179.4 63.6 -90.9 14.6 72 HIS -65.2 -17.2 -178.8 -58.0 -38.3 73 SER -116.7 15.8 176.5 60.2 74 ARG -77.4 154.1 -175.9 -76.1 -59.6 -104.7 123.0 75 CYS -57.2 -30.9 -179.7 -54.1 76 TYR -67.4 -12.6 178.3 59.7 87.3 77 ASN -101.2 9.3 176.0 -81.2 138.1 78 PHE -122.6 149.6 179.8 -77.7 -67.3 79 PRO -57.8 152.1 0.7 14.3 -26.8 80 PRO -76.5 11.4 178.7 38.8 -44.9 81 PHE 65.3 38.1 179.8 -51.3 -77.5 82 THR -110.7 154.9 179.8 57.3 83 HIS -96.6 148.5 -179.8 -66.4 -110.7 84 PHE -78.9 142.7 178.8 -64.5 -45.7 85 LYS -68.2 -51.6 178.2 -167.3 83.2 51.2 44.2 86 SER -135.9 128.2 -179.6 -169.6 87 GLU -123.4 138.2 179.3 177.4 165.2 36.8 88 CYS -74.7 168.2 179.3 -55.9 89 PRO -60.5 140.7 -176.7 -30.3 43.9 90 VAL -115.6 138.6 177.0 143.1 91 SER -99.6 120.1 -176.3 178.7 92 THR -111.5 130.4 179.5 -59.8 93 ARG -145.1 141.0 178.1 -95.5 158.0 -72.0 -172.3 94 ASP -75.7 148.3 -175.6 -151.5 -4.6 95 CYS -135.1 129.4 -176.6 168.8 96 GLU -139.6 73.7 -178.9 173.6 167.7 0.4 97 PRO -72.6 145.8 177.0 38.0 -44.5 98 VAL -101.3 -14.5 179.9 -85.1 99 PHE -144.2 157.5 178.8 93.1 83.2 100 GLY -165.4 159.7 177.7 101 TYR -108.0 125.3 -178.9 -66.4 -83.7 102 THR -67.4 174.3 176.5 60.0 103 VAL -51.9 -40.2 179.4 150.0 104 ALA -78.1 -0.4 178.9 105 GLY 87.2 -2.5 -179.3 106 GLU -72.2 152.6 177.0 -42.2 154.5 -82.5 107 PHE -88.0 134.1 -179.8 169.7 -85.1 108 ARG -141.6 154.2 176.5 -67.9 -72.0 178.0 -98.9 109 VAL -96.2 119.5 179.7 161.9 110 ILE -94.3 129.9 -177.9 -63.3 170.8 111 VAL -67.6 122.5 178.0 179.7 112 GLN -139.8 121.1 -179.4 -60.9 -62.7 -9.2 113 ALA -143.8 73.7 -180.0 114 PRO -53.7 -45.8 179.7 -28.5 43.4 115 ARG -60.4 -46.3 179.0 -169.2 175.9 161.5 160.6 116 ALA -69.9 -22.8 177.3 117 GLY 102.4 14.5 176.9 118 PHE -116.2 115.1 -179.4 -177.2 72.2 119 ARG -135.9 134.7 179.8 -59.5 -168.3 -67.1 133.3 120 GLN -111.7 128.0 -178.7 -54.1 179.4 -85.2 121 CYS -133.5 144.2 174.9 -77.4 122 VAL -148.0 111.9 179.5 -165.8 123 TRP -65.6 133.6 179.3 -69.7 76.5 124 GLN -99.3 137.3 -179.8 -59.1 -54.0 107.1 125 HIS -125.9 106.4 -178.2 -52.7 95.8 126 LYS -115.6 161.0 178.0 -63.3 173.3 83.3 172.9 127 CYS -59.6 122.2 -178.5 -66.2 128 ARG -54.9 -44.7 -179.7 -175.7 118.1 92.0 -157.3 129 PHE -123.3 54.1 179.8 -55.1 -79.9 130 GLY 51.9 -133.3 -178.4 131 SER -108.6 64.6 177.7 -65.3 132 ASN -82.2 169.0 -179.8 50.8 -68.6 133 SER -72.8 145.2 -175.9 53.9 134 CYS -144.7 -34.2 -179.6 54.0 135 GLY -85.1 -158.3 175.3 136 TYR -81.0 -8.4 -178.2 -67.2 85.5 137 ASN -165.4 16.0 -178.1 50.5 -16.2 138 GLY -92.0 178.2 -179.1 139 ARG -141.5 135.8 179.3 169.4 -148.0 -74.9 171.4 140 CYS -72.0 120.8 -176.9 -65.3 141 THR -129.4 138.8 179.1 -41.4 142 GLN -75.0 122.5 175.7 -172.6 59.9 64.6 143 GLN -104.8 149.0 -179.6 179.3 135.0 -59.7 144 ARG -131.7 169.0 176.2 -62.2 170.1 -167.5 86.5 145 SER -142.2 -167.1 -178.8 -166.3 146 VAL -133.4 133.5 177.4 166.0 147 VAL -120.9 154.1 178.3 -72.1 148 ARG -109.0 131.2 -178.3 -69.1 -140.4 109.9 -162.5 149 LEU -132.0 152.4 179.4 -63.9 172.7 150 VAL -73.0 125.8 178.6 177.9 151 THR -114.6 166.5 -179.9 67.2 152 TYR -119.1 125.3 178.3 179.0 56.7 153 ASN -89.5 112.0 -179.4 171.8 -8.8 154 LEU -63.3 -44.8 179.9 -101.1 151.3 155 GLU -60.0 -66.6 -178.1 164.3 83.7 -84.1 156 LYS -80.9 14.5 178.3 180.0 -165.0 176.3 170.0 157 ASP 41.0 36.2 -178.4 -74.1 40.5 158 GLY -129.3 157.3 -178.2 159 PHE -89.6 157.8 -178.0 -55.3 -78.9 160 LEU -162.3 147.5 177.0 -146.3 71.4 161 CYS -88.9 139.4 -179.9 -66.1 162 GLU -141.6 159.9 -177.6 -60.7 -104.4 36.2 163 SER -97.9 132.9 178.5 -62.6 164 PHE -132.5 147.8 178.1 -58.1 88.7 165 ARG -83.7 138.6 -179.1 -70.9 -174.0 -130.7 -90.3 166 THR -126.7 143.9 -178.0 -171.2 167 CYS -89.3 114.4 -174.9 -83.8 168 CYS -108.7 -16.4 -178.7 67.2 169 GLY -178.6 177.8 -179.2 170 CYS -136.1 72.7 179.6 -171.3 171 PRO -65.6 140.8 176.0 31.6 -44.5 172 CYS -83.3 98.9 -178.2 174.8 173 ARG -99.1 152.3 177.7 -57.5 -75.5 -162.2 -166.2 174 SER -73.8 73.5 -177.5 35.7 175 PHE 70.4 100.0 0.0 -74.1 78.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA -41.465 22.924 73.817 2 ASP -42.823 23.610 70.327 3 THR -39.596 23.946 68.332 4 ASN -36.895 22.150 70.323 5 ALA -33.496 20.798 69.257 6 PRO -30.049 20.660 70.972 7 ILE -28.240 20.881 67.599 8 CYS -24.676 19.509 67.328 9 LEU -21.931 20.988 65.188 10 CYS -22.402 20.004 61.534 11 ASP -25.819 18.398 62.320 12 GLU -27.957 17.979 59.204 13 PRO -30.592 15.397 58.105 14 GLY -29.428 14.989 54.506 15 VAL -26.343 12.843 55.186 16 LEU -25.043 15.572 57.534 17 GLY -24.000 18.250 55.064 18 ARG -24.496 21.982 54.558 19 THR -27.902 23.553 55.213 20 GLN -27.404 26.973 53.607 21 ILE -24.522 28.408 51.577 22 VAL -22.624 31.291 53.194 23 THR -21.863 34.231 50.875 24 THR -18.342 34.200 49.428 25 GLU -18.247 37.854 50.351 26 ILE -18.545 36.839 54.019 27 LYS -15.754 34.256 53.648 28 ASP -13.726 37.062 52.039 29 LYS -14.342 39.390 54.940 30 ILE -13.277 36.678 57.380 31 GLU -10.135 35.741 55.463 32 LYS -9.137 39.405 55.435 33 ALA -9.802 39.915 59.144 34 VAL -7.798 36.778 59.986 35 GLU -4.975 38.046 57.758 36 ALA -5.114 41.356 59.643 37 VAL -4.703 39.359 62.875 38 ALA -1.749 37.383 61.500 39 GLN 0.004 40.606 60.428 40 GLU -0.560 42.448 63.712 41 SER 1.578 39.523 64.919 42 GLY 4.259 38.829 62.321 43 VAL 6.709 37.436 64.872 44 SER 6.679 33.651 65.366 45 GLY 5.581 33.002 61.791 46 ARG 5.957 29.226 62.024 47 GLY 2.374 28.162 62.721 48 PHE -0.638 28.963 64.934 49 SER 1.734 31.237 66.825 50 ILE 0.891 34.022 64.384 51 PHE -2.598 34.001 65.935 52 SER -1.487 33.417 69.550 53 HIS -1.173 37.146 70.269 54 HIS -4.814 37.974 69.847 55 PRO -6.896 37.540 73.082 56 VAL -9.861 35.688 71.529 57 PHE -7.691 33.276 69.486 58 ARG -5.681 32.556 72.633 59 GLU -8.879 31.844 74.491 60 CYS -10.750 29.552 72.158 61 GLY -8.961 29.372 68.819 62 LYS -7.009 26.192 69.524 63 TYR -9.207 23.473 67.917 64 GLU -6.664 23.322 65.161 65 CYS -7.807 21.109 62.286 66 ARG -4.187 20.025 61.885 67 THR -3.935 18.627 65.456 68 VAL -7.397 17.582 66.553 69 ARG -7.879 13.816 66.628 70 PRO -11.279 12.108 67.021 71 GLU -10.636 10.769 70.541 72 HIS -10.219 14.354 71.869 73 SER -13.923 14.925 71.441 74 ARG -15.172 11.610 72.836 75 CYS -17.265 12.225 75.976 76 TYR -14.550 10.810 78.228 77 ASN -12.304 13.683 77.271 78 PHE -14.818 16.280 78.406 79 PRO -15.835 16.742 82.067 80 PRO -16.771 14.838 84.150 81 PHE -14.210 12.662 82.313 82 THR -15.990 9.412 82.910 83 HIS -16.352 6.365 80.659 84 PHE -19.591 4.749 79.556 85 LYS -20.286 1.264 80.879 86 SER -21.881 0.400 77.565 87 GLU -21.870 2.570 74.420 88 CYS -23.673 1.832 71.143 89 PRO -21.821 1.818 67.773 90 VAL -20.754 5.371 66.867 91 SER -20.544 7.224 63.538 92 THR -17.513 9.578 63.609 93 ARG -16.901 12.481 61.206 94 ASP -14.596 15.494 61.311 95 CYS -16.495 18.745 61.380 96 GLU -15.115 22.111 60.268 97 PRO -18.308 24.264 60.370 98 VAL -18.801 27.746 58.910 99 PHE -21.959 28.193 60.911 100 GLY -23.399 26.910 64.165 101 TYR -26.177 27.519 66.667 102 THR -24.937 28.346 70.097 103 VAL -25.992 26.773 73.377 104 ALA -28.562 29.637 73.541 105 GLY -29.893 28.728 70.086 106 GLU -28.524 31.779 68.242 107 PHE -27.172 31.527 64.709 108 ARG -23.458 32.340 64.415 109 VAL -20.683 32.403 61.857 110 ILE -17.797 30.228 63.004 111 VAL -14.411 31.389 61.747 112 GLN -12.736 29.246 59.037 113 ALA -9.967 30.866 56.949 114 PRO -8.104 28.054 55.158 115 ARG -6.133 30.396 52.908 116 ALA -4.927 32.449 55.930 117 GLY -4.151 29.254 57.787 118 PHE -6.787 29.259 60.506 119 ARG -9.208 26.266 60.590 120 GLN -11.367 24.965 63.447 121 CYS -12.317 21.319 63.765 122 VAL -14.189 19.152 66.275 123 TRP -14.901 15.540 65.371 124 GLN -18.563 14.562 65.913 125 HIS -19.487 11.171 67.322 126 LYS -23.151 10.235 66.868 127 CYS -25.310 7.181 67.427 128 ARG -24.704 5.048 64.373 129 PHE -28.338 3.938 64.061 130 GLY -30.143 6.655 65.922 131 SER -31.926 5.437 68.998 132 ASN -32.270 1.679 68.621 133 SER -32.604 -0.797 71.535 134 CYS -29.287 -1.880 73.031 135 GLY -29.195 -3.114 76.577 136 TYR -30.993 -6.102 77.951 137 ASN -33.456 -3.174 78.303 138 GLY -31.457 -0.089 77.159 139 ARG -31.702 2.583 74.471 140 CYS -28.964 4.239 72.351 141 THR -28.776 7.917 73.260 142 GLN -26.786 10.860 71.924 143 GLN -24.678 12.490 74.563 144 ARG -23.275 15.986 74.019 145 SER -20.831 18.359 75.580 146 VAL -19.953 22.027 74.925 147 VAL -16.949 23.517 73.076 148 ARG -15.980 27.165 72.692 149 LEU -15.039 28.257 69.181 150 VAL -13.985 31.548 67.626 151 THR -16.957 33.219 65.887 152 TYR -17.114 36.358 63.718 153 ASN -19.352 39.336 64.436 154 LEU -20.322 40.758 61.055 155 GLU -21.603 44.092 62.440 156 LYS -18.747 44.977 64.753 157 ASP -16.176 43.301 62.523 158 GLY -14.845 41.465 65.603 159 PHE -14.039 37.982 66.907 160 LEU -15.599 36.296 69.910 161 CYS -15.662 32.982 71.745 162 GLU -19.055 31.323 71.847 163 SER -20.473 28.065 73.121 164 PHE -21.629 25.246 70.891 165 ARG -22.938 21.769 71.574 166 THR -20.775 18.992 70.240 167 CYS -21.703 15.333 69.812 168 CYS -19.361 13.202 71.850 169 GLY -20.837 9.725 72.200 170 CYS -23.746 7.334 72.224 171 PRO -24.177 5.717 75.655 172 CYS -26.654 2.836 75.843 173 ARG -28.874 4.297 78.594 174 SER -31.875 2.477 80.102 175 PHE -34.040 4.808 78.004 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S/S S S S C 10 C T T T T/S S S S S S 20 S S S/H H H H H H H H 30 H H H H H H H H H H 40 H H C C C C C T T T 50 T C C H H H H H H H 60 C C C T T T T C H H 70 H H 3 3/T T T T C C/P C 80 S S S S S/S S S S S/S S 90 S S S S S S C S S S 100 S S/T T T T/S S S S S/S S 110 S S S/T T T T/S S S S S 120 S S S S S S S/T T T T/S 130 S S S C C S S S S S 140 S S/S S S S S S S S S/S 150 S S S/T T T T S S S S 160 S S S S S/S S S S S/S S 170 S S/S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S t T T 10 t t T T T t S S 20 h H H H H H H H 30 H H H H H H H H H h 40 T t S t T T g G G G 50 g T T h H H H H H H 60 h B T T T t g G 70 G G G g G G G g T T 80 t S S B e E 90 E E E e E E 100 E e T T t e E E E E 110 e B T T T T B B 120 E E E E e T t 130 S B S S S E E 140 e E E E E E E E E 150 E E E T T T T E E E 160 E E E E E E E E E 170 e E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 18.5 25.5 85.3 2 ASP 0.0 0.0 85.2 3 THR 0.0 0.0 84.6 4 ASN 34.5 28.5 79.2 5 ALA 30.2 41.5 62.5 6 PRO 61.9 49.7 74.5 7 ILE 85.0 59.2 62.5 8 CYS 99.1 99.9 55.8 9 LEU 143.3 97.0 37.4 10 CYS 59.0 59.5 61.5 11 ASP 82.1 74.3 59.6 12 GLU 112.7 81.3 56.3 13 PRO 13.6 10.9 85.4 14 GLY 0.4 1.2 77.0 15 VAL 0.0 0.0 85.5 16 LEU 116.2 78.6 71.9 17 GLY 6.6 19.0 75.0 18 ARG 35.1 16.8 79.7 19 THR 67.3 62.9 64.8 20 GLN 16.9 11.4 87.9 21 ILE 30.4 21.2 82.0 22 VAL 92.8 78.1 46.5 23 THR 43.4 40.6 68.8 24 THR 7.4 7.0 80.9 25 GLU 21.2 15.3 77.8 26 ILE 114.6 79.9 38.7 27 LYS 95.2 54.9 56.2 28 ASP 30.5 27.6 75.5 29 LYS 98.0 56.5 70.4 30 ILE 136.8 95.3 37.9 31 GLU 110.4 79.6 55.6 32 LYS 39.3 22.7 85.0 33 ALA 53.2 73.3 56.7 34 VAL 118.8 100.0 28.5 35 GLU 87.6 63.2 65.5 36 ALA 35.9 49.4 72.2 37 VAL 110.5 93.0 46.6 38 ALA 56.1 77.2 53.9 39 GLN 29.1 19.6 78.2 40 GLU 34.8 25.1 78.6 41 SER 80.4 96.2 66.0 42 GLY 2.8 7.9 83.3 43 VAL 4.5 3.8 87.8 44 SER 37.7 45.1 65.1 45 GLY 19.3 55.3 67.6 46 ARG 13.4 6.4 90.4 47 GLY 1.3 3.7 83.7 48 PHE 139.9 83.9 47.0 49 SER 42.5 50.8 70.8 50 ILE 107.6 75.0 61.2 51 PHE 165.1 99.0 37.8 52 SER 52.8 63.2 54.8 53 HIS 72.0 48.0 79.5 54 HIS 102.2 68.0 49.9 55 PRO 44.1 35.4 79.9 56 VAL 94.8 79.8 50.9 57 PHE 166.8 100.0 26.3 58 ARG 88.0 42.1 74.4 59 GLU 48.1 34.7 74.4 60 CYS 90.4 91.1 53.4 61 GLY 34.8 100.0 51.1 62 LYS 73.1 42.2 71.7 63 TYR 124.8 69.0 53.7 64 GLU 92.5 66.7 57.8 65 CYS 97.3 98.1 57.8 66 ARG 77.5 37.1 79.8 67 THR 34.0 31.8 78.0 68 VAL 109.0 91.8 54.6 69 ARG 62.0 29.7 77.5 70 PRO 84.6 68.0 58.6 71 GLU 87.7 63.3 67.4 72 HIS 75.9 50.5 64.7 73 SER 82.8 99.0 53.2 74 ARG 162.3 77.7 57.1 75 CYS 93.3 94.1 47.1 76 TYR 117.3 64.8 67.8 77 ASN 68.0 56.2 64.7 78 PHE 149.0 89.3 53.8 79 PRO 42.3 34.0 59.8 80 PRO 30.6 24.6 76.2 81 PHE 63.8 38.3 72.8 82 THR 27.3 25.6 73.2 83 HIS 41.0 27.3 74.8 84 PHE 144.4 86.6 60.5 85 LYS 0.0 0.0 90.4 86 SER 22.2 26.6 75.1 87 GLU 112.0 80.8 61.8 88 CYS 92.2 93.0 37.7 89 PRO 55.7 44.7 68.2 90 VAL 108.4 91.2 61.7 91 SER 61.3 73.3 70.4 92 THR 75.2 70.4 55.7 93 ARG 109.3 52.3 64.3 94 ASP 74.2 67.1 54.3 95 CYS 96.4 97.2 47.9 96 GLU 88.9 64.1 59.7 97 PRO 115.1 92.4 53.6 98 VAL 77.8 65.5 59.5 99 PHE 126.5 75.8 53.7 100 GLY 29.9 85.8 41.4 101 TYR 118.0 65.2 51.8 102 THR 103.3 96.7 55.8 103 VAL 71.4 60.1 62.5 104 ALA 19.0 26.2 76.4 105 GLY 6.3 18.0 77.3 106 GLU 70.6 51.0 75.8 107 PHE 77.4 46.4 61.8 108 ARG 133.3 63.8 65.7 109 VAL 107.5 90.5 40.2 110 ILE 143.5 100.0 41.2 111 VAL 118.8 100.0 31.8 112 GLN 141.6 95.3 48.5 113 ALA 72.6 100.0 45.9 114 PRO 59.9 48.1 71.8 115 ARG 18.8 9.0 90.8 116 ALA 64.7 89.1 59.5 117 GLY 17.0 48.8 77.8 118 PHE 162.4 97.3 37.5 119 ARG 154.2 73.8 64.4 120 GLN 148.4 99.9 47.7 121 CYS 96.4 97.2 55.8 122 VAL 118.5 99.8 37.6 123 TRP 144.8 70.6 62.2 124 GLN 142.7 96.0 49.4 125 HIS 147.6 98.3 50.2 126 LYS 127.7 73.6 59.8 127 CYS 92.9 93.6 54.9 128 ARG 101.1 48.4 65.5 129 PHE 46.6 27.9 78.1 130 GLY 0.0 0.0 79.0 131 SER 37.0 44.3 73.8 132 ASN 54.2 44.9 69.9 133 SER 4.2 5.0 82.9 134 CYS 79.2 79.9 54.6 135 GLY 18.2 52.4 63.2 136 TYR 0.0 0.0 90.9 137 ASN 13.1 10.8 77.9 138 GLY 31.8 91.3 54.5 139 ARG 112.1 53.7 65.6 140 CYS 97.8 98.6 46.6 141 THR 63.4 59.3 66.7 142 GLN 129.6 87.2 54.9 143 GLN 95.9 64.6 60.2 144 ARG 143.6 68.7 51.2 145 SER 60.7 72.6 49.2 146 VAL 67.6 56.9 63.1 147 VAL 114.3 96.2 36.3 148 ARG 105.9 50.7 73.1 149 LEU 147.4 99.7 30.9 150 VAL 118.8 100.0 37.3 151 THR 104.6 97.8 45.1 152 TYR 179.5 99.1 40.5 153 ASN 66.8 55.2 60.2 154 LEU 82.7 56.0 55.9 155 GLU 0.0 0.0 88.2 156 LYS 20.5 11.8 83.2 157 ASP 47.1 42.7 81.7 158 GLY 17.7 51.0 61.5 159 PHE 157.2 94.2 34.0 160 LEU 51.0 34.5 76.7 161 CYS 96.2 97.0 50.5 162 GLU 115.2 83.1 57.6 163 SER 60.8 72.7 54.8 164 PHE 166.4 99.7 40.1 165 ARG 136.7 65.4 57.7 166 THR 106.9 100.0 43.0 167 CYS 98.4 99.2 51.7 168 CYS 98.3 99.1 49.7 169 GLY 34.8 100.0 54.6 170 CYS 99.2 100.0 43.0 171 PRO 121.7 97.8 48.8 172 CYS 93.6 94.3 50.6 173 ARG 95.7 45.8 74.7 174 SER 20.9 25.0 75.6 175 PHE 54.0 32.4 79.6