Protein Data Bank File : 1iisc Title : IMMUNE SYSTEM 24-APR-01 1IIS Number of Amino Acid Residues : 167 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU PRO LYS ALA VAL VAL PHE LEU GLU PRO 10 GLN TRP TYR SER VAL LEU GLU LYS ASP SER 20 VAL THR LEU LYS CYS GLN GLY ALA TYR SER 30 PRO GLU ASP ASN SER THR GLN TRP PHE HIS 40 ASN GLU SER LEU ILE SER SER GLN ALA SER 50 SER TYR PHE ILE ASP ALA ALA THR VAL ASN 60 ASP SER GLY GLU TYR ARG CYS GLN THR ASN 70 LEU SER THR LEU SER ASP PRO VAL GLN LEU 80 GLU VAL HIS ILE GLY TRP LEU LEU LEU GLN 90 ALA PRO ARG TRP VAL PHE LYS GLU GLU ASP 100 PRO ILE HIS LEU ARG CYS HIS SER TRP LYS 110 ASN THR ALA LEU HIS LYS VAL THR TYR LEU 120 GLN ASN GLY LYS ASP ARG LYS TYR PHE HIS 130 HIS ASN SER ASP PHE HIS ILE PRO LYS ALA 140 THR LEU LYS ASP SER GLY SER TYR PHE CYS 150 ARG GLY LEU VAL GLY SER LYS ASN VAL SER 160 SER GLU THR VAL ASN ILE THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 160.4 -179.9 -79.9 -167.4 2 PRO -70.6 139.2 179.4 35.8 -44.7 3 LYS -83.2 125.1 -179.8 -160.3 173.8 -157.6 169.0 4 ALA -68.7 178.3 177.0 5 VAL -147.8 145.8 177.8 155.6 6 VAL -107.9 135.2 178.5 -159.5 7 PHE -119.8 145.5 178.8 -70.3 109.2 8 LEU -99.8 136.1 -179.3 -91.8 -163.1 9 GLU -120.7 98.4 -4.7 -162.5 79.5 68.5 10 PRO -80.1 179.5 -179.9 37.7 -46.9 11 GLN -53.8 -7.3 -178.9 51.2 161.2 152.8 12 TRP -75.3 111.4 178.8 -52.8 137.1 13 TYR -99.3 8.3 179.4 58.9 46.5 14 SER -136.7 106.3 -178.7 -162.9 15 VAL -128.7 -174.8 179.5 -55.0 16 LEU -106.9 174.4 -175.8 -69.7 167.1 17 GLU -72.1 36.9 176.9 -76.8 -170.7 -46.9 18 LYS -153.8 -17.5 178.4 -85.0 -52.4 177.9 49.4 19 ASP -48.8 124.2 177.0 -78.3 46.5 20 SER -84.0 135.3 -179.9 -66.5 21 VAL -128.5 141.9 177.4 -166.5 22 THR -125.8 134.9 -178.9 8.9 23 LEU -116.2 100.6 179.0 -54.8 68.4 24 LYS -87.1 132.2 -179.9 -69.6 -178.4 -170.3 -63.4 25 CYS -99.5 131.3 -178.3 -170.4 26 GLN -116.8 117.6 179.9 172.4 -131.8 68.4 27 GLY -173.8 -174.1 179.9 28 ALA -100.3 143.9 179.6 29 TYR -114.4 149.2 -178.9 -61.5 67.2 30 SER -75.9 179.7 179.9 54.2 31 PRO -57.8 -82.6 180.0 -34.7 45.6 32 GLU -86.7 56.3 -179.5 -50.6 -166.5 -171.0 33 ASP -168.9 108.3 179.9 167.6 -66.8 34 ASN -122.2 59.1 -178.9 61.1 -55.6 35 SER -126.3 151.3 -178.7 57.3 36 THR -121.7 146.4 177.7 -41.4 37 GLN -109.1 122.9 -179.7 -130.2 -45.4 -82.0 38 TRP -108.2 140.5 -179.8 -80.7 108.7 39 PHE -130.3 130.7 176.1 -72.0 96.4 40 HIS -116.1 82.0 -177.2 -176.4 -160.4 41 ASN 48.9 89.1 177.9 -16.1 -60.5 42 GLU 79.0 -63.4 -179.9 -89.2 -8.2 -56.9 43 SER -59.1 137.1 178.6 -53.0 44 LEU -96.1 132.4 178.5 -46.8 65.9 45 ILE -102.5 118.3 -177.7 26.8 -169.6 46 SER -36.8 -58.8 -177.9 -66.4 47 SER -38.4 140.8 -179.8 122.0 48 GLN -87.8 -30.4 -178.5 62.6 129.0 51.5 49 ALA -34.5 149.7 178.1 50 SER -81.7 3.1 179.7 72.3 51 SER -132.7 135.5 177.9 -96.4 52 TYR -107.9 135.2 -177.6 -167.3 49.8 53 PHE -120.7 127.6 177.5 -178.3 64.5 54 ILE -116.4 101.4 -179.3 -41.8 -179.2 55 ASP -65.8 -59.6 178.3 -159.7 40.3 56 ALA -128.2 111.1 -179.8 57 ALA -74.6 154.3 176.5 58 THR -129.1 173.2 -178.9 78.0 59 VAL -70.4 -9.2 179.7 -58.9 60 ASN -76.0 -18.2 178.6 -70.5 -68.7 61 ASP -81.2 -11.3 -180.0 -66.8 -78.6 62 SER -55.5 158.7 178.2 -58.7 63 GLY 129.3 -168.7 179.2 64 GLU -100.5 136.8 179.4 -51.8 -169.0 -48.9 65 TYR -122.4 137.6 178.0 -72.9 77.1 66 ARG -134.0 145.5 178.9 -48.6 -140.7 -162.2 -169.3 67 CYS -138.8 155.1 -178.9 73.1 68 GLN -163.9 177.3 178.4 -175.4 -161.6 -171.9 69 THR -136.7 -145.4 178.4 80.9 70 ASN -108.5 -16.5 179.4 66.2 68.6 71 LEU -107.2 -3.0 178.4 -60.3 -167.2 72 SER -116.3 145.0 178.0 24.7 73 THR -92.0 135.8 -179.0 72.3 74 LEU -29.9 129.5 -179.4 -170.5 65.1 75 SER -74.4 147.5 177.5 79.1 76 ASP -64.9 160.5 -179.8 -59.5 -52.1 77 PRO -69.2 164.4 178.9 34.2 -43.7 78 VAL -131.6 113.2 -179.0 177.0 79 GLN -77.7 121.0 178.3 -21.6 -76.5 -61.6 80 LEU -114.9 113.7 -178.5 169.2 72.9 81 GLU -96.9 114.3 179.4 -87.7 171.3 27.5 82 VAL -105.6 117.2 -178.4 -177.7 83 HIS -102.9 165.0 -179.8 -54.0 -81.1 84 ILE -121.2 132.6 179.5 -61.7 -164.8 85 GLY 144.8 -177.8 -179.7 86 TRP -76.7 -44.9 -179.5 -80.1 117.4 87 LEU -121.5 167.7 178.7 -63.4 -168.4 88 LEU -162.5 126.5 178.9 170.9 55.4 89 LEU -85.3 129.6 -178.8 179.4 71.3 90 GLN -118.0 156.1 -179.2 -58.1 169.3 -55.5 91 ALA 179.4 143.3 -180.0 92 PRO -58.6 -30.1 179.0 31.2 -44.5 93 ARG -174.1 152.6 -178.9 78.7 -176.4 -162.9 -53.2 94 TRP -110.7 10.2 178.8 -30.8 79.1 95 VAL -92.9 98.4 -179.6 -171.3 96 PHE -115.5 110.8 179.0 -71.2 59.1 97 LYS -80.3 164.7 179.9 -61.2 180.0 -178.2 -178.9 98 GLU -44.2 114.2 -179.5 -53.3 178.2 -64.5 99 GLU 76.1 105.1 -179.3 178.1 -175.2 -58.2 100 ASP 177.6 132.9 179.8 -179.0 65.3 101 PRO -67.4 142.1 -179.4 31.5 -44.9 102 ILE -107.8 135.3 -178.8 -55.3 -177.4 103 HIS -135.3 98.3 -179.9 -171.5 112.8 104 LEU -109.6 125.7 177.5 -36.5 -171.8 105 ARG -110.1 133.5 179.3 160.7 -165.5 174.6 -175.1 106 CYS -92.7 66.6 -178.8 176.8 107 HIS -53.3 125.7 179.4 -179.3 49.6 108 SER -110.3 150.8 179.3 76.4 109 TRP -46.9 138.2 -178.8 -167.9 47.0 110 LYS 43.3 30.6 -177.7 -89.6 -154.6 -84.2 50.4 111 ASN 52.6 8.6 177.0 -66.7 168.4 112 THR -36.9 139.9 -176.9 -59.4 113 ALA -68.5 107.4 179.3 114 LEU -90.3 141.4 -178.7 -174.8 60.6 115 HIS -132.8 158.7 -179.6 -70.4 83.7 116 LYS 48.7 48.0 -179.6 -67.9 -174.5 176.1 -171.8 117 VAL -71.3 148.9 178.2 -170.5 118 THR -148.6 130.5 178.0 42.0 119 TYR -95.6 133.1 179.9 -70.1 97.7 120 LEU -114.6 152.3 178.6 -66.4 80.0 121 GLN -136.7 93.9 179.8 166.6 177.5 42.2 122 ASN 72.8 60.5 178.9 -51.6 -169.1 123 GLY 59.9 9.8 -180.0 124 LYS -124.4 112.5 -179.2 -46.2 -59.4 -179.8 -179.0 125 ASP -65.0 102.6 179.2 -31.0 48.9 126 ARG -57.6 -38.8 179.7 -122.0 -104.7 -141.3 -68.6 127 LYS -152.6 155.9 -179.8 -67.3 178.6 -173.7 179.3 128 TYR -123.2 148.3 179.7 167.2 84.4 129 PHE -145.3 134.8 179.5 -69.4 65.9 130 HIS -57.8 -46.8 177.8 -91.8 118.7 131 HIS -116.9 167.9 -178.7 -67.8 -71.7 132 ASN -72.8 139.7 179.0 -175.3 26.2 133 SER -153.8 -152.0 179.4 55.0 134 ASP -121.8 164.1 -179.2 -65.0 178.1 135 PHE -107.4 130.6 -178.9 174.8 68.5 136 HIS -117.9 152.7 177.8 -121.2 179.1 137 ILE -163.0 138.6 179.9 -63.5 -165.7 138 PRO -83.6 -110.4 -179.7 -22.4 41.2 139 LYS -66.1 163.2 179.8 -74.2 -177.0 -177.3 179.8 140 ALA -67.4 173.5 179.2 141 THR -142.4 29.9 179.6 67.2 142 LEU 34.8 20.0 -179.5 -58.2 176.7 143 LYS -148.4 1.7 179.7 -61.2 179.9 -179.6 -179.1 144 ASP -58.1 -11.2 179.7 -60.6 -58.4 145 SER -63.6 55.7 180.0 -56.3 146 GLY -113.9 146.6 178.6 147 SER -77.6 109.6 -179.5 44.9 148 TYR -99.1 168.2 177.8 -71.8 74.1 149 PHE 173.3 160.4 -178.8 79.3 72.9 150 CYS -124.5 167.1 -179.6 57.9 151 ARG -151.8 158.1 178.8 61.1 174.3 58.7 148.3 152 GLY -174.9 -171.3 179.0 153 LEU -110.9 109.3 176.0 -71.1 -172.9 154 VAL -84.7 108.7 -177.6 164.3 155 GLY 55.0 -136.8 -179.4 156 SER -73.7 -33.3 -177.6 56.7 157 LYS -79.1 153.9 -180.0 67.2 -150.3 -59.9 -178.9 158 ASN -99.2 124.8 -178.3 -159.6 -52.9 159 VAL -112.6 146.8 -178.9 -60.8 160 SER -116.5 163.4 179.4 26.3 161 SER -124.5 150.2 179.5 84.4 162 GLU -58.2 140.1 -178.7 -167.6 168.4 -179.3 163 THR -91.0 122.7 179.2 126.2 164 VAL -89.5 178.9 -179.7 175.9 165 ASN -133.3 98.5 178.9 -88.8 15.8 166 ILE -81.8 111.3 -178.6 -50.8 173.4 167 THR -94.7 -22.7 0.0 -136.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 37.110 47.487 83.337 2 PRO 37.754 44.716 80.754 3 LYS 36.926 45.314 77.092 4 ALA 34.526 42.665 75.855 5 VAL 34.993 40.775 72.564 6 VAL 32.799 39.407 69.821 7 PHE 33.659 36.062 68.256 8 LEU 32.194 34.627 65.072 9 GLU 30.812 31.096 64.912 10 PRO 32.379 30.194 62.469 11 GLN 35.623 32.089 61.885 12 TRP 34.115 33.184 58.575 13 TYR 33.537 36.923 58.631 14 SER 32.669 36.767 54.915 15 VAL 29.687 34.610 53.915 16 LEU 26.867 34.131 51.426 17 GLU 23.146 34.830 51.660 18 LYS 21.859 31.826 53.552 19 ASP 24.838 31.418 55.742 20 SER 23.757 31.185 59.387 21 VAL 26.087 33.292 61.537 22 THR 26.505 33.358 65.322 23 LEU 28.101 36.095 67.338 24 LYS 29.164 34.973 70.768 25 CYS 29.935 37.794 73.152 26 GLN 32.707 37.245 75.708 27 GLY 32.854 39.173 78.968 28 ALA 31.962 39.223 82.654 29 TYR 28.413 39.526 83.972 30 SER 27.230 41.061 87.246 31 PRO 25.304 39.359 90.106 32 GLU 21.600 39.935 89.414 33 ASP 22.248 40.591 85.731 34 ASN 22.884 38.192 82.846 35 SER 22.226 40.504 79.886 36 THR 24.088 41.592 76.727 37 GLN 23.943 44.721 74.542 38 TRP 24.275 44.148 70.803 39 PHE 25.188 46.793 68.202 40 HIS 24.954 46.705 64.415 41 ASN 26.798 49.946 63.573 42 GLU 25.097 52.549 65.735 43 SER 21.782 50.732 65.733 44 LEU 21.020 48.710 68.864 45 ILE 19.735 45.168 68.407 46 SER 17.166 44.240 71.013 47 SER 17.930 40.652 72.135 48 GLN 19.605 40.256 75.562 49 ALA 21.301 36.923 74.799 50 SER 25.073 36.796 75.063 51 SER 24.699 35.409 71.542 52 TYR 23.308 36.938 68.336 53 PHE 21.924 34.629 65.677 54 ILE 21.637 35.132 61.934 55 ASP 19.758 32.074 60.659 56 ALA 19.788 33.166 57.057 57 ALA 21.945 36.200 56.437 58 THR 21.061 38.871 53.868 59 VAL 23.482 41.609 52.778 60 ASN 21.799 43.834 55.380 61 ASP 23.446 41.873 58.188 62 SER 26.716 43.028 56.708 63 GLY 28.631 45.435 58.927 64 GLU 30.365 46.065 62.206 65 TYR 29.107 44.374 65.342 66 ARG 29.721 45.324 68.949 67 CYS 28.363 43.628 72.074 68 GLN 28.783 44.571 75.696 69 THR 27.369 44.178 79.214 70 ASN 27.481 46.263 82.434 71 LEU 30.813 44.750 83.537 72 SER 32.423 44.902 80.093 73 THR 33.441 48.048 78.340 74 LEU 31.998 48.160 74.828 75 SER 33.696 45.748 72.408 76 ASP 35.542 46.890 69.300 77 PRO 33.511 46.227 66.147 78 VAL 33.453 43.024 64.097 79 GLN 33.086 43.454 60.339 80 LEU 30.640 40.937 58.899 81 GLU 30.569 40.855 55.049 82 VAL 27.481 39.387 53.408 83 HIS 27.914 38.539 49.718 84 ILE 25.583 37.407 46.926 85 GLY 26.188 34.543 44.508 86 TRP 26.986 30.881 43.851 87 LEU 30.515 30.705 45.219 88 LEU 32.641 32.575 47.770 89 LEU 36.316 32.167 48.670 90 GLN 36.927 31.955 52.417 91 ALA 39.924 32.268 54.707 92 PRO 40.565 33.632 58.246 93 ARG 42.773 36.308 56.728 94 TRP 44.676 36.961 53.513 95 VAL 47.348 38.798 55.430 96 PHE 50.200 36.317 55.349 97 LYS 53.536 37.359 56.776 98 GLU 56.745 35.475 55.894 99 GLU 56.029 31.840 56.839 100 ASP 52.385 31.055 57.665 101 PRO 49.817 28.337 56.634 102 ILE 47.044 29.061 54.059 103 HIS 43.448 27.775 54.352 104 LEU 40.923 28.433 51.549 105 ARG 37.438 26.960 51.535 106 CYS 35.403 27.478 48.347 107 HIS 32.067 28.059 50.077 108 SER 29.137 27.615 47.711 109 TRP 25.586 28.883 48.137 110 LYS 23.439 26.707 50.433 111 ASN 26.377 24.277 50.645 112 THR 24.801 23.249 47.300 113 ALA 27.040 20.465 45.895 114 LEU 29.949 21.864 43.945 115 HIS 31.859 19.506 41.669 116 LYS 35.079 19.526 39.648 117 VAL 36.276 22.390 41.803 118 THR 39.459 24.278 41.056 119 TYR 41.144 26.994 43.060 120 LEU 42.867 29.507 40.849 121 GLN 45.696 31.849 41.528 122 ASN 46.031 34.423 38.781 123 GLY 44.075 32.717 36.007 124 LYS 46.030 29.602 36.879 125 ASP 44.204 26.833 38.716 126 ARG 46.581 26.014 41.591 127 LYS 44.584 22.806 42.247 128 TYR 41.717 20.559 41.093 129 PHE 39.405 18.264 43.105 130 HIS 36.682 15.966 41.778 131 HIS 34.357 17.083 44.548 132 ASN 34.525 20.167 46.699 133 SER 36.929 20.290 49.621 134 ASP 39.442 22.891 50.818 135 PHE 42.842 24.203 49.660 136 HIS 45.922 23.997 52.005 137 ILE 49.434 25.589 52.045 138 PRO 52.240 25.909 54.723 139 LYS 54.946 28.628 54.696 140 ALA 54.799 31.832 52.628 141 THR 56.294 32.188 49.143 142 LEU 56.977 35.929 48.929 143 LYS 54.712 35.693 45.836 144 ASP 51.485 34.457 47.407 145 SER 50.298 37.956 46.481 146 GLY 48.054 36.392 43.857 147 SER 44.429 37.080 43.052 148 TYR 42.629 33.865 43.980 149 PHE 39.076 32.560 43.365 150 CYS 37.257 29.301 42.711 151 ARG 34.933 27.615 40.246 152 GLY 33.025 24.364 39.895 153 LEU 29.797 22.843 38.679 154 VAL 26.677 23.552 40.673 155 GLY 24.663 20.838 39.024 156 SER 25.005 21.369 35.287 157 LYS 25.973 25.073 35.367 158 ASN 29.399 26.526 35.960 159 VAL 29.704 28.990 38.805 160 SER 32.485 31.449 39.574 161 SER 33.530 33.167 42.779 162 GLU 34.603 36.748 43.409 163 THR 38.361 36.809 43.276 164 VAL 40.109 37.748 46.522 165 ASN 43.746 38.816 47.000 166 ILE 45.935 36.826 49.390 167 THR 48.857 39.154 49.996 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S/T T/P T 10 T C S S S S S S S S 20 S S S S S S S S C T 30 T T T/S S S S S S S/T T 40 T T/S S S S S S C C S 50 S S S S S S/S S S S C 60 C C S S S S S S T T 70 T T S S S S S/S S S S 80 S S S S S S/S S S S S 90 S S C S S S S S/S S S 100 S S S S S S S S/T T T 110 T S S S S S/S S S S S/T 120 T T T/S S S S S S S S/S 130 S S S S/S S S S S S S 140 S S C C S S S S S S 150 S S T T T T/S S S S S 160 S S S S S/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B E E E E E S 10 S e E E E e T t 20 E E E E E E t 30 T T t E E E E 40 e T E E E S e 50 E E E E S S g G G 60 G g E E E E E E S 70 S S B e E E 80 E E E S e E E E E 90 S S B S S 100 E E E E E E E e G 110 G g e E E E E E E E 120 E e S e E E E E E E 130 E e e E E E E S 140 S E E E E E 150 E E E E e T E E E E 160 e E E E B Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 58.7 39.7 72.0 2 PRO 50.6 40.6 68.2 3 LYS 67.8 39.1 89.8 4 ALA 70.8 97.5 55.2 5 VAL 59.3 50.0 63.1 6 VAL 118.8 100.0 39.1 7 PHE 65.7 39.4 72.6 8 LEU 140.1 94.8 42.4 9 GLU 55.2 39.8 65.5 10 PRO 62.9 50.5 73.5 11 GLN 66.8 45.0 57.5 12 TRP 187.3 91.4 56.2 13 TYR 109.0 60.2 68.6 14 SER 73.3 87.7 54.1 15 VAL 114.1 96.0 45.7 16 LEU 146.9 99.4 51.7 17 GLU 98.6 71.1 52.2 18 LYS 93.3 53.8 61.8 19 ASP 89.7 81.2 55.1 20 SER 41.0 49.1 71.7 21 VAL 117.4 98.8 38.5 22 THR 76.9 71.9 50.6 23 LEU 147.5 99.8 29.5 24 LYS 72.3 41.7 73.8 25 CYS 99.2 100.0 46.1 26 GLN 48.4 32.6 70.2 27 GLY 22.4 64.5 57.7 28 ALA 23.6 32.5 66.7 29 TYR 134.8 74.5 63.7 30 SER 69.7 83.3 49.5 31 PRO 16.2 13.0 75.7 32 GLU 0.0 0.0 86.1 33 ASP 68.8 62.3 86.2 34 ASN 16.1 13.3 79.2 35 SER 43.3 51.8 77.0 36 THR 106.2 99.3 48.7 37 GLN 91.1 61.3 61.5 38 TRP 204.9 99.9 44.5 39 PHE 125.9 75.5 57.5 40 HIS 117.2 78.0 61.4 41 ASN 58.7 48.6 70.2 42 GLU 1.2 0.9 87.7 43 SER 18.5 22.2 74.4 44 LEU 46.2 31.3 77.2 45 ILE 112.8 78.6 54.0 46 SER 0.0 0.0 89.4 47 SER 36.9 44.2 70.7 48 GLN 45.8 30.8 82.6 49 ALA 33.1 45.6 83.0 50 SER 41.5 49.7 72.3 51 SER 53.7 64.2 64.5 52 TYR 134.0 74.1 47.7 53 PHE 77.1 46.2 66.9 54 ILE 134.0 93.4 47.2 55 ASP 21.8 19.8 67.4 56 ALA 35.7 49.2 69.9 57 ALA 72.6 100.0 45.9 58 THR 46.3 43.3 76.9 59 VAL 65.3 54.9 67.2 60 ASN 10.1 8.4 83.9 61 ASP 83.6 75.6 52.9 62 SER 56.0 66.9 65.3 63 GLY 15.3 43.9 70.0 64 GLU 75.3 54.4 66.3 65 TYR 179.3 99.1 36.4 66 ARG 123.5 59.1 57.9 67 CYS 99.2 100.0 32.6 68 GLN 109.4 73.6 51.1 69 THR 103.6 96.9 58.2 70 ASN 67.5 55.9 71.4 71 LEU 92.7 62.7 65.1 72 SER 83.3 99.7 48.4 73 THR 55.0 51.4 67.4 74 LEU 94.1 63.7 65.0 75 SER 83.5 99.9 56.4 76 ASP 40.5 36.7 72.8 77 PRO 100.4 80.7 66.9 78 VAL 90.2 75.9 57.5 79 GLN 55.4 37.3 70.8 80 LEU 147.5 99.8 38.3 81 GLU 52.7 38.0 65.4 82 VAL 118.8 100.0 46.0 83 HIS 104.4 69.5 62.7 84 ILE 49.3 34.4 71.2 85 GLY 8.6 24.7 71.8 86 TRP 130.3 63.6 50.4 87 LEU 147.8 100.0 41.1 88 LEU 140.0 94.7 51.7 89 LEU 147.5 99.8 35.3 90 GLN 147.0 98.9 41.9 91 ALA 72.5 99.9 38.8 92 PRO 85.1 68.4 68.2 93 ARG 120.2 57.5 65.9 94 TRP 169.7 82.8 45.1 95 VAL 31.5 26.5 63.1 96 PHE 165.1 99.0 57.0 97 LYS 8.3 4.8 86.4 98 GLU 19.3 14.0 71.6 99 GLU 43.5 31.4 70.5 100 ASP 83.4 75.4 61.8 101 PRO 40.0 32.1 77.4 102 ILE 143.2 99.8 39.1 103 HIS 84.5 56.2 65.1 104 LEU 147.5 99.8 28.8 105 ARG 145.0 69.4 65.2 106 CYS 99.2 100.0 40.1 107 HIS 144.0 95.9 69.5 108 SER 82.0 98.0 54.8 109 TRP 133.1 64.9 61.1 110 LYS 78.5 45.3 67.7 111 ASN 35.4 29.3 85.3 112 THR 69.1 64.7 62.2 113 ALA 17.0 23.4 78.8 114 LEU 147.8 100.0 45.9 115 HIS 86.7 57.7 61.4 116 LYS 57.5 33.2 70.6 117 VAL 118.6 99.8 47.9 118 THR 91.0 85.1 47.6 119 TYR 179.6 99.2 39.0 120 LEU 146.2 98.9 58.4 121 GLN 128.1 86.2 61.1 122 ASN 58.1 48.1 72.1 123 GLY 4.7 13.6 64.0 124 LYS 22.1 12.7 87.1 125 ASP 66.6 60.2 64.6 126 ARG 133.1 63.7 62.2 127 LYS 79.4 45.8 65.8 128 TYR 99.0 54.7 59.3 129 PHE 107.7 64.6 65.3 130 HIS 29.5 19.6 74.7 131 HIS 39.9 26.6 78.9 132 ASN 89.3 73.8 62.2 133 SER 37.3 44.7 70.7 134 ASP 65.5 59.3 64.2 135 PHE 166.4 99.8 33.7 136 HIS 30.3 20.2 80.9 137 ILE 128.4 89.5 52.2 138 PRO 24.0 19.3 71.7 139 LYS 42.5 24.5 78.4 140 ALA 65.4 90.0 66.9 141 THR 48.6 45.5 75.7 142 LEU 23.9 16.2 77.2 143 LYS 12.4 7.1 90.1 144 ASP 105.3 95.3 55.7 145 SER 31.4 37.6 75.3 146 GLY 33.4 95.8 70.7 147 SER 44.2 52.9 74.8 148 TYR 180.4 99.7 44.2 149 PHE 135.2 81.1 58.2 150 CYS 99.2 100.0 32.8 151 ARG 118.8 56.9 66.7 152 GLY 32.9 94.6 52.5 153 LEU 94.1 63.7 66.2 154 VAL 108.2 91.1 36.3 155 GLY 0.0 0.0 83.0 156 SER 0.0 0.0 85.5 157 LYS 55.2 31.9 77.5 158 ASN 47.6 39.4 65.8 159 VAL 114.4 96.3 44.5 160 SER 15.9 19.0 72.3 161 SER 82.2 98.3 53.8 162 GLU 21.7 15.7 80.4 163 THR 53.9 50.5 63.5 164 VAL 81.9 69.0 58.1 165 ASN 28.5 23.6 72.8 166 ILE 143.4 99.9 30.0 167 THR 27.0 25.2 73.0