Protein Data Bank File : 1e6ba Title : TRANSFERASE 27-JUL-00 1E6B Number of Amino Acid Residues : 194 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS LEU LYS LEU TYR SER TYR TRP ARG SER 10 SER CYS ALA HIS ARG VAL ARG ILE ALA LEU 20 ALA LEU LYS GLY LEU ASP TYR GLU TYR ILE 30 PRO VAL ASN LEU LEU LYS GLY ASP GLN PHE 40 ASP SER ASP PHE LYS LYS ILE ASN PRO MET 50 GLY THR VAL PRO ALA LEU VAL ASP GLY ASP 60 VAL VAL ILE ASN ASP SER PHE ALA ILE ILE 70 MET TYR LEU ASP GLU LYS TYR PRO GLU PRO 80 PRO LEU LEU PRO ARG ASP LEU HIS LYS ARG 90 ALA VAL ASN TYR GLN ALA MET SER ILE VAL 100 LEU SER GLY ILE GLN PRO THR ALA TRP VAL 110 ASN ASN ALA ILE THR LYS GLY PHE THR ALA 120 LEU GLU LYS LEU LEU VAL ASN CYS ALA GLY 130 LYS HIS ALA THR GLY ASP GLU ILE TYR LEU 140 ALA ASP LEU PHE LEU ALA PRO GLN ILE HIS 150 GLY ALA ILE ASN ARG PHE GLN ILE ASN MET 160 GLU PRO TYR PRO THR LEU ALA LYS CYS TYR 170 GLU SER TYR ASN GLU LEU PRO ALA PHE GLN 180 ASN ALA LEU PRO GLU LYS GLN PRO ASP ALA 190 PRO SER SER THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 86.7 178.6 0.0 0.0 0.0 0.0 2 LEU -63.2 148.3 175.1 -61.5 169.2 3 LYS -125.9 140.7 176.4 -64.4 172.2 -166.1 176.5 4 LEU -127.4 120.2 174.4 176.7 76.3 5 TYR -85.1 120.0 -172.0 -75.0 -87.2 6 SER -141.0 158.7 173.2 172.4 7 TYR -128.0 132.1 -173.5 176.1 54.2 8 TRP -55.8 -38.6 -177.5 69.8 -76.6 9 ARG -90.3 -0.9 -177.7 -136.9 169.0 176.1 -173.4 10 SER -75.5 120.6 178.0 155.0 11 SER -64.6 -32.1 -177.7 68.8 12 CYS -66.5 -40.4 179.0 -65.4 13 ALA -69.3 -33.5 177.6 14 HIS -57.9 -46.5 -179.9 -178.9 176.8 15 ARG -53.6 -49.1 -177.7 -59.1 166.0 -173.2 160.4 16 VAL -63.7 -42.0 179.5 173.5 17 ARG -58.8 -33.7 178.6 -61.7 -171.8 -57.8 -102.2 18 ILE -65.7 -46.2 -176.8 -64.9 167.0 19 ALA -58.3 -46.6 -179.4 20 LEU -59.5 -43.7 179.1 -74.8 157.1 21 ALA -64.9 -44.0 177.7 22 LEU -66.1 -28.8 -179.9 -66.6 157.7 23 LYS -85.0 -7.2 180.0 -71.1 -60.8 -171.6 177.0 24 GLY 70.7 30.9 -176.6 25 LEU -98.6 124.0 177.8 -65.0 163.5 26 ASP -76.5 150.7 179.2 -59.3 -22.9 27 TYR -163.4 160.7 175.4 62.6 -80.0 28 GLU -88.2 117.0 178.3 -174.5 178.0 13.2 29 TYR -83.5 116.5 178.3 -171.8 -69.6 30 ILE -112.6 107.6 -178.7 -51.8 178.5 31 PRO -66.0 138.3 177.0 -14.3 30.1 32 VAL -133.8 101.2 -177.7 -172.3 33 ASN -71.9 100.3 -179.2 -166.2 -39.2 34 LEU -68.1 -32.8 176.7 -55.9 176.4 35 LEU -63.0 -45.0 -178.0 -72.4 -179.9 36 LYS -75.4 -2.1 -178.7 -65.9 -165.3 167.2 170.3 37 GLY 70.5 33.8 176.6 38 ASP -71.1 -17.2 178.3 -60.1 -16.4 39 GLN -73.7 -9.0 178.1 69.1 -79.3 34.5 40 PHE -103.2 6.8 174.8 -56.7 -67.7 41 ASP -64.0 135.2 -178.7 177.1 56.2 42 SER -66.8 -28.4 -179.7 -97.5 43 ASP -74.4 -38.6 176.1 -75.8 -29.5 44 PHE -61.9 -39.9 175.6 165.3 77.4 45 LYS -61.0 -30.3 175.5 -85.0 -89.9 -140.2 142.7 46 LYS -66.9 -42.3 -179.4 -165.1 -104.0 172.0 130.4 47 ILE -80.7 -36.5 -177.8 -63.6 -156.0 48 ASN -124.7 72.8 -177.3 -174.0 19.9 49 PRO -54.9 -33.5 175.7 7.3 -12.8 50 MET -64.7 -26.2 175.3 -63.1 -60.2 -66.3 51 GLY 78.2 3.9 -175.6 52 THR -103.1 159.8 176.3 51.7 53 VAL -124.9 131.3 7.5 167.2 54 PRO -77.7 158.3 177.2 33.2 -43.7 55 ALA -141.0 128.2 180.0 56 LEU -105.4 125.4 174.5 -177.2 76.3 57 VAL -105.3 121.2 -179.1 -172.3 58 ASP -122.7 80.9 -168.4 179.7 10.0 59 GLY 70.3 -118.2 176.7 60 ASP -80.0 -17.8 -177.0 -87.0 -2.8 61 VAL -91.2 126.5 178.1 -177.0 62 VAL -116.3 121.9 -179.9 177.2 63 ILE -115.5 129.3 174.0 -44.8 -67.0 64 ASN -111.2 170.6 -176.5 -56.6 81.1 65 ASP 78.8 122.2 -179.1 -175.4 76.1 66 SER -55.6 -41.8 -178.1 64.2 67 PHE -71.5 -45.2 179.9 173.3 67.5 68 ALA -64.3 -39.9 179.7 69 ILE -61.9 -43.6 -177.5 -67.3 166.4 70 ILE -64.7 -41.3 178.9 -71.3 165.7 71 MET -66.9 -39.6 177.8 -68.8 -58.9 89.3 72 TYR -62.1 -46.1 177.8 175.6 86.5 73 LEU -60.2 -41.5 -178.5 -59.9 170.2 74 ASP -67.2 -36.1 179.1 -162.2 42.0 75 GLU -78.0 -30.3 -177.9 -67.6 171.5 -3.9 76 LYS -83.6 -35.3 -176.1 -178.4 162.8 175.3 -172.8 77 TYR -128.4 81.7 -171.5 -52.6 -79.3 78 PRO -63.3 -24.2 -177.4 -13.4 22.5 79 GLU -92.3 156.2 -51.7 -46.7 -159.7 -25.7 80 PRO -43.9 143.2 -177.3 34.2 -26.8 81 PRO -66.4 135.6 173.7 27.6 -34.4 82 LEU -90.2 2.1 173.8 -61.8 173.0 83 LEU -131.4 143.1 -179.7 -73.4 160.1 84 PRO -74.4 173.6 176.2 32.2 -34.5 85 ARG -76.6 -37.0 -176.8 -90.2 -170.3 -25.8 -154.7 86 ASP -65.1 122.2 -176.7 -176.9 85.4 87 LEU -58.8 -40.0 177.0 -60.4 -179.3 88 HIS -64.1 -48.6 178.4 -173.8 -160.8 89 LYS -61.6 -34.0 172.9 -69.1 176.9 -168.9 142.9 90 ARG -62.4 -43.7 178.1 -67.7 170.0 80.8 88.8 91 ALA -61.5 -41.9 177.4 92 VAL -59.5 -39.6 179.1 175.0 93 ASN -61.9 -43.9 179.7 -87.3 -87.1 94 TYR -65.1 -33.8 179.6 -66.9 -49.4 95 GLN -68.8 -41.3 179.4 -71.8 174.7 78.2 96 ALA -63.7 -44.5 177.2 97 MET -55.8 -49.7 -177.3 -179.7 -75.9 -66.5 98 SER -66.8 -36.4 178.0 175.3 99 ILE -60.8 -43.4 178.4 -70.3 163.4 100 VAL -69.0 -51.2 -174.8 172.2 101 LEU -58.3 -47.4 -172.0 179.2 65.3 102 SER -120.0 -14.5 177.9 71.5 103 GLY -82.4 -65.7 -174.4 104 ILE -87.9 -55.3 -176.3 -49.0 175.7 105 GLN -32.0 -63.2 179.3 0.0 0.0 0.0 106 PRO -67.0 78.7 -159.2 -10.9 26.6 107 THR 42.3 160.7 179.1 79.2 108 ALA -140.9 145.9 179.6 109 TRP -86.7 131.3 179.2 -172.0 -112.3 110 VAL -108.3 121.0 -177.9 178.3 111 ASN -102.5 94.8 177.6 -171.5 -37.0 112 ASN -92.1 -9.9 167.7 -77.9 137.9 113 ALA -58.9 -43.8 175.1 114 ILE -60.1 -44.1 177.8 -80.8 172.9 115 THR -48.5 -53.0 -178.5 -63.7 116 LYS -57.1 -53.5 -179.2 178.2 -173.1 165.6 66.3 117 GLY -67.7 -40.6 176.5 118 PHE -64.6 -34.3 178.9 -78.6 13.1 119 THR -62.2 -44.7 -179.2 -63.1 120 ALA -65.3 -45.4 179.4 121 LEU -59.4 -40.0 178.0 -72.0 163.1 122 GLU -61.7 -46.2 175.0 179.9 76.4 19.3 123 LYS -54.4 -46.6 -178.0 -158.9 166.4 -77.4 100.2 124 LEU -67.9 -43.1 -171.7 176.1 75.6 125 LEU -93.4 -13.1 -175.0 -62.8 178.6 126 VAL -61.2 -24.6 -179.5 65.8 127 ASN -96.7 12.6 175.7 -67.8 -51.4 128 CYS -99.9 104.7 -176.8 -65.0 129 ALA -67.5 143.0 178.6 130 GLY 142.5 167.7 -178.8 131 LYS -68.3 -34.1 -173.7 -78.0 -178.3 139.5 165.6 132 HIS -118.7 -161.4 -174.7 -51.1 -58.7 133 ALA -59.5 -45.6 -178.4 134 THR -134.2 60.1 178.8 64.2 135 GLY 120.7 -167.7 -176.2 136 ASP -93.0 2.1 170.5 -69.2 -23.9 137 GLU -114.0 161.6 179.6 -49.8 -60.2 -47.5 138 ILE -82.7 129.7 178.8 -70.5 -65.3 139 TYR -130.7 -176.2 -177.4 -60.1 -61.2 140 LEU -48.1 -47.2 -178.8 174.4 76.7 141 ALA -54.2 -40.0 179.2 142 ASP -62.4 -35.9 178.3 -60.5 -67.2 143 LEU -69.8 -26.8 175.1 -81.7 62.8 144 PHE -83.2 -40.9 178.3 -84.9 76.9 145 LEU -67.5 -44.3 -176.3 -73.0 -171.7 146 ALA -53.3 -52.5 -176.8 147 PRO -66.1 -35.1 179.5 -16.1 25.5 148 GLN -66.5 -44.0 178.8 -172.6 83.0 -63.0 149 ILE -70.6 -36.7 -179.0 -63.5 164.2 150 HIS -64.1 -41.7 -179.2 -177.3 -86.2 151 GLY -68.3 -41.6 -179.6 152 ALA -59.4 -49.2 -179.3 153 ILE -66.2 -51.1 -175.8 -65.6 168.7 154 ASN -78.5 -27.7 178.9 -60.1 -64.3 155 ARG -104.3 -26.7 -177.3 -60.9 -174.7 -104.0 -168.1 156 PHE -119.2 3.1 -179.9 -64.5 -77.7 157 GLN 50.3 44.0 178.0 -55.7 173.4 177.3 158 ILE -76.6 131.2 174.3 -74.9 134.4 159 ASN -79.1 123.1 -177.5 -174.2 -19.9 160 MET -91.4 2.0 -179.9 -66.9 -63.9 -50.9 161 GLU -64.3 -28.3 177.4 65.6 174.8 -48.5 162 PRO -69.1 -10.6 -176.1 -23.0 30.4 163 TYR -123.6 72.9 -172.8 -41.1 -72.1 164 PRO -59.3 -39.0 177.9 20.6 -35.3 165 THR -63.9 -43.7 -179.4 -51.7 166 LEU -66.1 -38.5 -179.6 -58.0 -169.7 167 ALA -63.4 -42.1 176.6 168 LYS -57.1 -51.1 178.3 166.1 -164.4 82.9 179.8 169 CYS -52.0 -51.7 -176.7 -70.8 170 TYR -66.4 -36.6 176.2 -166.3 65.8 171 GLU -66.7 -36.0 178.3 174.6 50.6 43.6 172 SER -62.3 -18.7 179.8 87.9 173 TYR -89.4 -12.0 -172.4 -53.8 -36.5 174 ASN -63.8 -35.5 179.8 -166.2 53.9 175 GLU -90.1 -0.4 -174.8 67.4 -169.2 63.3 176 LEU -93.1 116.4 -177.1 -57.9 -177.9 177 PRO -53.6 -41.6 -177.0 -33.6 44.8 178 ALA -57.2 -40.7 178.6 179 PHE -70.9 -42.5 -179.8 -71.6 71.9 180 GLN -64.4 -44.5 -178.1 -84.1 -164.9 26.7 181 ASN -62.4 -33.6 -174.1 -68.5 -17.0 182 ALA -83.9 -6.1 -179.5 183 LEU -55.6 144.2 178.8 -65.6 167.2 184 PRO -51.2 -46.6 -175.8 -34.2 42.1 185 GLU -64.8 -18.0 178.9 46.2 -81.4 28.5 186 LYS -90.9 -2.6 -172.5 -57.0 -76.3 -145.6 -97.6 187 GLN -80.4 159.3 -177.1 -54.4 -49.6 -51.9 188 PRO -57.1 -33.3 -177.6 -27.0 33.4 189 ASP -97.7 7.9 -178.8 59.1 -40.6 190 ALA -73.6 154.7 177.4 191 PRO -59.0 140.9 -171.9 -12.2 22.9 192 SER -80.2 159.9 175.5 -25.6 193 SER -99.5 -20.7 173.8 -151.4 194 THR -78.7 11.5 0.0 17.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 31.434 23.678 106.069 2 LEU 29.091 24.732 103.280 3 LYS 25.894 26.597 104.058 4 LEU 22.836 26.824 101.793 5 TYR 20.219 29.547 102.234 6 SER 17.135 27.826 100.939 7 TYR 13.357 28.002 100.851 8 TRP 11.470 24.691 100.660 9 ARG 9.194 25.690 97.770 10 SER 11.783 27.561 95.688 11 SER 12.403 25.657 92.457 12 CYS 15.785 27.435 92.098 13 ALA 16.863 26.203 95.534 14 HIS 15.464 22.725 94.626 15 ARG 17.923 22.562 91.660 16 VAL 20.901 23.290 93.946 17 ARG 19.777 20.742 96.573 18 ILE 19.893 18.010 93.927 19 ALA 23.430 19.025 92.962 20 LEU 24.646 18.927 96.594 21 ALA 23.044 15.487 97.106 22 LEU 24.567 14.080 93.873 23 LYS 28.017 15.397 94.873 24 GLY 27.654 13.736 98.337 25 LEU 28.237 17.132 99.962 26 ASP 27.114 17.878 103.537 27 TYR 25.822 21.342 104.375 28 GLU 23.931 23.493 106.825 29 TYR 20.400 24.200 105.558 30 ILE 19.446 27.774 106.504 31 PRO 15.763 28.434 105.867 32 VAL 14.708 31.733 104.291 33 ASN 10.908 32.110 104.205 34 LEU 10.300 33.925 100.897 35 LEU 6.523 34.308 101.461 36 LYS 7.136 36.018 104.822 37 GLY 9.810 38.296 103.349 38 ASP 12.811 37.007 105.331 39 GLN 15.077 37.725 102.334 40 PHE 14.749 41.491 103.000 41 ASP 16.048 41.164 106.563 42 SER 19.110 43.383 107.116 43 ASP 21.279 40.740 108.851 44 PHE 20.732 38.226 106.057 45 LYS 21.604 41.074 103.649 46 LYS 24.882 41.445 105.517 47 ILE 25.808 37.843 104.795 48 ASN 24.146 37.754 101.346 49 PRO 24.414 41.271 99.905 50 MET 23.017 40.098 96.593 51 GLY 19.925 39.177 98.642 52 THR 18.738 36.244 96.585 53 VAL 17.880 32.634 97.453 54 PRO 19.362 30.185 96.852 55 ALA 22.717 31.344 98.155 56 LEU 25.678 29.052 98.859 57 VAL 28.243 30.114 101.467 58 ASP 31.602 28.399 101.142 59 GLY 33.659 30.109 103.874 60 ASP 34.142 33.717 102.785 61 VAL 32.653 32.986 99.374 62 VAL 28.980 33.611 98.744 63 ILE 27.554 32.411 95.446 64 ASN 24.092 33.380 94.228 65 ASP 22.162 32.115 91.207 66 SER 21.137 28.478 90.876 67 PHE 23.151 27.940 87.682 68 ALA 26.293 29.678 88.966 69 ILE 26.077 27.709 92.258 70 ILE 25.707 24.401 90.429 71 MET 28.686 25.205 88.113 72 TYR 30.791 26.232 91.094 73 LEU 29.966 22.931 92.792 74 ASP 30.706 20.915 89.642 75 GLU 34.005 22.704 89.144 76 LYS 35.150 22.538 92.785 77 TYR 33.943 18.965 93.387 78 PRO 34.091 17.297 89.987 79 GLU 32.760 13.817 90.836 80 PRO 30.204 12.623 89.579 81 PRO 30.397 15.032 86.652 82 LEU 27.269 17.118 85.959 83 LEU 28.258 17.561 82.298 84 PRO 29.034 14.833 79.771 85 ARG 32.198 14.604 77.728 86 ASP 30.594 15.004 74.280 87 LEU 30.667 18.677 73.248 88 HIS 27.325 18.451 71.479 89 LYS 25.600 16.780 74.478 90 ARG 27.133 19.459 76.725 91 ALA 25.595 22.078 74.427 92 VAL 22.163 20.413 74.726 93 ASN 22.494 20.464 78.503 94 TYR 23.266 24.200 78.470 95 GLN 20.326 24.854 76.098 96 ALA 17.937 22.872 78.333 97 MET 19.255 24.856 81.334 98 SER 18.695 28.156 79.529 99 ILE 15.096 27.366 78.424 100 VAL 14.221 26.698 82.047 101 LEU 16.333 29.491 83.573 102 SER 15.392 32.304 81.219 103 GLY 12.669 30.831 79.004 104 ILE 10.068 29.662 81.557 105 GLN 10.925 30.605 85.146 106 PRO 10.197 34.344 84.958 107 THR -12.576 29.284 87.269 108 ALA -9.114 27.799 86.607 109 TRP -5.798 29.345 85.568 110 VAL -4.351 28.066 82.316 111 ASN -0.546 28.306 82.151 112 ASN 0.515 28.312 78.526 113 ALA 3.922 29.895 79.268 114 ILE 4.739 26.374 80.528 115 THR 3.208 24.858 77.344 116 LYS 5.605 26.980 75.299 117 GLY 8.739 26.084 77.264 118 PHE 7.897 22.427 77.675 119 THR 7.245 22.202 73.915 120 ALA 10.778 23.565 73.291 121 LEU 12.359 21.246 75.854 122 GLU 10.596 18.247 74.279 123 LYS 11.773 19.366 70.839 124 LEU 15.323 19.672 72.152 125 LEU 15.577 16.419 74.106 126 VAL 13.558 13.901 72.071 127 ASN 16.580 12.991 69.954 128 CYS 18.822 12.226 72.935 129 ALA 18.708 8.453 73.498 130 GLY 18.831 7.463 77.169 131 LYS 17.157 7.079 80.547 132 HIS 17.447 10.748 81.475 133 ALA 17.610 14.057 79.594 134 THR 20.860 13.432 77.644 135 GLY 21.890 9.804 78.100 136 ASP 22.004 7.232 80.821 137 GLU 23.666 9.396 83.480 138 ILE 22.305 12.451 85.293 139 TYR 23.573 15.798 84.030 140 LEU 22.876 19.541 84.340 141 ALA 19.640 19.432 82.261 142 ASP 18.108 16.923 84.690 143 LEU 18.759 19.237 87.661 144 PHE 16.884 21.969 85.797 145 LEU 14.057 19.729 84.553 146 ALA 13.153 18.017 87.831 147 PRO 12.166 21.161 89.830 148 GLN 10.437 22.714 86.810 149 ILE 8.301 19.625 86.164 150 HIS 7.566 19.158 89.894 151 GLY 6.368 22.752 90.052 152 ALA 4.288 22.428 86.832 153 ILE 2.534 19.315 88.128 154 ASN 2.104 20.432 91.743 155 ARG 1.283 24.133 91.294 156 PHE -0.342 24.240 87.851 157 GLN -1.724 20.736 87.435 158 ILE -0.009 20.413 84.058 159 ASN -0.691 17.186 82.207 160 MET 2.620 15.725 81.045 161 GLU 1.298 13.364 78.351 162 PRO 2.015 15.757 75.498 163 TYR 5.769 15.672 76.391 164 PRO 6.749 11.997 76.414 165 THR 10.496 12.686 76.599 166 LEU 9.966 15.013 79.539 167 ALA 7.619 12.513 81.186 168 LYS 10.255 9.789 80.756 169 CYS 12.832 12.071 82.360 170 TYR 10.660 12.910 85.332 171 GLU 9.652 9.281 85.943 172 SER 13.369 8.390 85.769 173 TYR 14.041 10.628 88.842 174 ASN 11.556 8.914 91.165 175 GLU 13.998 6.166 92.211 176 LEU 17.132 8.341 92.590 177 PRO 17.832 9.212 96.203 178 ALA 19.559 12.516 95.389 179 PHE 16.358 13.655 93.649 180 GLN 13.970 12.284 96.285 181 ASN 15.866 13.896 99.138 182 ALA 15.936 17.317 97.457 183 LEU 12.108 17.532 96.990 184 PRO 10.395 20.565 98.503 185 GLU 8.184 18.440 100.775 186 LYS 11.247 16.809 102.422 187 GLN 13.030 20.023 103.479 188 PRO 13.503 21.205 107.050 189 ASP 11.218 24.240 106.543 190 ALA 8.507 22.370 104.601 191 PRO 4.952 22.182 105.905 192 SER 4.450 19.489 108.441 193 SER 2.744 16.138 108.640 194 THR 2.497 16.789 112.372 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S C C H 10 H H H H H H H H H H 20 H H H H/S S S S S/S S S 30 S S S/T T T T T T T T 40 H H H H H H H H/T T T 50 T/S S S/P S/S S S S S/T T T 60 T/S S S S S/H H H H H H 70 H H H H H H H H/T T T 80 T S S S S H H H H H 90 H H H H H H H H H H 100 H H/T T T T C/X X/S S S S 110 S/H H H H H H H H H H 120 H H H H H H S S S S 130 S T T T T S S S S/H H 140 H H H H H H/H H H H H 150 H H H H H C S S S S 160 S C H H H H H H H H 170 H H H H C H H H H H 180 H H H/T T T T C C C S 190 S 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 t T T h 10 H H H H H H H H H H 20 H H h T t E E E 30 E e t T T T g G G G 40 h H H H H H H h T T 50 t S e E E E E T T 60 E E E E h H H H H H 70 H H H H H H h S S 80 S S S h H H H H 90 H H H H H H H H H H 100 H H h T t 110 h H H H H H H H H H 120 H H H H H h T t S 130 S B T T B S S h H 140 H H H H H H H H H H 150 H H H H H H h t 160 T T h H H H H H H H 170 H H H h T h H H H H 180 H H h G G G g T T t 190 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 97.6 56.3 91.7 2 LEU 139.8 94.6 47.4 3 LYS 91.3 52.6 65.7 4 LEU 147.8 100.0 36.1 5 TYR 166.0 91.7 29.9 6 SER 83.6 100.0 43.9 7 TYR 167.8 92.7 48.8 8 TRP 161.7 78.9 52.0 9 ARG 102.5 49.1 59.1 10 SER 68.8 82.4 55.1 11 SER 64.1 76.7 75.5 12 CYS 56.8 57.3 73.4 13 ALA 72.6 100.0 57.6 14 HIS 147.5 98.2 43.8 15 ARG 206.1 98.6 37.6 16 VAL 118.8 100.0 30.4 17 ARG 206.6 98.9 53.8 18 ILE 143.5 100.0 37.0 19 ALA 72.6 100.0 35.9 20 LEU 147.8 100.0 31.1 21 ALA 46.8 64.5 68.5 22 LEU 120.7 81.6 37.6 23 LYS 173.4 100.0 50.7 24 GLY 0.0 0.0 84.7 25 LEU 123.0 83.2 46.7 26 ASP 0.0 0.0 88.1 27 TYR 144.3 79.7 49.4 28 GLU 46.3 33.4 67.1 29 TYR 165.5 91.4 50.2 30 ILE 100.1 69.8 53.3 31 PRO 70.0 56.2 64.3 32 VAL 114.2 96.1 42.4 33 ASN 75.9 62.8 59.7 34 LEU 107.4 72.6 53.8 35 LEU 21.9 14.8 87.8 36 LYS 31.4 18.1 87.5 37 GLY 18.2 52.3 74.5 38 ASP 54.2 49.1 65.8 39 GLN 118.7 79.9 46.1 40 PHE 41.6 24.9 79.0 41 ASP 38.2 34.5 76.1 42 SER 3.4 4.1 83.0 43 ASP 2.0 1.8 85.2 44 PHE 149.3 89.5 49.9 45 LYS 80.5 46.4 75.5 46 LYS 17.2 9.9 84.8 47 ILE 64.5 45.0 66.2 48 ASN 120.9 100.0 42.8 49 PRO 45.6 36.7 79.6 50 MET 32.1 20.1 85.3 51 GLY 29.7 85.2 64.7 52 THR 36.1 33.8 77.6 53 VAL 118.5 99.7 39.5 54 PRO 121.3 97.4 42.9 55 ALA 72.6 100.0 51.0 56 LEU 147.8 100.0 27.5 57 VAL 106.3 89.5 48.1 58 ASP 94.3 85.3 58.4 59 GLY 0.0 0.0 85.7 60 ASP 0.0 0.0 85.8 61 VAL 50.8 42.8 68.8 62 VAL 96.4 81.1 58.5 63 ILE 111.9 78.0 47.9 64 ASN 106.0 87.7 58.1 65 ASP 47.7 43.2 61.6 66 SER 82.8 99.0 39.9 67 PHE 120.7 72.4 40.1 68 ALA 33.9 46.7 65.9 69 ILE 143.5 100.0 35.3 70 ILE 143.5 100.0 28.8 71 MET 133.7 83.9 44.0 72 TYR 128.0 70.7 49.3 73 LEU 147.8 100.0 28.9 74 ASP 95.2 86.2 52.1 75 GLU 22.6 16.3 80.8 76 LYS 89.3 51.5 71.5 77 TYR 123.3 68.1 47.5 78 PRO 45.1 36.2 81.1 79 GLU 7.3 5.3 80.0 80 PRO 58.3 46.8 61.5 81 PRO 48.1 38.6 77.2 82 LEU 146.2 98.9 37.7 83 LEU 139.6 94.5 49.0 84 PRO 115.6 92.8 50.3 85 ARG 0.0 0.0 91.7 86 ASP 48.2 43.6 67.6 87 LEU 11.0 7.5 86.2 88 HIS 21.2 14.1 79.6 89 LYS 74.3 42.8 67.0 90 ARG 134.8 64.5 59.3 91 ALA 34.2 47.1 67.3 92 VAL 108.2 91.1 45.0 93 ASN 120.9 100.0 40.0 94 TYR 100.9 55.7 57.1 95 GLN 66.1 44.5 59.9 96 ALA 72.4 99.7 38.7 97 MET 142.9 89.7 29.3 98 SER 37.8 45.2 69.9 99 ILE 103.8 72.3 49.1 100 VAL 118.7 99.9 49.7 101 LEU 99.8 67.5 61.5 102 SER 29.0 34.7 75.4 103 GLY 8.2 23.6 71.7 104 ILE 133.6 93.1 47.0 105 GLN 123.6 83.2 71.5 106 PRO 41.6 33.5 76.6 107 THR 0.0 0.0 94.7 108 ALA 6.1 8.5 85.0 109 TRP 26.6 13.0 81.5 110 VAL 25.6 21.5 85.2 111 ASN 100.3 83.0 45.8 112 ASN 35.5 29.3 75.6 113 ALA 16.0 22.0 78.3 114 ILE 132.4 92.3 38.3 115 THR 51.8 48.5 79.1 116 LYS 13.0 7.5 85.0 117 GLY 28.7 82.5 48.7 118 PHE 166.8 100.0 27.1 119 THR 46.3 43.4 72.1 120 ALA 37.4 51.5 64.6 121 LEU 147.8 100.0 27.7 122 GLU 116.6 84.1 52.8 123 LYS 36.6 21.1 76.3 124 LEU 117.7 79.6 54.0 125 LEU 147.8 100.0 31.6 126 VAL 59.5 50.1 79.5 127 ASN 11.3 9.3 81.4 128 CYS 78.6 79.3 62.4 129 ALA 0.0 0.0 90.2 130 GLY 25.6 73.5 77.1 131 LYS 40.2 23.2 77.8 132 HIS 136.7 91.0 51.2 133 ALA 72.5 99.8 42.7 134 THR 106.6 99.7 42.0 135 GLY 22.5 64.6 73.3 136 ASP 38.5 34.9 66.9 137 GLU 31.9 23.0 78.3 138 ILE 129.1 90.0 35.6 139 TYR 154.3 85.3 57.5 140 LEU 147.8 100.0 24.6 141 ALA 72.6 100.0 44.9 142 ASP 110.4 99.9 42.6 143 LEU 147.8 100.0 29.2 144 PHE 166.6 99.9 39.6 145 LEU 147.6 99.9 28.1 146 ALA 67.4 92.8 37.2 147 PRO 124.5 100.0 49.6 148 GLN 129.3 87.0 45.5 149 ILE 143.5 100.0 28.2 150 HIS 127.9 85.1 54.8 151 GLY 29.6 85.1 79.3 152 ALA 72.6 100.0 37.9 153 ILE 89.5 62.4 62.0 154 ASN 61.2 50.6 67.1 155 ARG 121.1 58.0 70.6 156 PHE 101.0 60.5 61.6 157 GLN 6.0 4.0 91.1 158 ILE 121.6 84.8 45.8 159 ASN 34.3 28.3 77.6 160 MET 141.4 88.7 36.1 161 GLU 20.5 14.8 82.6 162 PRO 57.5 46.2 64.9 163 TYR 164.2 90.7 44.8 164 PRO 43.5 34.9 81.2 165 THR 94.8 88.7 53.4 166 LEU 147.8 100.0 31.2 167 ALA 41.8 57.6 62.4 168 LYS 106.3 61.3 71.0 169 CYS 99.2 100.0 47.5 170 TYR 128.4 70.9 49.4 171 GLU 22.7 16.4 83.0 172 SER 65.8 78.8 64.3 173 TYR 173.8 96.0 39.4 174 ASN 20.3 16.8 87.4 175 GLU 26.9 19.4 83.2 176 LEU 109.9 74.4 51.9 177 PRO 30.1 24.2 81.2 178 ALA 62.3 85.8 49.3 179 PHE 160.9 96.5 32.1 180 GLN 71.3 48.0 71.5 181 ASN 32.8 27.2 70.8 182 ALA 69.9 96.2 62.9 183 LEU 106.7 72.2 61.5 184 PRO 115.8 93.0 53.3 185 GLU 65.8 47.5 59.5 186 LYS 67.8 39.1 79.1 187 GLN 139.8 94.1 56.4 188 PRO 54.2 43.5 67.4 189 ASP 84.7 76.6 50.4 190 ALA 70.7 97.4 57.4 191 PRO 51.6 41.5 66.3 192 SER 25.4 30.4 85.0 193 SER 0.0 0.0 88.8 194 THR 0.0 0.0 76.8