Protein Data Bank File : 1am2 Title : INTEIN 20-JUN-97 1AM2 Number of Amino Acid Residues : 181 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA SER ILE THR GLY ASP ALA LEU VAL ALA 10 LEU PRO GLU GLY GLU SER VAL ARG ILE ALA 20 ASP ILE VAL PRO GLY ALA ARG PRO ASN SER 30 ASP ASN ALA ILE ASP LEU LYS VAL LEU ASP 40 ARG HIS GLY ASN PRO VAL LEU ALA ASP ARG 50 LEU PHE HIS SER GLY GLU HIS PRO VAL TYR 60 ALA VAL ARG THR VAL GLU GLY LEU ARG VAL 70 THR GLY THR ALA ASN HIS PRO LEU LEU CYS 80 LEU VAL ASP VAL ALA GLY VAL PRO THR LEU 90 LEU TRP LYS LEU ILE ASP GLU ILE LYS PRO 100 GLY ASP TYR ALA VAL ILE GLN ARG SER ALA 110 PHE SER THR VAL GLY VAL PRO GLY LEU VAL 120 ARG PHE LEU GLU ALA HIS HIS ARG ASP PRO 130 ASP ALA LYS ALA ILE ALA ASP GLU LEU THR 140 ASP GLY ARG PHE TYR TYR ALA LYS VAL ALA 150 SER VAL THR ASP ALA GLY VAL GLN PRO VAL 160 TYR SER LEU ARG VAL ASP THR ALA ASP HIS 170 ALA PHE ILE THR ASN GLY PHE VAL SER HIS 180 ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 137.1 0.7 2 SER -136.8 164.8 179.9 -63.1 3 ILE -128.0 161.2 -178.6 59.3 178.4 4 THR -63.1 143.2 -175.9 -104.4 5 GLY -57.3 -14.9 179.6 6 ASP -88.4 -12.6 -179.6 41.2 85.5 7 ALA -55.9 133.7 178.6 8 LEU -90.4 124.5 179.4 -69.3 171.0 9 VAL -90.4 121.1 179.2 170.1 10 ALA -69.0 128.4 -179.9 11 LEU -118.4 168.2 179.3 -55.1 173.4 12 PRO -66.9 158.9 179.0 -33.0 45.3 13 GLU 70.5 29.7 178.1 -108.1 87.5 -79.3 14 GLY 74.6 -0.4 179.9 15 GLU -79.1 158.4 177.9 -149.3 70.3 -77.9 16 SER -159.9 156.8 -177.3 67.5 17 VAL -142.6 139.5 177.8 61.5 18 ARG -64.3 137.7 -179.8 -62.0 -172.6 -40.3 123.4 19 ILE -56.9 -27.4 -179.9 -172.9 153.6 20 ALA -72.8 -13.4 -179.2 21 ASP -100.8 -0.4 179.4 -57.7 -14.2 22 ILE -68.3 -41.4 175.1 -69.8 175.5 23 VAL -125.3 86.6 -179.4 172.7 24 PRO -52.6 135.1 179.9 -28.2 46.0 25 GLY 68.6 15.9 177.1 26 ALA -50.4 137.5 178.0 27 ARG -72.3 149.2 179.1 -67.2 179.1 171.7 114.2 28 PRO -68.6 136.4 -177.0 -27.5 43.8 29 ASN 61.0 52.1 -179.6 -39.4 -55.7 30 SER -126.6 146.4 177.2 62.1 31 ASP -108.0 117.5 -175.7 172.1 -20.7 32 ASN -122.2 126.2 177.5 -50.3 -88.0 33 ALA -75.4 137.2 179.2 34 ILE -139.6 169.9 176.4 62.3 171.4 35 ASP -142.1 86.2 -175.6 -167.7 81.8 36 LEU -124.1 140.3 177.1 -138.0 -155.1 37 LYS -94.3 132.3 -174.8 -141.8 63.3 53.0 -160.9 38 VAL -139.6 156.1 178.3 112.9 39 LEU -78.4 145.4 179.2 -65.5 -167.1 40 ASP -98.4 -167.7 -178.1 77.9 -12.4 41 ARG -52.4 -34.6 179.2 168.5 -157.4 -74.3 -128.5 42 HIS -98.2 7.8 -177.9 -60.6 -64.7 43 GLY 83.9 14.3 179.5 44 ASN -97.2 140.0 -179.4 -68.8 -35.6 45 PRO -64.5 128.7 -174.4 30.7 -43.4 46 VAL -137.3 161.5 -178.1 86.5 47 LEU -95.2 128.1 177.4 -178.4 70.1 48 ALA -106.9 124.5 -178.8 49 ASP -111.8 -3.4 177.0 68.4 -27.8 50 ARG -142.9 139.8 174.9 -86.9 -169.9 -153.8 176.0 51 LEU -115.1 116.5 178.3 179.7 -78.7 52 PHE -107.9 130.1 176.8 -54.0 -74.7 53 HIS -106.8 104.3 -175.9 174.5 -50.2 54 SER -89.0 21.5 -179.7 -30.2 55 GLY 82.7 -166.0 -179.0 56 GLU -103.7 136.3 -178.2 -68.3 -176.2 -63.1 57 HIS -147.0 161.0 179.1 -62.6 -73.2 58 PRO -61.0 143.9 -174.7 -25.1 39.8 59 VAL -139.1 153.6 -179.6 106.0 60 TYR -132.3 139.1 -178.2 -45.0 78.6 61 ALA -95.3 119.6 177.8 62 VAL -98.9 122.5 -179.6 176.4 63 ARG -116.9 141.7 -176.7 -54.6 124.9 171.5 -45.4 64 THR -103.4 153.2 -178.7 -114.7 65 VAL -55.4 -25.4 -179.5 132.2 66 GLU -86.3 -10.3 -178.6 -62.4 85.1 -5.9 67 GLY 103.3 -3.9 179.2 68 LEU -64.8 152.1 -179.8 -56.0 171.6 69 ARG -152.6 147.0 173.1 167.7 -146.6 -18.5 -122.5 70 VAL -144.7 142.6 -178.2 68.0 71 THR -119.6 124.1 -178.5 -45.6 72 GLY -154.3 -177.8 -177.7 73 THR -76.7 164.2 -179.1 56.3 74 ALA -51.9 -41.8 179.4 75 ASN -92.4 18.9 178.9 60.9 154.6 76 HIS -84.1 127.6 179.5 -179.3 58.6 77 PRO -85.9 131.4 179.6 -13.4 33.4 78 LEU -123.2 141.6 -178.9 -72.3 -176.6 79 LEU -79.6 127.9 -177.4 -164.8 68.8 80 CYS -124.5 158.8 177.5 -70.6 81 LEU -96.4 108.2 -177.0 175.6 68.9 82 VAL -111.4 142.0 178.1 174.3 83 ASP -86.7 107.8 177.7 -169.2 -52.1 84 VAL -107.2 95.8 179.2 172.0 85 ALA 55.2 40.5 179.1 86 GLY 94.6 -12.0 177.4 87 VAL -106.0 122.7 179.8 12.5 88 PRO -68.3 116.0 -177.8 -17.7 37.6 89 THR -119.3 137.5 176.9 -55.0 90 LEU -83.2 115.2 -177.2 -61.6 178.9 91 LEU -139.1 146.5 177.6 -58.9 172.3 92 TRP -74.5 131.4 175.8 -62.4 113.5 93 LYS -125.1 142.4 178.6 -76.3 -169.3 66.4 161.1 94 LEU -80.1 153.1 179.6 -51.8 179.9 95 ILE -53.7 -35.8 177.4 -76.7 -171.2 96 ASP -48.2 -41.1 -175.0 -144.7 -0.7 97 GLU -98.1 -1.9 -179.2 -60.2 -57.1 -33.1 98 ILE -78.2 135.5 179.8 -67.5 165.8 99 LYS -128.4 160.6 179.3 -46.0 152.8 -66.2 -76.3 100 PRO -57.0 142.9 -179.0 -29.8 43.5 101 GLY 99.2 -24.7 176.8 102 ASP -65.2 162.5 179.7 -85.2 0.5 103 TYR -119.1 114.8 176.8 -83.7 -76.5 104 ALA -88.4 142.4 179.7 105 VAL -84.5 127.2 179.4 179.9 106 ILE -109.6 135.6 178.9 -57.2 -64.1 107 GLN -99.2 108.8 -177.8 167.4 47.0 58.7 108 ARG -61.2 -23.1 -179.7 -67.9 -160.2 -108.0 -124.9 109 SER -68.1 -15.2 177.8 -58.7 110 ALA -70.0 -3.3 -179.7 111 PHE -123.8 142.7 179.6 -55.9 -70.0 112 SER -139.3 52.0 127.0 -168.3 113 THR -127.3 -69.9 -177.7 -32.3 114 VAL -82.3 112.3 177.7 -162.6 115 GLY 72.2 161.1 178.1 116 VAL -71.3 113.0 179.5 -174.5 117 PRO -59.1 125.6 178.3 -34.5 46.1 118 GLY 78.7 8.6 -177.1 119 LEU -76.3 -39.4 -179.6 -176.2 64.0 120 VAL -59.7 -55.2 179.0 154.9 121 ARG -59.3 -36.0 -180.0 -55.8 -172.4 -57.1 -121.9 122 PHE -64.5 -43.7 -178.9 163.8 64.7 123 LEU -67.6 -50.7 180.0 -78.5 165.8 124 GLU -67.9 -34.5 178.1 64.8 -174.1 13.7 125 ALA -72.3 -51.2 179.8 126 HIS -93.5 -80.6 -178.3 -64.9 72.4 127 HIS 51.5 -62.0 178.1 70.6 78.2 128 ARG -88.8 56.1 176.0 -127.3 -53.1 60.5 81.6 129 ASP -113.1 120.4 -179.4 -159.4 49.2 130 PRO -42.5 -31.8 -179.9 -34.1 44.2 131 ASP -99.7 4.6 -180.0 -104.6 25.6 132 ALA -62.6 -30.3 179.6 133 LYS -77.9 -36.4 177.7 -154.8 -92.7 -86.0 60.2 134 ALA -67.2 -37.7 178.6 135 ILE -64.5 -54.3 -179.9 -80.8 177.0 136 ALA -53.1 -38.1 -179.7 137 ASP -59.2 -57.7 -179.1 -151.7 69.7 138 GLU -56.7 -45.9 -178.4 164.3 68.3 -27.2 139 LEU -67.5 -30.8 -176.1 -60.3 -177.3 140 THR -83.3 -11.5 177.8 -101.4 141 ASP -43.5 127.6 -177.9 177.8 -19.0 142 GLY -63.2 -21.0 177.8 143 ARG -77.9 -6.2 -178.4 -58.6 -171.7 173.7 169.7 144 PHE -97.2 148.9 176.4 -81.8 -31.4 145 TYR -140.7 142.2 179.4 174.5 69.7 146 TYR -111.0 107.2 -177.6 -55.6 -83.9 147 ALA -94.4 132.3 -178.4 148 LYS -84.0 126.1 179.6 -165.5 174.8 -173.2 70.5 149 VAL -68.7 130.7 -180.0 -178.8 150 ALA -98.8 -38.6 -178.4 151 SER -164.2 150.5 174.4 55.4 152 VAL -122.9 108.7 -178.0 178.5 153 THR -118.8 147.9 178.9 44.3 154 ASP -61.5 134.7 -177.9 175.8 71.0 155 ALA -117.4 13.1 178.1 156 GLY 91.0 -166.2 179.0 157 VAL -108.3 128.9 -177.3 178.7 158 GLN -148.0 158.3 178.3 -64.7 -165.7 46.3 159 PRO -64.5 140.5 -172.9 17.4 -36.0 160 VAL -134.4 136.8 -177.8 107.9 161 TYR -119.2 160.2 173.1 -52.4 73.4 162 SER -153.6 158.7 177.7 -154.2 163 LEU -108.1 162.3 172.4 -72.9 -169.7 164 ARG -119.0 120.6 178.5 -169.0 -133.1 -103.0 164.6 165 VAL -109.5 134.1 179.8 -15.6 166 ASP -76.3 82.6 -174.5 -102.5 44.2 167 THR -165.2 145.5 -179.1 -101.1 168 ALA -66.4 -29.5 -179.4 169 ASP -76.3 -36.3 -179.4 -171.1 23.1 170 HIS 60.8 40.7 -177.9 -68.8 -59.3 171 ALA -117.9 150.7 177.8 172 PHE -145.9 165.3 -174.7 61.1 -67.2 173 ILE -102.4 125.5 -178.0 -54.5 -49.2 174 THR -131.1 108.0 -177.2 52.1 175 ASN 60.5 35.9 -179.5 -75.8 -6.1 176 GLY 87.6 -25.7 -178.8 177 PHE -78.3 148.2 178.9 -71.4 81.5 178 VAL -93.6 106.4 -179.3 178.0 179 SER -97.6 149.6 174.9 -75.8 180 HIS -96.9 147.2 177.6 -175.6 -77.9 181 ASN -42.0 -41.8 0.0 -78.5 -2.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA -5.371 27.460 22.402 2 SER -3.910 30.030 21.999 3 ILE -3.510 33.346 23.648 4 THR -1.184 36.229 23.792 5 GLY 1.813 36.320 26.151 6 ASP 0.343 39.130 28.245 7 ALA -2.718 37.204 29.422 8 LEU -2.701 36.811 33.160 9 VAL -3.214 33.203 34.248 10 ALA -5.131 33.066 37.535 11 LEU -3.330 31.101 40.258 12 PRO -4.467 30.286 43.800 13 GLU -4.320 32.802 46.681 14 GLY -5.199 35.801 44.526 15 GLU -1.888 35.345 42.697 16 SER -1.499 35.415 38.874 17 VAL 1.232 35.168 36.229 18 ARG 1.498 36.288 32.591 19 ILE 1.476 33.191 30.411 20 ALA 4.836 34.226 28.770 21 ASP 6.479 34.004 32.208 22 ILE 5.497 30.482 33.208 23 VAL 8.574 29.189 31.254 24 PRO 10.579 32.402 30.978 25 GLY 12.283 32.540 27.641 26 ALA 10.394 29.503 26.225 27 ARG 11.373 28.755 22.640 28 PRO 8.829 29.434 19.914 29 ASN 7.143 26.162 18.847 30 SER 8.252 24.374 21.981 31 ASP 6.451 21.838 24.112 32 ASN 7.505 22.457 27.770 33 ALA 6.698 20.357 30.820 34 ILE 5.572 22.346 33.888 35 ASP 3.956 21.605 37.273 36 LEU 1.749 24.601 38.030 37 LYS -1.368 24.911 40.102 38 VAL -3.862 27.088 38.266 39 LEU -7.489 28.060 38.785 40 ASP -10.121 26.156 36.853 41 ARG -13.554 27.149 35.551 42 HIS -14.893 27.593 39.135 43 GLY -11.864 29.287 40.695 44 ASN -10.674 25.963 42.133 45 PRO -6.879 24.911 41.925 46 VAL -6.169 22.478 39.186 47 LEU -2.929 21.133 37.658 48 ALA -1.481 22.489 34.404 49 ASP 1.213 20.166 33.028 50 ARG 2.346 21.646 29.649 51 LEU 3.172 25.212 28.439 52 PHE 3.048 25.403 24.601 53 HIS 4.574 28.369 22.758 54 SER 2.906 27.926 19.361 55 GLY 4.861 30.462 17.325 56 GLU 3.287 33.638 15.938 57 HIS -0.233 33.727 14.598 58 PRO -2.941 36.282 13.797 59 VAL -4.624 37.303 17.008 60 TYR -7.907 39.216 17.909 61 ALA -8.753 41.300 20.948 62 VAL -12.018 40.552 22.702 63 ARG -13.135 43.529 24.778 64 THR -15.886 43.644 27.315 65 VAL -18.319 46.460 28.067 66 GLU -16.586 46.705 31.489 67 GLY -13.198 47.033 29.802 68 LEU -11.958 43.412 30.267 69 ARG -9.991 42.165 27.291 70 VAL -8.261 38.983 26.163 71 THR -6.339 38.493 22.947 72 GLY -6.041 35.116 21.282 73 THR -6.262 33.294 18.032 74 ALA -9.378 32.842 15.856 75 ASN -9.995 29.273 16.961 76 HIS -9.355 29.934 20.676 77 PRO -12.434 28.932 22.763 78 LEU -13.816 31.218 25.534 79 LEU -16.809 30.097 27.664 80 CYS -19.875 32.146 26.815 81 LEU -23.446 32.263 28.111 82 VAL -25.516 31.231 25.089 83 ASP -29.314 31.122 24.690 84 VAL -30.068 27.586 23.416 85 ALA -33.848 27.424 22.717 86 GLY -34.656 29.387 25.810 87 VAL -32.174 27.792 28.128 88 PRO -29.108 29.866 29.141 89 THR -26.317 27.403 28.480 90 LEU -22.565 27.751 29.243 91 LEU -20.830 26.846 25.921 92 TRP -17.429 27.220 24.316 93 LYS -17.447 29.713 21.400 94 LEU -14.321 30.367 19.322 95 ILE -12.935 33.902 19.226 96 ASP -13.760 33.668 15.524 97 GLU -17.480 33.566 16.417 98 ILE -17.794 36.036 19.229 99 LYS -19.741 39.169 18.478 100 PRO -20.558 42.277 20.478 101 GLY -23.527 41.504 22.699 102 ASP -22.392 37.926 23.418 103 TYR -21.815 37.201 27.088 104 ALA -18.425 35.877 28.026 105 VAL -18.173 34.044 31.439 106 ILE -15.869 35.782 33.911 107 GLN -14.409 33.933 36.934 108 ARG -14.366 36.521 39.753 109 SER -11.650 34.772 41.719 110 ALA -9.227 35.995 39.085 111 PHE -9.424 39.374 40.848 112 SER -8.280 40.211 44.444 113 THR -23.443 43.312 35.517 114 VAL -26.793 42.572 37.177 115 GLY -27.894 38.932 37.024 116 VAL -27.604 35.805 34.894 117 PRO -28.854 37.070 31.593 118 GLY -32.137 35.240 30.694 119 LEU -32.432 33.050 33.830 120 VAL -35.635 34.630 35.142 121 ARG -37.664 34.107 31.975 122 PHE -36.139 30.640 31.828 123 LEU -37.243 29.905 35.375 124 GLU -40.754 31.236 35.069 125 ALA -41.176 29.685 31.613 126 HIS -39.526 26.342 32.531 127 HIS -38.668 25.952 36.274 128 ARG -40.391 22.614 36.598 129 ASP -37.985 21.128 34.131 130 PRO -36.322 18.510 36.406 131 ASP -32.887 19.969 35.665 132 ALA -34.054 23.555 35.881 133 LYS -32.851 23.636 39.480 134 ALA -29.435 22.069 38.641 135 ILE -29.103 24.577 35.803 136 ALA -29.973 27.525 38.019 137 ASP -27.347 26.388 40.512 138 GLU -24.411 26.427 38.066 139 LEU -25.359 29.766 36.442 140 THR -25.998 31.213 39.797 141 ASP -22.552 30.327 41.329 142 GLY -21.352 33.529 43.091 143 ARG -17.938 33.276 41.506 144 PHE -19.348 33.889 37.939 145 TYR -19.901 37.212 36.248 146 TYR -21.381 37.678 32.737 147 ALA -19.570 40.418 30.786 148 LYS -21.132 41.798 27.629 149 VAL -18.823 41.759 24.629 150 ALA -18.285 45.224 23.165 151 SER -15.884 44.375 20.353 152 VAL -13.643 41.711 18.811 153 THR -10.835 43.572 16.948 154 ASP -7.800 42.418 14.947 155 ALA -4.733 42.589 17.094 156 GLY -2.041 41.655 14.634 157 VAL 0.323 38.730 14.490 158 GLN 1.850 37.733 17.765 159 PRO 3.672 34.942 19.619 160 VAL 0.900 32.878 21.112 161 TYR 0.731 30.482 24.146 162 SER -1.466 27.845 25.741 163 LEU -1.541 25.598 28.764 164 ARG -2.472 22.026 29.115 165 VAL -4.668 21.489 32.127 166 ASP -5.278 18.088 33.632 167 THR -9.041 18.233 33.645 168 ALA -11.905 16.796 31.641 169 ASP -13.081 20.358 31.209 170 HIS -9.628 21.651 30.078 171 ALA -10.272 25.205 31.192 172 PHE -8.151 27.874 32.791 173 ILE -8.598 31.530 33.621 174 THR -6.885 34.094 31.417 175 ASN -7.587 37.715 32.297 176 GLY -10.739 36.733 34.189 177 PHE -12.033 34.891 31.070 178 VAL -12.567 31.125 31.117 179 SER -10.300 29.722 28.371 180 HIS -10.143 26.287 26.897 181 ASN -6.704 24.480 26.455 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S/P S S S S S S S S S 10 S/T T T T/S S S S S/T T T 20 T S S S S/S S S S S S 30 S S S S S/S S S S S T 40 T T T/S S S S S/S S S S/S 50 S S S S S/S S S S/S S S 60 S S S S/T T T T/S S S S 70 S S S C S S S S S/S S 80 S S S/T T T T/S S S S S/S 90 S S S S/T T T T/S S S S 100 S S S S S S S C C C 110 C C/X X/C C C C C H H H 120 H H H H H H C C C C 130 H H H H H H H H H H 140 H C S S S S S S S S 150 S S S S/S S S S S S S 160 S S/S S S S S T T T T/S 170 S S S/T T T T/S S S S S 180 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E e T e E E E 10 e t T T e E E E e G 20 G g t T T t t T T E 30 E E E E E E E E E e 40 T T t e E E E E E E 50 E E E E E E E E E E 60 E E E E e T t e E E 70 E E t T T e E E E E 80 E E E E T T E E E E 90 E E E E e G G g t T 100 T e E E E E E e G G 110 g S t T h H H 120 H H H H H h t S t T 130 h H H H H H H H H H 140 h T e E E E E E E E 150 E E E E E E E E E E 160 E E E E E e S S S e 170 E E E E T T E E E E 180 e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 36.9 50.8 76.8 2 SER 77.4 92.5 47.2 3 ILE 143.1 99.8 35.5 4 THR 105.0 98.2 60.8 5 GLY 27.2 78.2 53.3 6 ASP 43.6 39.5 75.4 7 ALA 72.2 99.5 52.0 8 LEU 68.1 46.1 74.9 9 VAL 118.8 100.0 37.2 10 ALA 69.5 95.7 42.0 11 LEU 124.6 84.3 42.8 12 PRO 91.6 73.6 51.9 13 GLU 0.0 0.0 86.5 14 GLY 25.0 71.8 77.4 15 GLU 30.6 22.1 79.5 16 SER 58.5 70.0 55.6 17 VAL 82.6 69.5 51.7 18 ARG 108.1 51.7 69.8 19 ILE 143.5 100.0 39.5 20 ALA 56.9 78.4 64.6 21 ASP 63.8 57.7 69.6 22 ILE 134.8 93.9 31.8 23 VAL 83.3 70.1 52.1 24 PRO 35.7 28.7 82.8 25 GLY 0.0 0.0 87.8 26 ALA 67.5 93.0 59.3 27 ARG 16.8 8.1 82.0 28 PRO 51.0 40.9 71.2 29 ASN 29.7 24.6 77.2 30 SER 66.3 79.3 69.4 31 ASP 57.7 52.2 66.9 32 ASN 93.0 77.0 60.0 33 ALA 9.4 12.9 79.8 34 ILE 124.6 86.9 46.9 35 ASP 23.6 21.3 75.8 36 LEU 110.2 74.6 43.9 37 LYS 78.9 45.5 63.1 38 VAL 118.8 100.0 34.5 39 LEU 139.9 94.7 46.1 40 ASP 85.3 77.2 55.9 41 ARG 169.8 81.3 49.9 42 HIS 96.3 64.1 76.6 43 GLY 34.8 100.0 57.9 44 ASN 53.4 44.2 70.0 45 PRO 62.2 50.0 59.4 46 VAL 94.8 79.8 66.1 47 LEU 100.4 68.0 68.4 48 ALA 72.6 100.0 41.4 49 ASP 78.7 71.2 67.5 50 ARG 109.1 52.2 73.4 51 LEU 147.2 99.6 38.6 52 PHE 109.2 65.5 67.0 53 HIS 142.1 94.6 52.3 54 SER 48.4 57.9 72.6 55 GLY 26.6 76.5 65.2 56 GLU 50.1 36.2 65.5 57 HIS 75.3 50.1 59.7 58 PRO 56.5 45.4 69.0 59 VAL 118.8 100.0 49.9 60 TYR 119.9 66.2 54.4 61 ALA 69.1 95.2 59.3 62 VAL 118.8 100.0 30.7 63 ARG 135.5 64.9 69.6 64 THR 106.9 100.0 41.3 65 VAL 48.1 40.5 66.6 66 GLU 96.0 69.2 61.5 67 GLY 1.9 5.5 81.2 68 LEU 106.8 72.3 46.7 69 ARG 94.1 45.1 78.8 70 VAL 118.3 99.6 38.5 71 THR 97.3 91.1 46.1 72 GLY 34.8 100.0 43.4 73 THR 97.5 91.2 54.5 74 ALA 43.3 59.6 65.0 75 ASN 36.3 30.1 72.3 76 HIS 150.0 99.8 50.6 77 PRO 105.4 84.6 55.6 78 LEU 147.2 99.6 35.4 79 LEU 147.0 99.5 42.1 80 CYS 98.9 99.7 42.9 81 LEU 143.3 96.9 36.6 82 VAL 79.1 66.6 58.2 83 ASP 43.8 39.7 75.6 84 VAL 50.3 42.3 67.2 85 ALA 0.0 0.0 82.1 86 GLY 10.2 29.4 74.1 87 VAL 79.7 67.1 61.0 88 PRO 119.6 96.1 42.1 89 THR 69.4 64.9 54.9 90 LEU 140.4 95.0 41.9 91 LEU 77.9 52.7 56.8 92 TRP 150.1 73.2 59.0 93 LYS 137.2 79.1 57.6 94 LEU 81.5 55.1 62.1 95 ILE 143.0 99.6 40.7 96 ASP 42.5 38.5 65.0 97 GLU 39.5 28.5 76.6 98 ILE 143.5 100.0 35.4 99 LYS 62.8 36.2 78.1 100 PRO 56.8 45.6 67.7 101 GLY 20.5 59.0 69.8 102 ASP 88.5 80.1 54.3 103 TYR 130.2 71.9 58.6 104 ALA 72.3 99.6 42.5 105 VAL 118.8 100.0 35.8 106 ILE 140.4 97.9 36.7 107 GLN 148.6 100.0 43.6 108 ARG 100.6 48.2 69.2 109 SER 52.5 62.8 64.5 110 ALA 68.3 94.0 47.7 111 PHE 77.4 46.4 68.8 112 SER 28.5 34.1 69.0 113 THR 21.0 19.6 77.4 114 VAL 0.0 0.0 84.7 115 GLY 0.0 0.0 80.1 116 VAL 105.2 88.5 40.3 117 PRO 92.6 74.3 53.4 118 GLY 25.3 72.6 74.5 119 LEU 130.8 88.5 41.4 120 VAL 12.2 10.2 75.9 121 ARG 44.4 21.2 81.1 122 PHE 164.0 98.3 38.7 123 LEU 90.5 61.3 54.7 124 GLU 35.4 25.5 69.7 125 ALA 22.9 31.5 77.1 126 HIS 92.7 61.7 60.7 127 HIS 59.0 39.3 61.4 128 ARG 76.7 36.7 76.3 129 ASP 51.5 46.6 57.1 130 PRO 23.7 19.1 87.8 131 ASP 21.0 19.0 73.3 132 ALA 72.2 99.5 50.3 133 LYS 26.3 15.2 86.9 134 ALA 22.7 31.3 76.1 135 ILE 99.4 69.3 50.8 136 ALA 56.0 77.1 50.6 137 ASP 17.6 15.9 76.2 138 GLU 84.3 60.8 62.3 139 LEU 143.7 97.2 37.3 140 THR 46.3 43.3 68.0 141 ASP 72.8 65.8 65.2 142 GLY 0.0 0.0 87.2 143 ARG 104.2 49.9 82.6 144 PHE 166.4 99.8 56.3 145 TYR 153.0 84.5 53.4 146 TYR 173.3 95.7 34.0 147 ALA 72.6 100.0 50.9 148 LYS 87.7 50.6 67.3 149 VAL 118.8 100.0 48.4 150 ALA 40.4 55.6 62.4 151 SER 50.3 60.2 48.9 152 VAL 99.9 84.1 49.2 153 THR 46.5 43.5 77.3 154 ASP 38.7 35.0 70.0 155 ALA 52.9 72.9 62.6 156 GLY 7.1 20.3 76.1 157 VAL 46.2 38.9 65.2 158 GLN 92.0 61.9 65.4 159 PRO 72.0 57.8 66.6 160 VAL 118.0 99.3 48.9 161 TYR 161.7 89.3 47.1 162 SER 81.5 97.4 46.8 163 LEU 147.8 100.0 24.8 164 ARG 130.1 62.3 71.0 165 VAL 118.8 100.0 48.7 166 ASP 49.9 45.2 70.6 167 THR 81.6 76.4 56.3 168 ALA 0.0 0.0 85.0 169 ASP 69.9 63.2 61.2 170 HIS 87.0 58.0 71.1 171 ALA 72.4 99.8 51.9 172 PHE 166.7 99.9 39.7 173 ILE 143.4 100.0 44.8 174 THR 106.9 100.0 40.0 175 ASN 85.8 70.9 62.0 176 GLY 34.8 100.0 43.1 177 PHE 166.2 99.6 46.1 178 VAL 118.8 100.0 41.2 179 SER 83.6 100.0 48.9 180 HIS 103.5 68.9 51.5 181 ASN 103.0 85.2 53.4