Protein Data Bank File : 3stda Title : LYASE 16-OCT-98 3STD Number of Amino Acid Residues : 162 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY GLU ILE THR PHE SER ASP TYR LEU GLY 10 LEU MET THR CYS VAL TYR GLU TRP ALA ASP 20 SER TYR ASP SER LYS ASP TRP ASP ARG LEU 30 ARG LYS VAL ILE ALA PRO THR LEU ARG ILE 40 ASP TYR ARG SER PHE LEU ASP LYS LEU TRP 50 GLU ALA MET PRO ALA GLU GLU PHE VAL GLY 60 MET VAL SER SER LYS GLN VAL LEU GLY ASP 70 PRO THR LEU ARG THR GLN HIS PHE ILE GLY 80 GLY THR ARG TRP GLU LYS VAL SER GLU ASP 90 GLU VAL ILE GLY TYR HIS GLN LEU ARG VAL 100 PRO HIS GLN ARG TYR LYS ASP THR THR MET 110 LYS GLU VAL THR MET LYS GLY HIS ALA HIS 120 SER ALA ASN LEU HIS TRP TYR LYS LYS ILE 130 ASP GLY VAL TRP LYS PHE ALA GLY LEU LYS 140 PRO ASP ILE ARG TRP GLY GLU PHE ASP PHE 150 ASP ARG ILE PHE GLU ASP GLY ARG GLU THR 160 PHE GLY Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 53.4 178.7 2 GLU -126.9 154.1 176.9 -66.2 176.8 0.0 3 ILE -73.5 163.9 178.1 62.5 170.9 4 THR -100.8 169.9 179.3 63.7 5 PHE -65.7 -33.9 178.1 -177.7 64.7 6 SER -60.5 -42.7 179.0 -75.0 7 ASP -59.6 -47.5 179.8 -72.9 -21.0 8 TYR -54.2 -45.1 179.3 172.4 84.7 9 LEU -60.9 -43.9 179.4 -70.8 177.9 10 GLY -68.7 -38.1 179.0 11 LEU -66.8 -39.6 178.6 -69.1 159.3 12 MET -69.0 -35.7 178.0 -72.9 -50.4 -54.8 13 THR -62.9 -40.4 178.8 -69.3 14 CYS -58.9 -62.5 -177.9 -156.9 15 VAL -62.8 -34.5 178.5 71.1 16 TYR -65.9 -49.8 179.4 176.6 -82.7 17 GLU -63.0 -36.1 177.9 -71.9 -63.4 -67.3 18 TRP -61.0 -53.0 -179.3 164.0 81.6 19 ALA -64.6 -48.9 -178.0 20 ASP -70.3 -25.7 178.2 -153.1 52.3 21 SER -72.0 -37.8 177.1 64.3 22 TYR -61.1 -50.8 -177.9 -89.3 22.2 23 ASP -65.5 -38.3 178.8 -63.3 -26.8 24 SER -88.9 -0.8 -178.8 64.9 25 LYS 53.8 38.7 -179.6 -55.4 -176.7 -162.8 -64.8 26 ASP -100.9 90.6 -176.9 -166.6 -27.8 27 TRP -68.6 -25.4 176.8 -47.9 117.9 28 ASP -72.0 -35.3 178.1 -82.1 -13.0 29 ARG -64.2 -38.5 178.8 -104.8 178.2 81.9 -165.8 30 LEU -65.1 -43.7 179.7 178.5 58.0 31 ARG -57.5 -33.5 -179.6 -72.3 179.0 174.9 106.2 32 LYS -70.2 -18.0 -179.6 -67.1 163.5 -169.8 165.5 33 VAL -112.3 -9.3 -178.9 -63.0 34 ILE -91.6 152.7 178.7 61.8 -177.8 35 ALA -76.8 164.2 -179.9 36 PRO -58.1 -34.1 177.4 -30.7 44.4 37 THR -135.2 146.5 -177.9 64.3 38 LEU -129.6 147.5 177.4 -58.9 83.2 39 ARG -90.6 103.9 -179.1 179.1 179.3 179.9 85.5 40 ILE -103.6 97.6 -178.7 -55.0 -56.4 41 ASP -97.9 91.7 178.8 -166.5 -13.7 42 TYR -107.5 30.7 -178.3 -73.1 -14.8 43 ARG -60.1 -42.9 -179.7 -73.2 177.3 -66.6 -179.8 44 SER -68.6 -38.6 -179.1 62.4 45 PHE -76.4 -54.5 -179.3 -170.5 60.6 46 LEU -131.0 21.4 177.7 51.3 73.9 47 ASP 58.5 38.3 178.5 -64.8 -67.4 48 LYS -137.1 140.7 177.3 -70.7 -168.9 176.9 -178.1 49 LEU -129.9 119.3 176.4 165.7 68.1 50 TRP -108.3 112.7 -179.0 -69.7 -94.7 51 GLU -73.9 -24.6 -179.4 -65.6 -160.1 -67.9 52 ALA -151.0 62.6 179.3 53 MET -72.4 128.5 179.6 -175.6 -174.8 -81.2 54 PRO -59.0 140.8 -179.0 -32.9 45.1 55 ALA -47.2 -46.6 -179.6 56 GLU -66.0 -32.0 179.3 -76.3 -59.9 -52.2 57 GLU -71.6 -38.3 178.0 -60.2 -61.7 -65.4 58 PHE -64.1 -46.7 178.9 172.9 61.3 59 VAL -61.7 -42.0 178.8 176.3 60 GLY -60.3 -37.7 179.5 61 MET -69.2 -59.2 -179.0 173.3 165.7 63.7 62 VAL -61.4 -29.7 -179.2 -62.2 63 SER -88.8 -4.2 -179.7 72.6 64 SER -63.7 158.1 -179.5 66.3 65 LYS -65.6 -20.2 178.4 46.6 167.7 159.9 51.7 66 GLN -83.7 -7.8 179.6 -70.5 84.8 40.3 67 VAL -121.2 -119.3 -178.8 -170.5 68 LEU -82.6 -11.2 179.7 -61.6 -178.4 69 GLY -74.3 -7.4 179.0 70 ASP -68.4 117.2 -180.0 -172.0 -14.2 71 PRO -67.5 -14.9 179.5 32.7 -43.6 72 THR -95.4 6.6 179.0 67.6 73 LEU -111.6 130.3 178.6 174.4 66.1 74 ARG -118.8 135.5 -178.8 -78.5 -59.6 173.5 -84.8 75 THR -141.0 172.1 173.8 66.6 76 GLN -151.9 109.6 179.1 -175.2 -174.1 53.4 77 HIS -91.6 76.1 -176.9 -65.1 71.9 78 PHE -74.5 117.4 -178.8 -150.8 59.9 79 ILE -88.0 121.8 179.9 -52.7 160.5 80 GLY -108.0 -135.2 -179.4 81 GLY -55.5 136.8 -179.0 82 THR -137.7 132.2 176.2 -62.9 83 ARG -126.4 149.4 -175.8 76.6 171.0 176.5 81.9 84 TRP -117.5 156.0 177.7 -47.7 90.0 85 GLU -140.8 117.8 178.2 -66.2 -172.9 -6.0 86 LYS -85.0 118.8 180.0 -178.2 -172.6 175.9 -173.9 87 VAL -85.5 -45.6 179.8 178.6 88 SER -153.6 -178.4 -179.2 68.9 89 GLU -57.2 -29.5 -178.9 65.8 -79.2 -31.4 90 ASP -120.0 10.9 -179.2 71.4 -20.4 91 GLU -131.4 130.0 180.0 -70.2 -173.5 -20.9 92 VAL -135.7 140.0 177.2 166.8 93 ILE -107.6 132.7 178.4 -72.9 179.0 94 GLY -117.6 125.6 177.3 95 TYR -98.9 114.3 -178.0 -74.4 -83.2 96 HIS -122.5 131.8 175.2 -46.5 -81.9 97 GLN -75.4 139.6 179.1 -66.2 -175.0 -59.5 98 LEU -135.5 137.4 176.2 -130.5 67.4 99 ARG -128.3 114.2 -177.6 -169.3 -136.0 173.6 -136.4 100 VAL -119.9 94.2 178.9 -169.0 101 PRO -75.1 145.8 178.9 28.8 -42.5 102 HIS -129.0 140.3 179.4 -64.7 78.4 103 GLN -143.8 117.2 179.5 -170.8 156.3 -79.8 104 ARG -101.3 144.3 -179.8 -74.0 -172.0 172.5 -66.3 105 TYR -117.6 156.2 -180.0 -60.4 76.7 106 LYS -61.9 -41.1 179.5 -175.0 -173.4 173.7 -172.5 107 ASP -151.8 175.2 -178.7 52.1 58.3 108 THR -62.5 -4.4 178.6 48.5 109 THR -77.1 -18.1 179.4 -37.1 110 MET 60.6 31.9 -179.2 -52.7 -71.3 103.9 111 LYS -96.5 -21.9 -179.5 -71.2 173.5 178.8 171.9 112 GLU -130.6 119.0 178.9 -176.1 -170.2 -34.6 113 VAL -80.2 128.1 -179.3 171.9 114 THR -107.8 -21.5 180.0 53.0 115 MET -156.9 149.8 178.7 -165.9 -172.3 -63.4 116 LYS -137.3 152.3 -179.8 -64.8 174.3 67.8 170.0 117 GLY -174.9 114.3 -177.4 118 HIS -113.0 119.9 -178.7 -50.5 158.0 119 ALA -91.8 137.4 179.0 120 HIS -115.3 115.3 -175.5 -55.4 89.0 121 SER -136.1 162.0 175.7 173.7 122 ALA -118.3 98.6 -178.6 123 ASN -89.3 132.8 176.2 -93.3 -133.5 124 LEU -107.5 116.7 179.2 -174.2 171.9 125 HIS -113.8 142.1 178.0 -68.3 -172.5 126 TRP -105.4 136.3 179.4 -70.6 -79.0 127 TYR -126.6 141.9 179.5 -59.1 -82.9 128 LYS -129.7 138.8 179.4 -74.1 166.4 -164.6 156.0 129 LYS -90.2 115.5 -179.7 -155.2 179.7 179.8 -175.3 130 ILE -122.3 119.1 180.0 -61.6 168.7 131 ASP 56.3 38.6 179.5 -64.2 -39.1 132 GLY 80.5 4.6 -179.2 133 VAL -121.2 129.7 178.0 -175.5 134 TRP -72.0 133.1 -179.1 -75.9 104.0 135 LYS -123.4 147.7 177.7 -66.5 -69.0 176.8 -177.1 136 PHE -74.5 113.3 -176.3 -174.7 -83.8 137 ALA -109.1 7.3 179.6 138 GLY 149.9 168.9 -179.8 139 LEU -155.7 154.3 179.7 77.6 -170.8 140 LYS -137.3 92.9 179.9 178.6 -179.7 -175.3 -71.5 141 PRO -74.6 149.7 176.5 -21.6 39.3 142 ASP -138.1 85.0 -179.6 -179.9 16.3 143 ILE -77.4 111.0 -179.3 -59.1 169.3 144 ARG -75.0 -41.0 179.6 -81.1 67.0 177.0 -81.9 145 TRP -166.8 166.0 179.7 62.9 -75.5 146 GLY -131.7 146.4 177.5 147 GLU -92.3 146.0 -177.3 -169.1 -179.4 -9.8 148 PHE 65.8 -134.4 -177.4 -61.2 -68.3 149 ASP -116.2 61.3 -179.3 -55.3 -70.0 150 PHE -60.4 -36.2 -180.0 176.5 69.0 151 ASP -58.7 -23.7 179.5 59.0 -28.9 152 ARG -93.7 -20.8 -178.0 -68.0 164.3 52.7 -140.0 153 ILE -50.1 -49.8 -178.8 -67.2 -67.4 154 PHE -107.8 42.1 179.3 -66.9 -62.6 155 GLU -56.9 -49.8 179.2 -68.8 174.7 -86.1 156 ASP -65.3 -47.7 -179.6 -73.9 -6.1 157 GLY -56.5 -45.0 179.1 158 ARG -62.4 -43.3 178.8 -79.3 179.0 52.9 53.3 159 GLU -61.6 -51.6 -177.8 -72.1 162.6 17.6 160 THR -64.0 -50.4 -177.6 -62.5 161 PHE -92.2 -16.1 179.3 -62.1 -75.6 162 GLY -113.0 176.5 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 0.667 24.188 40.415 2 GLU 3.080 25.696 37.885 3 ILE 6.451 27.353 38.317 4 THR 6.638 31.139 37.795 5 PHE 8.858 32.962 35.285 6 SER 11.089 34.079 38.182 7 ASP 11.469 30.381 39.043 8 TYR 12.307 29.636 35.408 9 LEU 15.141 32.213 35.371 10 GLY 16.662 30.701 38.522 11 LEU 16.208 27.142 37.239 12 MET 17.920 27.985 33.929 13 THR 20.839 29.635 35.749 14 CYS 21.120 26.353 37.665 15 VAL 21.132 23.901 34.788 16 TYR 23.319 26.187 32.620 17 GLU 25.950 26.541 35.354 18 TRP 25.770 22.784 36.030 19 ALA 26.458 21.936 32.372 20 ASP 29.021 24.671 31.695 21 SER 30.938 24.035 34.949 22 TYR 31.284 20.394 33.835 23 ASP 32.554 21.504 30.406 24 SER 34.961 24.165 31.652 25 LYS 35.992 21.808 34.504 26 ASP 35.318 24.700 36.925 27 TRP 34.437 22.865 40.132 28 ASP 33.954 25.996 42.223 29 ARG 31.305 27.154 39.716 30 LEU 29.564 23.797 40.188 31 ARG 29.722 24.239 43.998 32 LYS 27.856 27.565 43.736 33 VAL 24.721 25.991 42.203 34 ILE 24.350 22.609 43.952 35 ALA 22.329 21.745 47.054 36 PRO 24.058 20.411 50.247 37 THR 22.969 16.837 49.391 38 LEU 21.959 15.375 46.040 39 ARG 19.867 12.494 44.732 40 ILE 22.314 10.830 42.330 41 ASP 20.427 8.197 40.353 42 TYR 22.951 6.372 38.155 43 ARG 21.005 3.105 38.226 44 SER 20.760 2.764 34.446 45 PHE 24.427 3.672 33.857 46 LEU 26.242 1.908 36.699 47 ASP 23.508 0.358 38.876 48 LYS 23.769 2.744 41.852 49 LEU 21.398 5.192 43.560 50 TRP 22.578 7.664 46.233 51 GLU 19.500 9.312 47.754 52 ALA 21.494 11.981 49.593 53 MET 25.104 12.205 48.434 54 PRO 26.987 15.089 50.154 55 ALA 27.827 17.948 47.767 56 GLU 31.614 17.556 48.146 57 GLU 31.468 13.826 47.472 58 PHE 29.484 14.452 44.281 59 VAL 32.022 17.095 43.195 60 GLY 34.835 14.702 44.102 61 MET 33.296 12.022 41.886 62 VAL 32.588 14.073 38.746 63 SER 35.918 15.924 38.999 64 SER 38.045 12.785 39.447 65 LYS 40.596 11.868 36.769 66 GLN 38.540 8.768 35.888 67 VAL 35.577 11.030 35.077 68 LEU 35.529 14.738 34.032 69 GLY 38.774 15.738 35.769 70 ASP 40.778 14.126 32.944 71 PRO 42.634 16.949 31.081 72 THR 42.693 14.769 27.940 73 LEU 38.875 14.570 27.873 74 ARG 36.672 17.145 26.116 75 THR 32.881 17.274 26.494 76 GLN 29.756 19.382 25.952 77 HIS 26.699 18.833 28.149 78 PHE 24.348 20.450 25.635 79 ILE 20.882 21.300 26.969 80 GLY 17.968 20.978 24.538 81 GLY 14.206 20.833 24.895 82 THR 12.965 21.281 28.447 83 ARG 9.596 20.830 30.179 84 TRP 8.923 21.383 33.889 85 GLU 6.913 19.851 36.722 86 LYS 6.400 21.591 40.053 87 VAL 6.369 18.911 42.776 88 SER 5.993 21.247 45.765 89 GLU 6.612 24.838 46.860 90 ASP 10.349 24.112 47.084 91 GLU 10.758 21.207 44.653 92 VAL 10.838 21.160 40.847 93 ILE 11.576 18.457 38.272 94 GLY 13.136 19.415 34.956 95 TYR 12.994 17.054 31.978 96 HIS 15.921 17.945 29.691 97 GLN 17.000 16.525 26.346 98 LEU 20.765 16.116 26.456 99 ARG 23.399 15.515 23.792 100 VAL 26.857 15.005 25.241 101 PRO 29.748 14.530 22.809 102 HIS 32.994 13.158 24.286 103 GLN 36.453 13.322 22.745 104 ARG 39.586 11.793 24.297 105 TYR 43.144 12.696 23.298 106 LYS 46.437 10.776 23.527 107 ASP 48.038 13.502 25.668 108 THR 47.648 17.059 26.978 109 THR 48.939 18.564 23.714 110 MET 45.448 17.842 22.345 111 LYS 46.879 16.916 18.916 112 GLU 45.635 13.340 18.482 113 VAL 42.088 12.123 19.112 114 THR 42.102 8.548 20.423 115 MET 38.415 7.983 21.183 116 LYS 34.973 9.496 20.544 117 GLY 31.541 8.768 22.022 118 HIS 28.431 10.938 21.944 119 ALA 25.521 10.294 24.338 120 HIS 21.847 10.998 23.592 121 SER 19.822 11.237 26.787 122 ALA 16.566 12.256 28.469 123 ASN 17.785 13.710 31.770 124 LEU 15.515 14.072 34.789 125 HIS 16.897 16.740 37.148 126 TRP 15.634 17.628 40.639 127 TYR 15.812 21.241 41.841 128 LYS 15.223 22.570 45.352 129 LYS 14.580 26.098 46.566 130 ILE 16.894 26.869 49.489 131 ASP 16.839 30.309 51.129 132 GLY 15.012 31.728 48.118 133 VAL 17.481 30.316 45.589 134 TRP 16.875 27.379 43.250 135 LYS 19.601 24.763 43.644 136 PHE 20.621 21.752 41.548 137 ALA 19.505 18.862 43.794 138 GLY 20.100 15.713 41.759 139 LEU 19.839 13.903 38.421 140 LYS 18.742 10.685 36.711 141 PRO 20.298 10.289 33.245 142 ASP 18.683 7.988 30.673 143 ILE 21.113 7.465 27.792 144 ARG 19.135 5.870 24.948 145 TRP 22.090 5.351 22.589 146 GLY 25.520 6.627 21.639 147 GLU 27.308 7.679 18.452 148 PHE 30.854 6.304 18.019 149 ASP 32.105 4.495 21.156 150 PHE 30.360 6.089 24.117 151 ASP 30.354 2.766 26.006 152 ARG 34.183 2.859 26.141 153 ILE 34.560 6.532 27.156 154 PHE 34.110 5.956 30.909 155 GLU 35.535 2.431 31.297 156 ASP 37.715 3.389 34.300 157 GLY 35.088 5.628 35.883 158 ARG 32.401 2.940 35.694 159 GLU 34.771 0.386 37.219 160 THR 35.801 2.749 40.006 161 PHE 32.438 4.262 40.992 162 GLY 30.128 1.436 39.945 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/H H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H 3 3 C S S S S S 40 S S/T T T T S S S S S 50 S/S S S S/H H H H H H H 60 H H H H/T T T T C C C 70 C S S S S S S S S S 80 S/S S S S S S S S/T T T 90 T/S S S S S S S/S S S S 100 S S S S S S T T T T 110 S S S S S/S S S S S S 120 S S/S S S S S S S S/T T 130 T T/S S S S S C C S S 140 S S S S C T T T T/T T 150 T T C H H H H H H H 160 H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H 10 H H H H H H H H H H 20 H H H H h h H H H H 30 H h e E E E E E E E 40 E E H H H H h E E E 50 E E E E H H H H H H 60 H H h t T T T T T t 70 T e E E E e E E E 80 E E E E E E E E T e 90 E E E E E E E E E E 100 E E E E E e t T T t 110 e E E E E E E E E 120 E E E E E E E E E E 130 T T E E E E E E E E 140 e E E E E E E h H 150 H H H h H H H H H H 160 H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.5 1.3 85.2 2 GLU 5.9 4.2 88.1 3 ILE 124.2 86.5 39.7 4 THR 27.6 25.8 82.0 5 PHE 38.0 22.8 68.0 6 SER 9.0 10.8 78.8 7 ASP 90.5 81.9 52.1 8 TYR 99.9 55.2 51.9 9 LEU 51.4 34.8 67.0 10 GLY 11.9 34.1 69.8 11 LEU 147.8 100.0 25.5 12 MET 106.3 66.7 54.3 13 THR 27.0 25.2 71.0 14 CYS 97.5 98.3 46.9 15 VAL 118.8 100.0 35.9 16 TYR 60.2 33.3 75.9 17 GLU 101.7 73.4 58.6 18 TRP 201.4 98.2 30.5 19 ALA 67.3 92.7 51.5 20 ASP 64.5 58.3 73.1 21 SER 83.6 100.0 58.0 22 TYR 170.3 94.1 38.7 23 ASP 91.6 82.9 70.2 24 SER 41.7 49.9 76.5 25 LYS 139.8 80.6 70.0 26 ASP 57.4 51.9 66.3 27 TRP 166.8 81.4 53.6 28 ASP 32.1 29.1 80.3 29 ARG 153.0 73.3 69.1 30 LEU 147.8 100.0 30.9 31 ARG 123.7 59.2 68.5 32 LYS 38.4 22.1 77.5 33 VAL 103.1 86.8 51.2 34 ILE 141.2 98.4 37.3 35 ALA 70.8 97.5 41.7 36 PRO 37.2 29.9 63.6 37 THR 49.5 46.3 65.6 38 LEU 147.4 99.7 43.8 39 ARG 142.8 68.3 58.5 40 ILE 143.5 100.0 29.9 41 ASP 109.1 98.7 46.9 42 TYR 149.5 82.6 38.4 43 ARG 95.8 45.8 73.2 44 SER 28.1 33.6 84.0 45 PHE 113.4 68.0 46.4 46 LEU 138.4 93.7 47.9 47 ASP 9.0 8.1 82.8 48 LYS 89.1 51.4 64.4 49 LEU 120.6 81.6 63.3 50 TRP 136.8 66.7 52.8 51 GLU 40.0 28.8 75.6 52 ALA 26.7 36.8 75.8 53 MET 144.7 90.8 37.3 54 PRO 53.5 43.0 65.7 55 ALA 53.8 74.1 56.6 56 GLU 49.2 35.5 74.7 57 GLU 35.9 25.9 68.4 58 PHE 166.8 100.0 32.1 59 VAL 117.4 98.8 47.1 60 GLY 5.1 14.7 80.6 61 MET 148.8 93.4 32.8 62 VAL 113.4 95.4 37.6 63 SER 66.1 79.1 52.3 64 SER 59.8 71.5 69.5 65 LYS 33.9 19.6 85.7 66 GLN 105.2 70.8 61.2 67 VAL 94.3 79.4 48.9 68 LEU 142.4 96.4 41.0 69 GLY 29.0 83.3 65.8 70 ASP 88.0 79.6 67.1 71 PRO 54.4 43.7 67.7 72 THR 83.0 77.6 61.0 73 LEU 147.8 100.0 48.4 74 ARG 105.3 50.4 66.4 75 THR 104.4 97.6 50.4 76 GLN 66.2 44.6 64.1 77 HIS 134.2 89.3 39.9 78 PHE 55.3 33.1 79.4 79 ILE 124.3 86.6 51.7 80 GLY 9.7 27.7 74.1 81 GLY 2.8 8.1 75.9 82 THR 95.4 89.2 57.0 83 ARG 70.8 33.9 71.4 84 TRP 180.7 88.2 35.2 85 GLU 73.7 53.1 71.7 86 LYS 114.6 66.1 63.8 87 VAL 59.7 50.3 66.5 88 SER 49.1 58.7 71.9 89 GLU 15.9 11.5 79.5 90 ASP 52.9 47.9 69.8 91 GLU 76.1 54.9 61.8 92 VAL 118.2 99.5 33.5 93 ILE 119.4 83.2 50.2 94 GLY 34.8 100.0 43.9 95 TYR 115.0 63.6 63.9 96 HIS 150.2 100.0 42.9 97 GLN 31.2 21.0 79.2 98 LEU 141.8 96.0 46.0 99 ARG 113.0 54.1 64.0 100 VAL 108.8 91.6 47.8 101 PRO 101.1 81.2 65.5 102 HIS 144.8 96.4 34.7 103 GLN 94.2 63.4 56.2 104 ARG 170.7 81.7 56.0 105 TYR 155.6 86.0 56.0 106 LYS 53.6 30.9 81.1 107 ASP 48.5 43.9 70.6 108 THR 33.3 31.2 62.5 109 THR 44.3 41.5 73.8 110 MET 122.5 76.8 61.1 111 LYS 27.3 15.7 80.4 112 GLU 48.8 35.2 70.2 113 VAL 77.6 65.4 58.7 114 THR 61.0 57.1 64.8 115 MET 127.8 80.2 64.9 116 LYS 103.0 59.4 57.0 117 GLY 34.8 100.0 46.7 118 HIS 133.6 88.9 57.7 119 ALA 69.7 95.9 37.8 120 HIS 113.0 75.2 57.5 121 SER 80.7 96.5 58.7 122 ALA 42.3 58.2 79.5 123 ASN 116.9 96.7 43.8 124 LEU 117.2 79.3 48.0 125 HIS 150.2 100.0 37.1 126 TRP 158.1 77.1 50.3 127 TYR 181.0 100.0 37.8 128 LYS 110.8 63.9 62.1 129 LYS 102.0 58.8 65.8 130 ILE 85.8 59.8 58.1 131 ASP 0.0 0.0 81.7 132 GLY 9.2 26.5 68.1 133 VAL 38.9 32.7 80.4 134 TRP 194.3 94.8 47.7 135 LYS 130.3 75.2 58.9 136 PHE 166.8 100.0 33.7 137 ALA 72.6 100.0 47.2 138 GLY 34.8 100.0 41.3 139 LEU 141.8 95.9 39.6 140 LYS 96.0 55.4 64.0 141 PRO 103.0 82.7 57.5 142 ASP 56.6 51.2 80.1 143 ILE 109.0 75.9 47.8 144 ARG 77.5 37.1 76.4 145 TRP 57.0 27.8 74.1 146 GLY 31.3 89.9 55.9 147 GLU 69.2 49.9 64.5 148 PHE 86.8 52.0 71.8 149 ASP 55.7 50.4 72.6 150 PHE 148.9 89.2 40.5 151 ASP 13.0 11.8 75.9 152 ARG 109.3 52.3 73.4 153 ILE 143.5 100.0 43.0 154 PHE 144.1 86.4 46.6 155 GLU 55.4 40.0 74.4 156 ASP 29.2 26.4 74.3 157 GLY 33.3 95.7 48.7 158 ARG 123.2 59.0 62.8 159 GLU 28.8 20.8 82.8 160 THR 48.2 45.1 66.3 161 PHE 119.3 71.5 52.5 162 GLY 34.0 97.6 57.1