Protein Data Bank File : 1ee6a Title : LYASE 31-JAN-00 1EE6 Number of Amino Acid Residues : 197 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA PRO THR VAL VAL HIS GLU THR ILE ARG 10 VAL PRO ALA GLY GLN THR PHE ASP GLY LYS 20 GLY GLN THR TYR VAL ALA ASN PRO ASN THR 30 LEU GLY ASP GLY SER GLN ALA GLU ASN GLN 40 LYS PRO ILE PHE ARG LEU GLU ALA GLY ALA 50 SER LEU LYS ASN VAL VAL ILE GLY ALA PRO 60 ALA ALA ASP GLY VAL HIS CYS TYR GLY ASP 70 CYS THR ILE THR ASN VAL ILE TRP GLU ASP 80 VAL GLY GLU ASP ALA LEU THR LEU LYS SER 90 SER GLY THR VAL ASN ILE SER GLY GLY ALA 100 ALA TYR LYS ALA TYR ASP LYS VAL PHE GLN 110 ILE ASN ALA ALA GLY THR ILE ASN ILE ARG 120 ASN PHE ARG ALA ASP ASP ILE GLY LYS LEU 130 VAL ARG GLN ASN GLY GLY THR THR TYR LYS 140 VAL VAL MET ASN VAL GLU ASN CYS ASN ILE 150 SER ARG VAL LYS ASP ALA ILE LEU ARG THR 160 ASP SER SER THR SER THR GLY ARG ILE VAL 170 ASN THR ARG TYR SER ASN VAL PRO THR LEU 180 PHE LYS GLY PHE LYS SER GLY ASN THR THR 190 ALA SER GLY ASN THR GLN TYR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 155.3 167.1 2 PRO -63.8 130.2 177.8 18.4 -26.3 3 THR -103.5 133.1 170.5 -58.1 4 VAL -88.6 123.1 -177.4 -179.9 5 VAL -97.0 124.9 -175.3 175.7 6 HIS -99.1 -33.6 -176.5 -61.1 -65.0 7 GLU -134.7 140.5 179.1 -11.5 -171.2 -173.5 8 THR -53.9 134.2 174.0 -62.0 9 ILE -85.7 119.1 173.6 -61.4 165.0 10 ARG -89.3 138.1 -176.0 -100.4 -143.6 -164.7 -159.8 11 VAL -123.3 102.2 -177.0 -170.7 12 PRO -62.6 164.6 -177.8 -16.5 36.8 13 ALA -50.9 126.9 178.7 14 GLY 76.4 -0.3 -179.8 15 GLN -97.4 157.6 178.7 -86.1 -51.8 126.1 16 THR -109.0 146.5 176.1 -48.3 17 PHE -127.5 117.0 175.9 171.6 -67.5 18 ASP -105.3 120.2 -178.7 -167.5 -22.9 19 GLY -90.9 -5.5 176.9 20 LYS 59.5 27.3 178.4 -58.3 -179.2 -180.0 -180.0 21 GLY 89.1 6.3 -177.1 22 GLN -85.7 154.0 -177.1 -61.1 -50.9 -70.9 23 THR -91.5 138.0 179.7 -57.6 24 TYR -130.2 122.6 176.9 -67.1 82.3 25 VAL -117.4 160.1 176.0 -47.2 26 ALA -85.2 155.7 168.5 27 ASN -88.7 118.3 -175.9 179.7 -61.3 28 PRO -64.3 -25.2 177.9 33.8 -47.4 29 ASN -76.1 -29.5 -178.5 -65.8 -20.8 30 THR -108.8 -39.1 178.4 60.1 31 LEU -106.5 -30.8 -179.8 -54.3 -172.5 32 GLY 131.0 157.7 -178.9 33 ASP -88.5 -13.7 -179.3 64.1 -14.8 34 GLY 91.5 19.3 177.8 35 SER -88.4 -163.2 174.2 69.3 36 GLN -87.0 1.6 179.2 -61.7 154.6 -120.0 37 ALA -53.8 130.5 -176.7 38 GLU -79.9 152.1 -173.2 -63.8 -164.2 124.9 39 ASN 43.7 71.3 171.2 127.4 -179.0 40 GLN -87.1 166.0 -178.3 -72.6 167.4 63.5 41 LYS -89.1 143.6 174.5 -66.0 171.4 74.0 67.7 42 PRO -60.3 152.5 169.9 33.0 -42.8 43 ILE -84.0 -28.1 -178.0 -72.8 178.4 44 PHE -132.1 133.4 172.8 -72.4 -85.3 45 ARG -120.8 113.7 -175.3 -164.8 -177.6 154.9 146.0 46 LEU -102.1 127.5 178.2 -64.6 -115.2 47 GLU -89.4 179.2 -171.0 -63.8 -50.7 -47.7 48 ALA -65.1 129.6 -178.9 49 GLY 77.3 9.8 -179.4 50 ALA -83.5 161.8 -178.8 51 SER -133.4 143.5 176.6 -57.3 52 LEU -120.2 139.1 -177.9 178.1 63.8 53 LYS -156.1 154.9 178.6 74.0 -177.9 -46.4 173.1 54 ASN 46.1 56.5 -175.2 -53.4 -41.5 55 VAL -125.2 140.5 176.0 155.5 56 VAL -113.6 119.9 175.8 170.5 57 ILE -98.8 116.0 173.9 -64.9 166.3 58 GLY -99.8 165.8 175.6 59 ALA -68.8 140.5 -3.7 60 PRO -70.6 126.6 -173.6 -6.0 27.5 61 ALA -98.0 2.0 -178.7 62 ALA 43.2 -118.7 179.1 63 ASP -120.7 36.6 169.2 -159.7 21.5 64 GLY 49.6 -112.5 -175.1 65 VAL -119.2 128.7 168.9 -177.3 66 HIS -111.2 141.8 177.5 -63.1 0.3 67 CYS -119.5 123.8 172.9 -58.0 68 TYR -102.7 84.6 -174.2 -74.7 76.1 69 GLY 103.5 -161.1 179.3 70 ASP -59.8 141.3 174.4 -64.7 152.1 71 CYS -156.3 139.3 175.2 58.6 72 THR -110.2 124.4 -177.0 -54.9 73 ILE -119.1 107.5 -175.9 -53.7 -60.3 74 THR -116.7 121.0 178.6 -49.2 75 ASN 53.5 52.7 178.1 179.7 36.0 76 VAL -106.6 132.6 179.5 167.0 77 ILE -112.9 119.4 173.0 -66.3 170.1 78 TRP -94.4 104.1 -177.6 -73.5 -95.5 79 GLU -71.6 -20.0 -176.9 -70.7 176.8 165.2 80 ASP -167.8 102.8 178.1 -172.0 149.4 81 VAL -65.9 135.0 174.8 169.6 82 GLY -78.6 -128.1 -179.8 83 GLU -63.8 -46.9 173.8 -163.8 -157.5 156.5 84 ASP -147.3 156.1 176.5 -48.2 -88.9 85 ALA -78.3 -58.1 -179.2 86 LEU -144.7 138.5 178.8 -177.6 138.0 87 THR -122.1 138.9 171.2 -53.0 88 LEU -92.8 107.7 -178.8 -178.4 63.5 89 LYS -86.7 -23.8 177.4 -54.4 -81.5 -78.1 174.0 90 SER -132.2 151.9 177.6 -58.5 91 SER -44.9 130.2 -179.3 -168.2 92 GLY 160.8 -171.9 -173.6 93 THR -119.0 121.1 178.6 -57.7 94 VAL -96.7 129.0 175.3 -174.5 95 ASN -121.9 119.8 174.5 -84.9 -68.5 96 ILE -108.0 131.4 171.2 -69.6 107.1 97 SER -138.5 130.0 -177.9 58.9 98 GLY 75.0 -172.3 -173.6 99 GLY 74.1 -164.8 -169.0 100 ALA -162.7 157.9 178.7 101 ALA -141.8 126.9 176.8 102 TYR -126.3 153.0 170.9 -58.0 90.7 103 LYS 50.2 50.9 178.0 -58.9 159.7 165.3 -75.6 104 ALA -98.1 113.3 -179.1 105 TYR -54.4 -41.5 176.4 -174.2 -95.3 106 ASP -132.0 -97.2 -173.4 -172.8 -168.1 107 LYS -101.2 148.7 177.4 40.5 -125.6 -159.5 -71.3 108 VAL -84.3 -65.8 -179.3 174.6 109 PHE -106.8 127.7 178.8 -57.3 113.3 110 GLN -117.4 121.4 -179.7 161.1 61.7 -17.9 111 ILE -107.3 119.1 -174.6 -50.1 -56.7 112 ASN -115.1 19.0 178.5 -74.9 -12.7 113 ALA -154.0 162.6 175.0 114 ALA -63.6 146.2 -178.0 115 GLY 165.3 -163.2 179.7 116 THR -132.8 153.2 175.5 -58.1 117 ILE -145.2 121.0 177.4 -178.2 159.6 118 ASN -112.1 130.2 -177.4 -60.8 -65.3 119 ILE -124.4 117.6 -176.2 -64.5 150.8 120 ARG -122.5 141.1 172.2 -55.5 -167.5 169.3 89.1 121 ASN 48.6 49.0 -175.8 -46.3 108.6 122 PHE -115.3 142.0 -179.4 -167.8 -103.3 123 ARG -104.5 127.5 176.1 -175.5 60.9 178.4 98.3 124 ALA -140.9 124.0 -178.1 125 ASP -133.3 137.0 -179.4 -177.7 -106.9 126 ASP 60.9 77.1 -177.2 173.2 -158.7 127 ILE -135.0 163.3 173.8 62.9 179.6 128 GLY -79.2 -61.1 169.8 129 LYS -144.3 150.9 -179.3 57.4 -83.0 -78.2 160.5 130 LEU -71.9 -47.3 179.0 -165.1 65.8 131 VAL -133.7 124.0 169.4 -175.3 132 ARG -115.3 132.4 168.5 -117.0 -119.7 73.1 152.8 133 GLN -79.4 137.3 176.3 174.5 169.7 -12.9 134 ASN -40.0 125.3 -172.5 -157.3 18.6 135 GLY -48.6 141.0 179.5 136 GLY 73.4 -31.2 -174.7 137 THR -59.9 151.9 -175.5 73.9 138 THR -119.7 8.5 171.0 52.6 139 TYR -71.0 164.3 -178.1 47.8 67.3 140 LYS -84.0 123.4 169.5 -174.4 171.1 168.3 -177.0 141 VAL -120.0 136.0 174.6 174.5 142 VAL -100.2 115.2 -179.9 167.6 143 MET -107.7 128.3 -174.4 -55.2 176.3 -177.4 144 ASN -136.8 126.0 -174.7 171.4 49.6 145 VAL -123.6 121.2 -177.6 179.7 146 GLU -129.3 132.0 173.3 -73.1 175.1 -11.3 147 ASN 51.9 41.9 178.0 -66.8 -98.6 148 CYS -101.2 173.4 172.0 -63.2 149 ASN -139.2 105.3 -171.9 178.0 -1.1 150 ILE -111.4 120.7 178.9 -51.4 -53.6 151 SER -136.3 154.3 179.4 54.1 152 ARG 52.6 71.9 -178.4 -60.1 -166.8 -105.0 142.8 153 VAL -101.4 124.8 -180.0 -177.9 154 LYS -66.9 -39.8 -172.1 -64.0 179.8 174.5 166.3 155 ASP -125.1 -62.6 -173.0 173.8 35.3 156 ALA -159.7 160.8 176.6 157 ILE -81.6 -51.2 -179.6 -69.1 -178.5 158 LEU -113.4 129.8 177.6 -98.5 26.7 159 ARG -137.2 137.2 -177.2 -167.6 167.6 180.0 -174.3 160 THR -151.2 171.8 175.1 -170.8 161 ASP -132.0 -2.1 178.8 -66.7 -53.4 162 SER -92.6 132.9 177.4 157.7 163 SER -77.8 -1.3 175.8 63.7 164 THR -107.8 -9.4 178.5 36.6 165 SER -69.8 144.5 180.0 -63.0 166 THR -117.1 150.3 179.6 62.7 167 GLY -132.2 133.0 -176.9 168 ARG -130.9 119.7 176.0 -176.7 174.4 178.2 -110.6 169 ILE -124.2 125.0 -166.8 -65.4 171.1 170 VAL -137.4 134.8 172.6 135.3 171 ASN 49.9 44.5 -175.0 -58.8 -43.8 172 THR -117.7 142.3 174.0 -68.8 173 ARG -91.8 137.3 -179.0 -40.1 -143.9 -58.5 137.0 174 TYR -146.6 151.3 -173.7 67.4 87.9 175 SER -151.9 130.0 -178.4 178.8 176 ASN 57.0 52.7 -178.6 -62.2 -41.0 177 VAL -112.6 114.2 176.9 166.9 178 PRO -54.2 -52.6 173.0 -27.0 43.0 179 THR -136.3 154.3 169.7 4.0 180 LEU -75.7 -47.4 -175.8 -58.0 168.7 181 PHE -121.9 150.9 -179.6 -49.5 89.7 182 LYS -150.4 114.9 173.0 -171.0 165.1 -176.6 171.9 183 GLY 106.8 -4.1 -178.0 184 PHE -78.4 141.4 173.6 -60.9 79.3 185 LYS -67.9 148.1 173.3 177.5 178.9 180.0 180.0 186 SER -47.0 133.2 -179.1 -63.5 187 GLY 93.5 -13.5 180.0 188 ASN -98.1 10.2 177.6 -83.7 0.7 189 THR -117.8 142.6 174.8 41.8 190 THR -127.4 146.0 167.5 -23.0 191 ALA -156.3 138.1 176.5 192 SER -157.0 150.6 177.2 42.6 193 GLY 72.1 17.7 -177.1 194 ASN -90.3 164.1 -179.7 -61.3 -49.4 195 THR -141.4 117.8 172.6 -67.6 196 GLN -83.7 132.1 179.2 -171.0 -171.2 -92.9 197 TYR -142.2 178.9 0.0 71.7 -86.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA -12.103 1.454 51.789 2 PRO -8.640 2.996 51.049 3 THR -6.068 0.266 51.187 4 VAL -2.513 1.150 52.160 5 VAL -0.440 -1.097 49.838 6 HIS 2.692 -2.524 51.386 7 GLU 3.763 -4.914 48.677 8 THR 3.030 -4.523 44.940 9 ILE -0.201 -6.121 43.788 10 ARG 0.463 -8.541 40.907 11 VAL -2.230 -8.979 38.286 12 PRO -1.339 -12.197 36.292 13 ALA -1.391 -12.530 32.533 14 GLY -4.744 -11.913 30.941 15 GLN -6.478 -11.105 34.245 16 THR -8.414 -8.036 35.453 17 PHE -8.244 -6.287 38.843 18 ASP -11.301 -4.294 39.534 19 GLY -10.879 -1.925 42.476 20 LYS -14.593 -1.117 42.333 21 GLY -13.872 2.632 42.562 22 GLN -11.823 2.216 45.769 23 THR -8.650 4.001 46.693 24 TYR -5.207 2.483 46.915 25 VAL -2.247 4.392 48.337 26 ALA 1.336 3.273 48.804 27 ASN 3.074 2.540 52.014 28 PRO 5.995 5.114 51.788 29 ASN 8.373 2.780 53.709 30 THR 7.960 -0.193 51.361 31 LEU 6.980 1.283 47.973 32 GLY 7.859 5.018 48.011 33 ASP 6.384 8.415 48.753 34 GLY 5.670 9.796 45.223 35 SER 8.480 12.283 45.196 36 GLN 11.184 12.487 42.457 37 ALA 13.271 9.922 44.352 38 GLU 14.337 7.317 41.802 39 ASN 13.188 3.804 41.370 40 GLN 10.216 3.611 43.742 41 LYS 7.974 0.422 43.582 42 PRO 4.772 0.182 41.545 43 ILE 1.541 -0.114 43.539 44 PHE 0.310 -2.412 40.699 45 ARG 2.261 -4.776 38.540 46 LEU 0.414 -5.970 35.512 47 GLU 1.531 -8.971 33.536 48 ALA 0.917 -9.412 29.822 49 GLY -2.655 -8.831 28.722 50 ALA -3.711 -7.931 32.272 51 SER -6.195 -5.130 33.022 52 LEU -6.565 -2.797 35.893 53 LYS -9.901 -0.997 36.171 54 ASN -12.072 1.249 38.403 55 VAL -9.157 2.073 40.664 56 VAL -8.321 5.359 42.428 57 ILE -4.547 5.824 43.246 58 GLY -4.157 8.356 45.970 59 ALA -1.029 10.028 47.334 60 PRO 1.546 8.733 48.358 61 ALA 1.381 7.098 44.908 62 ALA 4.989 5.770 44.762 63 ASP 5.539 4.638 41.125 64 GLY 1.983 3.815 40.232 65 VAL 1.402 1.078 37.664 66 HIS 3.965 -1.001 35.669 67 CYS 2.978 -3.098 32.671 68 TYR 5.144 -5.934 31.450 69 GLY 3.636 -6.335 28.025 70 ASP 0.090 -5.341 26.963 71 CYS -2.219 -3.735 29.492 72 THR -5.588 -2.162 29.442 73 ILE -6.204 0.510 31.992 74 THR -9.846 1.461 32.298 75 ASN -11.331 4.288 34.461 76 VAL -8.315 4.495 36.773 77 ILE -7.785 7.849 38.581 78 TRP -4.335 8.990 39.710 79 GLU -5.311 11.794 42.202 80 ASP -1.721 12.787 42.588 81 VAL 0.809 11.029 40.387 82 GLY 3.881 9.875 42.279 83 GLU 7.165 9.352 40.499 84 ASP 5.284 8.180 37.330 85 ALA 1.610 7.185 36.787 86 LEU 2.134 4.109 34.577 87 THR 5.347 2.804 32.973 88 LEU 5.663 0.272 30.141 89 LYS 8.547 -1.983 31.232 90 SER 8.393 -4.566 28.416 91 SER 7.388 -4.274 24.792 92 GLY 3.670 -4.067 24.251 93 THR 0.585 -1.923 24.014 94 VAL -0.844 0.121 26.725 95 ASN -4.464 1.158 26.190 96 ILE -5.970 3.828 28.562 97 SER -9.674 4.772 28.417 98 GLY -11.379 7.068 30.784 99 GLY -9.956 8.182 34.124 100 ALA -7.673 10.994 35.050 101 ALA -4.145 11.933 36.187 102 TYR -3.408 15.050 38.349 103 LYS -0.317 16.664 39.837 104 ALA 2.444 14.755 38.164 105 TYR 5.663 16.658 38.821 106 ASP 7.068 15.308 35.584 107 LYS 5.598 12.413 33.640 108 VAL 2.304 10.693 33.700 109 PHE 3.252 7.939 31.231 110 GLN 6.838 6.692 30.805 111 ILE 7.453 4.176 27.991 112 ASN 10.586 2.116 28.614 113 ALA 10.323 -0.484 25.865 114 ALA 9.297 -0.377 22.186 115 GLY 5.481 -0.371 21.976 116 THR 2.190 1.573 21.696 117 ILE 0.128 3.633 24.139 118 ASN -3.315 4.775 23.142 119 ILE -4.854 7.217 25.606 120 ARG -8.539 7.823 25.119 121 ASN -11.035 10.052 26.978 122 PHE -8.576 11.034 29.618 123 ARG -8.362 14.062 31.871 124 ALA -4.887 15.222 32.874 125 ASP -4.093 18.393 34.813 126 ASP -0.900 19.929 36.146 127 ILE 1.616 17.523 34.689 128 GLY 5.207 17.741 33.232 129 LYS 4.445 15.682 30.103 130 LEU 1.708 13.115 29.301 131 VAL 4.025 10.533 27.664 132 ARG 7.848 10.551 27.657 133 GLN 9.715 7.742 25.898 134 ASN 12.696 6.852 28.129 135 GLY 15.284 9.473 27.459 136 GLY 17.806 9.004 24.748 137 THR 16.322 5.681 23.472 138 THR 15.850 5.273 19.707 139 TYR 13.443 2.331 19.485 140 LYS 9.984 3.085 18.085 141 VAL 7.115 4.030 20.372 142 VAL 3.720 4.871 18.775 143 MET 1.977 7.482 20.968 144 ASN -1.718 8.127 20.420 145 VAL -4.092 10.580 22.228 146 GLU -7.780 10.698 21.377 147 ASN -10.669 12.793 22.758 148 CYS -8.720 13.921 25.855 149 ASN -8.580 17.119 27.893 150 ILE -5.036 18.018 28.915 151 SER -4.114 21.190 30.922 152 ARG -1.131 22.889 32.618 153 VAL 1.633 21.044 31.031 154 LYS 5.192 21.993 32.047 155 ASP 6.806 20.776 28.903 156 ALA 5.031 18.873 26.082 157 ILE 2.078 16.381 25.766 158 LEU 4.118 13.820 23.790 159 ARG 7.958 13.626 24.047 160 THR 10.585 11.282 22.419 161 ASP 14.228 11.308 21.196 162 SER 13.732 8.548 18.637 163 SER 13.384 9.452 15.036 164 THR 11.027 6.489 14.462 165 SER 8.512 7.248 17.265 166 THR 5.163 8.665 16.055 167 GLY 2.773 10.985 17.883 168 ARG -0.888 11.425 17.127 169 ILE -3.164 13.910 19.001 170 VAL -6.765 13.951 17.829 171 ASN -9.929 15.706 19.032 172 THR -8.333 16.849 22.257 173 ARG -8.918 19.971 24.338 174 TYR -5.722 21.466 25.763 175 SER -4.757 24.563 27.825 176 ASN -1.410 26.102 28.848 177 VAL 0.514 23.455 26.968 178 PRO 3.995 24.762 25.679 179 THR 4.126 22.287 22.686 180 LEU 1.880 19.378 21.769 181 PHE 4.783 17.133 20.508 182 LYS 8.505 17.255 21.256 183 GLY 11.438 15.444 19.648 184 PHE 9.723 13.718 16.668 185 LYS 11.184 13.851 13.108 186 SER 9.067 15.940 10.716 187 GLY 6.311 13.778 9.316 188 ASN 6.102 11.693 12.503 189 THR 3.457 13.858 14.120 190 THR -0.258 13.942 13.167 191 ALA -2.966 16.225 14.680 192 SER -6.621 17.046 13.987 193 GLY -9.802 18.264 15.742 194 ASN -7.957 19.798 18.649 195 THR -8.857 22.867 20.612 196 GLN -6.615 25.247 22.509 197 TYR -8.518 26.922 25.349 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S/S S S S S 10 S S S S S S S S S C 20 S S S S S S S/T T T T/S 30 S S S C C S S S S/S S 40 S S S/S S S S S S S S 50 S S S S/S S S S S S/P S 60 S S S S S S S/T T T T/S 70 S S S S S/S S S S S C 80 T T T T S S S S S S/S 90 S S S/S S S S S S/S S S 100 S S C T T T T S S S 110 S S S/S S S S/S S S S S 120 S/S S S S S S C S S S 130 S/S S S S C S S S S/S S 140 S S S S S S S/S S S S 150 S S C C C C S S S S 160 C C C S S S S S S S 170 S/S S S S S S/S S S S S 180 S S S C T T T T/S S S 190 S S S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E S S E E 10 E t T T e E E E E E 20 E E E E E E e T T T 30 T t S S S S S 40 e E E E e T T E 50 E E E E E E E e S S 60 t T T e E E E E e e 70 E E E E E E E E e S 80 S e E E E E E 90 S E E E E E E e e E 100 E E E E E E E E E E 110 E e S e E E E E E E 120 e e E E E E E E E E 130 E E E e T T t S e 140 E E E E E E e e E E 150 E E E E E E E E E e 160 t T T t E E E E E 170 e e E E E S S e 180 E E S t T T e E E 190 E E S E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 2.8 3.8 82.9 2 PRO 43.4 34.9 66.6 3 THR 47.2 44.2 69.0 4 VAL 55.2 46.4 68.0 5 VAL 113.7 95.7 40.3 6 HIS 64.3 42.8 68.5 7 GLU 7.8 5.6 80.0 8 THR 89.6 83.8 47.2 9 ILE 99.6 69.4 48.2 10 ARG 82.9 39.7 75.4 11 VAL 115.0 96.8 43.2 12 PRO 43.4 34.8 65.9 13 ALA 23.2 32.0 72.7 14 GLY 8.9 25.6 76.8 15 GLN 43.2 29.1 77.7 16 THR 61.8 57.8 64.1 17 PHE 120.9 72.5 46.5 18 ASP 63.2 57.2 60.6 19 GLY 34.0 97.8 56.8 20 LYS 21.7 12.5 84.5 21 GLY 11.6 33.5 67.8 22 GLN 72.3 48.7 79.3 23 THR 75.4 70.5 53.1 24 TYR 155.3 85.8 42.3 25 VAL 93.7 78.9 52.5 26 ALA 72.6 100.0 46.6 27 ASN 95.6 79.1 52.3 28 PRO 70.7 56.8 68.6 29 ASN 14.0 11.6 81.1 30 THR 54.4 50.9 72.7 31 LEU 147.6 99.9 52.3 32 GLY 24.4 70.1 61.9 33 ASP 48.5 43.9 65.5 34 GLY 32.5 93.4 72.9 35 SER 37.1 44.4 80.4 36 GLN 43.2 29.1 70.4 37 ALA 18.8 25.9 83.4 38 GLU 10.9 7.8 88.8 39 ASN 4.5 3.7 83.9 40 GLN 136.8 92.0 62.3 41 LYS 68.2 39.3 73.5 42 PRO 108.5 87.2 56.8 43 ILE 143.5 100.0 37.2 44 PHE 166.8 100.0 20.9 45 ARG 146.3 70.0 58.8 46 LEU 147.8 100.0 39.1 47 GLU 111.8 80.6 62.2 48 ALA 25.2 34.8 74.8 49 GLY 9.3 26.9 70.3 50 ALA 72.6 100.0 61.6 51 SER 59.9 71.6 60.9 52 LEU 147.8 100.0 21.4 53 LYS 105.7 61.0 61.6 54 ASN 81.0 67.0 65.3 55 VAL 118.8 100.0 35.6 56 VAL 97.9 82.4 60.9 57 ILE 143.5 100.0 35.9 58 GLY 31.9 91.7 59.0 59 ALA 35.1 48.4 68.1 60 PRO 82.8 66.5 61.1 61 ALA 72.4 99.7 51.5 62 ALA 72.6 100.0 54.1 63 ASP 100.8 91.3 64.4 64 GLY 34.7 99.6 62.5 65 VAL 118.8 100.0 33.1 66 HIS 137.3 91.4 52.1 67 CYS 99.1 99.9 36.7 68 TYR 129.9 71.7 65.8 69 GLY 26.8 77.0 62.1 70 ASP 44.6 40.3 69.1 71 CYS 98.5 99.3 40.0 72 THR 50.3 47.1 75.6 73 ILE 143.1 99.7 31.6 74 THR 64.1 60.0 63.3 75 ASN 51.8 42.8 67.0 76 VAL 118.5 99.8 40.1 77 ILE 87.6 61.1 55.7 78 TRP 204.5 99.8 30.1 79 GLU 61.1 44.1 61.6 80 ASP 67.4 61.0 65.0 81 VAL 118.6 99.9 47.7 82 GLY 33.5 96.3 66.5 83 GLU 112.1 80.9 70.9 84 ASP 98.5 89.1 67.5 85 ALA 72.6 100.0 32.2 86 LEU 147.8 100.0 29.6 87 THR 102.7 96.1 54.0 88 LEU 147.8 100.0 51.1 89 LYS 110.4 63.7 63.3 90 SER 40.8 48.8 61.3 91 SER 24.9 29.8 70.8 92 GLY 20.0 57.3 72.0 93 THR 67.3 63.0 70.8 94 VAL 118.8 100.0 34.4 95 ASN 78.5 64.9 70.4 96 ILE 142.1 99.0 36.0 97 SER 43.9 52.5 69.2 98 GLY 15.0 43.2 70.1 99 GLY 30.4 87.4 59.2 100 ALA 64.8 89.2 43.6 101 ALA 72.6 100.0 31.7 102 TYR 109.0 60.2 59.5 103 LYS 62.5 36.0 80.9 104 ALA 72.4 99.7 53.5 105 TYR 54.4 30.1 82.6 106 ASP 61.5 55.6 67.2 107 LYS 135.7 78.3 66.6 108 VAL 118.8 100.0 25.8 109 PHE 166.8 100.0 25.0 110 GLN 130.1 87.5 62.2 111 ILE 143.5 100.0 39.0 112 ASN 93.9 77.7 67.1 113 ALA 59.5 81.9 62.3 114 ALA 37.5 51.6 66.3 115 GLY 22.2 63.7 69.9 116 THR 75.9 71.0 62.8 117 ILE 143.5 100.0 25.9 118 ASN 102.4 84.7 61.4 119 ILE 143.5 100.0 25.8 120 ARG 127.5 61.0 73.5 121 ASN 41.7 34.5 67.7 122 PHE 166.7 99.9 38.0 123 ARG 130.0 62.2 69.4 124 ALA 72.6 100.0 38.3 125 ASP 94.8 85.8 59.4 126 ASP 64.5 58.4 65.4 127 ILE 143.5 100.0 46.4 128 GLY 33.6 96.6 56.6 129 LYS 155.1 89.4 53.5 130 LEU 147.8 100.0 19.3 131 VAL 118.8 100.0 29.9 132 ARG 184.5 88.3 53.9 133 GLN 148.5 99.9 54.8 134 ASN 64.4 53.3 78.8 135 GLY 14.2 40.9 83.7 136 GLY 0.5 1.6 76.3 137 THR 72.2 67.5 67.0 138 THR 22.4 21.0 86.6 139 TYR 119.0 65.8 65.2 140 LYS 76.2 44.0 69.3 141 VAL 118.8 100.0 42.7 142 VAL 70.5 59.4 66.3 143 MET 159.4 100.0 38.7 144 ASN 108.1 89.4 61.0 145 VAL 118.8 100.0 34.5 146 GLU 105.7 76.3 73.0 147 ASN 52.9 43.8 77.3 148 CYS 98.3 99.1 48.4 149 ASN 91.8 75.9 64.6 150 ILE 143.5 100.0 32.8 151 SER 76.1 91.1 66.2 152 ARG 77.7 37.2 79.0 153 VAL 118.8 100.0 48.6 154 LYS 83.4 48.1 68.3 155 ASP 90.3 81.8 59.7 156 ALA 72.6 100.0 53.3 157 ILE 143.5 100.0 22.8 158 LEU 147.8 100.0 32.7 159 ARG 141.8 67.9 63.2 160 THR 106.9 100.0 51.7 161 ASP 65.9 59.7 80.5 162 SER 83.6 100.0 72.8 163 SER 21.9 26.1 76.4 164 THR 37.6 35.2 81.9 165 SER 83.6 100.0 58.3 166 THR 65.2 61.0 63.3 167 GLY 34.8 99.9 43.1 168 ARG 117.9 56.5 64.3 169 ILE 143.5 100.0 33.2 170 VAL 109.8 92.4 73.9 171 ASN 56.1 46.4 72.5 172 THR 106.9 100.0 49.1 173 ARG 97.5 46.7 65.4 174 TYR 148.8 82.2 46.2 175 SER 71.4 85.4 55.9 176 ASN 20.4 16.9 76.9 177 VAL 118.4 99.6 42.8 178 PRO 63.2 50.8 78.6 179 THR 39.5 37.0 75.8 180 LEU 112.8 76.3 41.9 181 PHE 143.8 86.2 41.0 182 LYS 93.2 53.7 74.6 183 GLY 9.7 28.0 71.3 184 PHE 165.2 99.1 48.9 185 LYS 34.7 20.0 81.7 186 SER 0.0 0.0 84.8 187 GLY 0.0 0.0 87.3 188 ASN 90.4 74.8 62.3 189 THR 74.1 69.3 55.4 190 THR 27.5 25.8 74.3 191 ALA 52.5 72.3 63.2 192 SER 16.9 20.2 76.4 193 GLY 5.3 15.2 81.2 194 ASN 109.8 90.8 50.9 195 THR 36.8 34.4 71.8 196 GLN 38.6 26.0 76.8 197 TYR 122.5 67.7 74.9