Protein Data Bank File : 1cjka Title : LYASE/LYASE/SIGNALING PROTEIN 16-APR-99 1CJK Number of Amino Acid Residues : 189 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET MET PHE HIS LYS ILE TYR ILE GLN LYS 10 HIS ASP ASN VAL SER ILE LEU PHE ALA ASP 20 ILE GLU GLY PHE THR SER LEU ALA SER GLN 30 CYS THR ALA GLN GLU LEU VAL MET THR LEU 40 ASN GLU LEU PHE ALA ARG PHE ASP LYS LEU 50 ALA ALA GLU ASN HIS CYS LEU ARG ILE LYS 60 ILE LEU GLY ASP CYS TYR TYR CYS VAL SER 70 GLY LEU PRO GLU ALA ARG ALA ASP HIS ALA 80 HIS CYS CYS VAL GLU MET GLY MET ASP MET 90 ILE GLU ALA ILE SER LEU VAL ARG GLU MET 100 THR GLY VAL ASN VAL ASN MET ARG VAL GLY 110 ILE HIS SER GLY ARG VAL HIS CYS GLY VAL 120 LEU GLY LEU ARG LYS TRP GLN PHE ASP VAL 130 TRP SER ASN ASP VAL THR LEU ALA ASN HIS 140 MET GLU ALA GLY GLY LYS ALA GLY ARG ILE 150 HIS ILE THR LYS ALA THR LEU SER TYR LEU 160 ASN GLY ASP TYR GLU VAL GLU PRO GLY CYS 170 GLY GLY GLU ARG ASN ALA TYR LEU LYS GLU 180 HIS SER ILE GLU THR PHE LEU ILE LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 147.2 -179.2 61.0 -165.5 -48.7 2 MET -95.8 -18.2 178.2 -68.6 131.7 -68.4 3 PHE -106.7 131.4 178.6 -85.9 -77.9 4 HIS -56.6 138.1 179.4 -76.4 56.3 5 LYS -56.1 130.1 -179.7 -173.0 -171.6 -177.3 -59.2 6 ILE -97.6 129.1 -179.6 -172.9 173.0 7 TYR -100.5 70.6 -179.2 -61.3 78.4 8 ILE -141.1 148.8 179.3 -68.6 178.8 9 GLN -144.4 148.7 -179.3 50.4 -166.6 -143.7 10 LYS -91.1 146.3 179.4 -168.2 176.3 70.0 174.3 11 HIS -143.7 118.1 177.5 -77.5 87.1 12 ASP -90.1 162.4 178.1 -76.9 -89.1 13 ASN 57.1 67.2 179.3 -56.5 -64.4 14 VAL -137.9 161.1 179.7 -58.0 15 SER -117.2 143.2 -179.3 -73.1 16 ILE -124.6 131.0 179.6 -55.7 112.8 17 LEU -120.9 135.4 179.3 169.4 143.0 18 PHE -122.5 144.5 179.4 -84.6 83.4 19 ALA -141.9 126.3 -179.6 20 ASP -131.5 149.5 -179.9 -177.6 89.7 21 ILE -90.7 138.5 178.9 -54.5 178.3 22 GLU -76.1 137.6 -179.9 -81.9 -162.9 -1.1 23 GLY 48.7 43.9 -179.5 24 PHE -68.6 -42.5 179.0 173.2 74.4 25 THR -61.1 -38.3 179.0 -69.0 26 SER -68.4 -40.4 -179.7 -179.5 27 LEU -64.7 -39.8 179.7 -121.1 49.6 28 ALA -65.2 -15.0 179.7 29 SER -81.4 -22.9 -179.7 -64.8 30 GLN -88.3 -74.2 179.6 -70.3 138.0 75.7 31 CYS -71.9 157.8 -179.3 39.8 32 THR -63.8 152.9 179.6 -55.1 33 ALA -57.7 -28.9 179.7 34 GLN -70.5 -52.0 -179.8 -53.4 -179.1 -10.7 35 GLU -63.3 -43.8 180.0 174.6 -176.6 10.8 36 LEU -54.0 -46.8 -179.2 172.9 74.6 37 VAL -60.7 -32.1 179.4 -178.9 38 MET -68.0 -42.5 179.5 -59.9 -173.0 121.3 39 THR -65.8 -32.7 179.7 -53.2 40 LEU -74.9 -39.4 179.8 -127.8 60.4 41 ASN -67.8 -42.0 178.5 -165.4 14.1 42 GLU -58.8 -46.2 179.8 -162.3 56.3 46.1 43 LEU -68.3 -53.5 -178.5 -170.1 57.1 44 PHE -70.7 -14.8 178.2 -64.1 -55.0 45 ALA -74.9 -49.9 179.2 46 ARG -59.2 -45.6 179.7 -57.0 179.1 -174.6 -90.1 47 PHE -51.4 -51.8 -178.7 -81.1 9.1 48 ASP -62.3 -29.4 -179.5 -80.7 12.3 49 LYS -71.6 -47.0 179.7 -148.0 159.7 -59.1 175.4 50 LEU -64.6 -29.0 -178.6 -52.7 161.4 51 ALA -62.5 -47.6 -179.5 52 ALA -62.3 -37.7 179.3 53 GLU -65.1 -47.4 -178.5 -55.0 173.6 5.9 54 ASN -84.0 15.3 178.6 -54.5 4.5 55 HIS 57.3 35.8 178.6 -33.2 -70.3 56 CYS -109.0 130.3 179.2 -92.1 57 LEU -91.2 114.7 179.0 179.3 60.9 58 ARG -67.7 137.1 178.6 -157.3 -70.1 -64.7 -81.6 59 ILE -96.9 -80.6 177.9 -60.7 -60.4 60 LYS -156.4 169.1 -179.9 58.9 -173.3 -172.0 180.0 61 ILE -110.9 117.9 179.6 -62.8 178.1 62 LEU -101.5 65.1 -179.6 -58.8 178.3 63 GLY 85.5 -94.9 179.6 64 ASP -110.3 -1.1 -179.3 67.5 -29.3 65 CYS -94.1 116.2 179.6 175.4 66 TYR -109.5 133.2 178.7 179.9 -81.6 67 TYR -145.4 137.9 -179.2 68.0 -63.4 68 CYS -139.4 165.3 179.4 63.2 69 VAL -133.3 158.2 179.0 -57.5 70 SER -123.6 135.9 -179.1 179.7 71 GLY 113.0 8.0 179.8 72 LEU -131.3 147.9 -1.1 -87.9 -173.4 73 PRO -83.7 -19.8 179.9 35.5 -43.1 74 GLU -91.5 132.0 -179.4 178.1 69.6 40.6 75 ALA -56.8 151.1 -179.8 76 ARG -155.6 139.4 179.5 166.5 -174.7 -75.5 -107.6 77 ALA -92.9 -3.5 179.8 78 ASP -95.1 -3.8 -176.9 -168.5 20.6 79 HIS -42.3 -47.1 -179.7 76.9 66.8 80 ALA -61.7 -48.4 -179.1 81 HIS -59.2 -35.2 -179.9 -49.5 86.6 82 CYS -60.5 -49.7 179.8 -58.1 83 CYS -65.8 -34.4 179.0 -77.5 84 VAL -66.9 -48.4 178.8 -161.6 85 GLU -62.7 -29.0 178.9 -85.2 -58.3 -33.8 86 MET -63.0 -55.3 179.7 175.3 83.6 -128.3 87 GLY -57.3 -37.0 179.3 88 MET -54.3 -49.0 179.4 -62.2 -78.3 -74.4 89 ASP -70.4 -39.7 -179.5 -71.4 -15.5 90 MET -59.6 -60.8 -179.5 -64.9 -175.9 98.4 91 ILE -47.9 -37.7 179.8 -58.1 179.1 92 GLU -71.9 -42.0 -180.0 -176.3 175.0 60.3 93 ALA -61.9 -38.7 -179.3 94 ILE -61.7 -35.7 180.0 -58.8 166.2 95 SER -65.7 -45.5 180.0 -66.3 96 LEU -57.0 -51.5 179.5 -54.6 -179.0 97 VAL -57.7 -47.3 179.5 170.8 98 ARG -61.7 -29.7 179.8 179.7 162.5 43.0 75.6 99 GLU -81.4 -46.0 -179.5 -71.5 171.5 11.9 100 MET -79.6 -12.1 -178.1 71.3 169.0 -94.8 101 THR -110.3 -44.4 -179.4 -65.1 102 GLY 106.7 -25.6 179.4 103 VAL -62.0 147.3 -179.8 168.0 104 ASN -87.1 72.5 179.5 -178.1 40.4 105 VAL -96.8 122.2 178.7 -153.2 106 ASN -138.0 137.1 -179.3 -66.2 -84.6 107 MET -128.2 150.1 177.1 -63.0 -179.9 92.5 108 ARG -102.4 144.0 -179.7 -59.4 -175.3 -59.2 -90.2 109 VAL -120.0 135.5 180.0 -176.2 110 GLY -127.8 136.5 -179.9 111 ILE -135.8 145.5 178.2 -55.1 -179.1 112 HIS -158.3 154.4 -179.3 173.2 72.8 113 SER -126.8 145.9 179.9 -50.2 114 GLY 168.5 -148.3 -179.7 115 ARG -101.7 150.6 -179.9 62.5 163.5 169.2 -124.3 116 VAL -147.7 152.9 176.6 -51.0 117 HIS -103.4 145.5 -179.7 -92.9 125.7 118 CYS -146.9 153.0 -180.0 67.5 119 GLY 154.7 -140.8 179.9 120 VAL -137.9 163.0 179.9 -70.4 121 LEU -132.1 155.0 179.3 -61.2 171.9 122 GLY 80.4 -167.9 -179.1 123 LEU -111.6 -45.1 -177.6 -56.0 177.5 124 ARG -98.5 145.4 178.6 -41.6 -93.8 -93.6 102.4 125 LYS 49.8 70.5 178.4 -53.2 -139.8 178.8 -177.7 126 TRP -69.4 147.3 177.8 -80.1 0.5 127 GLN -154.3 112.7 -179.4 -72.4 -173.2 -15.2 128 PHE -48.9 130.9 -178.4 -170.1 57.3 129 ASP -145.7 177.2 179.8 -152.7 -4.8 130 VAL -134.0 149.2 179.7 -73.8 131 TRP -148.2 139.4 176.7 -46.4 -90.4 132 SER 163.4 161.3 179.1 73.8 133 ASN -58.9 -35.0 179.8 -72.2 -19.9 134 ASP -65.8 -26.1 178.6 -69.1 -22.9 135 VAL -81.4 -39.4 -179.4 -173.3 136 THR -59.6 -41.5 -179.8 -50.4 137 LEU -65.0 -45.8 179.6 174.8 52.8 138 ALA -56.2 -38.7 178.7 139 ASN -64.7 -36.7 179.2 171.1 -120.6 140 HIS -74.5 -23.7 178.5 -83.8 -82.0 141 MET -69.7 -30.6 179.2 -71.2 -69.6 -55.1 142 GLU -71.4 -39.9 179.4 163.6 -98.9 -76.7 143 ALA -66.5 -41.4 179.0 144 GLY -91.3 18.7 -180.0 145 GLY -87.0 -175.5 -179.7 146 LYS -128.0 134.0 -178.5 -89.4 -172.8 155.7 -174.2 147 ALA -47.3 121.1 179.7 148 GLY 67.9 33.8 -179.9 149 ARG -147.3 154.6 -180.0 -67.9 -64.2 -58.6 -76.9 150 ILE -99.2 111.4 -178.7 -70.8 -172.0 151 HIS -95.5 124.6 180.0 -164.1 -146.8 152 ILE -132.4 159.6 179.9 63.1 171.6 153 THR -92.8 176.6 179.9 67.7 154 LYS -72.1 -34.7 179.2 -173.6 -175.5 -179.9 -179.2 155 ALA -62.1 -32.3 179.2 156 THR -75.9 -38.3 179.6 -70.3 157 LEU -60.6 -31.8 179.9 -165.1 62.9 158 SER -69.8 -20.9 179.5 70.9 159 TYR -96.1 0.3 -179.5 -69.3 -70.8 160 LEU -89.6 -11.6 179.5 -97.4 64.3 161 ASN 53.2 23.0 178.2 -59.3 177.6 162 GLY 69.2 40.2 -179.9 163 ASP -90.6 -43.2 -179.8 -69.8 50.8 164 TYR -97.1 141.4 179.1 -52.1 -88.6 165 GLU -83.9 129.6 -179.1 -73.5 -161.4 52.0 166 VAL -116.7 176.3 179.0 -73.1 167 GLU -151.5 159.0 -180.0 60.5 159.4 -61.5 168 PRO -56.8 124.6 -178.8 -34.4 46.8 169 GLY -89.5 -23.3 -179.3 170 CYS 56.2 32.0 -179.2 -73.1 171 GLY -58.5 -23.4 -179.9 172 GLY -60.9 -38.1 -179.5 173 GLU -80.9 -7.5 -179.8 44.5 -155.9 76.4 174 ARG -101.5 -29.9 -179.4 -148.1 172.1 -62.5 101.8 175 ASN -133.1 127.1 -179.0 -177.4 -67.8 176 ALA -59.4 -34.2 -179.6 177 TYR -64.9 -43.8 179.7 -167.9 90.5 178 LEU -62.5 -42.0 179.7 -60.9 171.9 179 LYS -66.8 -60.0 -179.1 -177.9 -179.7 -178.1 178.2 180 GLU -53.7 -17.5 179.4 -64.7 -179.3 13.8 181 HIS -111.2 11.1 178.3 -75.3 110.0 182 SER 57.4 55.2 -178.7 -45.8 183 ILE -100.9 140.8 178.5 -58.4 -62.4 184 GLU -106.2 112.5 -178.9 -72.6 -177.7 71.6 185 THR -100.5 161.2 -179.3 62.3 186 PHE -144.6 157.9 179.8 -54.9 -78.6 187 LEU -120.4 147.8 179.9 -63.3 179.3 188 ILE -88.7 152.9 180.0 -64.2 -63.6 189 LEU -98.9 -52.6 0.0 -62.2 172.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 28.160 -26.198 33.536 2 MET 30.448 -23.398 32.296 3 PHE 31.757 -22.302 35.691 4 HIS 33.948 -24.700 37.671 5 LYS 32.049 -25.891 40.740 6 ILE 32.947 -23.566 43.591 7 TYR 33.698 -25.007 47.046 8 ILE 32.803 -22.015 49.263 9 GLN 30.182 -21.172 51.895 10 LYS 29.215 -18.087 53.933 11 HIS 29.352 -17.722 57.709 12 ASP 28.163 -14.770 59.853 13 ASN 29.219 -13.954 63.424 14 VAL 32.843 -15.146 63.588 15 SER 36.149 -13.851 64.938 16 ILE 39.497 -13.635 63.121 17 LEU 42.959 -13.415 64.689 18 PHE 46.253 -12.537 62.974 19 ALA 49.795 -12.772 64.326 20 ASP 52.984 -11.598 62.596 21 ILE 56.679 -11.474 63.579 22 GLU 58.635 -8.185 63.741 23 GLY 61.657 -7.786 61.480 24 PHE 61.343 -11.326 60.146 25 THR 62.998 -10.511 56.802 26 SER 65.793 -8.955 58.847 27 LEU 66.031 -11.988 61.159 28 ALA 66.349 -14.422 58.254 29 SER 69.467 -12.507 57.201 30 GLN 71.358 -13.439 60.394 31 CYS 70.762 -17.083 61.392 32 THR 70.958 -20.013 58.951 33 ALA 67.905 -21.105 56.972 34 GLN 68.136 -24.332 58.970 35 GLU 68.121 -22.695 62.415 36 LEU 65.407 -20.148 61.618 37 VAL 62.934 -22.896 60.687 38 MET 63.509 -24.579 64.033 39 THR 62.575 -21.420 65.936 40 LEU 59.510 -21.156 63.712 41 ASN 58.587 -24.827 64.208 42 GLU 59.044 -24.505 67.957 43 LEU 56.737 -21.486 67.948 44 PHE 54.029 -22.679 65.508 45 ALA 53.751 -26.149 67.066 46 ARG 52.739 -24.704 70.425 47 PHE 50.443 -22.252 68.615 48 ASP 48.553 -25.084 66.891 49 LYS 48.206 -26.925 70.200 50 LEU 46.664 -23.959 72.009 51 ALA 44.268 -23.451 69.089 52 ALA 42.443 -26.758 69.521 53 GLU 42.051 -26.095 73.261 54 ASN 40.598 -22.613 72.760 55 HIS 38.220 -23.861 70.032 56 CYS 40.031 -21.898 67.303 57 LEU 40.470 -23.298 63.799 58 ARG 43.950 -22.650 62.360 59 ILE 43.849 -21.585 58.715 60 LYS 47.413 -21.286 57.344 61 ILE 50.940 -19.922 57.754 62 LEU 52.168 -17.238 55.355 63 GLY 55.822 -17.359 56.322 64 ASP 55.804 -15.587 59.674 65 CYS 52.092 -14.692 59.546 66 TYR 49.890 -17.028 61.570 67 TYR 46.097 -16.853 61.446 68 CYS 43.139 -18.738 62.868 69 VAL 39.423 -18.148 63.334 70 SER 36.749 -18.953 65.939 71 GLY 33.152 -19.803 65.120 72 LEU 33.968 -22.322 62.409 73 PRO 32.856 -24.611 61.088 74 GLU 30.111 -24.965 63.739 75 ALA 28.618 -21.760 65.143 76 ARG 29.453 -20.567 68.663 77 ALA 28.430 -17.568 70.852 78 ASP 31.648 -17.876 72.861 79 HIS 33.668 -17.045 69.704 80 ALA 34.975 -13.608 70.650 81 HIS 36.313 -14.762 74.042 82 CYS 38.098 -17.674 72.386 83 CYS 40.271 -15.486 70.129 84 VAL 41.053 -13.116 73.006 85 GLU 42.084 -16.059 75.176 86 MET 44.057 -17.378 72.186 87 GLY 46.265 -14.297 71.984 88 MET 46.660 -14.490 75.763 89 ASP 48.277 -17.920 75.406 90 MET 50.192 -16.948 72.241 91 ILE 51.912 -13.843 73.601 92 GLU 53.042 -15.902 76.580 93 ALA 54.281 -18.767 74.408 94 ILE 56.349 -16.357 72.307 95 SER 58.146 -15.269 75.480 96 LEU 59.045 -18.839 76.397 97 VAL 60.533 -19.550 72.965 98 ARG 62.445 -16.261 73.031 99 GLU 63.710 -17.259 76.497 100 MET 64.616 -20.887 75.813 101 THR 66.078 -20.082 72.377 102 GLY 67.654 -16.642 72.565 103 VAL 66.208 -15.450 69.246 104 ASN 64.446 -12.061 69.233 105 VAL 60.897 -13.164 68.356 106 ASN 58.161 -10.626 68.991 107 MET 54.661 -10.648 67.551 108 ARG 51.722 -8.282 67.027 109 VAL 48.184 -9.634 67.397 110 GLY 45.103 -8.432 65.535 111 ILE 41.412 -9.265 66.043 112 HIS 38.103 -8.299 64.386 113 SER 34.647 -9.928 64.109 114 GLY 32.112 -10.292 61.331 115 ARG 31.178 -12.433 58.318 116 VAL 33.536 -14.496 56.147 117 HIS 33.465 -16.773 53.123 118 CYS 35.503 -19.951 53.417 119 GLY 36.602 -22.955 51.398 120 VAL 39.166 -23.613 48.691 121 LEU 40.062 -22.340 45.214 122 GLY 41.525 -23.822 42.049 123 LEU 42.079 -27.445 41.086 124 ARG 45.517 -28.323 42.383 125 LYS 46.819 -28.175 45.968 126 TRP 43.774 -27.162 47.982 127 GLN 44.235 -25.305 51.286 128 PHE 41.264 -24.122 53.404 129 ASP 41.088 -20.320 53.529 130 VAL 38.859 -17.327 54.301 131 TRP 37.933 -14.153 52.392 132 SER 35.940 -10.947 53.095 133 ASN 36.375 -7.248 53.942 134 ASP 36.139 -8.269 57.576 135 VAL 39.157 -10.519 57.038 136 THR 41.062 -7.789 55.191 137 LEU 40.456 -5.545 58.189 138 ALA 41.610 -8.156 60.702 139 ASN 44.837 -8.351 58.696 140 HIS 45.188 -4.553 58.960 141 MET 44.640 -4.674 62.728 142 GLU 47.806 -6.780 62.912 143 ALA 49.731 -4.185 60.907 144 GLY 48.450 -1.436 63.171 145 GLY 48.971 -3.548 66.277 146 LYS 51.560 -3.311 69.032 147 ALA 54.377 -5.724 69.878 148 GLY 53.343 -8.126 72.630 149 ARG 49.824 -6.694 72.961 150 ILE 46.302 -7.558 71.760 151 HIS 44.802 -5.026 69.333 152 ILE 41.027 -5.275 68.759 153 THR 38.236 -3.383 66.985 154 LYS 34.970 -2.047 68.410 155 ALA 32.971 -4.796 66.706 156 THR 35.007 -7.412 68.630 157 LEU 34.519 -5.553 71.911 158 SER 30.728 -5.862 71.546 159 TYR 30.987 -9.648 71.601 160 LEU 33.156 -9.576 74.735 161 ASN 30.312 -8.635 77.105 162 GLY 32.727 -6.542 79.179 163 ASP 34.881 -9.284 80.670 164 TYR 38.351 -8.013 79.745 165 GLU 39.500 -4.503 80.567 166 VAL 40.509 -2.446 77.542 167 GLU 42.092 0.909 76.644 168 PRO 42.298 3.291 73.610 169 GLY 44.472 1.757 70.912 170 CYS 44.783 4.798 68.664 171 GLY 45.009 2.372 65.753 172 GLY 43.869 5.147 63.456 173 GLU 47.201 6.924 63.751 174 ARG 49.294 3.804 63.087 175 ASN 47.642 2.366 59.935 176 ALA 46.111 4.346 57.052 177 TYR 43.451 1.700 56.320 178 LEU 42.054 1.918 59.857 179 LYS 41.874 5.709 59.649 180 GLU 40.442 5.970 56.120 181 HIS 37.675 3.550 57.109 182 SER 36.782 5.200 60.443 183 ILE 37.787 2.398 62.843 184 GLU 37.906 2.514 66.654 185 THR 40.612 0.277 68.112 186 PHE 41.312 -0.960 71.661 187 LEU 44.095 -2.718 73.597 188 ILE 43.929 -5.512 76.184 189 LEU 45.402 -5.254 79.704 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S/S S S S S S 10 S S S/S S S S S S S S/S 20 S S S/H H H H H H H 3 30 3 H H H H H H H H H 40 H H H H H H H H H H 50 H H H H H/S S S S S S 60 T T T T/S S S S S S S 70 S/T T/P T T/S S S S H H H 80 H H H H H H H H H H 90 H H H H H H H H H H 100 H H S S S S S S S S 110 S S S S S/S S S S S S/S 120 S S S S S S S S S S 130 S S/H H H H H H H H H 140 H H H H H T T T T/S S 150 S S S/H H H H H H H H/T 160 T T T/S S S S S S C H 170 H H H H H/H H H H H H 180 H H/S S S S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S E E E E 10 E E E E E E E E E E 20 E e h H H H H h T T 30 t h H H H H H H H H 40 H H H H H H H H H H 50 H H H h T t E E E E 60 E E T T E E E E E E 70 S S S S h H H 80 H H H H H H H H H H 90 H H H H H H H H H H 100 H h e E E E E 110 E E E E E E E E E E 120 S S S S E E 130 E h H H H H H H H H 140 H H H h t t T T e E 150 E E E H H H H h T T 160 T T t S e E E E e g 170 G G G g h H H H H H 180 h T t e E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 48.9 30.7 79.2 2 MET 2.3 1.5 84.9 3 PHE 0.0 0.0 88.9 4 HIS 24.4 16.2 77.1 5 LYS 58.0 33.5 73.0 6 ILE 38.0 26.5 72.0 7 TYR 84.7 46.8 63.9 8 ILE 121.0 84.4 43.1 9 GLN 36.4 24.5 74.6 10 LYS 80.7 46.5 74.5 11 HIS 107.0 71.2 62.2 12 ASP 52.8 47.8 68.4 13 ASN 39.7 32.8 74.4 14 VAL 117.5 98.9 49.6 15 SER 83.6 100.0 48.6 16 ILE 143.5 100.0 35.4 17 LEU 147.8 100.0 34.5 18 PHE 157.7 94.6 41.7 19 ALA 72.1 99.4 37.8 20 ASP 88.8 80.4 65.8 21 ILE 141.6 98.7 37.6 22 GLU 72.4 52.2 70.3 23 GLY 2.8 8.0 76.2 24 PHE 126.2 75.6 48.6 25 THR 0.0 0.0 81.4 26 SER 22.2 26.6 75.7 27 LEU 121.7 82.4 59.1 28 ALA 46.6 64.2 60.7 29 SER 19.8 23.6 83.0 30 GLN 44.5 29.9 79.8 31 CYS 75.8 76.5 60.1 32 THR 28.8 26.9 75.7 33 ALA 3.6 4.9 72.7 34 GLN 6.0 4.0 79.0 35 GLU 57.4 41.4 63.3 36 LEU 125.5 84.9 40.5 37 VAL 29.6 24.9 74.0 38 MET 19.2 12.0 82.7 39 THR 98.7 92.3 38.2 40 LEU 119.1 80.6 43.3 41 ASN 18.9 15.7 77.6 42 GLU 78.0 56.3 66.8 43 LEU 147.6 99.9 29.1 44 PHE 154.4 92.6 36.5 45 ALA 29.4 40.5 80.3 46 ARG 135.5 64.9 54.7 47 PHE 166.8 100.0 26.8 48 ASP 65.7 59.5 70.1 49 LYS 38.0 21.9 81.5 50 LEU 113.8 77.0 57.4 51 ALA 69.7 96.0 58.8 52 ALA 8.5 11.7 86.5 53 GLU 45.4 32.8 77.1 54 ASN 99.4 82.2 60.6 55 HIS 63.0 42.0 83.8 56 CYS 99.2 100.0 43.7 57 LEU 82.6 55.9 62.6 58 ARG 135.8 65.0 62.3 59 ILE 143.3 99.9 39.7 60 LYS 120.8 69.6 65.2 61 ILE 105.4 73.5 56.4 62 LEU 60.0 40.6 66.4 63 GLY 1.3 3.8 72.3 64 ASP 92.3 83.6 47.5 65 CYS 86.5 87.2 59.0 66 TYR 181.0 100.0 32.5 67 TYR 170.7 94.3 37.7 68 CYS 99.2 100.0 34.8 69 VAL 118.8 100.0 31.1 70 SER 83.5 99.9 48.4 71 GLY 34.1 98.0 60.4 72 LEU 147.1 99.5 32.1 73 PRO 34.9 28.0 67.9 74 GLU 5.2 3.8 84.8 75 ALA 4.6 6.3 84.9 76 ARG 130.6 62.5 67.3 77 ALA 0.0 0.0 82.0 78 ASP 50.2 45.5 66.6 79 HIS 144.9 96.5 47.1 80 ALA 72.2 99.5 56.6 81 HIS 113.8 75.7 67.0 82 CYS 92.2 92.9 58.2 83 CYS 99.2 100.0 40.8 84 VAL 118.8 100.0 29.8 85 GLU 71.3 51.4 66.5 86 MET 159.4 100.0 37.4 87 GLY 34.8 100.0 39.0 88 MET 87.6 54.9 66.0 89 ASP 70.5 63.8 70.7 90 MET 159.0 99.8 22.4 91 ILE 103.4 72.1 54.2 92 GLU 26.1 18.8 80.5 93 ALA 66.1 91.1 42.3 94 ILE 136.6 95.2 42.0 95 SER 54.8 65.5 75.3 96 LEU 62.1 42.0 72.6 97 VAL 118.8 100.0 44.0 98 ARG 131.5 62.9 75.9 99 GLU 38.7 28.0 77.7 100 MET 67.5 42.3 80.9 101 THR 78.4 73.3 58.9 102 GLY 2.6 7.5 84.9 103 VAL 94.9 79.9 50.2 104 ASN 30.6 25.3 72.7 105 VAL 115.9 97.6 28.3 106 ASN 78.5 64.9 64.2 107 MET 159.4 100.0 35.1 108 ARG 161.8 77.4 68.2 109 VAL 118.6 99.8 38.1 110 GLY 34.8 100.0 56.7 111 ILE 143.5 100.0 38.8 112 HIS 137.8 91.7 48.7 113 SER 83.6 100.0 49.2 114 GLY 20.0 57.4 70.6 115 ARG 70.6 33.8 78.4 116 VAL 118.1 99.4 34.6 117 HIS 70.2 46.7 58.5 118 CYS 96.0 96.8 38.6 119 GLY 25.1 72.1 47.1 120 VAL 101.6 85.5 45.0 121 LEU 57.4 38.8 69.3 122 GLY 0.0 0.0 77.2 123 LEU 38.5 26.0 74.3 124 ARG 24.7 11.8 82.1 125 LYS 7.4 4.3 89.7 126 TRP 110.7 54.0 66.3 127 GLN 40.0 26.9 79.5 128 PHE 101.5 60.8 52.1 129 ASP 91.6 82.9 56.8 130 VAL 118.7 100.0 24.3 131 TRP 131.6 64.2 56.7 132 SER 59.0 70.5 64.3 133 ASN 1.1 0.9 88.9 134 ASP 76.6 69.3 61.4 135 VAL 105.8 89.1 45.8 136 THR 48.1 45.0 72.6 137 LEU 130.9 88.6 38.3 138 ALA 72.6 100.0 46.5 139 ASN 63.5 52.5 63.4 140 HIS 104.3 69.4 56.3 141 MET 159.4 100.0 41.6 142 GLU 126.4 91.2 59.2 143 ALA 40.2 55.4 85.1 144 GLY 34.8 99.9 57.7 145 GLY 34.7 99.8 61.2 146 LYS 77.4 44.6 70.6 147 ALA 43.9 60.5 68.5 148 GLY 14.4 41.3 66.9 149 ARG 132.6 63.5 63.0 150 ILE 141.6 98.6 35.9 151 HIS 150.2 100.0 48.5 152 ILE 143.5 100.0 31.3 153 THR 104.7 97.9 42.7 154 LYS 52.8 30.5 75.9 155 ALA 33.8 46.6 76.2 156 THR 106.9 100.0 47.2 157 LEU 108.6 73.4 44.4 158 SER 21.4 25.6 77.2 159 TYR 108.5 59.9 74.7 160 LEU 147.3 99.7 38.3 161 ASN 26.7 22.1 86.3 162 GLY 1.4 4.1 81.1 163 ASP 42.1 38.1 72.9 164 TYR 140.8 77.8 47.6 165 GLU 13.2 9.5 77.8 166 VAL 96.0 80.8 43.9 167 GLU 77.1 55.7 59.5 168 PRO 29.0 23.3 72.0 169 GLY 34.7 99.8 61.2 170 CYS 35.1 35.4 82.0 171 GLY 34.8 100.0 62.8 172 GLY 20.0 57.5 67.5 173 GLU 26.5 19.1 76.9 174 ARG 142.4 68.2 68.8 175 ASN 99.5 82.3 58.3 176 ALA 13.2 18.1 79.8 177 TYR 123.8 68.4 56.4 178 LEU 147.8 100.0 39.6 179 LYS 32.8 18.9 79.5 180 GLU 27.4 19.8 75.9 181 HIS 57.7 38.4 70.4 182 SER 3.1 3.7 87.7 183 ILE 109.7 76.4 50.0 184 GLU 41.1 29.6 70.7 185 THR 106.8 99.9 44.9 186 PHE 131.7 78.9 48.8 187 LEU 140.8 95.2 55.4 188 ILE 134.9 94.0 37.4 189 LEU 72.8 49.3 68.8