Protein Data Bank File : 1cjma Title : TRANSFERASE 18-APR-99 1CJM Number of Amino Acid Residues : 223 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER ARG PRO PRO LEU GLU TYR VAL LYS GLY 10 VAL PRO LEU ILE LYS TYR PHE ALA GLU ALA 20 LEU GLY PRO LEU GLN SER PHE GLN ALA ARG 30 PRO ASP ASP LEU LEU ILE ASN THR TYR PRO 40 LYS SER GLY THR THR TRP VAL SER GLN ILE 50 LEU ASP MET ILE TYR GLN ARG VAL PRO PHE 60 LEU GLU VAL ASN ASP PRO GLY GLU PRO GLU 70 THR LEU LYS ASP THR PRO PRO PRO ARG LEU 80 ILE LYS SER HIS LEU PRO LEU ALA LEU LEU 90 PRO GLN THR LEU LEU ASP GLN LYS VAL LYS 100 VAL VAL TYR VAL ALA ARG ASN PRO LYS ASP 110 VAL ALA VAL SER TYR TYR HIS PHE HIS ARG 120 MET GLU LYS ALA HIS PRO GLU PRO GLY THR 130 TRP ASP SER PHE LEU GLU LYS PHE MET ALA 140 GLY GLU VAL SER TYR GLY SER TRP TYR GLN 150 HIS VAL GLN GLU TRP TRP GLU LEU SER ARG 160 THR HIS PRO VAL LEU TYR LEU PHE TYR GLU 170 ASP MET LYS GLU ASN PRO LYS ARG GLU ILE 180 GLN LYS ILE LEU GLU PHE VAL GLY ARG SER 190 LEU GLY ASP TRP LYS THR THR PHE THR VAL 200 ALA GLN ASN GLU ARG PHE ASP ALA ASP TYR 210 ALA GLU LYS MET ALA GLY CYS SER LEU SER 220 PHE ARG SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 17.2 -177.2 0.0 2 ARG 60.0 62.8 179.9 -69.1 -141.9 -176.6 -107.6 3 PRO -69.5 155.4 179.7 -19.8 36.8 4 PRO -69.7 169.8 179.0 -26.0 40.8 5 LEU -83.5 133.5 178.0 -63.5 166.7 6 GLU -103.6 127.6 -180.0 0.0 0.0 0.0 7 TYR -88.7 138.0 178.9 -72.4 69.5 8 VAL -133.4 110.6 -178.4 173.1 9 LYS 64.7 32.1 179.8 -75.0 -168.1 65.9 -174.9 10 GLY 84.1 -5.3 -179.8 11 VAL -102.7 125.5 179.9 -179.2 12 PRO -73.9 141.9 -180.0 32.0 -43.5 13 LEU -153.8 164.7 177.5 -72.2 166.2 14 ILE -80.1 149.7 -178.6 62.3 171.5 15 LYS -39.9 -51.9 -178.9 0.0 0.0 0.0 0.0 16 TYR -57.0 -37.0 179.8 0.0 0.0 17 PHE -75.2 -34.3 179.6 -65.1 -21.7 18 ALA -63.4 -43.0 179.3 19 GLU -59.1 -54.4 -179.7 -63.0 176.5 -2.2 20 ALA -60.9 -16.7 179.5 21 LEU -78.1 -11.3 179.8 0.0 0.0 22 GLY -73.0 -46.6 179.6 23 PRO -86.0 9.4 -178.6 -18.2 37.6 24 LEU -73.3 -28.3 -179.9 0.0 0.0 25 GLN -75.6 12.0 179.8 0.0 0.0 0.0 26 SER -114.9 10.5 179.7 -45.6 27 PHE -90.1 141.8 179.4 168.4 69.3 28 GLN -121.7 119.7 -179.2 -60.7 179.2 -0.3 29 ALA -88.2 134.7 178.2 30 ARG -86.7 151.7 180.0 -53.7 -159.8 -140.5 -69.3 31 PRO -61.2 -25.2 -179.1 -28.8 43.5 32 ASP -96.6 5.4 179.0 65.1 -29.7 33 ASP -63.6 169.0 177.6 -81.9 -13.6 34 LEU -145.8 127.3 -179.5 -176.1 106.9 35 LEU -113.5 131.3 178.0 174.5 71.6 36 ILE -106.4 114.3 -178.7 -60.3 156.8 37 ASN -130.3 130.8 178.1 -170.7 -64.1 38 THR -154.3 154.7 177.9 84.2 39 TYR -67.0 156.7 179.6 -173.7 84.1 40 PRO -49.0 143.8 -180.0 -38.2 43.2 41 LYS 58.1 36.4 -179.3 -68.0 -68.6 175.6 179.7 42 SER -125.3 19.3 177.7 -51.2 43 GLY 102.5 17.1 179.6 44 THR -63.0 -56.3 -179.9 -70.7 45 THR -61.7 -32.0 179.5 52.5 46 TRP -66.2 -60.7 -180.0 -167.6 -21.8 47 VAL -58.4 -43.3 179.7 178.6 48 SER -58.7 -40.7 179.7 66.4 49 GLN -63.0 -39.7 179.7 0.0 0.0 0.0 50 ILE -67.5 -55.7 179.7 -61.3 174.7 51 LEU -59.7 -26.1 179.2 -81.3 166.9 52 ASP -67.7 -34.0 179.9 -169.8 41.0 53 MET -79.0 -37.0 179.6 -66.5 -178.5 -173.1 54 ILE -60.0 -51.4 -179.9 -53.1 177.6 55 TYR -58.6 -33.6 178.8 -81.1 41.3 56 GLN -88.6 -108.2 124.8 0.0 0.0 0.0 57 ARG -67.7 112.8 178.4 0.0 0.0 0.0 0.0 58 VAL -102.9 94.4 -179.6 -170.2 59 PRO -74.2 145.8 177.4 -13.3 34.4 60 PHE -78.8 133.2 -178.8 -112.1 -64.5 61 LEU -67.2 -29.3 -177.6 -173.2 56.4 62 GLU -110.6 15.7 -179.8 61.6 -88.1 59.9 63 VAL -105.7 156.3 178.7 174.6 64 ASN -150.7 107.5 178.9 0.0 0.0 65 ASP -85.7 101.3 -179.8 0.0 0.0 66 PRO -50.4 131.7 -179.1 -30.9 44.8 67 GLY 90.5 -5.2 -179.3 68 GLU -134.4 119.0 178.9 -117.6 84.5 -79.1 69 PRO 27.8 -152.0 -64.1 0.0 0.0 70 GLU 99.7 -63.9 179.2 0.0 0.0 0.0 71 THR -85.3 -22.1 179.3 19.8 72 LEU -72.9 -39.3 178.7 0.0 0.0 73 LYS -60.2 -33.0 179.6 0.0 0.0 0.0 0.0 74 ASP -89.3 11.0 -178.6 0.0 0.0 75 THR -100.1 142.3 180.0 -64.7 76 PRO -72.2 133.5 179.5 -20.9 38.9 77 PRO -68.2 151.8 -0.3 -29.8 44.0 78 PRO -81.0 136.2 -178.9 35.1 -44.4 79 ARG -89.6 145.8 177.9 -56.9 -177.1 -58.2 -177.2 80 LEU -110.5 124.2 -179.7 -82.5 177.6 81 ILE -126.6 133.6 178.7 -49.2 173.1 82 LYS -120.0 147.7 -179.1 65.5 175.8 179.8 176.7 83 SER -162.7 160.0 178.1 -173.9 84 HIS -114.0 -3.4 -179.0 -71.7 -45.2 85 LEU -55.9 134.3 179.4 -76.2 -179.3 86 PRO -72.1 163.3 -179.8 30.1 -43.2 87 LEU -57.0 -31.7 -179.7 -169.2 59.2 88 ALA -65.4 -28.5 -179.3 89 LEU -110.9 5.5 -179.0 -60.0 -179.6 90 LEU -75.6 135.9 179.7 -165.9 77.2 91 PRO -51.8 124.6 -178.5 -35.7 45.0 92 GLN -54.4 -34.8 179.9 -167.4 58.4 -142.7 93 THR -57.5 -32.6 179.4 142.8 94 LEU -64.9 -40.7 179.6 -70.3 162.1 95 LEU -76.8 -33.5 -179.7 -62.5 175.4 96 ASP -63.8 -57.0 -179.7 0.0 0.0 97 GLN -72.6 12.9 179.7 -74.0 -59.0 -82.6 98 LYS 42.7 46.3 -179.6 -76.2 -82.6 -172.4 -65.8 99 VAL -67.3 143.5 179.8 -52.8 100 LYS -68.7 132.6 -180.0 -70.8 174.2 -62.9 -176.1 101 VAL -124.3 136.8 177.0 -175.3 102 VAL -109.1 105.7 -179.3 170.0 103 TYR -107.5 142.4 179.3 -173.7 83.5 104 VAL -127.4 126.1 179.1 -176.7 105 ALA -107.9 130.9 -179.6 106 ARG -113.4 162.2 178.9 -162.3 -167.5 -167.4 -179.0 107 ASN -58.7 130.1 -179.6 174.3 -90.3 108 PRO -51.2 -49.0 -178.7 -24.3 38.2 109 LYS -61.9 -39.4 178.6 -58.2 164.3 -179.2 176.2 110 ASP -70.7 -35.8 179.5 -81.1 -48.3 111 VAL -67.0 -42.3 -179.9 173.3 112 ALA -60.2 -47.2 -180.0 113 VAL -63.2 -45.8 179.4 -176.9 114 SER -67.3 -42.5 179.9 -82.6 115 TYR -65.1 -32.2 178.7 -148.1 16.2 116 TYR -63.6 -53.8 179.9 175.6 52.7 117 HIS -60.8 -33.6 179.0 -63.4 135.1 118 PHE -67.1 -38.3 179.0 178.1 67.3 119 HIS -63.5 -33.8 179.5 -88.9 71.2 120 ARG -71.5 -40.9 179.9 -73.6 173.2 69.3 113.1 121 MET -75.1 -43.0 -179.2 167.2 -169.4 -141.4 122 GLU -83.2 97.3 -178.0 -131.6 -58.7 -56.3 123 LYS -71.0 3.8 178.5 -59.4 -164.5 -58.1 176.7 124 ALA -99.7 -10.9 178.5 125 HIS -83.3 158.7 179.8 -86.9 67.8 126 PRO -65.6 156.6 179.7 29.0 -42.7 127 GLU -61.7 116.1 -179.9 172.4 68.4 28.0 128 PRO -73.1 -24.0 -179.7 33.6 -43.9 129 GLY 69.2 -142.6 179.9 130 THR -79.5 161.5 179.4 70.5 131 TRP -58.4 -36.7 179.9 161.7 -118.2 132 ASP -69.6 -38.7 179.0 -169.6 67.0 133 SER -64.0 -46.1 179.8 -67.1 134 PHE -64.0 -53.3 179.9 -178.9 81.9 135 LEU -50.3 -34.6 179.9 175.9 62.2 136 GLU -67.1 -40.2 178.9 -145.8 59.6 46.1 137 LYS -68.8 -45.4 179.7 -69.6 -179.5 -178.2 -57.8 138 PHE -53.7 -47.7 179.5 -176.1 -87.9 139 MET -64.3 -33.0 179.8 -70.7 175.4 82.6 140 ALA -88.4 5.2 -179.7 141 GLY 60.6 17.5 -179.5 142 GLU -86.3 51.2 179.8 -160.0 169.0 -25.9 143 VAL -136.1 165.6 -179.9 -65.9 144 SER -57.0 124.9 -178.9 -154.9 145 TYR 90.0 0.7 178.1 -74.2 -77.4 146 GLY 73.5 -164.5 -179.7 147 SER -57.4 129.6 178.3 164.6 148 TRP -68.2 -39.4 -179.1 168.3 90.0 149 TYR -57.6 -50.6 179.3 -52.3 -88.0 150 GLN -66.1 -50.2 -180.0 -82.4 -164.6 -4.4 151 HIS -50.6 -48.1 -179.2 -162.9 -62.6 152 VAL -72.3 -38.1 -179.5 133.3 153 GLN -75.6 -42.5 -179.4 -65.9 173.4 -55.3 154 GLU -61.4 -42.5 179.2 -65.7 -172.1 -14.3 155 TRP -70.2 -21.4 178.7 -79.8 100.2 156 TRP -75.0 -44.5 179.0 175.6 -115.8 157 GLU -68.4 -39.3 179.6 -84.1 -21.5 -65.8 158 LEU -62.4 -35.5 -179.4 -175.6 74.8 159 SER -62.7 -15.9 178.5 72.5 160 ARG -80.4 -21.2 -178.0 -101.7 79.2 178.3 93.8 161 THR -132.4 23.0 -177.1 56.7 162 HIS -157.4 150.4 179.9 -169.6 89.1 163 PRO -70.3 80.6 -180.0 30.1 -44.1 164 VAL -121.7 129.1 178.5 -178.8 165 LEU -94.9 95.0 -178.9 -148.2 -150.3 166 TYR -80.3 105.0 -179.8 -152.9 -81.7 167 LEU -106.7 164.9 179.2 -55.8 -178.9 168 PHE -121.9 130.8 -179.2 -65.5 -85.2 169 TYR -52.1 -43.3 -179.6 -166.4 -91.3 170 GLU -54.5 -43.2 -179.3 -60.7 75.6 66.0 171 ASP -67.5 -23.0 178.9 -57.7 -34.0 172 MET -79.6 -27.7 178.7 -67.4 175.6 62.0 173 LYS -79.2 -53.6 -178.7 -81.8 -72.2 -175.1 -172.2 174 GLU -67.8 -27.4 179.6 -62.4 166.3 21.9 175 ASN -158.7 83.3 180.0 -170.2 7.3 176 PRO -61.7 -40.1 -178.8 -29.0 43.5 177 LYS -51.2 -66.2 -178.4 0.0 0.0 0.0 0.0 178 ARG -58.2 -28.4 179.5 98.9 100.9 34.7 -136.4 179 GLU -74.6 -37.4 178.7 -66.3 -62.5 -71.9 180 ILE -67.8 -28.6 179.2 -70.0 -179.2 181 GLN -69.1 -46.6 179.2 -159.9 58.6 47.2 182 LYS -55.9 -46.0 179.9 -69.2 -179.5 174.8 174.7 183 ILE -61.4 -42.5 179.2 -63.5 179.2 184 LEU -64.3 -45.8 179.9 -75.4 168.8 185 GLU -68.9 -19.7 179.8 -61.9 175.5 -24.9 186 PHE -81.9 -50.8 179.8 179.0 55.0 187 VAL -75.8 -14.5 178.9 -64.8 188 GLY 83.4 24.1 179.9 189 ARG -117.5 170.0 -178.4 -56.5 171.6 -166.4 -123.1 190 SER -129.6 155.0 -179.4 -169.2 191 LEU -115.9 -113.4 -99.4 -119.7 26.6 192 GLY 7.1 34.4 178.1 193 ASP -79.5 -18.5 179.8 -70.1 81.4 194 TRP -71.8 -24.5 -179.3 56.3 -92.7 195 LYS -56.1 -28.7 -179.8 -66.5 -179.1 176.5 179.6 196 THR -82.4 -0.1 -179.4 67.9 197 THR -116.5 -44.2 180.0 -56.6 198 PHE -72.9 129.0 177.2 -89.3 74.8 199 THR -84.4 160.9 -179.6 64.0 200 VAL -62.4 -30.1 178.9 -175.8 201 ALA -68.8 -49.5 179.9 202 GLN -61.9 -41.3 -179.4 -69.7 170.9 -5.7 203 ASN -65.7 -39.3 179.7 -168.7 71.8 204 GLU -70.1 -39.6 179.0 -67.7 -175.9 -13.4 205 ARG -67.1 -34.3 179.8 169.1 163.3 175.0 55.8 206 PHE -70.9 -49.0 -179.5 -175.2 -77.7 207 ASP -60.5 -36.0 179.6 -74.1 35.6 208 ALA -70.6 -43.6 179.2 209 ASP -67.1 -38.2 179.4 170.6 85.2 210 TYR -68.2 -42.6 -179.1 174.7 -80.4 211 ALA -55.7 -35.7 -179.4 212 GLU -85.7 -38.7 179.1 55.8 -172.4 -9.2 213 LYS -68.7 -34.1 179.6 -69.8 -176.0 177.9 177.2 214 MET -87.5 5.5 178.8 -74.5 -70.9 -143.7 215 ALA -63.8 123.9 -179.0 216 GLY 72.8 68.6 179.7 217 CYS -172.5 105.9 -178.4 -179.1 218 SER -52.4 -4.9 179.2 45.8 219 LEU -57.8 138.1 -179.3 -88.5 176.6 220 SER -147.8 121.8 -179.4 -172.2 221 PHE -109.8 65.2 -179.8 -62.0 73.9 222 ARG -43.1 141.1 -176.8 0.0 0.0 0.0 0.0 223 SER -104.9 -173.4 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER -29.845 47.932 41.079 2 ARG -28.863 44.470 42.304 3 PRO -30.225 42.471 39.306 4 PRO -30.821 38.703 39.370 5 LEU -28.408 36.135 37.954 6 GLU -28.783 35.288 34.252 7 TYR -27.865 31.720 33.299 8 VAL -25.812 30.990 30.169 9 LYS -25.325 27.280 29.358 10 GLY -26.533 26.422 32.855 11 VAL -23.881 28.635 34.481 12 PRO -25.003 31.699 36.487 13 LEU -23.464 35.102 35.750 14 ILE -24.421 38.724 36.235 15 LYS -26.467 40.287 33.399 16 TYR -23.575 42.396 32.045 17 PHE -21.253 39.389 31.607 18 ALA -23.984 37.326 29.917 19 GLU -24.517 40.014 27.256 20 ALA -20.796 40.218 26.457 21 LEU -20.802 36.400 26.216 22 GLY -22.900 36.732 23.057 23 PRO -20.236 38.236 20.701 24 LEU -17.640 35.894 22.252 25 GLN -18.103 33.169 19.611 26 SER -16.544 35.595 17.086 27 PHE -13.133 35.548 18.796 28 GLN -10.190 33.838 17.097 29 ALA -7.352 32.616 19.309 30 ARG -3.776 32.784 18.094 31 PRO -1.445 29.844 18.864 32 ASP 0.813 32.215 20.865 33 ASP -1.961 33.734 23.004 34 LEU -1.923 33.354 26.758 35 LEU -4.930 33.090 29.007 36 ILE -4.940 33.799 32.725 37 ASN -7.959 32.065 34.223 38 THR -9.055 31.751 37.856 39 TYR -12.399 31.673 39.680 40 PRO -13.400 35.097 41.037 41 LYS -11.135 36.297 43.886 42 SER -8.536 33.623 43.084 43 GLY -5.526 35.539 41.779 44 THR -6.433 36.700 38.259 45 THR -5.293 40.298 38.774 46 TRP -2.219 39.070 40.680 47 VAL -0.973 36.681 37.965 48 SER -2.015 39.056 35.158 49 GLN 0.044 41.844 36.749 50 ILE 3.123 39.586 36.853 51 LEU 2.793 38.283 33.286 52 ASP 2.117 41.890 32.237 53 MET 5.609 42.787 33.484 54 ILE 7.347 39.760 31.945 55 TYR 6.081 40.603 28.433 56 GLN 7.277 44.221 28.831 57 ARG -2.958 45.759 28.412 58 VAL -4.461 42.573 29.834 59 PRO -8.123 42.802 28.691 60 PHE -10.906 40.865 30.366 61 LEU -12.285 38.282 27.952 62 GLU -15.917 38.735 29.109 63 VAL -16.108 42.490 29.737 64 ASN -17.493 45.334 27.622 65 ASP -17.150 48.893 28.918 66 PRO -20.148 50.596 27.232 67 GLY -19.011 53.674 25.364 68 GLU -15.479 52.262 25.089 69 PRO -13.927 50.176 22.264 70 GLU -12.769 43.867 20.183 71 THR -9.557 45.671 21.211 72 LEU -7.695 42.366 21.652 73 LYS -8.337 41.421 18.007 74 ASP -6.638 44.754 17.239 75 THR -3.730 43.880 19.584 76 PRO -0.138 42.858 18.592 77 PRO 0.993 39.282 19.399 78 PRO 1.773 37.744 21.781 79 ARG -1.549 38.599 23.438 80 LEU -2.385 38.389 27.141 81 ILE -5.996 37.529 27.942 82 LYS -7.571 37.283 31.394 83 SER -10.912 35.778 32.389 84 HIS -12.936 34.218 35.232 85 LEU -15.062 32.246 32.755 86 PRO -15.535 28.547 33.497 87 LEU -14.428 25.915 30.975 88 ALA -18.100 25.476 30.041 89 LEU -18.346 29.086 28.802 90 LEU -14.790 29.492 27.526 91 PRO -14.411 30.373 23.801 92 GLN -13.825 27.131 21.856 93 THR -11.053 28.687 19.754 94 LEU -8.878 28.895 22.908 95 LEU -9.079 25.121 23.443 96 ASP -8.699 24.417 19.708 97 GLN -5.445 26.337 19.201 98 LYS -4.122 24.680 22.395 99 VAL -3.271 28.097 23.883 100 LYS -1.201 28.150 27.089 101 VAL -3.250 28.864 30.226 102 VAL -2.142 29.976 33.699 103 TYR -4.857 28.866 36.131 104 VAL -4.893 29.575 39.875 105 ALA -6.954 27.680 42.460 106 ARG -7.539 29.244 45.892 107 ASN -8.855 27.812 49.180 108 PRO -12.679 27.501 48.919 109 LYS -13.258 29.099 52.330 110 ASP -11.084 32.161 51.617 111 VAL -12.760 32.676 48.219 112 ALA -16.251 32.512 49.772 113 VAL -15.382 35.141 52.391 114 SER -13.723 37.465 49.828 115 TYR -16.476 36.978 47.238 116 TYR -19.009 37.804 49.975 117 HIS -17.376 41.162 50.785 118 PHE -17.042 41.832 47.052 119 HIS -20.792 41.282 46.641 120 ARG -21.412 43.934 49.323 121 MET -19.122 46.524 47.673 122 GLU -20.155 45.753 44.089 123 LYS -23.727 47.060 43.807 124 ALA -24.288 45.504 40.365 125 HIS -24.005 41.979 41.825 126 PRO -27.063 40.244 43.298 127 GLU -27.872 40.859 46.984 128 PRO -25.622 38.491 49.001 129 GLY -27.726 38.875 52.139 130 THR -26.300 37.421 55.358 131 TRP -23.006 35.521 55.476 132 ASP -24.999 32.346 56.126 133 SER -27.327 33.033 53.162 134 PHE -24.356 33.642 50.868 135 LEU -22.267 30.664 52.045 136 GLU -25.303 28.526 51.210 137 LYS -25.374 29.870 47.619 138 PHE -21.605 29.489 47.155 139 MET -21.868 25.819 48.133 140 ALA -24.836 25.466 45.759 141 GLY -22.848 27.224 43.037 142 GLU -25.693 29.739 42.841 143 VAL -23.273 32.647 42.333 144 SER -21.769 34.616 39.433 145 TYR -19.478 32.275 37.419 146 GLY -21.097 29.235 38.975 147 SER -19.750 26.475 41.207 148 TRP -16.210 26.914 42.513 149 TYR -16.002 23.125 42.709 150 GLN -16.736 22.596 38.993 151 HIS -14.680 25.607 37.891 152 VAL -11.699 24.313 39.887 153 GLN -12.096 20.594 39.018 154 GLU -12.732 20.959 35.272 155 TRP -9.602 23.045 34.735 156 TRP -7.708 20.421 36.755 157 GLU -8.820 17.614 34.438 158 LEU -8.209 19.767 31.369 159 SER -4.630 20.368 32.577 160 ARG -4.015 16.628 32.063 161 THR -4.707 16.973 28.314 162 HIS -4.015 20.644 27.560 163 PRO -1.175 23.184 28.125 164 VAL -2.423 24.530 31.484 165 LEU -0.157 25.681 34.334 166 TYR -2.259 24.734 37.369 167 LEU -1.138 26.949 40.280 168 PHE -2.396 27.405 43.863 169 TYR -3.024 30.829 45.465 170 GLU -1.513 29.728 48.807 171 ASP 1.834 29.003 47.120 172 MET 1.915 32.507 45.599 173 LYS 1.530 34.048 49.084 174 GLU 3.971 31.726 50.881 175 ASN 6.589 31.789 48.079 176 PRO 6.134 34.293 45.202 177 LYS 9.636 33.608 43.835 178 ARG 9.386 29.917 42.883 179 GLU 5.876 30.465 41.449 180 ILE 7.044 33.292 39.164 181 GLN 9.741 30.877 37.976 182 LYS 7.123 28.253 37.058 183 ILE 5.241 30.933 35.110 184 LEU 8.460 32.024 33.343 185 GLU 9.417 28.449 32.434 186 PHE 5.865 27.909 31.154 187 VAL 5.608 30.919 28.830 188 GLY 9.250 30.396 27.887 189 ARG 10.655 33.768 29.015 190 SER 13.262 34.864 31.619 191 LEU 13.613 37.559 34.325 192 GLY -6.793 30.923 57.596 193 ASP -8.238 34.469 57.423 194 TRP -11.616 32.785 56.837 195 LYS -11.539 31.249 60.339 196 THR -12.698 34.553 61.852 197 THR -15.804 34.371 59.647 198 PHE -16.776 30.681 59.471 199 THR -18.694 29.338 62.466 200 VAL -17.932 25.758 63.549 201 ALA -21.403 24.782 62.319 202 GLN -20.800 26.366 58.895 203 ASN -17.312 24.887 58.691 204 GLU -18.473 21.337 59.465 205 ARG -21.326 21.569 56.940 206 PHE -18.840 22.893 54.373 207 ASP -16.214 20.196 54.994 208 ALA -18.819 17.414 54.709 209 ASP -20.212 18.882 51.481 210 TYR -16.668 19.414 50.195 211 ALA -15.644 15.846 51.083 212 GLU -18.311 14.422 48.754 213 LYS -18.138 16.820 45.768 214 MET -14.358 16.442 45.691 215 ALA -14.701 12.646 45.915 216 GLY -12.589 11.265 43.097 217 CYS -10.442 14.283 42.213 218 SER -6.671 14.380 42.839 219 LEU -6.885 18.056 43.906 220 SER -5.244 18.794 47.274 221 PHE -5.008 22.150 49.085 222 ARG -2.497 21.394 51.924 223 SER -2.766 23.794 54.915 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S C T T T T/S 10 S S S S/H H H H H H H 20 H H T T T T/S S S S S 30 S S S S S S S S S C 40 C C H H H H H H H H 50 H H H H H H/X X/S S S S 60 S S S S S/T T T T C/X X/H 70 H H H H H C C/P S S S 80 S S S S C T T T T C 90 H H H H 3 3 C S S S 100 S S/S S S S S S/H H H H 110 H H H H H H H H H H 120 H H C S S S S C C H 130 H H H H H H H H H H 140 H C T T T T H H H H 150 H H H H H H H H H H 160 3 S S S S/S S S S/H H H 170 H H H H H H H H H H 180 H H H H H H H H/S S S 190 S/X X/T T T T/T T T T H H 200 H H H H H H H H H H 210 H H H H H C C S S S 220 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 10 E E E E H H H H H H 20 h g G G G G g t 30 T T e E E E E E e T 40 T t h H H H H H H H 50 H H H H H h B 60 T T t t T T t t 70 T T T T t S S e E 80 E E E g G G G g 90 h H H H H H h T t E 100 E E E E E h H H H 110 H H H H H H H H H H 120 H h T T t h 130 H H H H H H H H H h 140 T t t T T t h H H H 150 H H H H H H H H h T 160 T t e E E E E E H H 170 H H H H h H H H H H 180 H H H H H H H h t 190 g G G G g t h H 200 H H H H H H H H H H 210 H H H h t S 220 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 0.0 0.0 85.4 2 ARG 168.5 80.7 58.7 3 PRO 77.7 62.4 64.2 4 PRO 15.7 12.6 79.8 5 LEU 130.6 88.4 48.3 6 GLU 100.2 72.3 67.0 7 TYR 87.5 48.4 65.8 8 VAL 77.6 65.3 53.5 9 LYS 43.9 25.3 77.2 10 GLY 1.2 3.6 70.3 11 VAL 100.7 84.8 44.8 12 PRO 117.1 94.0 48.4 13 LEU 147.7 99.9 35.8 14 ILE 129.3 90.1 44.9 15 LYS 132.9 76.7 67.2 16 TYR 127.6 70.5 68.6 17 PHE 130.4 78.2 51.2 18 ALA 61.7 84.9 49.0 19 GLU 16.4 11.8 84.1 20 ALA 61.9 85.2 60.6 21 LEU 137.7 93.1 49.9 22 GLY 0.9 2.5 77.8 23 PRO 39.6 31.8 83.0 24 LEU 126.0 85.3 65.0 25 GLN 77.3 52.0 86.9 26 SER 13.5 16.1 83.2 27 PHE 139.6 83.7 50.3 28 GLN 4.4 3.0 84.7 29 ALA 72.6 100.0 51.1 30 ARG 138.0 66.0 69.8 31 PRO 43.7 35.1 80.0 32 ASP 54.3 49.1 59.7 33 ASP 110.5 100.0 50.5 34 LEU 147.7 100.0 39.5 35 LEU 147.8 100.0 29.9 36 ILE 143.5 100.0 36.4 37 ASN 120.9 100.0 41.1 38 THR 106.9 100.0 58.0 39 TYR 180.2 99.5 42.0 40 PRO 117.7 94.6 39.4 41 LYS 91.6 52.8 64.3 42 SER 83.3 99.6 54.7 43 GLY 31.0 89.2 49.0 44 THR 105.5 98.7 50.3 45 THR 21.8 20.4 80.9 46 TRP 129.8 63.3 54.0 47 VAL 118.8 100.0 28.0 48 SER 78.2 93.6 43.8 49 GLN 101.9 68.6 75.0 50 ILE 119.3 83.2 40.0 51 LEU 147.8 100.0 23.9 52 ASP 57.1 51.6 66.3 53 MET 22.9 14.3 82.8 54 ILE 142.4 99.2 33.2 55 TYR 160.3 88.6 52.7 56 GLN 85.6 57.6 82.7 57 ARG 135.5 64.9 85.3 58 VAL 111.1 93.5 48.3 59 PRO 84.7 68.0 68.2 60 PHE 124.5 74.7 56.2 61 LEU 130.2 88.1 39.2 62 GLU 136.1 98.2 43.5 63 VAL 64.7 54.5 56.2 64 ASN 67.0 55.4 70.2 65 ASP 58.9 53.3 63.7 66 PRO 13.3 10.7 85.7 67 GLY 0.0 0.0 84.0 68 GLU 21.1 15.2 82.6 69 PRO 74.0 59.4 68.4 70 GLU 81.8 59.0 86.2 71 THR 34.5 32.3 64.1 72 LEU 131.8 89.2 54.5 73 LYS 121.9 70.3 85.3 74 ASP 51.0 46.1 81.0 75 THR 68.0 63.6 60.3 76 PRO 27.0 21.7 74.3 77 PRO 70.9 56.9 69.8 78 PRO 83.8 67.3 74.0 79 ARG 204.0 97.7 50.5 80 LEU 139.1 94.1 43.3 81 ILE 140.5 97.9 38.6 82 LYS 141.9 81.8 43.8 83 SER 83.6 100.0 42.7 84 HIS 123.0 81.9 54.8 85 LEU 144.1 97.5 36.1 86 PRO 117.2 94.1 44.6 87 LEU 120.3 81.4 43.8 88 ALA 37.0 50.9 65.2 89 LEU 139.2 94.2 35.6 90 LEU 147.5 99.8 36.1 91 PRO 114.3 91.8 39.3 92 GLN 26.9 18.1 77.2 93 THR 76.7 71.8 55.5 94 LEU 147.3 99.7 26.8 95 LEU 118.7 80.3 57.9 96 ASP 61.5 55.7 77.2 97 GLN 73.3 49.3 68.2 98 LYS 66.5 38.3 80.0 99 VAL 118.5 99.7 52.5 100 LYS 115.0 66.3 61.8 101 VAL 118.0 99.3 36.7 102 VAL 118.8 100.0 26.9 103 TYR 181.0 100.0 40.9 104 VAL 118.8 100.0 39.3 105 ALA 72.2 99.5 40.6 106 ARG 171.5 82.1 55.8 107 ASN 90.5 74.9 50.5 108 PRO 119.2 95.7 34.5 109 LYS 147.4 85.0 49.0 110 ASP 86.8 78.6 63.0 111 VAL 118.8 100.0 49.0 112 ALA 72.6 100.0 32.2 113 VAL 103.8 87.3 50.1 114 SER 55.0 65.8 70.8 115 TYR 178.7 98.7 34.9 116 TYR 166.3 91.9 47.0 117 HIS 55.8 37.2 65.5 118 PHE 111.5 66.8 54.5 119 HIS 147.6 98.2 35.2 120 ARG 72.7 34.8 76.2 121 MET 10.8 6.8 84.2 122 GLU 81.8 59.0 59.3 123 LYS 23.3 13.5 90.6 124 ALA 27.0 37.2 77.7 125 HIS 141.9 94.5 43.6 126 PRO 100.9 81.0 51.5 127 GLU 42.2 30.4 70.6 128 PRO 119.7 96.2 49.3 129 GLY 12.9 37.2 67.5 130 THR 21.2 19.8 81.1 131 TRP 178.0 86.8 41.8 132 ASP 36.9 33.4 77.5 133 SER 34.8 41.6 75.5 134 PHE 165.5 99.2 35.3 135 LEU 144.0 97.4 36.3 136 GLU 73.6 53.1 76.6 137 LYS 98.4 56.8 70.3 138 PHE 166.7 99.9 32.4 139 MET 152.5 95.7 56.5 140 ALA 25.6 35.3 81.2 141 GLY 32.6 93.6 65.4 142 GLU 65.1 47.0 68.4 143 VAL 116.1 97.7 47.1 144 SER 83.6 100.0 42.2 145 TYR 175.1 96.7 36.1 146 GLY 31.9 91.5 62.0 147 SER 63.9 76.4 58.5 148 TRP 204.8 99.9 26.6 149 TYR 177.1 97.8 41.7 150 GLN 38.5 25.9 79.7 151 HIS 149.5 99.5 54.6 152 VAL 118.4 99.7 43.4 153 GLN 114.8 77.3 48.3 154 GLU 79.9 57.6 60.3 155 TRP 205.0 100.0 33.1 156 TRP 171.6 83.7 59.2 157 GLU 48.5 35.0 74.3 158 LEU 119.0 80.5 46.3 159 SER 78.6 94.1 56.5 160 ARG 88.8 42.5 79.9 161 THR 15.5 14.5 80.8 162 HIS 144.7 96.4 44.7 163 PRO 81.1 65.2 52.2 164 VAL 118.8 100.0 39.1 165 LEU 118.3 80.0 41.7 166 TYR 174.7 96.5 36.1 167 LEU 144.9 98.0 38.8 168 PHE 127.5 76.5 59.8 169 TYR 152.2 84.1 49.4 170 GLU 100.0 72.1 55.0 171 ASP 57.0 51.6 70.0 172 MET 156.0 97.9 35.9 173 LYS 67.4 38.9 69.1 174 GLU 25.8 18.6 77.3 175 ASN 54.1 44.7 63.7 176 PRO 59.5 47.8 72.5 177 LYS 107.4 61.9 80.8 178 ARG 87.8 42.0 72.9 179 GLU 134.7 97.2 46.8 180 ILE 98.5 68.6 44.1 181 GLN 61.5 41.4 70.3 182 LYS 105.2 60.7 68.1 183 ILE 142.9 99.6 25.7 184 LEU 143.3 97.0 46.2 185 GLU 37.7 27.2 78.7 186 PHE 131.6 78.9 51.0 187 VAL 118.7 99.9 40.8 188 GLY 4.6 13.3 78.6 189 ARG 128.6 61.5 58.6 190 SER 10.6 12.7 78.1 191 LEU 70.8 47.9 55.5 192 GLY 23.8 68.5 72.6 193 ASP 0.0 0.0 89.2 194 TRP 174.0 84.9 51.5 195 LYS 50.5 29.1 69.8 196 THR 10.0 9.4 88.1 197 THR 77.1 72.2 57.2 198 PHE 166.1 99.6 37.4 199 THR 38.3 35.8 78.2 200 VAL 8.0 6.7 82.9 201 ALA 4.7 6.5 83.1 202 GLN 125.9 84.7 52.7 203 ASN 84.9 70.2 53.6 204 GLU 33.2 24.0 77.4 205 ARG 69.3 33.2 79.4 206 PHE 165.4 99.1 33.5 207 ASP 54.1 49.0 73.6 208 ALA 13.4 18.4 79.4 209 ASP 89.1 80.6 58.8 210 TYR 129.2 71.4 45.3 211 ALA 18.1 24.9 75.9 212 GLU 31.7 22.8 79.4 213 LYS 104.6 60.4 68.7 214 MET 149.3 93.6 40.8 215 ALA 19.8 27.3 82.4 216 GLY 0.0 0.0 84.2 217 CYS 89.5 90.2 59.4 218 SER 26.7 31.9 82.6 219 LEU 146.9 99.4 32.3 220 SER 15.7 18.8 82.2 221 PHE 156.0 93.5 55.0 222 ARG 131.0 62.7 90.1 223 SER 10.1 12.0 81.0