Protein Data Bank File : 3seb Title : TOXIN 26-NOV-97 3SEB Number of Amino Acid Residues : 238 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU SER GLN PRO ASP PRO LYS PRO ASP GLU 10 LEU HIS LYS SER SER LYS PHE THR GLY LEU 20 MET GLU ASN MET LYS VAL LEU TYR ASP ASP 30 ASN HIS VAL SER ALA ILE ASN VAL LYS SER 40 ILE ASP GLN PHE LEU TYR PHE ASP LEU ILE 50 TYR SER ILE LYS ASP THR LYS LEU GLY ASN 60 TYR ASP ASN VAL ARG VAL GLU PHE LYS ASN 70 LYS ASP LEU ALA ASP LYS TYR LYS ASP LYS 80 TYR VAL ASP VAL PHE GLY ALA ASN TYR TYR 90 TYR GLN CYS TYR PHE SER LYS LYS THR ASN 100 ASP ILE ASN SER HIS GLN THR ASP LYS ARG 110 LYS THR CYS MET TYR GLY GLY VAL THR GLU 120 HIS ASN GLY ASN GLN LEU ASP LYS TYR ARG 130 SER ILE THR VAL ARG VAL PHE GLU ASP GLY 140 LYS ASN LEU LEU SER PHE ASP VAL GLN THR 150 ASN LYS LYS LYS VAL THR ALA GLN GLU LEU 160 ASP TYR LEU THR ARG HIS TYR LEU VAL LYS 170 ASN LYS LYS LEU TYR GLU PHE ASN ASN SER 180 PRO TYR GLU THR GLY TYR ILE LYS PHE ILE 190 GLU ASN GLU ASN SER PHE TRP TYR ASP MET 200 MET PRO ALA PRO GLY ASP LYS PHE ASP GLN 210 SER LYS TYR LEU MET MET TYR ASN ASP ASN 220 LYS MET VAL ASP SER LYS ASP VAL LYS ILE 230 GLU VAL TYR LEU THR THR LYS LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 153.6 -176.1 120.2 -123.9 30.5 2 SER -115.9 124.6 166.5 -97.6 3 GLN -49.5 131.3 178.2 -164.5 -173.4 -15.0 4 PRO -62.8 144.7 179.9 16.7 -25.0 5 ASP -69.9 150.5 -169.8 -83.9 0.5 6 PRO -51.5 138.4 173.7 -22.9 27.4 7 LYS 162.8 -38.4 143.0 -128.0 -42.3 -95.3 51.5 8 PRO -71.7 133.9 -165.9 -10.8 26.6 9 ASP 60.2 72.0 178.9 49.5 21.7 10 GLU -77.7 165.8 -161.9 78.8 174.4 -9.7 11 LEU -75.4 152.9 170.0 -67.5 173.8 12 HIS -62.9 138.8 178.1 -71.4 156.0 13 LYS -102.7 122.6 -175.9 -67.9 -179.8 -174.3 36.2 14 SER -61.9 -30.9 -179.4 70.1 15 SER -63.5 -18.5 179.9 58.2 16 LYS -97.0 0.8 170.1 -56.1 -137.9 -154.0 174.2 17 PHE -91.8 122.5 -175.6 170.4 69.2 18 THR -114.9 6.4 174.8 58.5 19 GLY -80.9 -162.1 -176.4 20 LEU -89.1 107.4 -179.2 -138.8 -136.8 21 MET -62.7 -23.1 173.6 -172.3 66.8 72.8 22 GLU -52.3 -31.3 -175.5 -168.4 75.7 -11.9 23 ASN -72.8 -19.0 165.6 -78.3 -25.6 24 MET -87.5 -42.9 -178.0 169.1 72.3 89.5 25 LYS -54.4 -42.7 -173.4 179.0 171.7 -177.7 -82.2 26 VAL -62.9 -23.9 179.4 64.7 27 LEU -70.9 -23.3 -174.7 -58.4 177.5 28 TYR -121.3 20.7 173.3 -61.2 -77.2 29 ASP -87.2 -164.2 -170.6 -138.4 -60.7 30 ASP -61.6 -35.1 -172.4 -71.5 -12.9 31 ASN -86.9 134.0 177.9 -56.6 -56.5 32 HIS -159.6 165.4 176.5 64.8 -78.6 33 VAL -86.5 129.5 173.3 173.3 34 SER -145.0 118.7 175.7 -175.0 35 ALA -139.0 145.7 -175.9 36 ILE -119.9 127.7 175.6 -68.3 173.4 37 ASN 61.7 59.5 178.1 -151.2 3.8 38 VAL -122.3 156.8 -179.4 -71.0 39 LYS -122.4 145.6 178.7 172.6 179.0 95.4 51.4 40 SER -60.0 146.1 -177.8 61.1 41 ILE -120.3 -6.6 -177.8 58.8 160.2 42 ASP -167.2 -178.9 -179.9 -153.8 -10.2 43 GLN -155.1 133.8 179.0 172.1 168.5 59.1 44 PHE -93.8 -73.0 173.6 -179.3 44.3 45 LEU -101.3 167.1 -167.7 -51.3 179.1 46 TYR -71.2 -11.1 -178.6 65.7 88.6 47 PHE -113.7 18.0 171.5 51.4 -89.5 48 ASP -127.6 174.6 172.8 70.1 50.3 49 LEU -140.1 144.8 178.0 -64.5 173.0 50 ILE -112.3 134.2 -178.8 -62.5 165.0 51 TYR -119.8 143.2 169.0 -65.7 86.2 52 SER -94.8 97.3 178.7 37.9 53 ILE -119.7 111.8 -176.4 -62.2 168.4 54 LYS -90.4 140.8 172.0 165.7 84.1 -171.9 -120.0 55 ASP -76.4 79.5 -174.8 176.8 4.7 56 THR -57.2 -28.8 -175.9 35.1 57 LYS -77.1 -39.0 -179.6 171.0 -164.7 -165.3 -103.1 58 LEU -134.8 -6.0 179.2 -49.9 174.8 59 GLY 62.0 38.5 180.0 60 ASN -86.9 -12.0 177.8 -83.2 -36.5 61 TYR -150.7 152.0 173.3 52.9 83.8 62 ASP -121.3 -13.9 -177.5 -37.8 -46.8 63 ASN -140.3 138.1 -179.2 -71.0 -74.5 64 VAL -125.8 124.5 173.8 176.0 65 ARG -90.7 120.4 172.2 173.8 -169.0 -173.3 -145.9 66 VAL -102.1 119.3 -179.3 178.5 67 GLU -104.8 135.4 178.6 -173.6 179.6 -30.4 68 PHE -114.0 166.4 -177.4 -58.1 -81.4 69 LYS -69.2 -24.2 -173.5 172.0 -171.9 36.6 172.2 70 ASN -156.3 174.2 178.4 63.7 26.1 71 LYS -67.6 -37.9 -177.6 -177.3 172.9 173.7 -79.8 72 ASP -55.4 -41.4 -179.2 -81.8 -11.9 73 LEU -68.6 -41.4 177.0 -79.1 164.4 74 ALA -64.5 -39.5 -179.8 75 ASP -64.2 -36.4 -177.1 -72.4 -14.2 76 LYS -61.5 -38.1 -173.2 -179.5 177.9 -171.7 -74.7 77 TYR -102.9 -6.4 -176.1 -64.4 -65.5 78 LYS -58.2 132.0 175.2 -176.9 174.2 -89.1 -109.1 79 ASP 69.0 3.7 177.9 -77.8 -35.2 80 LYS -99.9 157.3 -179.9 -81.9 42.7 -97.0 -129.9 81 TYR -89.0 128.6 -172.1 -82.7 87.4 82 VAL -134.9 167.9 167.1 -56.0 83 ASP -106.1 141.8 -177.7 -55.9 -27.8 84 VAL -121.7 133.1 179.9 -174.2 85 PHE -147.1 125.9 174.3 -169.2 -74.7 86 GLY 176.5 179.5 -177.3 87 ALA -95.3 125.1 -173.6 88 ASN -111.2 160.3 178.9 57.3 -55.8 89 TYR -133.5 161.6 -173.2 64.2 -79.6 90 TYR -126.8 -45.4 -167.5 -61.4 -89.8 91 TYR -60.9 -35.7 -178.2 168.4 53.0 92 GLN -102.4 13.8 -173.1 -65.5 163.1 -73.0 93 CYS -89.4 128.0 169.3 175.7 94 TYR -147.5 142.7 167.1 173.7 73.9 95 PHE -161.4 162.5 173.1 54.1 -84.6 96 SER -115.5 149.7 178.4 145.0 97 LYS -101.2 135.9 178.0 0.0 0.0 0.0 0.0 98 LYS -92.0 68.6 -178.3 0.0 0.0 0.0 0.0 99 THR -97.1 16.9 176.9 0.0 100 ASN 57.6 58.7 176.1 0.0 0.0 101 ASP 74.3 -5.1 175.8 0.0 0.0 102 ILE 34.1 -177.7 177.6 0.0 0.0 103 ASN -162.7 -171.0 -178.0 0.0 0.0 104 SER 61.6 27.7 178.0 0.0 105 HIS 46.6 64.1 179.4 0.0 0.0 106 GLN -43.9 -42.4 173.9 0.0 0.0 0.0 107 THR 12.3 174.8 174.6 0.0 108 ASP 31.4 42.4 175.5 60.7 14.6 109 LYS -80.1 133.6 -178.4 0.0 0.0 0.0 0.0 110 ARG -105.8 123.4 -168.7 -75.4 156.4 -171.8 -171.4 111 LYS -108.6 147.4 168.2 -65.7 157.9 -171.1 -168.5 112 THR -145.3 166.9 -170.7 -168.3 113 CYS -135.5 151.4 175.7 -70.9 114 MET -156.9 177.7 178.3 65.7 -177.7 -84.1 115 TYR -124.9 135.7 173.9 -63.0 -89.5 116 GLY 58.2 -143.7 176.7 117 GLY 82.8 13.6 -169.1 118 VAL -114.5 132.6 175.8 171.1 119 THR -134.7 145.8 175.4 45.1 120 GLU -59.5 141.5 176.9 -55.7 -167.7 -4.3 121 HIS -75.3 -54.5 -172.6 -177.7 85.1 122 ASN -65.2 133.7 177.0 -70.4 -33.4 123 GLY 87.7 -13.9 -170.2 124 ASN -108.1 6.1 -173.3 -168.2 -135.5 125 GLN -92.6 132.5 167.1 -54.2 -54.4 126.2 126 LEU -89.0 149.3 177.2 -63.4 167.4 127 ASP -69.6 -37.2 -177.4 -63.9 -33.8 128 LYS -129.6 145.9 -176.7 -67.8 -177.9 169.3 113.4 129 TYR -58.6 150.3 173.5 72.0 86.5 130 ARG -108.5 138.7 178.2 175.8 167.1 -78.7 159.2 131 SER -101.1 139.3 177.0 -72.8 132 ILE -123.1 127.5 -177.3 -62.9 149.9 133 THR -85.0 136.4 174.9 -64.8 134 VAL -112.1 122.6 173.0 178.0 135 ARG -102.2 125.7 180.0 -69.9 -177.4 71.9 -142.6 136 VAL -104.7 125.1 176.8 -174.3 137 PHE -106.5 125.6 173.1 -60.4 82.2 138 GLU -113.6 117.3 -175.7 -69.7 164.7 -78.2 139 ASP 49.4 38.4 168.5 -58.2 -39.3 140 GLY 94.5 -8.6 -177.5 141 LYS -107.8 135.5 177.9 -65.4 179.6 148.4 52.7 142 ASN -83.7 96.7 -174.3 176.6 28.9 143 LEU -104.6 -9.4 -176.1 -61.1 177.7 144 LEU -150.6 133.3 170.9 164.9 76.9 145 SER -134.5 147.1 -178.9 -60.0 146 PHE -155.5 165.8 -179.4 65.6 -86.2 147 ASP -112.4 149.0 168.2 -76.5 -68.5 148 VAL -113.8 159.7 -174.7 -61.6 149 GLN -128.0 144.3 174.1 -73.7 122.5 -73.2 150 THR -144.1 157.5 177.2 -176.8 151 ASN -109.8 15.4 -178.4 -86.7 91.3 152 LYS -104.9 139.5 176.1 -60.5 172.5 -175.2 155.7 153 LYS -71.6 -51.0 169.5 -64.2 177.1 -158.8 -167.4 154 LYS -105.2 126.0 -173.0 -56.4 -64.2 177.0 175.0 155 VAL -126.2 143.2 178.8 64.5 156 THR -73.0 148.5 169.5 59.8 157 ALA -57.2 -34.1 176.6 158 GLN -56.5 -47.3 -179.7 179.5 175.6 -170.1 159 GLU -61.2 -45.5 179.6 170.2 169.2 -20.9 160 LEU -66.4 -37.4 177.7 -63.3 179.1 161 ASP -62.6 -48.0 178.3 -168.6 9.6 162 TYR -55.1 -52.7 -172.9 168.4 83.7 163 LEU -61.1 -36.6 -178.5 -64.3 169.2 164 THR -66.1 -52.1 -177.9 -64.6 165 ARG -68.3 -33.6 175.9 -60.3 -161.3 -150.4 -173.9 166 HIS -55.7 -45.9 178.2 179.9 81.4 167 TYR -60.2 -43.2 -174.2 -175.9 -89.2 168 LEU -72.7 -28.6 175.9 -67.4 170.9 169 VAL -66.9 -44.2 -175.1 168.0 170 LYS -73.2 -36.3 -169.6 -65.3 -16.3 -162.5 37.9 171 ASN -107.6 -20.6 -178.5 -69.5 -72.3 172 LYS -126.9 12.0 179.6 -66.9 -68.8 -98.6 -179.8 173 LYS 51.0 42.5 -176.1 -64.8 168.0 -98.6 -18.1 174 LEU -53.7 -40.5 171.4 168.3 66.6 175 TYR -127.2 135.6 174.3 -51.7 -57.8 176 GLU -118.0 -179.2 -179.4 -57.1 -164.9 -84.3 177 PHE -56.7 -45.5 -174.6 -179.3 75.0 178 ASN -130.8 20.5 178.8 55.7 -167.8 179 ASN -174.3 177.2 167.3 68.3 -75.7 180 SER -133.3 146.9 175.5 170.2 181 PRO -75.0 -10.7 179.6 22.6 -23.3 182 TYR -103.6 142.1 179.0 -60.7 -75.6 183 GLU -83.2 -46.9 178.5 176.4 72.2 -36.3 184 THR -132.9 156.7 174.5 68.0 185 GLY -157.8 138.3 169.5 186 TYR -137.3 150.6 175.4 62.1 -74.7 187 ILE -111.7 129.2 -175.7 179.8 163.9 188 LYS -118.2 128.9 178.6 -175.6 179.9 179.6 176.2 189 PHE -104.7 125.2 178.1 -62.1 -83.4 190 ILE -118.0 119.6 176.8 -54.0 92.0 191 GLU -129.2 104.4 -171.3 -167.8 -176.4 23.8 192 ASN 47.7 -127.6 -177.2 -57.0 -54.4 193 GLU -96.9 33.8 172.6 -61.5 -59.0 -56.3 194 ASN -121.3 144.8 174.8 -164.0 57.1 195 SER -154.8 151.8 -178.5 72.6 196 PHE -153.5 163.6 -174.4 56.6 -82.4 197 TRP -148.5 158.1 179.0 55.7 -92.1 198 TYR -125.1 137.8 174.6 -61.7 -35.9 199 ASP -75.4 128.7 -177.6 -171.2 -25.2 200 MET -89.7 -3.9 -175.4 -85.0 -167.8 -69.9 201 MET -109.9 153.6 177.3 -66.3 -66.9 -177.3 202 PRO -68.3 153.9 173.6 15.8 -18.2 203 ALA -63.7 156.3 -177.7 204 PRO -67.3 164.3 178.2 25.1 -34.2 205 GLY 111.1 -168.1 -168.9 206 ASP -109.0 4.1 177.5 70.7 -40.0 207 LYS -130.8 140.7 173.4 -64.3 147.5 -174.7 -52.5 208 PHE -110.0 121.9 178.8 178.0 58.1 209 ASP -93.4 99.3 -175.3 -175.9 -24.8 210 GLN -62.2 -42.6 -176.4 -68.9 175.1 -33.1 211 SER -64.3 -41.5 -179.1 175.6 212 LYS -68.9 -34.0 -179.9 179.9 143.1 -174.8 -126.6 213 TYR -66.2 -47.9 -175.7 -175.5 78.6 214 LEU -72.1 -17.2 179.8 -67.0 166.7 215 MET -58.8 -23.7 176.0 -164.1 171.1 -86.1 216 MET -57.0 -23.1 -179.8 62.4 176.1 178.4 217 TYR -84.2 2.7 -174.4 -63.7 -47.2 218 ASN -73.3 -4.0 175.0 73.2 -4.2 219 ASP -81.3 -6.5 -179.4 59.8 1.3 220 ASN 55.7 32.2 -175.4 -146.2 47.3 221 LYS -60.7 135.4 179.7 -175.9 151.8 -142.5 -60.0 222 MET -122.3 154.1 173.1 -59.0 170.8 -31.9 223 VAL -129.6 160.4 174.5 -64.0 224 ASP -82.8 122.5 -172.3 -172.7 -67.3 225 SER -66.1 -17.9 179.7 55.0 226 LYS -83.5 -21.8 -173.9 83.6 168.3 129.8 73.1 227 ASP -104.5 -17.6 -170.3 -70.8 -23.2 228 VAL -82.9 146.1 171.9 67.6 229 LYS -124.0 147.2 -178.9 -58.1 -178.7 -97.1 10.0 230 ILE -120.3 135.3 172.8 -57.8 175.3 231 GLU -126.4 139.3 176.8 -67.7 174.0 -4.5 232 VAL -120.3 130.0 -179.3 176.0 233 TYR -118.9 112.5 -179.8 -66.6 87.0 234 LEU -112.9 144.9 167.0 -57.5 162.8 235 THR -120.3 141.8 -173.8 64.5 236 THR -82.5 148.4 177.9 61.8 237 LYS -73.4 140.2 175.7 -87.3 -135.5 -100.2 91.4 238 LYS -44.7 -65.5 0.0 0.0 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 6.225 13.623 43.720 2 SER 3.780 16.218 45.025 3 GLN 4.503 19.479 46.813 4 PRO 2.418 19.417 50.011 5 ASP -0.696 21.593 49.750 6 PRO -0.423 24.945 51.533 7 LYS -0.299 25.245 55.335 8 PRO 3.408 24.937 55.579 9 ASP 4.001 28.249 53.864 10 GLU 0.508 29.468 54.584 11 LEU -0.866 31.647 51.864 12 HIS -0.524 35.359 51.347 13 LYS -3.644 37.216 52.460 14 SER -4.776 40.028 50.136 15 SER -6.221 41.968 53.061 16 LYS -2.687 42.401 54.434 17 PHE -1.330 43.859 51.197 18 THR -1.780 47.615 51.312 19 GLY 0.006 48.625 48.087 20 LEU -1.493 49.097 44.611 21 MET -3.130 45.838 43.445 22 GLU -2.973 47.184 39.857 23 ASN 0.729 46.363 39.913 24 MET -0.205 42.667 40.166 25 LYS -3.226 42.950 37.832 26 VAL -1.189 44.334 34.933 27 LEU 0.940 41.179 34.815 28 TYR -2.173 39.094 33.965 29 ASP -4.077 41.600 31.830 30 ASP -4.298 41.626 28.022 31 ASN -0.692 42.466 27.304 32 HIS 1.970 39.779 27.425 33 VAL 4.976 38.608 25.433 34 SER 4.231 36.049 22.763 35 ALA 6.578 35.228 19.902 36 ILE 6.799 32.228 17.612 37 ASN 9.999 30.914 15.960 38 VAL 12.518 33.539 17.047 39 LYS 16.251 33.312 17.868 40 SER 18.300 35.130 20.501 41 ILE 20.295 38.074 19.164 42 ASP 22.384 39.021 22.187 43 GLN 23.116 38.260 25.821 44 PHE 23.610 40.635 28.806 45 LEU 24.542 38.300 31.688 46 TYR 25.542 34.645 31.377 47 PHE 22.109 33.430 32.539 48 ASP 19.976 35.481 30.149 49 LEU 19.152 35.825 26.468 50 ILE 18.005 38.868 24.505 51 TYR 15.358 38.684 21.735 52 SER 14.128 41.238 19.222 53 ILE 10.426 40.858 19.812 54 LYS 8.393 43.851 18.751 55 ASP 5.165 44.779 20.502 56 THR 3.210 45.007 17.233 57 LYS 0.049 45.997 19.146 58 LEU 1.340 49.009 21.085 59 GLY 5.062 49.238 20.367 60 ASN 5.918 49.370 24.069 61 TYR 9.032 47.269 23.536 62 ASP 11.346 46.238 20.713 63 ASN 13.717 44.019 22.712 64 VAL 13.012 41.453 25.442 65 ARG 15.485 40.129 28.010 66 VAL 14.637 36.598 29.166 67 GLU 16.325 35.632 32.452 68 PHE 16.888 32.048 33.572 69 LYS 17.841 30.462 36.874 70 ASN 21.243 29.302 35.672 71 LYS 23.797 29.168 32.878 72 ASP 22.723 25.734 31.608 73 LEU 19.322 27.039 30.543 74 ALA 20.696 30.041 28.656 75 ASP 23.269 27.821 26.965 76 LYS 20.569 25.379 25.948 77 TYR 18.528 27.930 24.014 78 LYS 21.196 30.349 22.764 79 ASP 21.098 30.777 18.965 80 LYS 18.241 28.230 18.623 81 TYR 14.772 29.012 17.289 82 VAL 12.252 29.053 20.117 83 ASP 8.774 30.212 21.074 84 VAL 8.590 32.772 23.905 85 PHE 5.529 33.286 26.129 86 GLY 5.305 35.108 29.405 87 ALA 4.466 38.001 31.718 88 ASN 6.788 40.967 31.353 89 TYR 7.819 43.926 33.502 90 TYR 9.314 47.358 32.938 91 TYR 9.929 49.406 36.077 92 GLN 12.725 47.176 37.399 93 CYS 14.018 46.109 34.000 94 TYR 17.533 46.861 32.875 95 PHE 20.015 45.398 30.413 96 SER 22.598 46.602 27.931 97 LYS 22.973 45.301 24.388 98 LYS 26.309 44.002 23.081 99 THR 26.066 45.180 19.468 100 ASN 29.789 45.950 19.381 101 ASP 29.568 49.758 19.336 102 ILE 26.653 49.317 16.891 103 ASN 25.549 51.559 14.038 104 SER 22.469 52.611 12.066 105 HIS 21.617 54.827 15.047 106 GLN 20.311 52.041 17.299 107 THR 18.873 54.794 19.501 108 ASP 15.349 54.760 20.956 109 LYS 15.341 51.040 21.835 110 ARG 12.400 50.082 24.045 111 LYS 13.191 47.365 26.576 112 THR 11.190 44.911 28.640 113 CYS 12.136 41.961 30.842 114 MET 10.779 38.543 31.778 115 TYR 11.787 35.181 33.228 116 GLY 11.746 31.811 31.478 117 GLY 8.844 31.209 29.101 118 VAL 11.001 29.539 26.418 119 THR 10.429 26.298 24.488 120 GLU 12.159 24.983 21.361 121 HIS 10.073 25.654 18.270 122 ASN 10.945 22.721 16.026 123 GLY 9.282 19.484 17.026 124 ASN 7.116 21.054 19.675 125 GLN 4.175 22.142 17.530 126 LEU 0.711 20.596 17.508 127 ASP -1.311 20.760 14.278 128 LYS -4.467 21.710 16.170 129 TYR -4.841 23.468 19.546 130 ARG -5.097 21.404 22.708 131 SER -7.573 22.308 25.461 132 ILE -6.748 22.042 29.150 133 THR -9.513 22.144 31.734 134 VAL -9.244 24.414 34.729 135 ARG -11.415 23.663 37.742 136 VAL -11.967 26.655 40.042 137 PHE -12.829 26.120 43.713 138 GLU -14.333 29.000 45.685 139 ASP -14.405 28.262 49.415 140 GLY -13.981 24.584 48.625 141 LYS -16.752 24.316 46.038 142 ASN -16.242 23.852 42.300 143 LEU -18.580 26.499 40.908 144 LEU -16.745 27.305 37.681 145 SER -14.698 25.352 35.148 146 PHE -13.189 26.579 31.884 147 ASP -10.560 25.627 29.339 148 VAL -7.302 27.234 28.236 149 GLN -5.623 26.417 24.928 150 THR -2.079 25.925 23.686 151 ASN -0.477 24.611 20.494 152 LYS 2.659 23.304 22.254 153 LYS 3.401 19.700 23.196 154 LYS 5.631 20.766 26.063 155 VAL 4.356 24.043 27.535 156 THR 5.714 26.202 30.315 157 ALA 3.740 26.430 33.539 158 GLN 4.100 30.204 33.108 159 GLU 2.076 30.175 29.898 160 LEU -0.695 28.100 31.477 161 ASP -0.684 30.242 34.654 162 TYR -0.989 33.444 32.611 163 LEU -3.866 32.084 30.525 164 THR -5.667 30.848 33.652 165 ARG -5.344 34.083 35.590 166 HIS -6.208 36.210 32.543 167 TYR -9.584 34.502 32.347 168 LEU -10.118 34.983 36.070 169 VAL -9.171 38.692 35.979 170 LYS -11.646 39.314 33.179 171 ASN -14.471 37.124 34.465 172 LYS -14.108 36.900 38.251 173 LYS -12.265 40.155 39.034 174 LEU -9.405 38.188 40.598 175 TYR -7.367 41.392 40.766 176 GLU -8.793 44.900 40.714 177 PHE -7.120 48.326 40.850 178 ASN -6.946 48.502 44.662 179 ASN -8.137 45.159 46.001 180 SER -9.237 41.632 45.344 181 PRO -12.558 40.082 46.322 182 TYR -10.558 36.978 47.341 183 GLU -8.444 36.662 50.496 184 THR -6.168 33.804 49.341 185 GLY -5.574 31.987 46.083 186 TYR -3.266 29.287 44.789 187 ILE -2.956 27.590 41.421 188 LYS -2.084 23.885 41.368 189 PHE -0.610 21.972 38.432 190 ILE -1.083 18.183 38.301 191 GLU 0.991 16.059 35.949 192 ASN 0.631 12.316 36.534 193 GLU 1.981 11.660 40.050 194 ASN 3.688 15.060 40.337 195 SER 2.100 18.312 41.493 196 PHE 3.159 21.823 42.387 197 TRP 1.529 25.159 43.169 198 TYR 2.027 28.939 43.160 199 ASP 0.621 31.539 45.556 200 MET -1.488 34.010 43.570 201 MET -1.523 36.907 46.034 202 PRO 1.077 39.582 46.788 203 ALA 3.210 39.573 49.929 204 PRO 1.987 41.849 52.736 205 GLY 2.936 45.489 53.075 206 ASP 2.686 48.594 50.938 207 LYS 4.914 47.682 48.010 208 PHE 4.630 44.928 45.375 209 ASP 7.938 43.800 43.857 210 GLN 6.975 42.649 40.360 211 SER 10.424 41.369 39.475 212 LYS 10.766 39.247 42.588 213 TYR 7.291 37.811 42.067 214 LEU 7.878 36.861 38.442 215 MET 11.286 35.358 39.302 216 MET 9.537 32.128 40.277 217 TYR 9.214 31.427 36.567 218 ASN 12.983 31.501 35.993 219 ASP 13.203 27.702 36.234 220 ASN 11.473 27.479 32.818 221 LYS 9.399 24.611 34.244 222 MET 7.446 22.713 31.613 223 VAL 4.607 20.221 31.624 224 ASP 3.208 17.940 28.912 225 SER 0.019 19.614 27.628 226 LYS -1.688 16.271 27.157 227 ASP -1.170 15.125 30.781 228 VAL -1.534 18.290 32.864 229 LYS -4.624 19.327 34.845 230 ILE -5.111 22.709 36.565 231 GLU -6.951 23.455 39.792 232 VAL -7.443 26.921 41.311 233 TYR -8.405 27.339 44.986 234 LEU -9.756 30.702 46.053 235 THR -11.153 31.818 49.390 236 THR -13.469 34.760 49.608 237 LYS -12.737 37.848 51.650 238 LYS -14.883 38.440 54.731 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S C T T T T S 10 S S S/T T T T/S S S S H 20 H H H 3 3/T T T T C S 30 S S S/S S S S S/S S S S 40 S S/S S S S C S S S S 50 S S/S S S S/T T T T C S 60 S S S/S S S S S S S H 70 H H H H H H H H S S 80 S S S/S S S S S/S S S S 90 S S S S S S S S S C 100 S S S S C C C S S S 110 S S S S C C S S S S 120 S/T T T T/S S S S/S S S S 130 S S S S S S S/T T T T/S 140 S S S/S S S S/S S S S S 150 S S S S S S/H H H H H 160 H H H H H H H H H H 170 H H C C C T T T T C 180 S S S S/S S S S S S S 190 S/T T T T/S S S S/S S S S 200 S/S S S S C S S S S/H H 210 H H H H H C T T T T/S 220 S S S S/T T T T/S S S S 230 S S S S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B S S S S 10 g G G G B S t 20 h H H H H h G G g S 30 E E E E E E E e 40 B S t T e E E E 50 E t T T T t 60 S E E E E E e S h 70 H H H H H H H h T e 80 E E E E E E B t 90 T T t t T 100 T t S S e 110 E E E E E e e E E E 120 e T T e E E E E E E 130 E E E E E E E E e T 140 E E E E E E E E E E 150 E E e E E E H H H H 160 H H H H H H H H H H 170 H H h S S S S 180 e E E E E E E E E E 190 E e T E E E E E E e 200 S S B S h H 210 H H H H h G G G G g 220 e E E E e T e E E E 230 E E E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 0.1 0.0 94.6 2 SER 41.7 49.9 76.0 3 GLN 87.0 58.6 63.1 4 PRO 36.1 29.0 75.7 5 ASP 61.6 55.7 70.2 6 PRO 118.8 95.5 43.1 7 LYS 39.5 22.8 80.0 8 PRO 46.4 37.3 76.1 9 ASP 41.1 37.2 69.2 10 GLU 53.8 38.8 76.2 11 LEU 127.9 86.5 51.9 12 HIS 85.7 57.1 67.1 13 LYS 114.7 66.2 68.9 14 SER 82.8 99.0 46.9 15 SER 39.4 47.2 69.9 16 LYS 48.4 27.9 73.5 17 PHE 164.7 98.7 54.3 18 THR 31.4 29.4 76.5 19 GLY 28.5 81.9 62.3 20 LEU 83.4 56.4 62.6 21 MET 156.0 97.9 40.0 22 GLU 85.8 61.9 57.0 23 ASN 62.7 51.8 63.1 24 MET 158.9 99.7 33.8 25 LYS 125.1 72.2 65.7 26 VAL 50.2 42.3 72.9 27 LEU 143.8 97.3 43.1 28 TYR 180.7 99.8 43.8 29 ASP 83.9 75.9 64.3 30 ASP 51.9 47.0 80.1 31 ASN 53.1 43.9 69.1 32 HIS 110.7 73.7 60.8 33 VAL 118.8 100.0 39.2 34 SER 47.8 57.1 66.1 35 ALA 61.0 84.0 47.7 36 ILE 40.8 28.4 75.6 37 ASN 60.7 50.2 62.1 38 VAL 85.7 72.1 54.2 39 LYS 108.5 62.6 67.5 40 SER 81.5 97.5 50.1 41 ILE 74.3 51.8 77.1 42 ASP 86.9 78.7 55.2 43 GLN 116.4 78.3 61.9 44 PHE 119.9 71.9 56.2 45 LEU 74.5 50.4 62.8 46 TYR 47.2 26.1 67.2 47 PHE 122.5 73.4 57.3 48 ASP 110.5 100.0 44.8 49 LEU 147.8 100.0 47.8 50 ILE 141.8 98.8 43.7 51 TYR 180.9 100.0 33.9 52 SER 39.5 47.3 65.2 53 ILE 133.9 93.3 40.2 54 LYS 76.8 44.3 72.4 55 ASP 94.7 85.7 52.5 56 THR 5.4 5.1 82.0 57 LYS 57.0 32.9 79.1 58 LEU 75.9 51.4 82.3 59 GLY 27.4 78.8 72.7 60 ASN 51.5 42.6 66.8 61 TYR 165.6 91.5 55.0 62 ASP 77.4 70.0 65.3 63 ASN 90.8 75.1 47.9 64 VAL 118.8 100.0 34.8 65 ARG 189.2 90.5 43.0 66 VAL 118.8 100.0 37.1 67 GLU 117.9 85.1 54.1 68 PHE 166.8 100.0 41.5 69 LYS 78.4 45.2 73.3 70 ASN 64.3 53.1 61.3 71 LYS 63.5 36.6 75.9 72 ASP 8.5 7.7 83.9 73 LEU 118.5 80.2 57.3 74 ALA 72.6 100.0 60.5 75 ASP 58.9 53.3 71.3 76 LYS 75.4 43.5 73.1 77 TYR 176.1 97.3 46.0 78 LYS 107.5 62.0 73.9 79 ASP 42.0 38.0 72.7 80 LYS 63.5 36.6 76.9 81 TYR 79.4 43.9 71.7 82 VAL 118.8 100.0 45.3 83 ASP 109.8 99.4 58.8 84 VAL 118.8 100.0 33.1 85 PHE 150.0 90.0 54.8 86 GLY 34.8 100.0 49.2 87 ALA 71.8 99.0 49.6 88 ASN 112.6 93.1 46.5 89 TYR 172.8 95.5 49.4 90 TYR 95.2 52.6 71.3 91 TYR 5.6 3.1 87.0 92 GLN 92.9 62.5 62.9 93 CYS 97.0 97.8 50.2 94 TYR 49.4 27.3 72.3 95 PHE 165.0 98.9 29.1 96 SER 37.6 44.9 67.6 97 LYS 134.2 77.4 70.2 98 LYS 118.7 68.5 88.6 99 THR 60.0 56.1 68.7 100 ASN 43.2 35.7 86.5 101 ASP 32.3 29.2 86.9 102 ILE 114.2 79.6 60.6 103 ASN 51.2 42.3 81.7 104 SER 5.1 6.0 83.2 105 HIS 78.2 52.1 82.2 106 GLN 93.4 62.8 78.3 107 THR 46.1 43.1 78.5 108 ASP 1.2 1.1 85.5 109 LYS 145.0 83.6 75.6 110 ARG 74.2 35.5 84.1 111 LYS 109.3 63.0 60.5 112 THR 106.9 100.0 35.5 113 CYS 98.1 98.9 47.4 114 MET 159.4 100.0 42.4 115 TYR 178.4 98.6 51.8 116 GLY 34.8 100.0 57.6 117 GLY 34.8 100.0 66.4 118 VAL 118.8 100.0 37.4 119 THR 102.4 95.8 54.3 120 GLU 63.9 46.1 70.6 121 HIS 124.3 82.7 65.3 122 ASN 13.3 11.0 79.9 123 GLY 0.0 0.0 85.2 124 ASN 105.8 87.5 57.7 125 GLN 96.6 65.0 72.3 126 LEU 121.6 82.3 68.3 127 ASP 0.0 0.0 85.4 128 LYS 5.2 3.0 89.0 129 TYR 68.0 37.6 82.0 130 ARG 142.2 68.1 58.7 131 SER 49.2 58.9 59.4 132 ILE 138.6 96.6 46.3 133 THR 47.3 44.2 70.3 134 VAL 118.8 100.0 38.8 135 ARG 105.8 50.6 65.0 136 VAL 118.8 100.0 35.3 137 PHE 142.8 85.6 57.6 138 GLU 124.1 89.5 50.7 139 ASP 50.1 45.3 71.5 140 GLY 3.2 9.2 68.4 141 LYS 33.3 19.2 79.1 142 ASN 92.5 76.5 67.2 143 LEU 53.9 36.5 78.1 144 LEU 104.4 70.6 56.5 145 SER 53.0 63.4 63.7 146 PHE 147.8 88.6 41.7 147 ASP 59.5 53.9 70.4 148 VAL 110.7 93.2 44.1 149 GLN 72.3 48.7 69.1 150 THR 100.8 94.3 50.2 151 ASN 60.8 50.3 69.5 152 LYS 152.1 87.7 65.5 153 LYS 84.3 48.6 73.5 154 LYS 83.5 48.1 69.4 155 VAL 118.8 100.0 41.9 156 THR 103.7 97.0 55.6 157 ALA 71.4 98.4 43.3 158 GLN 145.1 97.6 49.8 159 GLU 130.2 94.0 46.0 160 LEU 147.8 100.0 26.3 161 ASP 110.5 100.0 44.9 162 TYR 176.0 97.2 44.3 163 LEU 109.0 73.8 53.0 164 THR 106.9 100.0 29.7 165 ARG 208.9 100.0 39.8 166 HIS 103.9 69.2 63.2 167 TYR 106.8 59.0 53.6 168 LEU 147.8 100.0 24.9 169 VAL 117.5 98.9 48.3 170 LYS 105.7 61.0 78.3 171 ASN 60.5 50.0 63.1 172 LYS 112.0 64.6 64.5 173 LYS 61.4 35.4 82.7 174 LEU 147.7 99.9 27.8 175 TYR 181.0 100.0 33.4 176 GLU 84.0 60.6 65.0 177 PHE 51.2 30.7 70.1 178 ASN 37.6 31.1 71.1 179 ASN 74.2 61.4 69.2 180 SER 83.6 100.0 47.2 181 PRO 78.3 62.9 69.1 182 TYR 170.7 94.3 43.0 183 GLU 103.4 74.6 57.7 184 THR 91.2 85.3 48.2 185 GLY 34.8 100.0 44.3 186 TYR 155.8 86.1 37.9 187 ILE 143.5 100.0 38.8 188 LYS 136.2 78.5 58.0 189 PHE 166.8 100.0 29.5 190 ILE 114.4 79.7 60.0 191 GLU 108.3 78.1 60.2 192 ASN 31.0 25.6 80.8 193 GLU 0.0 0.0 88.1 194 ASN 78.3 64.8 76.4 195 SER 79.3 94.9 56.3 196 PHE 147.3 88.3 46.6 197 TRP 191.4 93.4 48.1 198 TYR 153.7 84.9 45.3 199 ASP 89.1 80.6 55.8 200 MET 159.4 100.0 46.5 201 MET 159.4 100.0 45.7 202 PRO 124.0 99.6 27.4 203 ALA 26.1 36.0 68.0 204 PRO 58.4 46.9 65.7 205 GLY 3.1 8.9 81.4 206 ASP 35.9 32.5 72.4 207 LYS 22.3 12.8 88.9 208 PHE 158.9 95.2 40.1 209 ASP 50.5 45.7 71.0 210 GLN 125.6 84.5 46.9 211 SER 68.7 82.2 60.0 212 LYS 25.7 14.8 83.1 213 TYR 150.9 83.4 56.5 214 LEU 147.1 99.5 36.8 215 MET 84.1 52.7 73.9 216 MET 111.7 70.1 61.0 217 TYR 176.6 97.6 52.9 218 ASN 93.5 77.3 52.2 219 ASP 74.0 66.9 65.6 220 ASN 117.5 97.2 51.5 221 LYS 104.9 60.5 70.7 222 MET 100.3 62.9 65.5 223 VAL 116.7 98.2 40.6 224 ASP 99.0 89.6 64.3 225 SER 83.6 100.0 46.2 226 LYS 63.1 36.4 88.7 227 ASP 70.6 63.9 76.9 228 VAL 118.8 100.0 36.0 229 LYS 61.9 35.7 73.1 230 ILE 143.5 100.0 33.1 231 GLU 102.4 73.9 53.6 232 VAL 118.8 100.0 26.6 233 TYR 124.2 68.6 54.4 234 LEU 147.7 99.9 31.1 235 THR 49.3 46.1 72.5 236 THR 54.7 51.2 71.8 237 LYS 122.3 70.5 69.9 238 LYS 90.0 51.9 80.9