Protein Data Bank File : 1lkfa Title : TOXIN 28-JUL-98 1LKF Number of Amino Acid Residues : 292 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU GLY LYS ILE THR PRO VAL SER VAL LYS 10 LYS VAL ASP ASP LYS VAL THR LEU TYR LYS 20 THR THR ALA THR ALA ASP SER ASP LYS PHE 30 LYS ILE SER GLN ILE LEU THR PHE ASN PHE 40 ILE LYS ASP LYS SER TYR ASP LYS ASP THR 50 LEU VAL LEU LYS ALA THR GLY ASN ILE ASN 60 SER GLY PHE VAL LYS PRO ASN PRO ASN ASP 70 TYR ASP PHE SER LYS LEU TYR TRP GLY ALA 80 LYS TYR ASN VAL SER ILE SER SER GLN SER 90 ASN ASP SER VAL ASN VAL VAL ASP TYR ALA 100 PRO LYS ASN GLN ASN GLU GLU PHE GLN VAL 110 GLN ASN THR LEU GLY TYR THR PHE GLY GLY 120 ASP ILE SER ILE SER ASN GLY LEU THR ALA 130 PHE SER GLU THR ILE ASN TYR LYS GLN GLU 140 SER TYR ARG THR THR LEU SER ARG ASN THR 150 ASN TYR LYS ASN VAL GLY TRP GLY VAL GLU 160 ALA HIS LYS ILE MET ASN ASN GLY TRP GLY 170 PRO TYR GLY ARG ASP SER PHE HIS PRO THR 180 TYR GLY ASN GLU LEU PHE LEU ALA GLY ARG 190 GLN SER SER ALA TYR ALA GLY GLN ASN PHE 200 ILE ALA GLN HIS GLN MET PRO LEU LEU SER 210 ARG SER ASN PHE ASN PRO GLU PHE LEU SER 220 VAL LEU SER HIS ARG GLN ASP GLY ALA LYS 230 LYS SER LYS ILE THR VAL THR TYR GLN ARG 240 GLU MET ASP LEU TYR GLN ILE ARG TRP ASN 250 GLY PHE TYR TRP ALA GLY ALA ASN TYR LYS 260 ASN PHE LYS THR ARG THR PHE LYS SER THR 270 TYR GLU ILE ASP TRP GLU ASN HIS LYS VAL 280 LYS LEU LEU ASP THR LYS GLU THR GLU ASN 290 ASN LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 113.3 -179.9 0.0 0.0 0.0 2 GLY -172.8 -140.3 -178.7 3 LYS -144.8 167.6 179.6 69.5 168.3 -163.6 172.5 4 ILE -129.2 121.6 -179.6 -57.6 170.0 5 THR -72.6 160.3 179.1 64.3 6 PRO -74.8 167.4 -178.9 -27.2 42.6 7 VAL -77.4 133.5 176.5 -171.2 8 SER -103.0 143.9 -179.0 47.7 9 VAL -119.9 143.0 179.6 -45.8 10 LYS -139.5 106.3 178.0 156.5 112.0 -150.8 -108.3 11 LYS -79.5 120.5 -179.1 -162.0 175.9 -177.3 180.0 12 VAL -83.4 -72.1 179.4 176.3 13 ASP -112.0 -132.6 176.9 -101.9 15.9 14 ASP -121.9 -4.5 180.0 0.0 0.0 15 LYS -100.6 -40.2 -178.5 0.0 0.0 0.0 0.0 16 VAL -112.6 136.7 176.0 169.6 17 THR -133.1 127.6 178.5 -52.2 18 LEU -97.9 136.2 179.8 -53.1 172.4 19 TYR -124.2 133.1 -178.0 -59.8 -86.6 20 LYS -132.9 140.4 178.6 173.9 -172.3 -77.9 -169.4 21 THR -150.8 136.7 -178.9 -177.4 22 THR -115.2 129.8 179.9 -55.4 23 ALA -113.4 141.9 179.6 24 THR -128.5 122.7 177.4 -80.2 25 ALA -129.1 126.0 -177.5 26 ASP -122.8 157.1 175.2 -53.4 -68.5 27 SER -125.2 100.2 178.6 169.9 28 ASP -64.6 -39.2 -179.7 -71.5 -54.9 29 LYS -58.8 -50.9 179.8 -170.7 -166.0 -175.1 -179.8 30 PHE -88.8 -2.2 -177.2 -64.5 -14.9 31 LYS 57.4 44.6 177.4 -72.1 174.6 -176.5 178.8 32 ILE -117.9 131.6 179.8 -61.9 171.3 33 SER -126.1 125.0 179.5 157.3 34 GLN -108.0 125.0 177.7 -61.5 -165.0 153.0 35 ILE -120.9 111.6 -177.5 -56.9 174.7 36 LEU -114.4 113.2 -179.8 -52.1 173.1 37 THR -103.8 112.4 -179.5 -54.9 38 PHE -96.0 112.7 179.4 -62.9 83.0 39 ASN -105.3 103.3 178.9 -63.3 -81.5 40 PHE -87.5 129.9 -180.0 -66.0 -89.8 41 ILE -115.0 107.2 178.1 -50.7 175.2 42 LYS -99.2 112.2 -178.2 -69.6 -54.1 -170.9 -171.5 43 ASP -123.1 108.9 -179.0 -171.5 4.2 44 LYS -63.3 -18.1 179.5 -53.1 167.8 -172.3 -178.0 45 SER -89.3 5.7 179.9 78.1 46 TYR -133.5 142.4 -178.8 0.0 0.0 47 ASP -86.8 25.3 178.4 63.0 -35.8 48 LYS -143.2 146.9 176.9 -72.7 -175.1 173.6 -176.2 49 ASP -94.0 137.0 -178.2 -68.6 -35.9 50 THR -115.4 137.2 178.7 -55.3 51 LEU -124.5 120.3 177.4 164.2 59.2 52 VAL -107.4 105.9 179.6 174.7 53 LEU -96.2 120.7 176.6 172.9 59.4 54 LYS -105.2 119.3 180.0 -173.3 171.6 177.2 172.8 55 ALA -105.3 119.1 178.1 56 THR -133.0 -166.3 179.1 67.9 57 GLY 123.2 -136.8 -177.7 58 ASN -149.9 144.4 175.8 -177.7 75.5 59 ILE -134.1 107.8 179.0 -57.9 175.2 60 ASN -62.7 152.6 -179.2 -173.3 -104.9 61 SER -75.5 -26.2 -177.8 67.1 62 GLY 75.9 17.4 -179.8 63 PHE -59.4 135.2 177.4 171.3 84.2 64 VAL -126.6 120.2 -180.0 -178.7 65 LYS -61.1 157.1 178.7 -38.0 165.2 164.2 172.5 66 PRO -80.9 161.9 177.4 33.4 -43.7 67 ASN -82.5 117.1 -179.4 178.5 -10.2 68 PRO -61.1 -11.8 -179.9 33.7 -43.7 69 ASN -91.1 -4.5 179.3 -56.4 -52.6 70 ASP -67.5 121.7 -177.3 -70.9 -9.8 71 TYR -90.3 -59.8 -179.3 -169.4 66.4 72 ASP -101.2 -11.1 -179.6 -77.2 -14.6 73 PHE -144.9 134.1 179.1 164.9 66.8 74 SER -153.1 159.4 -178.6 -166.6 75 LYS -148.3 160.7 178.0 64.1 -179.1 -173.2 165.7 76 LEU -144.3 158.8 176.9 111.2 -156.5 77 TYR -114.2 141.5 -179.3 -75.6 -89.5 78 TRP -140.6 152.4 -180.0 62.2 -72.7 79 GLY -79.1 99.5 -176.5 80 ALA -89.1 -27.1 179.8 81 LYS -155.1 136.4 178.5 -174.4 172.5 -176.7 178.5 82 TYR -114.3 128.4 179.9 -62.7 -88.3 83 ASN -120.9 129.9 177.2 -64.7 -50.6 84 VAL -123.8 125.7 -178.5 167.4 85 SER -129.2 141.8 179.9 -55.0 86 ILE -125.7 129.7 -179.5 -42.6 -95.3 87 SER -136.3 128.3 176.6 -173.7 88 SER -82.3 107.8 -175.4 -155.5 89 GLN -87.9 -8.2 -179.7 -59.7 -100.6 -86.2 90 SER -165.5 173.5 -179.5 73.4 91 ASN 70.1 101.7 -178.3 -162.6 -23.7 92 ASP -68.0 -3.8 178.7 -154.6 38.5 93 SER -88.4 -14.0 179.9 -67.7 94 VAL -103.3 134.2 179.4 -179.1 95 ASN -137.1 150.5 175.1 -74.9 168.0 96 VAL -87.7 109.2 -176.6 173.9 97 VAL -100.4 -29.9 179.0 -61.8 98 ASP -150.3 168.7 -178.4 -61.8 -77.0 99 TYR -171.2 166.1 178.6 41.4 83.3 100 ALA -145.8 129.8 -0.3 101 PRO -68.8 153.3 -177.1 23.3 -37.8 102 LYS -106.8 -8.9 -177.9 58.1 -171.5 178.6 179.5 103 ASN -141.4 158.3 178.8 -157.7 -143.7 104 GLN -54.0 141.5 -176.1 176.9 178.1 111.0 105 ASN -150.3 119.5 179.0 -168.9 -37.6 106 GLU -110.6 16.9 178.8 59.2 -177.1 85.3 107 GLU -71.6 148.1 -179.8 -59.1 -56.1 -61.7 108 PHE -60.1 -32.1 -179.2 -70.3 -6.0 109 GLN -130.1 113.1 179.1 -170.7 81.3 -132.7 110 VAL -88.9 121.8 -179.2 -177.9 111 GLN -136.6 123.8 180.0 -61.4 -173.6 -36.4 112 ASN -140.0 161.5 176.9 -82.1 -178.4 113 THR -131.0 133.6 177.3 -61.2 114 LEU -114.5 121.2 179.7 -175.4 142.4 115 GLY -118.1 140.1 178.5 116 TYR -112.3 128.2 -179.2 176.1 -82.2 117 THR -104.5 142.2 178.2 -66.4 118 PHE -51.7 121.5 -178.1 -55.5 89.2 119 GLY 121.1 -16.5 177.3 120 GLY 109.7 -5.9 -178.2 121 ASP -69.8 125.9 178.9 -168.6 31.5 122 ILE -108.0 124.6 179.7 -58.7 -75.3 123 SER -122.6 131.3 177.9 -70.3 124 ILE -118.2 127.8 -178.6 -67.4 146.2 125 SER -129.6 157.4 178.6 64.3 126 ASN -74.2 145.2 179.7 -179.2 56.3 127 GLY 86.4 -179.0 -178.5 128 LEU -96.3 106.2 17.1 -58.1 176.0 129 THR 111.6 137.0 -179.5 78.1 130 ALA -82.6 -27.2 -179.6 131 PHE -150.0 144.1 -179.5 173.6 81.2 132 SER -145.6 144.5 176.1 -158.7 133 GLU -148.6 158.1 -179.4 -106.8 -54.5 -0.8 134 THR -129.8 155.7 174.5 61.0 135 ILE -123.3 140.0 -177.3 59.5 97.6 136 ASN -152.7 116.1 177.6 169.8 -117.0 137 TYR -150.9 149.6 -180.0 62.4 81.7 138 LYS -95.8 136.3 179.8 -151.8 162.7 -178.1 -176.3 139 GLN -148.3 44.4 -180.0 52.6 152.7 -151.2 140 GLU -52.4 129.5 -179.9 -174.6 167.3 -6.7 141 SER 80.6 -5.9 -179.7 -56.8 142 TYR -110.7 171.6 -179.2 -74.6 48.0 143 ARG -137.1 138.1 178.6 -171.7 172.0 58.3 171.7 144 THR -99.0 130.3 177.5 -67.7 145 THR -132.4 156.6 178.2 55.1 146 LEU -88.5 132.6 -179.0 -89.0 -66.7 147 SER -56.3 147.8 -179.0 72.8 148 ARG -64.0 -35.5 -179.2 -73.8 -177.6 170.0 -79.4 149 ASN -78.4 15.0 178.1 57.5 37.0 150 THR -68.1 126.0 -179.4 -68.1 151 ASN -148.7 -163.4 -177.2 59.3 32.0 152 TYR -67.7 -4.8 179.1 78.2 -38.7 153 LYS -136.4 9.7 -178.0 -62.4 -172.4 169.9 167.5 154 ASN -146.1 138.7 174.4 -61.2 89.9 155 VAL -141.9 141.0 178.5 63.1 156 GLY -149.7 158.0 178.7 157 TRP -134.5 149.0 176.8 -57.0 -98.0 158 GLY -126.4 132.9 178.8 159 VAL -117.8 100.1 -174.8 -177.7 160 GLU -118.2 145.4 179.2 -176.8 -178.6 7.6 161 ALA -49.5 129.0 -175.0 162 HIS -123.6 -70.8 -179.1 180.0 47.8 163 LYS -125.3 93.8 -178.4 -73.4 169.8 174.3 -174.3 164 ILE -108.9 118.2 178.9 -67.8 165.1 165 MET -91.4 140.5 178.4 -49.6 -62.1 -75.0 166 ASN -82.3 -68.1 177.4 -171.1 -64.2 167 ASN -130.1 -86.4 176.6 0.0 0.0 168 GLY -111.9 -7.7 -178.8 169 TRP -79.0 142.0 -179.8 0.0 0.0 170 GLY 119.6 -159.5 0.3 171 PRO -72.4 157.5 179.1 34.0 -41.3 172 TYR -121.0 158.1 178.2 -61.3 -61.2 173 GLY -133.5 -172.2 -180.0 174 ARG -67.5 -21.6 -177.5 -55.8 171.5 77.6 -178.7 175 ASP -101.0 -14.8 -175.8 59.2 -31.1 176 SER -58.0 145.0 -178.4 56.4 177 PHE -156.5 122.5 177.1 -157.4 -90.3 178 HIS -91.2 134.7 -179.5 -174.9 103.3 179 PRO -49.5 -30.8 -180.0 -28.5 42.9 180 THR -102.6 -53.2 -177.1 -58.8 181 TYR -89.7 9.5 178.8 -46.0 -75.9 182 GLY 56.6 -149.1 178.8 183 ASN -80.1 115.5 -178.0 -166.0 -47.2 184 GLU -96.7 12.5 -179.7 -55.8 -168.4 85.8 185 LEU -36.7 -57.5 -178.3 -160.5 57.0 186 PHE -119.6 22.7 178.7 -54.1 -53.2 187 LEU -78.7 124.6 -179.3 -179.4 60.5 188 ALA -77.8 -30.6 -179.6 189 GLY -162.1 139.1 179.6 190 ARG -70.5 -28.2 -177.8 -67.7 175.9 173.0 166.2 191 GLN -125.6 22.9 -177.6 -54.6 -65.0 156.7 192 SER -58.4 128.9 177.4 -54.4 193 SER -87.6 78.7 -176.4 -176.9 194 ALA -147.8 169.7 176.1 195 TYR -74.1 145.8 178.3 -92.4 64.3 196 ALA -56.0 -42.0 -178.1 197 GLY -64.3 -16.2 178.5 198 GLN -116.7 24.0 179.0 -61.4 -172.6 -38.2 199 ASN -119.2 28.6 176.3 -161.5 31.8 200 PHE -106.2 162.0 177.8 -61.6 88.5 201 ILE -72.2 161.6 -179.9 59.8 173.0 202 ALA -66.5 155.9 180.0 203 GLN -59.7 -36.3 179.6 -111.1 -178.0 91.5 204 HIS -69.9 -13.4 179.5 62.6 90.6 205 GLN -94.1 -6.6 178.2 -60.9 171.0 -94.3 206 MET -93.2 156.8 179.3 -64.3 168.9 83.5 207 PRO -61.2 147.3 177.7 -26.8 39.2 208 LEU -56.0 -37.2 -180.0 -94.2 -47.7 209 LEU -70.0 -27.9 -179.0 -64.0 -150.4 210 SER -76.3 -32.3 -177.7 77.3 211 ARG -122.2 1.2 179.8 51.6 67.9 169.0 -158.5 212 SER -119.0 -88.7 -179.7 175.5 213 ASN -169.1 176.6 177.7 67.7 -68.2 214 PHE -128.6 129.8 178.1 177.0 48.4 215 ASN -107.9 93.4 -179.4 -66.4 125.6 216 PRO -67.6 148.3 173.2 34.7 -44.8 217 GLU -144.4 102.0 -179.0 -74.1 -153.7 3.2 218 PHE -131.5 146.0 179.2 -64.6 -74.7 219 LEU -121.7 137.9 177.3 -72.8 164.5 220 SER -135.4 139.0 -179.6 62.1 221 VAL -109.9 116.9 177.0 -174.2 222 LEU -103.2 142.7 -178.3 -83.5 71.8 223 SER -121.8 135.9 178.7 -164.8 224 HIS -115.3 125.3 -177.9 -175.0 -59.8 225 ARG -65.3 -4.5 179.7 -72.9 -157.9 -92.3 103.2 226 GLN 65.4 25.5 177.9 -74.9 -174.9 5.5 227 ASP -142.7 148.3 -179.3 0.0 0.0 228 GLY 75.6 176.8 -177.2 229 ALA -31.7 140.4 179.7 230 LYS -84.0 -12.5 -179.9 -64.0 -85.6 -174.2 130.9 231 LYS -118.1 152.7 178.0 -56.4 -173.7 -179.1 173.5 232 SER -147.9 157.0 -179.0 68.3 233 LYS -97.2 143.5 178.9 -111.0 -172.8 175.8 175.8 234 ILE -141.1 143.3 176.8 -155.6 177.8 235 THR -125.3 137.4 178.1 60.7 236 VAL -122.6 125.8 -177.7 177.6 237 THR -120.2 124.9 176.1 -55.6 238 TYR -113.0 134.5 -176.8 -79.8 18.6 239 GLN -148.1 153.8 175.5 172.6 -170.9 87.0 240 ARG -129.6 138.7 176.1 58.2 163.5 173.1 -81.9 241 GLU -105.5 122.5 -179.5 -64.0 -171.7 6.4 242 MET -107.2 129.3 179.3 -63.6 155.3 57.6 243 ASP -98.4 144.9 177.8 -71.1 10.3 244 LEU -97.2 110.2 179.8 178.5 50.8 245 TYR -103.5 122.7 -179.3 -175.9 73.2 246 GLN -133.4 148.4 179.2 60.0 -179.8 -122.8 247 ILE -123.8 153.2 -177.8 59.1 172.6 248 ARG -150.4 140.0 178.1 166.9 176.0 -91.3 117.7 249 TRP -96.0 128.1 -179.9 174.0 -107.5 250 ASN -105.7 11.9 -178.4 72.5 -7.5 251 GLY 101.7 -16.3 -178.7 252 PHE -122.5 -44.8 -177.6 -60.7 88.0 253 TYR -150.9 173.4 177.3 52.7 78.5 254 TRP -100.4 144.0 178.0 -72.7 99.7 255 ALA -139.0 141.0 -179.3 256 GLY -107.9 158.9 178.5 257 ALA -146.7 129.7 179.4 258 ASN -114.3 114.6 178.5 -169.0 62.3 259 TYR -86.9 106.8 -178.1 -69.4 77.6 260 LYS -66.7 129.1 179.3 -169.9 156.3 169.4 178.1 261 ASN 47.4 56.9 -179.2 -165.2 -157.1 262 PHE -80.6 -20.2 175.8 -153.8 76.7 263 LYS -141.7 138.3 179.2 -72.0 -164.3 174.9 162.2 264 THR -129.7 136.9 177.8 -48.7 265 ARG -128.1 120.7 -176.7 -62.1 -59.2 -178.4 -93.6 266 THR -124.9 139.7 178.1 -50.2 267 PHE -131.0 118.1 -178.8 -178.6 64.9 268 LYS -117.1 135.5 176.7 178.3 -174.9 155.0 172.2 269 SER -120.3 147.1 178.9 64.2 270 THR -124.2 126.0 -179.5 -59.1 271 TYR -122.2 150.8 175.6 -73.4 89.0 272 GLU -104.8 119.5 -180.0 172.0 -172.5 66.6 273 ILE -90.9 124.4 178.2 -59.4 166.3 274 ASP -103.2 95.9 -178.6 -174.1 -22.1 275 TRP -66.0 -28.7 178.4 -63.0 81.9 276 GLU -72.5 -44.8 -179.3 170.8 175.4 41.3 277 ASN -100.2 7.1 178.6 -61.0 -58.2 278 HIS 47.0 46.3 -179.7 -28.4 -75.5 279 LYS -126.6 162.4 176.6 -73.5 -179.8 -172.2 176.4 280 VAL -132.2 152.0 -178.9 -65.0 281 LYS -137.7 127.3 178.7 172.3 -159.4 177.8 -175.3 282 LEU -68.8 125.7 179.7 -177.3 63.7 283 LEU -104.1 -34.4 -177.2 -65.6 -175.9 284 ASP -166.6 155.1 174.2 -175.4 55.7 285 THR -136.1 144.2 -179.2 54.0 286 LYS -145.2 125.6 178.5 -171.2 -177.4 178.2 -169.5 287 GLU -103.2 128.9 179.1 -61.1 172.9 -28.1 288 THR -132.4 147.3 -178.0 52.1 289 GLU -129.6 148.0 172.4 -69.1 -171.5 13.1 290 ASN -128.2 136.1 -179.1 -164.5 -101.6 291 ASN -141.2 109.6 -179.8 -64.6 -78.0 292 LYS -82.4 173.2 0.0 -63.8 -177.6 -173.8 -177.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 1.949 30.875 81.869 2 GLY 3.738 32.955 79.233 3 LYS 4.736 33.325 75.587 4 ILE 6.910 32.002 72.762 5 THR 8.775 34.394 70.440 6 PRO 8.806 33.739 66.669 7 VAL 11.905 32.096 65.200 8 SER 14.912 34.206 64.308 9 VAL 17.229 32.730 61.669 10 LYS 20.935 33.233 61.253 11 LYS 22.708 31.700 58.277 12 VAL 26.291 31.116 59.417 13 ASP 28.109 29.511 56.442 14 ASP 26.300 27.551 53.717 15 LYS 26.530 24.432 55.913 16 VAL 25.163 25.781 59.227 17 THR 22.012 27.813 59.931 18 LEU 21.089 28.844 63.487 19 TYR 17.431 29.084 64.530 20 LYS 16.355 30.665 67.795 21 THR 13.137 30.884 69.775 22 THR 12.523 31.847 73.419 23 ALA 9.764 30.452 75.597 24 THR 8.679 31.900 78.925 25 ALA 6.601 29.983 81.511 26 ASP 5.916 31.529 84.932 27 SER 4.493 30.708 88.328 28 ASP 3.329 33.962 89.889 29 LYS 2.345 31.965 92.974 30 PHE 5.793 30.376 93.649 31 LYS 7.717 33.382 92.234 32 ILE 9.519 31.117 89.739 33 SER 10.226 32.310 86.189 34 GLN 11.513 30.066 83.356 35 ILE 13.178 31.625 80.314 36 LEU 14.069 28.914 77.816 37 THR 16.101 29.804 74.762 38 PHE 16.137 27.070 72.124 39 ASN 19.035 27.353 69.675 40 PHE 18.574 24.907 66.789 41 ILE 21.723 24.102 64.824 42 LYS 21.230 22.664 61.316 43 ASP 24.615 21.518 60.020 44 LYS 24.694 19.782 56.641 45 SER 28.155 18.430 57.484 46 TYR 26.851 16.421 60.461 47 ASP 24.383 13.536 60.643 48 LYS 22.642 14.867 63.759 49 ASP 20.482 17.912 64.573 50 THR 21.672 19.844 67.555 51 LEU 19.602 21.828 70.027 52 VAL 21.318 24.080 72.530 53 LEU 18.844 24.950 75.248 54 LYS 19.755 27.798 77.586 55 ALA 17.609 27.841 80.740 56 THR 17.519 31.102 82.673 57 GLY 15.076 33.147 84.701 58 ASN 14.373 33.240 88.409 59 ILE 13.669 30.957 91.389 60 ASN 12.633 32.829 94.564 61 SER 14.182 31.571 97.816 62 GLY 10.836 31.357 99.596 63 PHE 12.509 32.959 102.629 64 VAL 10.158 33.797 105.533 65 LYS 11.360 36.177 108.313 66 PRO 10.939 35.078 111.921 67 ASN 8.142 36.636 114.064 68 PRO 10.074 39.120 116.285 69 ASN 7.655 38.412 119.175 70 ASP 8.622 34.724 119.499 71 TYR 10.346 34.577 122.939 72 ASP 11.806 31.135 123.714 73 PHE 11.264 29.408 120.363 74 SER 11.404 30.820 116.836 75 LYS 11.858 29.717 113.261 76 LEU 12.503 31.008 109.776 77 TYR 12.359 29.387 106.326 78 TRP 15.230 29.747 103.899 79 GLY 16.081 28.724 100.329 80 ALA 18.495 25.881 100.879 81 LYS 18.713 24.209 97.462 82 TYR 17.712 25.081 93.922 83 ASN 17.088 22.297 91.434 84 VAL 16.732 22.745 87.685 85 SER 15.975 19.589 85.612 86 ILE 15.673 18.970 81.851 87 SER 14.175 15.735 80.540 88 SER 13.723 14.331 77.021 89 GLN 10.276 12.728 77.465 90 SER 9.754 10.979 74.151 91 ASN 11.192 10.105 70.756 92 ASP 14.004 7.562 71.015 93 SER 15.979 9.471 68.361 94 VAL 16.610 12.370 70.777 95 ASN 19.239 12.232 73.559 96 VAL 20.759 14.683 76.088 97 VAL 24.415 14.577 74.967 98 ASP 26.157 17.526 76.648 99 TYR 25.630 20.338 79.156 100 ALA 27.132 23.154 81.250 101 PRO 28.049 23.104 84.003 102 LYS 29.311 19.572 83.438 103 ASN 31.065 19.112 86.805 104 GLN 30.567 19.990 90.521 105 ASN 31.417 23.643 91.170 106 GLU 31.620 25.576 94.452 107 GLU 33.021 28.842 93.043 108 PHE 31.153 32.021 93.975 109 GLN 30.624 32.758 90.275 110 VAL 30.085 29.883 87.841 111 GLN 31.142 30.847 84.326 112 ASN 31.373 28.430 81.400 113 THR 31.320 28.642 77.608 114 LEU 29.786 26.001 75.319 115 GLY 31.036 26.005 71.716 116 TYR 29.778 24.122 68.652 117 THR 32.210 23.523 65.769 118 PHE 31.166 22.981 62.111 119 GLY 31.065 19.178 62.000 120 GLY 29.290 18.569 65.312 121 ASP 31.975 18.989 68.000 122 ILE 30.742 20.348 71.352 123 SER 33.409 21.912 73.583 124 ILE 32.814 23.218 77.123 125 SER 35.365 25.497 78.771 126 ASN 35.793 27.389 82.029 127 GLY 35.161 31.129 81.953 128 LEU 33.408 33.391 79.435 129 THR 33.102 27.915 65.962 130 ALA 29.641 28.060 64.351 131 PHE 27.736 28.698 67.613 132 SER 28.700 29.814 71.113 133 GLU 26.842 30.384 74.427 134 THR 27.761 31.126 78.030 135 ILE 26.323 30.422 81.512 136 ASN 26.967 32.858 84.310 137 TYR 25.491 32.791 87.793 138 LYS 26.328 33.800 91.302 139 GLN 26.029 31.169 94.058 140 GLU 28.125 32.440 97.014 141 SER 28.146 29.933 99.930 142 TYR 26.409 27.331 97.735 143 ARG 27.583 24.448 95.565 144 THR 26.469 23.180 92.167 145 THR 26.292 19.429 91.658 146 LEU 24.918 17.347 88.815 147 SER 21.755 15.483 89.792 148 ARG 22.115 11.752 90.366 149 ASN 19.454 10.794 87.843 150 THR 21.446 12.384 84.984 151 ASN 21.505 9.978 82.032 152 TYR 21.193 9.896 78.189 153 LYS 17.788 11.642 78.209 154 ASN 18.045 13.661 81.456 155 VAL 20.207 16.362 83.006 156 GLY 19.819 18.250 86.269 157 TRP 21.719 20.551 88.615 158 GLY 21.392 21.307 92.283 159 VAL 22.674 24.584 93.743 160 GLU 22.766 23.832 97.464 161 ALA 23.801 25.616 100.682 162 HIS 27.412 24.524 101.221 163 LYS 29.814 26.644 103.314 164 ILE 27.954 29.365 105.215 165 MET 29.815 31.580 107.710 166 ASN 27.919 33.299 110.535 167 ASN 30.618 35.847 111.476 168 GLY 33.972 34.127 111.854 169 TRP 32.117 30.982 112.891 170 GLY 31.690 28.081 110.492 171 PRO 31.451 27.138 107.782 172 TYR 28.009 25.597 108.351 173 GLY 25.674 23.578 106.154 174 ARG 22.149 22.163 106.163 175 ASP 23.557 19.216 108.081 176 SER 25.874 20.772 110.652 177 PHE 25.317 20.002 114.315 178 HIS 27.153 20.929 117.490 179 PRO 26.531 18.343 120.255 180 THR 25.243 21.175 122.488 181 TYR 24.157 24.081 120.259 182 GLY 22.702 22.071 117.380 183 ASN 22.749 23.642 113.907 184 GLU 24.159 27.167 114.371 185 LEU 23.708 28.278 110.759 186 PHE 21.709 31.414 111.507 187 LEU 22.036 31.690 115.319 188 ALA 23.167 35.173 116.400 189 GLY 24.338 34.222 119.888 190 ARG 24.571 31.170 122.111 191 GLN 23.701 33.185 125.264 192 SER 21.799 36.201 123.898 193 SER 19.457 37.883 126.342 194 ALA 16.982 38.314 123.523 195 TYR 13.696 37.197 122.091 196 ALA 14.078 34.008 120.028 197 GLY 12.486 35.891 117.144 198 GLN 15.285 38.416 117.461 199 ASN 18.227 36.008 117.870 200 PHE 19.002 35.081 114.250 201 ILE 21.730 36.831 112.258 202 ALA 20.594 39.684 110.010 203 GLN 19.290 38.918 106.529 204 HIS 22.201 40.799 104.940 205 GLN 24.577 38.451 106.762 206 MET 22.921 35.433 105.153 207 PRO 23.839 34.303 101.620 208 LEU 21.863 36.042 98.828 209 LEU 20.525 32.624 97.677 210 SER 19.229 31.732 101.118 211 ARG 17.068 34.836 101.609 212 SER 16.610 36.404 98.164 213 ASN 16.528 34.282 94.987 214 PHE 18.560 32.323 92.444 215 ASN 18.946 33.391 88.805 216 PRO 19.834 30.149 87.005 217 GLU 21.913 29.860 83.824 218 PHE 22.178 26.314 82.528 219 LEU 22.865 24.808 79.117 220 SER 21.823 21.414 77.801 221 VAL 22.573 19.952 74.364 222 LEU 19.965 17.663 72.859 223 SER 20.839 15.603 69.816 224 HIS 18.393 14.207 67.220 225 ARG 19.544 11.154 65.169 226 GLN 17.905 12.328 61.886 227 ASP 15.834 9.179 61.731 228 GLY 12.358 8.881 63.314 229 ALA 9.828 11.588 64.453 230 LYS 10.499 15.306 63.818 231 LYS 8.997 16.372 67.159 232 SER 9.961 15.368 70.690 233 LYS 8.751 16.158 74.213 234 ILE 10.826 17.990 76.819 235 THR 10.105 19.011 80.425 236 VAL 11.964 21.730 82.318 237 THR 11.625 21.859 86.135 238 TYR 12.722 24.711 88.442 239 GLN 12.462 23.911 92.147 240 ARG 13.440 25.144 95.605 241 GLU 13.985 23.122 98.736 242 MET 13.181 25.304 101.724 243 ASP 14.664 24.452 105.130 244 LEU 12.984 25.213 108.429 245 TYR 15.640 26.758 110.680 246 GLN 14.681 27.106 114.320 247 ILE 16.235 28.212 117.565 248 ARG 15.178 27.586 121.135 249 TRP 16.202 28.743 124.618 250 ASN 16.250 25.902 127.149 251 GLY 16.895 28.103 130.184 252 PHE 20.692 27.853 129.735 253 TYR 21.681 28.368 126.120 254 TRP 20.348 28.709 122.582 255 ALA 20.374 25.731 120.204 256 GLY 19.472 25.603 116.511 257 ALA 17.841 22.903 114.397 258 ASN 17.553 22.764 110.638 259 TYR 14.772 20.694 109.027 260 LYS 16.065 19.810 105.551 261 ASN 13.574 20.304 102.625 262 PHE 10.628 20.938 105.000 263 LYS 8.743 22.719 102.186 264 THR 9.158 22.219 98.413 265 ARG 7.837 24.395 95.573 266 THR 8.117 23.022 92.040 267 PHE 7.291 24.426 88.614 268 LYS 7.420 22.138 85.557 269 SER 6.793 23.127 81.945 270 THR 6.329 20.611 79.101 271 TYR 7.144 21.585 75.539 272 GLU 6.830 19.868 72.195 273 ILE 9.989 20.517 70.201 274 ASP 9.517 20.709 66.405 275 TRP 13.018 19.975 65.055 276 GLU 11.893 20.382 61.403 277 ASN 10.343 23.822 61.913 278 HIS 12.629 24.933 64.789 279 LYS 9.634 25.829 66.922 280 VAL 8.465 24.853 70.408 281 LYS 4.934 24.616 71.716 282 LEU 3.804 24.727 75.336 283 LEU 1.914 21.545 76.166 284 ASP 1.538 21.875 79.927 285 THR 2.579 23.659 83.132 286 LYS 2.286 22.215 86.642 287 GLU 2.812 23.753 90.062 288 THR 3.403 21.254 92.841 289 GLU 4.063 21.737 96.531 290 ASN 5.392 19.606 99.283 291 ASN 4.809 20.546 102.951 292 LYS 6.037 18.363 105.865 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S/S S S S 10 S S S/T T T T/S S S S S 20 S S S S S S S/T T T T 30 S S S S S S S S S S 40 S S S/T T T T S S S S 50 S S S S S S S S/S S S 60 S S S S S S S C C T 70 T T T S S S S S S S 80 S S S S S S S S S S 90 C C S S S S C C C C/P 100 C S S S S S C S S S 110 S S S S S S S/T T T T/S 120 S S S S S S S CPX X/C S 130 S S S/S S S S S S S/T T 140 T T/S S S S S S C C C 150 T T T T/S S S S S S S 160 S S S S S/T T T T C C/P 170 S S S S/S S S S S/T T T 180 T C C C S S S S C S 190 S S S C T T T T S S 200 S S/T T T T C H H H H 210 H H S S S S S S S S 220 S S S S S S C C C S 230 S S S S S S S S S S 240 S S S S S S S S S/T T 250 T T/S S S S S S S S S 260 S S S S S S S S S S 270 S S S S/T T T T S S S 280 S S S S/S S S S S S S 290 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E e E E E 10 E e S S e E E E E E 20 E E E E E E E T T T 30 e E E E E E E E E E 40 E E E e T t S S E E 50 E E E E E E E E E E 60 e B t T T t 70 e E E E E E E E E 80 E E E E E E E E e S 90 t T e E E E E E E E 100 S S B e E E 110 E E E E E E e T T t 120 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 T T t 150 B T e E E E E E E E 160 E e B S S S S 170 B t T T t B T T 180 T B t T T B S S 190 S S g G G G g B 200 g G G G g h H H H 210 H h E E E E E 220 E E E E e S S S e 230 E E E E E E E E E E 240 E E E E E E E E E e 250 S S e E E E E E E E 260 E E E E E E E E E E 270 E E E E e T T T E E 280 E E E E E E E E E E 290 E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 69.8 50.3 85.0 2 GLY 19.7 56.5 69.8 3 LYS 28.5 16.4 76.6 4 ILE 105.4 73.5 63.7 5 THR 62.6 58.6 64.4 6 PRO 9.5 7.6 83.8 7 VAL 102.1 85.9 53.4 8 SER 22.9 27.4 72.4 9 VAL 39.7 33.4 68.3 10 LYS 44.6 25.7 73.3 11 LYS 53.6 30.9 80.0 12 VAL 101.1 85.1 53.1 13 ASP 40.5 36.6 67.5 14 ASP 46.3 41.9 77.3 15 LYS 145.5 83.9 59.8 16 VAL 118.8 100.0 40.5 17 THR 83.2 77.9 50.8 18 LEU 123.1 83.3 42.0 19 TYR 141.4 78.1 47.8 20 LYS 83.5 48.2 76.7 21 THR 105.2 98.5 49.0 22 THR 76.9 71.9 62.1 23 ALA 72.6 100.0 44.4 24 THR 72.7 68.0 67.1 25 ALA 72.6 100.0 52.1 26 ASP 74.9 67.8 66.3 27 SER 82.9 99.2 49.0 28 ASP 0.0 0.0 85.2 29 LYS 51.8 29.9 82.8 30 PHE 162.1 97.2 49.9 31 LYS 40.4 23.3 86.6 32 ILE 143.5 100.0 44.5 33 SER 54.5 65.1 60.8 34 GLN 148.6 100.0 43.6 35 ILE 77.6 54.1 74.3 36 LEU 147.8 100.0 40.4 37 THR 86.6 81.0 58.3 38 PHE 166.8 100.0 24.1 39 ASN 117.7 97.4 38.0 40 PHE 165.6 99.3 41.3 41 ILE 143.5 100.0 33.6 42 LYS 127.4 73.5 65.7 43 ASP 110.3 99.8 53.7 44 LYS 36.0 20.8 87.0 45 SER 36.2 43.3 70.4 46 TYR 168.0 92.8 76.6 47 ASP 2.0 1.9 82.4 48 LYS 81.8 47.2 74.7 49 ASP 94.9 85.9 59.3 50 THR 95.7 89.5 44.6 51 LEU 147.8 100.0 27.7 52 VAL 118.8 100.0 31.0 53 LEU 147.8 100.0 35.4 54 LYS 141.9 81.8 62.7 55 ALA 72.3 99.6 42.7 56 THR 82.4 77.1 53.5 57 GLY 31.0 89.1 54.7 58 ASN 82.3 68.1 65.4 59 ILE 143.5 100.0 38.5 60 ASN 87.2 72.1 66.6 61 SER 82.7 98.9 61.1 62 GLY 25.0 71.9 72.5 63 PHE 154.0 92.4 52.4 64 VAL 37.7 31.7 74.6 65 LYS 33.0 19.0 76.7 66 PRO 102.6 82.4 56.5 67 ASN 44.3 36.6 77.0 68 PRO 58.3 46.8 80.2 69 ASN 22.0 18.2 77.3 70 ASP 71.3 64.5 71.9 71 TYR 54.6 30.2 77.1 72 ASP 49.5 44.8 58.1 73 PHE 97.6 58.5 70.0 74 SER 82.9 99.1 45.2 75 LYS 90.1 52.0 59.9 76 LEU 144.0 97.5 31.1 77 TYR 163.9 90.6 42.6 78 TRP 205.0 100.0 36.9 79 GLY 34.7 99.8 58.3 80 ALA 72.6 100.0 53.4 81 LYS 129.2 74.5 68.7 82 TYR 180.9 99.9 40.8 83 ASN 95.4 78.9 63.0 84 VAL 117.8 99.2 32.1 85 SER 40.7 48.6 62.2 86 ILE 142.1 99.0 32.8 87 SER 69.4 83.0 74.7 88 SER 83.0 99.3 50.9 89 GLN 84.2 56.6 71.3 90 SER 34.8 41.6 70.0 91 ASN 103.8 85.8 61.2 92 ASP 29.5 26.7 87.4 93 SER 76.4 91.4 64.1 94 VAL 118.8 100.0 54.8 95 ASN 86.5 71.5 54.8 96 VAL 118.7 100.0 47.1 97 VAL 73.9 62.2 66.7 98 ASP 66.4 60.1 46.1 99 TYR 136.2 75.2 43.5 100 ALA 72.6 100.0 38.0 101 PRO 122.3 98.3 50.4 102 LYS 75.9 43.8 65.3 103 ASN 14.4 11.9 78.9 104 GLN 74.2 50.0 70.5 105 ASN 93.7 77.5 58.3 106 GLU 82.7 59.7 74.4 107 GLU 31.5 22.7 85.1 108 PHE 53.9 32.3 78.8 109 GLN 90.7 61.0 66.1 110 VAL 118.5 99.7 54.0 111 GLN 93.8 63.2 58.9 112 ASN 108.3 89.6 52.0 113 THR 82.3 77.0 71.0 114 LEU 147.8 100.0 31.5 115 GLY 27.2 78.1 60.7 116 TYR 180.1 99.5 41.3 117 THR 52.3 48.9 64.8 118 PHE 105.7 63.4 60.9 119 GLY 15.2 43.7 82.4 120 GLY 23.8 68.5 66.4 121 ASP 27.9 25.3 83.5 122 ILE 133.2 92.8 46.0 123 SER 24.7 29.5 80.0 124 ILE 134.4 93.6 49.6 125 SER 23.9 28.6 77.6 126 ASN 12.5 10.3 87.8 127 GLY 16.7 47.9 73.8 128 LEU 81.4 55.1 70.2 129 THR 42.9 40.1 77.5 130 ALA 72.3 99.6 37.3 131 PHE 149.1 89.4 41.7 132 SER 39.6 47.3 66.2 133 GLU 106.0 76.4 57.9 134 THR 66.3 62.0 64.8 135 ILE 143.5 100.0 42.6 136 ASN 74.0 61.2 63.5 137 TYR 175.3 96.8 46.2 138 LYS 51.0 29.4 81.7 139 GLN 148.6 100.0 48.1 140 GLU 64.8 46.8 61.5 141 SER 65.3 78.1 47.3 142 TYR 181.0 100.0 41.9 143 ARG 130.0 62.2 68.9 144 THR 106.9 100.0 46.2 145 THR 72.7 68.0 68.2 146 LEU 125.2 84.7 59.5 147 SER 53.7 64.2 81.3 148 ARG 0.0 0.0 94.9 149 ASN 9.6 7.9 83.9 150 THR 91.0 85.1 66.0 151 ASN 48.3 39.9 74.6 152 TYR 55.5 30.7 79.7 153 LYS 130.1 75.0 69.4 154 ASN 81.0 67.0 72.3 155 VAL 118.8 100.0 30.0 156 GLY 34.2 98.2 57.6 157 TRP 204.8 99.9 35.7 158 GLY 32.3 92.9 65.7 159 VAL 117.8 99.1 37.2 160 GLU 101.6 73.3 63.8 161 ALA 72.6 100.0 35.6 162 HIS 121.2 80.7 63.0 163 LYS 68.8 39.7 71.2 164 ILE 142.5 99.3 42.6 165 MET 80.5 50.5 72.9 166 ASN 104.6 86.6 56.2 167 ASN 58.5 48.4 85.7 168 GLY 0.0 0.0 76.5 169 TRP 161.0 78.5 72.8 170 GLY 32.3 92.7 51.8 171 PRO 70.0 56.2 56.6 172 TYR 145.4 80.3 60.7 173 GLY 30.7 88.2 69.6 174 ARG 204.0 97.6 50.3 175 ASP 13.6 12.3 81.8 176 SER 54.4 65.1 70.7 177 PHE 58.0 34.8 79.2 178 HIS 82.9 55.2 64.9 179 PRO 24.5 19.6 79.5 180 THR 59.2 55.4 61.5 181 TYR 141.2 78.0 55.6 182 GLY 32.8 94.2 56.0 183 ASN 117.9 97.6 54.7 184 GLU 127.2 91.7 55.8 185 LEU 147.8 100.0 39.6 186 PHE 166.7 99.9 23.6 187 LEU 145.8 98.6 54.4 188 ALA 47.9 66.0 70.8 189 GLY 15.5 44.5 81.9 190 ARG 111.3 53.3 67.0 191 GLN 59.4 40.0 70.1 192 SER 54.6 65.3 66.7 193 SER 0.0 0.0 88.8 194 ALA 43.7 60.1 68.4 195 TYR 85.7 47.3 70.6 196 ALA 72.6 100.0 48.1 197 GLY 34.8 100.0 53.9 198 GLN 49.7 33.5 73.5 199 ASN 118.6 98.1 46.6 200 PHE 160.8 96.4 46.6 201 ILE 137.1 95.5 56.9 202 ALA 36.2 49.9 74.2 203 GLN 87.0 58.5 54.4 204 HIS 34.1 22.7 76.9 205 GLN 78.4 52.8 69.7 206 MET 157.8 99.0 34.4 207 PRO 112.2 90.1 52.3 208 LEU 46.4 31.4 82.6 209 LEU 138.4 93.6 44.4 210 SER 83.6 100.0 39.7 211 ARG 156.5 74.9 53.0 212 SER 53.9 64.4 72.5 213 ASN 87.6 72.5 81.7 214 PHE 166.4 99.7 31.6 215 ASN 43.0 35.5 76.6 216 PRO 124.5 100.0 37.8 217 GLU 100.3 72.4 55.2 218 PHE 166.4 99.8 29.4 219 LEU 147.7 100.0 39.0 220 SER 83.5 99.8 30.5 221 VAL 118.4 99.7 35.1 222 LEU 147.5 99.8 36.4 223 SER 75.5 90.3 47.0 224 HIS 146.2 97.4 52.7 225 ARG 105.8 50.6 74.0 226 GLN 87.3 58.8 78.2 227 ASP 55.2 50.0 84.6 228 GLY 1.8 5.1 84.9 229 ALA 19.4 26.7 83.6 230 LYS 61.2 35.3 77.3 231 LYS 77.3 44.6 77.2 232 SER 80.7 96.6 54.8 233 LYS 84.5 48.8 63.0 234 ILE 143.5 100.0 30.4 235 THR 99.8 93.3 54.4 236 VAL 118.8 100.0 40.0 237 THR 80.6 75.4 54.6 238 TYR 181.0 100.0 37.2 239 GLN 109.4 73.6 57.0 240 ARG 193.6 92.7 44.2 241 GLU 115.0 83.0 67.8 242 MET 149.4 93.7 54.3 243 ASP 110.5 100.0 54.5 244 LEU 138.6 93.7 43.0 245 TYR 181.0 100.0 41.5 246 GLN 129.2 87.0 43.3 247 ILE 143.1 99.7 40.6 248 ARG 86.9 41.6 68.9 249 TRP 140.6 68.6 67.4 250 ASN 65.4 54.1 63.3 251 GLY 10.5 30.3 64.7 252 PHE 25.2 15.1 80.0 253 TYR 121.6 67.2 61.2 254 TRP 202.1 98.6 48.2 255 ALA 46.7 64.4 65.4 256 GLY 34.8 100.0 60.8 257 ALA 37.6 51.8 63.0 258 ASN 120.7 99.8 49.3 259 TYR 85.7 47.4 67.2 260 LYS 74.2 42.8 78.8 261 ASN 85.3 70.6 70.6 262 PHE 125.0 74.9 53.5 263 LYS 119.1 68.7 63.6 264 THR 93.4 87.4 69.2 265 ARG 177.1 84.8 54.5 266 THR 89.2 83.5 55.3 267 PHE 164.5 98.6 47.7 268 LYS 102.7 59.2 71.3 269 SER 83.5 99.9 46.3 270 THR 96.2 90.0 45.1 271 TYR 179.8 99.4 35.6 272 GLU 99.8 72.0 51.9 273 ILE 143.3 99.9 36.1 274 ASP 93.4 84.5 54.0 275 TRP 203.5 99.2 43.7 276 GLU 58.7 42.4 77.2 277 ASN 52.4 43.3 71.6 278 HIS 129.0 85.9 43.8 279 LYS 49.0 28.3 69.9 280 VAL 118.3 99.6 29.7 281 LYS 52.7 30.4 73.9 282 LEU 103.5 70.0 55.0 283 LEU 109.8 74.3 52.8 284 ASP 37.6 34.0 70.2 285 THR 76.6 71.7 55.5 286 LYS 55.3 31.9 72.9 287 GLU 87.4 63.1 57.3 288 THR 55.4 51.8 63.7 289 GLU 94.7 68.3 70.1 290 ASN 40.4 33.4 75.2 291 ASN 72.9 60.3 73.3 292 LYS 70.9 40.9 80.6