Protein Data Bank File : 1cby Title : TOXIN 05-SEP-95 1CBY Number of Amino Acid Residues : 227 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 CYS SER ALA PRO ILE ILE ARG LYS PRO PHE 10 LYS HIS ILE VAL LEU THR VAL PRO SER SER 20 ASP LEU ASP ASN PHE ASN THR VAL PHE TYR 30 VAL GLN PRO GLN TYR ILE ASN GLN ALA LEU 40 HIS LEU ALA ASN ALA PHE GLN GLY ALA ILE 50 ASP PRO LEU ASN LEU ASN PHE ASN PHE GLU 60 LYS ALA LEU GLN ILE ALA ASN GLY ILE PRO 70 ASN SER ALA ILE VAL LYS THR LEU ASN GLN 80 SER VAL ILE GLN GLN THR VAL GLU ILE SER 90 VAL MET VAL GLU GLN LEU LYS LYS ILE ILE 100 GLN GLU VAL LEU GLY LEU VAL ILE ASN SER 110 THR SER PHE TRP ASN SER VAL GLU ALA THR 120 ILE LYS GLY THR PHE THR ASN LEU ASP THR 130 GLN ILE ASP GLU ALA TRP ILE PHE TRP HIS 140 SER LEU SER ALA HIS ASN THR SER TYR TYR 150 TYR ASN ILE LEU PHE SER ILE GLN ASN GLU 160 ASP THR GLY ALA VAL MET ALA VAL LEU PRO 170 LEU ALA PHE GLU VAL SER VAL ASP VAL GLU 180 LYS GLN LYS VAL LEU PHE PHE THR ILE LYS 190 ASP SER ALA ARG TYR GLU VAL LYS MET LYS 200 ALA LEU THR LEU VAL GLN ALA LEU HIS SER 210 SER ASN ALA PRO ILE VAL ASP ILE PHE ASN 220 VAL ASN ASN TYR ASN LEU TYR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 CYS 0.0 -179.1 -179.7 -62.8 2 SER -73.5 130.4 178.9 34.8 3 ALA -81.5 145.1 -179.9 4 PRO -60.1 140.1 179.6 30.6 -44.5 5 ILE -75.5 130.6 -178.6 -64.6 176.9 6 ILE -106.4 146.0 -180.0 -52.7 -55.5 7 ARG -131.2 163.9 -179.8 -62.3 178.0 -176.3 -146.6 8 LYS -58.8 125.6 -179.7 -144.4 -143.1 79.1 62.5 9 PRO -69.7 137.4 179.3 33.7 -44.2 10 PHE -138.2 146.3 177.5 -80.8 87.7 11 LYS -95.2 138.2 178.6 -71.7 -170.8 169.8 -57.3 12 HIS -120.0 94.8 -177.8 -170.6 -102.4 13 ILE -114.5 119.2 176.5 -52.8 169.1 14 VAL -89.2 106.5 -178.4 -175.2 15 LEU -97.7 123.2 176.5 -121.8 -165.5 16 THR -124.6 103.9 -177.9 -52.7 17 VAL -128.7 139.6 179.8 68.7 18 PRO -58.2 128.6 -177.9 19.7 -38.0 19 SER -89.7 152.6 178.7 -174.2 20 SER -83.6 -15.7 -179.6 -73.1 21 ASP -144.4 177.5 -178.4 -140.6 -41.7 22 LEU -66.6 140.0 -179.9 -57.2 -178.9 23 ASP -138.1 108.5 179.7 -166.0 -26.2 24 ASN -114.8 34.3 -179.1 -61.3 105.7 25 PHE -124.4 136.9 175.3 -92.2 -62.1 26 ASN -89.2 106.0 -176.3 -164.1 171.0 27 THR -92.2 135.2 178.6 -44.5 28 VAL -128.6 116.6 -179.2 174.3 29 PHE -114.7 123.1 176.9 -80.3 2.2 30 TYR -124.9 83.4 -177.5 -174.8 -80.6 31 VAL -146.1 178.7 178.2 -58.1 32 GLN -95.4 151.8 -179.6 -68.8 174.6 -127.8 33 PRO -44.5 -50.8 -179.0 -32.8 45.1 34 GLN -64.2 -6.8 -179.9 60.8 -91.1 81.3 35 TYR -115.3 6.1 179.7 -61.5 -66.1 36 ILE -64.8 -40.7 179.9 -73.0 173.0 37 ASN -59.1 -45.9 179.5 -157.3 164.6 38 GLN -61.4 -44.4 179.9 179.0 177.2 4.4 39 ALA -61.8 -44.0 -179.4 40 LEU -63.5 -38.2 178.7 -143.3 39.9 41 HIS -63.2 -50.6 179.8 -87.3 54.8 42 LEU -59.7 -40.1 179.2 -74.0 153.4 43 ALA -60.8 -53.2 -179.9 44 ASN -58.7 -39.1 -179.8 -69.5 -7.7 45 ALA -58.7 -36.5 -179.7 46 PHE -81.1 -0.6 177.6 -74.9 -70.8 47 GLN -64.6 -38.9 -179.5 -69.2 -72.3 -9.0 48 GLY -58.5 -9.5 179.7 49 ALA -82.8 -18.2 179.4 50 ILE -86.9 118.1 179.3 -45.5 -64.2 51 ASP -62.6 119.0 -179.4 -169.4 -60.0 52 PRO -56.7 -25.4 -179.4 30.4 -43.7 53 LEU -96.0 -50.4 180.0 -68.3 174.3 54 ASN -95.8 -1.3 178.9 33.0 -57.5 55 LEU 54.5 24.1 179.2 -71.9 173.1 56 ASN -95.6 147.0 179.2 -170.7 43.2 57 PHE -78.3 125.1 -179.7 -173.1 83.6 58 ASN -99.5 106.0 -179.4 -172.6 -70.0 59 PHE -57.0 -45.6 -179.4 -168.8 58.6 60 GLU -55.9 -49.0 -179.7 -63.3 -61.6 -17.6 61 LYS -68.9 -29.1 178.6 -164.9 179.6 179.5 -178.4 62 ALA -61.9 -42.3 178.8 63 LEU -67.2 -43.2 178.6 -94.3 42.7 64 GLN -55.2 -47.4 179.4 143.4 106.4 36.3 65 ILE -66.8 -43.2 -179.8 -62.9 171.9 66 ALA -55.5 -52.9 -179.6 67 ASN -70.8 9.3 179.6 -69.6 135.3 68 GLY -115.0 -14.9 179.6 69 ILE -68.3 128.3 179.9 -55.1 -66.6 70 PRO -72.1 141.6 178.5 29.6 -43.3 71 ASN 58.1 51.5 -179.2 -46.8 -39.5 72 SER -144.1 179.1 179.4 53.8 73 ALA -158.0 138.0 179.9 74 ILE -82.9 111.7 -179.1 -59.6 178.5 75 VAL -71.2 -58.9 -178.2 172.5 76 LYS -152.6 146.5 179.4 -154.7 -88.0 -178.2 177.2 77 THR -124.6 166.4 179.2 58.6 78 LEU -159.0 145.6 -179.9 -175.2 82.5 79 ASN -166.3 90.8 -178.7 176.0 -154.8 80 GLN -174.9 169.4 178.4 62.5 179.0 72.2 81 SER -73.0 126.3 -178.9 -68.7 82 VAL -110.6 -14.1 179.6 -62.3 83 ILE -144.1 120.9 179.2 -59.3 -75.1 84 GLN -143.4 77.5 -178.7 -57.5 178.8 158.7 85 GLN -176.7 171.7 176.7 69.2 -172.7 86.9 86 THR -82.9 127.8 -179.7 -59.3 87 VAL -147.9 159.2 177.2 -102.5 88 GLU -88.3 130.4 -178.5 -176.5 177.5 -28.7 89 ILE -49.4 -38.7 179.4 -59.9 173.2 90 SER -53.9 -52.8 -179.2 58.0 91 VAL -60.7 -40.1 -179.4 -171.2 92 MET -62.2 -40.4 179.8 178.8 163.8 58.6 93 VAL -58.4 -38.2 179.7 174.5 94 GLU -64.8 -45.0 179.1 -68.0 176.3 -31.1 95 GLN -59.0 -52.4 -179.2 -124.6 -59.4 -100.7 96 LEU -59.9 -39.6 179.3 -56.5 176.2 97 LYS -63.3 -35.9 179.9 -177.8 -177.8 -162.9 170.4 98 LYS -73.4 -36.4 179.1 -160.9 176.0 -172.7 -64.5 99 ILE -69.3 -37.0 178.4 -60.8 176.3 100 ILE -65.1 -48.1 179.3 -69.2 177.5 101 GLN -51.7 -45.9 179.7 -178.2 -164.3 53.4 102 GLU -62.4 -55.8 -179.2 -175.0 65.4 73.2 103 VAL -59.5 -32.9 -179.8 173.0 104 LEU -63.4 -32.7 179.2 -173.9 53.0 105 GLY 74.5 -67.6 179.7 106 LEU -61.5 135.1 179.5 -54.8 -42.1 107 VAL -92.5 115.5 -179.0 -64.8 108 ILE -101.3 135.4 179.2 -52.4 -61.3 109 ASN -107.0 93.7 179.2 -81.2 -66.2 110 SER -165.4 117.4 179.0 -169.9 111 THR -61.5 -48.4 179.3 -54.5 112 SER -55.3 -45.8 -179.9 -66.4 113 PHE -59.2 -54.0 -179.7 173.7 72.0 114 TRP -64.3 -22.1 177.3 -67.3 110.5 115 ASN -76.2 -38.6 178.7 -84.6 170.6 116 SER -63.2 -44.7 179.1 -63.1 117 VAL -59.7 -47.6 -179.4 170.1 118 GLU -66.3 -45.0 179.2 -162.3 -178.1 42.1 119 ALA -57.7 -46.7 178.9 120 THR -60.1 -43.8 180.0 -67.4 121 ILE -62.9 -44.4 178.9 -59.1 -52.9 122 LYS -59.1 -40.0 -179.4 -70.8 -177.8 177.0 178.6 123 GLY -66.6 -14.9 179.4 124 THR -78.3 -16.8 -178.9 -60.6 125 PHE -124.9 -18.8 -179.1 -55.1 -84.7 126 THR -123.5 160.7 -179.9 53.7 127 ASN 58.8 32.5 179.5 -72.6 -32.7 128 LEU -68.3 -23.4 178.9 -70.3 -178.2 129 ASP -61.5 -28.9 -179.7 62.1 -45.5 130 THR -91.1 0.3 -179.3 -39.9 131 GLN -119.3 14.8 -179.7 -58.3 179.0 56.1 132 ILE -74.5 130.7 -180.0 -164.9 166.0 133 ASP 84.6 14.8 178.5 -63.8 -19.6 134 GLU -92.6 147.2 -177.9 -59.4 -70.2 -0.8 135 ALA -63.1 -27.2 -178.6 136 TRP -75.8 -6.6 179.1 60.2 83.2 137 ILE -125.2 125.4 -179.8 179.3 170.2 138 PHE -123.8 112.3 179.6 178.5 69.2 139 TRP -80.9 165.5 178.9 -51.4 86.8 140 HIS -179.4 174.9 -179.6 65.0 86.6 141 SER 46.9 22.4 -179.0 -54.6 142 LEU -57.3 138.2 179.7 -60.8 -171.3 143 SER -154.7 177.3 178.8 -56.0 144 ALA -80.9 -15.1 -179.8 145 HIS -117.1 6.0 -178.7 -49.8 -48.5 146 ASN -160.9 149.0 178.8 -177.2 -86.0 147 THR -143.3 123.4 -180.0 -62.3 148 SER -123.9 156.0 179.2 -62.6 149 TYR -168.4 160.8 178.6 57.6 87.4 150 TYR -108.8 140.4 179.2 -65.2 -40.5 151 TYR -135.7 117.5 -178.5 -158.3 -73.3 152 ASN -107.1 131.5 -178.8 -52.6 -41.8 153 ILE -132.6 149.9 177.5 -60.6 169.8 154 LEU -141.2 120.2 179.4 -177.5 124.2 155 PHE -103.2 140.7 177.7 -67.1 -70.0 156 SER -137.1 112.3 -177.3 -167.6 157 ILE -122.3 133.7 -179.7 162.0 72.5 158 GLN -153.2 119.4 179.5 171.4 -84.6 -55.6 159 ASN -162.2 -165.4 -179.8 71.5 -5.9 160 GLU -55.2 -37.3 -179.4 -52.0 79.3 54.9 161 ASP -68.4 -37.0 -179.6 -51.8 -64.7 162 THR -72.6 -25.9 178.7 48.9 163 GLY 71.5 -115.4 -178.1 164 ALA -88.0 2.5 180.0 165 VAL -133.5 164.9 177.9 -63.0 166 MET -112.2 141.8 179.8 175.2 178.4 -84.1 167 ALA -106.9 129.0 179.3 168 VAL -118.3 139.9 -178.9 -174.7 169 LEU -136.4 90.9 179.0 -148.4 -174.4 170 PRO -74.4 115.4 -178.5 -29.5 44.4 171 LEU -120.8 129.5 179.4 176.0 71.2 172 ALA -135.4 128.7 179.7 173 PHE -108.2 136.4 175.8 -72.6 -66.8 174 GLU -109.6 103.2 -177.9 -68.9 -169.4 8.1 175 VAL -101.6 141.9 178.5 -174.4 176 SER -139.5 130.4 -179.0 178.4 177 VAL -128.3 143.3 -179.8 -161.2 178 ASP -79.3 34.9 179.3 68.0 -34.2 179 VAL -140.5 174.3 -179.7 -65.4 180 GLU -88.1 141.9 -179.2 57.0 -176.7 56.7 181 LYS -42.7 -38.8 179.8 178.4 169.8 148.4 170.2 182 GLN -60.8 -31.2 178.7 -91.5 -62.2 -72.8 183 LYS -81.5 -44.0 179.0 -69.0 -169.4 173.4 -178.6 184 VAL -56.8 -43.0 -179.4 173.1 185 LEU -55.5 -27.7 -179.2 -67.9 177.5 186 PHE -113.0 27.5 178.2 -63.8 -85.1 187 PHE -72.0 144.5 179.0 -95.1 2.7 188 THR -120.2 168.4 179.8 60.8 189 ILE -53.3 -27.2 -178.6 -74.4 -64.9 190 LYS -87.6 0.1 -178.7 -52.1 179.1 179.9 -176.0 191 ASP -85.3 152.5 -179.6 -76.1 -57.2 192 SER -121.2 155.0 179.1 -50.5 193 ALA -176.2 154.9 178.4 194 ARG -73.4 113.6 -178.9 160.0 72.9 168.6 169.4 195 TYR -110.5 146.0 176.4 -86.9 -88.5 196 GLU -130.1 114.2 -178.2 172.4 54.3 83.5 197 VAL -130.5 120.7 177.3 175.7 198 LYS -106.9 142.0 -178.3 179.0 161.7 -177.4 179.0 199 MET -125.1 135.4 179.2 -169.1 174.1 126.1 200 LYS -127.3 116.3 -177.7 -68.5 166.0 -72.0 176.8 201 ALA -154.0 157.0 178.1 202 LEU -156.8 140.3 179.1 78.2 163.4 203 THR -107.2 127.7 -179.6 -48.5 204 LEU -123.4 133.7 178.1 177.1 127.1 205 VAL -111.2 137.7 179.3 -65.9 206 GLN -131.2 141.1 -179.6 175.4 -174.5 53.8 207 ALA -53.8 135.3 -179.4 208 LEU -57.4 134.5 -179.5 -119.5 44.5 209 HIS -135.7 102.8 -178.9 -166.8 79.0 210 SER -72.2 144.7 179.5 -177.8 211 SER -153.9 126.7 179.2 172.3 212 ASN -117.9 45.0 -179.5 -173.8 24.3 213 ALA -71.2 161.8 179.6 214 PRO -61.0 124.8 -177.7 -32.8 45.4 215 ILE -43.6 -41.9 179.9 -169.7 175.1 216 VAL -67.2 -41.1 179.8 -179.2 217 ASP -56.2 -39.5 -179.7 -69.2 16.5 218 ILE -59.3 -49.2 -179.3 -65.3 -179.7 219 PHE -76.8 -1.9 178.5 -67.7 87.8 220 ASN -87.9 -13.9 -179.7 -85.3 -179.3 221 VAL -61.7 135.9 -179.8 178.3 222 ASN -102.6 -170.7 -179.5 57.1 -168.1 223 ASN -92.8 33.0 -178.1 -48.1 151.4 224 TYR -131.7 148.8 -179.4 -64.0 83.5 225 ASN 60.4 64.0 -179.4 -54.0 -55.9 226 LEU -128.8 -19.5 179.9 -64.2 -177.4 227 TYR -138.4 -38.7 0.0 61.3 -83.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 CYS 22.414 48.597 99.288 2 SER 21.227 45.104 98.364 3 ALA 23.724 42.956 96.463 4 PRO 22.397 41.065 93.390 5 ILE 21.160 37.513 93.957 6 ILE 23.425 34.947 92.292 7 ARG 22.492 31.547 90.837 8 LYS 24.380 28.568 89.406 9 PRO 25.680 29.665 85.979 10 PHE 24.408 27.991 82.810 11 LYS 25.140 28.816 79.191 12 HIS 22.142 29.412 76.945 13 ILE 23.356 28.955 73.377 14 VAL 21.072 28.779 70.349 15 LEU 23.286 26.765 68.014 16 THR 22.698 26.743 64.272 17 VAL 25.492 24.715 62.717 18 PRO 25.592 23.035 59.248 19 SER 24.630 19.352 59.511 20 SER 26.289 16.326 57.903 21 ASP 22.882 14.733 57.333 22 LEU 19.204 15.702 57.183 23 ASP 17.722 17.301 60.309 24 ASN 13.981 17.925 60.646 25 PHE 13.930 18.389 64.426 26 ASN 13.823 21.546 66.527 27 THR 16.356 20.356 69.096 28 VAL 16.537 21.328 72.787 29 PHE 19.466 19.992 74.848 30 TYR 19.731 20.291 78.641 31 VAL 22.807 18.155 79.318 32 GLN 26.461 18.282 80.390 33 PRO 29.307 18.701 77.834 34 GLN 30.585 15.131 78.162 35 TYR 27.111 13.822 77.285 36 ILE 26.464 16.033 74.259 37 ASN 27.807 13.311 71.950 38 GLN 25.356 10.791 73.419 39 ALA 22.479 13.244 73.054 40 LEU 23.424 14.008 69.449 41 HIS 23.542 10.294 68.648 42 LEU 20.074 9.718 70.101 43 ALA 18.766 12.772 68.257 44 ASN 20.095 11.586 64.871 45 ALA 18.767 8.070 65.406 46 PHE 15.248 9.461 65.625 47 GLN 15.601 11.346 62.332 48 GLY 14.676 8.066 60.673 49 ALA 11.205 8.386 62.172 50 ILE 10.425 11.326 59.857 51 ASP 9.129 10.071 56.495 52 PRO 11.509 11.551 53.856 53 LEU 8.683 12.110 51.363 54 ASN 5.601 13.218 53.321 55 LEU 7.590 14.588 56.272 56 ASN 5.247 13.059 58.849 57 PHE 6.538 11.536 62.079 58 ASN 5.931 7.796 61.971 59 PHE 5.180 6.521 65.463 60 GLU 5.537 2.870 64.462 61 LYS 9.027 3.361 63.068 62 ALA 9.819 5.544 66.093 63 LEU 9.102 2.516 68.299 64 GLN 11.105 0.259 65.976 65 ILE 14.090 2.605 66.364 66 ALA 13.444 2.973 70.106 67 ASN 13.547 -0.763 70.804 68 GLY 16.857 -0.916 68.946 69 ILE 18.895 1.645 70.884 70 PRO 21.444 -0.202 73.053 71 ASN 21.278 0.104 76.869 72 SER 17.974 1.959 77.067 73 ALA 14.305 1.559 77.990 74 ILE 11.047 3.118 76.776 75 VAL 9.458 4.917 79.724 76 LYS 6.121 6.089 78.318 77 THR 4.612 6.574 74.854 78 LEU 1.696 8.608 73.504 79 ASN -0.079 8.915 70.153 80 GLN -3.481 10.643 70.006 81 SER -5.512 13.837 69.615 82 VAL -4.905 16.024 72.648 83 ILE -6.782 19.189 71.644 84 GLN -10.073 19.304 69.705 85 GLN -11.816 22.586 70.500 86 THR -11.760 26.348 70.135 87 VAL -9.056 27.565 72.531 88 GLU -6.849 30.486 73.429 89 ILE -3.246 29.524 72.651 90 SER -2.186 30.484 76.188 91 VAL -4.476 27.876 77.733 92 MET -3.437 25.229 75.195 93 VAL 0.260 25.581 76.020 94 GLU -0.516 24.725 79.661 95 GLN -2.383 21.543 78.761 96 LEU 0.430 20.348 76.491 97 LYS 3.103 21.240 79.066 98 LYS 1.231 19.125 81.614 99 ILE 0.901 16.271 79.112 100 ILE 4.637 16.453 78.377 101 GLN 5.393 16.387 82.116 102 GLU 3.263 13.244 82.365 103 VAL 4.770 11.497 79.319 104 LEU 8.311 12.383 80.416 105 GLY 7.840 10.284 83.557 106 LEU 11.092 11.365 85.190 107 VAL 10.557 14.409 87.415 108 ILE 13.073 17.134 86.581 109 ASN 13.773 19.995 88.984 110 SER 14.797 22.992 86.905 111 THR 13.076 26.328 86.287 112 SER 15.195 26.850 83.174 113 PHE 14.261 23.428 81.805 114 TRP 10.523 23.903 82.242 115 ASN 10.860 27.404 80.797 116 SER 12.580 25.888 77.754 117 VAL 9.737 23.396 77.497 118 GLU 7.076 26.106 77.718 119 ALA 8.899 28.461 75.346 120 THR 9.255 25.627 72.813 121 ILE 5.553 24.731 73.111 122 LYS 4.556 28.361 72.589 123 GLY 6.787 28.430 69.510 124 THR 4.806 25.536 68.064 125 PHE 1.782 27.832 67.716 126 THR 3.126 31.405 67.729 127 ASN 5.806 33.345 65.857 128 LEU 5.496 30.919 62.955 129 ASP 6.278 33.860 60.671 130 THR 9.861 33.713 61.962 131 GLN 9.956 29.954 61.369 132 ILE 8.905 29.860 57.737 133 ASP 11.148 27.645 55.579 134 GLU 12.697 25.813 58.540 135 ALA 12.994 22.016 58.365 136 TRP 11.058 21.247 61.563 137 ILE 7.798 22.589 60.137 138 PHE 5.915 21.137 57.160 139 TRP 2.709 22.819 55.993 140 HIS -0.090 21.125 54.056 141 SER -3.858 21.055 53.434 142 LEU -3.706 24.854 53.192 143 SER -7.008 26.567 52.447 144 ALA -8.775 29.865 53.112 145 HIS -10.678 28.098 55.897 146 ASN -7.905 25.809 57.162 147 THR -4.174 25.566 57.834 148 SER -2.371 22.342 58.748 149 TYR 1.256 21.550 59.523 150 TYR 3.732 19.168 61.111 151 TYR 6.050 20.361 63.863 152 ASN 8.891 18.157 65.082 153 ILE 10.654 18.753 68.401 154 LEU 13.253 16.710 70.289 155 PHE 14.083 17.172 73.951 156 SER 17.225 15.670 75.466 157 ILE 17.585 16.032 79.249 158 GLN 20.375 14.927 81.594 159 ASN 21.163 16.228 85.081 160 GLU 21.253 15.417 88.804 161 ASP 17.597 14.363 88.633 162 THR 18.075 11.835 85.792 163 GLY 20.905 10.082 87.609 164 ALA 22.419 7.196 85.656 165 VAL 20.419 7.736 82.463 166 MET 19.676 10.388 79.856 167 ALA 16.100 11.102 78.830 168 VAL 15.199 11.668 75.172 169 LEU 11.788 12.831 74.014 170 PRO 10.967 12.822 70.263 171 LEU 7.837 14.981 70.068 172 ALA 5.753 15.666 66.956 173 PHE 2.555 17.670 66.677 174 GLU 0.078 17.412 63.810 175 VAL -1.692 20.779 63.951 176 SER -4.848 21.884 62.122 177 VAL -6.463 25.330 62.493 178 ASP -9.759 26.708 61.183 179 VAL -8.070 29.782 59.662 180 GLU -5.845 30.905 56.788 181 LYS -2.042 30.810 57.005 182 GLN -1.640 34.608 56.760 183 LYS -3.533 34.919 60.041 184 VAL -1.846 31.908 61.670 185 LEU 1.612 33.338 60.897 186 PHE 0.872 36.331 63.131 187 PHE -0.881 34.526 65.979 188 THR -0.064 35.541 69.558 189 ILE -0.429 33.793 72.945 190 LYS -3.740 35.643 73.357 191 ASP -5.356 34.343 70.162 192 SER -8.144 31.803 69.895 193 ALA -9.126 29.348 67.158 194 ARG -10.719 25.931 66.682 195 TYR -7.742 23.608 67.077 196 GLU -7.155 19.961 66.252 197 VAL -3.845 18.792 67.673 198 LYS -2.495 15.270 67.529 199 MET 0.618 14.428 69.529 200 LYS 3.128 11.614 68.974 201 ALA 5.759 11.148 71.664 202 LEU 7.791 8.619 73.600 203 THR 10.360 8.981 76.363 204 LEU 13.438 6.789 76.229 205 VAL 16.138 6.538 78.883 206 GLN 19.633 5.287 78.039 207 ALA 22.534 4.544 80.378 208 LEU 24.849 7.537 80.649 209 HIS 27.842 7.390 78.308 210 SER 30.560 10.021 78.736 211 SER 32.569 11.233 75.730 212 ASN 35.291 13.867 75.318 213 ALA 35.738 13.343 71.565 214 PRO 37.017 16.070 69.196 215 ILE 34.132 18.526 68.759 216 VAL 34.261 18.347 64.949 217 ASP 34.233 14.546 65.024 218 ILE 31.022 14.808 67.019 219 PHE 29.223 16.894 64.393 220 ASN 30.445 14.657 61.543 221 VAL 28.243 11.796 62.744 222 ASN 25.415 11.046 60.310 223 ASN 22.008 9.418 60.730 224 TYR 23.324 5.922 59.995 225 ASN 24.607 2.947 61.997 226 LEU 23.187 4.055 65.340 227 TYR 20.811 1.317 66.533 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S/S S S 10 S S S S/S S S S S C S 20 S S S S C S S S S S 30 S S C C H H H H H H 40 H H H H H H H C C C 50 T T T T S S S S/H H H 60 H H H H H H H H H C 70 S S S S S S/S S S S S 80 S S S S S S C H H H 90 H H H H H H H H H H 100 H H H H H/S S S S S S/H 110 H H H H H H H H H H 120 H H H H H H H H H H 130 H H C C C S S S S S 140 S C T T T T/S S S S/S S 150 S S S S S S S S S/T T 160 T T/T T T T/S S S S S S 170 S S S S S S S S C H 180 H H H H H H H C C S 190 S S S S/S S S S S S S 200 S S S S S S S S/S S S 210 S S S S/H H H H H H H 220 3 C C C S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 10 S 20 S E E E E E 30 g G G h H H H H H 40 H H H H H h G G G B 50 t T T T t B h H H 60 H H H H H H h T t T 70 e E E E E E E E E E 80 E E E E E E E E H H 90 H H H H H H H H H H 100 H H H H h S h 110 H H H H H H H H H H 120 H H H h T t g G G G 130 G g T t T e E E E E 140 S S S E E E E 150 E E E E E E E e t T 160 T T T e E E E E E E 170 E E E E E E E e S h 180 H H H H h T t t T T 190 e E E E E E E E E E 200 E E E E E E E e 210 h H H H H H h 220 t S S S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 CYS 0.0 0.0 96.2 2 SER 0.0 0.0 85.7 3 ALA 6.6 9.1 78.0 4 PRO 22.3 17.9 77.1 5 ILE 12.5 8.7 88.1 6 ILE 27.4 19.1 79.9 7 ARG 27.1 13.0 84.3 8 LYS 47.4 27.3 69.2 9 PRO 23.5 18.9 82.2 10 PHE 71.0 42.6 72.6 11 LYS 19.2 11.1 81.3 12 HIS 14.1 9.4 83.6 13 ILE 48.5 33.8 70.6 14 VAL 11.1 9.4 84.1 15 LEU 58.3 39.5 67.6 16 THR 2.2 2.0 82.6 17 VAL 65.3 55.0 53.4 18 PRO 11.4 9.2 82.6 19 SER 44.2 52.8 81.7 20 SER 50.1 60.0 80.0 21 ASP 81.2 73.4 60.7 22 LEU 14.0 9.5 88.6 23 ASP 64.1 58.0 81.1 24 ASN 95.0 78.6 52.4 25 PHE 166.1 99.6 50.9 26 ASN 80.6 66.7 55.4 27 THR 79.0 73.9 55.8 28 VAL 87.9 74.0 57.7 29 PHE 135.1 81.0 47.0 30 TYR 141.3 78.0 48.7 31 VAL 115.5 97.2 47.3 32 GLN 73.1 49.2 70.2 33 PRO 28.9 23.2 74.6 34 GLN 79.8 53.7 68.5 35 TYR 148.9 82.3 55.7 36 ILE 81.5 56.8 53.6 37 ASN 104.0 86.0 47.0 38 GLN 136.6 91.9 46.8 39 ALA 72.6 100.0 42.4 40 LEU 116.7 79.0 50.4 41 HIS 87.2 58.1 58.3 42 LEU 143.9 97.4 36.6 43 ALA 67.5 93.0 50.0 44 ASN 103.3 85.5 57.3 45 ALA 69.6 95.9 44.0 46 PHE 166.8 100.0 30.0 47 GLN 137.8 92.7 62.2 48 GLY 7.3 21.1 72.9 49 ALA 72.6 100.0 42.3 50 ILE 140.2 97.7 54.5 51 ASP 65.0 58.8 67.6 52 PRO 36.0 28.9 75.1 53 LEU 8.6 5.8 88.7 54 ASN 41.6 34.4 71.9 55 LEU 103.9 70.3 59.7 56 ASN 84.7 70.0 70.8 57 PHE 166.5 99.8 38.3 58 ASN 53.9 44.6 69.2 59 PHE 141.9 85.1 48.1 60 GLU 16.7 12.1 80.5 61 LYS 77.0 44.4 66.4 62 ALA 72.6 100.0 33.4 63 LEU 100.6 68.0 54.2 64 GLN 35.3 23.8 74.1 65 ILE 143.3 99.9 38.7 66 ALA 72.6 100.0 35.5 67 ASN 34.1 28.2 73.7 68 GLY 15.5 44.5 74.5 69 ILE 139.0 96.8 40.8 70 PRO 51.5 41.3 82.1 71 ASN 15.9 13.2 75.2 72 SER 77.9 93.2 53.8 73 ALA 15.3 21.0 71.1 74 ILE 119.8 83.5 54.2 75 VAL 82.3 69.3 53.5 76 LYS 96.4 55.6 59.7 77 THR 68.6 64.1 45.0 78 LEU 124.5 84.3 50.1 79 ASN 85.3 70.5 49.5 80 GLN 49.9 33.6 71.6 81 SER 57.3 68.5 66.2 82 VAL 109.6 92.3 39.1 83 ILE 135.3 94.3 39.8 84 GLN 63.5 42.7 81.2 85 GLN 60.1 40.5 70.7 86 THR 35.8 33.5 65.0 87 VAL 101.7 85.6 50.4 88 GLU 75.3 54.3 70.5 89 ILE 143.3 99.9 39.4 90 SER 53.7 64.3 55.8 91 VAL 40.2 33.9 77.2 92 MET 158.2 99.2 26.1 93 VAL 116.4 97.9 38.8 94 GLU 33.9 24.5 78.1 95 GLN 71.2 47.9 59.9 96 LEU 147.8 100.0 24.6 97 LYS 126.2 72.8 55.9 98 LYS 35.7 20.6 87.8 99 ILE 113.2 78.9 47.7 100 ILE 142.1 99.1 25.5 101 GLN 51.7 34.8 65.6 102 GLU 20.6 14.8 82.6 103 VAL 118.0 99.4 45.1 104 LEU 146.7 99.3 34.9 105 GLY 15.9 45.6 69.6 106 LEU 96.7 65.4 46.1 107 VAL 4.1 3.5 86.9 108 ILE 143.4 99.9 38.7 109 ASN 19.2 15.9 82.9 110 SER 68.0 81.3 62.5 111 THR 15.3 14.3 87.5 112 SER 22.8 27.3 72.3 113 PHE 163.2 97.8 25.3 114 TRP 163.2 79.6 53.1 115 ASN 44.5 36.8 74.4 116 SER 52.2 62.4 59.5 117 VAL 118.3 99.6 26.2 118 GLU 94.8 68.4 57.0 119 ALA 19.1 26.3 73.9 120 THR 86.9 81.3 47.8 121 ILE 143.5 100.0 30.3 122 LYS 96.1 55.4 61.0 123 GLY 17.6 50.7 85.4 124 THR 106.9 100.0 30.1 125 PHE 166.8 100.0 31.7 126 THR 98.9 92.6 51.7 127 ASN 23.4 19.4 87.9 128 LEU 147.8 100.0 46.7 129 ASP 72.5 65.6 57.5 130 THR 16.3 15.2 84.3 131 GLN 127.0 85.5 56.9 132 ILE 81.5 56.8 75.4 133 ASP 4.4 4.0 80.6 134 GLU 74.6 53.8 66.7 135 ALA 32.0 44.0 79.5 136 TRP 152.8 74.5 63.8 137 ILE 143.2 99.8 47.7 138 PHE 100.0 60.0 57.8 139 TRP 179.7 87.7 35.9 140 HIS 93.4 62.2 61.7 141 SER 23.3 27.8 82.5 142 LEU 91.3 61.8 65.1 143 SER 31.3 37.4 78.2 144 ALA 19.4 26.7 73.7 145 HIS 5.7 3.8 81.6 146 ASN 77.0 63.7 75.9 147 THR 106.9 100.0 41.1 148 SER 75.1 89.9 61.1 149 TYR 180.5 99.7 33.5 150 TYR 146.6 81.0 61.5 151 TYR 177.5 98.1 50.7 152 ASN 116.6 96.5 44.3 153 ILE 143.5 100.0 37.0 154 LEU 147.7 100.0 35.8 155 PHE 164.8 98.8 29.9 156 SER 83.5 99.9 36.1 157 ILE 143.4 99.9 29.2 158 GLN 144.3 97.1 37.3 159 ASN 114.5 94.7 59.7 160 GLU 3.9 2.8 85.6 161 ASP 80.7 73.0 73.1 162 THR 105.5 98.7 53.1 163 GLY 3.7 10.5 87.9 164 ALA 2.4 3.2 75.6 165 VAL 80.4 67.7 54.7 166 MET 159.4 100.0 43.8 167 ALA 72.6 100.0 33.6 168 VAL 118.6 99.9 38.5 169 LEU 146.0 98.8 34.7 170 PRO 124.5 100.0 33.2 171 LEU 147.8 100.0 27.7 172 ALA 70.7 97.5 49.7 173 PHE 166.8 100.0 27.0 174 GLU 97.1 70.0 60.0 175 VAL 118.8 100.0 38.9 176 SER 59.2 70.8 65.9 177 VAL 118.3 99.6 46.4 178 ASP 56.4 51.1 62.3 179 VAL 85.5 72.0 52.0 180 GLU 72.6 52.4 64.1 181 LYS 124.9 72.0 42.5 182 GLN 36.8 24.8 71.3 183 LYS 46.1 26.6 74.8 184 VAL 118.3 99.6 35.0 185 LEU 137.1 92.8 41.6 186 PHE 51.4 30.8 84.3 187 PHE 149.3 89.5 51.8 188 THR 32.6 30.5 74.4 189 ILE 95.1 66.3 47.5 190 LYS 15.9 9.2 86.0 191 ASP 62.9 56.9 67.8 192 SER 40.0 47.9 67.0 193 ALA 65.1 89.6 44.4 194 ARG 100.9 48.3 75.3 195 TYR 180.3 99.6 33.6 196 GLU 70.7 51.0 70.6 197 VAL 118.8 100.0 35.1 198 LYS 99.4 57.3 71.7 199 MET 159.0 99.7 27.6 200 LYS 165.6 95.5 51.5 201 ALA 72.6 100.0 35.3 202 LEU 147.8 100.0 26.5 203 THR 106.9 100.0 43.3 204 LEU 147.3 99.6 36.9 205 VAL 100.8 84.8 38.5 206 GLN 125.7 84.6 46.5 207 ALA 28.3 39.0 69.0 208 LEU 123.9 83.8 62.5 209 HIS 24.5 16.3 81.9 210 SER 36.0 43.0 67.1 211 SER 58.8 70.3 71.2 212 ASN 0.0 0.0 90.2 213 ALA 43.7 60.2 64.5 214 PRO 38.6 31.0 79.2 215 ILE 22.9 15.9 68.7 216 VAL 19.4 16.4 79.0 217 ASP 37.8 34.2 64.5 218 ILE 127.5 88.9 51.6 219 PHE 116.7 69.9 48.4 220 ASN 42.6 35.2 76.7 221 VAL 83.3 70.1 74.6 222 ASN 65.5 54.2 70.3 223 ASN 106.7 88.3 56.1 224 TYR 44.8 24.8 86.8 225 ASN 0.0 0.0 84.5 226 LEU 131.0 88.6 55.2 227 TYR 118.0 65.2 60.8