Protein Data Bank File : 1bu2 Title : CELL CYCLE REGULATION 10-SEP-98 1BU2 Number of Amino Acid Residues : 229 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ARG VAL LEU ASN ASN LEU LYS LEU ARG GLU 10 LEU LEU LEU PRO LYS PHE THR SER LEU TRP 20 GLU ILE GLN THR GLU VAL THR VAL ASP ASN 30 ARG THR ILE LEU LEU THR TRP MET HIS LEU 40 LEU CYS GLU SER PHE GLU LEU ASP LYS SER 50 VAL PHE PRO LEU SER VAL SER ILE LEU ASP 60 ARG TYR LEU CYS LYS LYS GLN GLY THR LYS 70 LYS THR LEU GLN LYS ILE GLY ALA ALA CYS 80 VAL LEU ILE GLY SER LYS ILE ARG THR VAL 90 LYS PRO MET THR VAL SER LYS LEU THR TYR 100 LEU SER CYS ASP CYS PHE THR ASN LEU GLU 110 LEU ILE ASN GLN GLU LYS ASP ILE LEU GLU 120 ALA LEU LYS TRP ASP THR GLU ALA VAL LEU 130 ALA THR ASP PHE LEU ILE PRO LEU CYS ASN 140 ALA LEU LYS ILE PRO GLU ASP LEU TRP PRO 150 GLN LEU TYR GLU ALA ALA SER THR THR ILE 160 CYS LYS ALA LEU ILE GLN PRO ASN ILE ALA 170 LEU LEU SER PRO GLY LEU ILE CYS ALA GLY 180 GLY LEU LEU THR THR ILE GLU THR ASP ASN 190 THR ASN CYS ARG PRO TRP THR CYS TYR LEU 200 GLU ASP LEU SER SER ILE LEU ASN PHE SER 210 THR ASN THR VAL ARG THR VAL LYS ASP GLN 220 VAL SER GLU ALA PHE SER LEU TYR ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ARG 0.0 101.8 179.6 0.0 0.0 0.0 0.0 2 VAL -94.3 15.1 178.5 -58.7 3 LEU -77.2 -33.3 179.4 -77.4 -179.5 4 ASN -64.4 -49.2 178.7 -71.0 -60.2 5 ASN -56.4 -52.5 179.3 -53.5 -61.4 6 LEU -51.6 -47.8 180.0 -75.4 179.8 7 LYS -63.2 -32.1 179.8 0.0 0.0 0.0 0.0 8 LEU -69.6 -64.4 -179.6 -94.3 174.6 9 ARG -69.6 7.1 178.1 59.4 -172.2 179.7 81.9 10 GLU -94.3 -17.9 179.0 175.8 -173.0 66.7 11 LEU -89.0 -14.4 179.0 -65.3 174.0 12 LEU -84.8 10.5 179.6 0.0 0.0 13 LEU -89.6 131.1 -178.5 -65.3 179.0 14 PRO -63.6 121.2 178.4 21.7 -31.1 15 LYS -79.0 84.8 -178.4 0.0 0.0 0.0 0.0 16 PHE -44.3 -68.5 -179.0 -75.1 -39.6 17 THR 72.2 -14.4 -178.9 0.0 18 SER -144.3 67.1 178.9 0.0 19 LEU -43.5 96.0 178.2 -72.6 167.1 20 TRP 77.2 27.2 -179.7 -67.5 24.2 21 GLU -49.2 -43.4 -179.3 0.0 0.0 0.0 22 ILE -69.7 -14.5 -178.3 -54.6 -176.8 23 GLN -71.3 122.6 178.8 0.0 0.0 0.0 24 THR -82.8 -78.5 179.3 -73.3 25 GLU -56.3 -81.6 -179.6 -71.5 -179.8 53.3 26 VAL -51.6 142.9 -179.6 -57.5 27 THR -135.6 172.3 -178.5 54.7 28 VAL -41.8 -32.9 -179.5 74.5 29 ASP -79.3 -16.5 176.6 38.6 62.9 30 ASN -82.7 -17.6 179.4 -73.6 -63.3 31 ARG -76.1 -40.9 179.3 177.1 176.6 170.7 -65.7 32 THR -64.7 -37.9 179.3 -61.1 33 ILE -67.1 -54.9 180.0 -65.2 -179.4 34 LEU -55.6 -43.6 179.6 -179.2 59.6 35 LEU -69.1 -24.3 179.5 -75.3 -168.2 36 THR -75.3 -35.5 178.4 -62.8 37 TRP -66.9 -51.4 179.6 176.5 70.0 38 MET -60.3 -38.5 178.6 -60.4 174.3 58.2 39 HIS -61.6 -47.8 179.6 179.5 68.1 40 LEU -60.9 -38.5 -179.9 173.1 66.6 41 LEU -65.2 -47.2 179.6 -171.2 59.0 42 CYS -67.0 -27.7 179.7 -69.7 43 GLU -78.7 -36.9 179.6 -72.4 -60.2 -59.6 44 SER -62.7 -24.0 -179.6 0.0 45 PHE -101.9 -6.7 179.9 -72.7 78.8 46 GLU 50.1 47.6 -179.6 -54.7 173.2 -52.6 47 LEU -81.8 160.7 178.4 -52.7 173.4 48 ASP -44.4 146.2 179.8 -71.6 42.4 49 LYS -60.2 -16.4 -179.8 -67.7 -66.4 169.8 57.3 50 SER -87.9 -16.9 -179.0 63.6 51 VAL -65.2 -45.6 179.6 -174.8 52 PHE -67.7 -54.5 180.0 178.2 66.1 53 PRO -55.8 -28.2 180.0 26.5 -45.9 54 LEU -78.1 -34.8 179.2 -158.8 -171.5 55 SER -69.4 -34.4 178.5 76.3 56 VAL -60.5 -48.5 177.9 -179.6 57 SER -54.5 -52.0 177.9 173.3 58 ILE -55.0 -54.0 -178.4 -59.6 -70.1 59 LEU -52.8 -53.4 -179.5 169.4 72.2 60 ASP -67.0 -19.3 177.6 -63.9 -40.4 61 ARG -82.5 -64.0 178.9 -80.0 -166.8 -82.2 171.7 62 TYR -38.5 -55.3 -179.3 175.6 63.6 63 LEU -72.0 0.8 178.1 -74.2 -178.0 64 CYS -94.0 6.7 180.0 174.7 65 LYS -143.2 -49.6 178.1 -70.4 -163.3 168.8 -174.0 66 LYS -89.6 175.1 -179.0 -73.0 -58.9 -179.8 176.2 67 GLN -110.5 143.9 179.4 -167.8 64.3 63.9 68 GLY -121.2 161.2 178.8 69 THR -117.4 158.4 179.9 62.6 70 LYS -60.9 -31.9 -178.8 0.0 0.0 0.0 0.0 71 LYS -77.8 -7.3 -179.2 0.0 0.0 0.0 0.0 72 THR -120.9 -1.7 180.0 55.9 73 LEU -54.3 -34.1 179.5 -67.8 175.5 74 GLN -74.2 -32.3 179.1 -65.8 178.3 -74.4 75 LYS -69.1 -55.0 178.9 -165.7 173.1 59.0 177.9 76 ILE -52.4 -53.9 179.3 -61.6 179.3 77 GLY -64.4 -24.8 179.2 78 ALA -78.7 -36.8 -179.7 79 ALA -66.6 -38.2 179.8 80 CYS -64.2 -39.0 178.6 -66.7 81 VAL -67.8 -34.0 178.9 171.2 82 LEU -70.4 -55.5 179.9 -178.5 76.1 83 ILE -49.8 -46.1 179.5 -62.6 -177.3 84 GLY -63.0 -39.2 178.8 85 SER -72.8 -33.4 179.6 57.5 86 LYS -65.6 -15.1 -179.5 -85.8 -173.6 179.8 179.3 87 ILE -110.8 -28.1 -178.8 77.2 -177.7 88 ARG -93.4 -61.2 -179.2 -68.5 -37.7 -152.3 75.3 89 THR -60.7 156.0 178.4 56.9 90 VAL -76.2 -34.0 178.5 51.0 91 LYS -114.3 74.6 -179.6 -68.5 -176.7 -63.5 -177.6 92 PRO -57.0 101.5 178.8 29.7 -47.8 93 MET -35.9 137.0 -179.0 175.5 170.7 55.0 94 THR -91.1 159.9 -179.9 0.0 95 VAL -58.1 -23.6 -179.9 59.0 96 SER -76.3 -63.2 -177.7 -46.4 97 LYS -51.9 -15.9 -179.6 -168.5 175.7 -176.5 -170.7 98 LEU -94.1 -23.5 177.6 -177.7 53.1 99 THR -88.3 -42.5 -179.8 -85.2 100 TYR -74.4 -35.1 -179.0 -177.2 50.0 101 LEU -69.5 -28.1 178.5 0.0 0.0 102 SER -102.5 30.7 179.8 64.5 103 CYS 36.8 91.1 -178.4 -58.1 104 ASP 13.4 47.7 178.3 0.0 0.0 105 CYS -58.0 -35.8 175.5 -174.8 106 PHE -140.7 160.6 178.4 -21.6 69.9 107 THR -77.1 133.2 179.3 53.5 108 ASN -40.8 -25.0 178.9 163.9 -51.8 109 LEU -81.6 -35.4 178.5 -161.5 66.3 110 GLU -63.9 -49.3 178.4 -64.0 -175.9 -66.2 111 LEU -58.3 -50.0 178.6 -68.4 -171.6 112 ILE -43.1 -57.5 -178.0 -56.8 -67.3 113 ASN -68.8 -15.8 -179.6 -163.7 63.9 114 GLN -89.8 -42.1 177.8 177.9 59.1 -63.1 115 GLU -53.5 -66.0 -179.4 -174.4 -166.0 11.5 116 LYS -41.7 -51.9 179.6 -168.2 167.2 73.6 66.4 117 ASP -51.4 -45.7 -179.6 -66.7 -5.4 118 ILE -65.7 -43.8 178.7 -55.6 -179.8 119 LEU -59.2 -48.3 179.4 -73.3 -56.8 120 GLU -58.5 -56.9 178.8 -63.1 -159.5 66.8 121 ALA -47.7 -44.2 179.9 122 LEU -84.1 10.7 179.4 -61.8 -167.5 123 LYS 53.4 45.5 177.8 -64.2 178.1 -173.9 -58.7 124 TRP 49.0 22.7 178.2 -53.3 83.9 125 ASP -116.0 87.9 178.9 -174.7 52.3 126 THR -109.5 103.2 -179.7 64.3 127 GLU -165.0 143.1 -178.4 178.5 59.1 -69.2 128 ALA -163.3 149.3 177.7 129 VAL -85.3 130.7 -177.9 -156.2 130 LEU -112.4 148.9 179.2 -43.8 172.8 131 ALA -50.4 -33.1 178.5 132 THR -51.6 -37.0 -179.0 -94.7 133 ASP -68.0 -10.4 -179.4 -54.4 -38.6 134 PHE -96.7 -18.4 -179.7 -76.5 71.0 135 LEU -51.6 -65.7 -180.0 -59.9 178.7 136 ILE -57.5 -54.0 -180.0 0.0 0.0 137 PRO -53.5 -34.8 179.2 -33.9 50.9 138 LEU -93.1 -11.4 179.7 -63.5 173.7 139 CYS -68.0 -43.5 178.8 -97.1 140 ASN -79.3 -45.8 179.6 67.5 72.4 141 ALA -50.8 -23.3 178.9 142 LEU -91.1 22.2 179.3 -87.8 179.3 143 LYS 52.3 42.3 178.7 -173.2 -161.2 -56.4 175.2 144 ILE -114.9 118.6 -179.9 0.0 0.0 145 PRO -63.2 149.8 -179.7 33.4 -49.2 146 GLU -65.9 29.1 179.9 -57.7 177.6 57.0 147 ASP -106.9 -23.8 -179.6 -55.8 -54.5 148 LEU -113.7 6.2 178.8 0.0 0.0 149 TRP -64.5 -49.9 -180.0 -83.5 11.3 150 PRO -53.0 -35.9 179.8 27.2 -47.1 151 GLN -91.0 -21.2 -179.2 0.0 0.0 0.0 152 LEU -82.7 -25.3 -179.8 -173.6 64.0 153 TYR -80.2 -23.7 179.9 -176.7 70.7 154 GLU -78.1 -49.4 -178.8 -177.8 62.1 52.8 155 ALA -72.0 -36.8 -179.4 156 ALA -68.4 -38.3 179.2 157 SER -69.8 -40.7 -179.9 -64.4 158 THR -64.0 -34.8 179.2 -54.7 159 THR -69.6 -58.6 179.1 -59.9 160 ILE -54.5 -53.2 -179.5 -60.8 177.6 161 CYS -60.7 -29.4 179.0 -65.8 162 LYS -83.3 -33.7 -179.9 0.0 0.0 0.0 0.0 163 ALA -70.3 -37.6 -179.8 164 LEU -61.9 -8.4 179.2 -81.3 171.9 165 ILE -71.1 -27.2 -178.9 -57.0 -178.4 166 GLN -83.7 136.0 179.6 -52.9 -58.4 167.2 167 PRO -64.3 2.1 179.6 31.9 -48.7 168 ASN -77.8 -67.1 -180.0 -43.3 -50.8 169 ILE -51.8 -25.2 -179.2 -63.2 63.4 170 ALA -69.8 27.2 179.2 171 LEU -148.9 25.4 -178.1 -66.5 -179.5 172 LEU -121.5 161.3 177.6 -54.0 172.4 173 SER -68.9 135.2 179.7 168.9 174 PRO -57.4 -25.9 -179.8 28.2 -47.5 175 GLY -63.8 -51.5 179.1 176 LEU -61.0 -55.7 -178.6 -64.5 170.3 177 ILE -52.8 -19.7 178.6 65.3 179.7 178 CYS -88.1 -26.4 179.3 172.7 179 ALA -72.7 -59.3 179.6 180 GLY -54.2 -32.3 180.0 181 GLY -81.1 -28.2 178.8 182 LEU -76.5 -28.7 179.5 -166.4 60.9 183 LEU -78.8 -53.6 -178.9 -65.7 -179.8 184 THR -55.4 -19.3 178.7 57.5 185 THR -84.7 -48.5 179.2 -62.0 186 ILE -65.7 -21.1 179.3 0.0 0.0 187 GLU -67.4 -68.1 179.9 -176.5 -165.9 66.0 188 THR -49.6 -29.6 178.9 53.5 189 ASP -120.8 64.2 -178.9 0.0 0.0 190 ASN -70.9 122.4 177.5 -75.8 127.1 191 THR -113.2 -29.8 179.9 0.0 192 ASN -135.9 161.1 179.1 165.7 -43.9 193 CYS -72.0 -164.2 179.8 0.0 194 ARG -106.8 42.0 179.5 -61.1 162.2 43.9 -173.3 195 PRO -62.7 -6.1 -177.7 -27.7 46.1 196 TRP -72.2 -9.3 179.8 -19.3 83.1 197 THR -61.1 -24.4 178.7 0.0 198 CYS -94.2 -42.8 -179.6 0.0 199 TYR -54.1 -45.9 179.1 -142.9 87.9 200 LEU -70.8 -34.1 -179.8 -78.6 172.8 201 GLU -47.1 -13.0 -179.8 0.0 0.0 0.0 202 ASP -101.1 -28.4 -179.1 -60.4 64.9 203 LEU -72.8 -60.8 -179.9 -51.4 172.5 204 SER -85.3 1.3 -179.6 0.0 205 SER 45.7 101.5 179.7 -61.3 206 ILE 158.4 159.2 180.0 0.0 0.0 207 LEU -134.8 -47.5 178.8 179.1 54.7 208 ASN -89.2 -18.5 179.5 0.0 0.0 209 PHE -86.3 -21.5 179.2 0.0 0.0 210 SER -87.5 -1.1 179.3 0.0 211 THR -95.8 -46.1 179.7 0.0 212 ASN -53.4 -37.5 179.7 0.0 0.0 213 THR -60.8 -42.3 179.2 0.0 214 VAL -61.1 -45.5 -179.7 175.5 215 ARG -64.8 -30.0 -179.9 0.0 0.0 0.0 0.0 216 THR -83.1 -43.5 179.0 0.0 217 VAL -59.7 -62.8 -179.8 -177.1 218 LYS -56.0 -34.2 179.3 0.0 0.0 0.0 0.0 219 ASP -71.5 -40.5 179.2 0.0 0.0 220 GLN -67.5 -43.7 -180.0 0.0 0.0 0.0 221 VAL -58.9 -42.3 179.9 0.0 222 SER -71.1 16.4 -179.8 64.6 223 GLU -120.9 36.0 179.9 -63.1 -56.3 -13.9 224 ALA -98.9 80.2 178.0 225 PHE -93.1 93.5 179.8 0.0 0.0 226 SER -56.3 -15.4 -179.7 -171.9 227 LEU -78.5 15.7 179.5 0.0 0.0 228 TYR -106.0 -11.5 -179.3 0.0 0.0 229 ASP -104.3 0.8 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ARG -14.133 29.271 116.652 2 VAL -11.915 32.225 117.568 3 LEU -11.797 33.454 113.982 4 ASN -14.807 35.764 114.442 5 ASN -13.208 37.467 117.424 6 LEU -9.988 37.635 115.435 7 LYS -11.792 39.141 112.441 8 LEU -13.463 41.641 114.796 9 ARG -10.509 42.987 116.739 10 GLU -8.722 42.817 113.403 11 LEU -10.967 45.653 112.284 12 LEU -9.800 47.579 115.345 13 LEU -6.414 47.783 113.549 14 PRO -5.393 51.230 112.263 15 LYS -5.673 51.406 108.518 16 PHE -2.410 53.294 108.004 17 THR -2.567 53.952 104.234 18 SER 0.563 55.991 104.878 19 LEU 3.403 53.899 106.377 20 TRP 5.373 56.554 108.281 21 GLU 3.709 59.570 106.605 22 ILE 4.646 61.881 109.483 23 GLN 8.313 60.883 109.167 24 THR 10.673 63.631 107.906 25 GLU 14.187 62.175 107.916 26 VAL 13.502 58.457 108.060 27 THR 11.416 57.058 105.190 28 VAL 9.688 53.836 104.107 29 ASP 13.122 52.572 103.081 30 ASN 14.643 53.136 106.535 31 ARG 11.807 50.879 107.727 32 THR 12.842 47.971 105.550 33 ILE 16.358 48.277 106.928 34 LEU 15.301 48.614 110.581 35 LEU 12.807 45.715 110.408 36 THR 15.432 43.422 108.898 37 TRP 17.622 44.367 111.825 38 MET 14.811 43.816 114.395 39 HIS 14.015 40.476 112.779 40 LEU 17.636 39.363 113.192 41 LEU 17.461 40.633 116.758 42 CYS 14.318 38.645 117.531 43 GLU 15.852 35.541 115.941 44 SER 19.152 35.882 117.792 45 PHE 17.079 35.685 120.987 46 GLU 14.725 32.927 119.775 47 LEU 11.761 34.875 121.151 48 ASP 8.138 33.868 120.581 49 LYS 6.971 34.051 116.979 50 SER 4.592 36.783 118.111 51 VAL 7.279 39.170 119.426 52 PHE 8.599 40.353 116.038 53 PRO 5.246 40.766 114.318 54 LEU 4.062 42.703 117.396 55 SER 7.084 45.007 117.457 56 VAL 6.448 45.833 113.785 57 SER 2.913 46.874 114.823 58 ILE 4.256 48.984 117.724 59 LEU 6.925 50.554 115.470 60 ASP 4.658 51.663 112.639 61 ARG 2.318 53.052 115.243 62 TYR 4.829 54.885 117.390 63 LEU 6.328 56.434 114.240 64 CYS 2.876 57.314 112.974 65 LYS 2.831 60.076 115.634 66 LYS 6.249 60.832 117.102 67 GLN 9.359 61.619 115.085 68 GLY 12.384 59.430 114.606 69 THR 15.928 60.029 113.439 70 LYS 18.076 57.743 111.306 71 LYS 20.373 57.609 114.350 72 THR 17.686 56.380 116.735 73 LEU 15.783 53.813 114.663 74 GLN 17.692 51.023 116.390 75 LYS 16.886 52.366 119.833 76 ILE 13.229 52.758 118.786 77 GLY 13.205 49.377 117.058 78 ALA 14.918 47.743 120.030 79 ALA 12.377 49.244 122.393 80 CYS 9.569 47.910 120.220 81 VAL 11.039 44.444 120.482 82 LEU 11.227 44.889 124.297 83 ILE 7.700 46.218 124.560 84 GLY 6.572 43.251 122.441 85 SER 8.269 40.489 124.436 86 LYS 6.967 42.114 127.597 87 ILE 3.369 41.585 126.504 88 ARG 3.237 38.305 124.627 89 THR 5.812 35.916 126.057 90 VAL 5.553 34.430 129.547 91 LYS 9.182 35.402 130.361 92 PRO 9.370 38.973 128.929 93 MET 12.984 39.782 128.164 94 THR 14.349 42.547 130.414 95 VAL 16.029 45.830 129.443 96 SER 19.141 44.178 130.820 97 LYS 19.109 40.898 128.892 98 LEU 18.576 43.150 125.855 99 THR 21.518 45.491 126.456 100 TYR 24.068 42.776 127.258 101 LEU 22.992 40.279 124.603 102 SER 23.347 43.015 121.960 103 CYS 26.715 44.068 123.448 104 ASP 26.001 47.487 125.037 105 CYS 24.667 48.695 121.647 106 PHE 22.807 51.262 123.867 107 THR 23.012 52.060 127.575 108 ASN 20.608 50.076 129.736 109 LEU 19.178 53.581 130.656 110 GLU 18.466 54.802 127.054 111 LEU 16.142 51.858 126.216 112 ILE 14.401 52.361 129.533 113 ASN 13.680 55.953 128.564 114 GLN 12.817 54.985 124.922 115 GLU 10.488 52.155 125.844 116 LYS 8.550 54.548 128.098 117 ASP 8.269 57.261 125.429 118 ILE 6.704 54.667 123.098 119 LEU 4.327 53.321 125.724 120 GLU 3.312 56.923 126.358 121 ALA 3.034 57.851 122.669 122 LEU 0.811 54.768 122.121 123 LYS -1.335 55.551 125.197 124 TRP -0.274 52.369 126.932 125 ASP -2.272 50.238 124.526 126 THR 0.217 47.915 122.912 127 GLU -1.784 45.034 121.532 128 ALA -2.395 43.721 118.052 129 VAL -3.744 40.823 116.110 130 LEU -0.696 39.495 114.309 131 ALA -0.830 37.308 111.180 132 THR 0.859 34.935 113.602 133 ASP -2.405 34.687 115.508 134 PHE -4.109 33.106 112.471 135 LEU -1.827 30.092 111.795 136 ILE -3.218 27.653 114.351 137 PRO -6.815 28.989 113.989 138 LEU -6.820 28.688 110.180 139 CYS -4.869 25.420 110.286 140 ASN -7.768 23.284 111.447 141 ALA -10.391 25.393 109.646 142 LEU -8.363 24.358 106.584 143 LYS -9.070 20.665 107.169 144 ILE -5.421 20.111 108.130 145 PRO -4.801 17.450 110.852 146 GLU -2.773 18.107 114.031 147 ASP 0.039 15.970 112.631 148 LEU 1.546 18.614 110.388 149 TRP 0.736 21.622 112.592 150 PRO 4.095 21.665 114.464 151 GLN 6.070 21.942 111.195 152 LEU 3.479 24.134 109.478 153 TYR 3.514 26.695 112.278 154 GLU 7.297 27.020 111.961 155 ALA 7.530 27.624 108.234 156 ALA 4.401 29.749 108.049 157 SER 5.640 31.993 110.855 158 THR 9.130 32.262 109.307 159 THR 7.543 33.236 105.976 160 ILE 5.184 35.798 107.506 161 CYS 7.774 37.245 109.893 162 LYS 10.161 37.571 106.937 163 ALA 7.421 38.923 104.683 164 LEU 6.336 41.569 107.213 165 ILE 9.710 43.204 106.623 166 GLN 8.293 44.559 103.349 167 PRO 6.165 47.744 103.189 168 ASN 3.736 45.767 100.968 169 ILE 2.255 43.427 103.547 170 ALA 2.148 46.458 105.876 171 LEU -1.225 47.347 104.352 172 LEU -2.986 44.029 104.733 173 SER -5.411 42.329 107.076 174 PRO -3.351 40.259 109.460 175 GLY -5.803 37.591 108.382 176 LEU -4.918 37.726 104.721 177 ILE -1.186 38.005 105.355 178 CYS -1.540 34.812 107.388 179 ALA -3.394 33.018 104.630 180 GLY -0.946 33.815 101.840 181 GLY 1.940 32.905 104.113 182 LEU 0.206 29.745 105.197 183 LEU -0.328 28.947 101.517 184 THR 3.103 29.837 100.157 185 THR 4.377 27.409 102.803 186 ILE 2.095 24.463 101.982 187 GLU 3.069 25.231 98.371 188 THR 6.815 24.739 98.683 189 ASP 6.170 21.624 100.804 190 ASN 3.245 19.985 98.961 191 THR 1.694 16.830 100.450 192 ASN -1.670 17.835 98.908 193 CYS -2.379 20.372 96.125 194 ARG -3.687 23.857 96.933 195 PRO -7.516 23.373 96.836 196 TRP -7.468 25.369 100.067 197 THR -7.503 28.594 98.020 198 CYS -11.254 28.130 98.001 199 TYR -11.477 26.598 101.489 200 LEU -9.873 29.701 103.075 201 GLU -11.962 31.917 100.804 202 ASP -14.821 31.418 103.314 203 LEU -12.967 32.125 106.534 204 SER -11.411 35.434 105.533 205 SER -14.203 35.758 102.941 206 ILE -12.756 36.534 99.459 207 LEU -11.465 34.535 96.474 208 ASN -9.576 36.662 93.946 209 PHE -8.556 38.898 96.855 210 SER -7.140 35.949 98.841 211 THR -4.778 35.181 95.954 212 ASN -3.175 38.589 95.669 213 THR -2.149 38.265 99.327 214 VAL -0.307 35.041 98.429 215 ARG 1.449 36.746 95.539 216 THR 2.411 39.591 97.876 217 VAL 3.439 37.475 100.913 218 LYS 5.579 35.050 98.866 219 ASP 6.978 37.913 96.767 220 GLN 7.871 39.850 99.918 221 VAL 9.418 36.809 101.626 222 SER 11.702 36.204 98.675 223 GLU 13.015 39.688 99.455 224 ALA 15.134 39.079 102.559 225 PHE 18.581 40.399 101.586 226 SER 20.316 40.415 104.965 227 LEU 22.907 42.251 102.862 228 TYR 20.851 45.443 103.145 229 ASP 21.633 45.918 106.880 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C H H H H H H H H H 10 H H H C C C S S S S 20 C C T T T T H H H H 30 H H H H H H H H H H 40 H H H H H H C C C H 50 H H H H H H H H H H 60 H H H H H H/S S S S S 70 C H H H H H H H H H 80 H H H H H H H H H S 90 S S S H H H H H H H 100 H H H C C C H H H H 110 3 3/H H H H H H H H H 120 H H H S S S S S S H 130 H H H 3 3/H H H H H 3 140 3 C S S S S C H H H 150 H H H H H H H H H H 160 H H H H H C H H H H 170 3 3 H H H H H H H H 180 H H H H H H H H H H 190 S S S S C H H H H H 200 H 3 3 S S S S/H H H H 210 H H H H H H H H H H 220 H H H/S S S S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H h T 10 T t S S t T T 20 T T t S S S h H H H 30 H H H H H H H H H H 40 H H H H h T t t T h 50 H H H H H H H H H H 60 H H h T T t t T 70 T h H H H H H H H H 80 H H H H H H H h S S 90 S h H H H H H H 100 h T T T t S h H H H 110 H H H H H H H H H H 120 H h T T t g 130 G G G h H H H H H H 140 H h T t t T T h H H 150 H H H H H H H H H H 160 H H H h T t T g G G 170 G g h H H H H H H H 180 H H H H H H H H h t 190 S S t h H H H H h 200 G G g T T t S h H H 210 H H H H H H H H H H 220 H h G g g G G G g Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ARG 146.2 70.0 90.0 2 VAL 37.3 31.4 71.3 3 LEU 118.5 80.2 41.6 4 ASN 14.6 12.1 78.5 5 ASN 42.1 34.8 68.3 6 LEU 141.5 95.7 44.0 7 LYS 127.9 73.8 75.0 8 LEU 31.1 21.0 79.1 9 ARG 97.7 46.8 63.5 10 GLU 120.8 87.2 47.0 11 LEU 29.2 19.8 85.2 12 LEU 88.7 60.0 77.8 13 LEU 110.4 74.7 56.3 14 PRO 58.3 46.8 63.0 15 LYS 96.0 55.4 89.1 16 PHE 133.7 80.2 52.5 17 THR 46.0 43.0 73.0 18 SER 39.7 47.5 67.9 19 LEU 136.3 92.2 45.4 20 TRP 204.1 99.6 41.3 21 GLU 90.6 65.4 68.9 22 ILE 59.8 41.7 78.6 23 GLN 148.0 99.6 61.3 24 THR 12.4 11.6 80.3 25 GLU 51.2 36.9 67.4 26 VAL 118.6 99.9 40.5 27 THR 50.2 46.9 80.0 28 VAL 59.1 49.7 56.3 29 ASP 26.9 24.3 79.1 30 ASN 86.4 71.4 56.0 31 ARG 208.6 99.9 40.1 32 THR 72.2 67.5 66.5 33 ILE 61.8 43.0 73.5 34 LEU 143.7 97.2 31.4 35 LEU 147.8 100.0 43.3 36 THR 89.9 84.1 52.0 37 TRP 164.7 80.4 42.7 38 MET 159.4 100.0 31.8 39 HIS 117.3 78.1 46.6 40 LEU 40.0 27.1 74.5 41 LEU 132.3 89.5 34.1 42 CYS 95.5 96.2 45.4 43 GLU 59.7 43.0 70.3 44 SER 34.6 41.3 72.0 45 PHE 147.7 88.6 41.6 46 GLU 6.6 4.7 90.9 47 LEU 125.6 85.0 43.7 48 ASP 39.8 36.0 71.5 49 LYS 129.4 74.6 73.2 50 SER 73.4 87.8 45.0 51 VAL 118.8 100.0 42.4 52 PHE 161.0 96.5 40.2 53 PRO 124.0 99.6 38.6 54 LEU 147.8 100.0 41.8 55 SER 83.6 100.0 40.6 56 VAL 111.5 93.9 50.0 57 SER 58.5 70.0 61.0 58 ILE 143.5 100.0 34.9 59 LEU 147.8 100.0 31.5 60 ASP 105.6 95.5 43.8 61 ARG 173.6 83.1 52.4 62 TYR 168.1 92.9 37.6 63 LEU 147.6 99.9 37.4 64 CYS 58.4 58.8 60.1 65 LYS 58.1 33.5 73.3 66 LYS 59.7 34.4 73.8 67 GLN 86.6 58.3 68.6 68 GLY 33.7 96.9 44.5 69 THR 55.5 51.9 67.4 70 LYS 125.9 72.6 72.0 71 LYS 103.1 59.4 81.5 72 THR 72.6 68.0 67.7 73 LEU 135.8 91.9 39.7 74 GLN 64.9 43.7 56.7 75 LYS 120.6 69.5 50.8 76 ILE 140.6 98.0 39.6 77 GLY 34.8 100.0 38.2 78 ALA 72.3 99.6 36.7 79 ALA 72.6 100.0 42.2 80 CYS 99.2 100.0 34.5 81 VAL 118.6 99.8 37.9 82 LEU 147.8 100.0 47.4 83 ILE 141.0 98.2 34.2 84 GLY 34.8 100.0 50.6 85 SER 83.2 99.5 48.7 86 LYS 100.9 58.2 70.2 87 ILE 107.3 74.8 62.0 88 ARG 163.4 78.2 68.6 89 THR 97.5 91.2 60.4 90 VAL 0.0 0.0 78.3 91 LYS 11.0 6.4 79.1 92 PRO 82.3 66.1 73.0 93 MET 150.4 94.3 38.0 94 THR 61.6 57.7 68.2 95 VAL 98.2 82.7 49.7 96 SER 25.8 30.8 74.0 97 LYS 35.2 20.3 72.4 98 LEU 146.7 99.3 33.8 99 THR 89.6 83.8 60.7 100 TYR 3.0 1.6 86.1 101 LEU 115.7 78.3 63.2 102 SER 64.6 77.2 52.0 103 CYS 6.0 6.0 85.6 104 ASP 54.7 49.5 80.1 105 CYS 59.0 59.5 67.7 106 PHE 148.4 89.0 49.5 107 THR 24.6 23.0 72.4 108 ASN 60.7 50.2 62.0 109 LEU 12.8 8.6 83.1 110 GLU 62.9 45.4 68.6 111 LEU 147.8 100.0 38.8 112 ILE 76.8 53.5 63.7 113 ASN 35.1 29.0 77.3 114 GLN 137.3 92.4 49.5 115 GLU 119.4 86.2 43.7 116 LYS 74.4 42.9 74.3 117 ASP 57.7 52.2 79.7 118 ILE 143.5 100.0 33.0 119 LEU 121.6 82.3 39.3 120 GLU 64.9 46.9 72.6 121 ALA 62.9 86.6 50.5 122 LEU 135.1 91.4 50.0 123 LYS 27.9 16.1 87.8 124 TRP 65.5 31.9 68.4 125 ASP 21.6 19.6 82.0 126 THR 99.3 92.9 37.6 127 GLU 57.0 41.1 79.7 128 ALA 67.4 92.8 51.3 129 VAL 116.7 98.3 41.3 130 LEU 141.0 95.4 48.6 131 ALA 72.6 100.0 36.4 132 THR 101.2 94.6 47.0 133 ASP 86.7 78.5 60.5 134 PHE 157.4 94.4 38.4 135 LEU 147.7 100.0 42.3 136 ILE 94.9 66.1 52.8 137 PRO 100.3 80.6 53.7 138 LEU 145.1 98.2 33.7 139 CYS 97.2 98.0 36.2 140 ASN 46.3 38.3 71.3 141 ALA 51.0 70.3 60.3 142 LEU 138.7 93.8 32.7 143 LYS 37.9 21.8 78.5 144 ILE 129.6 90.3 50.0 145 PRO 37.2 29.8 82.1 146 GLU 27.3 19.7 72.1 147 ASP 11.5 10.4 76.6 148 LEU 93.1 63.0 69.3 149 TRP 147.9 72.2 54.5 150 PRO 39.2 31.5 76.5 151 GLN 82.7 55.6 76.7 152 LEU 118.1 79.9 45.6 153 TYR 102.0 56.3 63.8 154 GLU 48.6 35.1 81.0 155 ALA 33.6 46.2 67.0 156 ALA 72.6 100.0 46.7 157 SER 83.6 100.0 48.0 158 THR 36.5 34.1 75.8 159 THR 82.5 77.2 61.1 160 ILE 142.4 99.2 39.4 161 CYS 94.1 94.8 42.2 162 LYS 159.3 91.9 59.4 163 ALA 71.8 98.9 46.4 164 LEU 132.7 89.8 41.0 165 ILE 138.3 96.4 47.9 166 GLN 128.2 86.3 56.4 167 PRO 94.8 76.1 64.8 168 ASN 50.8 42.0 63.2 169 ILE 142.6 99.4 35.6 170 ALA 60.4 83.1 61.1 171 LEU 68.0 46.0 73.3 172 LEU 109.0 73.8 54.5 173 SER 51.4 61.5 58.5 174 PRO 116.6 93.6 43.2 175 GLY 32.4 93.2 51.9 176 LEU 110.1 74.5 49.2 177 ILE 134.4 93.7 38.2 178 CYS 99.2 100.0 42.3 179 ALA 71.4 98.3 41.6 180 GLY 34.8 100.0 44.9 181 GLY 34.8 100.0 56.0 182 LEU 145.7 98.6 37.1 183 LEU 143.1 96.8 44.1 184 THR 98.7 92.3 44.3 185 THR 96.8 90.5 60.7 186 ILE 119.8 83.5 66.2 187 GLU 70.0 50.5 70.7 188 THR 22.1 20.7 83.8 189 ASP 48.4 43.8 85.9 190 ASN 71.8 59.4 69.7 191 THR 31.4 29.4 85.5 192 ASN 48.2 39.9 63.7 193 CYS 38.5 38.9 73.5 194 ARG 124.0 59.3 60.2 195 PRO 43.1 34.6 78.1 196 TRP 164.9 80.4 47.4 197 THR 66.7 62.4 71.1 198 CYS 42.8 43.2 73.9 199 TYR 94.6 52.3 67.3 200 LEU 145.4 98.4 31.5 201 GLU 129.5 93.4 60.4 202 ASP 19.6 17.7 82.1 203 LEU 112.0 75.8 50.7 204 SER 59.7 71.4 56.8 205 SER 18.1 21.7 83.2 206 ILE 115.6 80.5 62.8 207 LEU 41.6 28.2 73.2 208 ASN 45.3 37.4 82.1 209 PHE 114.1 68.4 69.7 210 SER 78.1 93.4 52.6 211 THR 53.7 50.3 77.2 212 ASN 61.4 50.8 78.4 213 THR 103.9 97.2 47.0 214 VAL 102.0 85.8 54.5 215 ARG 146.3 70.1 77.4 216 THR 77.4 72.4 59.5 217 VAL 118.2 99.5 40.7 218 LYS 141.9 81.9 60.1 219 ASP 58.6 53.0 83.1 220 GLN 148.3 99.8 51.2 221 VAL 102.7 86.5 59.1 222 SER 20.0 24.0 81.4 223 GLU 46.3 33.4 85.3 224 ALA 36.8 50.6 72.9 225 PHE 108.5 65.0 74.9 226 SER 13.6 16.2 75.0 227 LEU 76.0 51.4 81.8 228 TYR 138.9 76.7 73.3 229 ASP 95.9 86.8 62.2