Protein Data Bank File : 2bc2a Title : HYDROLASE 09-SEP-97 2BC2 Number of Amino Acid Residues : 217 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR VAL ILE LYS ASN GLU THR GLY THR ILE 10 SER ILE SER GLN LEU ASN LYS ASN VAL TRP 20 VAL HIS THR GLU LEU GLY SER GLU ALA VAL 30 PRO SER ASN GLY LEU VAL LEU ASN THR SER 40 LYS GLY LEU VAL LEU VAL ASP SER SER TRP 50 ASP ASP LYS LEU THR LYS GLU LEU ILE GLU 60 MET VAL GLU LYS LYS PHE GLN LYS ARG VAL 70 THR ASP VAL ILE ILE THR HIS ALA HIS ALA 80 ASP ARG ILE GLY GLY ILE LYS THR LEU LYS 90 GLU ARG GLY ILE LYS ALA HIS SER THR ALA 100 LEU THR ALA GLU LEU ALA LYS LYS ASN GLY 110 TYR GLU GLU PRO LEU GLY ASP LEU GLN THR 120 VAL THR ASN LEU LYS PHE GLY ASN MET LYS 130 VAL GLU THR PHE TYR PRO GLY LYS GLY HIS 140 THR GLU ASP ASN ILE VAL VAL TRP LEU PRO 150 GLN TYR ASN ILE LEU VAL GLY GLY LEU VAL 160 LYS SER THR SER ALA LYS ASP LEU GLY ASN 170 VAL ALA ASP ALA TYR VAL ASN GLU TRP SER 180 THR SER ILE GLU ASN VAL LEU LYS ARG TYR 190 ARG ASN ILE ASN ALA VAL VAL PRO GLY HIS 200 GLY GLU VAL GLY ASP LYS GLY LEU LEU LEU 210 HIS THR LEU ASP LEU LEU LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 132.8 -179.6 167.9 2 VAL -117.4 145.2 179.4 -170.8 3 ILE -137.8 121.9 -178.9 172.5 177.7 4 LYS -124.9 177.6 178.1 -56.4 -173.6 -179.2 -179.5 5 ASN -98.3 165.3 -179.1 49.4 -14.7 6 GLU -56.1 -34.9 179.5 -70.3 -55.1 -17.7 7 THR -79.1 -20.4 179.6 61.3 8 GLY 82.0 3.5 -179.7 9 THR -72.3 -28.2 179.3 53.0 10 ILE -118.8 125.7 -179.0 -61.9 -176.5 11 SER -132.6 145.2 178.6 167.3 12 ILE -131.9 122.3 -179.1 -62.5 160.6 13 SER -119.4 136.3 -179.3 -50.5 14 GLN -81.2 127.2 177.9 -176.0 168.8 43.8 15 LEU -91.4 -43.4 178.9 -96.6 -174.6 16 ASN -155.7 -170.9 -179.5 56.8 74.3 17 LYS -39.5 -53.4 -178.4 55.3 178.1 64.3 -176.6 18 ASN -121.4 11.1 -179.3 -63.2 -36.0 19 VAL -118.5 126.5 179.7 179.7 20 TRP -131.0 158.3 177.9 -62.6 66.6 21 VAL -112.0 126.8 177.0 175.1 22 HIS -101.2 136.3 -179.5 68.9 82.0 23 THR -133.0 127.6 179.0 -55.4 24 GLU -124.6 142.4 179.2 -54.7 77.6 49.7 25 LEU -98.1 121.7 179.0 -62.6 169.4 26 GLY -103.0 113.0 -179.9 27 SER -73.1 153.1 -80.8 -62.8 28 GLU 31.9 102.3 179.4 -59.2 172.1 -19.5 29 ALA -76.8 127.8 -179.4 30 VAL -120.7 113.5 -179.6 -167.5 31 PRO -76.1 156.9 179.0 35.6 -43.1 32 SER -146.5 132.8 180.0 -177.0 33 ASN -100.9 151.0 176.7 -68.1 -29.2 34 GLY -155.4 179.1 178.5 35 LEU -120.4 152.9 176.4 -74.6 -165.9 36 VAL -123.5 118.0 180.0 179.9 37 LEU -108.4 118.7 179.8 -50.5 175.9 38 ASN -91.0 104.2 -179.4 -174.5 16.1 39 THR -111.6 168.6 -179.8 87.5 40 SER -65.6 -15.7 -179.3 62.4 41 LYS -119.4 23.4 179.4 -61.1 -171.8 173.9 -176.2 42 GLY 125.9 -179.8 179.7 43 LEU -97.4 140.0 178.6 -59.7 170.2 44 VAL -125.7 130.4 180.0 176.3 45 LEU -110.3 149.8 174.0 -51.5 -171.6 46 VAL -110.0 107.7 -179.1 172.4 47 ASP 78.0 144.2 178.8 -76.8 -35.9 48 SER -94.4 -131.6 179.9 72.1 49 SER -142.1 178.2 -178.3 -160.2 50 TRP -43.9 -43.7 -179.9 -59.8 97.3 51 ASP -147.5 -172.5 -179.8 53.9 38.3 52 ASP -74.4 -32.6 179.3 -73.8 -53.8 53 LYS -65.3 -47.6 179.3 177.7 -176.6 -178.2 60.2 54 LEU -67.3 -42.5 -179.9 -77.3 175.2 55 THR -63.0 -46.0 179.3 -62.9 56 LYS -62.4 -43.9 179.7 179.2 177.6 174.9 177.7 57 GLU -61.2 -41.3 178.4 -168.7 178.0 -9.2 58 LEU -61.0 -51.8 179.5 169.0 58.8 59 ILE -58.0 -45.4 179.0 -67.2 166.7 60 GLU -58.2 -40.9 -179.5 -67.8 -70.0 -37.0 61 MET -63.4 -54.1 -179.1 -176.1 176.9 -54.2 62 VAL -67.8 -35.1 179.8 -59.0 63 GLU -66.1 -38.8 178.5 -67.4 -169.4 -13.1 64 LYS -70.7 -39.9 -179.7 169.1 -171.9 180.0 -179.1 65 LYS -62.7 -55.7 -177.9 170.6 68.1 174.4 -177.2 66 PHE -92.2 -4.4 179.3 -56.0 -79.1 67 GLN 57.5 43.4 179.3 -70.5 -69.8 -53.9 68 LYS -150.1 167.9 -179.1 51.7 -174.4 70.7 171.0 69 ARG -83.6 139.1 174.7 165.4 -164.7 171.9 -148.3 70 VAL -82.8 116.8 -176.9 167.2 71 THR -96.2 -37.5 -177.9 61.4 72 ASP -139.0 156.4 177.9 -55.8 73.5 73 VAL -142.7 133.1 177.8 173.4 74 ILE -102.9 121.8 179.7 -66.0 168.8 75 ILE -94.8 119.3 -178.1 -55.3 -57.3 76 THR -80.1 -22.9 175.1 61.5 77 HIS -169.1 162.1 -176.6 75.5 -85.2 78 ALA -82.0 42.6 177.4 79 HIS -111.7 157.4 -178.3 -79.8 165.5 80 ALA -43.3 -49.4 -179.1 81 ASP -62.3 -18.8 -178.8 63.2 -26.8 82 ARG -103.8 -43.8 -176.3 -52.0 -62.6 144.2 179.5 83 ILE -115.7 9.8 -178.8 -157.3 173.6 84 GLY -55.8 -30.6 -179.5 85 GLY -102.5 26.8 -179.3 86 ILE -55.7 -40.7 179.2 178.6 66.6 87 LYS -60.5 -40.5 179.2 176.0 -175.5 170.4 -178.2 88 THR -63.2 -41.5 -179.7 -61.3 89 LEU -61.7 -51.1 -178.9 -56.1 -171.5 90 LYS -63.5 -34.1 179.5 -55.2 -171.8 80.8 172.0 91 GLU -75.7 -19.9 -179.6 81.6 -170.1 0.4 92 ARG -101.7 10.8 179.5 -64.2 176.2 76.3 100.1 93 GLY 68.7 23.4 179.9 94 ILE -88.2 124.8 -179.9 -60.2 170.2 95 LYS -72.6 115.9 -179.9 -60.9 178.6 176.6 179.4 96 ALA -94.9 93.6 -179.9 97 HIS -76.2 145.4 178.4 -55.8 -86.5 98 SER -169.3 164.0 176.5 82.2 99 THR -76.9 165.1 179.1 58.0 100 ALA -61.3 -39.9 179.8 101 LEU -62.3 -41.7 178.5 -177.2 55.7 102 THR -63.1 -35.9 178.9 -66.2 103 ALA -67.4 -42.8 178.8 104 GLU -60.0 -49.9 179.6 178.1 -169.2 -49.4 105 LEU -67.9 -30.4 178.9 -59.7 -177.5 106 ALA -63.3 -44.1 179.2 107 LYS -61.2 -47.5 179.5 -168.9 -173.9 -165.2 171.6 108 LYS -60.9 -33.4 -179.8 174.9 -166.8 179.2 -57.1 109 ASN -87.0 5.1 178.9 -60.5 -9.8 110 GLY 85.5 8.2 179.6 111 TYR -92.9 154.6 177.3 -61.0 -72.9 112 GLU -64.9 151.8 -177.1 -77.0 -175.1 9.5 113 GLU -81.0 131.2 178.8 -90.6 -164.2 53.8 114 PRO -78.8 -179.7 -177.6 29.1 -41.9 115 LEU -60.4 -37.3 -179.1 -67.1 171.2 116 GLY 69.2 24.4 -178.1 117 ASP -85.5 -28.0 -177.9 58.6 -34.1 118 LEU -65.4 131.5 177.4 -55.9 -179.9 119 GLN -98.4 178.1 -179.7 -54.6 -55.2 -62.3 120 THR -50.9 -40.1 177.7 -66.1 121 VAL -131.4 112.0 -179.5 173.5 122 THR -130.8 123.1 178.5 -50.7 123 ASN -101.8 128.2 -179.3 -66.6 103.8 124 LEU -126.5 140.7 178.6 -59.3 160.6 125 LYS -129.5 123.6 -179.8 -170.5 173.9 -173.6 176.5 126 PHE -116.5 99.1 -177.6 -50.3 -86.7 127 GLY 73.8 -118.0 179.1 128 ASN -101.7 -10.4 -179.5 -176.6 40.0 129 MET -75.8 117.1 179.0 178.7 63.8 71.0 130 LYS -98.0 136.8 -179.0 -59.7 -178.5 -175.1 -178.8 131 VAL -136.1 135.1 177.5 179.4 132 GLU -124.1 127.4 177.5 -179.2 -171.4 -72.7 133 THR -103.5 142.1 -177.6 67.8 134 PHE -140.7 129.0 177.0 174.0 51.3 135 TYR -96.3 106.9 -179.1 174.2 62.5 136 PRO -86.2 -5.5 -177.8 40.7 -43.7 137 GLY 118.3 178.9 -178.9 138 LYS -70.7 145.1 179.5 -49.2 173.7 -174.4 -179.4 139 GLY -159.0 -106.7 178.1 140 HIS -55.0 -37.7 177.2 168.7 62.9 141 THR -143.2 171.8 179.6 56.4 142 GLU -70.5 -26.7 -175.8 -178.8 -173.3 9.7 143 ASP -104.3 -7.0 -177.9 66.3 -45.9 144 ASN -48.3 132.2 178.4 58.0 -157.8 145 ILE -123.4 163.4 177.3 60.2 166.2 146 VAL -117.5 160.4 179.6 -62.5 147 VAL -124.0 133.6 -178.3 -177.8 148 TRP -121.5 131.1 178.2 172.7 -109.5 149 LEU -108.3 93.7 -179.3 -52.0 -179.0 150 PRO -57.1 -23.9 179.8 32.2 -43.6 151 GLN -79.0 -21.1 -179.0 -60.0 163.5 -53.1 152 TYR -118.3 -12.1 -177.1 -54.3 -85.4 153 ASN 58.4 42.6 179.0 -76.4 -169.8 154 ILE -102.2 132.3 179.3 -68.9 179.8 155 LEU -114.3 124.0 177.4 176.9 70.2 156 VAL -98.0 105.7 -178.4 -178.9 157 GLY -82.6 -18.6 -177.7 158 GLY 65.2 -80.1 64.0 159 LEU 59.2 -20.5 -178.7 -177.5 80.3 160 VAL -119.5 127.6 179.4 179.7 161 LYS -94.3 153.3 179.4 -54.2 -60.0 151.9 179.3 162 SER -78.4 168.4 -177.0 64.5 163 THR -57.9 -33.6 179.8 -150.5 164 SER -90.9 -13.5 -179.5 -63.4 165 ALA -67.5 125.6 179.6 166 LYS -118.6 -1.8 -178.5 -62.4 163.1 178.1 60.9 167 ASP -118.7 133.7 179.3 -164.3 -42.8 168 LEU -75.1 -12.2 -179.5 -66.1 168.5 169 GLY 87.9 -152.4 179.9 170 ASN -69.0 115.9 179.7 -178.0 -25.0 171 VAL -112.2 11.1 179.3 -68.3 172 ALA -64.5 -34.9 179.9 173 ASP -105.3 8.2 -178.4 -57.4 -43.8 174 ALA -90.4 158.6 177.4 175 TYR -117.9 76.4 -177.8 -68.0 74.6 176 VAL -49.9 -46.9 -179.9 178.3 177 ASN -66.1 -40.3 -179.8 -170.6 68.8 178 GLU -77.7 -21.2 -179.0 -65.7 -178.8 36.6 179 TRP -50.4 -42.2 179.9 -161.9 -30.5 180 SER -62.1 -43.1 179.1 -75.1 181 THR -64.3 -39.3 -179.7 -58.6 182 SER -63.0 -42.3 178.3 -59.0 183 ILE -65.9 -37.9 178.9 -71.6 174.0 184 GLU -62.6 -34.2 179.2 -66.2 -64.5 -8.5 185 ASN -66.9 -34.0 179.2 -70.2 -21.7 186 VAL -70.4 -43.6 179.7 175.8 187 LEU -63.4 -40.9 179.3 -68.1 169.5 188 LYS -69.3 -39.1 -179.1 -67.9 170.2 -174.2 -179.5 189 ARG -68.8 -42.9 -179.0 -179.5 172.0 -174.4 75.6 190 TYR -112.0 95.8 -178.2 -48.4 -67.3 191 ARG -78.1 -13.8 179.6 -61.9 -44.1 -140.3 -52.7 192 ASN -134.2 76.2 -179.3 -72.3 -92.9 193 ILE -89.6 141.4 177.1 -56.0 167.8 194 ASN -104.4 -90.1 179.6 -76.2 -9.6 195 ALA -90.5 147.5 178.8 196 VAL -129.4 124.4 179.7 174.1 197 VAL -100.3 117.3 179.8 -173.4 198 PRO -81.9 164.8 179.6 36.7 -42.3 199 GLY -51.8 -39.4 176.4 200 HIS -153.2 149.7 -177.3 59.3 -94.2 201 GLY 108.9 -177.3 -178.4 202 GLU -76.4 146.5 178.0 -59.3 -61.9 -76.6 203 VAL -63.4 137.8 179.5 166.6 204 GLY -138.9 -139.7 179.9 205 ASP -137.1 -163.2 -179.3 62.4 4.7 206 LYS -54.2 -23.8 178.7 -179.1 178.3 162.9 179.4 207 GLY -60.2 -23.6 178.5 208 LEU -68.9 -33.8 178.2 -71.8 -178.2 209 LEU -70.1 -40.1 178.9 -69.5 152.3 210 LEU -67.6 -37.3 178.4 -54.1 -177.9 211 HIS -62.8 -45.1 179.7 167.7 55.4 212 THR -64.2 -39.0 177.8 -52.2 213 LEU -64.4 -35.8 179.2 -76.4 168.1 214 ASP -63.4 -46.0 179.3 -173.6 26.4 215 LEU -60.6 -35.9 -179.3 -65.3 -179.0 216 LEU -76.1 -16.6 -179.6 -70.8 155.4 217 LYS -59.5 128.4 0.0 -69.8 -159.1 167.8 -165.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR 15.324 7.209 26.852 2 VAL 15.983 9.236 23.688 3 ILE 13.800 11.853 21.961 4 LYS 14.475 13.310 18.507 5 ASN 12.955 15.440 15.761 6 GLU 11.591 14.168 12.419 7 THR 14.767 15.220 10.614 8 GLY 16.876 13.564 13.316 9 THR 19.156 16.593 13.715 10 ILE 18.186 17.151 17.371 11 SER 18.252 14.400 19.989 12 ILE 17.850 14.363 23.779 13 SER 18.906 11.363 25.875 14 GLN 18.289 10.841 29.577 15 LEU 21.303 10.294 31.855 16 ASN 19.284 10.279 35.072 17 LYS 16.128 11.605 36.756 18 ASN 16.696 15.289 35.905 19 VAL 19.750 15.200 33.630 20 TRP 19.573 14.776 29.871 21 VAL 22.081 15.202 27.076 22 HIS 21.107 17.266 24.043 23 THR 22.867 16.506 20.761 24 GLU 22.606 18.438 17.485 25 LEU 24.103 17.681 14.073 26 GLY 25.668 20.620 12.276 27 SER 25.888 20.105 8.517 28 GLU 28.695 16.392 6.624 29 ALA 26.708 16.290 9.868 30 VAL 28.810 17.291 12.886 31 PRO 27.388 16.537 16.383 32 SER 27.688 18.634 19.529 33 ASN 26.730 17.622 23.089 34 GLY 25.213 19.736 25.823 35 LEU 23.040 19.114 28.896 36 VAL 19.392 19.767 29.692 37 LEU 18.692 20.081 33.407 38 ASN 15.076 19.686 34.473 39 THR 14.683 21.669 37.709 40 SER 11.776 22.672 39.952 41 LYS 12.158 26.238 38.662 42 GLY 12.657 25.727 34.928 43 LEU 15.050 24.188 32.405 44 VAL 18.785 24.876 32.417 45 LEU 21.049 24.063 29.499 46 VAL 24.781 23.597 29.365 47 ASP 25.615 25.022 25.914 48 SER 23.325 26.094 23.064 49 SER 23.773 24.904 19.454 50 TRP 25.480 25.526 16.089 51 ASP 23.157 28.371 15.073 52 ASP 19.911 30.146 15.931 53 LYS 17.661 27.803 13.936 54 LEU 18.966 24.719 15.757 55 THR 19.041 26.476 19.137 56 LYS 15.458 27.742 18.854 57 GLU 14.326 24.283 17.717 58 LEU 16.175 22.704 20.670 59 ILE 14.547 25.124 23.136 60 GLU 11.097 24.558 21.562 61 MET 11.608 20.809 21.981 62 VAL 12.557 20.709 25.668 63 GLU 10.028 23.387 26.648 64 LYS 7.229 21.406 25.011 65 LYS 8.632 18.236 26.554 66 PHE 8.918 19.443 30.159 67 GLN 6.234 22.139 29.890 68 LYS 8.505 24.796 31.350 69 ARG 10.748 27.745 30.499 70 VAL 14.469 27.426 29.727 71 THR 15.763 30.017 32.179 72 ASP 19.555 29.782 31.966 73 VAL 22.276 28.452 29.688 74 ILE 25.943 27.986 30.542 75 ILE 28.264 28.652 27.571 76 THR 31.522 26.625 27.781 77 HIS 33.509 28.519 25.112 78 ALA 33.068 31.083 22.323 79 HIS 32.704 28.779 19.284 80 ALA 29.636 28.197 17.070 81 ASP 28.687 24.815 18.551 82 ARG 28.558 26.394 22.016 83 ILE 27.404 29.983 21.515 84 GLY 25.844 29.839 18.033 85 GLY 22.327 30.468 19.305 86 ILE 23.122 33.405 21.612 87 LYS 20.723 35.727 19.755 88 THR 17.900 33.206 20.326 89 LEU 18.751 33.064 24.038 90 LYS 18.740 36.825 24.445 91 GLU 15.462 37.289 22.551 92 ARG 13.732 34.698 24.764 93 GLY 14.944 36.192 28.033 94 ILE 17.280 33.262 28.658 95 LYS 20.259 34.167 30.828 96 ALA 23.435 33.269 28.929 97 HIS 26.109 32.684 31.573 98 SER 29.789 32.778 30.625 99 THR 33.147 33.899 31.970 100 ALA 34.238 37.462 31.107 101 LEU 36.868 36.057 28.717 102 THR 34.239 34.004 26.854 103 ALA 32.152 37.187 26.490 104 GLU 35.197 39.076 25.158 105 LEU 35.956 36.348 22.592 106 ALA 32.257 36.012 21.620 107 LYS 32.282 39.689 20.651 108 LYS 35.524 39.218 18.677 109 ASN 34.020 36.242 16.808 110 GLY 30.953 38.286 15.859 111 TYR 28.483 36.744 18.320 112 GLU 26.200 38.701 20.629 113 GLU 27.704 38.942 24.105 114 PRO 26.835 36.530 26.929 115 LEU 26.725 37.717 30.573 116 GLY 30.409 37.354 31.486 117 ASP 29.337 36.663 35.069 118 LEU 31.129 33.367 35.731 119 GLN 34.261 33.461 37.872 120 THR 36.931 30.699 37.951 121 VAL 34.757 28.778 40.433 122 THR 31.042 29.604 40.382 123 ASN 28.336 27.586 42.138 124 LEU 24.796 27.964 40.829 125 LYS 21.636 26.378 42.153 126 PHE 18.414 26.186 40.168 127 GLY 15.760 24.760 42.451 128 ASN 17.385 21.643 43.902 129 MET 19.796 21.233 40.977 130 LYS 23.375 22.152 41.872 131 VAL 25.881 23.228 39.216 132 GLU 29.539 24.216 39.506 133 THR 31.438 25.914 36.683 134 PHE 35.219 25.741 36.654 135 TYR 37.866 27.434 34.502 136 PRO 40.786 24.951 34.426 137 GLY 43.052 27.023 32.205 138 LYS 43.672 27.170 28.444 139 GLY 43.154 24.107 26.251 140 HIS 40.821 23.681 23.267 141 THR 40.462 27.467 23.503 142 GLU 41.814 30.167 25.814 143 ASP 38.424 30.393 27.556 144 ASN 37.099 26.817 27.868 145 ILE 35.384 25.883 31.148 146 VAL 33.979 22.622 32.505 147 VAL 30.705 22.059 34.376 148 TRP 30.326 19.794 37.420 149 LEU 27.076 18.440 38.890 150 PRO 28.128 17.549 42.499 151 GLN 24.899 15.653 43.262 152 TYR 25.583 13.209 40.406 153 ASN 29.366 13.582 40.110 154 ILE 28.840 14.235 36.411 155 LEU 31.483 16.217 34.525 156 VAL 30.697 18.131 31.347 157 GLY 34.086 18.478 29.707 158 GLY 33.039 20.368 26.593 159 LEU 38.444 20.135 26.354 160 VAL 37.592 16.412 26.421 161 LYS 37.594 14.067 23.438 162 SER 35.444 10.949 23.051 163 THR 36.686 7.341 23.071 164 SER 36.807 6.911 19.249 165 ALA 38.275 10.382 18.732 166 LYS 41.849 10.315 17.465 167 ASP 41.764 13.952 16.394 168 LEU 41.919 16.973 18.745 169 GLY 39.827 18.999 16.299 170 ASN 40.379 22.687 15.525 171 VAL 43.638 23.750 17.218 172 ALA 44.000 27.171 15.572 173 ASP 42.590 28.820 18.718 174 ALA 43.953 26.129 21.011 175 TYR 46.796 26.131 23.525 176 VAL 47.948 22.581 22.858 177 ASN 50.870 22.647 25.282 178 GLU 48.830 24.082 28.181 179 TRP 45.868 21.795 27.451 180 SER 47.505 18.948 29.403 181 THR 47.959 21.031 32.561 182 SER 44.341 22.175 32.293 183 ILE 43.065 18.600 32.145 184 GLU 45.295 17.798 35.130 185 ASN 43.615 20.665 37.039 186 VAL 40.204 19.091 36.391 187 LEU 41.471 15.694 37.572 188 LYS 43.007 17.192 40.741 189 ARG 39.891 19.209 41.531 190 TYR 37.384 16.360 41.143 191 ARG 38.751 13.194 42.764 192 ASN 35.587 11.096 42.412 193 ILE 34.103 11.467 38.937 194 ASN 31.356 9.211 37.587 195 ALA 30.102 10.144 34.093 196 VAL 31.982 12.492 31.745 197 VAL 30.263 14.179 28.790 198 PRO 32.654 15.047 25.932 199 GLY 32.108 17.994 23.559 200 HIS 30.897 15.449 21.025 201 GLY 30.705 11.674 21.061 202 GLU 29.417 9.206 23.658 203 VAL 29.228 9.798 27.411 204 GLY 32.017 8.007 29.252 205 ASP 34.047 8.328 32.425 206 LYS 37.348 9.652 33.792 207 GLY 39.050 7.485 31.158 208 LEU 38.055 10.109 28.559 209 LEU 40.291 12.671 30.295 210 LEU 43.187 10.166 30.276 211 HIS 42.463 9.428 26.601 212 THR 42.628 13.148 25.781 213 LEU 45.945 13.479 27.683 214 ASP 47.187 10.548 25.598 215 LEU 46.244 12.338 22.361 216 LEU 48.071 15.478 23.559 217 LYS 51.327 13.616 24.305 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S T T T T S S 10 S S S S S S/T T T T/S S 20 S S S S S S/T T/X X/T T/S S 30 S S S S S S S S S/T T 40 T T/S S S S S S/S S S S 50 H H H H H H H H H H 60 H H H H H H H/S S S S 70 S S/S S S S S S C T T 80 T T C C H H H H H H 90 H H H/S S S S S S S/H H 100 H H H H H H H H H H/S 110 S S S C C C S S S S/S 120 S S S S S/T T T T/S S S 130 S S S S S S S T T T 140 T S S S S S S S S/T T 150 T T S S S S S S/X X/S S 160 S S S C C C C C C C 170 T T T T C C C H H H 180 H H H H H H H H H H 190 H/S S S S S/S S S S S/S S 200 S S/S S S S/H H H H 3 3/H 210 H H H H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E e T T t e E 10 E E E E E E T e E E 20 E E E E E E E 30 E E E E E E E E E T 40 T E E E E E e S 50 h H H H H H H H H H 60 H H H H H H h t e E 70 E E E E e S S h H 80 H H H h h H H H H H 90 H h T t E E E h H 100 H H H H H H H H h T 110 t B e 120 E E E E E E T T E E 130 E E E E e S S S 140 S S S E E E E T 150 T T T E E E E E 160 t T T t 170 S S h H H H H H 180 H H H H H H H H H h 190 S S e E E E e S 200 S B t h H H H H 210 H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 36.6 34.2 74.2 2 VAL 60.0 50.5 70.8 3 ILE 93.7 65.3 52.8 4 LYS 75.1 43.3 72.1 5 ASN 103.7 85.8 67.1 6 GLU 0.0 0.0 87.7 7 THR 24.4 22.8 81.1 8 GLY 16.9 48.5 74.6 9 THR 67.8 63.4 68.3 10 ILE 143.5 100.0 45.5 11 SER 70.3 84.1 50.7 12 ILE 142.6 99.4 32.1 13 SER 45.6 54.6 62.3 14 GLN 105.4 70.9 58.5 15 LEU 116.0 78.5 42.3 16 ASN 85.6 70.8 47.6 17 LYS 33.2 19.1 85.8 18 ASN 69.5 57.5 68.7 19 VAL 118.8 100.0 34.3 20 TRP 192.1 93.7 47.4 21 VAL 108.0 90.9 46.4 22 HIS 149.4 99.5 51.3 23 THR 72.9 68.2 65.7 24 GLU 138.2 99.7 46.2 25 LEU 90.6 61.3 57.1 26 GLY 28.0 80.5 52.9 27 SER 21.6 25.9 76.2 28 GLU 0.0 0.0 91.8 29 ALA 41.5 57.1 61.2 30 VAL 50.3 42.4 64.1 31 PRO 81.3 65.3 53.2 32 SER 81.5 97.5 64.4 33 ASN 115.6 95.6 58.5 34 GLY 34.7 99.6 55.9 35 LEU 147.8 100.0 24.5 36 VAL 118.8 100.0 27.8 37 LEU 147.8 100.0 28.9 38 ASN 93.2 77.1 54.0 39 THR 102.1 95.5 53.9 40 SER 24.0 28.7 72.2 41 LYS 27.8 16.0 88.0 42 GLY 31.5 90.5 63.2 43 LEU 147.8 100.0 38.2 44 VAL 118.4 99.7 40.4 45 LEU 147.8 100.0 32.3 46 VAL 118.8 100.0 32.7 47 ASP 109.7 99.3 54.8 48 SER 83.6 100.0 44.4 49 SER 83.6 100.0 52.1 50 TRP 151.1 73.7 54.0 51 ASP 47.6 43.1 67.4 52 ASP 65.3 59.1 69.6 53 LYS 15.0 8.6 87.0 54 LEU 128.6 87.0 57.5 55 THR 106.9 100.0 44.5 56 LYS 70.6 40.7 76.6 57 GLU 83.5 60.3 59.3 58 LEU 147.8 100.0 35.0 59 ILE 143.5 100.0 37.5 60 GLU 63.5 45.8 72.5 61 MET 135.1 84.8 48.3 62 VAL 118.8 100.0 23.9 63 GLU 106.8 77.1 63.3 64 LYS 16.1 9.3 89.7 65 LYS 99.0 57.1 52.4 66 PHE 147.8 88.6 41.4 67 GLN 28.0 18.9 83.7 68 LYS 110.2 63.5 74.1 69 ARG 83.2 39.8 75.4 70 VAL 118.8 100.0 32.7 71 THR 88.7 82.9 65.3 72 ASP 98.6 89.3 41.3 73 VAL 118.8 100.0 34.0 74 ILE 143.5 100.0 23.6 75 ILE 143.5 100.0 40.8 76 THR 106.1 99.2 50.0 77 HIS 142.0 94.5 57.6 78 ALA 70.6 97.3 46.0 79 HIS 114.2 76.0 65.4 80 ALA 38.4 52.8 66.6 81 ASP 90.1 81.5 51.9 82 ARG 203.8 97.5 67.4 83 ILE 143.5 100.0 36.0 84 GLY 33.7 96.9 63.2 85 GLY 34.8 100.0 66.2 86 ILE 139.2 97.0 38.3 87 LYS 56.0 32.3 82.2 88 THR 104.0 97.3 44.5 89 LEU 147.8 100.0 29.7 90 LYS 90.4 52.1 74.9 91 GLU 58.0 41.8 68.7 92 ARG 148.9 71.3 62.9 93 GLY 0.0 0.0 83.2 94 ILE 142.3 99.1 48.4 95 LYS 53.5 30.9 77.0 96 ALA 70.7 97.3 38.1 97 HIS 136.9 91.2 43.3 98 SER 83.6 100.0 46.6 99 THR 93.6 87.6 53.2 100 ALA 10.8 14.8 78.0 101 LEU 100.1 67.7 65.2 102 THR 106.6 99.7 55.1 103 ALA 65.8 90.6 61.7 104 GLU 35.1 25.4 71.4 105 LEU 117.0 79.2 59.5 106 ALA 72.6 100.0 44.7 107 LYS 41.0 23.6 85.7 108 LYS 32.8 18.9 83.6 109 ASN 79.2 65.5 63.9 110 GLY 0.5 1.3 83.9 111 TYR 129.9 71.7 59.8 112 GLU 62.3 44.9 61.4 113 GLU 81.5 58.8 62.6 114 PRO 123.9 99.5 43.9 115 LEU 72.3 48.9 70.2 116 GLY 30.8 88.6 65.9 117 ASP 62.3 56.3 64.7 118 LEU 147.4 99.7 45.5 119 GLN 32.1 21.6 89.3 120 THR 39.1 36.6 65.6 121 VAL 75.0 63.1 72.4 122 THR 81.7 76.4 59.3 123 ASN 43.0 35.6 70.6 124 LEU 113.6 76.9 46.8 125 LYS 86.7 50.0 71.1 126 PHE 140.4 84.1 47.9 127 GLY 29.1 83.6 68.5 128 ASN 15.9 13.1 84.4 129 MET 154.2 96.7 44.7 130 LYS 83.8 48.3 67.1 131 VAL 118.8 100.0 32.0 132 GLU 120.7 87.1 59.5 133 THR 105.9 99.0 38.2 134 PHE 148.3 88.9 50.0 135 TYR 133.0 73.5 54.8 136 PRO 123.7 99.4 42.2 137 GLY 16.5 47.4 64.3 138 LYS 109.8 63.3 69.3 139 GLY 34.8 100.0 54.9 140 HIS 128.5 85.5 57.2 141 THR 102.4 95.8 54.5 142 GLU 92.8 67.0 50.5 143 ASP 109.2 98.8 43.0 144 ASN 117.6 97.3 57.7 145 ILE 142.0 98.9 41.5 146 VAL 118.6 99.8 35.4 147 VAL 118.8 100.0 27.9 148 TRP 183.0 89.3 45.0 149 LEU 147.7 100.0 28.0 150 PRO 88.6 71.2 60.5 151 GLN 100.7 67.8 62.1 152 TYR 141.5 78.2 50.6 153 ASN 81.1 67.1 64.9 154 ILE 135.8 94.6 39.8 155 LEU 147.8 100.0 26.3 156 VAL 115.9 97.6 37.7 157 GLY 34.8 100.0 47.1 158 GLY 31.8 91.3 63.4 159 LEU 147.5 99.8 41.4 160 VAL 118.8 100.0 38.9 161 LYS 157.1 90.6 47.0 162 SER 73.8 88.3 51.9 163 THR 21.7 20.3 72.4 164 SER 11.9 14.3 83.0 165 ALA 55.7 76.8 72.4 166 LYS 29.3 16.9 79.0 167 ASP 13.7 12.4 83.5 168 LEU 120.9 81.8 41.1 169 GLY 6.7 19.3 79.9 170 ASN 38.9 32.2 74.6 171 VAL 62.9 52.9 62.1 172 ALA 9.5 13.1 88.9 173 ASP 39.4 35.7 78.7 174 ALA 72.6 100.0 51.5 175 TYR 105.0 58.0 72.3 176 VAL 61.1 51.4 57.1 177 ASN 0.0 0.0 84.0 178 GLU 63.4 45.7 72.5 179 TRP 205.0 100.0 39.4 180 SER 47.4 56.6 61.3 181 THR 25.4 23.8 79.2 182 SER 80.9 96.8 57.2 183 ILE 143.5 100.0 35.4 184 GLU 75.4 54.4 56.9 185 ASN 72.7 60.1 61.8 186 VAL 118.8 100.0 26.8 187 LEU 132.6 89.7 45.0 188 LYS 55.1 31.8 81.5 189 ARG 128.8 61.7 59.1 190 TYR 170.1 94.0 41.7 191 ARG 61.9 29.6 86.0 192 ASN 10.7 8.9 83.8 193 ILE 143.4 100.0 40.8 194 ASN 31.2 25.8 81.5 195 ALA 51.4 70.8 46.7 196 VAL 118.8 100.0 38.5 197 VAL 118.2 99.5 31.4 198 PRO 124.5 100.0 56.4 199 GLY 28.9 83.0 70.4 200 HIS 75.6 50.4 70.3 201 GLY 13.3 38.1 67.4 202 GLU 3.0 2.2 85.6 203 VAL 89.1 75.0 46.6 204 GLY 12.9 37.0 64.5 205 ASP 31.3 28.3 74.8 206 LYS 89.8 51.8 56.9 207 GLY 11.8 33.8 70.6 208 LEU 139.3 94.3 53.1 209 LEU 147.6 99.9 26.6 210 LEU 60.1 40.7 62.6 211 HIS 108.6 72.3 63.1 212 THR 106.9 100.0 43.4 213 LEU 126.8 85.8 52.0 214 ASP 29.7 26.9 73.6 215 LEU 118.9 80.5 57.5 216 LEU 145.9 98.7 45.9 217 LYS 25.7 14.8 90.1