Protein Data Bank File : 1dfmb Title : HYDROLASE/DNA 06-DEC-99 1DFM Number of Amino Acid Residues : 213 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS ILE ASP ILE THR ASP TYR ASN HIS ALA 10 ASP GLU ILE LEU ASN PRO GLN LEU TRP LYS 20 GLU ILE GLU GLU THR LEU LEU LYS PRO LEU 30 HIS VAL LYS ALA SER ASP GLN ALA SER LYS 40 VAL GLY SER LEU ILE PHE ASP PRO VAL GLY 50 THR ASN GLN TYR ILE LYS ASP GLU LEU VAL 60 PRO LYS HIS TRP LYS ASN ASN ILE PRO ILE 70 PRO LYS ARG PHE ASP PHE LEU GLY THR ASP 80 ILE ASP PHE GLY LYS ARG ASP THR LEU VAL 90 GLU VAL GLN PHE SER ASN TYR PRO PHE LEU 100 LEU ASN ASN THR VAL ARG SER GLU LEU PHE 110 HIS LYS SER ASN ASP ILE ASP GLU GLU GLY 120 LYS VAL ALA ILE ILE ILE THR LYS GLY HIS 130 PHE PRO ALA SER ASN SER SER LEU TYR TYR 140 GLU GLN ALA GLN ASN GLN LEU ASN SER LEU 150 ALA GLU TYR ASN VAL PHE ASP VAL PRO ILE 160 ARG LEU VAL GLY LEU ILE GLU ASP PHE GLU 170 THR ASP ILE ASP ILE VAL SER THR THR TYR 180 ALA ASP LYS ARG TYR SER ARG THR ILE THR 190 LYS ARG ASP THR VAL LYS GLY LYS VAL ILE 200 ASP THR ASN THR ARG LYS ARG GLY THR ILE 210 VAL THR TYR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 164.0 -178.6 -66.6 -166.4 176.2 -49.3 2 ILE -140.0 153.6 174.0 62.3 173.3 3 ASP -128.3 144.8 -177.6 -164.4 66.9 4 ILE -127.0 141.4 172.9 -62.7 154.2 5 THR -133.6 126.8 -178.1 -55.7 6 ASP -107.7 143.3 178.8 -70.9 -49.2 7 TYR -125.3 146.9 178.7 -58.5 -85.6 8 ASN 50.8 43.4 175.2 -69.3 -54.8 9 HIS 63.7 29.9 179.4 -58.3 -72.9 10 ALA -58.8 -26.6 -179.5 11 ASP -60.5 -37.9 179.6 54.1 -53.5 12 GLU -97.1 -19.3 -178.8 42.7 168.0 3.0 13 ILE -84.8 -35.9 -179.7 -67.9 172.8 14 LEU -62.6 129.5 179.1 179.1 61.8 15 ASN -61.0 124.0 -179.1 -178.5 -85.1 16 PRO -57.5 -37.5 -178.3 -26.0 38.2 17 GLN -69.1 -44.4 177.2 170.8 58.0 38.8 18 LEU -63.0 -41.9 175.6 -59.0 -176.7 19 TRP -58.5 -42.1 -178.8 173.7 -122.1 20 LYS -56.6 -37.8 -177.5 175.6 -89.8 -162.2 -172.0 21 GLU -68.4 -36.1 179.2 -63.8 174.8 14.7 22 ILE -76.0 -46.5 -177.1 -61.9 -56.9 23 GLU -60.9 -43.2 -177.9 -174.3 172.5 54.3 24 GLU -63.4 -33.2 178.1 73.4 -169.0 -12.8 25 THR -66.8 -46.9 -179.2 -71.1 26 LEU -66.6 -36.4 -178.4 -56.3 -176.3 27 LEU -70.2 -33.2 -177.5 -70.7 168.1 28 LYS -84.7 73.8 23.7 68.4 -179.1 -69.6 -145.4 29 PRO -129.3 159.6 175.6 20.7 -30.3 30 LEU -69.3 130.6 178.8 167.0 60.4 31 HIS -103.5 132.8 -179.2 -72.1 76.4 32 VAL -134.2 160.2 177.3 -55.1 33 LYS -153.6 174.9 -179.7 63.1 84.2 96.7 -152.4 34 ALA -82.1 135.5 173.2 35 SER -72.0 150.7 172.0 173.4 36 ASP -118.0 17.9 178.1 -157.9 46.7 37 GLN -69.6 137.7 -173.3 -178.7 -178.5 -36.9 38 ALA -45.9 -45.5 -177.6 39 SER -86.5 2.3 -172.5 68.1 40 LYS -148.6 38.9 -179.0 54.9 -177.2 60.5 175.7 41 VAL -59.2 130.5 -179.5 173.8 42 GLY 90.8 -16.0 179.1 43 SER -65.8 147.4 -179.3 65.4 44 LEU -78.7 132.4 179.7 -62.4 177.5 45 ILE -133.0 162.3 174.6 56.6 170.1 46 PHE -56.1 130.6 -178.8 -173.4 89.9 47 ASP -100.8 104.8 -179.7 171.6 15.5 48 PRO -70.2 -29.6 -179.5 32.7 -39.3 49 VAL -65.6 -52.1 -179.8 173.9 50 GLY -65.2 -38.0 179.5 51 THR -64.3 -48.9 178.1 -56.6 52 ASN -57.8 -42.7 -177.9 -86.9 -54.2 53 GLN -67.7 -37.6 179.7 -174.0 65.9 49.3 54 TYR -61.7 -47.8 179.1 -176.9 -78.9 55 ILE -61.2 -44.4 177.9 -68.0 168.5 56 LYS -58.9 -44.3 -178.3 179.3 175.6 166.5 -170.8 57 ASP -66.2 -25.2 179.0 -69.1 -20.2 58 GLU -89.1 -38.0 -175.2 -66.8 -72.4 -42.9 59 LEU -82.5 -33.1 -178.3 -63.5 -171.2 60 VAL -60.7 -42.0 179.4 173.5 61 PRO -69.0 -15.7 176.3 -23.0 35.5 62 LYS -91.9 13.9 177.9 -68.6 -162.3 -75.7 -154.3 63 HIS 73.7 23.6 172.7 -61.7 -60.2 64 TRP -91.9 113.5 -179.6 -74.6 77.2 65 LYS -71.7 140.9 -178.0 -59.5 -153.8 177.0 -66.2 66 ASN -103.6 142.3 178.2 175.8 -113.9 67 ASN 50.4 55.7 177.5 -74.2 172.8 68 ILE -67.9 130.8 -179.9 -67.6 169.7 69 PRO -69.2 142.6 177.0 27.9 -37.4 70 ILE -86.0 128.3 -179.5 -74.8 169.2 71 PRO -52.3 149.9 -178.3 -30.8 42.1 72 LYS -51.7 -38.5 -178.6 -172.1 -177.6 178.9 179.9 73 ARG -60.6 -17.8 -179.5 67.6 -165.7 171.6 104.5 74 PHE -123.6 19.3 -176.7 -55.0 -31.8 75 ASP -60.1 -20.4 178.1 68.6 -11.5 76 PHE -71.9 -13.1 177.0 54.9 83.6 77 LEU -89.9 -10.9 179.2 -66.8 170.0 78 GLY 144.1 178.7 -179.3 79 THR -98.6 -33.2 -177.9 57.2 80 ASP -158.8 169.3 178.8 57.9 18.2 81 ILE -118.7 145.0 -174.3 -67.6 168.6 82 ASP -56.5 -56.1 178.5 -74.5 -12.2 83 PHE -146.1 160.1 175.1 -59.7 -84.8 84 GLY -160.3 147.8 175.1 85 LYS -151.4 131.7 -176.1 -173.0 170.9 174.9 176.7 86 ARG 53.7 -121.2 -176.4 -50.6 -56.8 -169.7 -173.6 87 ASP -104.5 19.4 -175.0 59.1 -4.9 88 THR -118.7 128.7 178.6 -57.2 89 LEU -101.5 145.2 175.9 166.9 163.7 90 VAL -129.6 131.1 172.8 174.7 91 GLU -119.5 132.0 176.8 -63.4 -68.4 6.9 92 VAL -105.6 115.8 -169.0 179.1 93 GLN -128.7 98.6 -179.9 -170.9 50.4 -98.1 94 PHE -116.1 6.8 178.4 -53.3 -50.1 95 SER -80.1 -164.4 -173.4 -177.6 96 ASN -71.0 151.6 -171.8 63.7 148.4 97 TYR -47.3 -33.3 179.0 68.3 -87.1 98 PRO -63.7 -19.5 176.1 23.9 -37.6 99 PHE -59.1 -23.5 179.3 -89.4 -68.0 100 LEU -62.9 -49.2 -179.3 -178.3 -84.0 101 LEU -73.3 -30.8 176.1 -69.0 175.6 102 ASN -65.7 -44.6 -179.5 160.4 -72.9 103 ASN -67.4 -35.8 178.3 -76.7 -172.8 104 THR -67.6 -49.2 -177.9 -64.1 105 VAL -67.0 -40.7 -179.4 173.3 106 ARG -68.7 -30.0 176.9 80.3 -172.5 -156.4 155.3 107 SER -66.4 -37.9 176.6 -65.6 108 GLU -60.8 -44.3 -179.0 176.4 77.0 -24.8 109 LEU -71.4 -35.5 177.0 -64.5 172.0 110 PHE -61.6 -39.1 -179.8 -65.1 -20.9 111 HIS -68.7 -47.9 -177.9 -175.1 -125.5 112 LYS -63.1 -33.2 -180.0 -71.6 -145.2 179.3 73.7 113 SER -95.9 8.3 179.8 72.8 114 ASN 51.2 143.7 15.8 -59.8 -63.2 115 ASP -117.8 134.3 179.0 -73.5 -30.2 116 ILE -95.9 -73.8 180.0 -65.6 -54.1 117 ASP -133.5 76.5 -179.5 170.8 30.8 118 GLU 64.8 12.0 178.4 -49.0 -73.8 50.6 119 GLU -141.8 148.5 178.8 -66.7 -174.1 27.4 120 GLY -67.1 -115.3 24.4 121 LYS -177.7 -24.1 -177.3 -65.1 -56.7 -163.3 -73.1 122 VAL -153.9 147.1 176.0 53.8 123 ALA -118.5 144.7 174.1 124 ILE -115.8 127.0 178.3 -63.7 171.1 125 ILE -118.5 119.1 -178.3 -62.7 -179.8 126 ILE -100.5 130.8 -177.1 -64.5 163.1 127 THR -136.9 168.5 178.0 62.7 128 LYS -104.5 144.0 177.6 60.5 179.5 167.8 59.4 129 GLY -65.5 151.0 175.2 130 HIS -54.5 55.0 76.6 178.0 -95.7 131 PHE 14.6 132.5 177.1 -53.9 -69.3 132 PRO -64.7 148.9 -175.4 19.3 -31.6 133 ALA -163.4 170.5 176.5 134 SER -52.5 145.8 178.1 61.7 135 ASN -58.3 140.1 176.7 -80.6 -14.2 136 SER 69.1 1.6 174.5 -61.5 137 SER -65.2 140.4 -179.6 53.1 138 LEU -58.8 145.7 173.6 178.8 68.1 139 TYR -134.2 158.3 -173.5 56.7 -86.9 140 TYR -56.1 -45.9 -175.0 177.6 63.6 141 GLU -68.5 -31.5 177.5 -66.8 87.4 -16.4 142 GLN -69.9 -43.9 179.1 152.4 180.0 60.7 143 ALA -62.2 -41.5 179.3 144 GLN -61.7 -46.1 -179.6 -171.9 164.3 43.8 145 ASN -63.6 -41.1 178.7 -71.8 -20.9 146 GLN -67.7 -48.5 -179.4 -66.6 -167.0 -12.6 147 LEU -68.1 -32.0 177.4 -66.8 -179.5 148 ASN -62.1 -41.0 -179.6 -78.1 174.1 149 SER -69.0 -42.8 176.6 -176.7 150 LEU -59.4 -38.1 -179.8 -85.7 61.3 151 ALA -70.0 -37.5 178.6 152 GLU -61.2 -31.2 -179.7 171.9 -170.0 -0.8 153 TYR -101.0 14.3 177.2 -72.8 -87.2 154 ASN 49.8 45.2 -178.3 -161.8 -151.0 155 VAL -78.3 -37.0 -177.5 175.9 156 PHE -127.2 155.7 -176.9 68.6 -84.2 157 ASP -114.3 -16.0 -175.7 -54.2 -24.9 158 VAL -70.2 139.7 178.7 61.5 159 PRO -69.4 131.9 178.4 -28.1 40.2 160 ILE -133.9 127.3 171.5 -60.2 -179.0 161 ARG -101.9 117.4 -179.7 167.4 155.5 -74.8 -178.2 162 LEU -96.6 126.9 -177.6 175.7 69.1 163 VAL -117.7 132.7 177.4 -176.2 164 GLY -112.0 124.8 177.5 165 LEU -83.4 126.1 -178.0 -63.0 169.9 166 ILE -142.4 175.1 174.9 51.8 173.6 167 GLU -143.9 159.4 172.9 -64.1 -80.1 2.0 168 ASP -74.3 148.5 176.1 -75.6 -20.6 169 PHE -81.5 156.9 173.3 -75.9 89.8 170 GLU 56.9 28.1 -177.8 -53.7 -65.3 -5.7 171 THR -130.0 134.5 178.7 -47.6 172 ASP -65.2 130.5 -179.2 -70.5 -2.0 173 ILE -136.2 163.5 176.2 54.7 166.4 174 ASP -77.3 132.4 -178.6 -64.1 -46.9 175 ILE -135.0 144.1 173.8 -67.3 177.5 176 VAL -111.6 122.1 -179.7 170.0 177 SER -113.2 123.7 -174.5 -175.4 178 THR -124.6 144.2 172.7 -51.5 179 THR -114.3 128.4 179.7 -67.5 180 TYR -99.0 172.5 -174.9 -65.9 -85.4 181 ALA -67.8 -25.4 177.9 182 ASP -131.2 153.4 -174.2 -60.3 -69.3 183 LYS -70.2 -15.2 176.7 -73.4 -177.1 175.5 163.1 184 ARG -137.9 141.1 172.1 -62.2 173.3 -161.4 -178.7 185 TYR 71.7 -27.8 -176.1 -44.0 -64.3 186 SER -57.5 140.1 174.3 179.9 187 ARG -111.6 8.9 -178.1 -55.3 -171.6 -169.8 171.6 188 THR -88.9 116.0 -179.5 -59.1 189 ILE -74.0 129.5 177.3 -60.4 168.3 190 THR -103.4 -39.2 179.9 -71.4 191 LYS -151.2 134.0 177.8 -176.2 82.6 -177.0 -38.7 192 ARG -135.3 130.3 -178.2 174.3 163.9 -86.0 -177.2 193 ASP -123.4 135.9 175.1 -49.4 -32.3 194 THR -102.3 119.1 -175.1 -67.4 195 VAL -141.3 179.0 173.7 -65.8 196 LYS -103.0 154.7 178.3 -63.4 -72.4 -166.9 171.9 197 GLY -167.8 -166.9 -179.4 198 LYS -161.2 163.0 176.4 61.6 -177.9 171.3 -172.2 199 VAL -108.3 114.3 -178.3 -179.0 200 ILE -83.4 134.6 -177.8 -60.2 179.2 201 ASP -106.7 128.1 175.7 -164.4 -7.9 202 THR -108.2 3.6 177.5 55.6 203 ASN -69.8 156.1 178.7 -73.8 -62.1 204 THR -97.7 -28.1 83.5 -91.5 205 ARG -128.5 137.9 179.0 -73.7 -80.7 109.3 178.8 206 LYS -105.0 154.5 177.1 -63.7 -173.0 63.1 -179.6 207 ARG -71.6 155.9 178.3 -62.9 -168.6 -169.0 -118.4 208 GLY -81.6 -177.3 175.8 209 THR -122.2 127.5 -179.7 -57.0 210 ILE -90.8 133.5 176.3 -56.9 164.8 211 VAL -129.3 150.3 176.7 -64.8 212 THR -125.2 158.7 -176.8 57.5 213 TYR -110.3 -29.8 0.0 -54.5 -38.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 35.841 24.097 4.305 2 ILE 38.783 23.241 6.500 3 ASP 41.567 24.839 8.522 4 ILE 44.620 22.843 9.610 5 THR 47.138 23.182 12.444 6 ASP 50.093 20.825 12.587 7 TYR 52.136 19.681 15.582 8 ASN 55.479 17.837 15.735 9 HIS 56.007 18.212 12.008 10 ALA 52.838 16.376 10.947 11 ASP 52.916 18.489 7.753 12 GLU 55.935 16.672 6.516 13 ILE 55.431 13.341 8.270 14 LEU 51.832 12.715 7.212 15 ASN 51.643 10.663 3.964 16 PRO 50.296 13.054 1.275 17 GLN 48.153 10.381 -0.338 18 LEU 46.502 9.400 2.942 19 TRP 45.864 13.039 3.733 20 LYS 44.305 13.454 0.241 21 GLU 41.818 10.673 1.042 22 ILE 40.740 12.403 4.278 23 GLU 40.738 15.891 2.807 24 GLU 38.664 15.043 -0.236 25 THR 36.028 13.550 2.045 26 LEU 35.842 16.591 4.295 27 LEU 35.781 19.058 1.441 28 LYS 32.868 17.390 -0.355 29 PRO 27.799 19.151 3.368 30 LEU 27.318 20.722 6.836 31 HIS 25.035 18.402 8.872 32 VAL 22.552 19.950 11.271 33 LYS 19.762 18.844 13.598 34 ALA 17.512 20.285 16.244 35 SER 18.778 21.120 19.726 36 ASP 16.829 19.745 22.661 37 GLN 18.541 22.124 25.151 38 ALA 15.975 23.804 27.434 39 SER 16.261 27.365 26.304 40 LYS 16.556 26.631 22.602 41 VAL 14.558 23.650 21.668 42 GLY 14.402 23.292 17.907 43 SER 17.243 25.694 17.113 44 LEU 19.614 24.252 14.520 45 ILE 22.973 22.942 15.743 46 PHE 25.933 21.027 14.311 47 ASP 24.847 17.322 14.066 48 PRO 27.700 15.013 15.188 49 VAL 25.724 11.867 14.389 50 GLY 25.162 12.710 10.734 51 THR 28.666 14.056 10.364 52 ASN 30.241 10.954 11.865 53 GLN 28.152 8.617 9.724 54 TYR 28.976 10.565 6.556 55 ILE 32.708 10.287 7.254 56 LYS 32.401 6.569 8.056 57 ASP 30.460 5.870 4.806 58 GLU 33.155 7.611 2.756 59 LEU 36.248 6.333 4.464 60 VAL 35.448 2.683 4.942 61 PRO 35.163 2.010 1.161 62 LYS 38.530 3.747 0.795 63 HIS 40.076 1.092 3.081 64 TRP 40.260 3.100 6.217 65 LYS 39.290 0.582 8.886 66 ASN 36.698 1.806 11.382 67 ASN 36.728 1.157 15.118 68 ILE 40.029 -0.684 15.078 69 PRO 40.342 -2.532 18.392 70 ILE 42.983 -1.344 20.810 71 PRO 45.273 -4.313 21.764 72 LYS 44.837 -5.844 25.197 73 ARG 48.220 -4.429 26.402 74 PHE 46.773 -0.944 26.066 75 ASP 43.155 -1.664 26.984 76 PHE 43.257 0.779 29.858 77 LEU 43.497 3.481 27.100 78 GLY 40.277 2.337 25.469 79 THR 38.483 -0.191 23.353 80 ASP 38.935 1.241 19.853 81 ILE 40.133 3.992 17.536 82 ASP 37.853 5.667 14.992 83 PHE 39.796 4.981 11.830 84 GLY 43.191 3.898 10.712 85 LYS 44.983 3.136 7.475 86 ARG 48.667 2.120 7.246 87 ASP 50.445 4.049 10.035 88 THR 47.867 6.781 10.389 89 LEU 45.136 7.100 13.021 90 VAL 42.106 9.396 12.653 91 GLU 39.784 10.510 15.508 92 VAL 36.613 12.447 14.654 93 GLN 35.872 14.218 17.917 94 PHE 32.645 16.112 18.580 95 SER 32.017 14.807 22.115 96 ASN 32.905 16.825 25.205 97 TYR 36.050 18.901 25.363 98 PRO 38.126 16.669 27.690 99 PHE 38.166 14.132 24.865 100 LEU 40.690 16.357 23.113 101 LEU 43.357 15.729 25.760 102 ASN 42.300 12.084 26.227 103 ASN 42.673 11.512 22.449 104 THR 45.981 13.405 22.374 105 VAL 47.537 11.544 25.282 106 ARG 46.472 8.134 24.179 107 SER 47.841 8.915 20.636 108 GLU 51.135 9.877 22.327 109 LEU 51.196 6.485 24.108 110 PHE 50.183 4.587 20.979 111 HIS 53.132 6.243 19.268 112 LYS 55.704 5.633 22.028 113 SER 54.720 1.975 22.253 114 ASN 54.462 1.458 18.499 115 ASP 49.882 -1.398 15.160 116 ILE 47.217 0.641 13.442 117 ASP 46.766 -1.148 10.119 118 GLU 49.682 -3.597 9.894 119 GLU 52.106 -0.726 10.576 120 GLY 53.199 0.966 13.778 121 LYS 53.251 7.298 13.193 122 VAL 50.764 10.166 12.958 123 ALA 47.336 11.144 14.213 124 ILE 44.667 13.292 12.521 125 ILE 42.064 14.802 14.894 126 ILE 38.957 16.237 13.208 127 THR 36.911 18.861 15.023 128 LYS 34.199 21.418 14.284 129 GLY 34.749 25.194 14.360 130 HIS 33.422 27.385 17.181 131 PHE 28.610 26.533 14.674 132 PRO 26.077 26.432 17.452 133 ALA 26.330 23.004 19.058 134 SER 25.659 21.061 22.223 135 ASN 27.182 22.603 25.319 136 SER 30.773 21.548 26.020 137 SER 31.194 19.744 22.711 138 LEU 34.794 20.220 21.568 139 TYR 35.545 22.934 19.030 140 TYR 38.594 23.606 16.878 141 GLU 39.851 26.803 18.375 142 GLN 39.765 25.350 21.890 143 ALA 41.656 22.294 20.600 144 GLN 44.176 24.599 18.864 145 ASN 44.698 26.657 22.007 146 GLN 45.202 23.564 24.141 147 LEU 47.592 21.796 21.784 148 ASN 49.463 25.096 21.141 149 SER 50.079 25.402 24.865 150 LEU 51.207 21.761 25.135 151 ALA 53.585 22.428 22.209 152 GLU 54.973 25.592 23.827 153 TYR 55.897 23.439 26.827 154 ASN 57.157 20.498 24.696 155 VAL 54.712 18.093 26.358 156 PHE 54.011 15.637 23.545 157 ASP 56.015 14.303 20.644 158 VAL 53.600 12.487 18.358 159 PRO 52.840 14.231 15.031 160 ILE 49.238 15.484 15.021 161 ARG 47.359 17.193 12.247 162 LEU 44.417 19.058 13.864 163 VAL 41.582 19.765 11.414 164 GLY 38.812 22.257 11.920 165 LEU 35.580 21.963 9.875 166 ILE 34.282 25.432 8.945 167 GLU 32.132 27.360 6.420 168 ASP 32.142 30.931 5.181 169 PHE 29.532 33.045 6.965 170 GLU 26.594 34.676 5.139 171 THR 26.998 32.527 2.095 172 ASP 24.546 29.950 0.769 173 ILE 25.899 26.458 1.342 174 ASP 24.799 22.831 1.087 175 ILE 23.286 21.465 4.277 176 VAL 21.860 18.121 5.353 177 SER 19.150 18.612 7.992 178 THR 18.044 15.508 9.860 179 THR 15.357 14.525 12.300 180 TYR 16.140 11.388 14.269 181 ALA 13.690 9.035 15.958 182 ASP 14.245 10.501 19.434 183 LYS 15.088 14.030 20.434 184 ARG 18.319 12.973 22.110 185 TYR 21.009 10.373 21.266 186 SER 19.201 8.531 18.518 187 ARG 21.136 7.651 15.381 188 THR 17.976 6.354 13.643 189 ILE 16.974 8.692 10.825 190 THR 13.241 9.635 10.618 191 LYS 13.606 12.420 8.042 192 ARG 16.580 13.763 6.145 193 ASP 16.553 16.771 3.818 194 THR 19.335 18.050 1.540 195 VAL 18.804 21.800 1.314 196 LYS 20.559 25.114 0.970 197 GLY 21.128 27.305 4.005 198 LYS 23.655 29.648 5.596 199 VAL 25.374 30.555 8.804 200 ILE 24.326 34.065 9.817 201 ASP 26.918 36.238 11.487 202 THR 26.013 38.923 14.018 203 ASN 29.685 39.775 14.684 204 THR 31.123 43.154 13.760 205 ARG 33.561 36.154 18.484 206 LYS 30.003 34.937 18.758 207 ARG 28.774 31.743 17.245 208 GLY 26.608 31.997 14.171 209 THR 22.965 31.002 13.679 210 ILE 22.241 28.290 11.108 211 VAL 19.223 28.703 8.835 212 THR 17.918 26.495 6.068 213 TYR 15.710 27.257 3.075 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S H H 10 H H H H H H H H H H 20 H H H H H H H H/X X/S S 30 S S S S S S T T T T 40 C S S S S S H H H H 50 H H H H H H H H H H 60 3 3 S S S S S/S S S S 70 S/T T T T/T T T T C C C 80 C S S S S/T T T T/S S S 90 S S S S C C C H H H 100 H H H H H H H H H H 110 H H H HPX X/T T T T C C/X 120 X/S S S S S S S S S S/X 130 X/S S S S C C C C H H 140 H H H H H H H H H H 150 H H H H S S S S/S S S 160 S S S S S S S S S S/S 170 S S S S/S S S S S S S 180 S T T T T C S S S S/S 190 S S S S S S/S S S S S 200 S S/S S S/X SXS S S S S S 210 S 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 T h H 10 H H H h h H H H H H 20 H H H H H H H h E 30 E E E E e g G G G 40 g T e E E E h H H H 50 H H H H H H H H H h 60 G G g t E E E E E e 70 g G G G G G G g e E 80 E E E E E T e E E E 90 E E e S B h H H H 100 H H H H H H H H H H 110 H H h t S S 120 E E E E E E E e 130 t T T B h H 140 H H H H H H H H H H 150 H H h T t S e E 160 E E E E E e t T T 170 t E E E E E E E E 180 e S S S S e E E 190 E E E E E E E E E E 200 E E 210 E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 68.9 39.7 77.0 2 ILE 134.8 93.9 37.8 3 ASP 50.2 45.4 66.5 4 ILE 105.3 73.4 65.5 5 THR 79.8 74.7 66.3 6 ASP 92.0 83.3 56.5 7 TYR 171.1 94.5 47.1 8 ASN 85.4 70.6 61.5 9 HIS 35.4 23.6 80.1 10 ALA 72.6 100.0 54.1 11 ASP 47.1 42.7 72.4 12 GLU 37.9 27.3 81.9 13 ILE 74.7 52.0 63.1 14 LEU 146.1 98.8 43.1 15 ASN 53.0 43.8 61.7 16 PRO 20.7 16.6 83.9 17 GLN 52.2 35.1 74.0 18 LEU 138.2 93.5 48.9 19 TRP 180.7 88.1 41.1 20 LYS 67.8 39.1 80.4 21 GLU 123.6 89.2 57.5 22 ILE 142.6 99.4 26.3 23 GLU 92.8 66.9 48.1 24 GLU 88.5 63.9 62.7 25 THR 106.2 99.3 41.9 26 LEU 141.0 95.4 30.5 27 LEU 69.0 46.7 68.9 28 LYS 63.9 36.8 84.4 29 PRO 92.8 74.6 57.1 30 LEU 136.4 92.3 35.6 31 HIS 144.2 96.0 51.5 32 VAL 118.8 100.0 35.6 33 LYS 135.3 78.0 61.5 34 ALA 30.4 41.8 67.4 35 SER 79.2 94.8 53.9 36 ASP 90.3 81.7 58.5 37 GLN 86.6 58.2 79.9 38 ALA 0.0 0.0 81.2 39 SER 17.6 21.1 77.2 40 LYS 79.6 45.9 81.0 41 VAL 53.8 45.3 79.8 42 GLY 11.9 34.1 68.4 43 SER 36.7 43.9 66.1 44 LEU 112.2 75.9 63.5 45 ILE 128.5 89.5 53.9 46 PHE 162.7 97.5 29.2 47 ASP 110.2 99.7 44.2 48 PRO 77.9 62.5 58.9 49 VAL 84.0 70.7 58.4 50 GLY 34.4 98.8 66.5 51 THR 95.6 89.4 43.4 52 ASN 65.4 54.1 60.6 53 GLN 70.2 47.3 76.8 54 TYR 129.2 71.4 58.5 55 ILE 139.3 97.1 26.1 56 LYS 87.2 50.3 72.5 57 ASP 38.6 34.9 75.4 58 GLU 96.3 69.5 63.4 59 LEU 147.1 99.5 33.4 60 VAL 60.2 50.7 62.7 61 PRO 47.4 38.1 77.5 62 LYS 124.3 71.7 65.9 63 HIS 21.2 14.1 85.3 64 TRP 205.0 100.0 37.8 65 LYS 49.6 28.6 80.4 66 ASN 99.0 81.8 51.0 67 ASN 60.2 49.8 83.1 68 ILE 124.3 86.6 53.0 69 PRO 27.9 22.4 78.2 70 ILE 142.5 99.3 48.9 71 PRO 67.3 54.1 71.4 72 LYS 0.0 0.0 90.1 73 ARG 86.3 41.3 69.6 74 PHE 142.3 85.3 47.9 75 ASP 41.1 37.2 71.1 76 PHE 44.4 26.6 76.1 77 LEU 122.8 83.1 39.1 78 GLY 15.0 43.1 71.8 79 THR 1.3 1.2 83.1 80 ASP 65.2 59.0 70.3 81 ILE 135.5 94.5 45.3 82 ASP 75.1 67.9 70.4 83 PHE 160.6 96.3 40.6 84 GLY 34.8 100.0 43.5 85 LYS 147.9 85.3 54.4 86 ARG 72.6 34.7 73.5 87 ASP 79.4 71.9 57.4 88 THR 106.9 100.0 43.5 89 LEU 141.4 95.7 40.0 90 VAL 118.8 100.0 30.7 91 GLU 133.1 96.0 52.5 92 VAL 118.2 99.5 36.9 93 GLN 130.9 88.1 52.1 94 PHE 165.3 99.1 42.8 95 SER 33.0 39.5 74.4 96 ASN 59.2 49.0 56.3 97 TYR 83.1 45.9 70.4 98 PRO 58.5 47.0 68.0 99 PHE 90.3 54.1 77.7 100 LEU 147.8 100.0 37.4 101 LEU 84.2 56.9 59.6 102 ASN 46.9 38.8 73.2 103 ASN 115.5 95.5 54.1 104 THR 106.3 99.5 30.7 105 VAL 40.4 34.0 64.3 106 ARG 184.6 88.4 56.7 107 SER 81.9 98.0 38.6 108 GLU 126.3 91.1 53.0 109 LEU 77.5 52.4 56.4 110 PHE 150.7 90.4 41.2 111 HIS 98.2 65.4 61.3 112 LYS 72.4 41.8 79.4 113 SER 51.9 62.1 66.1 114 ASN 34.1 28.2 83.0 115 ASP 33.7 30.5 79.9 116 ILE 128.3 89.4 48.5 117 ASP 87.5 79.2 53.9 118 GLU 8.5 6.1 87.6 119 GLU 67.9 49.0 73.0 120 GLY 29.4 84.4 65.3 121 LYS 76.6 44.2 76.1 122 VAL 117.0 98.5 44.6 123 ALA 71.4 98.4 40.1 124 ILE 143.5 100.0 26.6 125 ILE 143.5 100.0 37.9 126 ILE 143.4 99.9 24.9 127 THR 106.9 100.0 37.7 128 LYS 170.6 98.4 42.8 129 GLY 32.4 93.2 51.7 130 HIS 106.3 70.8 61.4 131 PHE 157.3 94.3 38.9 132 PRO 99.3 79.8 52.9 133 ALA 71.1 97.9 63.6 134 SER 25.1 30.0 72.9 135 ASN 26.5 21.9 90.1 136 SER 30.9 37.0 64.6 137 SER 78.7 94.1 71.0 138 LEU 147.7 100.0 46.1 139 TYR 128.6 71.1 67.4 140 TYR 174.2 96.2 54.5 141 GLU 73.0 52.7 60.7 142 GLN 113.3 76.3 53.2 143 ALA 72.6 100.0 36.6 144 GLN 106.5 71.7 65.2 145 ASN 25.1 20.8 77.1 146 GLN 95.3 64.2 53.1 147 LEU 147.8 100.0 30.4 148 ASN 59.3 49.0 63.7 149 SER 34.7 41.5 70.2 150 LEU 115.4 78.1 38.8 151 ALA 37.5 51.6 63.9 152 GLU 27.9 20.1 79.5 153 TYR 43.3 23.9 83.3 154 ASN 18.6 15.4 90.3 155 VAL 43.9 36.9 65.7 156 PHE 161.9 97.1 42.4 157 ASP 42.4 38.4 79.3 158 VAL 115.3 97.1 45.0 159 PRO 117.2 94.1 47.4 160 ILE 143.5 100.0 32.5 161 ARG 183.6 87.9 40.8 162 LEU 147.8 100.0 38.8 163 VAL 118.8 100.0 30.8 164 GLY 34.8 100.0 50.2 165 LEU 125.7 85.1 38.2 166 ILE 85.3 59.5 58.9 167 GLU 113.5 81.9 45.2 168 ASP 40.1 36.3 66.7 169 PHE 92.8 55.6 73.3 170 GLU 75.1 54.2 66.3 171 THR 41.5 38.9 76.7 172 ASP 47.2 42.7 66.5 173 ILE 121.4 84.6 57.5 174 ASP 46.1 41.8 65.6 175 ILE 143.5 100.0 41.0 176 VAL 106.5 89.6 53.3 177 SER 62.9 75.3 55.5 178 THR 106.6 99.7 56.3 179 THR 29.6 27.7 70.6 180 TYR 173.5 95.8 56.0 181 ALA 42.1 58.1 75.4 182 ASP 23.9 21.7 82.3 183 LYS 21.9 12.6 84.7 184 ARG 69.3 33.2 79.7 185 TYR 9.8 5.4 83.8 186 SER 68.3 81.6 67.9 187 ARG 32.6 15.6 79.8 188 THR 19.2 18.0 79.0 189 ILE 85.5 59.6 67.7 190 THR 40.1 37.5 66.9 191 LYS 49.3 28.4 81.6 192 ARG 146.4 70.1 55.0 193 ASP 58.9 53.3 65.9 194 THR 27.8 26.0 71.0 195 VAL 82.9 69.8 61.0 196 LYS 63.7 36.7 73.6 197 GLY 34.8 100.0 44.5 198 LYS 113.8 65.6 62.2 199 VAL 112.7 94.9 36.4 200 ILE 87.5 61.0 57.7 201 ASP 87.9 79.6 55.8 202 THR 32.0 30.0 78.8 203 ASN 107.3 88.8 67.2 204 THR 0.0 0.0 86.2 205 ARG 60.0 28.7 90.7 206 LYS 33.9 19.5 88.5 207 ARG 137.2 65.7 68.6 208 GLY 33.5 96.4 57.6 209 THR 30.4 28.4 66.5 210 ILE 143.5 100.0 32.7 211 VAL 76.0 63.9 49.5 212 THR 82.8 77.5 42.4 213 TYR 103.3 57.0 70.9