Protein Data Bank File : 1euva Title : HYDROLASE 17-APR-00 1EUV Number of Amino Acid Residues : 221 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY SER LEU VAL PRO GLU LEU ASN GLU LYS 10 ASP ASP ASP GLN VAL GLN LYS ALA LEU ALA 20 SER ARG GLU ASN THR GLN LEU MET ASN ARG 30 ASP ASN ILE GLU ILE THR VAL ARG ASP PHE 40 LYS THR LEU ALA PRO ARG ARG TRP LEU ASN 50 ASP THR ILE ILE GLU PHE PHE MET LYS TYR 60 ILE GLU LYS SER THR PRO ASN THR VAL ALA 70 PHE ASN SER PHE PHE TYR THR ASN LEU SER 80 GLU ARG GLY TYR GLN GLY VAL ARG ARG TRP 90 MET LYS ARG LYS LYS THR GLN ILE ASP LYS 100 LEU ASP LYS ILE PHE THR PRO ILE ASN LEU 110 ASN GLN SER HIS TRP ALA LEU GLY ILE ILE 120 ASP LEU LYS LYS LYS THR ILE GLY TYR VAL 130 ASP SER LEU SER ASN GLY PRO ASN ALA MET 140 SER PHE ALA ILE LEU THR ASP LEU GLN LYS 150 TYR VAL MET GLU GLU SER LYS HIS THR ILE 160 GLY GLU ASP PHE ASP LEU ILE HIS LEU ASP 170 CYS PRO GLN GLN PRO ASN GLY TYR ASP CYS 180 GLY ILE TYR VAL CYS MET ASN THR LEU TYR 190 GLY SER ALA ASP ALA PRO LEU ASP PHE ASP 200 TYR LYS ASP ALA ILE ARG MET ARG ARG PHE 210 ILE ALA HIS LEU ILE LEU THR ASP ALA LEU 220 LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 -98.3 175.5 2 SER -163.1 143.7 175.7 179.7 3 LEU -89.5 -1.5 177.4 -69.4 -178.0 4 VAL -104.5 112.9 -176.8 -179.5 5 PRO -81.2 161.3 174.7 32.7 -35.7 6 GLU -94.3 143.2 179.5 173.6 94.8 -25.7 7 LEU -82.0 147.7 175.0 -66.7 -167.5 8 ASN -75.0 170.6 -177.3 57.3 42.6 9 GLU -60.1 -39.7 -178.4 -178.3 99.0 -11.3 10 LYS -62.4 -47.8 -179.4 110.2 -126.0 -171.3 -123.9 11 ASP -64.9 -40.2 177.7 -68.1 -19.1 12 ASP -63.0 -40.2 -178.4 177.2 -11.9 13 ASP -65.2 -33.3 177.9 -81.1 -12.0 14 GLN -63.3 -46.8 174.9 -173.4 -174.0 18.9 15 VAL -57.1 -50.1 -179.0 170.7 16 GLN -58.9 -40.1 177.2 -164.7 82.0 -18.1 17 LYS -64.5 -44.6 178.6 -50.5 -175.5 159.6 -60.3 18 ALA -62.2 -37.6 178.6 19 LEU -67.0 -22.5 178.6 -69.7 168.8 20 ALA -97.1 4.8 -174.6 21 SER -70.6 138.1 177.5 140.8 22 ARG -78.4 89.2 169.8 -150.2 92.2 179.5 -179.9 23 GLU 112.6 151.7 -171.9 -76.6 174.5 51.3 24 ASN -79.5 75.1 -179.2 -161.9 -155.4 25 THR -93.3 160.3 176.6 73.0 26 GLN -78.4 123.9 -179.1 -163.6 -168.3 75.4 27 LEU -99.6 -24.4 -178.2 -72.3 174.6 28 MET -159.0 147.3 178.9 -160.9 -154.6 78.0 29 ASN -154.9 96.7 -176.1 -170.3 24.0 30 ARG -156.1 142.4 176.3 178.2 88.3 58.8 175.9 31 ASP 59.1 32.2 -179.9 -155.7 4.3 32 ASN 63.9 35.8 173.8 -108.3 106.4 33 ILE -137.2 114.6 177.5 -179.8 66.3 34 GLU -100.6 131.8 -177.5 173.9 -175.6 32.3 35 ILE -123.8 120.5 177.1 -56.2 173.1 36 THR -99.2 173.1 176.4 65.1 37 VAL -60.7 -38.5 178.6 171.4 38 ARG -57.0 -45.0 176.2 -176.8 177.0 178.9 -77.2 39 ASP -63.6 -45.6 -177.4 -60.1 -54.2 40 PHE -59.4 -36.1 -179.6 -171.1 82.1 41 LYS -66.4 -13.7 175.9 -73.2 180.0 171.8 -157.2 42 THR -71.5 -10.0 174.8 68.5 43 LEU -89.1 -4.3 178.1 -75.3 160.1 44 ALA -61.1 161.6 -179.1 45 PRO -54.4 139.6 174.6 -28.0 37.2 46 ARG 66.8 6.5 -179.3 -62.0 -179.2 170.1 -95.7 47 ARG -94.5 146.2 176.5 -59.1 -62.5 -177.9 173.0 48 TRP -69.5 127.3 176.0 -74.5 24.5 49 LEU -68.7 149.4 173.1 -55.2 -158.0 50 ASN -105.3 178.4 -175.4 72.8 -1.7 51 ASP -63.0 -28.8 -178.9 60.9 -89.1 52 THR -65.8 -42.4 177.2 -50.0 53 ILE -69.2 -42.6 175.6 -58.7 -53.8 54 ILE -58.8 -43.3 -177.9 -65.4 -66.1 55 GLU -66.8 -42.0 177.7 -178.2 163.9 8.3 56 PHE -55.8 -46.2 -177.9 168.5 74.9 57 PHE -66.8 -34.7 174.5 -161.0 75.6 58 MET -61.3 -44.1 179.2 -60.8 -58.5 103.1 59 LYS -62.5 -42.5 177.3 -73.9 -85.9 -160.3 171.7 60 TYR -58.1 -45.4 177.2 165.5 76.6 61 ILE -64.4 -38.8 176.4 -73.5 -58.0 62 GLU -64.4 -46.0 179.9 -80.2 -178.4 -31.6 63 LYS -57.9 -34.6 -176.5 -175.1 69.9 -172.8 -164.1 64 SER -104.4 5.0 -176.4 57.2 65 THR -131.5 128.9 -179.5 -47.6 66 PRO -72.8 149.3 176.0 19.7 -17.8 67 ASN 52.5 40.2 -176.2 -52.5 -46.2 68 THR -127.8 139.1 171.1 -71.0 69 VAL -116.3 138.4 174.6 161.9 70 ALA -131.1 107.4 -178.0 71 PHE -76.7 159.0 169.7 -76.6 116.8 72 ASN -71.2 174.3 -175.9 60.9 47.4 73 SER -75.7 -11.6 179.4 55.4 74 PHE -74.5 -17.8 176.1 -62.5 106.9 75 PHE -62.3 -52.3 179.9 171.0 87.1 76 TYR -64.8 -38.2 177.8 -172.2 74.7 77 THR -53.9 -52.1 179.2 -59.4 78 ASN -61.9 -46.7 -177.8 -77.1 -3.5 79 LEU -60.3 -40.3 -178.6 174.4 65.4 80 SER -75.9 -41.8 -177.4 62.7 81 GLU -83.3 -32.7 -170.4 -64.4 -178.4 1.9 82 ARG -128.3 20.1 173.8 -71.7 170.1 -85.9 -67.9 83 GLY 64.8 -172.5 177.7 84 TYR -59.4 -33.4 177.4 172.5 69.0 85 GLN -57.8 -33.2 178.2 -63.5 -60.7 -35.3 86 GLY -69.5 -13.5 -178.9 87 VAL -132.5 10.1 -178.6 -68.5 88 ARG -51.3 -38.4 -175.7 153.0 -163.9 141.7 -131.6 89 ARG -88.6 -4.8 -173.7 -57.0 165.6 56.6 92.5 90 TRP -71.5 -40.6 -179.2 -69.1 42.0 91 MET -63.6 -33.1 179.2 -172.3 66.5 76.5 92 LYS -58.7 -40.3 178.1 -162.1 168.7 163.7 -157.2 93 ARG -71.5 -5.1 174.8 -81.6 -7.6 159.8 162.6 94 LYS -89.4 -5.5 179.7 -74.4 -70.9 175.3 176.4 95 LYS 63.6 38.9 179.8 -56.4 -34.3 -157.1 171.9 96 THR -163.8 176.2 -176.9 -170.1 97 GLN -127.9 149.5 -177.9 -56.5 80.5 36.7 98 ILE -53.9 -34.7 179.8 -167.4 159.7 99 ASP -71.8 -4.3 175.5 73.3 7.9 100 LYS -100.9 0.9 -175.4 -72.8 -175.5 -162.4 62.7 101 LEU -99.2 154.7 174.3 -61.7 175.8 102 ASP -92.1 -46.5 -177.2 -74.8 -15.9 103 LYS -139.9 153.3 170.1 -64.1 -165.4 -176.9 56.7 104 ILE -127.5 124.8 178.9 -67.4 163.9 105 PHE -101.7 137.1 179.0 -72.7 95.1 106 THR -133.2 95.2 174.2 60.1 107 PRO -64.4 138.3 -174.6 28.5 -35.3 108 ILE -122.7 127.2 177.0 -65.1 165.5 109 ASN -95.9 128.5 -178.6 -176.7 -107.3 110 LEU -111.9 108.6 171.4 -65.5 157.9 111 ASN 54.9 32.1 -178.3 -55.6 -55.3 112 GLN 56.6 26.2 -179.6 -65.2 -79.8 -3.4 113 SER -138.6 -10.4 -178.0 67.4 114 HIS -153.5 154.0 177.2 -173.2 53.5 115 TRP -118.7 142.9 174.9 -73.3 113.2 116 ALA -143.2 -175.9 -175.4 117 LEU -144.3 139.9 172.1 178.0 65.9 118 GLY -104.7 142.0 176.7 119 ILE -125.9 112.1 173.5 -57.0 178.7 120 ILE -93.7 118.1 178.8 -66.9 161.1 121 ASP -106.2 98.5 -177.8 -162.3 -40.5 122 LEU -67.3 -34.0 -179.8 -61.3 137.0 123 LYS -70.9 -40.7 179.3 173.4 -151.2 -47.8 164.6 124 LYS -87.9 -5.3 -178.7 -56.8 173.1 -169.7 62.2 125 LYS 57.0 52.3 -179.3 -69.6 -160.9 177.3 -88.0 126 THR -139.5 148.8 174.7 59.6 127 ILE -120.7 124.8 -176.2 -56.4 -165.7 128 GLY -124.1 147.2 178.4 129 TYR -117.5 123.4 -173.9 173.3 73.4 130 VAL -126.9 123.0 -172.4 67.5 131 ASP -136.0 131.2 -179.0 -177.4 -29.7 132 SER -87.9 5.2 170.9 57.3 133 LEU -142.7 70.6 -177.7 -161.9 64.0 134 SER -128.3 144.0 173.6 169.6 135 ASN -94.8 -3.4 174.5 -61.6 -49.3 136 GLY 128.6 179.6 -178.1 137 PRO -41.4 126.8 -178.8 -22.9 21.0 138 ASN -143.9 179.7 -177.0 89.2 11.7 139 ALA -76.8 -29.7 -178.7 140 MET -68.7 -33.1 -179.1 -36.5 -47.4 -29.9 141 SER -67.2 -33.0 176.3 83.5 142 PHE -71.1 -40.8 175.2 -85.1 118.1 143 ALA -57.6 -41.7 177.5 144 ILE -62.5 -52.3 -178.4 -68.3 168.0 145 LEU -58.6 -42.9 179.1 -64.1 163.0 146 THR -67.9 -28.4 176.6 61.2 147 ASP -65.3 -42.4 -177.6 -88.4 -6.2 148 LEU -70.6 -36.5 179.0 -63.4 170.0 149 GLN -65.9 -38.7 175.5 178.2 175.8 42.9 150 LYS -60.1 -43.2 179.4 178.3 170.9 64.3 175.2 151 TYR -57.6 -49.2 -177.2 178.6 74.8 152 VAL -60.4 -45.7 179.5 177.5 153 MET -62.7 -44.0 -179.7 -70.8 175.5 -32.7 154 GLU -72.1 -45.1 -179.3 -58.0 -66.2 -37.0 155 GLU -63.9 -32.4 178.9 -176.8 62.9 25.7 156 SER -86.5 3.4 -176.8 67.1 157 LYS 59.3 47.6 178.7 -73.9 163.7 -175.8 138.8 158 HIS 53.7 40.8 176.4 -64.1 93.9 159 THR -101.9 -30.8 -176.1 50.1 160 ILE -141.1 159.2 177.1 53.7 171.7 161 GLY 111.0 -33.7 -175.9 162 GLU -63.5 -22.9 179.9 83.7 176.9 -35.9 163 ASP -107.0 12.0 177.6 60.7 -5.2 164 PHE -69.7 149.0 176.9 -79.2 28.2 165 ASP -86.9 126.2 179.3 -159.6 15.3 166 LEU -93.8 123.3 -173.7 -51.9 -176.5 167 ILE -133.9 139.0 174.0 178.5 70.3 168 HIS -90.4 101.7 -175.4 -172.7 117.0 169 LEU -76.4 137.1 177.2 -56.6 164.4 170 ASP -74.5 146.4 173.0 -68.3 -45.9 171 CYS -156.7 164.1 176.6 75.7 172 PRO -56.0 134.2 -173.7 -20.3 33.6 173 GLN -97.5 142.6 -179.2 -66.1 -66.2 -72.7 174 GLN -70.5 144.7 179.7 68.9 -168.5 67.1 175 PRO -94.8 10.5 -175.0 40.3 -42.2 176 ASN -146.0 176.6 -178.9 58.2 59.3 177 GLY -98.7 10.6 -173.0 178 TYR -123.0 -10.4 -175.6 43.2 83.0 179 ASP -86.4 3.7 -174.4 -88.6 -22.5 180 CYS -51.5 -45.7 -176.0 55.4 181 GLY -64.8 -35.5 177.3 182 ILE -66.2 -41.9 178.8 -71.1 -68.8 183 TYR -64.9 -34.9 176.9 -83.8 67.2 184 VAL -59.9 -49.4 179.8 165.9 185 CYS -61.2 -42.2 178.1 -67.5 186 MET -64.7 -42.7 177.6 -62.3 -168.8 -73.4 187 ASN -62.3 -32.1 177.9 -85.9 -45.8 188 THR -74.2 -45.5 179.6 -54.9 189 LEU -59.0 -51.4 -177.8 168.3 67.5 190 TYR -69.6 -43.0 179.0 -78.4 63.6 191 GLY -63.0 -40.4 179.8 192 SER -63.0 -31.0 179.9 72.0 193 ALA -91.9 3.5 -174.6 194 ASP 49.4 48.2 -179.5 -74.5 -56.4 195 ALA -105.4 145.9 179.2 196 PRO -57.6 140.6 -176.7 -27.3 40.4 197 LEU -83.8 81.3 -175.5 -54.0 -177.7 198 ASP -118.9 15.8 175.8 55.0 10.4 199 PHE -68.3 167.5 179.4 50.6 79.2 200 ASP -141.9 -170.0 -174.2 61.6 30.5 201 TYR -69.9 -22.1 175.3 79.9 105.4 202 LYS -72.2 -37.1 174.1 -61.2 -179.2 -174.8 -168.7 203 ASP -60.8 -38.1 -180.0 -66.5 -56.4 204 ALA -61.8 -39.0 174.8 205 ILE -60.9 -44.6 177.7 -64.9 162.1 206 ARG -68.2 -33.3 -177.8 -60.7 -160.9 -163.9 89.7 207 MET -59.7 -42.7 179.1 -172.5 78.7 165.3 208 ARG -55.4 -45.0 178.9 -70.0 176.9 177.8 -89.8 209 ARG -68.9 -34.2 -178.8 -51.5 -51.4 -82.5 -162.8 210 PHE -67.0 -49.5 179.0 174.5 52.1 211 ILE -60.5 -43.2 178.2 -59.5 171.1 212 ALA -57.6 -44.3 177.4 213 HIS -59.9 -41.8 179.5 170.7 74.9 214 LEU -59.6 -40.8 179.1 -63.1 175.9 215 ILE -64.7 -49.3 -176.4 -68.8 168.4 216 LEU -67.4 -26.3 180.0 -62.3 -178.3 217 THR -96.1 13.0 174.1 60.1 218 ASP 50.8 56.0 -175.1 -162.2 13.8 219 ALA -64.7 -15.0 -179.9 220 LEU -89.5 5.5 176.2 -51.1 172.7 221 LYS 30.6 -148.9 0.0 58.4 161.3 -101.8 166.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 34.959 17.863 92.389 2 SER 33.593 19.410 89.176 3 LEU 32.156 18.045 85.960 4 VAL 33.683 20.963 84.021 5 PRO 37.313 20.171 83.266 6 GLU 40.213 22.546 82.896 7 LEU 41.903 22.531 79.517 8 ASN 45.598 21.797 79.140 9 GLU 47.684 24.665 77.761 10 LYS 47.782 23.220 74.238 11 ASP 43.998 22.806 74.077 12 ASP 43.434 26.311 75.507 13 ASP 45.726 27.835 72.859 14 GLN 43.725 26.129 70.124 15 VAL 40.577 27.777 71.508 16 GLN 42.305 31.223 71.647 17 LYS 43.497 30.890 68.012 18 ALA 40.061 29.907 66.748 19 LEU 38.502 32.928 68.551 20 ALA 40.925 35.169 66.695 21 SER 40.428 33.802 63.210 22 ARG 40.244 36.346 60.509 23 GLU 36.966 35.458 58.893 24 ASN 33.724 33.638 59.273 25 THR 34.702 30.138 58.285 26 GLN 32.982 26.855 59.105 27 LEU 34.639 25.301 62.188 28 MET 32.508 22.182 62.580 29 ASN 29.748 20.434 60.663 30 ARG 28.476 17.228 62.191 31 ASP 25.164 15.664 63.275 32 ASN 23.245 18.491 61.558 33 ILE 24.836 21.341 63.502 34 GLU 27.087 23.636 61.549 35 ILE 29.257 26.019 63.625 36 THR 30.940 29.080 62.136 37 VAL 33.495 31.412 63.651 38 ARG 30.692 33.944 64.248 39 ASP 28.883 31.366 66.411 40 PHE 32.100 30.246 68.128 41 LYS 32.969 33.788 69.187 42 THR 29.833 33.861 71.383 43 LEU 31.910 31.625 73.715 44 ALA 34.556 34.360 74.105 45 PRO 34.786 35.874 77.559 46 ARG 31.738 37.892 78.659 47 ARG 29.759 37.166 75.475 48 TRP 26.139 36.105 75.144 49 LEU 25.751 32.578 73.733 50 ASN 23.617 32.195 70.626 51 ASP 21.294 29.362 69.628 52 THR 24.010 27.552 67.636 53 ILE 26.202 27.037 70.678 54 ILE 23.193 26.021 72.822 55 GLU 22.177 23.478 70.134 56 PHE 25.708 22.117 69.855 57 PHE 25.779 21.509 73.619 58 MET 22.376 19.810 73.550 59 LYS 23.750 17.460 70.828 60 TYR 26.836 16.734 72.895 61 ILE 24.677 15.743 75.910 62 GLU 22.502 13.576 73.646 63 LYS 25.637 11.933 72.195 64 SER 26.973 11.055 75.698 65 THR 23.874 10.237 77.705 66 PRO 21.580 7.290 77.300 67 ASN 17.882 7.496 76.691 68 THR 18.032 11.308 76.475 69 VAL 16.715 13.872 74.015 70 ALA 17.914 17.453 74.210 71 PHE 16.057 19.708 71.814 72 ASN 17.469 22.913 70.358 73 SER 15.871 26.120 71.671 74 PHE 13.496 26.490 68.688 75 PHE 11.468 23.564 70.146 76 TYR 10.241 25.668 73.065 77 THR 9.673 28.679 70.757 78 ASN 7.359 26.589 68.548 79 LEU 5.615 24.824 71.459 80 SER 4.873 28.104 73.219 81 GLU 3.881 30.114 70.154 82 ARG 2.188 27.393 68.067 83 GLY 1.152 24.726 70.561 84 TYR 1.840 20.996 70.398 85 GLN 0.959 21.163 66.714 86 GLY 4.035 23.339 66.255 87 VAL 6.376 20.548 67.489 88 ARG 4.289 17.434 66.723 89 ARG 6.774 16.105 64.133 90 TRP 9.951 16.828 66.092 91 MET 10.357 13.667 68.207 92 LYS 10.063 11.518 65.058 93 ARG 13.157 13.256 63.687 94 LYS 15.024 12.243 66.879 95 LYS 14.621 8.600 65.772 96 THR 12.975 7.621 69.039 97 GLN 9.724 7.776 70.997 98 ILE 8.834 9.464 74.294 99 ASP 8.173 6.129 76.050 100 LYS 11.827 5.064 75.640 101 LEU 13.338 8.128 77.273 102 ASP 14.654 8.980 80.712 103 LYS 14.861 12.766 80.175 104 ILE 14.024 15.466 77.619 105 PHE 15.939 18.778 77.885 106 THR 14.430 21.983 76.447 107 PRO 16.660 25.108 76.490 108 ILE 14.492 28.241 76.501 109 ASN 15.243 31.625 74.991 110 LEU 13.405 34.404 76.826 111 ASN 12.839 37.585 74.828 112 GLN 16.230 37.545 73.105 113 SER 17.808 38.469 76.418 114 HIS 18.077 35.398 78.679 115 TRP 18.452 31.617 78.550 116 ALA 16.818 29.128 80.964 117 LEU 16.102 25.382 80.859 118 GLY 13.259 22.949 81.118 119 ILE 13.961 19.393 82.287 120 ILE 11.299 16.725 81.676 121 ASP 12.301 13.744 83.832 122 LEU 10.199 10.834 82.599 123 LYS 11.695 8.410 85.115 124 LYS 11.062 10.677 88.120 125 LYS 7.767 11.927 86.682 126 THR 8.746 15.561 87.174 127 ILE 8.913 18.681 85.013 128 GLY 11.439 21.235 86.200 129 TYR 12.249 24.815 85.244 130 VAL 15.818 25.864 86.151 131 ASP 16.922 29.466 85.757 132 SER 20.242 30.997 86.832 133 LEU 18.818 34.515 87.294 134 SER 15.539 33.920 89.094 135 ASN 13.945 35.281 92.263 136 GLY 11.720 32.219 92.314 137 PRO 8.483 30.615 91.290 138 ASN 6.665 33.207 89.241 139 ALA 3.881 33.169 86.653 140 MET 5.943 33.051 83.437 141 SER 7.710 29.986 84.853 142 PHE 4.279 28.441 85.248 143 ALA 3.312 28.898 81.608 144 ILE 6.597 27.158 80.714 145 LEU 5.971 24.239 83.093 146 THR 2.410 23.752 81.835 147 ASP 3.586 23.924 78.212 148 LEU 6.120 21.147 78.866 149 GLN 3.462 19.079 80.712 150 LYS 1.165 19.575 77.740 151 TYR 3.909 18.345 75.403 152 VAL 4.385 15.135 77.406 153 MET 0.652 14.423 77.505 154 GLU 0.181 15.005 73.757 155 GLU 3.378 13.327 72.502 156 SER 2.605 10.236 74.590 157 LYS -0.977 10.070 73.286 158 HIS -2.246 10.757 76.800 159 THR -0.446 7.850 78.422 160 ILE 1.937 9.804 80.635 161 GLY 2.398 13.268 82.091 162 GLU -0.894 14.265 83.803 163 ASP 0.382 13.368 87.291 164 PHE 3.869 14.845 86.925 165 ASP 5.046 17.272 89.628 166 LEU 5.817 20.740 88.179 167 ILE 8.763 22.332 90.009 168 HIS 10.759 25.581 89.879 169 LEU 14.184 23.990 90.507 170 ASP 16.844 25.760 92.553 171 CYS 20.318 26.223 91.010 172 PRO 23.518 28.285 91.440 173 GLN 22.731 31.830 90.337 174 GLN 24.967 33.723 87.887 175 PRO 26.856 36.702 89.356 176 ASN 26.821 38.599 86.049 177 GLY 24.568 39.415 83.156 178 TYR 26.145 37.336 80.362 179 ASP 26.597 33.756 81.601 180 CYS 22.970 32.593 81.394 181 GLY 23.611 30.365 78.313 182 ILE 26.664 28.816 80.097 183 TYR 24.513 28.141 83.214 184 VAL 21.917 26.471 80.896 185 CYS 24.745 24.225 79.586 186 MET 26.014 23.444 83.132 187 ASN 22.424 22.671 84.251 188 THR 22.011 20.287 81.285 189 LEU 25.396 18.656 81.965 190 TYR 24.757 18.186 85.696 191 GLY 21.056 17.274 85.231 192 SER 21.994 14.639 82.554 193 ALA 24.477 13.086 84.997 194 ASP 21.996 13.318 87.887 195 ALA 24.601 15.336 89.833 196 PRO 23.931 17.860 92.645 197 LEU 23.906 21.420 91.243 198 ASP 26.990 22.694 93.045 199 PHE 28.898 24.313 90.190 200 ASP 29.844 27.974 90.466 201 TYR 30.998 30.987 88.477 202 LYS 34.536 29.637 88.115 203 ASP 33.041 26.540 86.512 204 ALA 31.201 28.929 84.157 205 ILE 34.524 30.487 83.090 206 ARG 35.949 27.000 82.408 207 MET 32.727 25.913 80.700 208 ARG 33.181 28.429 77.908 209 ARG 36.611 27.001 77.142 210 PHE 35.353 23.406 77.523 211 ILE 32.527 23.864 75.035 212 ALA 34.911 25.624 72.624 213 HIS 37.329 22.651 72.937 214 LEU 34.491 20.168 72.213 215 ILE 33.720 22.059 68.995 216 LEU 37.342 22.218 67.795 217 THR 37.874 18.535 68.575 218 ASP 34.752 17.468 66.657 219 ALA 33.275 15.864 69.770 220 LEU 30.151 14.556 68.024 221 LYS 32.184 12.071 65.922 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S S/H H H 10 H H H H H H H H H H 20 H C S S S S C C T T 30 T T/S S S S S/H H H H H 40 H H C C C S S S S S/H 50 H H H H H H H H H H 60 H H H H H C S S S S 70 S S S/H H H H H H H H 80 H H H H H H H H H H 90 H H H H 3 C T T T T/S 100 S S S/S S S S S S S/T T 110 T T S S S S S S S S 120 S/T T T T S S S S S S 130 S S S C C C C H H H 140 H H H H H H H H H H 150 H H H H H H H C C C 160 C S S S S/S S S S/S S S 170 S S/S S S S/S S S S H H 180 H H H H H H H H H H 190 H H H H/S S S S/S S S S/H 200 H H H H H H H H H H 210 H H H H H H H H S S/S 220 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S h H H 10 H H H H H H H H H h 20 t S S e E E E E E 30 T T E E E E H H H H 40 h G G g T T t h 50 H H H H H H H H H H 60 H H H H h T e E E E 70 e t h H H H H H H H 80 H H h G G G g T T T 90 g G G G g t g G G G 100 g e E E E E E E E E 110 T T T E E E E E E E 120 E e T T e E E E E E 130 e S S S h H H 140 H H H H H H H H H H 150 H H H H H h T t S S 160 t T T t E E E E E 170 S S S t h H 180 H H H H H H H H H H 190 H H h T t h 200 H H H H H H H H H H 210 H H H H H H h T T T 220 t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 93.4 2 SER 58.5 70.0 81.8 3 LEU 81.0 54.8 53.8 4 VAL 118.8 100.0 39.7 5 PRO 64.0 51.4 64.7 6 GLU 31.9 23.0 81.3 7 LEU 135.9 91.9 50.9 8 ASN 53.0 43.9 76.0 9 GLU 9.2 6.6 88.6 10 LYS 37.9 21.8 86.7 11 ASP 93.8 84.9 63.3 12 ASP 57.1 51.7 70.0 13 ASP 43.4 39.3 69.8 14 GLN 76.7 51.6 64.3 15 VAL 117.9 99.3 44.7 16 GLN 42.7 28.8 81.9 17 LYS 28.6 16.5 80.1 18 ALA 60.4 83.1 48.1 19 LEU 133.7 90.4 53.7 20 ALA 12.4 17.0 85.1 21 SER 43.7 52.2 77.1 22 ARG 13.1 6.3 93.5 23 GLU 13.9 10.0 82.4 24 ASN 67.7 56.0 59.1 25 THR 41.5 38.9 74.3 26 GLN 76.6 51.6 72.7 27 LEU 119.3 80.7 48.9 28 MET 149.2 93.6 48.2 29 ASN 55.3 45.8 72.9 30 ARG 106.1 50.8 75.9 31 ASP 54.7 49.5 60.4 32 ASN 0.0 0.0 90.0 33 ILE 133.1 92.7 47.0 34 GLU 57.3 41.4 73.4 35 ILE 143.5 100.0 30.6 36 THR 73.6 68.8 67.1 37 VAL 115.7 97.4 56.0 38 ARG 43.2 20.7 87.4 39 ASP 96.4 87.3 62.5 40 PHE 166.8 100.0 31.3 41 LYS 85.4 49.3 72.1 42 THR 82.6 77.2 63.4 43 LEU 147.0 99.5 37.9 44 ALA 54.2 74.6 51.4 45 PRO 45.4 36.5 69.9 46 ARG 48.3 23.1 77.0 47 ARG 56.9 27.3 82.2 48 TRP 78.3 38.2 80.8 49 LEU 147.8 100.0 46.8 50 ASN 90.5 74.9 67.4 51 ASP 61.8 55.9 58.4 52 THR 88.7 82.9 62.0 53 ILE 143.5 100.0 38.8 54 ILE 143.5 100.0 32.8 55 GLU 108.7 78.4 52.1 56 PHE 166.8 100.0 28.6 57 PHE 166.8 100.0 26.6 58 MET 158.8 99.6 38.7 59 LYS 142.1 81.9 66.0 60 TYR 142.4 78.7 38.0 61 ILE 141.4 98.6 40.6 62 GLU 116.0 83.7 58.9 63 LYS 97.2 56.0 68.9 64 SER 37.8 45.2 73.3 65 THR 88.1 82.4 64.6 66 PRO 28.4 22.8 82.7 67 ASN 49.6 41.0 75.2 68 THR 105.4 98.6 45.4 69 VAL 114.0 96.0 29.6 70 ALA 72.6 100.0 41.1 71 PHE 165.2 99.0 35.0 72 ASN 91.8 76.0 53.4 73 SER 80.6 96.4 44.8 74 PHE 68.5 41.1 78.2 75 PHE 166.8 100.0 25.2 76 TYR 164.3 90.8 44.8 77 THR 63.7 59.6 73.8 78 ASN 88.9 73.5 65.9 79 LEU 147.8 100.0 37.4 80 SER 61.2 73.1 63.5 81 GLU 51.7 37.3 80.7 82 ARG 87.6 42.0 77.4 83 GLY 18.2 52.4 79.5 84 TYR 151.2 83.5 52.0 85 GLN 35.4 23.8 75.3 86 GLY 23.1 66.5 64.4 87 VAL 118.5 99.7 39.2 88 ARG 95.9 45.9 76.3 89 ARG 69.4 33.2 85.0 90 TRP 143.8 70.1 61.5 91 MET 157.8 99.0 41.9 92 LYS 21.8 12.6 88.8 93 ARG 64.3 30.8 86.6 94 LYS 134.5 77.6 57.8 95 LYS 20.5 11.8 90.6 96 THR 80.8 75.6 53.8 97 GLN 53.0 35.7 75.9 98 ILE 137.2 95.6 30.4 99 ASP 30.6 27.7 72.5 100 LYS 58.6 33.8 86.2 101 LEU 142.4 96.3 46.1 102 ASP 73.1 66.2 66.4 103 LYS 162.7 93.8 59.7 104 ILE 143.5 100.0 25.6 105 PHE 166.8 100.0 32.6 106 THR 106.8 99.9 28.8 107 PRO 124.5 100.0 36.5 108 ILE 143.1 99.7 36.1 109 ASN 91.6 75.8 60.2 110 LEU 107.2 72.6 60.1 111 ASN 4.7 3.9 83.3 112 GLN 8.1 5.5 91.2 113 SER 35.5 42.5 68.8 114 HIS 120.3 80.1 61.6 115 TRP 188.9 92.1 45.9 116 ALA 72.3 99.6 47.2 117 LEU 147.8 100.0 40.0 118 GLY 34.8 100.0 52.6 119 ILE 126.7 88.3 41.9 120 ILE 143.5 100.0 30.8 121 ASP 103.9 94.0 54.7 122 LEU 141.0 95.4 42.6 123 LYS 70.8 40.8 85.3 124 LYS 85.1 49.1 76.8 125 LYS 86.7 50.0 69.7 126 THR 67.5 63.2 56.8 127 ILE 143.5 100.0 36.0 128 GLY 33.8 97.1 48.1 129 TYR 173.3 95.7 38.0 130 VAL 118.7 99.9 41.3 131 ASP 99.8 90.3 56.5 132 SER 82.9 99.1 54.4 133 LEU 62.3 42.2 81.8 134 SER 69.3 82.9 75.2 135 ASN 0.0 0.0 91.8 136 GLY 21.3 61.3 62.6 137 PRO 49.4 39.7 64.9 138 ASN 41.7 34.5 73.9 139 ALA 9.7 13.4 71.7 140 MET 27.6 17.3 82.2 141 SER 79.7 95.4 47.4 142 PHE 65.3 39.1 67.8 143 ALA 19.4 26.8 82.5 144 ILE 135.5 94.4 36.2 145 LEU 145.7 98.6 44.2 146 THR 43.3 40.5 68.9 147 ASP 87.3 79.0 58.2 148 LEU 147.8 100.0 33.6 149 GLN 121.0 81.4 50.4 150 LYS 95.6 55.1 65.7 151 TYR 181.0 100.0 27.7 152 VAL 118.8 100.0 31.9 153 MET 112.2 70.4 60.9 154 GLU 88.2 63.6 56.3 155 GLU 118.3 85.4 55.1 156 SER 77.7 93.0 58.3 157 LYS 9.7 5.6 92.1 158 HIS 52.7 35.1 79.4 159 THR 27.3 25.5 77.7 160 ILE 100.2 69.9 60.2 161 GLY 34.8 100.0 42.0 162 GLU 13.0 9.4 77.2 163 ASP 28.0 25.3 73.7 164 PHE 166.7 99.9 51.4 165 ASP 17.6 16.0 76.8 166 LEU 120.3 81.4 52.9 167 ILE 70.1 48.8 65.7 168 HIS 136.2 90.6 51.0 169 LEU 97.2 65.7 52.6 170 ASP 0.0 0.0 90.1 171 CYS 95.5 96.3 57.0 172 PRO 95.2 76.5 52.0 173 GLN 86.4 58.1 73.8 174 GLN 147.4 99.2 47.2 175 PRO 66.5 53.4 69.9 176 ASN 90.1 74.6 59.5 177 GLY 5.3 15.4 73.2 178 TYR 140.3 77.5 71.7 179 ASP 106.2 96.2 53.5 180 CYS 91.6 92.4 62.9 181 GLY 34.8 100.0 40.3 182 ILE 143.5 100.0 35.9 183 TYR 179.5 99.2 43.6 184 VAL 115.6 97.3 45.1 185 CYS 99.2 100.0 33.8 186 MET 159.4 100.0 30.0 187 ASN 119.1 98.5 33.5 188 THR 106.9 100.0 29.8 189 LEU 127.2 86.1 41.3 190 TYR 176.2 97.4 43.7 191 GLY 23.8 68.5 58.0 192 SER 79.2 94.7 50.0 193 ALA 35.2 48.4 70.4 194 ASP 57.8 52.3 81.6 195 ALA 56.8 78.2 48.5 196 PRO 20.4 16.4 80.7 197 LEU 115.2 78.0 56.3 198 ASP 26.4 23.9 74.3 199 PHE 165.2 99.0 40.2 200 ASP 45.8 41.5 67.4 201 TYR 80.9 44.7 59.2 202 LYS 66.6 38.4 76.2 203 ASP 101.6 91.9 56.9 204 ALA 72.6 100.0 48.7 205 ILE 40.4 28.2 69.7 206 ARG 130.1 62.3 65.1 207 MET 159.4 100.0 27.8 208 ARG 198.9 95.2 53.2 209 ARG 168.3 80.6 51.9 210 PHE 148.6 89.1 38.6 211 ILE 143.5 100.0 23.7 212 ALA 71.9 99.1 35.6 213 HIS 115.9 77.2 52.6 214 LEU 132.1 89.4 36.5 215 ILE 143.5 100.0 25.0 216 LEU 136.3 92.2 48.2 217 THR 61.6 57.6 73.4 218 ASP 65.0 58.8 73.9 219 ALA 55.5 76.4 56.1 220 LEU 147.8 100.0 37.5 221 LYS 31.2 18.0 84.2