Protein Data Bank File : 1lbu Title : HYDROLASE 16-MAR-96 1LBU Number of Amino Acid Residues : 213 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP GLY CYS TYR THR TRP SER GLY THR LEU 10 SER GLU GLY SER SER GLY GLU ALA VAL ARG 20 GLN LEU GLN ILE ARG VAL ALA GLY TYR PRO 30 GLY THR GLY ALA GLN LEU ALA ILE ASP GLY 40 GLN PHE GLY PRO ALA THR LYS ALA ALA VAL 50 GLN ARG PHE GLN SER ALA TYR GLY LEU ALA 60 ALA ASP GLY ILE ALA GLY PRO ALA THR PHE 70 ASN LYS ILE TYR GLN LEU GLN ASP ASP ASP 80 CYS THR PRO VAL ASN PHE THR TYR ALA GLU 90 LEU ASN ARG CYS ASN SER ASP TRP SER GLY 100 GLY LYS VAL SER ALA ALA THR ALA ARG ALA 110 ASN ALA LEU VAL THR MET TRP LYS LEU GLN 120 ALA MET ARG HIS ALA MET GLY ASP LYS PRO 130 ILE THR VAL ASN GLY GLY PHE ARG SER VAL 140 THR CYS ASN SER ASN VAL GLY GLY ALA SER 150 ASN SER ARG HIS MET TYR GLY HIS ALA ALA 160 ASP LEU GLY ALA GLY SER GLN GLY PHE CYS 170 ALA LEU ALA GLN ALA ALA ARG ASN HIS GLY 180 PHE THR GLU ILE LEU GLY PRO GLY TYR PRO 190 GLY HIS ASN ASP HIS THR HIS VAL ALA GLY 200 GLY ASP GLY ARG PHE TRP SER ALA PRO SER 210 CYS GLY ILE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 103.3 -178.4 0.0 0.0 2 GLY -127.7 -59.6 -178.7 3 CYS -53.7 -69.2 -178.0 169.4 4 TYR -155.2 144.6 178.9 -168.0 84.4 5 THR -125.6 127.5 179.8 -37.7 6 TRP -83.2 136.7 -178.6 -81.0 -88.8 7 SER -86.0 -27.2 179.0 14.5 8 GLY -166.9 171.6 -179.3 9 THR -52.8 146.1 179.7 -57.2 10 LEU -127.2 136.7 178.0 -59.2 171.2 11 SER -150.8 174.7 180.0 66.5 12 GLU -48.0 130.7 179.8 -73.1 169.9 -51.6 13 GLY 108.4 -19.4 178.2 14 SER -72.7 154.2 178.7 -69.8 15 SER -156.4 149.7 -178.4 63.9 16 GLY 136.0 179.5 -178.7 17 GLU -62.2 -33.8 178.8 -139.1 -27.7 69.0 18 ALA -61.4 -37.1 179.8 19 VAL -74.7 -42.8 179.2 174.4 20 ARG -56.1 -46.9 180.0 -139.4 -166.7 53.3 109.0 21 GLN -62.1 -41.7 -179.7 -124.1 40.8 -75.1 22 LEU -67.8 -38.8 -179.8 170.5 74.3 23 GLN -59.8 -39.3 179.0 -68.1 164.6 -39.6 24 ILE -57.3 -46.3 -176.5 -66.0 -174.2 25 ARG -61.8 -35.5 -178.0 -48.3 -39.8 -162.9 -104.4 26 VAL -104.6 13.0 -178.9 -60.4 27 ALA -60.4 -20.2 179.4 28 GLY -77.5 0.9 -179.1 29 TYR -125.0 52.0 -179.5 -63.7 -79.9 30 PRO -87.1 -8.2 -177.4 48.4 -50.9 31 GLY 100.5 156.8 -180.0 32 THR -57.7 132.7 178.2 -53.3 33 GLY 61.5 26.9 179.1 34 ALA -128.0 167.2 -180.0 35 GLN -137.8 126.1 178.7 -140.3 -169.2 -179.6 36 LEU -77.2 136.6 178.9 -177.3 66.8 37 ALA -81.5 130.7 178.6 38 ILE -97.8 84.2 -178.7 -57.3 165.2 39 ASP -118.6 3.4 178.1 72.3 -10.6 40 GLY 74.7 7.6 179.6 41 GLN -112.7 121.0 178.8 -128.6 94.2 -178.4 42 PHE -81.8 96.5 179.7 -156.2 -48.7 43 GLY -113.6 -169.2 -178.5 44 PRO -60.0 -29.7 -176.5 -25.9 42.8 45 ALA -74.1 -28.8 179.5 46 THR -73.3 -42.7 177.6 -59.3 47 LYS -61.3 -44.0 179.2 167.4 146.0 179.7 -46.3 48 ALA -59.9 -45.6 -179.4 49 ALA -61.0 -42.7 179.6 50 VAL -61.9 -41.8 -178.7 171.1 51 GLN -59.0 -42.0 179.8 -135.0 149.8 -153.9 52 ARG -64.6 -39.9 178.7 -67.5 179.5 -165.7 100.9 53 PHE -64.4 -47.2 -178.7 165.7 70.1 54 GLN -57.3 -48.9 -179.8 -75.0 160.2 -21.6 55 SER -59.0 -39.7 -177.6 -93.6 56 ALA -65.1 -25.1 -179.6 57 TYR -113.9 18.4 178.5 -74.6 -84.5 58 GLY 62.0 41.4 175.5 59 LEU -105.1 165.5 177.2 -91.3 37.1 60 ALA -69.0 121.0 -176.9 61 ALA -90.4 83.0 179.1 62 ASP -111.2 -6.0 -178.8 54.9 10.0 63 GLY 78.0 14.2 178.2 64 ILE -109.0 121.6 179.5 -67.1 170.1 65 ALA -82.6 97.6 179.5 66 GLY -109.0 -165.7 -176.6 67 PRO -66.0 -24.7 -178.2 -11.1 21.3 68 ALA -81.0 -28.2 179.8 69 THR -72.7 -43.2 178.4 -68.7 70 PHE -69.5 -35.1 178.3 -53.4 -53.8 71 ASN -62.3 -34.0 178.7 -67.5 153.9 72 LYS -72.9 -47.9 176.2 -176.8 69.6 -132.6 178.5 73 ILE -55.0 -43.4 -179.2 -72.9 154.7 74 TYR -58.2 -32.0 179.9 -62.5 -49.1 75 GLN -73.6 -23.7 179.6 -72.3 178.3 134.3 76 LEU -96.3 -9.6 -176.7 -64.2 179.6 77 GLN -96.0 131.9 177.8 -157.5 170.6 -114.3 78 ASP -92.7 166.1 179.3 -95.0 -18.4 79 ASP -46.5 -45.9 -176.8 34.2 -85.5 80 ASP -83.6 8.8 177.4 63.2 3.9 81 CYS 83.9 -7.7 177.7 -73.3 82 THR -76.8 162.7 176.1 62.4 83 PRO -71.4 160.7 -176.5 17.9 -15.0 84 VAL -58.0 -28.6 -175.4 -77.4 85 ASN -103.0 2.4 -178.6 -63.2 -63.2 86 PHE -134.6 152.7 178.0 -62.6 -81.3 87 THR -135.2 162.0 178.0 66.4 88 TYR -60.4 -47.7 -178.7 -87.9 -55.1 89 ALA -57.0 -40.6 -179.9 90 GLU -67.0 -26.7 -179.8 177.9 -151.7 0.7 91 LEU -91.1 3.1 178.7 -100.2 -56.6 92 ASN -149.4 92.9 -180.0 -175.3 -6.4 93 ARG -98.1 16.1 -178.7 -72.6 -40.2 -162.4 -170.8 94 CYS -95.9 -76.1 -179.7 168.2 95 ASN -132.9 -179.2 -178.5 65.2 32.6 96 SER -114.2 35.5 -179.1 67.5 97 ASP -149.0 -4.5 178.9 89.1 -33.2 98 TRP 58.3 30.2 179.4 -67.8 63.8 99 SER -102.8 152.9 179.7 133.1 100 GLY 120.4 -30.8 -179.4 101 GLY -58.1 -174.6 -179.5 102 LYS -96.4 8.9 179.7 -66.8 -93.7 165.1 -82.6 103 VAL -156.1 165.8 179.4 -65.4 104 SER -52.3 162.9 179.1 -72.8 105 ALA -73.3 -32.5 -179.7 106 ALA -75.8 -36.2 177.6 107 THR -69.3 -38.0 179.7 -72.6 108 ALA -63.5 -50.3 179.4 109 ARG -66.4 -34.4 -179.6 -50.0 177.6 77.5 118.8 110 ALA -71.5 -35.4 179.2 111 ASN -67.6 -37.4 -179.8 -76.2 -18.0 112 ALA -62.6 -44.9 -178.8 113 LEU -56.0 -44.2 178.7 -173.7 73.4 114 VAL -61.9 -40.9 -178.2 -175.2 115 THR -59.9 -42.9 178.0 -80.1 116 MET -57.6 -44.7 -179.1 -62.4 -175.3 -134.2 117 TRP -68.1 -35.7 177.2 -79.4 98.2 118 LYS -64.8 -43.9 178.7 -72.5 164.6 166.5 168.0 119 LEU -61.7 -36.0 179.2 -70.7 -177.9 120 GLN -62.0 -46.9 178.7 -170.0 73.4 -135.5 121 ALA -60.0 -47.2 -178.8 122 MET -63.2 -40.6 178.3 -170.0 175.9 85.5 123 ARG -57.4 -47.5 179.6 -179.1 -169.9 -157.0 -76.3 124 HIS -67.7 -41.3 -180.0 -175.6 55.6 125 ALA -59.8 -31.9 179.6 126 MET -83.4 -0.3 177.3 -56.8 -166.3 88.3 127 GLY 105.2 21.8 177.2 128 ASP 60.2 44.1 178.3 -59.5 -52.5 129 LYS -115.2 148.3 -178.2 -57.1 148.7 -50.9 155.7 130 PRO -56.1 134.8 177.7 10.7 -18.1 131 ILE -104.2 123.2 178.6 -75.8 173.3 132 THR -79.6 122.1 178.6 -59.3 133 VAL -102.7 120.9 -180.0 -178.6 134 ASN -95.8 -25.0 -177.5 -63.7 151.4 135 GLY -168.7 166.8 -179.6 136 GLY -151.0 -93.7 -179.9 137 PHE -76.9 143.3 176.7 178.4 70.0 138 ARG -140.9 120.9 176.3 -53.7 -164.1 -54.1 -129.7 139 SER -72.9 178.3 179.3 52.4 140 VAL -63.1 -35.0 179.0 -177.9 141 THR -63.2 -50.5 -178.5 -73.4 142 CYS -58.6 -43.2 -177.7 -86.0 143 ASN -65.1 -39.4 179.9 -175.1 66.8 144 SER -73.6 -43.2 -179.9 -58.2 145 ASN -54.1 -29.5 -178.7 -79.7 175.8 146 VAL -89.4 -20.8 -179.9 102.6 147 GLY 82.0 33.5 -179.0 148 GLY -66.2 174.7 179.4 149 ALA -83.5 145.4 -179.8 150 SER -54.3 -36.1 -178.8 -11.9 151 ASN -86.0 -18.2 -178.4 -59.4 -173.7 152 SER -24.5 124.5 179.8 -169.9 153 ARG -75.5 -8.4 179.6 -38.6 -174.1 161.3 175.8 154 HIS -61.8 -36.1 -178.6 -85.8 -85.8 155 MET -74.8 2.8 179.7 -21.1 -179.7 57.0 156 TYR -114.5 -16.5 178.2 -66.9 85.3 157 GLY 94.2 1.5 180.0 158 HIS -81.0 -23.7 -177.0 -71.6 -47.4 159 ALA -107.8 163.6 176.1 160 ALA -144.7 142.4 176.9 161 ASP -106.2 125.1 -176.7 -76.5 -26.0 162 LEU -103.3 137.9 178.7 -81.0 35.0 163 GLY -93.2 166.8 -177.8 164 ALA -55.0 -45.8 -178.5 165 GLY 54.9 -156.3 179.4 166 SER -79.5 -4.1 -178.3 44.3 167 GLN -87.6 -43.0 -177.1 -62.0 100.3 164.2 168 GLY 98.7 152.3 -178.0 169 PHE -57.0 -43.3 -176.3 -57.3 -60.4 170 CYS -69.8 -42.0 178.7 -75.7 171 ALA -59.4 -37.8 -179.9 172 LEU -68.5 -43.4 -177.5 -69.4 165.1 173 ALA -67.4 -34.3 -179.4 174 GLN -70.1 -44.1 -177.9 -77.6 173.4 169.0 175 ALA -68.7 -32.1 -175.9 176 ALA -55.8 -23.4 178.7 177 ARG -62.9 -25.7 178.5 -79.9 -173.5 -47.1 -164.8 178 ASN -95.7 -0.8 -174.9 -49.1 140.5 179 HIS -121.5 25.1 176.1 -56.7 -75.9 180 GLY 82.5 21.6 178.1 181 PHE -96.9 115.4 -178.3 -72.4 -64.7 182 THR -87.1 -20.8 178.5 47.7 183 GLU -118.7 116.0 179.4 -175.4 165.1 72.3 184 ILE -133.6 121.4 179.9 -58.9 158.2 185 LEU -125.6 136.6 -178.7 -65.1 173.2 186 GLY -158.5 -163.7 -178.8 187 PRO -34.0 121.1 176.1 -38.0 39.0 188 GLY 101.6 -11.1 177.7 189 TYR -98.1 135.3 -177.7 -176.1 -86.1 190 PRO -47.0 123.4 179.0 -31.3 42.4 191 GLY 72.4 18.2 -178.7 192 HIS -128.8 35.3 177.9 -71.7 88.7 193 ASN -90.6 -21.6 -174.4 -76.4 173.8 194 ASP -104.0 35.7 179.1 89.8 47.9 195 HIS 167.7 158.8 178.9 68.6 -89.4 196 THR -114.5 125.0 179.3 -69.1 197 HIS -96.1 126.0 176.2 170.0 90.7 198 VAL -125.7 139.6 178.3 -60.8 199 ALA -151.3 146.8 176.1 200 GLY -90.7 -172.9 178.7 201 GLY 108.9 164.9 179.9 202 ASP -69.9 141.7 177.6 -82.6 1.2 203 GLY 87.3 114.7 -177.7 204 ARG -83.5 126.0 178.0 -153.7 -130.2 -115.3 84.2 205 PHE -148.0 103.7 179.8 176.6 40.3 206 TRP -112.9 118.4 176.4 -75.6 -2.7 207 SER -151.4 121.0 177.0 -175.0 208 ALA -158.9 68.1 -176.7 209 PRO -48.0 -40.4 180.0 14.0 -27.5 210 SER -69.9 -11.9 -179.2 -64.3 211 CYS -106.2 6.4 -180.0 -62.5 212 GLY 90.0 -2.8 -179.9 213 ILE -92.0 123.3 0.0 -49.5 147.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP 58.295 31.182 54.682 2 GLY 55.175 29.542 53.258 3 CYS 54.416 27.305 50.272 4 TYR 57.053 24.591 50.706 5 THR 60.577 24.398 52.179 6 TRP 63.127 21.793 50.976 7 SER 65.010 20.184 53.904 8 GLY 68.101 18.981 52.047 9 THR 69.766 18.206 48.741 10 LEU 68.172 15.940 46.146 11 SER 69.917 13.857 43.487 12 GLU 69.235 10.677 41.481 13 GLY 67.919 7.927 43.730 14 SER 65.880 10.349 45.834 15 SER 62.129 9.777 46.127 16 GLY 59.304 11.397 48.091 17 GLU 57.071 14.484 48.148 18 ALA 60.157 16.680 48.148 19 VAL 60.948 15.115 44.768 20 ARG 57.353 15.438 43.502 21 GLN 57.342 19.199 44.493 22 LEU 60.685 19.901 42.731 23 GLN 59.460 18.122 39.562 24 ILE 56.525 20.561 39.387 25 ARG 58.937 23.538 39.601 26 VAL 61.123 22.251 36.763 27 ALA 58.305 20.760 34.651 28 GLY 59.009 23.632 32.168 29 TYR 62.404 22.056 31.338 30 PRO 61.821 18.524 29.887 31 GLY 63.695 18.946 26.593 32 THR 62.083 19.613 23.197 33 GLY 59.044 17.406 22.513 34 ALA 59.223 15.612 25.898 35 GLN 57.187 15.741 29.135 36 LEU 58.546 15.234 32.679 37 ALA 56.625 12.550 34.678 38 ILE 55.557 13.912 38.112 39 ASP 56.053 10.662 40.022 40 GLY 58.224 11.605 43.019 41 GLN 61.176 9.532 41.769 42 PHE 64.419 11.407 40.972 43 GLY 65.760 9.617 37.861 44 PRO 67.861 10.751 34.932 45 ALA 65.024 12.724 33.333 46 THR 64.703 14.727 36.577 47 LYS 68.462 15.377 36.763 48 ALA 68.336 16.700 33.150 49 ALA 65.414 19.021 33.949 50 VAL 67.186 20.412 37.003 51 GLN 70.349 21.033 34.956 52 ARG 68.345 23.011 32.372 53 PHE 66.706 25.122 35.099 54 GLN 70.074 25.839 36.718 55 SER 71.477 26.893 33.348 56 ALA 68.521 29.169 32.550 57 TYR 69.113 31.281 35.658 58 GLY 72.932 31.295 35.646 59 LEU 73.472 28.771 38.464 60 ALA 76.121 25.953 38.396 61 ALA 74.433 23.314 36.250 62 ASP 75.331 19.941 37.892 63 GLY 71.822 18.460 38.055 64 ILE 71.893 18.306 41.880 65 ALA 69.119 20.224 43.737 66 GLY 71.065 21.917 46.580 67 PRO 70.421 25.089 48.567 68 ALA 71.190 27.588 45.721 69 THR 68.839 25.725 43.452 70 PHE 66.171 26.013 46.200 71 ASN 66.947 29.785 46.831 72 LYS 66.214 30.486 43.099 73 ILE 62.908 28.553 43.275 74 TYR 62.142 30.556 46.439 75 GLN 62.590 33.771 44.368 76 LEU 60.095 32.543 41.762 77 GLN 57.556 31.152 44.247 78 ASP 54.556 33.064 45.589 79 ASP 52.898 32.375 48.943 80 ASP 50.272 30.133 47.354 81 CYS 52.911 28.084 45.512 82 THR 52.157 29.680 42.092 83 PRO 55.112 31.197 40.223 84 VAL 55.634 35.028 40.574 85 ASN 54.190 35.972 37.177 86 PHE 50.994 33.855 37.006 87 THR 47.972 33.423 39.289 88 TYR 45.063 31.003 39.771 89 ALA 42.491 33.780 38.939 90 GLU 44.245 34.620 35.646 91 LEU 44.029 30.864 34.868 92 ASN 40.283 30.629 35.563 93 ARG 38.043 33.293 33.991 94 CYS 35.220 30.798 34.283 95 ASN 34.167 30.377 37.915 96 SER 35.751 30.759 41.352 97 ASP 35.765 27.166 42.747 98 TRP 37.234 25.243 39.870 99 SER 34.190 22.965 39.866 100 GLY 32.410 21.832 36.710 101 GLY 35.315 20.064 35.027 102 LYS 35.980 16.442 33.929 103 VAL 38.043 15.879 37.075 104 SER 37.964 17.063 40.694 105 ALA 38.536 20.754 41.588 106 ALA 41.709 19.717 43.418 107 THR 42.971 17.674 40.444 108 ALA 42.012 20.639 38.196 109 ARG 43.999 23.170 40.296 110 ALA 46.959 20.760 40.577 111 ASN 46.993 20.273 36.798 112 ALA 46.762 24.114 36.501 113 LEU 49.680 24.577 38.840 114 VAL 51.973 22.539 36.581 115 THR 50.824 24.670 33.603 116 MET 51.759 27.841 35.567 117 TRP 55.304 26.535 36.248 118 LYS 55.700 25.591 32.550 119 LEU 54.539 29.174 31.574 120 GLN 57.043 30.725 34.024 121 ALA 59.930 28.866 32.326 122 MET 58.626 29.934 28.896 123 ARG 58.201 33.567 30.104 124 HIS 61.894 33.726 31.084 125 ALA 63.101 31.912 27.912 126 MET 61.211 34.550 25.784 127 GLY 62.952 37.523 27.505 128 ASP 61.014 38.294 30.685 129 LYS 58.120 40.092 28.979 130 PRO 54.558 39.566 30.157 131 ILE 52.690 36.604 28.652 132 THR 48.949 37.368 28.227 133 VAL 46.658 34.542 29.496 134 ASN 43.156 34.840 28.041 135 GLY 41.593 31.698 29.568 136 GLY 42.471 28.452 31.350 137 PHE 40.059 26.275 33.287 138 ARG 36.592 25.768 31.832 139 SER 33.818 23.871 33.641 140 VAL 31.441 21.888 31.327 141 THR 29.074 24.899 31.118 142 CYS 31.859 27.325 30.297 143 ASN 33.203 24.938 27.615 144 SER 29.812 24.635 25.894 145 ASN 29.195 28.412 26.187 146 VAL 32.355 28.697 24.056 147 GLY 31.352 25.794 21.757 148 GLY 34.535 23.989 22.851 149 ALA 35.341 20.333 22.004 150 SER 33.884 17.480 24.086 151 ASN 37.406 16.181 24.785 152 SER 38.911 19.642 25.590 153 ARG 41.833 19.543 28.014 154 HIS 40.605 22.941 29.313 155 MET 38.075 21.042 31.475 156 TYR 41.020 19.244 33.124 157 GLY 43.056 22.315 34.036 158 HIS 45.842 21.301 31.623 159 ALA 45.391 24.100 29.036 160 ALA 45.735 27.892 28.728 161 ASP 44.817 30.158 25.777 162 LEU 47.480 32.837 25.161 163 GLY 47.009 36.305 23.584 164 ALA 49.679 37.817 21.271 165 GLY 51.346 40.326 23.691 166 SER 54.664 41.664 22.418 167 GLN 55.721 38.125 21.248 168 GLY 53.041 37.250 18.699 169 PHE 51.070 33.979 18.365 170 CYS 53.668 32.125 16.332 171 ALA 56.596 32.941 18.589 172 LEU 54.532 31.579 21.487 173 ALA 53.549 28.344 19.668 174 GLN 57.152 27.761 18.596 175 ALA 58.659 28.205 22.088 176 ALA 55.914 26.013 23.657 177 ARG 57.575 23.016 21.958 178 ASN 60.414 23.354 24.504 179 HIS 58.321 23.497 27.634 180 GLY 56.259 20.342 28.117 181 PHE 53.126 21.291 26.187 182 THR 52.043 18.091 24.352 183 GLU 49.102 19.861 22.741 184 ILE 49.770 23.139 20.864 185 LEU 47.220 24.670 18.471 186 GLY 47.671 28.041 16.742 187 PRO 47.596 29.974 13.487 188 GLY 46.341 28.021 10.482 189 TYR 44.559 25.406 12.598 190 PRO 40.765 25.768 12.510 191 GLY 39.427 28.229 15.048 192 HIS 42.920 29.020 16.336 193 ASN 44.093 32.125 14.490 194 ASP 43.264 34.585 17.312 195 HIS 45.206 32.852 20.177 196 THR 47.736 30.177 20.819 197 HIS 46.403 27.115 22.733 198 VAL 48.966 25.253 24.914 199 ALA 48.143 22.170 27.049 200 GLY 49.876 19.493 29.139 201 GLY 48.522 15.885 29.465 202 ASP 49.202 12.570 27.642 203 GLY 49.443 12.480 23.839 204 ARG 51.231 14.880 21.571 205 PHE 49.249 16.828 18.980 206 TRP 50.987 19.911 17.529 207 SER 49.383 22.011 14.774 208 ALA 49.917 25.694 13.802 209 PRO 50.465 25.535 10.026 210 SER 50.868 29.322 9.650 211 CYS 53.675 29.149 12.172 212 GLY 55.559 26.326 10.459 213 ILE 54.301 23.577 12.860 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S S/S S S 10 S S S S S S/H H H H H 20 H H H H H H H C C C 30 C C S S S S S S S S 40 S S S/H H H H H H H H 50 H H H H H H H H S S 60 S S S S S S/H H H H H 70 H H H H H H H T T T 80 T C T T T T H H H H 90 H H C S S S S C S S 100 S S C H H H H H H H 110 H H H H H H H H H H 120 H H H H H H H C S S 130 S S S S S S S S S/H H 140 H H H H H H H/S S S S 150 C C T T T T C S S S 160 S S S S/T T T T H H H 170 H H H H H H 3 3 3/S S 180 S S/S S S S S S C T T 190 T T/T T T T/S S S S S S 200 S S/S S S S S S S/T T T 210 T/S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S B 10 t T T t B h H H H H 20 H H H H H h T T t S 30 t T T t S S 40 B h H H H H H H H 50 H H H H H H h T t 60 S S B h H H H H 70 H H H H H H h t T T 80 t S B T T t t T T T 90 T t S S S S S 100 S S S h H H H H H H 110 H H H H H H H H H H 120 H H H H H h T t 130 e E E E h H 140 H H H H H H h t t T 150 T g G G G G g e E E 160 E E e t T T T h H H 170 H H H H H h G G g T 180 t e E E E e T T t T 190 T t S S S E E E E e 200 S S S E E E g G G 210 G g t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 38.8 35.1 94.8 2 GLY 10.5 30.2 81.8 3 CYS 93.7 94.5 63.0 4 TYR 125.0 69.1 61.1 5 THR 30.3 28.3 70.3 6 TRP 204.1 99.6 38.8 7 SER 0.0 0.0 89.3 8 GLY 0.6 1.6 79.9 9 THR 56.4 52.8 56.4 10 LEU 129.9 87.9 43.9 11 SER 41.2 49.3 59.5 12 GLU 73.8 53.2 56.5 13 GLY 0.0 0.0 85.5 14 SER 55.7 66.6 60.9 15 SER 44.9 53.7 74.6 16 GLY 2.3 6.6 79.8 17 GLU 58.7 42.4 79.3 18 ALA 47.5 65.4 56.7 19 VAL 118.5 99.7 43.6 20 ARG 114.0 54.6 71.3 21 GLN 124.9 84.1 59.7 22 LEU 147.8 100.0 26.3 23 GLN 147.4 99.2 52.4 24 ILE 136.3 95.0 49.3 25 ARG 207.2 99.2 31.8 26 VAL 118.8 100.0 35.4 27 ALA 71.3 98.2 49.1 28 GLY 34.8 99.9 48.4 29 TYR 160.8 88.8 42.7 30 PRO 121.6 97.7 61.2 31 GLY 19.4 55.6 75.7 32 THR 37.7 35.3 76.6 33 GLY 30.0 86.3 66.3 34 ALA 29.6 40.8 77.9 35 GLN 110.8 74.6 65.4 36 LEU 140.8 95.3 49.5 37 ALA 10.0 13.8 81.2 38 ILE 115.3 80.4 52.6 39 ASP 44.0 39.8 73.6 40 GLY 28.7 82.5 64.2 41 GLN 37.1 24.9 81.0 42 PHE 166.8 100.0 44.5 43 GLY 12.1 34.7 57.8 44 PRO 22.9 18.4 77.6 45 ALA 10.4 14.4 72.8 46 THR 104.0 97.3 41.6 47 LYS 111.3 64.2 71.4 48 ALA 44.5 61.3 78.1 49 ALA 72.6 100.0 53.5 50 VAL 118.8 100.0 39.6 51 GLN 90.0 60.6 68.7 52 ARG 117.9 56.5 61.9 53 PHE 162.6 97.5 31.4 54 GLN 145.3 97.8 55.5 55 SER 32.0 38.2 73.9 56 ALA 44.4 61.1 63.2 57 TYR 159.3 88.0 50.2 58 GLY 0.0 0.0 84.2 59 LEU 114.8 77.7 57.3 60 ALA 0.0 0.0 84.8 61 ALA 53.5 73.7 71.1 62 ASP 44.2 40.0 74.3 63 GLY 34.8 100.0 56.1 64 ILE 69.9 48.7 65.8 65 ALA 72.6 100.0 35.0 66 GLY 25.0 71.7 51.8 67 PRO 23.9 19.2 77.9 68 ALA 11.9 16.4 75.7 69 THR 102.6 96.0 40.9 70 PHE 157.9 94.7 42.5 71 ASN 35.0 28.9 69.7 72 LYS 129.5 74.7 49.2 73 ILE 143.0 99.7 28.8 74 TYR 124.6 68.8 65.1 75 GLN 46.1 31.0 80.1 76 LEU 131.3 88.8 42.5 77 GLN 140.0 94.2 53.0 78 ASP 70.8 64.1 75.9 79 ASP 12.3 11.2 78.1 80 ASP 51.9 47.0 69.4 81 CYS 68.3 68.9 64.5 82 THR 106.6 99.7 48.6 83 PRO 124.5 100.0 43.4 84 VAL 76.2 64.2 77.1 85 ASN 76.8 63.5 72.4 86 PHE 165.0 98.9 44.6 87 THR 40.3 37.7 72.8 88 TYR 141.6 78.2 55.5 89 ALA 11.9 16.3 86.2 90 GLU 101.3 73.1 70.2 91 LEU 145.3 98.3 37.9 92 ASN 119.9 99.2 59.4 93 ARG 72.4 34.6 79.4 94 CYS 92.8 93.6 58.4 95 ASN 76.8 63.6 74.2 96 SER 0.0 0.0 83.5 97 ASP 36.5 33.1 78.7 98 TRP 196.4 95.8 44.6 99 SER 31.7 37.9 78.9 100 GLY 11.0 31.5 72.3 101 GLY 34.8 100.0 57.0 102 LYS 94.2 54.3 60.4 103 VAL 80.1 67.5 61.0 104 SER 16.0 19.1 80.9 105 ALA 45.3 62.4 67.6 106 ALA 3.8 5.3 74.4 107 THR 47.5 44.4 66.8 108 ALA 72.6 100.0 50.8 109 ARG 118.6 56.8 56.7 110 ALA 24.2 33.3 76.4 111 ASN 93.2 77.1 56.6 112 ALA 70.8 97.5 46.9 113 LEU 129.1 87.3 50.1 114 VAL 97.4 82.0 48.9 115 THR 104.7 97.9 46.6 116 MET 159.4 100.0 31.1 117 TRP 200.3 97.7 46.3 118 LYS 164.6 94.9 49.8 119 LEU 147.8 100.0 23.6 120 GLN 141.6 95.3 46.9 121 ALA 69.7 96.0 60.0 122 MET 159.4 100.0 31.8 123 ARG 173.5 83.0 59.2 124 HIS 106.5 70.9 71.3 125 ALA 33.0 45.5 73.6 126 MET 135.1 84.7 48.8 127 GLY 5.1 14.8 78.5 128 ASP 49.0 44.3 74.4 129 LYS 104.4 60.2 69.3 130 PRO 32.2 25.8 83.0 131 ILE 143.5 100.0 41.9 132 THR 44.4 41.5 76.6 133 VAL 118.8 100.0 46.5 134 ASN 62.2 51.4 64.0 135 GLY 21.6 62.2 65.5 136 GLY 34.6 99.5 61.9 137 PHE 166.7 99.9 51.5 138 ARG 168.7 80.8 53.9 139 SER 76.2 91.2 49.0 140 VAL 59.1 49.8 74.7 141 THR 15.3 14.3 81.7 142 CYS 71.0 71.6 54.0 143 ASN 113.9 94.2 54.1 144 SER 24.8 29.7 80.0 145 ASN 23.7 19.6 77.2 146 VAL 50.1 42.2 78.3 147 GLY 0.8 2.2 81.6 148 GLY 24.8 71.3 76.8 149 ALA 11.2 15.5 79.9 150 SER 2.2 2.6 88.7 151 ASN 2.4 2.0 85.3 152 SER 69.0 82.5 62.9 153 ARG 166.3 79.6 62.8 154 HIS 146.3 97.4 66.4 155 MET 157.3 98.7 51.3 156 TYR 114.2 63.1 59.8 157 GLY 33.8 97.2 58.0 158 HIS 106.4 70.8 62.6 159 ALA 72.6 100.0 54.0 160 ALA 72.6 100.0 35.2 161 ASP 95.5 86.4 60.2 162 LEU 147.8 100.0 35.5 163 GLY 25.3 72.6 65.5 164 ALA 41.7 57.4 57.8 165 GLY 15.0 43.1 84.8 166 SER 26.3 31.4 75.3 167 GLN 143.2 96.4 53.7 168 GLY 9.8 28.0 69.9 169 PHE 118.3 70.9 58.8 170 CYS 60.2 60.7 60.1 171 ALA 41.7 57.5 67.9 172 LEU 147.8 100.0 41.8 173 ALA 72.6 100.0 40.0 174 GLN 77.2 51.9 74.3 175 ALA 54.3 74.8 61.2 176 ALA 72.6 100.0 37.7 177 ARG 130.9 62.6 54.8 178 ASN 65.2 53.9 71.7 179 HIS 139.5 92.9 45.0 180 GLY 33.9 97.4 56.3 181 PHE 166.8 100.0 44.0 182 THR 90.4 84.6 67.0 183 GLU 115.7 83.5 53.1 184 ILE 143.5 100.0 37.9 185 LEU 131.0 88.6 46.8 186 GLY 34.8 100.0 46.0 187 PRO 109.9 88.3 51.1 188 GLY 20.0 57.4 73.3 189 TYR 118.3 65.3 54.5 190 PRO 24.2 19.4 75.7 191 GLY 0.0 0.0 85.1 192 HIS 119.5 79.6 62.1 193 ASN 44.7 36.9 75.0 194 ASP 1.2 1.1 82.2 195 HIS 114.9 76.5 66.8 196 THR 106.9 100.0 37.3 197 HIS 139.6 92.9 54.2 198 VAL 118.8 100.0 31.2 199 ALA 72.6 100.0 48.5 200 GLY 32.9 94.6 75.0 201 GLY 23.2 66.8 73.5 202 ASP 0.0 0.0 90.1 203 GLY 0.0 0.0 80.3 204 ARG 94.8 45.4 67.0 205 PHE 77.4 46.4 69.7 206 TRP 166.9 81.4 51.6 207 SER 63.4 75.8 44.9 208 ALA 72.6 100.0 42.5 209 PRO 68.0 54.6 78.8 210 SER 28.9 34.6 67.8 211 CYS 95.4 96.2 45.9 212 GLY 0.0 0.0 80.2 213 ILE 133.7 93.2 52.6