Protein Data Bank File : 1hu3a Title : TRANSLATION 03-JAN-01 1HU3 Number of Amino Acid Residues : 196 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER ASP PRO GLU ASN ILE LYS THR GLN GLU 10 LEU PHE ARG LYS VAL ARG SER ILE LEU ASN 20 LYS LEU THR PRO GLN PHE ASN GLN LEU LYS 30 GLN VAL SER GLY LEU THR VAL ASP THR GLU 40 GLU ARG LEU LYS GLY VAL ILE ASP LEU VAL 50 PHE GLU LYS ALA ILE ASP GLU PRO SER PHE 60 SER VAL ALA TYR ALA ASN CYS ARG CYS LEU 70 VAL THR LEU LYS VAL PRO ASN PHE ARG LYS 80 LEU LEU LEU ASN ARG CYS GLN LYS GLU PHE 90 GLU LYS ASP LYS ALA ALA LYS ASP LYS ALA 100 ARG ARG ARG SER ILE GLY ASN ILE LYS PHE 110 ILE GLY GLU LEU PHE LYS LEU LYS LEU THR 120 GLU ALA ILE HIS ASP CYS VAL VAL LYS LEU 130 LEU LYS ASN HIS ASP GLU GLU SER LEU GLU 140 CYS LEU CYS ARG LEU LEU THR THR ILE GLY 150 LYS ASP LEU ASP PHE GLU LYS ALA LYS PRO 160 ARG ASP GLN TYR PHE ASN GLN GLU LYS ILE 170 VAL LYS GLU ARG LYS THR SER SER ARG ILE 180 ARG PHE LEU GLN ASP VAL ILE ASP LEU ARG 190 LEU CYS ASN TRP VAL SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 -13.1 -176.8 0.0 2 ASP 40.2 -77.8 -179.6 -78.6 34.3 3 PRO -63.6 -33.8 178.8 -19.1 33.4 4 GLU -65.9 -42.2 178.9 -66.0 -71.0 -64.1 5 ASN -53.1 -30.4 179.4 -70.8 -33.9 6 ILE -70.3 -48.4 -180.0 -75.4 -163.8 7 LYS -65.0 -35.3 179.0 -60.9 -166.6 164.9 -178.0 8 THR -65.4 -30.3 -179.7 -59.5 9 GLN -68.8 -50.1 -179.8 -157.1 61.1 48.5 10 GLU -65.1 -32.5 179.7 -63.8 167.4 -29.3 11 LEU -63.4 -55.9 -179.2 160.4 61.5 12 PHE -55.5 -40.6 -179.7 -70.7 178.9 13 ARG -68.7 -37.8 178.1 -73.3 -170.6 179.9 -87.8 14 LYS -63.3 -44.4 179.4 -78.4 167.8 73.8 63.5 15 VAL -65.6 -40.3 178.6 -175.8 16 ARG -63.1 -35.4 179.1 -76.4 -177.6 -178.1 -78.3 17 SER -62.3 -51.6 179.9 175.4 18 ILE -55.5 -45.9 -179.5 -63.2 178.7 19 LEU -73.6 -28.3 -177.3 -60.4 147.2 20 ASN -84.9 9.6 177.7 -66.3 -26.6 21 LYS -70.1 123.1 -178.6 -62.8 -58.0 178.5 -172.7 22 LEU -61.3 -10.7 176.3 -164.3 32.8 23 THR -115.9 106.9 -180.0 -74.4 24 PRO -43.1 133.3 -179.8 -38.0 45.8 25 GLN -83.6 -160.4 49.1 0.0 0.0 0.0 26 PHE -73.9 -67.0 -178.5 -165.5 67.4 27 ASN -44.5 -53.6 -179.9 -64.0 -30.8 28 GLN -63.5 -28.3 179.3 74.6 -175.4 77.2 29 LEU -64.7 24.8 74.8 -122.0 41.4 30 LYS 25.7 -44.7 179.2 150.1 -157.4 -58.3 -38.9 31 GLN -63.1 -48.1 -179.8 -78.0 159.7 160.6 32 VAL -63.0 -24.4 179.4 170.5 33 SER -78.0 -1.2 179.7 81.5 34 GLY -106.4 14.8 -178.9 35 LEU -112.4 155.0 178.5 -57.2 169.9 36 THR -126.2 99.4 179.2 -54.8 37 VAL -107.7 82.4 -178.5 -165.5 38 ASP -100.8 5.4 -178.7 41.6 34.6 39 THR -134.8 152.1 179.8 -92.6 40 GLU -68.0 -37.0 179.7 178.4 138.3 -68.0 41 GLU -63.8 -29.8 -179.1 0.0 0.0 0.0 42 ARG -78.1 -42.5 178.9 -67.2 -179.2 167.1 144.8 43 LEU -62.0 -48.3 -179.9 -140.8 -147.9 44 LYS -61.9 -33.4 179.0 136.1 84.0 176.2 169.1 45 GLY -72.0 -45.0 179.7 46 VAL -59.2 -51.8 178.4 172.8 47 ILE -54.3 -42.9 177.6 -81.0 173.0 48 ASP -61.1 -40.8 -179.7 -82.6 -15.4 49 LEU -60.1 -40.0 -179.1 -74.7 178.1 50 VAL -67.2 -42.7 179.1 174.2 51 PHE -63.6 -44.4 179.7 -87.7 77.1 52 GLU -57.0 -38.2 179.6 -79.6 167.9 39.5 53 LYS -72.5 -44.9 -179.9 -129.2 -57.8 171.5 -61.9 54 ALA -62.5 -26.9 178.7 55 ILE -77.3 -28.2 179.5 -59.8 -55.1 56 ASP -80.4 -34.8 179.5 177.2 57.0 57 GLU -134.0 76.3 -179.7 -64.2 165.7 55.4 58 PRO -54.4 -34.1 -178.6 -21.2 37.6 59 SER -51.7 -32.3 -179.6 -57.1 60 PHE -96.3 19.4 -178.4 -64.3 -25.0 61 SER -62.1 -18.0 177.5 49.6 62 VAL -69.5 -42.4 -179.7 161.5 63 ALA -63.6 -50.9 -178.9 64 TYR -61.8 -34.3 178.5 -55.0 -48.7 65 ALA -68.2 -39.6 178.4 66 ASN -64.7 32.4 74.6 -82.8 -48.5 67 CYS 24.4 -39.3 -179.8 -76.4 68 ARG -60.0 -31.2 179.2 -151.0 -156.5 168.1 -160.1 69 CYS -76.8 -39.7 -179.4 -73.9 70 LEU -66.7 -27.1 -178.8 -78.7 -24.9 71 VAL -69.5 3.3 178.6 87.6 72 THR -100.4 34.4 -178.9 -60.0 73 LEU -141.8 142.0 179.5 -50.8 -171.4 74 LYS -104.7 133.8 -179.6 0.0 0.0 0.0 0.0 75 VAL -144.5 124.0 -179.7 -175.0 76 PRO -62.8 69.7 178.1 32.0 -44.6 77 ASN 108.9 -1.2 -179.4 56.1 -45.1 78 PHE -65.5 -59.9 -179.9 -174.5 88.6 79 ARG -49.8 -32.6 179.6 -81.3 148.3 -161.5 154.0 80 LYS -62.6 -48.4 179.2 0.0 0.0 0.0 0.0 81 LEU -64.8 -37.1 178.8 -58.6 -177.4 82 LEU -61.9 -56.6 179.5 -109.5 -161.5 83 LEU -51.3 -54.0 179.4 0.0 0.0 84 ASN -49.9 -50.7 -179.3 -63.5 174.5 85 ARG -62.1 -38.7 179.2 -175.2 65.6 -172.9 82.5 86 CYS -65.4 -56.6 -179.6 -77.3 87 GLN -58.2 -11.2 178.7 -61.7 -153.9 -35.1 88 LYS -68.2 -45.7 179.8 0.0 0.0 0.0 0.0 89 GLU -63.7 -36.5 -179.9 -70.2 -71.4 -49.4 90 PHE -73.1 -52.5 179.0 -67.4 144.7 91 GLU -61.2 -19.7 180.0 0.0 0.0 0.0 92 LYS -94.8 -26.8 179.4 0.0 0.0 0.0 0.0 93 ASP -76.3 -16.4 179.3 0.0 0.0 94 LYS -83.1 -3.4 179.8 0.0 0.0 0.0 0.0 95 ALA -103.7 -22.5 -10.9 96 ALA -3.7 59.2 175.2 97 LYS -111.4 36.4 179.4 -134.6 -115.6 -82.0 60.0 98 ASP -133.3 10.7 178.1 0.0 0.0 99 LYS -119.3 -9.5 177.7 0.0 0.0 0.0 0.0 100 ALA -75.9 -26.8 179.0 101 ARG -63.0 -43.8 179.2 -78.9 159.5 -162.1 165.3 102 ARG -57.9 -49.8 179.7 0.0 0.0 0.0 0.0 103 ARG -64.5 -35.6 179.6 180.0 -160.2 175.6 160.4 104 SER -64.1 -36.2 179.5 158.2 105 ILE -65.4 -43.0 -179.5 -54.9 -51.9 106 GLY -62.6 -44.6 -179.4 107 ASN -61.5 -51.0 179.7 -172.1 52.7 108 ILE -57.7 -36.9 178.3 -61.5 171.2 109 LYS -61.4 -42.0 -179.0 177.3 177.5 177.4 65.0 110 PHE -68.1 -51.8 179.1 178.6 45.4 111 ILE -55.3 -36.1 179.4 -72.7 176.4 112 GLY -72.0 -30.8 178.7 113 GLU -70.7 -39.0 179.1 -141.1 46.9 60.0 114 LEU -67.2 -42.8 -179.6 -75.4 179.5 115 PHE -61.0 -28.4 -178.7 170.7 83.4 116 LYS -76.0 -7.9 179.5 -72.9 -167.6 -100.0 -177.4 117 LEU -113.6 20.1 177.3 -65.0 173.1 118 LYS 66.0 76.6 67.0 0.0 0.0 0.0 0.0 119 LEU -6.8 161.8 -178.0 -67.5 -177.3 120 THR -90.5 148.4 179.3 66.8 121 GLU -60.5 -25.0 -179.8 -46.6 173.1 68.7 122 ALA -63.4 -37.7 -179.3 123 ILE -73.8 40.0 72.0 -161.7 67.5 124 HIS 30.7 -38.3 178.2 -82.0 -80.3 125 ASP -59.1 -45.0 -179.1 -86.1 -6.2 126 CYS -58.9 -50.3 179.7 -66.0 127 VAL -56.1 -51.6 179.2 167.5 128 VAL -56.7 -40.3 179.3 167.7 129 LYS -66.2 -37.8 180.0 172.8 59.9 -178.6 173.9 130 LEU -70.0 -39.5 179.1 -69.5 173.9 131 LEU -68.8 -35.3 179.1 -80.0 167.7 132 LYS -54.6 -54.5 178.1 0.0 0.0 0.0 0.0 133 ASN -89.6 110.0 -178.3 -11.4 -31.4 134 HIS -92.1 35.3 179.6 63.6 -50.2 135 ASP -85.2 156.0 179.6 65.9 -66.3 136 GLU -43.0 -54.3 180.0 -92.9 -175.6 46.9 137 GLU -53.1 -45.1 -179.3 -84.6 -165.5 69.8 138 SER -65.5 -45.4 -179.7 -73.4 139 LEU -61.3 -42.0 -180.0 -67.2 -175.2 140 GLU -66.7 -39.6 178.1 -177.4 158.1 7.5 141 CYS -60.1 -40.6 -179.8 -179.2 142 LEU -64.1 -43.2 -179.0 176.2 62.3 143 CYS -66.7 -41.7 179.5 -76.0 144 ARG -69.1 -43.9 179.3 -73.3 174.6 172.3 -87.8 145 LEU -59.4 -64.6 -179.3 -167.6 71.5 146 LEU -55.2 -28.5 179.7 -72.2 175.9 147 THR -67.8 -40.2 -178.4 -67.2 148 THR -79.7 -37.3 -179.3 -80.2 149 ILE -119.1 1.7 -179.3 62.4 164.5 150 GLY -40.6 -59.2 -177.5 151 LYS -66.4 -30.1 178.4 75.0 170.1 172.6 -176.2 152 ASP -62.4 -42.2 -179.7 -66.8 -42.8 153 LEU -74.4 -23.9 -178.9 -67.8 -177.5 154 ASP -78.2 65.7 -179.8 -136.9 -177.4 155 PHE -93.6 145.3 -179.5 0.0 0.0 156 GLU -39.0 -36.3 -179.3 0.0 0.0 0.0 157 LYS -84.5 -17.8 -179.7 0.0 0.0 0.0 0.0 158 ALA -99.0 -8.2 -179.9 159 LYS -41.6 -46.2 180.0 -62.8 -62.9 -177.2 -167.3 160 PRO -61.5 -44.7 178.8 25.6 -41.4 161 ARG -69.6 29.0 72.5 -79.3 172.9 -65.1 166.6 162 ASP 34.5 -38.8 -178.8 -80.5 4.0 163 GLN -72.8 -42.7 -179.7 -170.2 164.9 64.3 164 TYR -56.6 -54.0 -178.4 -64.5 151.0 165 PHE -61.9 -29.7 178.2 -72.5 70.1 166 ASN -76.3 -31.2 177.9 -69.1 -17.0 167 GLN -68.0 30.4 73.9 -62.5 -173.5 68.5 168 GLU 28.4 -37.1 179.6 -164.5 -81.3 -29.4 169 LYS -64.9 -39.6 178.6 0.0 0.0 0.0 0.0 170 ILE -64.9 -31.0 179.0 -70.0 166.5 171 VAL -71.6 -55.1 -178.3 167.6 172 LYS -50.7 -40.2 179.1 -149.2 172.8 -177.8 -165.5 173 GLU -93.9 112.4 -176.8 -77.7 -70.2 -43.2 174 ARG -75.9 49.9 177.5 -51.6 -155.8 163.9 -149.1 175 LYS -92.5 6.3 179.5 0.0 0.0 0.0 0.0 176 THR -125.4 156.0 179.1 50.3 177 SER -59.4 148.7 178.8 57.7 178 SER -63.4 -25.6 178.8 57.8 179 ARG -61.1 -61.0 178.9 171.0 -162.2 164.4 -122.3 180 ILE -57.7 -28.4 -178.9 -69.5 -70.2 181 ARG -70.8 -32.8 178.6 -158.9 -177.6 -56.9 130.8 182 PHE -76.9 28.1 75.7 -89.7 106.3 183 LEU 24.6 -46.2 179.9 -72.8 165.8 184 GLN -62.9 -19.2 179.0 -72.3 -169.1 -45.4 185 ASP -77.4 -41.7 -179.9 -108.5 45.2 186 VAL -69.1 -34.8 178.8 -164.8 187 ILE -69.2 -37.2 179.7 -62.8 169.6 188 ASP -64.2 -45.2 180.0 -79.8 -14.5 189 LEU -51.0 -62.8 -179.9 -131.2 -158.3 190 ARG -53.5 -55.2 178.7 -161.0 -164.6 178.8 -154.7 191 LEU -50.9 -18.3 -179.8 -69.2 -174.3 192 CYS -103.5 24.6 -179.6 -81.4 193 ASN 56.5 35.3 -179.4 -27.8 -39.3 194 TRP 58.1 35.4 176.8 -55.2 100.0 195 VAL -116.2 142.0 -178.6 175.8 196 SER -98.9 167.5 0.0 -174.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER 5.786 22.151 2.805 2 ASP 4.835 25.817 2.110 3 PRO 5.144 27.671 5.475 4 GLU 8.456 25.914 6.357 5 ASN 9.658 26.615 2.818 6 ILE 9.286 30.246 3.744 7 LYS 11.561 30.073 6.817 8 THR 14.126 27.972 4.957 9 GLN 14.055 30.759 2.415 10 GLU 14.704 33.496 4.951 11 LEU 17.408 31.363 6.560 12 PHE 19.277 30.961 3.317 13 ARG 18.906 34.644 2.533 14 LYS 20.134 35.602 5.989 15 VAL 23.161 33.320 5.463 16 ARG 23.868 34.716 1.945 17 SER 23.717 38.153 3.534 18 ILE 26.274 37.199 6.198 19 LEU 28.587 35.749 3.574 20 ASN 27.994 38.586 1.087 21 LYS 29.368 41.486 3.109 22 LEU 32.095 42.740 0.753 23 THR 34.252 43.163 3.871 24 PRO 34.835 39.789 5.566 25 GLN 33.308 39.638 9.053 26 PHE 34.815 35.957 14.560 27 ASN 33.036 37.906 17.328 28 GLN 30.547 39.578 15.003 29 LEU 30.148 36.156 13.361 30 LYS 26.399 37.300 17.160 31 GLN 25.169 36.941 13.570 32 VAL 24.936 33.140 13.668 33 SER 22.931 33.435 16.897 34 GLY 20.268 35.226 14.887 35 LEU 19.809 32.162 12.728 36 THR 17.568 29.161 13.106 37 VAL 19.073 25.954 11.767 38 ASP 16.545 23.443 13.137 39 THR 16.658 20.934 10.269 40 GLU 19.235 18.692 8.679 41 GLU 18.169 19.949 5.257 42 ARG 18.824 23.421 6.622 43 LEU 22.225 22.692 8.180 44 LYS 23.279 20.993 4.934 45 GLY 21.972 23.958 2.931 46 VAL 23.759 26.584 5.061 47 ILE 26.959 24.552 4.857 48 ASP 26.499 24.324 1.070 49 LEU 26.080 28.075 1.028 50 VAL 29.414 28.490 2.800 51 PHE 31.359 26.218 0.472 52 GLU 29.873 27.908 -2.566 53 LYS 31.084 31.242 -1.221 54 ALA 34.499 29.835 -0.244 55 ILE 34.862 28.414 -3.775 56 ASP 34.167 31.879 -5.228 57 GLU 36.583 33.739 -2.932 58 PRO 39.151 31.258 -1.578 59 SER 41.117 34.230 -0.178 60 PHE 38.552 34.795 2.561 61 SER 38.561 31.154 3.574 62 VAL 39.815 32.097 7.035 63 ALA 36.590 34.008 7.476 64 TYR 34.395 31.233 6.078 65 ALA 36.226 28.722 8.224 66 ASN 35.525 30.913 11.257 67 CYS 31.905 27.154 10.125 68 ARG 33.510 27.308 13.536 69 CYS 30.407 29.205 14.680 70 LEU 27.905 26.789 13.110 71 VAL 29.450 23.765 14.852 72 THR 27.875 25.201 18.022 73 LEU 24.478 23.844 16.929 74 LYS 22.535 20.573 17.266 75 VAL 20.279 19.419 14.421 76 PRO 18.189 16.203 14.036 77 ASN 26.934 15.517 13.276 78 PHE 28.294 18.804 11.941 79 ARG 31.845 17.678 11.156 80 LYS 30.235 14.705 9.403 81 LEU 28.339 16.953 7.001 82 LEU 31.519 19.022 6.597 83 LEU 33.706 16.006 5.827 84 ASN 30.988 14.762 3.506 85 ARG 30.826 18.166 1.795 86 CYS 34.611 18.340 1.498 87 GLN 34.987 14.835 0.064 88 LYS 32.334 15.861 -2.421 89 GLU 34.862 18.064 -4.234 90 PHE 37.371 15.216 -3.954 91 GLU 35.010 12.394 -4.916 92 LYS 34.064 14.732 -7.797 93 ASP 37.627 15.700 -8.695 94 LYS 38.266 11.975 -9.224 95 ALA 35.743 12.148 -12.102 96 ALA 41.249 23.299 -19.493 97 LYS 40.973 20.580 -16.888 98 ASP 44.146 22.483 -16.059 99 LYS 41.896 25.251 -14.752 100 ALA 40.388 22.721 -12.368 101 ARG 43.758 23.008 -10.619 102 ARG 43.075 26.669 -9.912 103 ARG 39.732 25.778 -8.347 104 SER 41.392 22.845 -6.585 105 ILE 43.933 25.180 -5.006 106 GLY 41.137 27.355 -3.646 107 ASN 39.233 24.425 -2.204 108 ILE 42.307 22.972 -0.550 109 LYS 43.096 26.398 0.990 110 PHE 39.618 26.382 2.537 111 ILE 39.763 22.752 3.594 112 GLY 43.122 23.500 5.178 113 GLU 41.621 26.427 7.037 114 LEU 38.877 24.140 8.353 115 PHE 41.435 21.497 9.340 116 LYS 43.310 24.109 11.373 117 LEU 40.271 24.580 13.559 118 LYS 39.918 20.838 14.189 119 LEU 38.432 18.068 9.643 120 THR 40.449 14.853 9.750 121 GLU 44.164 14.412 9.072 122 ALA 43.050 11.797 6.584 123 ILE 41.511 14.445 4.314 124 HIS 46.649 13.540 3.032 125 ASP 44.208 13.552 0.143 126 CYS 45.115 17.227 -0.367 127 VAL 48.863 16.567 -0.310 128 VAL 48.541 13.683 -2.793 129 LYS 46.418 15.944 -5.010 130 LEU 49.046 18.691 -4.870 131 LEU 51.914 16.320 -5.736 132 LYS 49.858 14.870 -8.574 133 ASN 49.794 18.275 -10.307 134 HIS 53.437 19.377 -10.186 135 ASP 52.837 22.953 -11.325 136 GLU 54.337 25.940 -9.435 137 GLU 50.988 26.892 -7.876 138 SER 50.330 23.418 -6.609 139 LEU 53.850 23.057 -5.245 140 GLU 53.716 26.387 -3.439 141 CYS 50.337 25.480 -1.989 142 LEU 51.971 22.218 -0.855 143 CYS 54.906 24.011 0.703 144 ARG 52.730 26.471 2.543 145 LEU 50.371 23.718 3.657 146 LEU 53.071 21.297 4.883 147 THR 54.975 24.137 6.545 148 THR 51.922 24.980 8.591 149 ILE 50.479 21.537 9.378 150 GLY 53.399 19.296 8.543 151 LYS 54.181 18.024 12.028 152 ASP 50.539 17.527 12.978 153 LEU 50.224 15.180 10.005 154 ASP 53.616 13.684 10.828 155 PHE 52.287 11.092 13.295 156 GLU 54.233 7.926 14.089 157 LYS 51.703 5.929 12.058 158 ALA 51.731 8.334 9.116 159 LYS 55.546 8.543 9.071 160 PRO 55.694 6.159 6.062 161 ARG 53.295 8.130 3.820 162 ASP 58.358 9.681 4.077 163 GLN 57.078 9.083 0.584 164 TYR 55.716 12.596 0.099 165 PHE 59.070 14.064 1.020 166 ASN 61.039 11.698 -1.160 167 GLN 58.723 12.665 -4.043 168 GLU 63.324 15.762 -3.323 169 LYS 62.888 14.105 -6.715 170 ILE 61.064 17.208 -7.983 171 VAL 64.071 19.192 -6.726 172 LYS 66.737 17.009 -8.267 173 GLU 65.114 17.325 -11.680 174 ARG 65.246 20.973 -12.632 175 LYS 61.919 21.132 -14.510 176 THR 60.863 23.646 -11.801 177 SER 61.990 27.174 -10.931 178 SER 64.919 27.440 -8.537 179 ARG 62.482 29.447 -6.513 180 ILE 60.066 26.553 -5.990 181 ARG 63.148 24.364 -5.546 182 PHE 64.335 26.503 -2.617 183 LEU 60.689 22.683 -1.483 184 GLN 64.122 22.412 0.151 185 ASP 62.794 24.479 3.058 186 VAL 60.014 22.072 3.921 187 ILE 62.523 19.249 3.598 188 ASP 64.969 21.119 5.844 189 LEU 62.162 21.700 8.375 190 ARG 61.185 18.059 8.662 191 LEU 64.800 16.851 8.795 192 CYS 64.918 19.268 11.737 193 ASN 61.973 17.574 13.519 194 TRP 59.668 20.445 12.505 195 VAL 61.595 22.962 14.638 196 SER 62.726 26.180 12.979 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 H H H H H H H 20 H S S S S/X X/C C C C/X X/H 30 H H H H H/S S S S H H 40 H H H H H H H H H H 50 H H H H H H H H C H 60 H H H H H H/X X/H H H H 70 H 3 3/S S S S/X X/H H H H 80 H H H H H H H H H H 90 H H H H HPX X/C H H H H 100 H 3 3/H H H H H H H H 110 H H H H H H H H/X X/C C 120 C C C/X X/H H H H H H H 130 H H H H H H H H H H 140 H H H H H H H H H/H H 150 H H H H T T T T C C 160 C/X X/H H H H H H/X X/H H H 170 H H H C C C H H H H 180 H H/X X/H H H H H H H H 190 H H H S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t h H H H H H H H H 10 H H H H H H H H H h 20 t S S t T T t 30 g G G G g h H 40 H H H H H H H H H H 50 H H H H H H h T T h 60 H H H H H h t T g G 70 G G g h H H H 80 H H H H H H H H H H 90 H H H h t S h H 100 H H H H H H H H H H 110 H H H H H h T t t 120 T T t h H H H H H H 130 H H h h H H H H H 140 H H H H H H H H H H 150 H H H h t T T T T T 160 t h H H H H h h H H 170 H H h S S h H H H 180 H h h H H H H H H H 190 H h T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 32.9 39.4 81.4 2 ASP 2.2 2.0 80.3 3 PRO 24.8 19.9 75.5 4 GLU 46.7 33.7 75.5 5 ASN 48.2 39.8 74.3 6 ILE 35.8 25.0 78.3 7 LYS 38.3 22.1 86.8 8 THR 74.5 69.7 55.2 9 GLN 56.5 38.0 75.1 10 GLU 44.2 31.9 64.6 11 LEU 141.2 95.5 37.7 12 PHE 116.2 69.6 54.7 13 ARG 53.2 25.5 78.9 14 LYS 74.5 43.0 67.5 15 VAL 113.4 95.4 29.7 16 ARG 90.2 43.2 71.4 17 SER 34.4 41.2 74.9 18 ILE 117.6 82.0 48.3 19 LEU 131.5 89.0 41.5 20 ASN 60.4 50.0 70.0 21 LYS 66.3 38.2 88.2 22 LEU 5.9 4.0 90.2 23 THR 4.8 4.5 80.8 24 PRO 86.8 69.7 53.6 25 GLN 146.0 98.3 63.9 26 PHE 89.5 53.7 72.4 27 ASN 0.0 0.0 83.8 28 GLN 64.0 43.0 64.4 29 LEU 130.6 88.3 51.3 30 LYS 30.8 17.8 83.9 31 GLN 106.1 71.4 51.2 32 VAL 103.4 87.0 41.3 33 SER 13.2 15.7 82.4 34 GLY 2.6 7.4 85.7 35 LEU 144.7 97.9 38.3 36 THR 22.1 20.6 79.6 37 VAL 118.8 100.0 32.1 38 ASP 51.9 46.9 67.9 39 THR 61.2 57.2 60.0 40 GLU 60.9 43.9 66.0 41 GLU 75.8 54.7 66.3 42 ARG 194.0 92.9 52.2 43 LEU 147.1 99.5 35.2 44 LYS 64.6 37.3 70.5 45 GLY 24.0 69.0 60.9 46 VAL 118.3 99.6 23.9 47 ILE 141.4 98.5 31.5 48 ASP 86.5 78.3 64.2 49 LEU 137.1 92.8 52.6 50 VAL 113.4 95.4 34.2 51 PHE 166.7 99.9 39.2 52 GLU 57.2 41.3 74.0 53 LYS 132.2 76.2 66.3 54 ALA 72.6 100.0 41.1 55 ILE 118.5 82.6 61.9 56 ASP 32.4 29.3 80.2 57 GLU 93.5 67.5 57.4 58 PRO 84.2 67.6 65.8 59 SER 16.7 19.9 64.8 60 PHE 101.1 60.6 62.2 61 SER 83.6 100.0 44.7 62 VAL 40.0 33.6 81.0 63 ALA 59.2 81.5 56.3 64 TYR 164.3 90.8 44.8 65 ALA 72.4 99.7 43.4 66 ASN 90.1 74.5 45.0 67 CYS 97.0 97.8 35.0 68 ARG 90.8 43.5 64.5 69 CYS 80.2 80.8 52.6 70 LEU 137.7 93.2 30.3 71 VAL 88.1 74.2 64.0 72 THR 14.1 13.2 81.5 73 LEU 100.2 67.8 62.1 74 LYS 99.4 57.3 83.9 75 VAL 118.8 100.0 48.1 76 PRO 24.9 20.0 80.1 77 ASN 62.8 51.9 78.0 78 PHE 159.8 95.8 35.5 79 ARG 72.3 34.6 70.9 80 LYS 124.8 71.9 69.9 81 LEU 117.0 79.1 55.5 82 LEU 139.4 94.3 28.6 83 LEU 118.4 80.1 57.8 84 ASN 35.2 29.1 69.2 85 ARG 165.9 79.4 54.5 86 CYS 99.2 100.0 32.0 87 GLN 58.3 39.2 66.8 88 LYS 134.0 77.3 75.5 89 GLU 116.6 84.1 70.2 90 PHE 139.9 83.9 47.0 91 GLU 79.2 57.1 76.3 92 LYS 120.7 69.6 77.6 93 ASP 72.0 65.2 74.8 94 LYS 112.1 64.6 83.8 95 ALA 9.5 13.1 76.7 96 ALA 13.3 18.4 78.4 97 LYS 23.3 13.4 85.8 98 ASP 69.9 63.3 75.0 99 LYS 126.0 72.7 72.2 100 ALA 29.4 40.5 68.5 101 ARG 112.1 53.6 69.5 102 ARG 157.2 75.3 75.0 103 ARG 84.0 40.2 75.5 104 SER 66.7 79.8 51.4 105 ILE 115.0 80.1 59.3 106 GLY 29.5 84.8 53.3 107 ASN 116.1 96.1 36.7 108 ILE 142.2 99.1 37.4 109 LYS 83.3 48.0 75.6 110 PHE 166.8 100.0 36.8 111 ILE 141.7 98.7 35.7 112 GLY 29.4 84.5 54.2 113 GLU 117.0 84.4 56.0 114 LEU 142.8 96.6 31.4 115 PHE 144.1 86.4 46.7 116 LYS 97.9 56.5 67.1 117 LEU 93.6 63.3 69.3 118 LYS 110.1 63.5 87.9 119 LEU 142.9 96.7 33.2 120 THR 26.5 24.8 65.6 121 GLU 54.9 39.6 65.3 122 ALA 13.6 18.7 75.6 123 ILE 135.9 94.7 46.3 124 HIS 134.4 89.5 55.4 125 ASP 50.8 46.0 64.8 126 CYS 90.7 91.4 37.5 127 VAL 118.1 99.4 25.0 128 VAL 37.7 31.7 70.7 129 LYS 112.0 64.6 60.5 130 LEU 147.8 100.0 38.8 131 LEU 138.7 93.9 46.1 132 LYS 123.1 71.0 78.0 133 ASN 109.1 90.3 64.1 134 HIS 36.3 24.1 74.3 135 ASP 62.9 56.9 68.0 136 GLU 62.8 45.3 70.9 137 GLU 33.9 24.5 72.9 138 SER 83.6 100.0 56.0 139 LEU 147.8 100.0 35.0 140 GLU 91.9 66.3 70.2 141 CYS 81.5 82.1 44.8 142 LEU 140.8 95.3 30.7 143 CYS 79.6 80.2 50.3 144 ARG 44.1 21.1 82.5 145 LEU 126.7 85.7 39.3 146 LEU 133.9 90.6 30.7 147 THR 45.7 42.8 65.3 148 THR 53.5 50.0 69.7 149 ILE 131.4 91.5 36.6 150 GLY 34.6 99.3 44.8 151 LYS 49.3 28.4 75.9 152 ASP 35.8 32.4 68.5 153 LEU 136.8 92.6 47.0 154 ASP 94.8 85.8 64.0 155 PHE 120.1 72.0 79.2 156 GLU 70.9 51.2 72.5 157 LYS 97.9 56.4 82.4 158 ALA 65.9 90.8 70.3 159 LYS 87.3 50.3 76.4 160 PRO 48.3 38.8 75.7 161 ARG 93.7 44.9 67.9 162 ASP 49.5 44.8 78.7 163 GLN 33.6 22.6 78.5 164 TYR 161.9 89.5 39.3 165 PHE 142.3 85.3 45.4 166 ASN 21.7 17.9 76.3 167 GLN 75.4 50.8 57.9 168 GLU 56.7 40.9 62.9 169 LYS 122.8 70.8 78.2 170 ILE 110.1 76.8 45.8 171 VAL 104.0 87.6 48.8 172 LYS 30.4 17.5 85.3 173 GLU 10.8 7.8 85.3 174 ARG 56.3 27.0 89.2 175 LYS 108.3 62.4 77.8 176 THR 94.6 88.5 56.9 177 SER 48.2 57.7 68.2 178 SER 31.7 37.9 73.0 179 ARG 83.6 40.0 76.3 180 ILE 135.0 94.1 47.7 181 ARG 187.2 89.6 57.0 182 PHE 29.6 17.7 82.0 183 LEU 131.0 88.6 39.6 184 GLN 67.6 45.5 61.9 185 ASP 14.0 12.7 83.7 186 VAL 110.9 93.3 40.9 187 ILE 109.8 76.5 47.8 188 ASP 30.6 27.7 73.8 189 LEU 116.2 78.6 56.6 190 ARG 168.9 80.9 58.2 191 LEU 33.0 22.3 77.9 192 CYS 31.2 31.4 83.2 193 ASN 10.6 8.7 80.8 194 TRP 188.6 92.0 44.1 195 VAL 19.9 16.8 81.9 196 SER 4.0 4.8 72.4