Protein Data Bank File : 1qqp2 Title : VIRUS/VIRAL PROTEIN 20-MAY-99 1QQP Number of Amino Acid Residues : 216 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP LYS LYS THR THR THR LEU LEU GLU ASP 10 ARG ILE LEU THR THR ARG ASN GLY HIS THR 20 THR SER THR THR GLN SER SER VAL GLY VAL 30 THR TYR GLY TYR ALA THR ALA GLU ASP PHE 40 VAL SER GLY PRO ASN THR SER GLY LEU GLU 50 THR ARG VAL VAL GLN ALA GLU ARG PHE PHE 60 LYS THR HIS LEU PHE ASP TRP VAL THR SER 70 ASP SER PHE GLY ARG CYS HIS LEU LEU GLU 80 LEU PRO THR ASP HIS LYS GLY VAL TYR GLY 90 SER LEU THR ASP SER TYR ALA TYR MET ARG 100 ASN GLY TRP ASP VAL GLU VAL THR ALA VAL 110 GLY ASN GLN PHE ASN GLY GLY CYS LEU LEU 120 VAL ALA MET VAL PRO GLU LEU CYS SER ILE 130 GLN LYS ARG GLU LEU TYR GLN LEU THR LEU 140 PHE PRO HIS GLN PHE ILE ASN PRO ARG THR 150 ASN MET THR ALA HIS ILE THR VAL PRO PHE 160 VAL GLY VAL ASN ARG TYR ASP GLN TYR LYS 170 VAL HIS LYS PRO TRP THR LEU VAL VAL MET 180 VAL VAL ALA PRO LEU THR VAL ASN THR GLU 190 GLY ALA PRO GLN ILE LYS VAL TYR ALA ASN 200 ILE ALA PRO THR ASN VAL HIS VAL ALA GLY 210 GLU PHE PRO SER LYS GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 -30.6 -178.7 -29.2 159.1 2 LYS 70.3 64.1 -178.5 -52.1 175.6 -177.5 -170.3 3 LYS -157.9 -56.5 -179.8 53.8 62.4 170.3 179.9 4 THR 156.9 -133.5 140.7 -135.0 5 THR -24.2 -97.4 177.4 -163.3 6 THR -88.6 -176.4 179.5 -77.3 7 LEU -52.4 116.6 -177.2 -34.5 86.5 8 LEU -149.1 -150.7 -179.1 116.2 178.9 9 GLU 33.1 -117.0 177.2 -137.4 42.1 -51.1 10 ASP -88.0 23.3 176.7 -131.6 -16.3 11 ARG -102.5 9.0 175.5 -58.6 -126.4 -75.1 128.9 12 ILE -99.8 118.0 -179.0 -62.3 -163.4 13 LEU -129.5 133.6 176.9 173.0 67.0 14 THR -115.2 128.7 179.5 -67.2 15 THR -112.5 134.5 178.7 -61.1 16 ARG -121.2 128.4 175.8 178.6 -177.5 157.5 -129.1 17 ASN -131.1 106.0 -179.0 -76.7 116.0 18 GLY 66.6 -139.8 -179.9 19 HIS -91.9 33.8 178.7 -56.7 -38.6 20 THR -131.9 139.6 179.1 65.9 21 THR -131.6 157.4 178.1 66.0 22 SER -142.1 128.9 -179.2 -178.9 23 THR -119.6 136.9 175.1 -60.1 24 THR -131.1 143.0 177.8 -178.0 25 GLN -98.6 6.9 176.5 -59.2 -166.8 56.2 26 SER -132.3 47.5 -179.1 63.4 27 SER -69.4 149.2 178.3 175.7 28 VAL -121.2 17.6 -179.8 108.9 29 GLY 95.9 -174.3 -178.8 30 VAL -121.2 133.3 176.9 175.6 31 THR -93.6 122.7 175.0 -69.1 32 TYR -94.6 123.0 -179.0 -72.7 -85.8 33 GLY -99.5 128.5 175.0 34 TYR 68.7 -22.4 180.0 -56.8 -39.1 35 ALA -170.6 160.7 176.4 36 THR -107.0 5.4 178.6 52.2 37 ALA -155.8 159.5 178.6 38 GLU -73.9 157.8 174.5 -65.8 -84.4 -35.1 39 ASP -83.4 -170.1 -177.3 61.6 -34.6 40 PHE -62.5 134.7 -175.6 -42.1 82.5 41 VAL -98.3 -13.2 179.2 118.2 42 SER -120.1 96.2 179.0 -59.0 43 GLY -117.7 -173.2 -179.5 44 PRO -67.8 -21.1 -176.7 25.6 -38.9 45 ASN -70.8 -13.0 178.7 69.6 -54.4 46 THR -115.2 2.7 177.1 54.7 47 SER 47.4 39.0 178.8 -58.1 48 GLY 67.7 16.3 -177.6 49 LEU -99.8 1.7 -178.9 -93.1 -3.5 50 GLU -78.1 154.1 175.4 72.6 -74.7 -18.0 51 THR -141.8 157.2 179.0 54.6 52 ARG -91.8 140.9 176.3 173.0 136.9 178.1 -141.1 53 VAL -123.3 89.9 -176.6 7.0 54 VAL -59.9 -28.7 -179.9 125.1 55 GLN -64.2 -15.7 -179.7 -68.9 80.3 7.7 56 ALA -91.6 -10.2 -175.1 57 GLU -86.3 79.2 -176.1 -59.1 174.5 1.3 58 ARG -158.2 163.0 -175.9 60.6 -161.6 -39.7 -66.9 59 PHE -72.8 140.3 172.6 -78.5 120.9 60 PHE -129.1 163.2 -172.1 66.9 95.1 61 LYS -131.1 151.1 173.8 -55.4 174.1 -162.1 -61.0 62 THR -152.4 152.8 173.8 -14.3 63 HIS -84.2 143.1 178.4 167.6 67.6 64 LEU -101.9 -68.1 179.0 -96.3 13.6 65 PHE -164.8 172.0 178.5 72.4 -73.8 66 ASP -106.5 118.1 -179.8 -65.0 -23.8 67 TRP -80.3 117.8 -178.9 -174.8 17.6 68 VAL -121.6 162.3 -177.3 -63.4 69 THR -60.2 -23.8 -179.1 57.5 70 SER -81.0 -8.1 178.9 63.4 71 ASP -72.5 135.7 178.4 -69.8 -34.8 72 SER -112.6 175.3 179.9 59.6 73 PHE -46.0 135.1 177.0 162.5 69.2 74 GLY 95.8 -13.9 177.7 75 ARG -65.7 128.0 -176.9 -172.7 -94.0 -162.1 -103.1 76 CYS -128.1 158.1 173.1 -74.3 77 HIS -131.8 127.4 -178.9 -178.7 80.7 78 LEU -113.2 136.4 177.1 -89.1 56.7 79 LEU -130.3 108.5 178.5 174.4 71.6 80 GLU -72.6 145.7 -178.4 -63.0 -176.2 148.9 81 LEU -127.6 139.9 -0.1 -96.3 3.8 82 PRO -69.6 155.3 178.4 26.5 -38.2 83 THR -112.3 -176.8 178.7 -168.3 84 ASP -59.1 133.6 -177.6 -62.8 -56.8 85 HIS -140.4 125.6 -177.1 -171.2 -68.8 86 LYS -101.7 14.1 -179.7 -62.6 -172.1 167.2 173.7 87 GLY -111.8 -150.7 -176.6 88 VAL -63.4 -45.2 179.5 50.7 89 TYR -56.9 -44.9 179.5 177.3 -96.8 90 GLY -61.6 -37.9 -179.6 91 SER -67.7 -27.5 178.6 75.5 92 LEU -61.2 -37.7 -178.7 -104.5 22.5 93 THR -67.6 -18.1 177.5 70.6 94 ASP -98.6 -6.0 -177.9 -74.0 138.4 95 SER -109.2 -20.4 -178.8 -61.0 96 TYR -132.1 144.1 -178.2 -64.2 -88.3 97 ALA -76.2 -30.2 -176.9 98 TYR -126.5 141.4 -179.2 -57.4 -75.1 99 MET -151.3 161.4 173.1 -70.4 179.7 64.9 100 ARG -153.7 148.5 176.6 60.6 173.3 -79.0 154.8 101 ASN -169.9 157.4 174.7 60.8 -88.2 102 GLY -99.6 -167.2 -179.6 103 TRP -140.3 139.9 175.2 -59.9 104.5 104 ASP -113.8 112.6 -173.4 -172.5 -152.5 105 VAL -116.9 129.0 177.3 -179.5 106 GLU -122.6 126.2 177.6 -174.1 171.9 -105.7 107 VAL -118.3 132.4 179.6 169.4 108 THR -122.2 149.3 179.9 62.7 109 ALA -141.2 84.5 -176.6 110 VAL -85.1 107.2 174.1 176.9 111 GLY -124.8 -129.9 171.4 112 ASN -137.9 -175.4 -176.1 66.3 -163.8 113 GLN -80.4 2.2 178.9 66.0 -82.2 -119.5 114 PHE -100.4 -1.0 172.8 -66.6 -84.4 115 ASN -85.5 159.0 177.0 -78.7 112.2 116 GLY -131.9 177.0 -178.3 117 GLY 111.5 -179.3 -176.3 118 CYS -162.0 138.8 177.3 177.7 119 LEU -113.8 146.6 174.1 -64.9 177.6 120 LEU -111.4 124.6 176.2 173.1 57.9 121 VAL -111.8 129.3 -176.9 -0.9 122 ALA -138.3 153.7 176.4 123 MET -110.6 121.7 -174.8 -77.9 -67.6 -74.8 124 VAL -123.9 125.5 179.9 -176.5 125 PRO -77.8 147.0 175.7 26.0 -29.5 126 GLU 50.2 53.7 -177.1 -47.7 -66.0 -9.5 127 LEU -119.4 109.7 175.1 179.0 75.9 128 CYS -93.9 -44.6 179.6 178.5 129 SER -149.7 160.0 -179.0 70.8 130 ILE -141.4 145.5 179.1 -178.2 168.9 131 GLN -84.1 161.0 -178.4 -47.3 -172.9 106.5 132 LYS -56.8 -46.7 -179.2 163.4 55.9 97.7 62.9 133 ARG -63.7 -31.5 -179.6 -71.9 -122.2 -81.8 149.6 134 GLU -67.9 -24.2 179.5 -62.0 175.3 -36.1 135 LEU -60.9 -27.1 178.9 -64.0 179.8 136 TYR -66.7 -11.4 -180.0 -75.9 -105.2 137 GLN -121.4 22.9 -180.0 -62.9 -178.0 32.1 138 LEU -63.5 -20.5 178.9 -122.9 -136.3 139 THR -70.1 -5.1 175.1 44.1 140 LEU -70.9 -19.5 -178.7 -69.0 174.4 141 PHE -97.2 157.2 179.5 -59.8 107.7 142 PRO -52.0 124.0 -175.8 -33.4 42.1 143 HIS -151.6 174.2 174.1 68.3 -84.6 144 GLN -159.1 151.8 178.2 -135.6 174.7 52.5 145 PHE -101.8 156.0 172.8 -68.2 88.5 146 ILE -119.8 116.3 -175.7 -68.4 174.3 147 ASN -128.8 107.1 -178.2 -170.3 -171.2 148 PRO -41.4 -38.4 -179.7 -29.6 40.0 149 ARG -66.0 -18.4 -177.6 60.9 -178.5 -66.5 102.3 150 THR -116.0 -45.9 -174.4 -56.3 151 ASN -151.1 165.5 178.9 67.8 135.8 152 MET -122.4 -4.8 -175.8 -51.1 -168.3 -78.2 153 THR -129.0 137.0 175.9 -52.6 154 ALA -117.5 143.4 -178.1 155 HIS -139.7 121.3 -179.2 -164.9 -37.1 156 ILE -130.4 138.0 179.4 -59.2 167.8 157 THR -125.5 126.8 -178.7 -58.5 158 VAL -132.6 152.2 179.5 -62.6 159 PRO -88.5 173.8 174.3 38.5 -42.2 160 PHE -68.9 142.4 175.2 173.7 -103.7 161 VAL -135.6 159.1 176.4 -66.6 162 GLY 158.4 160.9 177.5 163 VAL -68.6 -24.0 179.7 -59.7 164 ASN -110.2 146.4 -178.8 -66.5 139.6 165 ARG -69.1 -29.9 174.8 -167.0 170.5 -53.5 99.1 166 TYR -126.5 155.7 -176.0 -83.6 -113.8 167 ASP -121.4 169.5 175.5 -144.9 159.6 168 GLN -120.0 91.4 -174.9 -69.4 174.9 95.0 169 TYR -61.6 -18.6 178.6 -67.2 -41.8 170 LYS -69.8 -21.7 -179.4 -69.7 167.3 -173.3 -53.9 171 VAL -119.6 -4.1 -179.6 -62.1 172 HIS -148.1 137.0 179.7 176.0 -106.9 173 LYS -122.0 106.8 -179.1 -59.7 -65.5 -167.6 -72.1 174 PRO -69.5 -27.1 -176.4 28.3 -37.1 175 TRP -124.1 146.3 174.9 -76.1 106.5 176 THR -131.1 126.1 177.1 -61.8 177 LEU -84.6 124.8 177.0 168.5 58.2 178 VAL -121.7 134.2 177.5 1.9 179 VAL -119.6 125.4 -177.1 -180.0 180 MET -126.7 141.6 176.7 175.1 179.5 77.6 181 VAL -78.9 120.4 178.0 173.7 182 VAL -93.6 -50.3 177.8 175.7 183 ALA -128.4 134.0 -178.7 184 PRO -55.1 148.7 178.0 -17.6 31.8 185 LEU -65.4 133.8 174.3 176.6 70.8 186 THR -117.4 144.0 -176.9 59.0 187 VAL -109.8 -38.0 -178.6 174.7 188 ASN 54.5 -142.2 -179.3 -71.2 125.7 189 THR -97.0 -30.3 -177.3 54.8 190 GLU -107.2 -2.6 -178.7 -65.9 -65.4 116.2 191 GLY -75.8 166.4 176.3 192 ALA -68.2 146.9 -179.2 193 PRO -65.8 -25.9 176.3 26.4 -39.7 194 GLN -160.6 167.3 -180.0 55.6 169.3 -142.8 195 ILE -129.2 118.8 178.2 -64.7 -179.7 196 LYS -82.7 131.6 -178.4 -62.6 -177.2 138.8 -72.3 197 VAL -103.9 125.0 -177.7 -175.2 198 TYR -123.5 153.3 178.1 -75.2 92.5 199 ALA -119.8 142.3 178.4 200 ASN -127.7 110.3 -173.6 -167.9 28.7 201 ILE -125.3 140.7 176.7 -57.6 168.8 202 ALA -128.0 132.5 178.2 203 PRO -73.4 146.0 179.0 -15.7 27.2 204 THR -124.9 151.3 177.8 58.3 205 ASN 47.7 53.9 -177.3 -59.5 -63.4 206 VAL -74.6 117.6 177.1 178.4 207 HIS -123.2 142.9 -179.6 -68.7 73.6 208 VAL -131.4 157.7 177.6 -59.3 209 ALA -157.4 149.2 176.1 210 GLY 84.3 71.6 -178.5 211 GLU -63.6 134.6 178.9 43.3 -92.3 -124.2 212 PHE -86.1 162.3 178.0 -81.2 138.2 213 PRO -76.9 168.4 176.2 26.7 -39.9 214 SER -87.2 170.5 177.8 60.3 215 LYS -76.1 -15.3 -177.4 -78.8 82.4 163.3 -177.1 216 GLU -55.2 -137.3 0.0 75.6 174.3 -57.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP 8.504 38.304 117.605 2 LYS 8.020 38.629 113.832 3 LYS 4.167 38.588 113.779 4 THR 2.003 41.699 114.523 5 THR -1.210 44.503 120.001 6 THR -1.468 41.690 122.679 7 LEU 0.077 38.150 122.274 8 LEU -0.836 37.176 118.593 9 GLU -0.635 36.286 114.837 10 ASP 1.550 33.508 113.573 11 ARG 2.488 33.472 117.247 12 ILE -0.541 31.279 117.922 13 LEU 0.652 27.661 118.083 14 THR -1.331 24.551 119.020 15 THR 0.560 21.383 119.943 16 ARG -1.152 18.030 120.021 17 ASN 0.245 14.895 121.710 18 GLY -2.269 12.041 121.769 19 HIS -5.647 13.161 123.128 20 THR -4.091 16.246 124.784 21 THR -3.524 19.689 123.242 22 SER -1.847 22.888 124.376 23 THR -2.322 26.288 122.735 24 THR -0.315 29.433 123.257 25 GLN -0.894 32.866 121.734 26 SER 2.654 34.071 122.311 27 SER 4.771 31.402 120.672 28 VAL 8.313 32.203 119.617 29 GLY 8.502 28.905 117.687 30 VAL 9.905 25.480 118.586 31 THR 13.565 24.643 119.125 32 TYR 14.531 21.199 117.754 33 GLY 17.607 19.994 119.584 34 TYR 20.344 17.879 117.924 35 ALA 18.091 16.265 115.301 36 THR 14.634 16.637 113.788 37 ALA 13.885 12.866 113.975 38 GLU 14.879 9.820 116.099 39 ASP 17.746 7.499 115.009 40 PHE 16.931 3.722 114.575 41 VAL 14.592 2.267 117.123 42 SER 15.176 -1.402 116.166 43 GLY 18.743 -2.491 116.629 44 PRO 20.401 -5.710 117.687 45 ASN 20.172 -5.076 121.444 46 THR 16.416 -5.808 121.582 47 SER 16.322 -8.751 119.094 48 GLY 13.197 -7.455 117.347 49 LEU 11.183 -7.719 120.563 50 GLU 10.564 -3.974 121.130 51 THR 7.147 -2.363 120.595 52 ARG 5.814 1.175 120.485 53 VAL 3.269 2.323 123.084 54 VAL 1.352 5.203 121.629 55 GLN -0.935 5.498 124.678 56 ALA 1.955 7.017 126.673 57 GLU 2.628 9.828 124.185 58 ARG 0.607 12.633 125.764 59 PHE 1.173 15.625 128.056 60 PHE 1.779 15.382 131.834 61 LYS 2.406 18.377 134.125 62 THR 4.551 19.613 137.020 63 HIS 5.277 22.838 138.818 64 LEU 8.990 23.811 138.546 65 PHE 9.547 26.850 140.851 66 ASP 8.311 30.359 141.616 67 TRP 10.383 33.109 140.018 68 VAL 10.650 35.994 142.506 69 THR 12.454 39.352 142.475 70 SER 15.103 38.111 144.900 71 ASP 16.382 35.389 142.540 72 SER 19.580 36.562 140.906 73 PHE 21.490 35.606 137.770 74 GLY 22.403 31.921 137.862 75 ARG 19.541 30.741 140.057 76 CYS 18.512 27.410 138.454 77 HIS 15.907 24.733 138.752 78 LEU 16.790 21.258 137.424 79 LEU 14.320 18.494 136.564 80 GLU 15.798 15.092 135.586 81 LEU 13.764 13.115 133.044 82 PRO 12.024 10.775 133.216 83 THR 10.534 12.001 136.432 84 ASP 7.781 10.395 138.610 85 HIS 4.801 9.664 136.445 86 LYS 1.567 8.253 137.779 87 GLY -0.104 7.581 134.472 88 VAL 0.484 5.206 131.602 89 TYR 4.070 6.216 130.852 90 GLY 4.984 5.644 134.520 91 SER 3.442 2.196 134.564 92 LEU 5.593 1.216 131.532 93 THR 8.732 1.725 133.641 94 ASP 7.465 -0.910 136.078 95 SER 6.438 -3.306 133.311 96 TYR 9.414 -3.387 130.913 97 ALA 13.143 -3.557 131.577 98 TYR 14.268 -1.373 128.645 99 MET 12.827 1.831 127.172 100 ARG 13.587 4.835 124.998 101 ASN 11.681 8.008 124.129 102 GLY 12.331 11.636 123.244 103 TRP 10.574 14.638 124.848 104 ASP 8.278 17.422 123.638 105 VAL 8.684 20.142 126.314 106 GLU 6.701 23.279 126.962 107 VAL 7.684 25.588 129.871 108 THR 5.476 28.583 130.757 109 ALA 6.180 31.571 133.024 110 VAL 2.962 33.576 133.047 111 GLY 3.274 37.104 134.517 112 ASN 2.266 40.046 132.306 113 GLN 3.975 42.302 129.747 114 PHE 4.847 44.865 132.449 115 ASN 7.251 42.469 134.134 116 GLY 10.896 42.563 132.978 117 GLY 13.734 40.073 133.413 118 CYS 14.524 36.913 131.485 119 LEU 14.658 33.117 131.872 120 LEU 16.726 30.679 129.804 121 VAL 15.163 27.233 129.370 122 ALA 17.406 24.405 128.120 123 MET 17.386 20.610 127.697 124 VAL 20.790 19.231 128.705 125 PRO 21.989 15.644 128.291 126 GLU 23.720 13.757 131.152 127 LEU 23.513 16.598 133.661 128 CYS 23.617 15.983 137.379 129 SER 25.240 19.360 138.369 130 ILE 26.841 22.399 136.731 131 GLN 29.367 25.067 137.869 132 LYS 28.672 28.782 137.962 133 ARG 31.070 29.664 135.104 134 GLU 29.538 26.953 132.881 135 LEU 26.147 28.654 133.089 136 TYR 27.539 31.357 130.757 137 GLN 27.574 28.660 128.075 138 LEU 24.203 26.989 128.711 139 THR 23.190 28.191 125.195 140 LEU 25.358 25.415 123.713 141 PHE 22.356 23.176 124.593 142 PRO 18.881 23.126 122.908 143 HIS 17.205 26.212 124.426 144 GLN 14.744 29.084 124.198 145 PHE 14.346 32.248 126.326 146 ILE 11.243 33.507 128.135 147 ASN 11.289 37.360 128.115 148 PRO 7.980 38.853 129.482 149 ARG 7.853 41.727 126.981 150 THR 7.708 39.043 124.245 151 ASN 6.516 35.642 125.392 152 MET 5.303 33.412 128.219 153 THR 6.047 30.029 126.635 154 ALA 9.242 28.182 125.653 155 HIS 8.985 24.977 123.553 156 ILE 11.871 22.535 122.929 157 THR 11.680 19.115 121.257 158 VAL 14.530 16.590 121.609 159 PRO 15.145 12.947 120.560 160 PHE 16.339 10.083 122.769 161 VAL 20.165 10.208 123.265 162 GLY 22.618 7.889 125.012 163 VAL 25.607 5.551 124.835 164 ASN 22.985 2.724 124.657 165 ARG 20.125 2.416 122.096 166 TYR 17.603 1.541 124.904 167 ASP 17.900 2.621 128.538 168 GLN 17.186 1.386 132.067 169 TYR 15.529 4.489 133.499 170 LYS 15.655 3.259 137.087 171 VAL 19.431 3.768 136.985 172 HIS 20.092 6.433 134.336 173 LYS 18.380 9.724 133.356 174 PRO 19.601 10.937 129.944 175 TRP 18.021 14.419 129.959 176 THR 17.711 17.254 132.450 177 LEU 15.386 20.232 131.917 178 VAL 17.035 23.378 133.268 179 VAL 15.446 26.793 133.809 180 MET 17.875 29.541 134.739 181 VAL 17.399 33.190 135.712 182 VAL 19.391 35.317 133.215 183 ALA 18.183 38.818 134.291 184 PRO 16.245 39.234 137.590 185 LEU 12.467 39.607 137.577 186 THR 11.264 43.215 137.754 187 VAL 7.727 44.084 138.868 188 ASN 7.657 47.872 138.696 189 THR 4.169 49.214 139.259 190 GLU 2.025 47.140 136.873 191 GLY 3.807 43.766 136.576 192 ALA 2.669 40.526 138.218 193 PRO 4.232 40.250 141.738 194 GLN 5.913 36.906 140.995 195 ILE 5.780 34.326 138.208 196 LYS 5.068 30.628 138.796 197 VAL 6.947 28.422 136.288 198 TYR 5.232 25.223 135.061 199 ALA 6.197 22.459 132.643 200 ASN 3.881 20.575 130.263 201 ILE 5.834 17.587 128.927 202 ALA 5.091 14.691 126.595 203 PRO 7.266 11.560 126.050 204 THR 7.627 10.955 122.277 205 ASN 8.230 7.777 120.230 206 VAL 7.937 5.574 123.278 207 HIS 9.383 2.054 122.760 208 VAL 9.696 -0.698 125.368 209 ALA 11.297 -4.175 125.492 210 GLY 11.782 -6.958 128.024 211 GLU 8.558 -7.600 129.885 212 PHE 8.909 -8.029 133.654 213 PRO 7.096 -10.620 135.809 214 SER 4.255 -9.265 137.947 215 LYS 4.750 -8.867 141.720 216 GLU 2.062 -11.576 142.244 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C C/X X/C C C T T T 10 T/S S S S S S S/T T T T/S 20 S S S S S S C S S S 30 S S/T T T T S S S S S 40 C C T T T T/T T T T/S S 50 S S S/T T T T S S S S 60 S S S S S/S S S S S S 70 S S S S S S S S S S 80 S/P S S S S S H H H H 90 H H H H H H C C S S 100 S S S S S S S S S S 110 S S C S S S S S S S 120 S S S S S S/S S S S C 130 H H H H H 3 3 C C C 140 S S S S S S S/T T T T 150 C S S S S S S S S S/S 160 S S S C S S S S/T T T 170 T/S S S S S/S S S S S S 180 S S S/S S S S S/T T T T 190 C C S S S S S S S S 200 S S S S S/S S S S S S/S 210 S S S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S g G G 10 G g E E E E E T T E 20 E E E E S S 30 E E e S S S 40 S g G G G g T t 50 E E e G G G g S E 60 E E E E E E E t T T 70 t t T T e E E E E E 80 E S h H H H 90 H H H H H E E E E E 100 E E E E E E E E E e 110 t T T t E E E E E 120 E E E E E e t S 130 t g G G G G G G G G 140 g e E E E E t T T T 150 t e E E E E E E 160 S S S S B t T T 170 T t e E E E E E E 180 E E E E E E t T T T 190 t S E E E E E E 200 E E E E E E E E E E 210 E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 76.7 69.4 65.1 2 LYS 0.0 0.0 92.2 3 LYS 145.7 84.0 64.1 4 THR 46.5 43.5 55.5 5 THR 4.1 3.9 86.4 6 THR 33.2 31.1 68.5 7 LEU 94.9 64.2 55.0 8 LEU 111.0 75.1 59.0 9 GLU 51.8 37.4 64.4 10 ASP 1.4 1.3 80.8 11 ARG 198.6 95.1 49.7 12 ILE 76.5 53.3 70.8 13 LEU 90.2 61.0 66.1 14 THR 52.4 49.0 68.1 15 THR 87.4 81.7 65.9 16 ARG 63.0 30.2 77.2 17 ASN 97.3 80.5 54.7 18 GLY 13.4 38.4 82.4 19 HIS 5.6 3.7 90.6 20 THR 80.0 74.9 69.2 21 THR 46.5 43.5 64.2 22 SER 63.1 75.5 74.6 23 THR 56.1 52.5 70.4 24 THR 90.2 84.4 62.8 25 GLN 51.8 34.8 66.7 26 SER 83.6 100.0 54.4 27 SER 76.6 91.7 53.1 28 VAL 83.7 70.4 70.6 29 GLY 5.3 15.3 80.3 30 VAL 98.3 82.7 58.6 31 THR 72.9 68.2 62.9 32 TYR 84.5 46.7 68.0 33 GLY 32.6 93.8 49.7 34 TYR 100.4 55.5 52.2 35 ALA 33.8 46.5 73.5 36 THR 19.7 18.4 70.5 37 ALA 5.8 7.9 88.0 38 GLU 124.0 89.4 63.5 39 ASP 32.5 29.4 81.4 40 PHE 4.9 2.9 85.8 41 VAL 88.4 74.4 65.7 42 SER 35.5 42.4 76.4 43 GLY 27.5 79.1 60.5 44 PRO 20.1 16.1 83.2 45 ASN 65.8 54.5 67.5 46 THR 98.7 92.4 57.3 47 SER 16.2 19.4 79.2 48 GLY 5.5 15.9 84.2 49 LEU 31.3 21.2 85.5 50 GLU 124.6 89.9 56.0 51 THR 23.1 21.6 77.6 52 ARG 113.9 54.5 71.7 53 VAL 96.3 81.1 50.8 54 VAL 39.0 32.8 78.6 55 GLN 25.8 17.3 71.5 56 ALA 72.6 100.0 35.0 57 GLU 120.4 86.8 63.4 58 ARG 125.1 59.9 65.9 59 PHE 164.8 98.8 60.7 60 PHE 135.7 81.4 51.9 61 LYS 49.7 28.7 81.8 62 THR 54.5 51.0 60.5 63 HIS 90.0 59.9 67.8 64 LEU 146.9 99.4 34.1 65 PHE 156.3 93.7 48.8 66 ASP 74.4 67.4 64.4 67 TRP 204.9 99.9 36.3 68 VAL 71.5 60.2 73.3 69 THR 48.6 45.5 69.2 70 SER 8.0 9.6 81.9 71 ASP 93.3 84.4 59.3 72 SER 16.1 19.2 77.7 73 PHE 113.3 68.0 56.3 74 GLY 34.5 99.2 43.4 75 ARG 122.9 58.8 68.7 76 CYS 85.6 86.3 45.4 77 HIS 101.5 67.6 57.4 78 LEU 110.8 75.0 51.3 79 LEU 123.3 83.4 50.0 80 GLU 66.5 48.0 64.3 81 LEU 147.8 100.0 31.7 82 PRO 117.6 94.4 38.1 83 THR 78.8 73.7 58.9 84 ASP 0.0 0.0 84.1 85 HIS 133.6 88.9 47.8 86 LYS 2.5 1.4 89.7 87 GLY 6.1 17.5 75.3 88 VAL 72.6 61.2 54.3 89 TYR 178.6 98.7 28.9 90 GLY 30.1 86.6 66.5 91 SER 26.0 31.1 77.4 92 LEU 131.8 89.2 37.7 93 THR 79.4 74.2 56.6 94 ASP 50.8 46.0 84.1 95 SER 38.9 46.6 63.6 96 TYR 124.6 68.9 55.2 97 ALA 52.1 71.8 52.9 98 TYR 91.4 50.5 64.8 99 MET 155.0 97.2 41.1 100 ARG 208.0 99.6 50.2 101 ASN 120.9 100.0 46.5 102 GLY 34.8 100.0 72.3 103 TRP 203.6 99.3 36.1 104 ASP 100.5 91.0 53.3 105 VAL 118.3 99.6 35.1 106 GLU 131.3 94.7 48.2 107 VAL 118.7 99.9 28.5 108 THR 71.1 66.5 58.0 109 ALA 72.4 99.7 36.3 110 VAL 42.6 35.9 69.8 111 GLY 33.2 95.5 55.0 112 ASN 77.4 64.0 70.2 113 GLN 59.7 40.2 68.5 114 PHE 59.9 35.9 77.1 115 ASN 120.9 100.0 50.2 116 GLY 12.3 35.3 77.7 117 GLY 32.2 92.6 55.0 118 CYS 79.2 79.8 45.5 119 LEU 147.8 100.0 28.3 120 LEU 143.3 97.0 32.0 121 VAL 118.1 99.4 31.4 122 ALA 72.6 100.0 40.6 123 MET 159.4 100.0 23.7 124 VAL 116.2 97.8 28.1 125 PRO 99.4 79.9 46.6 126 GLU 64.7 46.7 71.1 127 LEU 131.5 89.0 46.5 128 CYS 7.3 7.3 85.6 129 SER 12.2 14.6 70.9 130 ILE 124.5 86.8 42.1 131 GLN 24.1 16.2 82.2 132 LYS 58.7 33.8 66.8 133 ARG 7.9 3.8 83.5 134 GLU 61.6 44.4 69.3 135 LEU 139.2 94.2 35.9 136 TYR 53.5 29.6 71.6 137 GLN 38.2 25.7 77.8 138 LEU 147.3 99.7 31.8 139 THR 56.4 52.8 61.7 140 LEU 36.8 24.9 80.6 141 PHE 116.0 69.5 55.3 142 PRO 114.1 91.6 42.6 143 HIS 105.5 70.3 49.8 144 GLN 130.7 87.9 57.4 145 PHE 91.1 54.6 54.1 146 ILE 143.1 99.7 46.2 147 ASN 74.4 61.5 58.5 148 PRO 118.4 95.1 61.7 149 ARG 47.1 22.5 89.1 150 THR 81.1 75.8 66.3 151 ASN 116.9 96.7 56.2 152 MET 110.6 69.4 60.0 153 THR 100.9 94.3 50.0 154 ALA 72.6 100.0 47.3 155 HIS 141.3 94.1 54.3 156 ILE 143.1 99.7 44.9 157 THR 76.7 71.7 55.5 158 VAL 118.1 99.4 36.3 159 PRO 109.5 88.0 55.9 160 PHE 161.7 97.0 65.5 161 VAL 81.4 68.5 51.7 162 GLY 26.7 76.8 71.3 163 VAL 0.0 0.0 89.9 164 ASN 32.3 26.7 83.0 165 ARG 127.7 61.1 67.8 166 TYR 180.7 99.8 44.3 167 ASP 96.6 87.4 48.8 168 GLN 56.6 38.1 72.6 169 TYR 174.9 96.6 48.3 170 LYS 64.6 37.2 76.8 171 VAL 26.8 22.5 77.9 172 HIS 90.5 60.3 75.0 173 LYS 116.4 67.1 72.1 174 PRO 123.2 99.0 59.2 175 TRP 204.7 99.9 38.2 176 THR 105.7 98.9 50.0 177 LEU 147.1 99.5 25.5 178 VAL 118.3 99.5 34.0 179 VAL 118.3 99.6 28.5 180 MET 154.2 96.8 37.5 181 VAL 118.8 100.0 47.8 182 VAL 76.9 64.7 45.4 183 ALA 32.7 45.0 55.9 184 PRO 63.2 50.7 72.0 185 LEU 147.8 100.0 46.2 186 THR 45.3 42.4 76.5 187 VAL 86.1 72.5 64.8 188 ASN 21.3 17.6 84.3 189 THR 1.1 1.0 85.1 190 GLU 30.2 21.8 78.5 191 GLY 34.8 100.0 69.1 192 ALA 48.1 66.2 64.9 193 PRO 26.1 20.9 70.8 194 GLN 82.8 55.8 56.1 195 ILE 142.8 99.5 44.4 196 LYS 87.7 50.6 75.4 197 VAL 118.8 100.0 35.1 198 TYR 83.8 46.3 71.7 199 ALA 72.6 99.9 43.6 200 ASN 104.2 86.2 54.4 201 ILE 143.0 99.6 31.9 202 ALA 72.6 100.0 46.8 203 PRO 124.5 100.0 43.3 204 THR 84.6 79.1 63.9 205 ASN 73.0 60.4 66.0 206 VAL 118.8 100.0 43.7 207 HIS 131.7 87.7 45.0 208 VAL 117.6 99.0 37.8 209 ALA 67.4 92.8 42.5 210 GLY 7.9 22.6 67.5 211 GLU 29.6 21.3 80.0 212 PHE 103.1 61.8 65.1 213 PRO 16.7 13.4 81.8 214 SER 33.6 40.2 74.6 215 LYS 18.1 10.5 87.3 216 GLU 4.9 3.5 83.0