Protein Data Bank File : 1fjgc Title : RIBOSOME 08-AUG-00 1FJG Number of Amino Acid Residues : 206 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG 10 LEU GLY ILE THR ARG ASP TRP GLU SER ARG 20 TRP TYR ALA GLY LYS LYS GLN TYR ARG HIS 30 LEU LEU LEU GLU ASP GLN ARG ILE ARG GLY 40 LEU LEU GLU LYS GLU LEU TYR SER ALA GLY 50 LEU ALA ARG VAL ASP ILE GLU ARG ALA ALA 60 ASP ASN VAL ALA VAL THR VAL HIS VAL ALA 70 LYS PRO GLY VAL VAL ILE GLY ARG GLY GLY 80 GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU 90 ALA LYS LEU THR GLY LYS ASN VAL ALA LEU 100 ASN VAL GLN GLU VAL GLN ASN PRO ASN LEU 110 SER ALA PRO LEU VAL ALA GLN ARG VAL ALA 120 GLU GLN ILE GLU ARG ARG PHE ALA VAL ARG 130 ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL 140 MET GLU SER GLY ALA LYS GLY ALA LYS VAL 150 ILE VAL SER GLY ARG ILE GLY GLY ALA GLU 160 GLN ALA ARG THR GLU TRP ALA ALA GLN GLY 170 ARG VAL PRO LEU HIS THR LEU ARG ALA ASN 180 ILE ASP TYR GLY PHE ALA LEU ALA ARG THR 190 THR TYR GLY VAL LEU GLY VAL LYS ALA TYR 200 ILE PHE LEU GLY GLU VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 94.4 -178.8 2 ASN -163.3 -171.6 179.1 29.5 174.9 3 LYS 78.0 111.5 179.0 -67.4 -66.7 -172.9 -175.6 4 ILE -76.0 156.0 177.1 35.3 66.3 5 HIS -56.8 130.1 -179.4 -171.8 100.0 6 PRO -67.3 -22.9 178.6 29.7 -39.6 7 ILE -79.1 -61.8 179.4 -75.9 175.4 8 GLY -47.6 -32.2 -179.1 9 PHE -67.2 -21.7 -179.8 -178.1 49.5 10 ARG -128.1 31.8 178.4 39.1 -151.6 118.5 -154.5 11 LEU -60.1 -47.7 178.9 -85.2 166.9 12 GLY -55.1 -48.0 -179.3 13 ILE -91.4 -161.5 -179.4 -25.4 -58.3 14 THR -27.6 66.2 -180.0 67.8 15 ARG 168.1 101.8 179.7 -167.3 72.1 -177.8 -168.6 16 ASP -79.2 165.3 179.9 -65.5 -53.8 17 TRP -75.4 172.3 179.0 -77.9 -114.4 18 GLU -106.9 12.6 179.0 -68.1 -172.0 56.2 19 SER -160.0 108.5 -179.7 -86.9 20 ARG -125.0 96.8 178.8 30.5 -153.9 173.0 -162.1 21 TRP -144.5 136.8 -178.7 34.3 -94.2 22 TYR -42.5 164.1 -179.1 63.9 66.6 23 ALA -23.5 -162.9 178.5 24 GLY 128.4 71.8 -179.1 25 LYS -75.1 -0.7 179.4 -63.9 -162.4 172.5 -173.9 26 LYS -121.5 -11.8 -179.0 -76.5 -168.5 174.0 -178.8 27 GLN -121.5 -11.3 -179.6 -57.7 175.4 57.3 28 TYR -47.1 -49.0 -179.8 -156.7 101.3 29 ARG -71.7 12.1 179.9 77.8 166.8 175.8 -53.4 30 HIS -120.7 -42.6 178.6 -62.2 -57.8 31 LEU -68.7 -38.2 179.7 -58.8 -162.9 32 LEU -61.4 -55.2 179.6 -167.1 176.1 33 LEU -50.9 -41.2 180.0 -152.1 -174.7 34 GLU -62.0 -57.7 179.1 -165.2 169.3 -57.0 35 ASP -47.3 -36.3 179.6 -74.3 -174.1 36 GLN -69.4 -64.1 179.0 -116.6 36.6 48.7 37 ARG -37.6 -49.4 179.1 -72.6 -86.2 -177.5 51.4 38 ILE -49.6 -76.1 -180.0 -70.5 173.5 39 ARG -40.6 -30.1 179.2 -59.3 -149.4 171.3 63.7 40 GLY -49.6 -65.6 180.0 41 LEU -59.0 -61.8 -178.9 -63.7 -177.8 42 LEU -43.1 -33.2 179.1 -48.3 -171.0 43 GLU -94.5 44.1 -179.0 -67.1 179.2 52.1 44 LYS -158.9 -82.1 179.9 -107.2 -67.6 178.5 -177.3 45 GLU -69.4 36.2 180.0 -47.9 -71.6 -64.6 46 LEU -164.4 6.6 -179.9 -154.4 58.4 47 TYR -54.7 -61.7 179.9 176.1 38.6 48 SER -68.8 83.1 -179.8 55.2 49 ALA 177.1 -15.3 -180.0 50 GLY 90.6 48.6 178.2 51 LEU -56.2 107.1 -178.3 57.4 -178.1 52 ALA -117.9 8.9 179.6 53 ARG 162.2 127.0 179.6 -164.6 -165.1 -171.6 -158.9 54 VAL -116.1 92.0 178.7 173.5 55 ASP -74.0 160.7 -179.7 -68.1 53.5 56 ILE -155.5 126.1 178.1 -66.1 -176.2 57 GLU -120.8 167.1 -179.8 -60.5 -169.2 -52.9 58 ARG -152.0 169.5 179.4 -73.7 167.2 175.9 -69.0 59 ALA 178.7 77.4 179.4 60 ALA 59.7 93.5 179.9 61 ASP 46.0 45.6 179.1 -75.1 -60.3 62 ASN -150.4 106.2 -179.1 -72.4 -54.7 63 VAL -103.9 140.4 -179.6 -145.0 64 ALA -87.8 -71.7 -179.8 65 VAL 68.8 110.1 -179.8 169.6 66 THR -125.9 91.3 -179.8 -53.2 67 VAL -76.5 111.7 178.4 172.0 68 HIS -87.5 132.3 -178.4 -59.1 -129.3 69 VAL -144.6 156.8 179.6 -78.1 70 ALA -86.6 -24.1 179.8 71 LYS -131.1 72.1 -179.9 -58.2 -170.7 66.0 179.5 72 PRO -55.2 -34.4 179.5 27.9 -42.3 73 GLY -48.8 -41.3 -179.2 74 VAL -65.9 -28.0 179.6 -155.7 75 VAL -78.1 -58.2 -179.7 178.1 76 ILE -50.7 -60.6 -180.0 -59.3 -59.5 77 GLY 106.8 172.9 -179.9 78 ARG -52.0 107.9 -179.6 -73.2 -179.7 175.6 175.2 79 GLY 71.7 -25.5 -180.0 80 GLY 122.8 49.6 -179.4 81 GLU -105.6 -27.7 -179.7 64.1 73.9 55.8 82 ARG -72.6 -46.3 179.4 177.2 176.8 -165.1 162.4 83 ILE -55.0 -18.6 178.5 177.4 -179.1 84 ARG -84.8 -37.0 179.1 138.2 62.9 -178.0 170.9 85 VAL -68.0 -42.6 179.1 -177.5 86 LEU -56.1 -73.7 -179.7 -63.1 -179.1 87 ARG -31.2 -50.2 180.0 -91.2 152.6 174.5 161.7 88 GLU -69.8 -62.0 -180.0 171.9 -175.9 51.6 89 GLU -52.9 -23.6 -179.8 -168.5 -75.9 167.4 90 LEU -75.4 -44.9 179.5 168.0 158.8 91 ALA -72.3 7.3 178.4 92 LYS -89.6 -17.3 178.2 -55.9 -56.8 176.4 -174.3 93 LEU -81.2 -48.7 -179.0 -84.5 171.8 94 THR -136.8 139.6 177.7 65.4 95 GLY -60.5 -91.1 177.1 96 LYS 51.4 -36.6 -177.5 -63.8 -79.9 -166.9 169.9 97 ASN 64.9 78.1 -177.6 -178.4 -59.4 98 VAL -104.2 139.3 179.3 31.6 99 ALA -67.6 -153.7 179.3 100 LEU 178.4 168.6 -179.3 -140.5 -159.9 101 ASN -163.8 169.2 179.0 -69.2 -69.6 102 VAL -151.3 83.8 178.3 176.9 103 GLN -89.8 136.1 -178.4 178.8 -173.2 -58.1 104 GLU -88.9 158.3 179.7 -172.2 -176.2 61.6 105 VAL -93.0 102.0 179.8 -178.1 106 GLN -70.0 86.4 179.6 -57.9 -56.4 -61.7 107 ASN 87.8 89.1 180.0 -179.8 50.8 108 PRO -66.6 -4.4 179.3 31.8 -44.0 109 ASN -75.3 -15.5 178.5 -81.7 52.2 110 LEU -109.8 18.5 178.6 -68.4 -167.8 111 SER -114.4 99.0 179.8 177.5 112 ALA -47.1 -51.0 -179.6 113 PRO -50.9 -40.6 -179.4 -27.4 41.8 114 LEU -71.7 -50.8 178.9 -70.5 173.3 115 VAL -51.1 -38.6 179.2 178.1 116 ALA -59.7 -49.7 -179.4 117 GLN -57.3 -41.7 179.8 -69.0 176.4 -75.3 118 ARG -61.0 -51.3 -179.4 172.6 48.9 178.8 164.3 119 VAL -64.9 -40.0 179.8 176.4 120 ALA -65.0 -35.1 179.7 121 GLU -58.3 -62.2 179.3 -102.6 -173.0 53.2 122 GLN -51.1 -51.8 179.7 -53.4 -172.4 57.5 123 ILE -49.5 -48.6 179.8 -64.0 179.1 124 GLU -55.4 -35.6 178.8 -65.0 175.9 -56.2 125 ARG -70.0 -69.3 177.5 -62.5 -171.7 -154.4 170.1 126 ARG 154.7 31.2 179.8 -124.2 150.5 -62.4 -159.7 127 PHE -76.0 167.2 179.1 -67.7 48.8 128 ALA -72.1 110.5 -178.6 129 VAL -47.7 -60.7 -178.9 176.1 130 ARG -44.7 -45.0 179.4 -174.4 163.9 -60.1 -173.9 131 ARG -59.8 -65.3 -180.0 164.7 -177.1 -57.5 -59.3 132 ALA -36.6 -49.2 -179.5 133 ILE -63.1 -55.1 -179.5 -50.5 178.9 134 LYS -50.6 -49.0 -179.5 -66.8 164.8 -178.2 169.4 135 GLN -58.5 -56.0 179.3 -54.1 -174.3 -46.4 136 ALA -53.9 -48.8 179.3 137 VAL -53.2 -43.0 179.0 -177.1 138 GLN -59.2 -67.1 179.8 -105.8 -59.9 174.0 139 ARG -37.4 -64.6 -179.5 -54.1 157.6 -165.4 162.2 140 VAL -48.2 -40.1 -179.8 177.8 141 MET -77.5 -40.8 -179.3 -151.6 60.8 -92.6 142 GLU -54.9 -40.4 -179.6 -166.0 170.3 60.3 143 SER -98.7 56.6 179.9 59.2 144 GLY 92.0 -130.6 179.1 145 ALA 60.6 148.0 179.1 146 LYS -104.5 -5.5 179.6 -69.4 -156.1 -67.5 -172.7 147 GLY -179.9 156.9 179.9 148 ALA -156.9 155.2 -179.5 149 LYS -158.1 134.1 -178.6 174.9 176.5 175.0 177.7 150 VAL -127.3 142.9 -178.0 175.4 151 ILE -137.3 112.3 178.3 -60.4 163.8 152 VAL -103.6 138.7 -177.7 175.7 153 SER -102.1 -104.0 -179.4 61.8 154 GLY 11.8 -158.4 179.7 155 ARG -79.7 64.8 -179.0 -57.9 174.3 54.7 169.3 156 ILE -41.4 120.5 179.1 -66.1 178.7 157 GLY 75.1 20.4 179.8 158 GLY 76.8 4.2 179.5 159 ALA -56.3 157.9 -180.0 160 GLU -84.5 -28.9 -179.6 -173.5 172.9 179.2 161 GLN -98.0 105.3 -179.6 -167.5 70.9 62.5 162 ALA -51.3 143.7 -179.3 163 ARG -138.4 -159.9 -179.4 -37.5 -171.1 -66.1 87.6 164 THR -160.6 110.8 179.6 -61.1 165 GLU -86.7 137.8 -177.0 -74.2 -56.5 -61.1 166 TRP -87.5 -124.4 178.9 -129.0 76.0 167 ALA 92.4 119.6 179.2 168 ALA -165.2 151.8 179.9 169 GLN -135.9 162.2 -179.6 -75.9 -178.6 57.1 170 GLY 57.6 -145.7 -179.9 171 ARG -109.9 143.2 177.9 -48.6 -167.9 -26.5 179.5 172 VAL -143.3 68.0 -179.3 -173.7 173 PRO -72.9 73.8 -179.3 35.4 -44.4 174 LEU -52.2 -23.3 -179.3 -54.6 -171.7 175 HIS -82.8 -42.7 180.0 -87.6 59.9 176 THR -60.3 98.3 -178.4 -178.0 177 LEU -70.3 68.6 -178.9 178.5 67.1 178 ARG 170.6 -11.2 -179.6 137.5 -74.7 -89.3 -73.4 179 ALA -51.3 -39.2 -177.8 180 ASN 76.6 81.4 -178.7 171.9 27.9 181 ILE -115.1 119.2 179.3 -58.1 -176.0 182 ASP -78.1 132.7 -179.8 -168.0 -174.6 183 TYR -112.3 148.2 179.3 175.4 74.2 184 GLY -155.8 142.4 179.7 185 PHE -129.6 147.6 179.3 165.6 70.7 186 ALA -143.1 134.8 178.9 187 LEU -74.1 -159.4 179.1 -129.5 -93.0 188 ALA 172.7 83.1 179.2 189 ARG -70.1 140.1 -175.8 -62.8 -179.9 177.2 178.6 190 THR -142.0 160.8 179.4 -83.9 191 THR -56.4 -20.8 -177.8 -37.7 192 TYR -124.2 19.2 -179.9 56.2 70.1 193 GLY 122.3 169.5 -178.6 194 VAL -78.5 160.7 179.3 -169.5 195 LEU -144.8 120.6 179.7 -83.1 -79.6 196 GLY -83.3 149.8 179.8 197 VAL -135.8 115.2 -178.3 -166.9 198 LYS -110.2 138.4 -178.9 -60.8 177.1 -174.3 178.6 199 ALA -128.2 131.1 179.7 200 TYR -121.8 126.9 179.2 -66.5 61.8 201 ILE -127.0 119.4 -179.3 -62.0 176.2 202 PHE -93.3 123.0 179.8 -178.9 36.7 203 LEU -121.7 135.4 179.1 -34.5 158.3 204 GLY 31.2 -145.5 -179.6 205 GLU -159.0 -76.9 -177.5 -168.5 172.7 179.3 206 VAL -38.0 -22.5 0.0 -171.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 205.961 127.908 8.151 2 ASN 205.993 131.657 7.576 3 LYS 204.871 135.046 8.973 4 ILE 207.183 137.202 11.177 5 HIS 206.135 138.012 14.699 6 PRO 204.035 141.123 14.106 7 ILE 205.612 142.811 17.106 8 GLY 209.252 141.956 16.484 9 PHE 208.626 143.070 12.926 10 ARG 207.956 146.633 14.002 11 LEU 210.087 147.359 17.049 12 GLY 211.975 150.111 15.297 13 ILE 208.667 151.603 14.234 14 THR 205.245 151.651 15.920 15 ARG 206.211 149.418 18.884 16 ASP 208.516 149.912 21.901 17 TRP 210.331 147.149 23.775 18 GLU 209.154 145.563 27.034 19 SER 212.582 146.169 28.572 20 ARG 214.416 149.429 27.990 21 TRP 217.752 149.847 29.759 22 TYR 221.206 151.188 28.803 23 ALA 224.307 149.280 27.641 24 GLY 226.140 146.501 29.506 25 LYS 228.378 143.951 27.771 26 LYS 229.274 142.111 30.992 27 GLN 225.913 142.211 32.731 28 TYR 223.436 142.033 29.862 29 ARG 223.169 138.278 30.379 30 HIS 222.377 139.051 34.027 31 LEU 219.916 141.893 33.855 32 LEU 218.124 139.878 31.176 33 LEU 217.977 136.743 33.288 34 GLU 216.643 139.052 35.993 35 ASP 214.039 140.689 33.752 36 GLN 213.079 137.118 32.966 37 ARG 213.055 135.878 36.563 38 ILE 210.863 138.906 37.217 39 ARG 208.273 138.222 34.509 40 GLY 208.350 134.684 35.834 41 LEU 206.413 135.549 38.983 42 LEU 204.400 138.405 37.544 43 GLU 203.130 135.980 34.885 44 LYS 201.855 133.721 37.669 45 GLU 201.092 135.418 40.965 46 LEU 199.294 138.013 38.853 47 TYR 197.396 136.072 36.149 48 SER 193.873 136.718 37.418 49 ALA 193.967 140.474 36.856 50 GLY 194.729 140.615 33.181 51 LEU 198.519 140.629 33.056 52 ALA 198.826 142.270 29.639 53 ARG 202.414 143.553 29.619 54 VAL 205.294 143.781 32.065 55 ASP 207.541 146.735 31.180 56 ILE 210.921 147.094 32.880 57 GLU 213.460 149.921 33.176 58 ARG 216.772 150.141 35.054 59 ALA 219.615 152.309 36.352 60 ALA 222.202 150.738 38.681 61 ASP 220.544 148.343 41.135 62 ASN 217.193 150.030 40.530 63 VAL 214.396 148.227 38.732 64 ALA 211.144 149.917 37.707 65 VAL 208.641 147.233 36.626 66 THR 205.260 148.394 35.372 67 VAL 202.636 145.671 35.423 68 HIS 199.740 146.652 33.156 69 VAL 196.451 145.019 34.104 70 ALA 192.724 145.118 33.375 71 LYS 191.871 144.503 37.054 72 PRO 194.494 146.349 39.205 73 GLY 192.376 145.897 42.289 74 VAL 193.422 142.262 42.158 75 VAL 197.053 143.375 42.007 76 ILE 196.981 146.018 44.743 77 GLY 195.007 143.962 47.246 78 ARG 192.684 144.692 50.168 79 GLY 193.294 148.361 50.866 80 GLY 196.701 147.792 49.323 81 GLU 198.436 144.946 51.115 82 ARG 199.245 142.565 48.248 83 ILE 201.171 145.057 46.127 84 ARG 203.193 145.132 49.350 85 VAL 203.521 141.338 49.429 86 LEU 204.680 141.375 45.811 87 ARG 207.350 144.036 46.250 88 GLU 208.846 142.126 49.189 89 GLU 208.511 138.536 47.968 90 LEU 209.828 140.076 44.746 91 ALA 213.048 141.524 46.154 92 LYS 213.636 137.945 47.318 93 LEU 214.451 137.124 43.700 94 THR 216.876 140.007 43.420 95 GLY 218.240 142.400 46.002 96 LYS 218.335 145.510 43.828 97 ASN 215.577 147.232 45.847 98 VAL 213.080 147.411 43.007 99 ALA 209.993 149.584 42.647 100 LEU 206.694 148.415 41.147 101 ASN 203.545 149.829 39.601 102 VAL 200.016 149.079 38.493 103 GLN 198.772 150.973 35.466 104 GLU 195.348 149.759 34.328 105 VAL 194.223 148.631 30.881 106 GLN 191.615 151.082 29.638 107 ASN 189.472 148.495 27.816 108 PRO 190.957 144.967 27.556 109 ASN 188.904 144.420 24.408 110 LEU 191.618 146.288 22.542 111 SER 194.428 144.343 24.200 112 ALA 195.465 141.424 22.004 113 PRO 197.407 139.734 24.825 114 LEU 194.227 139.735 26.883 115 VAL 191.864 138.663 24.104 116 ALA 194.114 135.662 23.513 117 GLN 193.745 134.784 27.186 118 ARG 189.952 135.075 27.149 119 VAL 189.603 132.701 24.217 120 ALA 192.222 130.360 25.558 121 GLU 190.258 130.543 28.819 122 GLN 186.898 129.469 27.422 123 ILE 188.578 126.719 25.404 124 GLU 190.189 125.462 28.623 125 ARG 186.683 125.331 30.125 126 ARG 184.976 123.702 27.142 127 PHE 183.246 126.317 24.990 128 ALA 182.555 126.089 21.252 129 VAL 185.866 127.193 19.742 130 ARG 184.337 128.603 16.580 131 ARG 181.945 130.612 18.770 132 ALA 184.565 131.877 21.181 133 ILE 186.498 133.158 18.206 134 LYS 183.568 134.824 16.428 135 GLN 182.583 136.570 19.675 136 ALA 186.084 137.784 20.579 137 VAL 186.596 139.035 17.050 138 GLN 183.325 140.859 17.647 139 ARG 184.161 142.350 21.057 140 VAL 187.535 143.621 19.805 141 MET 185.751 144.962 16.767 142 GLU 182.770 145.950 18.917 143 SER 184.896 148.255 21.068 144 GLY 186.500 150.360 18.341 145 ALA 189.444 148.831 16.472 146 LYS 189.942 149.054 12.730 147 GLY 190.407 145.313 12.359 148 ALA 190.814 142.123 14.373 149 LYS 191.750 138.461 13.870 150 VAL 191.854 135.347 16.077 151 ILE 193.390 131.938 15.402 152 VAL 192.893 128.798 17.476 153 SER 194.992 125.824 16.421 154 GLY 195.162 122.411 18.075 155 ARG 192.647 119.550 18.265 156 ILE 189.662 121.865 18.081 157 GLY 186.844 120.378 20.125 158 GLY 188.892 117.447 21.358 159 ALA 188.901 116.134 17.806 160 GLU 191.635 113.667 16.861 161 GLN 192.621 115.477 13.661 162 ALA 194.150 118.854 14.521 163 ARG 192.653 121.795 12.616 164 THR 192.730 125.574 12.791 165 GLU 189.748 127.908 13.211 166 TRP 189.984 131.335 11.577 167 ALA 187.829 134.485 12.035 168 ALA 188.653 138.121 11.365 169 GLN 187.018 141.512 10.675 170 GLY 188.073 144.874 9.280 171 ARG 191.717 145.187 8.266 172 VAL 194.715 143.335 9.691 173 PRO 197.504 144.378 7.266 174 LEU 200.463 142.336 8.559 175 HIS 202.639 143.599 5.692 176 THR 202.075 147.331 6.105 177 LEU 205.026 147.971 8.401 178 ARG 203.421 150.790 10.361 179 ALA 199.816 149.726 10.879 180 ASN 200.376 149.208 14.618 181 ILE 198.850 145.843 15.202 182 ASP 198.764 144.460 18.719 183 TYR 199.693 140.809 18.843 184 GLY 198.915 138.283 21.524 185 PHE 199.244 134.547 22.019 186 ALA 197.722 132.253 24.599 187 LEU 198.352 128.603 25.375 188 ALA 195.552 126.273 26.478 189 ARG 196.296 123.118 28.412 190 THR 193.485 120.624 27.937 191 THR 192.394 117.145 28.963 192 TYR 193.474 116.179 25.457 193 GLY 196.416 118.422 24.536 194 VAL 197.425 122.011 23.828 195 LEU 195.744 124.647 21.630 196 GLY 197.523 127.815 20.538 197 VAL 195.499 131.004 20.453 198 LYS 196.530 134.018 18.438 199 ALA 194.994 137.478 18.550 200 TYR 195.584 140.382 16.184 201 ILE 194.212 143.830 16.858 202 PHE 194.513 146.625 14.382 203 LEU 194.541 150.116 15.904 204 GLY 194.866 153.301 13.869 205 GLU 197.840 153.328 11.514 206 VAL 200.391 156.147 11.114 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S/H H H H H H 10 H/T T T T/S S S S S/S S S 20 S S S/S S S S H H H H 30 H H H H H H H H H H 40 H H H H H H H/T T T T 50 C S S S S S S S T T 60 T T/S S S S S S S S S 70 H H H H H H H/T T T T 80 H H H H H H H H H H 90 H H H H C C S S S S 100 S/S S S S S S C C C C 110 H H H H H H H H H H 120 H H H H H H C H H H 130 H H H H H H H H H H 140 H H H H C C S S S S 150 S S S S S/T T T T C S 160 S S S S S S S S S S/S 170 S S S S C C C C S S 180 S S S S S S S S S S/T 190 T T T/S S S S S S S S 200 S S S S/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T g G G G 10 g S S S S B 20 t T T h H H H 30 H H H H H H H H H H 40 H H h T T T t T T t 50 E E E B B S S 60 S B E E E E S 70 h H H H H H h S S S 80 h H H H H H H H H H 90 h T T t S 100 e E E E e S g G G G 110 h H H H H H H H H H 120 H H H H H h t h H H 130 H H H H H H H H H H 140 H H h t e E E E E 150 E E e T g G G G g S 160 S B e E E E 170 e t T T t T T t e 180 E E E E E E t 190 T T t e E E E E 200 E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 92.9 2 ASN 14.2 11.8 84.9 3 LYS 69.5 40.1 73.7 4 ILE 54.3 37.8 70.6 5 HIS 65.4 43.5 58.6 6 PRO 119.1 95.7 43.2 7 ILE 113.9 79.4 62.4 8 GLY 13.8 39.7 52.6 9 PHE 105.7 63.4 60.8 10 ARG 206.9 99.0 49.6 11 LEU 107.5 72.8 55.5 12 GLY 2.4 6.8 66.2 13 ILE 55.1 38.4 66.1 14 THR 74.3 69.5 54.1 15 ARG 160.1 76.7 64.1 16 ASP 29.9 27.0 81.2 17 TRP 74.4 36.3 71.5 18 GLU 74.1 53.5 76.2 19 SER 61.7 73.8 66.5 20 ARG 117.5 56.3 77.0 21 TRP 189.1 92.2 52.2 22 TYR 53.8 29.7 73.4 23 ALA 0.0 0.0 79.4 24 GLY 15.6 44.9 71.2 25 LYS 0.0 0.0 88.9 26 LYS 4.8 2.8 88.7 27 GLN 43.4 29.2 66.3 28 TYR 60.2 33.2 69.4 29 ARG 55.1 26.4 78.4 30 HIS 66.9 44.5 74.1 31 LEU 128.2 86.7 54.6 32 LEU 67.4 45.6 60.7 33 LEU 68.3 46.2 73.3 34 GLU 123.3 88.9 45.7 35 ASP 107.6 97.3 55.7 36 GLN 58.4 39.3 67.5 37 ARG 88.9 42.6 61.3 38 ILE 138.3 96.3 33.4 39 ARG 178.3 85.4 59.7 40 GLY 0.1 0.2 80.4 41 LEU 102.5 69.3 55.9 42 LEU 143.0 96.7 24.9 43 GLU 62.7 45.2 61.1 44 LYS 33.6 19.4 83.7 45 GLU 43.8 31.6 68.9 46 LEU 144.0 97.4 38.2 47 TYR 84.9 46.9 72.6 48 SER 4.9 5.9 75.4 49 ALA 72.1 99.4 46.7 50 GLY 24.9 71.6 55.1 51 LEU 131.4 88.9 55.7 52 ALA 68.2 94.0 55.8 53 ARG 144.5 69.2 70.8 54 VAL 114.8 96.6 40.4 55 ASP 104.5 94.5 66.1 56 ILE 143.0 99.6 47.8 57 GLU 52.6 38.0 68.9 58 ARG 202.9 97.1 43.4 59 ALA 23.3 32.1 68.7 60 ALA 5.4 7.5 89.5 61 ASP 27.4 24.8 76.4 62 ASN 41.9 34.7 81.0 63 VAL 118.6 99.9 46.0 64 ALA 46.3 63.8 64.3 65 VAL 118.8 100.0 30.6 66 THR 77.2 72.2 60.4 67 VAL 118.6 99.8 29.7 68 HIS 123.5 82.2 59.7 69 VAL 118.8 100.0 40.6 70 ALA 62.8 86.5 41.5 71 LYS 40.7 23.4 70.9 72 PRO 96.7 77.7 53.7 73 GLY 0.0 0.0 68.9 74 VAL 69.4 58.5 69.2 75 VAL 118.7 99.9 28.4 76 ILE 90.5 63.1 51.9 77 GLY 25.1 72.2 71.6 78 ARG 0.0 0.0 89.6 79 GLY 0.0 0.0 85.2 80 GLY 28.3 81.4 59.8 81 GLU 51.5 37.2 64.7 82 ARG 136.7 65.4 62.1 83 ILE 120.6 84.0 47.7 84 ARG 66.3 31.7 75.7 85 VAL 46.7 39.3 71.5 86 LEU 131.3 88.8 43.2 87 ARG 118.7 56.8 61.5 88 GLU 69.7 50.3 76.9 89 GLU 57.3 41.4 58.0 90 LEU 142.1 96.1 40.6 91 ALA 46.5 64.1 73.6 92 LYS 57.5 33.1 78.2 93 LEU 107.3 72.6 54.8 94 THR 87.7 82.0 55.4 95 GLY 0.0 0.0 81.5 96 LYS 141.8 81.8 65.5 97 ASN 0.0 0.0 84.3 98 VAL 117.5 98.9 50.8 99 ALA 22.5 31.0 79.6 100 LEU 147.7 99.9 41.2 101 ASN 57.0 47.2 67.1 102 VAL 115.4 97.1 39.2 103 GLN 47.6 32.0 77.5 104 GLU 79.1 57.1 70.3 105 VAL 96.8 81.5 52.8 106 GLN 26.4 17.7 84.6 107 ASN 72.9 60.3 59.6 108 PRO 74.8 60.1 61.0 109 ASN 78.3 64.8 58.0 110 LEU 104.0 70.4 64.8 111 SER 72.2 86.3 46.5 112 ALA 72.6 100.0 45.3 113 PRO 93.3 74.9 70.2 114 LEU 134.4 90.9 49.4 115 VAL 109.5 92.2 41.6 116 ALA 72.5 99.9 52.6 117 GLN 117.2 78.8 53.5 118 ARG 126.6 60.6 76.4 119 VAL 118.8 100.0 37.7 120 ALA 67.1 92.4 49.8 121 GLU 81.8 59.0 76.4 122 GLN 146.6 98.7 52.4 123 ILE 141.0 98.2 38.9 124 GLU 80.7 58.2 72.1 125 ARG 92.0 44.0 74.9 126 ARG 31.5 15.1 89.6 127 PHE 96.0 57.6 69.4 128 ALA 22.4 30.8 76.8 129 VAL 114.9 96.7 32.8 130 ARG 79.0 37.8 75.7 131 ARG 81.6 39.1 72.8 132 ALA 72.6 100.0 51.6 133 ILE 142.0 99.0 39.4 134 LYS 57.9 33.4 65.7 135 GLN 80.8 54.4 71.5 136 ALA 72.6 100.0 47.4 137 VAL 116.4 98.0 45.7 138 GLN 66.2 44.5 75.2 139 ARG 153.9 73.7 66.4 140 VAL 117.4 98.8 37.1 141 MET 132.1 82.9 65.2 142 GLU 33.0 23.8 81.4 143 SER 53.6 64.1 72.5 144 GLY 0.0 0.0 80.3 145 ALA 69.8 96.1 48.3 146 LYS 83.4 48.1 67.0 147 GLY 34.8 100.0 48.7 148 ALA 72.0 99.2 44.7 149 LYS 140.2 80.9 35.7 150 VAL 117.0 98.5 34.9 151 ILE 112.5 78.4 49.7 152 VAL 118.8 100.0 28.0 153 SER 44.8 53.6 64.0 154 GLY 22.4 64.3 58.4 155 ARG 124.7 59.7 63.0 156 ILE 134.7 93.8 52.1 157 GLY 1.0 3.0 75.5 158 GLY 26.9 77.3 59.9 159 ALA 34.4 47.4 82.2 160 GLU 4.3 3.1 90.1 161 GLN 3.8 2.5 89.2 162 ALA 27.5 37.9 69.7 163 ARG 111.3 53.3 73.3 164 THR 50.4 47.2 62.4 165 GLU 123.3 89.0 58.6 166 TRP 57.4 28.0 75.8 167 ALA 49.7 68.4 46.9 168 ALA 63.2 87.1 42.0 169 GLN 81.4 54.8 65.1 170 GLY 9.8 28.0 66.6 171 ARG 79.9 38.3 70.5 172 VAL 110.2 92.8 38.6 173 PRO 91.0 73.1 52.1 174 LEU 132.6 89.7 52.9 175 HIS 6.3 4.2 87.3 176 THR 68.9 64.5 64.1 177 LEU 78.3 53.0 62.3 178 ARG 110.5 52.9 66.1 179 ALA 72.6 100.0 43.3 180 ASN 77.4 64.1 64.0 181 ILE 143.5 100.0 46.6 182 ASP 95.2 86.1 61.6 183 TYR 158.4 87.5 44.8 184 GLY 30.2 86.9 48.5 185 PHE 94.0 56.4 57.2 186 ALA 63.7 87.8 48.7 187 LEU 78.3 53.0 58.4 188 ALA 72.6 99.9 48.3 189 ARG 17.4 8.3 82.8 190 THR 93.3 87.3 57.7 191 THR 9.8 9.2 79.3 192 TYR 121.4 67.1 62.9 193 GLY 6.4 18.4 70.4 194 VAL 52.8 44.5 61.6 195 LEU 147.0 99.4 47.4 196 GLY 24.9 71.4 55.8 197 VAL 118.8 100.0 38.2 198 LYS 88.0 50.7 64.5 199 ALA 72.1 99.3 42.4 200 TYR 165.0 91.2 31.9 201 ILE 142.5 99.3 39.7 202 PHE 166.7 100.0 43.8 203 LEU 99.7 67.5 63.1 204 GLY 6.7 19.3 71.7 205 GLU 98.9 71.3 74.0 206 VAL 0.0 0.0 79.7