Protein Data Bank File : 1fg9c Title : IMMUNE SYSTEM 28-JUL-00 1FG9 Number of Amino Acid Residues : 210 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 VAL PRO THR PRO THR ASN VAL THR ILE GLU 10 SER TYR ASN MET ASN PRO ILE VAL TYR TRP 20 GLU TYR GLN ILE MET PRO GLN VAL PRO VAL 30 PHE THR VAL GLU VAL LYS ASN TYR GLY VAL 40 LYS ASN SER GLU TRP ILE ASP ALA CYS ILE 50 ASN ILE SER HIS HIS TYR CYS ASN ILE SER 60 ASP HIS VAL GLY ASP PRO SER ASN SER LEU 70 TRP VAL ARG VAL LYS ALA ARG VAL GLY GLN 80 LYS GLU SER ALA TYR ALA LYS SER GLU GLU 90 PHE ALA VAL CYS ARG ASP GLY LYS ILE GLY 100 PRO PRO LYS LEU ASP ILE ARG LYS GLU GLU 110 LYS GLN ILE MET ILE ASP ILE PHE HIS PRO 120 SER VAL PHE VAL ASN GLY ASP GLU GLN GLU 130 ASP PRO GLU THR THR CYS TYR ILE ARG VAL 140 TYR ASN VAL TYR VAL ARG MET ASN GLY SER 150 GLU ILE GLN TYR LYS ILE LEU THR GLN LYS 160 GLU ASP ASP CYS ASP GLU ILE GLN CYS GLN 170 LEU ALA ILE PRO VAL SER SER LEU ASN SER 180 GLN TYR CYS VAL SER ALA GLU GLY VAL LEU 190 HIS VAL TRP GLY VAL THR THR GLU LYS SER 200 LYS GLU VAL CYS ILE THR ILE PHE ASN SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 VAL 0.0 177.8 179.7 0.0 2 PRO -58.9 167.9 -177.2 -36.3 46.7 3 THR -106.3 141.1 179.9 42.2 4 PRO -57.9 152.9 -179.2 -34.6 46.7 5 THR -130.2 156.7 178.7 148.7 6 ASN 50.3 53.3 178.1 -65.0 0.2 7 VAL -63.6 144.8 -175.7 -177.4 8 THR -158.3 127.5 176.2 -89.1 9 ILE -100.2 155.1 179.3 -50.1 -176.2 10 GLU -153.5 145.1 -179.9 -77.3 -175.6 17.9 11 SER -140.8 150.1 178.0 -176.2 12 TYR -147.9 130.8 -177.9 -177.4 95.6 13 ASN 49.9 35.2 176.8 -90.0 -37.6 14 MET 62.2 72.0 176.1 -77.0 -172.7 -149.0 15 ASN 179.7 99.2 -179.6 66.3 83.6 16 PRO -87.1 149.9 -180.0 37.8 -38.5 17 ILE -128.0 128.8 179.2 -44.2 -76.4 18 VAL -81.7 134.1 -179.4 -154.6 19 TYR -125.6 141.3 179.2 -63.2 -8.2 20 TRP -153.1 142.5 177.9 69.0 95.6 21 GLU -83.2 -174.8 177.7 -47.3 -67.3 -109.0 22 TYR 178.2 142.7 179.1 -156.4 21.9 23 GLN -75.8 157.7 -179.9 36.9 64.6 -145.1 24 ILE -77.8 115.0 -179.7 -43.7 173.0 25 MET -91.7 146.8 179.7 -85.3 -147.9 91.4 26 PRO -38.1 -62.9 177.0 -39.1 43.9 27 GLN -98.8 144.9 176.9 -43.2 97.4 -65.8 28 VAL -59.6 123.7 -179.8 98.9 29 PRO -95.6 160.8 175.7 39.6 -42.0 30 VAL -109.0 175.5 179.6 -80.6 31 PHE -144.0 155.7 177.1 -52.8 -69.0 32 THR -137.6 119.7 179.4 -63.1 33 VAL -104.0 127.9 179.0 123.4 34 GLU -118.8 135.0 -178.9 -68.6 171.4 -46.9 35 VAL -111.7 136.1 176.5 177.1 36 LYS -129.4 123.4 -178.4 168.6 -179.0 -88.4 168.9 37 ASN -119.1 130.1 179.6 40.7 16.2 38 TYR -34.4 136.4 -179.8 -169.2 86.6 39 GLY 87.7 48.3 179.4 40 VAL -88.9 134.3 179.6 172.9 41 LYS -51.0 -53.3 179.6 166.4 -169.1 168.9 -176.6 42 ASN -118.6 -100.6 179.9 -53.6 111.9 43 SER -154.9 10.6 -180.0 -171.9 44 GLU -75.7 137.9 176.7 153.0 114.9 84.7 45 TRP -85.9 179.2 -178.5 -75.5 81.8 46 ILE -132.0 138.8 -179.5 -135.7 -51.7 47 ASP -85.1 114.3 -178.8 -66.1 -121.5 48 ALA -87.7 -42.8 -179.8 49 CYS -146.0 110.8 -178.1 25.8 50 ILE -92.1 122.9 -178.3 48.9 -177.8 51 ASN 38.1 63.3 179.3 54.1 45.5 52 ILE -89.0 151.5 -178.8 -97.2 -49.5 53 SER -94.6 -23.5 -178.9 58.3 54 HIS -74.2 -161.9 -178.6 35.8 99.0 55 HIS -132.1 38.3 -179.6 -82.3 24.8 56 TYR -158.0 162.3 178.3 70.1 -98.8 57 CYS -157.3 118.2 179.3 -171.9 58 ASN -82.8 104.2 -178.7 -172.3 -26.2 59 ILE -90.6 15.5 -180.0 50.7 -177.8 60 SER -39.4 -33.2 178.0 -73.2 61 ASP -91.6 40.2 178.3 -94.5 77.3 62 HIS -145.9 0.5 177.7 -51.9 -51.7 63 VAL -92.0 93.9 178.2 177.5 64 GLY -76.6 -122.1 178.3 65 ASP -64.3 119.6 -179.5 -178.1 -53.9 66 PRO -57.0 10.2 179.1 31.5 -43.4 67 SER -115.0 -11.7 -178.6 -77.3 68 ASN -88.0 93.7 179.3 -72.9 41.9 69 SER -29.8 140.3 177.8 -73.8 70 LEU -138.1 150.8 178.5 45.8 59.9 71 TRP -124.5 135.0 179.7 -59.8 -104.1 72 VAL -123.0 146.0 179.3 62.3 73 ARG -128.6 154.0 179.4 59.0 176.2 -165.9 -169.1 74 VAL -137.8 155.8 178.3 57.5 75 LYS -146.6 177.9 179.1 63.1 175.4 167.3 176.4 76 ALA -129.2 175.0 176.1 77 ARG -154.0 140.1 175.7 171.6 -165.2 -50.5 179.5 78 VAL -172.5 146.4 -176.7 174.5 79 GLY 91.2 -60.4 178.6 80 GLN 162.8 -2.8 179.9 0.0 0.0 0.0 81 LYS -99.6 118.5 179.1 -49.8 -13.0 126.8 -20.7 82 GLU -72.8 170.1 -179.8 -94.1 174.2 -37.8 83 SER -133.8 179.9 178.7 -172.2 84 ALA -70.4 156.3 -179.9 85 TYR -79.6 158.4 178.5 -71.2 -89.9 86 ALA -113.1 131.2 -177.8 87 LYS -105.7 127.8 177.5 -168.3 162.3 98.9 55.1 88 SER -80.5 156.8 176.1 63.0 89 GLU -75.8 169.5 177.8 -68.6 -166.3 116.4 90 GLU -58.2 130.1 179.7 174.1 -159.2 -121.4 91 PHE -116.1 146.7 179.3 -175.5 61.8 92 ALA -135.9 108.4 -179.6 93 VAL -43.0 -58.0 -178.7 176.5 94 CYS -61.6 -36.3 178.6 -147.9 95 ARG -83.3 -40.2 -176.0 174.0 -157.1 -170.8 -91.4 96 ASP -95.0 -7.0 179.3 -54.6 -68.1 97 GLY -96.5 -172.7 176.8 98 LYS -137.8 149.6 -177.1 -165.1 68.4 167.8 -170.8 99 ILE -127.1 135.9 -178.0 -73.0 -160.9 100 GLY -51.6 154.7 -179.5 101 PRO -65.5 166.9 179.2 30.9 -42.2 102 PRO -80.9 172.2 -179.2 36.9 -45.6 103 LYS -111.8 108.1 -177.5 -61.9 165.4 -175.3 -171.4 104 LEU -86.6 143.8 177.8 -83.5 -172.4 105 ASP -139.2 115.9 178.8 -102.3 -35.5 106 ILE -105.6 156.2 -178.4 177.0 160.1 107 ARG -165.6 -153.8 179.4 73.9 173.4 112.2 111.1 108 LYS -151.3 148.0 179.2 -83.8 -159.0 -166.3 -171.2 109 GLU -149.3 125.7 -179.1 -71.7 -172.8 -0.6 110 GLU 17.7 -100.4 -179.7 -65.8 177.4 78.1 111 LYS -93.7 7.7 -179.9 -163.3 -178.8 -67.2 171.2 112 GLN -137.4 133.2 176.4 64.8 -178.6 17.9 113 ILE -79.3 132.4 178.9 -65.8 178.2 114 MET -106.6 140.5 178.6 -46.6 -46.0 -82.7 115 ILE -123.8 130.6 179.6 -64.0 179.7 116 ASP -117.4 122.2 -178.3 -112.1 -42.7 117 ILE -114.5 97.8 180.0 -47.3 142.4 118 PHE -80.1 129.4 -179.1 -60.6 96.4 119 HIS -54.4 142.2 179.9 -56.9 -36.0 120 PRO -45.2 144.0 -179.6 -41.0 49.3 121 SER -35.0 -55.9 -179.7 -26.5 122 VAL -46.8 -57.2 -178.0 -87.0 123 PHE -61.2 -49.5 179.9 -47.6 -63.7 124 VAL -67.2 108.8 -178.7 -173.3 125 ASN -158.0 -33.1 -175.2 72.5 -29.1 126 GLY 76.4 65.3 -176.4 127 ASP -24.3 128.2 177.1 -64.4 -114.7 128 GLU -137.9 -33.4 178.6 0.0 0.0 0.0 129 GLN 73.9 90.1 179.5 0.0 0.0 0.0 130 GLU 174.5 7.7 62.9 0.0 0.0 0.0 131 ASP -134.9 67.5 -179.9 0.0 0.0 132 PRO -69.5 139.0 177.3 -30.6 45.8 133 GLU 58.4 39.5 177.7 -47.2 -69.8 24.5 134 THR -150.9 139.3 -179.5 170.7 135 THR -88.8 18.5 178.9 37.1 136 CYS -101.9 77.6 179.0 -164.5 137 TYR -137.7 175.3 -179.8 59.6 68.8 138 ILE -87.7 131.6 177.7 -49.5 -100.4 139 ARG -100.0 -51.9 176.4 67.6 172.6 -86.8 -86.7 140 VAL -123.0 141.1 175.1 -73.4 141 TYR -102.7 138.7 178.5 -90.5 -67.6 142 ASN -108.0 95.4 179.0 -74.1 -14.1 143 VAL -85.9 121.8 178.8 178.8 144 TYR -103.7 144.9 178.8 -58.1 69.7 145 VAL -134.8 116.4 179.7 173.9 146 ARG -102.6 132.7 179.8 -168.7 -136.7 -63.7 122.7 147 MET -132.2 -173.9 -178.0 -161.3 -159.1 84.1 148 ASN 2.7 -78.4 179.6 -160.9 -85.6 149 GLY -158.5 36.9 -178.6 150 SER -141.5 158.4 179.3 -33.0 151 GLU -133.3 145.4 178.9 166.2 159.7 11.8 152 ILE -138.9 133.0 179.1 84.1 -161.8 153 GLN -83.1 173.9 178.3 -86.0 -164.5 -151.4 154 TYR -153.5 98.8 -177.1 -90.2 -104.7 155 LYS -66.8 162.2 179.8 -49.7 -79.7 -178.4 162.2 156 ILE -163.2 112.1 -177.0 -75.3 -173.4 157 LEU -86.6 108.5 179.4 -74.7 58.4 158 THR -59.0 -25.2 -179.0 68.8 159 GLN -92.3 -83.6 -179.8 -53.2 -64.2 -102.5 160 LYS -73.2 77.6 -178.7 48.2 173.9 176.2 157.0 161 GLU 172.3 142.4 179.5 138.7 91.1 109.3 162 ASP -111.7 46.0 177.1 -163.0 -164.8 163 ASP -102.8 -34.5 179.6 -84.1 10.1 164 CYS -93.8 162.2 177.5 -59.4 165 ASP -156.6 177.2 -179.0 67.0 107.2 166 GLU -46.0 -24.9 179.6 -61.5 -54.1 94.5 167 ILE -100.9 -67.2 -176.7 -55.6 -58.7 168 GLN -119.1 -164.8 -179.5 53.9 -166.3 67.3 169 CYS -150.1 149.9 -179.9 -73.1 170 GLN -122.0 157.2 176.9 -34.8 -67.0 125.3 171 LEU -159.7 97.2 179.6 -169.8 139.9 172 ALA -81.2 152.4 -178.8 173 ILE -136.8 139.0 179.9 -67.4 174.7 174 PRO -77.3 142.8 179.9 34.9 -45.7 175 VAL -65.5 88.5 -176.3 -172.4 176 SER -76.0 169.5 176.7 161.0 177 SER 15.6 63.6 -179.4 -56.6 178 LEU 39.6 -57.6 177.9 -78.9 -120.9 179 ASN -116.9 130.1 -176.3 -132.0 -81.1 180 SER -41.1 -160.1 -178.4 -36.0 181 GLN 76.6 68.1 174.7 -163.2 53.6 -131.4 182 TYR -85.9 139.3 -179.6 -72.6 99.6 183 CYS -125.8 117.1 -177.0 -70.9 184 VAL -103.4 138.8 178.4 -174.5 185 SER -145.2 153.7 -178.5 11.8 186 ALA -154.7 143.2 179.0 187 GLU -123.0 155.4 178.4 56.3 -167.6 37.0 188 GLY -105.3 152.6 177.5 189 VAL -125.7 132.2 -175.6 -179.4 190 LEU -91.6 162.7 -179.0 -53.1 160.0 191 HIS -67.4 -171.1 -177.5 -163.7 90.6 192 VAL 36.8 -64.5 179.1 -147.1 193 TRP -94.5 -17.2 178.4 -72.2 -87.8 194 GLY 66.8 45.6 -179.5 195 VAL -85.4 132.6 179.7 179.8 196 THR -81.1 144.0 176.7 -12.6 197 THR -79.8 -174.2 -179.5 67.8 198 GLU -78.8 146.0 -179.4 -52.6 -152.8 -85.8 199 LYS -85.0 117.3 177.9 -178.0 -164.2 170.0 179.6 200 SER -51.9 158.5 -179.0 78.0 201 LYS -78.9 137.6 179.8 174.3 -153.9 170.5 66.8 202 GLU -52.8 124.2 178.9 -110.6 168.8 -121.6 203 VAL -115.8 90.1 -180.0 52.4 204 CYS -74.7 -173.5 -179.4 -50.7 205 ILE -171.1 153.5 -177.2 -154.9 -169.1 206 THR -132.7 139.3 -176.6 -143.0 207 ILE -117.3 141.1 177.2 -53.7 -155.6 208 PHE -138.3 112.5 -177.9 -50.5 93.3 209 ASN -150.6 169.3 177.8 -72.6 -48.2 210 SER -165.8 102.4 0.0 -168.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 VAL 74.808 8.788 30.865 2 PRO 71.765 8.777 33.274 3 THR 68.131 9.136 32.166 4 PRO 65.800 12.134 32.542 5 THR 63.032 11.668 35.074 6 ASN 59.412 12.651 35.672 7 VAL 58.757 14.024 32.169 8 THR 55.698 16.228 32.057 9 ILE 53.980 18.366 29.482 10 GLU 51.766 21.232 30.651 11 SER 49.721 23.800 28.820 12 TYR 47.946 27.127 29.336 13 ASN 46.183 29.148 26.679 14 MET 47.483 26.656 24.169 15 ASN 51.265 26.410 24.315 16 PRO 52.656 23.416 26.204 17 ILE 56.110 23.145 27.811 18 VAL 57.890 19.828 28.444 19 TYR 59.388 19.494 31.917 20 TRP 61.871 16.904 33.249 21 GLU 64.073 16.367 36.287 22 TYR 67.694 15.093 36.313 23 GLN 70.252 14.318 39.050 24 ILE 73.174 16.691 39.413 25 MET 75.970 15.434 37.166 26 PRO 79.739 16.197 37.518 27 GLN 79.668 18.148 34.287 28 VAL 76.697 20.207 33.301 29 PRO 74.692 18.111 30.750 30 VAL 72.670 19.196 27.851 31 PHE 69.294 17.840 26.716 32 THR 67.266 17.205 23.595 33 VAL 63.490 16.976 23.586 34 GLU 61.805 15.401 20.561 35 VAL 58.075 15.572 19.730 36 LYS 56.021 13.055 17.711 37 ASN 52.427 13.833 17.045 38 TYR 49.768 11.381 15.867 39 GLY 49.241 11.341 12.167 40 VAL 52.909 11.180 11.299 41 LYS 53.655 10.752 7.589 42 ASN 56.168 8.016 8.379 43 SER 57.694 7.464 11.827 44 GLU 60.313 10.252 12.444 45 TRP 60.297 12.274 15.658 46 ILE 61.060 15.991 15.713 47 ASP 63.724 17.938 17.589 48 ALA 62.035 20.696 19.598 49 CYS 65.035 21.888 21.603 50 ILE 68.444 20.412 20.620 51 ASN 71.112 20.020 23.369 52 ILE 69.690 22.525 25.821 53 SER 71.082 23.112 29.309 54 HIS 67.824 23.907 31.158 55 HIS 64.954 21.736 32.383 56 TYR 62.002 22.855 30.275 57 CYS 60.964 23.165 26.620 58 ASN 58.316 25.267 24.877 59 ILE 57.087 22.969 22.094 60 SER 54.572 25.414 20.604 61 ASP 55.747 24.715 17.089 62 HIS 54.775 21.031 17.251 63 VAL 51.221 21.592 18.440 64 GLY 49.233 21.063 15.227 65 ASP 45.457 20.654 15.586 66 PRO 45.140 21.180 19.333 67 SER 43.121 17.948 19.566 68 ASN 45.734 15.608 18.074 69 SER 47.686 13.732 20.776 70 LEU 51.464 14.087 20.772 71 TRP 54.245 12.285 22.612 72 VAL 57.541 13.958 23.420 73 ARG 60.741 12.298 24.557 74 VAL 63.886 13.738 26.067 75 LYS 67.502 12.735 26.615 76 ALA 70.817 14.104 27.829 77 ARG 74.396 14.066 26.689 78 VAL 77.576 14.507 28.777 79 GLY 81.165 13.375 28.723 80 GLN 79.928 13.036 25.208 81 LYS 77.657 10.270 26.304 82 GLU 74.122 10.343 25.662 83 SER 71.533 8.305 27.275 84 ALA 68.323 6.484 26.633 85 TYR 65.196 8.581 26.038 86 ALA 62.475 9.498 28.511 87 LYS 58.890 9.212 27.220 88 SER 56.067 11.579 28.030 89 GLU 52.648 10.008 28.033 90 GLU 50.317 10.836 25.114 91 PHE 49.388 14.501 25.539 92 ALA 46.378 16.129 24.009 93 VAL 46.391 19.893 24.197 94 CYS 42.543 20.245 24.258 95 ARG 41.877 17.466 26.800 96 ASP 44.962 18.104 28.892 97 GLY 45.490 21.878 28.874 98 LYS 43.763 24.825 30.552 99 ILE 42.565 28.081 28.946 100 GLY 42.353 31.508 30.452 101 PRO 38.940 32.786 31.504 102 PRO 36.731 34.819 29.192 103 LYS 36.433 38.610 29.650 104 LEU 33.114 39.778 31.123 105 ASP 31.363 43.143 30.851 106 ILE 28.150 44.034 32.677 107 ARG 26.156 47.335 32.117 108 LYS 22.616 48.675 31.728 109 GLU 19.777 49.416 29.335 110 GLU 16.316 50.401 30.629 111 LYS 14.756 47.191 31.984 112 GLN 17.720 44.971 31.104 113 ILE 21.300 44.346 32.288 114 MET 23.557 43.523 29.359 115 ILE 26.436 41.054 29.608 116 ASP 29.355 40.825 27.257 117 ILE 31.520 37.730 27.320 118 PHE 34.555 38.263 25.204 119 HIS 36.023 34.925 24.075 120 PRO 39.272 33.900 25.820 121 SER 42.444 35.575 24.582 122 VAL 43.647 32.528 22.626 123 PHE 40.646 32.164 20.358 124 VAL 40.173 35.821 19.454 125 ASN 42.947 36.359 16.934 126 GLY 42.260 36.417 13.202 127 ASP 44.106 33.122 12.935 128 GLU 47.793 32.817 12.123 129 GLN 48.351 30.044 14.707 130 GLU 51.237 30.652 17.138 131 ASP 39.802 28.759 14.972 132 PRO 39.671 27.148 11.477 133 GLU 39.659 23.367 11.057 134 THR 39.726 22.297 14.710 135 THR 37.016 21.114 17.017 136 CYS 38.810 22.855 19.850 137 TYR 36.562 25.860 20.388 138 ILE 34.056 26.918 23.011 139 ARG 30.569 25.392 22.500 140 VAL 28.703 26.588 25.523 141 TYR 29.448 29.478 27.896 142 ASN 28.112 29.045 31.415 143 VAL 27.158 32.505 32.644 144 TYR 26.366 32.330 36.339 145 VAL 24.531 35.214 37.869 146 ARG 24.381 35.682 41.621 147 MET 21.830 38.036 43.073 148 ASN 20.308 38.599 46.530 149 GLY 20.972 35.134 47.841 150 SER 20.164 32.874 44.933 151 GLU 21.992 31.639 41.801 152 ILE 21.117 30.813 38.179 153 GLN 23.343 29.413 35.398 154 TYR 22.861 30.504 31.753 155 LYS 23.801 28.179 28.900 156 ILE 24.795 29.959 25.670 157 LEU 25.553 28.216 22.471 158 THR 28.361 30.004 20.709 159 GLN 27.446 28.134 17.532 160 LYS 23.701 27.539 17.125 161 GLU 22.810 30.987 18.430 162 ASP 23.474 34.453 17.053 163 ASP 24.484 36.151 20.299 164 CYS 28.109 35.200 19.851 165 ASP 30.425 36.057 17.016 166 GLU 34.203 35.773 16.419 167 ILE 34.724 38.323 19.169 168 GLN 32.002 38.285 21.871 169 CYS 28.716 36.868 23.193 170 GLN 25.631 38.607 24.610 171 LEU 23.189 37.781 27.353 172 ALA 20.473 40.246 28.416 173 ILE 18.826 39.746 31.812 174 PRO 15.600 41.184 33.244 175 VAL 16.034 43.353 36.366 176 SER 14.949 40.547 38.693 177 SER 13.720 40.027 42.264 178 LEU 13.747 43.719 43.203 179 ASN 17.171 44.226 44.683 180 SER 20.470 44.279 43.102 181 GLN 24.112 43.556 43.273 182 TYR 23.948 41.160 40.408 183 CYS 27.259 39.344 40.099 184 VAL 28.447 37.816 36.850 185 SER 31.136 35.086 36.252 186 ALA 31.515 32.812 33.262 187 GLU 33.284 29.682 32.008 188 GLY 33.739 28.269 28.569 189 VAL 33.180 24.590 27.668 190 LEU 35.062 22.995 24.817 191 HIS 34.062 20.620 21.986 192 VAL 34.998 16.995 22.090 193 TRP 36.248 16.494 25.681 194 GLY 34.235 19.242 27.244 195 VAL 37.020 20.853 29.269 196 THR 36.103 24.081 31.072 197 THR 38.070 27.294 30.613 198 GLU 38.898 29.226 33.798 199 LYS 35.985 30.868 35.463 200 SER 36.400 34.630 35.235 201 LYS 36.436 36.815 38.347 202 GLU 33.106 38.218 39.379 203 VAL 32.245 41.593 37.849 204 CYS 29.193 42.876 39.713 205 ILE 26.676 45.756 39.337 206 THR 23.980 47.291 41.481 207 ILE 20.477 48.536 40.510 208 PHE 18.096 51.044 42.183 209 ASN 14.562 51.498 40.554 210 SER 10.767 51.743 41.379 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S/S S S S S 10 S/T T T T/S S S S S S S 20 S S S S C C S S S S 30 S S S S S S S S S C 40 C S S S S S S S S S 50 S S S/S S S S/S S S S/T T 60 T T/S S S S C S S S S 70 S S S S S C T T T T/S 80 S S S S S S S S S/S S 90 S S/T T T T S S S S S 100 S S S S S S S S S/T T 110 T T/S S S S S S S S S/T 120 T T T C C C C C C C/X 130 X/C C C C C S S S S S/S 140 S S S S S S/T T T T/S S 150 S S S S S S S/T T T T/S 160 S S S C T T T T/S S S 170 S S S S S C C S S S 180 S/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 S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E 10 B S S S e E E E E 20 E S S E 30 E E E E E E E e S 40 S S S E E E E E 50 E E S S e E E E e G 60 G G g t T T t e E 70 E E E E E E E t T T 80 t E E e 90 B h H H H H h 100 E E E E e B T 110 e E E e E E E E t 120 T T T t S S 130 t T T t S e E E E 140 E E E E E E E T T E 150 E E B S S S 160 S S S S S B 170 E E e S S 180 E E E E E E E E E 190 e T T t B 200 E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 VAL 101.1 85.1 61.3 2 PRO 69.9 56.2 56.6 3 THR 51.4 48.1 68.7 4 PRO 124.5 100.0 41.8 5 THR 50.7 47.4 72.1 6 ASN 13.7 11.3 85.3 7 VAL 114.8 96.6 45.4 8 THR 55.4 51.8 68.2 9 ILE 140.4 97.8 33.9 10 GLU 48.2 34.8 66.3 11 SER 80.8 96.7 49.0 12 TYR 84.7 46.8 75.3 13 ASN 93.7 77.5 50.0 14 MET 126.4 79.3 43.5 15 ASN 63.3 52.3 75.9 16 PRO 124.5 100.0 35.3 17 ILE 112.0 78.1 62.7 18 VAL 118.8 100.0 24.9 19 TYR 100.2 55.3 61.2 20 TRP 203.7 99.4 38.9 21 GLU 44.7 32.2 73.9 22 TYR 178.8 98.8 39.0 23 GLN 69.5 46.8 60.4 24 ILE 0.0 0.0 93.0 25 MET 126.8 79.6 52.6 26 PRO 32.3 26.0 74.6 27 GLN 56.0 37.7 67.7 28 VAL 11.0 9.3 77.3 29 PRO 110.0 88.4 47.2 30 VAL 78.9 66.4 57.8 31 PHE 165.2 99.1 42.0 32 THR 95.3 89.1 52.3 33 VAL 118.8 100.0 26.5 34 GLU 123.3 89.0 56.0 35 VAL 118.6 99.8 29.7 36 LYS 125.2 72.2 54.4 37 ASN 72.9 60.3 60.1 38 TYR 40.8 22.5 73.0 39 GLY 3.0 8.6 73.1 40 VAL 90.7 76.3 69.8 41 LYS 10.1 5.8 90.5 42 ASN 33.0 27.3 71.4 43 SER 17.8 21.3 74.8 44 GLU 5.5 4.0 85.5 45 TRP 173.2 84.5 57.6 46 ILE 61.4 42.8 70.4 47 ASP 64.5 58.4 57.7 48 ALA 72.3 99.5 46.7 49 CYS 82.3 83.0 41.8 50 ILE 35.7 24.9 78.2 51 ASN 65.9 54.5 71.9 52 ILE 96.4 67.2 61.4 53 SER 30.6 36.6 63.4 54 HIS 89.9 59.9 62.4 55 HIS 81.9 54.5 62.6 56 TYR 70.9 39.2 62.8 57 CYS 94.4 95.2 34.9 58 ASN 58.4 48.3 66.8 59 ILE 143.1 99.7 30.6 60 SER 56.1 67.1 64.1 61 ASP 6.7 6.1 79.6 62 HIS 115.4 76.8 49.5 63 VAL 104.6 88.0 45.5 64 GLY 0.0 0.0 85.0 65 ASP 69.6 63.0 68.1 66 PRO 106.5 85.5 43.8 67 SER 72.4 86.6 59.1 68 ASN 54.1 44.8 75.8 69 SER 67.1 80.3 54.0 70 LEU 144.2 97.6 34.2 71 TRP 150.9 73.6 57.2 72 VAL 118.8 100.0 26.4 73 ARG 156.4 74.9 48.0 74 VAL 118.8 100.0 30.3 75 LYS 136.2 78.6 61.3 76 ALA 72.3 99.6 44.1 77 ARG 114.4 54.8 68.8 78 VAL 106.7 89.8 52.5 79 GLY 12.4 35.6 79.5 80 GLN 101.5 68.3 65.3 81 LYS 46.9 27.0 79.1 82 GLU 82.5 59.6 71.1 83 SER 73.5 87.9 61.6 84 ALA 10.9 15.0 75.8 85 TYR 129.3 71.4 68.4 86 ALA 60.2 82.9 57.2 87 LYS 61.5 35.5 71.9 88 SER 80.5 96.3 51.4 89 GLU 0.0 0.0 91.2 90 GLU 59.8 43.2 68.9 91 PHE 152.2 91.3 45.7 92 ALA 67.0 92.3 59.2 93 VAL 112.9 95.0 33.6 94 CYS 95.3 96.0 44.3 95 ARG 72.8 34.9 72.7 96 ASP 79.9 72.3 62.6 97 GLY 31.0 89.0 70.4 98 LYS 87.4 50.4 70.7 99 ILE 136.2 94.9 31.8 100 GLY 32.2 92.4 58.1 101 PRO 82.3 66.1 65.7 102 PRO 124.5 100.0 47.6 103 LYS 53.5 30.8 79.7 104 LEU 145.6 98.5 43.3 105 ASP 40.1 36.3 67.6 106 ILE 137.5 95.8 41.1 107 ARG 104.3 49.9 71.8 108 LYS 120.1 69.3 56.4 109 GLU 65.1 46.9 73.0 110 GLU 0.0 0.0 89.7 111 LYS 9.5 5.5 81.5 112 GLN 76.4 51.4 64.9 113 ILE 143.3 99.9 28.5 114 MET 133.8 83.9 60.7 115 ILE 143.3 99.9 32.2 116 ASP 101.9 92.2 61.6 117 ILE 143.5 100.0 27.6 118 PHE 111.5 66.8 64.1 119 HIS 132.3 88.1 50.6 120 PRO 124.5 100.0 47.5 121 SER 37.1 44.4 76.8 122 VAL 93.4 78.6 46.6 123 PHE 144.0 86.4 37.4 124 VAL 81.6 68.7 64.5 125 ASN 73.4 60.7 81.7 126 GLY 0.0 0.0 85.5 127 ASP 73.3 66.4 67.7 128 GLU 66.9 48.3 83.6 129 GLN 83.5 56.2 85.9 130 GLU 77.3 55.7 76.1 131 ASP 91.1 82.4 62.8 132 PRO 44.2 35.5 76.2 133 GLU 0.0 0.0 87.1 134 THR 92.8 86.8 62.6 135 THR 49.0 45.8 64.4 136 CYS 98.9 99.7 42.5 137 TYR 126.7 70.0 57.6 138 ILE 138.1 96.3 34.1 139 ARG 95.9 45.9 61.6 140 VAL 110.3 92.8 53.9 141 TYR 181.0 100.0 30.2 142 ASN 105.9 87.6 56.3 143 VAL 118.8 100.0 27.9 144 TYR 147.0 81.2 65.0 145 VAL 114.7 96.6 35.7 146 ARG 100.8 48.3 75.2 147 MET 141.8 89.0 56.5 148 ASN 27.7 22.9 76.3 149 GLY 3.5 10.0 84.7 150 SER 11.6 13.8 81.6 151 GLU 62.8 45.3 62.9 152 ILE 54.3 37.9 73.7 153 GLN 83.1 55.9 64.6 154 TYR 132.1 73.0 47.5 155 LYS 54.9 31.7 81.3 156 ILE 135.2 94.3 42.0 157 LEU 99.0 67.0 59.0 158 THR 100.2 93.7 46.6 159 GLN 61.6 41.4 73.2 160 LYS 17.0 9.8 76.0 161 GLU 88.9 64.2 70.3 162 ASP 0.4 0.4 89.3 163 ASP 65.4 59.2 69.9 164 CYS 97.9 98.7 49.0 165 ASP 38.5 34.8 73.1 166 GLU 4.3 3.1 83.0 167 ILE 59.5 41.5 62.7 168 GLN 105.6 71.0 66.1 169 CYS 99.2 100.0 37.4 170 GLN 91.3 61.4 74.9 171 LEU 133.4 90.3 39.4 172 ALA 50.0 68.9 64.3 173 ILE 138.7 96.6 34.2 174 PRO 37.0 29.7 74.2 175 VAL 104.1 87.6 57.4 176 SER 40.1 48.0 68.4 177 SER 14.6 17.5 73.7 178 LEU 6.6 4.5 89.4 179 ASN 45.8 37.9 78.7 180 SER 83.4 99.8 51.7 181 GLN 57.2 38.5 67.4 182 TYR 177.4 98.0 33.9 183 CYS 95.9 96.7 52.1 184 VAL 118.5 99.8 32.3 185 SER 79.9 95.6 51.2 186 ALA 72.6 100.0 37.1 187 GLU 111.8 80.7 54.8 188 GLY 34.8 100.0 42.3 189 VAL 97.4 82.0 60.2 190 LEU 142.9 96.7 42.1 191 HIS 83.6 55.6 56.6 192 VAL 64.3 54.1 62.3 193 TRP 123.0 60.0 60.1 194 GLY 18.5 53.2 68.2 195 VAL 89.7 75.5 67.3 196 THR 66.9 62.6 71.1 197 THR 106.6 99.7 42.1 198 GLU 79.9 57.6 57.5 199 LYS 81.5 47.0 74.1 200 SER 77.1 92.2 57.2 201 LYS 0.8 0.5 93.0 202 GLU 99.4 71.7 68.8 203 VAL 71.0 59.8 67.6 204 CYS 72.8 73.4 67.7 205 ILE 105.4 73.5 47.4 206 THR 64.5 60.3 55.9 207 ILE 141.9 98.9 39.6 208 PHE 28.8 17.3 83.1 209 ASN 42.5 35.2 76.9 210 SER 0.0 0.0 80.0