Protein Data Bank File : 1g44c Title : IMMUNE SYSTEM 26-OCT-00 1G44 Number of Amino Acid Residues : 228 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 CYS CYS THR ILE PRO SER ARG PRO ILE ASN 10 MET LYS PHE LYS ASN SER GLU THR ASP ALA 20 ASN ALA ASN TYR ASN ILE GLY ASP THR ILE 30 GLU TYR LEU CYS LEU PRO GLY TYR ARG LYS 40 GLN LYS MET GLY PRO ILE TYR ALA LYS CYS 50 THR GLY TRP THR PHE ASN GLN CYS ILE LYS 60 ARG ARG CYS PRO SER PRO ARG ASP ASP GLY 70 GLN LEU ASP ILE GLY GLY VAL ASP PHE GLY 80 SER SER ILE THR TYR SER CYS ASN SER GLY 90 TYR HIS LEU ILE GLY GLU SER LYS SER TYR 100 CYS GLU LEU GLY THR GLY SER MET VAL TRP 110 ASN PRO GLU ALA PRO ILE CYS GLU VAL LYS 120 CYS GLN SER PRO PRO SER ILE SER ASN GLY 130 ARG HIS ASN GLY TYR GLU ASP PHE TYR THR 140 ASP GLY SER VAL VAL THR TYR SER CYS ASN 150 TYR LEU ILE GLY ASN SER GLY VAL LEU CYS 160 SER GLY GLY GLU TRP SER ASP PRO PRO THR 170 CYS GLN VAL CYS PRO HIS PRO THR ILE SER 180 ASN GLY TYR LEU SER SER GLY PHE ARG SER 190 TYR SER TYR ASN ASP ASN VAL ASP PHE LYS 200 CYS LYS GLY TYR LYS LEU SER GLY SER SER 210 SER SER THR CYS SER PRO GLY ASN THR TRP 220 LYS PRO GLU LEU PRO LYS CYS VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 CYS 0.0 135.4 179.9 -60.0 2 CYS -88.9 163.9 -176.4 -112.9 3 THR -103.5 -173.9 -177.2 -20.4 4 ILE -63.6 161.8 -176.5 56.5 151.5 5 PRO -60.6 176.0 -176.0 4.5 -8.6 6 SER -60.9 162.7 -175.2 59.9 7 ARG -117.3 -62.7 -176.8 64.4 -90.7 -141.4 -76.3 8 PRO -38.3 144.5 180.0 -28.8 25.3 9 ILE -95.0 137.8 -178.6 -43.1 146.6 10 ASN 58.9 71.5 -177.7 -73.3 -56.6 11 MET -147.5 -175.2 -179.2 -147.1 -156.7 66.8 12 LYS -78.3 142.2 -178.7 44.4 -158.2 -169.8 180.0 13 PHE -114.0 158.6 179.8 -77.7 -86.3 14 LYS -103.2 105.9 179.6 -44.5 164.0 -167.8 64.8 15 ASN -148.2 82.6 -179.7 -172.8 51.3 16 SER -170.2 10.4 6.7 60.0 17 GLU -18.9 111.2 177.8 -93.7 91.8 -118.9 18 THR -122.9 82.0 -178.9 -44.6 19 ASP -109.0 167.5 178.1 -70.1 -52.0 20 ALA -78.5 -56.1 176.3 21 ASN -111.5 105.5 -176.1 -86.7 -60.0 22 ALA -124.7 -92.1 -176.7 23 ASN -53.5 122.4 -178.9 -55.9 -72.2 24 TYR -132.7 -121.3 -179.6 -104.2 -84.7 25 ASN -129.5 159.3 179.0 64.3 162.2 26 ILE 44.8 71.5 176.9 -47.8 142.9 27 GLY 139.0 71.6 179.8 28 ASP -150.4 108.0 177.2 -95.2 -60.0 29 THR -133.0 108.4 -179.7 -43.5 30 ILE -112.4 130.6 -179.9 -31.0 149.8 31 GLU -98.4 146.1 -178.1 -62.3 -174.9 -56.6 32 TYR -112.8 149.9 177.9 -61.7 -82.6 33 LEU -125.5 123.7 -179.7 -84.6 160.5 34 CYS -84.9 168.0 -179.6 -81.6 35 LEU -75.5 165.3 -178.3 -83.3 -62.3 36 PRO -21.9 -73.8 176.8 -42.5 34.4 37 GLY -111.9 77.1 -179.8 38 TYR -138.7 140.8 -176.8 -96.3 -84.8 39 ARG -113.5 168.8 178.2 -41.3 -69.6 -88.6 -171.2 40 LYS -99.0 143.5 -177.6 -64.8 -160.2 -164.4 -64.5 41 GLN -79.5 -163.9 -177.9 -104.9 -75.3 123.7 42 LYS -78.3 -162.2 -179.7 -66.1 177.3 -178.6 179.3 43 MET 24.0 88.4 -179.2 -64.5 94.2 72.8 44 GLY 137.9 96.2 -178.8 45 PRO -73.9 -47.8 -178.2 24.6 -24.0 46 ILE -102.7 -178.6 -178.1 53.2 150.6 47 TYR -76.8 -176.7 -176.2 -62.8 -75.5 48 ALA -68.7 125.9 179.9 49 LYS -125.5 148.2 -176.9 -92.0 -164.4 180.0 180.0 50 CYS -115.9 125.1 176.4 -172.4 51 THR -132.9 -66.4 47.8 -28.4 52 GLY -12.9 -175.6 179.0 53 TRP -77.6 131.3 -176.0 -77.8 103.8 54 THR -111.7 83.0 -49.2 -35.6 55 PHE -88.9 -173.2 -179.7 -68.7 -82.8 56 ASN -161.4 133.2 177.8 63.1 -97.2 57 GLN -167.4 143.2 179.1 -117.9 -152.3 10.4 58 CYS -131.7 130.2 -177.6 178.3 59 ILE -149.1 -159.2 179.5 61.5 145.5 60 LYS -139.3 112.1 179.2 -160.8 179.9 -179.9 -180.0 61 ARG -165.4 138.5 178.5 -118.1 167.8 -69.5 -173.4 62 ARG -113.4 168.9 178.6 -70.8 94.8 169.2 -165.6 63 CYS -88.2 141.2 -176.8 -144.1 64 PRO -71.5 180.0 -178.8 20.5 -21.3 65 SER -63.1 150.0 -176.9 60.0 66 PRO -69.3 128.4 -179.7 12.9 -13.4 67 ARG -57.3 122.0 -179.1 45.1 -95.4 175.2 -81.6 68 ASP -91.4 155.4 49.9 -86.1 72.4 69 ASP -123.8 32.1 0.5 -101.7 -127.4 70 GLY 63.9 114.0 -179.9 71 GLN -133.4 140.4 179.8 -101.4 162.3 61.0 72 LEU -101.6 136.9 -178.9 31.3 -76.1 73 ASP -115.0 67.9 176.1 -85.4 -49.7 74 ILE -140.3 -135.4 -179.9 -37.8 -52.9 75 GLY -156.7 -112.5 179.5 76 GLY -114.6 140.1 -177.0 77 VAL -137.9 166.9 177.6 83.3 78 ASP -81.6 -86.1 175.5 -62.4 -60.7 79 PHE -153.3 8.9 -179.0 147.4 -79.5 80 GLY -123.1 89.2 178.2 81 SER -179.3 144.9 177.4 73.2 82 SER -107.7 121.1 -178.4 50.6 83 ILE -97.1 128.3 179.9 40.5 -76.6 84 THR -94.3 137.5 -178.4 -44.0 85 TYR -97.1 130.3 -179.6 -91.0 75.0 86 SER -108.8 127.5 -179.6 70.7 87 CYS -121.3 162.4 179.1 -55.3 88 ASN -97.1 143.2 -178.7 -63.4 64.0 89 SER -38.7 108.1 -176.4 52.2 90 GLY 160.2 -98.3 -178.8 91 TYR -48.3 144.0 -179.2 -51.8 66.3 92 HIS -111.1 143.6 -179.6 -70.2 -85.0 93 LEU -74.6 129.5 179.6 -82.0 152.6 94 ILE -102.4 96.7 -177.9 -42.0 147.9 95 GLY 143.0 178.9 177.1 96 GLU -63.1 147.1 -177.9 -166.7 -93.3 -50.7 97 SER -101.8 88.9 178.8 -179.3 98 LYS 159.8 130.5 -179.6 -106.8 -179.9 -180.0 179.9 99 SER -115.1 136.4 -179.3 -67.3 100 TYR -128.5 157.6 174.5 -61.3 82.5 101 CYS -85.2 132.1 -174.1 179.6 102 GLU -54.4 124.0 -177.0 -100.9 -83.1 88.8 103 LEU -89.4 126.5 -179.6 41.3 79.6 104 GLY -134.4 -36.0 39.4 105 THR -79.5 -63.3 -178.1 -37.0 106 GLY -29.2 -93.1 177.9 107 SER 168.5 151.5 -179.9 -98.8 108 MET -148.4 -159.2 -179.6 -129.3 -62.9 -73.2 109 VAL -83.9 156.0 -177.7 -157.0 110 TRP -69.9 166.8 -179.4 -56.6 82.9 111 ASN -85.3 -97.0 -178.4 -169.8 -41.4 112 PRO -66.0 118.8 -178.6 18.1 -17.7 113 GLU -146.2 -34.9 179.8 -169.0 -98.1 -63.1 114 ALA -63.6 -39.2 -179.2 115 PRO -83.1 133.4 -179.3 28.6 -28.5 116 ILE -114.4 168.8 178.6 -14.5 80.6 117 CYS -90.2 110.7 -176.9 178.1 118 GLU -164.2 154.9 -75.5 -145.6 174.3 -94.0 119 VAL 40.8 88.0 -175.4 152.6 120 LYS -155.2 158.5 174.2 57.6 96.9 -179.9 179.9 121 CYS -123.7 140.7 -179.0 -61.7 122 GLN -107.9 -177.1 -179.0 -83.1 -148.4 92.4 123 SER -77.9 122.9 -178.2 -180.0 124 PRO -40.7 125.3 179.1 -30.1 27.2 125 PRO -67.1 140.7 -180.0 16.8 -18.2 126 SER -69.4 131.9 179.9 59.2 127 ILE -84.5 -175.3 -179.5 57.1 151.8 128 SER -49.9 -73.3 178.3 -59.9 129 ASN -126.9 71.8 -178.4 -95.8 84.9 130 GLY -158.1 157.9 179.6 131 ARG -115.8 166.8 179.6 -78.6 91.1 -173.1 78.4 132 HIS -119.2 126.2 -179.3 53.0 96.5 133 ASN -123.9 129.6 -179.8 -90.9 -96.2 134 GLY -154.3 162.6 179.1 135 TYR -65.6 -60.7 179.6 -59.0 -87.8 136 GLU -99.0 -151.0 -179.6 64.2 -94.8 -95.9 137 ASP -112.6 -116.0 -179.6 -82.7 -75.6 138 PHE -61.8 123.5 -173.5 -32.3 -88.3 139 TYR -109.9 84.9 171.5 -14.1 76.4 140 THR 53.4 -135.7 177.4 78.8 141 ASP -115.0 -127.8 -177.0 -165.2 65.9 142 GLY -60.1 116.4 -179.1 143 SER -152.2 166.6 -179.9 61.3 144 VAL -98.7 128.2 -179.2 -169.4 145 VAL -109.0 136.5 179.5 -156.6 146 THR -117.2 139.8 -179.7 -38.4 147 TYR -120.5 155.5 -179.3 -89.3 84.4 148 SER -119.4 163.4 -180.0 -68.1 149 CYS -129.7 168.1 178.9 -67.6 150 ASN -87.5 -27.9 5.1 -64.3 -94.3 151 TYR 101.7 -171.6 28.4 -91.4 101.3 152 LEU -135.3 138.2 177.8 -71.5 -57.0 153 ILE -114.1 120.1 -179.3 -35.5 -57.6 154 GLY -171.9 -169.0 177.1 155 ASN -87.8 -88.4 175.6 -179.4 68.4 156 SER -160.0 46.3 -179.9 60.1 157 GLY 142.1 156.7 177.3 158 VAL -100.5 131.8 -178.3 -174.3 159 LEU -113.5 137.5 -179.4 -168.4 81.1 160 CYS -132.8 133.4 179.8 157.8 161 SER -144.7 58.9 175.1 -173.6 162 GLY 128.7 13.0 178.3 163 GLY 111.1 60.1 -179.4 164 GLU -171.5 134.0 179.1 -114.4 171.9 -65.4 165 TRP -103.0 125.7 -179.2 -51.2 100.7 166 SER -129.8 74.7 176.4 60.0 167 ASP 164.3 93.9 -178.4 -161.4 83.4 168 PRO -78.5 118.9 -179.6 28.4 -27.5 169 PRO -83.5 126.9 -179.6 27.9 -27.1 170 THR -124.0 136.9 178.7 27.1 171 CYS -101.1 107.5 -178.3 -73.6 172 GLN -123.7 -117.8 17.6 -74.0 -71.7 92.3 173 VAL 104.1 -177.3 7.4 62.7 174 CYS -125.4 128.8 -178.2 -117.1 175 PRO -88.3 165.3 179.2 34.2 -33.1 176 HIS -50.4 124.3 -179.6 -84.1 121.8 177 PRO -60.7 135.0 179.7 3.9 -3.7 178 THR -95.1 112.9 -179.6 50.8 179 ILE -147.0 141.7 -179.6 -171.8 149.6 180 SER -88.2 -64.2 179.2 -60.0 181 ASN -121.9 89.9 -179.9 -74.2 -78.2 182 GLY 171.4 145.8 178.6 183 TYR -134.2 138.7 -178.2 47.5 86.6 184 LEU -98.5 128.2 179.5 67.8 -46.7 185 SER -134.8 88.2 178.2 180.0 186 SER -171.3 98.8 -178.3 -180.0 187 GLY 56.5 68.6 -178.8 188 PHE -87.1 150.8 38.8 -171.3 80.7 189 ARG -109.6 -58.0 178.2 -60.0 173.2 -166.3 76.4 190 SER -119.9 125.6 179.9 180.0 191 TYR -98.8 165.4 179.2 -48.1 -85.4 192 SER -111.8 -95.2 -180.0 52.1 193 TYR -62.2 176.9 -177.8 -143.2 -80.0 194 ASN -65.4 162.5 -179.4 79.7 109.8 195 ASP -109.5 -141.3 -177.4 -91.4 -121.7 196 ASN 168.8 4.1 -175.1 -159.3 -107.0 197 VAL -48.6 131.4 -179.3 -67.6 198 ASP -98.2 145.7 -178.9 -57.8 82.6 199 PHE -106.6 137.0 179.3 -55.9 -80.4 200 LYS -103.6 132.0 -178.1 -173.8 -176.7 176.7 65.7 201 CYS -93.9 162.6 -177.2 -74.1 202 LYS -89.7 8.7 -15.2 -163.1 179.9 -180.0 -180.0 203 GLY -52.1 94.7 179.4 204 TYR -142.0 156.5 -179.7 -73.7 -41.8 205 LYS -113.3 158.5 -178.6 -157.7 -179.7 179.0 65.8 206 LEU -94.1 137.0 178.0 -78.6 -61.3 207 SER -124.1 75.4 -178.9 180.0 208 GLY 160.4 158.4 178.8 209 SER -58.7 147.1 -179.0 179.9 210 SER -107.9 88.0 179.2 -61.8 211 SER 172.2 136.5 -178.9 62.3 212 SER -131.4 115.9 -177.5 -96.6 213 THR -109.8 160.6 -177.7 -20.2 214 CYS -97.1 147.8 -179.6 -164.2 215 SER -131.1 160.8 -178.6 -80.6 216 PRO -77.3 143.0 -178.6 24.0 -24.6 217 GLY 109.3 -99.4 176.3 218 ASN -167.1 65.9 -179.2 -156.5 72.8 219 THR -150.2 153.4 177.9 23.9 220 TRP -116.4 139.5 -179.8 -81.6 66.9 221 LYS -137.5 124.1 1.7 -102.1 -152.7 -82.6 81.6 222 PRO -76.3 145.5 -178.3 24.1 -24.0 223 GLU -37.7 138.9 -178.7 -161.4 77.9 76.4 224 LEU -45.0 114.4 -178.4 -66.0 -52.2 225 PRO -81.9 160.5 180.0 27.8 -27.6 226 LYS -118.0 146.7 -179.6 -165.7 179.9 -90.1 74.5 227 CYS -106.0 123.1 -178.0 -175.5 228 VAL -122.3 -51.4 0.0 -85.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 CYS 80.048 28.865 46.702 2 CYS 79.057 32.201 48.192 3 THR 75.978 34.348 47.545 4 ILE 75.178 38.073 46.957 5 PRO 76.205 41.079 49.077 6 SER 74.869 42.494 52.364 7 ARG 71.433 43.833 53.242 8 PRO 70.833 45.695 56.529 9 ILE 70.407 49.468 56.715 10 ASN 72.751 51.423 59.038 11 MET 75.336 48.691 59.498 12 LYS 79.014 47.844 58.890 13 PHE 80.399 47.923 55.364 14 LYS 83.078 45.921 53.588 15 ASN 85.706 48.335 52.284 16 SER 89.193 46.885 52.649 17 GLU 89.384 43.288 48.203 18 THR 86.414 45.243 46.827 19 ASP 85.514 43.339 43.645 20 ALA 82.291 42.824 41.660 21 ASN 82.598 39.033 41.534 22 ALA 84.640 38.150 44.605 23 ASN 83.388 35.676 47.252 24 TYR 83.217 32.176 45.820 25 ASN 84.513 29.045 47.667 26 ILE 87.502 27.873 49.759 27 GLY 89.095 31.191 50.743 28 ASP 86.813 33.948 52.060 29 THR 87.336 36.145 55.119 30 ILE 85.765 39.587 54.732 31 GLU 86.322 42.218 57.411 32 TYR 83.786 44.930 58.187 33 LEU 84.129 48.579 59.169 34 CYS 81.287 50.338 61.008 35 LEU 80.441 54.040 60.590 36 PRO 81.910 56.796 62.827 37 GLY 80.264 56.162 66.225 38 TYR 79.035 52.617 65.551 39 ARG 79.662 49.340 67.393 40 LYS 79.183 45.656 66.401 41 GLN 76.089 43.793 67.706 42 LYS 75.726 40.302 69.316 43 MET 75.802 36.778 67.696 44 GLY 78.975 36.617 65.616 45 PRO 82.474 36.641 67.088 46 ILE 84.711 36.821 64.005 47 TYR 84.367 38.566 60.598 48 ALA 82.437 37.311 57.546 49 LYS 83.132 33.703 56.623 50 CYS 81.708 31.531 53.866 51 THR 80.117 28.087 53.959 52 GLY 74.249 31.241 53.933 53 TRP 76.909 33.526 55.425 54 THR 78.416 31.753 58.423 55 PHE 76.220 36.339 60.920 56 ASN 76.483 40.175 60.731 57 GLN 75.169 43.285 62.542 58 CYS 76.253 46.813 63.551 59 ILE 74.543 48.887 66.259 60 LYS 75.434 51.184 69.225 61 ARG 75.978 50.050 72.836 62 ARG 78.723 50.150 75.497 63 CYS 79.176 48.065 78.669 64 PRO 77.665 49.808 81.692 65 SER 79.344 50.843 84.956 66 PRO 81.024 48.105 86.956 67 ARG 78.824 46.406 89.541 68 ASP 79.877 47.527 93.003 69 ASP 80.931 45.149 99.056 70 GLY 85.059 42.795 95.572 71 GLN 86.764 45.675 93.748 72 LEU 88.224 45.881 90.238 73 ASP 91.453 47.852 89.744 74 ILE 91.094 48.930 86.090 75 GLY 88.331 51.634 85.500 76 GLY 85.537 52.251 82.993 77 VAL 85.413 50.334 79.701 78 ASP 83.778 49.905 76.289 79 PHE 83.868 46.066 76.027 80 GLY 87.617 45.311 75.919 81 SER 89.254 44.633 79.265 82 SER 89.247 41.748 81.742 83 ILE 88.549 43.016 85.247 84 THR 90.148 41.111 88.096 85 TYR 88.250 41.168 91.377 86 SER 90.138 41.955 94.554 87 CYS 88.854 40.651 97.865 88 ASN 90.256 40.844 101.402 89 SER 91.606 37.641 103.050 90 GLY 88.536 35.587 103.941 91 TYR 85.668 35.421 101.495 92 HIS 85.852 33.264 98.350 93 LEU 84.801 34.344 94.844 94 ILE 81.714 32.381 93.754 95 GLY 82.216 32.110 89.993 96 GLU 85.213 32.021 87.605 97 SER 87.979 34.367 88.835 98 LYS 88.262 37.048 86.172 99 SER 85.215 39.024 84.978 100 TYR 84.549 39.994 81.359 101 CYS 81.725 41.807 79.538 102 GLU 80.172 38.995 77.444 103 LEU 81.898 38.740 74.095 104 GLY 79.861 38.328 70.939 105 THR 82.998 44.094 69.229 106 GLY 80.321 46.461 70.611 107 SER 78.899 45.491 74.046 108 MET 76.320 43.458 75.978 109 VAL 75.726 42.486 79.665 110 TRP 78.694 41.164 81.729 111 ASN 79.473 37.474 82.348 112 PRO 79.972 36.671 86.075 113 GLU 77.583 38.922 87.993 114 ALA 75.174 36.740 89.984 115 PRO 78.093 35.440 92.034 116 ILE 79.757 37.582 94.705 117 CYS 82.957 37.069 96.754 118 GLU 81.699 35.524 100.000 119 VAL 83.019 32.365 105.839 120 LYS 83.448 36.077 106.595 121 CYS 83.490 39.018 108.996 122 GLN 82.267 42.501 107.996 123 SER 82.902 45.997 109.411 124 PRO 81.640 46.208 112.979 125 PRO 78.151 47.574 113.525 126 SER 77.841 50.733 115.637 127 ILE 76.597 50.030 119.171 128 SER 74.284 52.237 121.308 129 ASN 76.762 54.931 122.469 130 GLY 80.031 53.599 121.086 131 ARG 82.525 53.699 118.223 132 HIS 84.572 50.966 116.522 133 ASN 88.370 51.087 116.363 134 GLY 90.591 48.570 114.577 135 TYR 93.872 48.272 112.663 136 GLU 92.391 47.249 109.286 137 ASP 88.706 47.207 108.125 138 PHE 86.705 43.921 107.637 139 TYR 88.796 41.454 109.632 140 THR 88.982 37.942 108.153 141 ASP 87.081 35.076 109.886 142 GLY 88.132 34.273 113.534 143 SER 89.738 37.417 114.896 144 VAL 89.639 39.593 118.028 145 VAL 87.456 42.703 117.685 146 THR 87.947 45.798 119.859 147 TYR 85.336 48.517 120.439 148 SER 85.599 52.093 121.722 149 CYS 83.406 54.411 123.807 150 ASN 82.934 58.188 124.156 151 TYR 82.046 55.425 129.412 152 LEU 83.014 48.551 127.989 153 ILE 81.299 45.352 129.145 154 GLY 82.528 42.220 127.319 155 ASN 84.807 39.171 127.689 156 SER 88.173 40.320 126.220 157 GLY 87.318 40.800 122.557 158 VAL 84.414 40.401 120.120 159 LEU 84.606 37.084 118.261 160 CYS 83.223 36.335 114.806 161 SER 83.497 33.023 112.923 162 GLY 81.533 33.035 109.672 163 GLY 79.123 35.982 109.870 164 GLU 77.953 36.279 113.508 165 TRP 79.206 38.384 116.447 166 SER 79.285 36.461 119.730 167 ASP 80.299 38.787 122.550 168 PRO 78.210 41.963 122.713 169 PRO 79.991 45.193 123.607 170 THR 78.116 47.703 125.772 171 CYS 79.161 51.218 126.732 172 GLN 77.974 51.738 130.286 173 VAL 80.662 51.628 135.503 174 CYS 85.302 48.148 138.417 175 PRO 86.047 48.535 142.121 176 HIS 88.402 46.753 144.566 177 PRO 87.502 43.073 144.827 178 THR 86.039 41.941 148.154 179 ILE 87.752 38.808 149.482 180 SER 88.585 37.577 152.992 181 ASN 91.303 34.921 152.616 182 GLY 92.694 35.153 149.109 183 TYR 94.789 37.670 147.157 184 LEU 94.674 38.446 143.438 185 SER 97.939 38.869 141.562 186 SER 97.433 39.560 137.865 187 GLY 97.431 43.236 136.840 188 PHE 96.658 44.771 140.246 189 ARG 93.893 50.648 142.337 190 SER 90.807 51.637 140.349 191 TYR 89.782 49.547 137.353 192 SER 87.580 50.615 134.424 193 TYR 86.555 47.712 132.116 194 ASN 86.226 44.038 133.092 195 ASP 89.001 41.990 134.655 196 ASN 89.564 38.163 134.758 197 VAL 91.731 38.066 137.941 198 ASP 92.580 34.792 139.598 199 PHE 92.895 34.500 143.364 200 LYS 95.808 32.811 145.099 201 CYS 94.977 31.300 148.490 202 LYS 97.085 31.368 151.631 203 GLY 96.415 25.346 152.505 204 TYR 92.874 26.572 151.838 205 LYS 90.300 25.643 149.153 206 LEU 88.214 27.918 146.899 207 SER 84.437 28.168 147.287 208 GLY 83.512 30.040 144.131 209 SER 84.655 29.971 140.470 210 SER 88.326 30.908 140.014 211 SER 88.331 33.769 137.525 212 SER 86.773 37.188 138.205 213 THR 85.023 39.374 135.627 214 CYS 83.280 42.754 135.740 215 SER 79.627 43.685 135.233 216 PRO 77.604 46.866 134.724 217 GLY 76.114 48.875 137.599 218 ASN 78.156 47.934 140.690 219 THR 78.516 44.148 140.568 220 TRP 81.144 41.537 139.664 221 LYS 80.195 38.331 137.782 222 PRO 80.503 35.791 138.912 223 GLU 80.118 37.362 142.369 224 LEU 83.204 37.736 144.567 225 PRO 84.206 34.335 145.903 226 LYS 85.576 33.361 149.313 227 CYS 88.475 31.019 150.086 228 VAL 87.916 28.537 152.915 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 S S S S X/P S/X S S S/S 20 S S S/S S S S/S S S S S 30 S S S S S S/S S S S S 40 S S S/S S S S S S S S 50 S/X X/S S S/X X/S S S S S S 60 S S/S S S S C C C/X XPC S/X 70 S S S S C C T T T T/S 80 S S S S S S S S S S 90 S S S S S C S S S S 100 S/S S S S/X X/S S S S S/S S 110 S S C S S S S S/X X/S S 120 S C S S S S S S C S 130 S S S S S/S S S S/S S S 140 S/S S S S/S S S S S S CPX 150 X/C S/X S S S S S S S S/T 160 T T T/S S S S S/S S S S 170 S SPX XPC C/X S S S S S S 180 S S S S S S C C/X X/S S 190 S S S/S S S S S S S S 200 S SPX SXS S S S S S/S S S 210 S/S S S S S/T T T T C T 220 T/P T T/S S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S 10 B S 20 S S S e E E 30 B t T T t E E 40 e S S S S E E e 50 B e E E 60 70 E E e S S S 80 B e E E S S 90 E E e S S S B 100 B B 110 S S S e E E 120 S t T e E 130 E E e S S S S 140 S S E E E e E E E e 150 B S S S S E E E 160 S S S B S B 170 S 180 S E E e S 190 S B e E E 200 E E E S S 210 B E E E T T T E E 220 E S E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 CYS 28.9 29.1 77.4 2 CYS 96.1 96.8 51.7 3 THR 23.1 21.6 73.9 4 ILE 7.5 5.2 74.9 5 PRO 25.2 20.2 77.4 6 SER 56.2 67.3 64.5 7 ARG 49.4 23.7 80.3 8 PRO 94.6 76.0 59.1 9 ILE 0.7 0.5 89.6 10 ASN 29.0 24.0 74.0 11 MET 153.7 96.4 49.1 12 LYS 158.8 91.6 38.2 13 PHE 46.0 27.6 78.1 14 LYS 141.0 81.3 52.8 15 ASN 22.4 18.6 80.8 16 SER 30.3 36.3 72.6 17 GLU 5.5 4.0 94.1 18 THR 36.5 34.2 87.5 19 ASP 44.1 39.9 69.8 20 ALA 0.0 0.0 85.6 21 ASN 12.1 10.0 79.6 22 ALA 46.6 64.2 77.3 23 ASN 94.0 77.8 48.5 24 TYR 53.0 29.3 80.8 25 ASN 52.5 43.4 63.8 26 ILE 0.0 0.0 90.2 27 GLY 0.0 0.0 84.7 28 ASP 91.7 83.0 68.3 29 THR 46.1 43.2 65.8 30 ILE 122.9 85.6 55.4 31 GLU 52.4 37.8 66.3 32 TYR 176.5 97.5 47.4 33 LEU 35.6 24.1 85.4 34 CYS 92.5 93.2 52.0 35 LEU 71.9 48.7 58.8 36 PRO 16.3 13.1 77.4 37 GLY 4.0 11.6 78.0 38 TYR 122.5 67.7 58.1 39 ARG 161.6 77.4 59.3 40 LYS 142.7 82.3 61.6 41 GLN 122.3 82.3 57.2 42 LYS 107.3 61.9 57.6 43 MET 11.4 7.1 79.4 44 GLY 23.3 66.8 69.1 45 PRO 37.4 30.1 72.0 46 ILE 49.8 34.7 69.3 47 TYR 94.3 52.1 62.9 48 ALA 68.0 93.6 52.2 49 LYS 72.4 41.8 74.2 50 CYS 95.2 96.0 54.1 51 THR 10.5 9.8 73.8 52 GLY 0.0 0.0 92.2 53 TRP 161.4 78.7 61.4 54 THR 33.4 31.2 81.7 55 PHE 26.1 15.6 90.0 56 ASN 108.3 89.6 48.2 57 GLN 63.4 42.7 61.9 58 CYS 99.1 99.9 34.5 59 ILE 105.5 73.5 69.9 60 LYS 79.9 46.1 70.7 61 ARG 75.6 36.2 76.3 62 ARG 81.0 38.8 77.8 63 CYS 99.1 99.9 47.7 64 PRO 46.3 37.2 78.9 65 SER 4.8 5.8 75.1 66 PRO 95.9 77.0 56.9 67 ARG 158.5 75.9 55.0 68 ASP 8.3 7.5 83.1 69 ASP 1.0 0.9 90.5 70 GLY 31.0 89.1 58.8 71 GLN 20.7 13.9 86.9 72 LEU 128.3 86.8 54.2 73 ASP 12.4 11.2 85.2 74 ILE 54.9 38.2 76.4 75 GLY 3.0 8.6 74.6 76 GLY 4.0 11.5 75.1 77 VAL 89.9 75.7 63.8 78 ASP 32.6 29.5 76.7 79 PHE 138.7 83.1 60.5 80 GLY 0.8 2.2 75.9 81 SER 58.9 70.4 52.6 82 SER 58.6 70.1 60.3 83 ILE 139.1 96.9 46.4 84 THR 38.0 35.6 72.0 85 TYR 153.1 84.6 55.1 86 SER 31.4 37.6 79.9 87 CYS 83.8 84.4 55.0 88 ASN 33.5 27.7 74.8 89 SER 8.4 10.0 75.7 90 GLY 23.8 68.3 70.1 91 TYR 149.7 82.7 51.6 92 HIS 14.4 9.6 86.9 93 LEU 110.1 74.5 59.1 94 ILE 42.7 29.8 77.0 95 GLY 11.7 33.6 66.6 96 GLU 33.5 24.2 78.6 97 SER 36.2 43.3 70.4 98 LYS 82.7 47.7 80.2 99 SER 76.9 92.0 50.9 100 TYR 87.5 48.4 64.2 101 CYS 98.3 99.1 47.5 102 GLU 66.8 48.2 73.0 103 LEU 35.1 23.7 74.2 104 GLY 15.8 45.3 60.1 105 THR 25.6 24.0 67.3 106 GLY 33.1 95.0 65.1 107 SER 83.5 99.8 54.1 108 MET 104.8 65.8 56.5 109 VAL 32.0 26.9 62.9 110 TRP 195.0 95.1 44.3 111 ASN 50.3 41.6 68.3 112 PRO 102.9 82.7 68.2 113 GLU 55.7 40.2 69.9 114 ALA 0.0 0.0 79.5 115 PRO 92.8 74.5 49.4 116 ILE 42.5 29.6 83.1 117 CYS 95.8 96.6 40.6 118 GLU 63.8 46.1 53.2 119 VAL 27.6 23.2 82.0 120 LYS 132.0 76.1 59.9 121 CYS 97.4 98.2 56.9 122 GLN 72.2 48.6 68.4 123 SER 50.6 60.5 53.2 124 PRO 122.7 98.5 45.9 125 PRO 52.5 42.2 77.3 126 SER 21.4 25.6 80.7 127 ILE 116.0 80.8 59.4 128 SER 0.0 0.0 83.5 129 ASN 40.5 33.5 77.6 130 GLY 34.8 100.0 57.7 131 ARG 67.7 32.4 83.0 132 HIS 86.9 57.9 67.4 133 ASN 34.7 28.7 79.8 134 GLY 22.7 65.2 70.8 135 TYR 0.0 0.0 90.2 136 GLU 39.0 28.1 71.6 137 ASP 13.3 12.1 75.9 138 PHE 115.9 69.5 68.3 139 TYR 160.6 88.7 57.4 140 THR 51.0 47.7 74.6 141 ASP 74.9 67.8 60.9 142 GLY 17.4 50.1 71.0 143 SER 57.1 68.3 65.6 144 VAL 31.2 26.3 79.0 145 VAL 117.7 99.0 43.2 146 THR 19.5 18.2 82.4 147 TYR 175.5 97.0 37.1 148 SER 52.3 62.6 63.6 149 CYS 95.0 95.8 47.8 150 ASN 66.2 54.7 64.9 151 TYR 98.6 54.5 72.6 152 LEU 130.2 88.1 52.3 153 ILE 117.3 81.7 57.1 154 GLY 22.0 63.2 74.2 155 ASN 32.0 26.5 85.2 156 SER 10.7 12.8 86.5 157 GLY 23.8 68.5 67.7 158 VAL 112.2 94.4 42.5 159 LEU 50.8 34.4 74.8 160 CYS 97.5 98.3 50.8 161 SER 32.5 38.8 73.1 162 GLY 27.6 79.2 69.6 163 GLY 20.2 57.9 72.0 164 GLU 3.1 2.3 85.6 165 TRP 149.4 72.9 49.4 166 SER 20.2 24.1 78.4 167 ASP 82.1 74.3 55.3 168 PRO 19.5 15.6 80.3 169 PRO 109.1 87.6 43.6 170 THR 41.8 39.1 67.1 171 CYS 99.2 100.0 41.5 172 GLN 61.5 41.4 59.3 173 VAL 92.6 78.0 58.4 174 CYS 98.6 99.4 46.2 175 PRO 66.1 53.1 73.9 176 HIS 55.9 37.2 64.9 177 PRO 122.3 98.3 32.8 178 THR 14.7 13.7 75.9 179 ILE 128.9 89.8 53.4 180 SER 33.4 40.0 69.8 181 ASN 56.4 46.7 69.9 182 GLY 34.8 100.0 48.0 183 TYR 68.2 37.7 64.1 184 LEU 138.4 93.6 42.3 185 SER 20.3 24.3 73.5 186 SER 25.1 30.0 81.5 187 GLY 0.0 0.0 87.0 188 PHE 71.0 42.6 72.6 189 ARG 3.6 1.7 90.4 190 SER 9.4 11.3 83.1 191 TYR 153.9 85.0 60.0 192 SER 3.7 4.4 82.2 193 TYR 102.6 56.7 72.0 194 ASN 117.3 97.0 56.4 195 ASP 91.4 82.7 48.7 196 ASN 35.1 29.1 77.5 197 VAL 112.4 94.6 53.9 198 ASP 35.0 31.6 75.6 199 PHE 166.7 99.9 37.2 200 LYS 41.8 24.1 82.1 201 CYS 91.1 91.8 48.5 202 LYS 29.2 16.8 75.0 203 GLY 0.0 0.0 92.1 204 TYR 99.8 55.1 69.8 205 LYS 10.1 5.8 86.7 206 LEU 108.2 73.2 62.4 207 SER 26.3 31.5 76.2 208 GLY 11.8 34.0 70.7 209 SER 28.5 34.1 76.3 210 SER 47.3 56.6 70.9 211 SER 48.8 58.3 83.3 212 SER 83.5 99.9 45.5 213 THR 79.6 74.4 73.4 214 CYS 96.1 96.9 47.9 215 SER 79.3 94.9 50.4 216 PRO 83.8 67.3 53.5 217 GLY 0.0 0.0 75.4 218 ASN 23.9 19.7 75.4 219 THR 43.8 41.0 79.4 220 TRP 199.9 97.5 41.6 221 LYS 42.2 24.4 81.8 222 PRO 58.6 47.1 78.5 223 GLU 37.5 27.1 73.3 224 LEU 129.8 87.8 55.1 225 PRO 115.8 93.0 62.4 226 LYS 61.7 35.6 77.0 227 CYS 99.2 100.0 39.0 228 VAL 29.2 24.6 66.5