Protein Data Bank File : 1et6b Title : IMMUNE SYSTEM 12-APR-00 1ET6 Number of Amino Acid Residues : 201 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP ASN ASN SER LEU LEU ARG ASN ILE TYR 10 SER THR ILE VAL TYR GLU TYR SER ASP ILE 20 VAL ILE ASP PHE LYS THR SER HIS ASN LEU 30 VAL THR LYS LYS LEU ASP VAL ARG ASP ALA 40 ARG ASP PHE PHE ILE ASN SER GLU MET ASP 50 GLU TYR ALA ALA ASN ASP PHE LYS THR GLY 60 ASP LYS ILE ALA VAL PHE SER VAL PRO PHE 70 ASP TRP ASN TYR LEU SER LYS GLY LYS VAL 80 THR ALA TYR THR TYR GLY GLY ILE THR PRO 90 TYR GLN LYS THR SER ILE PRO LYS ASN ILE 100 PRO VAL ASN LEU TRP ILE ASN GLY LYS GLN 110 ILE SER VAL PRO TYR ASN GLU ILE SER THR 120 ASN LYS THR THR VAL THR ALA GLN GLU ILE 130 ASP LEU LYS VAL ARG LYS PHE LEU ILE ALA 140 GLN HIS GLN LEU TYR SER SER GLY SER SER 150 TYR LYS SER GLY ARG LEU VAL PHE HIS THR 160 LYS TYR SER PHE ASP LEU PHE TYR VAL GLY 170 TYR ARG ASP LYS GLU SER ILE PHE LYS VAL 180 TYR LYS ASP ASN LYS SER PHE ASN ILE ASP 190 LYS ILE GLY HIS LEU ASP ILE GLU ILE ASP 200 SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 164.6 -179.4 61.2 -69.2 2 ASN -65.4 -37.5 -179.7 -63.1 -28.8 3 ASN -62.3 -49.0 179.7 -74.5 -34.8 4 SER -61.4 -41.8 -179.5 176.6 5 LEU -58.5 -57.5 -179.1 171.9 65.4 6 LEU -66.1 -32.4 178.9 -69.3 166.7 7 ARG -66.9 -42.5 -180.0 179.7 -159.7 -39.7 137.3 8 ASN -71.1 -44.3 178.9 -75.5 -50.6 9 ILE -58.6 -50.1 -178.2 -66.8 -67.9 10 TYR -81.1 6.5 176.6 -85.8 -76.6 11 SER -98.3 0.0 179.8 70.2 12 THR -62.3 141.5 -179.4 -59.9 13 ILE -54.2 140.3 178.9 -179.3 177.6 14 VAL -103.7 134.8 179.1 178.8 15 TYR -97.2 120.0 179.3 -65.5 -40.0 16 GLU -127.5 114.9 179.9 165.0 169.3 43.1 17 TYR -141.5 122.1 -177.6 -67.2 -87.9 18 SER -96.2 -11.1 -179.1 60.0 19 ASP -133.9 85.0 -179.2 -176.6 -177.6 20 ILE -128.0 152.1 178.4 -52.8 170.8 21 VAL -109.1 142.3 178.7 176.2 22 ILE -82.2 117.6 -179.8 -64.1 178.5 23 ASP -75.4 -55.4 179.9 -161.4 36.8 24 PHE -136.1 149.1 -180.0 -71.0 68.6 25 LYS -134.7 133.2 179.1 158.9 -164.2 155.4 55.2 26 THR -111.2 -176.9 -179.5 -43.3 27 SER -61.7 -29.6 179.5 65.0 28 HIS -145.9 38.7 -179.1 53.1 -131.6 29 ASN -161.6 138.5 179.5 -169.8 -77.6 30 LEU -127.6 141.4 177.9 -57.0 -178.8 31 VAL -127.6 131.0 -179.0 -177.9 32 THR -86.5 161.2 176.2 69.6 33 LYS -76.8 179.0 -179.9 -75.7 -176.0 172.6 -67.6 34 LYS -51.8 132.7 -179.0 177.0 178.0 179.9 178.0 35 LEU -104.0 -41.8 -178.1 -57.1 171.8 36 ASP -160.7 -160.9 177.3 -108.1 -44.9 37 VAL -126.6 125.1 -179.7 175.7 38 ARG -127.9 113.0 -179.1 -64.5 -62.2 -178.2 178.8 39 ASP 49.1 59.3 178.9 -62.3 -28.0 40 ALA 63.2 19.4 -179.7 41 ARG -130.2 139.5 178.1 -63.0 157.5 168.6 -76.2 42 ASP -65.5 133.2 -177.2 -65.5 -42.9 43 PHE -101.9 128.2 178.9 -177.7 48.8 44 PHE -130.7 152.3 179.1 -54.4 78.5 45 ILE -119.1 133.1 178.8 -75.5 174.5 46 ASN -110.9 125.4 179.3 176.0 -52.4 47 SER -117.7 120.4 178.9 174.4 48 GLU -97.7 134.0 179.7 173.2 80.3 39.5 49 MET -153.2 163.9 179.0 60.2 174.7 74.7 50 ASP -54.2 144.4 179.8 -65.3 166.9 51 GLU -55.4 -39.9 179.7 -46.6 -145.1 -36.5 52 TYR -56.6 -46.5 -179.6 172.9 64.3 53 ALA -64.9 -37.8 -179.2 54 ALA -65.7 -22.1 179.9 55 ASN -56.7 -25.0 -178.8 -60.7 -39.6 56 ASP -72.6 -14.2 -178.2 -58.0 -31.3 57 PHE -122.2 159.3 179.4 -45.4 89.8 58 LYS -148.4 153.2 178.9 -40.4 -166.3 79.8 59.9 59 THR -51.0 137.3 179.8 -65.3 60 GLY 95.4 -22.9 179.7 61 ASP -61.6 146.9 177.4 -75.8 173.6 62 LYS -92.0 134.8 -178.4 -75.3 62.1 -178.7 179.2 63 ILE -139.4 173.1 178.3 56.0 176.0 64 ALA -121.3 143.0 -179.3 65 VAL -124.6 134.0 177.0 -179.5 66 PHE -145.5 98.2 -177.6 -163.5 -65.9 67 SER -159.3 171.0 179.0 59.9 68 VAL -116.3 134.7 -179.6 59.2 69 PRO -81.2 147.0 178.5 38.5 -44.9 70 PHE -114.2 -2.5 179.4 57.5 77.2 71 ASP -174.8 165.1 -179.9 -150.5 161.8 72 TRP -136.7 154.3 179.5 -68.9 -98.4 73 ASN -118.2 104.0 179.1 -173.2 -53.5 74 TYR -105.5 23.1 -179.1 -71.3 84.1 75 LEU -69.7 -33.6 -179.5 -59.4 176.8 76 SER -93.5 139.7 -179.7 -60.2 77 LYS -64.3 143.9 179.8 -60.8 -178.1 -62.4 -180.0 78 GLY 51.6 23.3 -179.4 79 LYS -145.4 147.2 178.8 176.7 178.7 -179.0 179.8 80 VAL -146.7 127.8 179.2 57.8 81 THR -117.1 126.4 179.1 -66.4 82 ALA -96.1 137.7 179.3 83 TYR -100.3 134.0 -179.1 -63.9 95.9 84 THR -141.5 172.5 177.9 63.8 85 TYR -118.6 122.3 179.1 -81.5 -55.1 86 GLY 53.8 -139.2 -179.7 87 GLY 75.1 18.0 -178.4 88 ILE -106.8 135.2 178.5 -51.7 -60.7 89 THR -138.8 152.6 180.0 49.7 90 PRO -64.0 145.1 179.9 30.1 -43.1 91 TYR -50.5 142.4 179.9 171.7 69.8 92 GLN -131.0 111.3 -179.2 -176.2 179.9 -47.5 93 LYS -54.9 -63.0 -177.9 -57.7 178.5 -179.0 179.5 94 THR -97.2 125.0 179.1 -48.3 95 SER -70.8 130.5 -179.9 174.9 96 ILE -125.5 83.1 -179.9 -54.8 172.3 97 PRO -56.6 128.5 179.7 27.1 -42.1 98 LYS -140.3 139.4 179.1 -66.3 -173.2 179.9 -179.6 99 ASN -96.4 143.6 -180.0 -64.1 -50.4 100 ILE -116.6 117.2 -179.9 -51.8 175.9 101 PRO -58.4 140.0 -179.8 24.6 -39.6 102 VAL -121.6 133.0 177.1 173.2 103 ASN -112.6 113.8 -178.4 -69.2 -38.9 104 LEU -114.5 128.8 178.3 168.0 71.2 105 TRP -126.6 114.1 179.2 -69.6 73.0 106 ILE -112.4 118.4 -178.1 -61.7 -176.9 107 ASN 52.6 44.3 178.3 -82.8 -47.9 108 GLY 83.2 -7.6 -179.8 109 LYS -107.1 122.3 178.9 -171.9 174.2 68.6 170.7 110 GLN -71.2 134.3 -179.0 -177.4 178.9 -68.3 111 ILE -121.3 132.8 -178.9 -60.6 177.0 112 SER -69.1 144.3 179.1 69.7 113 VAL -129.8 126.0 179.9 178.3 114 PRO -46.1 135.3 -178.7 -36.1 45.0 115 TYR -50.4 -33.3 -178.5 77.0 102.9 116 ASN -103.8 27.0 -180.0 65.1 -24.5 117 GLU -68.6 -48.9 -179.1 -170.0 68.0 55.9 118 ILE -112.5 120.7 -179.8 -58.4 -58.1 119 SER -147.2 168.7 179.1 62.7 120 THR -151.8 157.9 179.9 176.7 121 ASN -100.8 -1.9 -177.2 -69.1 156.6 122 LYS -95.3 148.0 177.9 -55.6 -173.8 -178.7 61.1 123 THR -84.4 -29.5 177.0 -63.7 124 THR -123.8 116.5 -177.7 -65.9 125 VAL -126.5 141.5 -179.8 62.7 126 THR -80.2 147.8 177.2 61.7 127 ALA -58.6 -33.0 179.8 128 GLN -58.9 -49.8 179.7 179.3 169.9 3.4 129 GLU -55.6 -48.9 -179.5 -179.2 176.6 -36.4 130 ILE -63.8 -39.2 -179.9 -61.8 169.7 131 ASP -63.7 -45.0 -180.0 -170.0 28.4 132 LEU -62.0 -38.6 179.4 -67.9 167.4 133 LYS -71.2 -41.7 179.3 -71.9 175.7 166.5 174.3 134 VAL -62.7 -50.2 -179.5 166.9 135 ARG -64.0 -35.2 178.8 -56.0 -155.9 -161.5 -164.5 136 LYS -64.6 -42.1 178.8 0.0 0.0 0.0 0.0 137 PHE -62.6 -49.9 -179.7 152.1 61.2 138 LEU -61.7 -38.8 179.3 -62.6 172.0 139 ILE -65.4 -45.5 -178.9 -68.4 170.3 140 ALA -74.9 -32.2 -175.9 141 GLN -107.6 -24.0 -177.3 -58.7 -91.0 69.7 142 HIS -129.8 32.2 176.7 -64.6 -71.1 143 GLN 56.2 15.6 179.6 -54.4 67.6 55.3 144 LEU -57.5 125.6 179.8 -179.2 57.7 145 TYR 72.1 7.6 178.3 -54.6 152.9 146 SER -66.6 147.4 -178.4 165.7 147 SER -67.1 -13.8 178.2 -89.8 148 GLY -111.2 24.9 -179.7 149 SER -93.0 138.3 179.5 167.1 150 SER -89.2 -1.9 -178.8 71.4 151 TYR -61.6 144.3 -179.4 -52.8 -32.3 152 LYS -130.7 -20.6 -178.7 -62.7 -178.3 179.2 -179.6 153 SER -150.2 165.6 -179.5 63.9 154 GLY 172.6 163.0 -178.7 155 ARG -154.9 142.6 177.0 -177.0 170.0 -69.6 -69.3 156 LEU -108.5 116.9 -179.3 162.7 58.7 157 VAL -114.7 132.5 179.2 -179.5 158 PHE -91.1 109.7 -179.0 -68.3 74.7 159 HIS -93.5 93.1 -179.2 -151.1 157.9 160 THR -89.5 -35.7 -101.2 64.3 161 LYS 119.7 -70.9 -179.7 -99.5 62.0 180.0 -179.9 162 TYR -65.3 139.4 -179.7 -169.5 84.3 163 SER -154.2 168.2 177.2 66.5 164 PHE -127.6 139.4 177.2 -68.9 115.4 165 ASP -84.5 116.0 -177.5 178.3 147.5 166 LEU -67.7 -10.6 179.0 -60.0 176.7 167 PHE -121.7 30.7 177.6 -68.3 76.9 168 TYR -78.0 123.6 -178.9 175.7 59.0 169 VAL -109.9 1.5 179.3 -64.5 170 GLY 43.2 -124.2 178.7 171 TYR -104.4 22.7 178.4 -67.5 123.8 172 ARG 65.9 33.9 176.9 -52.6 -139.7 159.7 -134.1 173 ASP -145.0 162.6 -178.7 63.7 8.4 174 LYS -56.4 -43.8 -178.2 -62.9 -176.4 -66.7 -64.1 175 GLU -56.7 -49.2 -179.7 -173.8 -82.4 -32.6 176 SER -70.5 -38.2 -179.5 56.1 177 ILE -70.4 -39.2 179.5 -69.2 174.1 178 PHE -84.2 -3.2 -179.8 -60.6 -27.5 179 LYS -63.7 -18.8 179.2 -170.4 168.8 -177.3 179.6 180 VAL -64.2 -14.9 179.9 -60.1 181 TYR -95.2 -1.0 -178.6 -53.1 -51.5 182 LYS -58.0 -24.4 179.7 -168.2 175.9 -179.3 -174.2 183 ASP -75.1 -11.0 -178.9 60.8 -176.8 184 ASN 56.3 28.2 179.8 -163.0 -119.0 185 LYS -46.8 129.3 -179.5 175.1 65.3 -180.0 174.8 186 SER -136.1 163.5 179.4 -55.7 187 PHE -137.8 149.9 175.6 -49.8 82.6 188 ASN -78.4 127.8 -177.8 171.4 -50.6 189 ILE -52.5 -34.1 -179.4 -168.2 58.8 190 ASP -75.7 -3.2 -179.2 -57.1 -52.9 191 LYS -98.4 -17.9 179.8 -56.2 -65.5 -172.9 174.3 192 ILE -82.8 106.8 179.4 -57.8 -179.5 193 GLY -65.8 -58.8 179.4 194 HIS -167.5 169.2 -179.7 58.1 -79.5 195 LEU -107.7 126.9 178.5 -47.5 171.1 196 ASP -104.5 123.8 -179.5 -67.0 -37.6 197 ILE -120.2 133.0 177.2 -59.0 171.3 198 GLU -130.5 138.9 178.9 59.5 -161.7 110.0 199 ILE -139.6 132.2 -179.3 -58.7 174.7 200 ASP -138.5 154.0 179.6 -62.0 -69.8 201 SER -99.6 19.4 0.0 -64.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP 80.752 5.553 26.014 2 ASN 77.382 7.255 25.696 3 ASN 78.771 10.416 24.105 4 SER 80.443 8.587 21.237 5 LEU 77.344 6.424 20.802 6 LEU 74.856 9.303 20.602 7 ARG 77.149 11.518 18.541 8 ASN 77.471 8.758 15.949 9 ILE 73.806 7.766 16.118 10 TYR 72.609 11.345 15.699 11 SER 75.091 12.101 12.943 12 THR 73.075 9.641 10.830 13 ILE 71.798 11.073 7.531 14 VAL 68.356 12.678 7.635 15 TYR 65.785 11.987 4.908 16 GLU 63.721 14.989 3.859 17 TYR 61.209 14.650 1.014 18 SER 58.145 16.889 0.785 19 ASP 56.337 15.343 -2.182 20 ILE 55.986 11.566 -1.944 21 VAL 53.158 9.141 -2.657 22 ILE 52.308 6.214 -0.388 23 ASP 52.675 3.037 -2.437 24 PHE 51.351 0.605 0.189 25 LYS 49.959 0.951 3.726 26 THR 49.594 -1.609 6.532 27 SER 47.980 -1.338 9.979 28 HIS 51.220 0.123 11.349 29 ASN 53.484 0.586 8.361 30 LEU 53.768 2.771 5.253 31 VAL 55.966 2.326 2.194 32 THR 56.629 5.132 -0.270 33 LYS 56.882 4.896 -4.041 34 LYS 60.340 5.490 -5.532 35 LEU 61.917 8.599 -3.976 36 ASP 65.298 8.807 -5.650 37 VAL 68.225 6.793 -6.894 38 ARG 70.813 5.794 -4.300 39 ASP 74.032 4.123 -5.408 40 ALA 72.482 2.692 -8.593 41 ARG 69.373 1.596 -6.694 42 ASP 65.798 2.885 -6.689 43 PHE 65.235 4.377 -3.244 44 PHE 62.181 3.724 -1.064 45 ILE 61.340 4.533 2.554 46 ASN 59.432 2.262 4.908 47 SER 57.919 3.949 7.968 48 GLU 56.765 1.927 10.965 49 MET 54.426 3.729 13.394 50 ASP 51.756 3.114 16.045 51 GLU 48.513 1.779 14.564 52 TYR 46.750 4.846 15.967 53 ALA 49.103 7.133 14.052 54 ALA 48.752 5.168 10.798 55 ASN 44.984 5.787 10.702 56 ASP 45.828 9.241 9.351 57 PHE 47.222 7.829 6.116 58 LYS 46.039 5.628 3.259 59 THR 47.581 4.168 0.109 60 GLY 47.784 6.846 -2.574 61 ASP 47.998 9.797 -0.180 62 LYS 50.648 12.416 -0.908 63 ILE 52.951 12.927 2.066 64 ALA 56.093 14.604 3.372 65 VAL 58.898 12.714 5.088 66 PHE 61.445 13.963 7.613 67 SER 63.203 11.143 9.435 68 VAL 66.330 9.201 10.273 69 PRO 66.809 5.522 9.216 70 PHE 67.760 2.658 11.547 71 ASP 68.416 0.050 8.870 72 TRP 68.402 -0.617 5.124 73 ASN 67.303 -3.445 2.862 74 TYR 69.722 -4.117 0.008 75 LEU 68.258 -7.577 -0.616 76 SER 66.537 -6.618 -3.884 77 LYS 68.475 -5.768 -7.053 78 GLY 68.545 -2.151 -8.208 79 LYS 66.508 -1.324 -5.117 80 VAL 67.096 -0.111 -1.579 81 THR 64.555 0.413 1.184 82 ALA 65.389 2.425 4.293 83 TYR 63.560 1.590 7.504 84 THR 62.417 4.424 9.739 85 TYR 60.013 5.223 12.562 86 GLY 57.320 7.815 11.890 87 GLY 58.383 11.167 10.481 88 ILE 55.319 11.322 8.228 89 THR 53.060 14.329 7.632 90 PRO 50.378 15.062 5.015 91 TYR 51.548 16.695 1.778 92 GLN 51.721 20.503 1.838 93 LYS 51.574 22.406 -1.446 94 THR 52.924 25.757 -0.257 95 SER 55.943 26.017 2.057 96 ILE 55.392 28.287 5.070 97 PRO 58.739 28.867 6.855 98 LYS 58.360 29.473 10.587 99 ASN 60.851 29.933 13.414 100 ILE 60.283 28.279 16.790 101 PRO 61.688 30.083 19.853 102 VAL 64.126 28.052 21.922 103 ASN 64.878 28.363 25.633 104 LEU 68.168 26.642 26.458 105 TRP 69.559 26.003 29.949 106 ILE 72.925 24.257 30.240 107 ASN 73.987 23.380 33.788 108 GLY 71.527 25.882 35.233 109 LYS 72.552 28.781 32.995 110 GLN 70.195 30.058 30.316 111 ILE 72.001 30.527 27.001 112 SER 70.623 32.664 24.166 113 VAL 69.659 30.977 20.906 114 PRO 69.179 32.919 17.630 115 TYR 65.475 33.442 16.895 116 ASN 65.850 31.575 13.585 117 GLU 67.961 28.677 14.868 118 ILE 65.133 26.141 14.747 119 SER 62.544 26.379 11.978 120 THR 60.256 24.349 9.708 121 ASN 58.245 24.811 6.489 122 LYS 55.363 22.643 7.700 123 THR 51.978 23.538 9.158 124 THR 51.970 20.075 10.705 125 VAL 55.420 19.038 11.914 126 THR 56.660 15.916 13.687 127 ALA 58.385 15.997 17.056 128 GLN 60.999 13.922 15.205 129 GLU 61.830 16.664 12.701 130 ILE 62.278 19.232 15.472 131 ASP 64.341 16.830 17.628 132 LEU 66.733 16.086 14.764 133 LYS 67.161 19.810 14.109 134 VAL 67.600 20.639 17.794 135 ARG 70.229 17.944 18.394 136 LYS 72.154 18.842 15.234 137 PHE 72.226 22.432 16.495 138 LEU 73.274 21.392 20.019 139 ILE 75.978 19.058 18.714 140 ALA 77.492 21.718 16.477 141 GLN 77.066 24.644 18.873 142 HIS 76.958 23.359 22.446 143 GLN 79.225 20.324 22.549 144 LEU 76.330 17.879 22.905 145 TYR 77.734 14.321 22.663 146 SER 81.319 15.589 22.204 147 SER 83.890 13.087 23.535 148 GLY 85.283 15.652 25.951 149 SER 81.844 16.664 27.225 150 SER 80.826 16.501 30.871 151 TYR 77.063 16.376 30.117 152 LYS 75.146 13.449 31.639 153 SER 71.478 14.355 31.229 154 GLY 69.084 16.539 29.291 155 ARG 65.624 16.870 27.820 156 LEU 63.877 18.560 24.903 157 VAL 60.385 19.631 25.937 158 PHE 57.730 20.893 23.551 159 HIS 55.969 23.767 25.281 160 THR 52.673 23.986 23.404 161 LYS 54.358 18.452 27.796 162 TYR 55.696 16.094 25.128 163 SER 59.441 15.507 25.418 164 PHE 62.505 13.440 24.499 165 ASP 65.288 12.327 26.880 166 LEU 68.473 13.594 25.205 167 PHE 70.548 10.819 26.734 168 TYR 68.340 7.816 26.054 169 VAL 70.613 5.043 24.773 170 GLY 68.093 2.199 24.404 171 TYR 69.933 -0.978 23.419 172 ARG 72.766 1.061 21.920 173 ASP 71.677 0.859 18.281 174 LYS 69.680 3.071 15.911 175 GLU 66.502 0.981 15.974 176 SER 66.024 1.163 19.748 177 ILE 67.127 4.800 20.018 178 PHE 64.910 6.025 17.160 179 LYS 62.001 3.926 18.405 180 VAL 60.963 6.991 20.416 181 TYR 59.645 8.380 17.108 182 LYS 57.327 5.409 16.432 183 ASP 54.298 7.353 17.689 184 ASN 54.703 9.801 14.770 185 LYS 53.904 12.566 17.275 186 SER 53.124 15.770 15.379 187 PHE 52.057 19.346 16.124 188 ASN 50.099 22.116 14.415 189 ILE 52.837 24.746 14.046 190 ASP 50.659 27.456 15.610 191 LYS 50.329 25.319 18.741 192 ILE 54.023 25.074 19.617 193 GLY 54.769 27.951 21.967 194 HIS 58.468 27.212 22.302 195 LEU 61.008 24.482 22.929 196 ASP 62.598 24.188 26.358 197 ILE 65.965 22.452 26.417 198 GLU 67.944 21.482 29.490 199 ILE 71.341 19.771 29.545 200 ASP 73.230 19.040 32.760 201 SER 76.499 17.505 33.899 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H/S S S S S S S S/S S 20 S S S S C T T T T/S S 30 S S S S C C T T T T/S 40 S S S S S S S S S S/H 50 H H H H H S S S S S/S 60 S S S S S S S S S S 70 S/S S S S C T T T T/S S 80 S S S S S S S S S S 90 S/S S S S/S S S S S S S 100 S S S S S/T T T T/S S S 110 S S S S C C S S S S 120 S S S S S S/H H H H H 130 H H H H H H H H H H 140 H H C C C C C C C S 150 S S S/S S S S S S S S/X 160 X/S S S S S S C C T T 170 T T H H H H H H H C 180 T T T T/S S S S S/T T T 190 T C S S S S S S S S 200 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H H H h 10 T t E E E E E E 20 E E E E E E T e E E 30 E E e E E E T T 40 E E E E E E E E e h 50 H H H H h T t t T T 60 e E E E E E E e E E 70 E E E t T e E E 80 E E E E E e e E E E 90 e S S E E e 100 e E E E E E e T E E 110 E t T T t e E E 120 S e E E E H H H H 130 H H H H H H H H H H 140 H h t T T t T T t 150 E E E E E E E 160 e E E E e T t t T 170 T t h H H H H H h G 180 G g T t e E E E e G 190 G g E E E E E E E 200 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 34.2 30.9 83.8 2 ASN 57.3 47.4 66.0 3 ASN 99.9 82.6 68.7 4 SER 51.6 61.8 85.1 5 LEU 119.0 80.5 53.1 6 LEU 147.7 100.0 38.9 7 ARG 139.2 66.6 63.8 8 ASN 38.7 32.0 82.0 9 ILE 128.1 89.3 38.9 10 TYR 177.9 98.3 43.7 11 SER 26.5 31.7 83.8 12 THR 87.4 81.7 53.4 13 ILE 54.0 37.7 69.1 14 VAL 80.2 67.5 52.8 15 TYR 168.2 92.9 39.6 16 GLU 50.2 36.2 71.2 17 TYR 146.6 81.0 54.4 18 SER 18.1 21.6 72.7 19 ASP 36.5 33.0 71.6 20 ILE 136.2 94.9 45.3 21 VAL 80.1 67.4 52.0 22 ILE 143.4 99.9 40.9 23 ASP 76.6 69.3 55.6 24 PHE 30.6 18.3 81.7 25 LYS 140.8 81.2 62.1 26 THR 29.6 27.7 77.9 27 SER 30.5 36.5 72.3 28 HIS 79.4 52.9 73.1 29 ASN 98.5 81.5 62.6 30 LEU 146.9 99.4 34.7 31 VAL 77.9 65.6 67.3 32 THR 105.1 98.3 38.9 33 LYS 74.2 42.8 70.1 34 LYS 86.8 50.1 63.3 35 LEU 142.6 96.5 36.9 36 ASP 53.6 48.5 62.8 37 VAL 46.7 39.3 71.6 38 ARG 104.8 50.2 66.1 39 ASP 0.5 0.4 83.9 40 ALA 2.7 3.7 76.7 41 ARG 147.7 70.7 64.7 42 ASP 62.8 56.8 59.5 43 PHE 164.7 98.7 41.6 44 PHE 134.5 80.6 53.0 45 ILE 143.5 100.0 32.6 46 ASN 99.7 82.4 50.6 47 SER 82.6 98.8 55.6 48 GLU 101.1 72.9 63.5 49 MET 159.4 100.0 43.2 50 ASP 54.9 49.7 58.8 51 GLU 45.5 32.8 78.6 52 TYR 3.2 1.7 86.3 53 ALA 63.9 88.0 59.7 54 ALA 72.5 99.8 59.0 55 ASN 37.0 30.6 80.0 56 ASP 23.8 21.6 75.1 57 PHE 159.0 95.3 44.9 58 LYS 45.5 26.2 78.0 59 THR 45.9 43.0 68.9 60 GLY 9.3 26.6 69.3 61 ASP 58.6 53.1 62.1 62 LYS 68.2 39.3 69.4 63 ILE 142.7 99.5 31.4 64 ALA 69.3 95.5 57.5 65 VAL 118.7 99.9 41.7 66 PHE 154.9 92.9 51.3 67 SER 83.6 100.0 51.5 68 VAL 117.8 99.1 36.9 69 PRO 124.5 100.0 43.5 70 PHE 143.9 86.3 41.4 71 ASP 35.9 32.5 63.5 72 TRP 145.5 71.0 52.8 73 ASN 82.9 68.6 60.3 74 TYR 85.9 47.5 71.6 75 LEU 18.3 12.4 89.9 76 SER 30.3 36.3 74.0 77 LYS 0.0 0.0 93.2 78 GLY 9.7 28.0 73.5 79 LYS 90.1 51.9 66.3 80 VAL 116.3 97.9 41.9 81 THR 91.6 85.7 46.5 82 ALA 72.6 100.0 38.1 83 TYR 120.0 66.3 62.4 84 THR 106.8 99.9 48.7 85 TYR 167.0 92.3 45.7 86 GLY 34.8 100.0 64.6 87 GLY 34.8 100.0 62.7 88 ILE 142.9 99.6 33.5 89 THR 104.3 97.6 41.4 90 PRO 51.2 41.2 63.9 91 TYR 120.4 66.5 63.8 92 GLN 112.3 75.6 65.1 93 LYS 19.6 11.3 84.1 94 THR 11.6 10.9 80.1 95 SER 35.6 42.6 73.9 96 ILE 67.0 46.7 71.5 97 PRO 45.1 36.2 82.0 98 LYS 112.5 64.9 64.4 99 ASN 72.9 60.3 59.9 100 ILE 140.2 97.7 34.4 101 PRO 52.7 42.3 74.7 102 VAL 117.9 99.2 39.3 103 ASN 65.4 54.1 71.4 104 LEU 147.8 100.0 33.7 105 TRP 89.3 43.6 72.0 106 ILE 131.0 91.3 48.4 107 ASN 65.3 54.0 69.7 108 GLY 0.8 2.3 72.5 109 LYS 30.0 17.3 82.1 110 GLN 58.4 39.3 68.6 111 ILE 99.8 69.5 59.6 112 SER 0.0 0.0 83.3 113 VAL 118.5 99.7 44.5 114 PRO 50.6 40.7 78.6 115 TYR 26.1 14.4 86.5 116 ASN 54.3 44.9 70.4 117 GLU 104.5 75.4 49.5 118 ILE 140.9 98.2 36.7 119 SER 47.9 57.3 72.4 120 THR 104.1 97.4 54.4 121 ASN 51.5 42.6 70.0 122 LYS 152.2 87.8 62.0 123 THR 56.1 52.5 68.4 124 THR 62.7 58.7 54.5 125 VAL 118.8 100.0 41.1 126 THR 105.2 98.4 56.4 127 ALA 71.6 98.6 34.0 128 GLN 145.7 98.0 43.7 129 GLU 137.2 99.0 47.2 130 ILE 142.6 99.3 23.9 131 ASP 110.5 100.0 43.8 132 LEU 141.4 95.7 41.7 133 LYS 118.2 68.1 59.2 134 VAL 118.8 100.0 24.6 135 ARG 202.9 97.1 45.0 136 LYS 120.8 69.7 75.7 137 PHE 153.4 92.0 42.8 138 LEU 147.8 100.0 23.5 139 ILE 107.2 74.7 55.0 140 ALA 15.3 21.1 78.2 141 GLN 61.7 41.5 74.4 142 HIS 121.8 81.1 46.3 143 GLN 48.4 32.6 79.4 144 LEU 147.8 100.0 29.5 145 TYR 181.0 100.0 37.0 146 SER 41.3 49.3 68.4 147 SER 34.1 40.8 83.4 148 GLY 0.0 0.0 85.5 149 SER 77.0 92.1 64.0 150 SER 15.1 18.0 81.3 151 TYR 162.1 89.6 56.1 152 LYS 32.8 18.9 85.2 153 SER 30.9 36.9 69.1 154 GLY 32.5 93.4 46.5 155 ARG 119.5 57.2 67.9 156 LEU 147.8 100.0 31.1 157 VAL 87.0 73.3 62.6 158 PHE 166.8 100.0 27.9 159 HIS 66.5 44.3 79.4 160 THR 68.2 63.8 51.1 161 LYS 0.0 0.0 93.4 162 TYR 130.4 72.1 53.0 163 SER 69.2 82.8 54.8 164 PHE 158.5 95.0 50.7 165 ASP 59.2 53.5 71.9 166 LEU 147.8 100.0 46.5 167 PHE 151.6 90.9 52.2 168 TYR 87.2 48.2 70.6 169 VAL 87.8 73.9 57.6 170 GLY 29.8 85.5 54.5 171 TYR 10.2 5.6 84.7 172 ARG 104.6 50.0 67.7 173 ASP 45.3 41.0 71.3 174 LYS 115.6 66.7 54.4 175 GLU 78.3 56.5 60.2 176 SER 78.0 93.3 59.8 177 ILE 141.3 98.5 44.4 178 PHE 166.6 99.9 37.9 179 LYS 73.7 42.5 74.8 180 VAL 73.0 61.5 58.4 181 TYR 178.4 98.6 48.5 182 LYS 114.9 66.2 64.8 183 ASP 71.3 64.5 68.7 184 ASN 112.4 93.0 52.0 185 LYS 97.7 56.4 61.3 186 SER 65.8 78.7 56.9 187 PHE 152.7 91.5 36.8 188 ASN 62.2 51.4 62.6 189 ILE 138.6 96.6 46.0 190 ASP 32.8 29.7 80.8 191 LYS 44.6 25.7 79.1 192 ILE 143.4 99.9 32.2 193 GLY 5.6 16.1 82.5 194 HIS 107.0 71.2 60.1 195 LEU 147.8 100.0 26.3 196 ASP 72.0 65.1 62.4 197 ILE 143.5 100.0 29.3 198 GLU 59.0 42.6 66.8 199 ILE 143.5 100.0 27.7 200 ASP 62.6 56.7 77.6 201 SER 66.5 79.6 69.2