Protein Data Bank File : 1aiph Title : COMPLEX OF TWO ELONGATION FACTORS 22-APR-97 1AIP Number of Amino Acid Residues : 194 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLN MET GLU LEU ILE LYS LYS LEU ARG GLU 10 ALA THR GLY ALA GLY MET MET ASP VAL LYS 20 ARG ALA LEU GLU ASP ALA GLY TRP ASP GLU 30 GLU LYS ALA VAL GLN LEU LEU ARG GLU ARG 40 GLY ALA MET LYS ALA ALA LYS LYS ALA ASP 50 ARG GLU ALA ARG GLU GLY ILE ILE GLY HIS 60 TYR ILE HIS HIS ASN GLN ARG VAL GLY VAL 70 LEU VAL GLU LEU ASN CYS GLU THR ASP PHE 80 VAL ALA ARG ASN GLU LEU PHE GLN ASN LEU 90 ALA LYS ASP LEU ALA MET HIS ILE ALA MET 100 MET ASN PRO ARG TYR VAL SER ALA GLU GLU 110 ILE PRO ALA GLU GLU LEU GLU LYS GLU ARG 120 GLN ILE TYR ILE GLN ALA ALA LEU ASN GLU 130 GLY LYS PRO GLN GLN ILE ALA GLU LYS ILE 140 ALA GLU GLY ARG LEU LYS LYS TYR LEU GLU 150 GLU VAL VAL LEU LEU GLU GLN PRO PHE VAL 160 LYS ASP ASP LYS VAL LYS VAL LYS GLU LEU 170 ILE GLN GLN ALA ILE ALA LYS ILE GLY GLU 180 ASN ILE VAL VAL ARG ARG PHE CYS ARG PHE 190 GLU LEU GLY ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLN 0.0 158.0 -179.4 128.7 -83.4 113.4 2 MET -121.9 -27.5 -179.8 -155.1 -144.0 54.3 3 GLU -80.2 21.2 178.7 -126.4 70.5 -10.1 4 LEU -116.5 21.7 176.8 0.0 0.0 5 ILE -143.2 -27.8 179.8 -72.4 -170.8 6 LYS -79.6 -28.8 -179.8 122.6 76.8 136.3 -61.9 7 LYS -95.6 -29.4 178.7 -49.2 -116.1 142.0 -67.4 8 LEU -85.0 -23.4 177.4 -113.5 -127.7 9 ARG -90.2 -24.9 178.9 153.9 151.1 -158.1 -72.6 10 GLU -65.9 -41.3 -179.1 140.3 58.9 30.2 11 ALA -80.6 -68.2 -179.4 12 THR -66.4 -10.0 -179.4 38.7 13 GLY 48.4 52.0 -179.7 14 ALA -110.0 -174.4 -179.0 15 GLY -63.8 125.0 179.7 16 MET -38.4 -56.2 -180.0 -165.9 50.1 92.4 17 MET -69.1 -33.1 179.3 -74.0 -51.8 -71.3 18 ASP -64.7 -33.4 179.1 -78.8 -32.3 19 VAL -66.8 -44.8 179.6 -172.4 20 LYS -62.0 -58.7 179.5 -144.4 -173.8 -147.9 -138.5 21 ARG -42.1 -57.3 179.7 -117.8 107.5 50.0 177.8 22 ALA -56.2 -49.7 179.5 23 LEU -55.6 -39.1 178.8 -79.0 133.1 24 GLU -70.2 -60.9 -179.4 -65.5 176.0 -32.2 25 ASP -49.8 -10.4 -179.4 -76.8 86.1 26 ALA -156.3 55.5 179.3 27 GLY 54.5 132.0 -178.6 28 TRP -72.8 55.4 178.2 -73.5 66.1 29 ASP -101.3 123.3 180.0 171.1 32.3 30 GLU -39.4 -22.9 -178.8 161.7 71.2 82.0 31 GLU -104.9 -56.4 -179.9 -116.4 96.8 -0.8 32 LYS -58.0 -3.2 179.6 0.0 0.0 0.0 0.0 33 ALA -79.4 -64.5 -179.7 34 VAL -53.4 -44.9 -179.1 -58.8 35 GLN -57.5 -30.0 177.7 -122.8 -59.0 -52.2 36 LEU -72.8 -47.3 -179.7 -155.7 47.9 37 LEU -51.4 -58.5 179.2 -73.5 -165.9 38 ARG -54.1 -48.4 -179.2 -63.9 -180.0 30.7 156.6 39 GLU -58.2 -31.7 179.6 -120.3 158.9 -13.4 40 ARG -85.0 -32.4 178.7 0.0 0.0 0.0 0.0 41 GLY -51.6 -39.3 179.8 42 ALA -53.4 -33.3 -179.8 43 MET -70.1 -54.4 179.9 -92.9 144.2 -94.4 44 LYS -44.2 -46.8 179.8 -23.9 -112.0 -115.5 -164.4 45 ALA -53.9 -54.1 -179.4 46 ALA -64.0 -7.6 -179.8 47 LYS -92.5 -41.2 178.8 -88.0 -154.9 -79.5 -164.7 48 LYS -85.3 -14.0 -178.7 -41.9 -122.9 150.3 -13.2 49 ALA -44.9 -13.3 179.3 50 ASP -117.1 -8.9 179.0 -86.1 -47.0 51 ARG -60.9 145.9 -179.5 -75.6 -122.5 -77.3 -89.9 52 GLU -75.6 132.9 180.0 -91.2 -104.4 -75.6 53 ALA -134.1 102.7 -179.7 54 ARG -117.0 3.8 178.1 -112.0 79.9 129.3 -70.2 55 GLU -91.8 -170.7 179.4 -89.5 -51.4 -44.2 56 GLY 116.4 -159.1 -179.5 57 ILE -146.9 -178.3 178.2 69.2 175.6 58 ILE -109.6 110.0 -179.7 -60.4 -75.6 59 GLY -86.3 157.3 -179.9 60 HIS -151.6 156.5 176.7 75.8 -60.0 61 TYR -146.3 125.2 178.4 175.7 69.2 62 ILE -118.8 114.2 -179.3 -62.3 -53.2 63 HIS -52.3 152.9 -179.2 -154.8 22.5 64 HIS -56.7 -34.5 179.7 60.7 85.0 65 ASN -90.0 8.7 179.2 72.4 20.3 66 GLN 58.7 15.5 -179.6 -45.1 -176.4 -66.1 67 ARG -90.6 -11.2 178.3 -72.0 -172.4 78.3 92.7 68 VAL -140.3 133.3 -179.4 -179.3 69 GLY -138.4 145.6 -178.0 70 VAL -136.3 139.3 177.6 155.5 71 LEU -116.3 145.7 178.2 -88.7 -167.5 72 VAL -152.5 123.6 -179.9 68.7 73 GLU -91.3 112.2 179.5 -172.4 177.5 -22.3 74 LEU -111.6 114.7 -179.5 -167.1 66.0 75 ASN -100.3 145.9 174.9 -58.4 140.9 76 CYS -134.4 -175.5 -178.5 55.8 77 GLU -87.0 -46.8 179.9 -56.2 -161.7 63.3 78 THR -113.2 148.3 -179.8 84.9 79 ASP -71.2 -12.1 178.8 78.0 26.0 80 PHE -65.2 -46.7 179.2 -85.8 -66.8 81 VAL -63.3 -49.4 179.1 148.4 82 ALA -44.8 -43.4 -179.4 83 ARG -73.6 -14.9 -178.6 -57.0 176.0 97.7 98.1 84 ASN -68.3 132.6 -179.6 -179.6 -123.4 85 GLU -41.6 -33.3 -179.2 -160.5 -127.8 17.3 86 LEU -72.7 -40.9 178.7 -90.8 59.6 87 PHE -64.5 -49.8 179.5 -164.8 66.2 88 GLN -48.0 -57.8 -178.8 -66.3 -66.5 149.2 89 ASN -60.4 -49.2 179.2 -63.9 -20.3 90 LEU -49.7 -43.0 179.5 165.5 50.5 91 ALA -65.9 -49.2 179.4 92 LYS -54.5 -48.8 -178.5 -81.6 -29.8 114.8 -160.4 93 ASP -63.0 -39.9 178.1 -69.5 -13.9 94 LEU -64.8 -43.6 179.4 -74.3 165.3 95 ALA -58.3 -48.7 179.6 96 MET -56.7 -49.3 179.7 -165.0 164.4 -35.3 97 HIS -52.1 -53.1 -179.7 178.4 -85.9 98 ILE -56.3 -43.1 -179.4 -47.4 -173.3 99 ALA -50.6 -44.8 -179.0 100 MET -81.7 -58.0 -177.8 -178.0 57.1 -121.9 101 MET -68.1 -16.6 179.9 -109.4 40.6 145.3 102 ASN 42.3 59.1 179.8 -172.5 25.8 103 PRO -63.7 164.9 179.2 23.0 -34.4 104 ARG -107.9 -33.3 179.4 -149.7 -134.9 -128.9 -140.2 105 TYR -125.9 168.5 178.6 -56.5 90.0 106 VAL -89.9 -63.4 -179.3 -173.0 107 SER -114.7 171.1 179.5 68.7 108 ALA -67.2 -52.1 179.7 109 GLU -54.0 -19.0 179.4 32.9 -80.3 -57.0 110 GLU -62.1 -14.1 -178.9 -168.0 152.1 -57.3 111 ILE -96.9 123.9 179.3 -43.9 179.0 112 PRO -64.3 143.5 -179.2 21.1 -32.0 113 ALA -60.4 -47.2 -179.7 114 GLU -58.6 -7.1 178.6 75.1 -79.9 18.1 115 GLU -92.1 -38.4 178.6 -126.5 -71.4 -75.7 116 LEU -68.3 -36.9 -179.9 -75.0 114.0 117 GLU -62.2 -51.3 179.6 -82.9 -3.3 77.7 118 LYS -50.4 -32.8 -179.7 0.0 0.0 0.0 0.0 119 GLU -86.2 -68.1 -179.5 -81.9 -77.7 -36.9 120 ARG -36.4 -34.5 -179.1 165.6 156.2 10.7 132.5 121 GLN -76.4 -16.8 177.3 -86.3 -3.0 107.7 122 ILE -89.8 -6.4 179.2 -53.6 173.4 123 TYR -83.2 -28.1 -179.1 -88.1 47.0 124 ILE -97.6 -20.7 -179.7 -26.2 -95.7 125 GLN -63.7 -48.9 180.0 -129.4 94.2 -11.8 126 ALA -95.3 15.5 177.7 127 ALA -111.5 -58.8 178.8 128 LEU -68.1 -7.2 179.8 165.1 52.8 129 ASN -75.8 -91.4 180.0 -121.2 -113.3 130 GLU -72.2 80.5 179.9 24.2 82.3 -82.8 131 GLY 102.3 -132.0 179.4 132 LYS 0.8 127.1 179.7 -29.8 78.6 -176.0 69.6 133 PRO -73.3 -135.7 179.3 27.5 -32.4 134 GLN -104.1 -44.9 179.7 168.6 -74.5 133.8 135 GLN -50.7 -40.6 179.9 0.0 0.0 0.0 136 ILE -90.2 -37.1 180.0 -37.6 -176.5 137 ALA -67.2 -39.5 179.1 138 GLU -75.5 -2.8 179.1 0.0 0.0 0.0 139 LYS -109.1 -22.3 178.7 -134.2 -92.6 135.0 -116.8 140 ILE -89.4 -24.8 178.8 -95.5 141.5 141 ALA -84.9 -36.6 179.4 142 GLU -58.8 -18.3 -179.3 0.0 0.0 0.0 143 GLY -111.2 -6.0 179.7 144 ARG -85.1 -33.5 178.8 -165.6 -118.0 -124.6 104.6 145 LEU -52.7 -38.8 178.9 -99.3 -161.2 146 LYS -50.9 -47.7 179.7 168.1 154.6 -179.0 -42.1 147 LYS -56.9 -46.8 179.6 -161.9 176.8 142.2 -103.8 148 TYR -54.1 -50.9 179.3 178.7 74.4 149 LEU -61.3 -34.1 179.8 -58.7 -176.9 150 GLU -66.4 -16.9 -179.2 -44.4 -132.8 -26.2 151 GLU -94.2 -54.6 -177.7 -58.6 174.4 -0.1 152 VAL -84.8 -24.1 -178.4 -43.4 153 VAL -97.0 118.4 -178.9 172.5 154 LEU -46.6 -50.0 -178.9 163.9 56.2 155 LEU -61.8 -39.2 -178.1 -84.8 -18.5 156 GLU -82.8 -5.8 -180.0 -48.9 -51.9 -27.3 157 GLN -75.0 145.7 179.6 -81.0 177.7 -6.8 158 PRO -75.1 120.7 -178.6 29.1 -35.2 159 PHE -47.2 126.9 -179.2 -175.0 46.4 160 VAL -57.2 -19.5 179.5 102.1 161 LYS -108.4 6.1 178.8 -70.2 -137.3 -136.2 -155.8 162 ASP -172.6 83.7 -178.9 -178.0 -0.3 163 ASP -56.0 -7.5 -179.9 48.2 -28.4 164 LYS -76.0 -27.2 -179.7 0.0 0.0 0.0 0.0 165 VAL -118.3 141.6 179.3 -24.6 166 LYS -78.3 150.1 -179.4 -75.6 -177.8 164.3 -173.9 167 VAL -45.8 -57.9 -179.6 170.5 168 LYS -40.8 -48.2 -179.7 48.7 -154.2 -61.8 -177.8 169 GLU -56.3 -47.1 -179.4 -80.9 178.9 64.6 170 LEU -53.4 -41.6 -179.2 172.9 38.5 171 ILE -66.0 -57.7 179.8 -76.8 168.1 172 GLN -45.8 -48.5 179.3 -67.9 159.1 12.2 173 GLN -51.8 -45.2 179.7 -135.3 30.3 47.0 174 ALA -61.4 -56.6 179.5 175 ILE -42.6 -48.3 -179.7 -71.5 174.5 176 ALA -53.5 -52.6 -179.1 177 LYS -69.0 -18.2 -178.4 3.3 -169.3 102.8 -153.2 178 ILE -101.6 -50.9 179.2 -85.7 103.8 179 GLY 99.4 14.5 179.3 180 GLU -126.8 136.7 179.3 -76.5 -168.6 31.9 181 ASN -60.2 134.6 179.6 178.4 -142.3 182 ILE -122.4 121.7 -178.1 -59.5 -170.9 183 VAL -125.3 153.7 178.8 166.6 184 VAL -104.2 97.9 -178.2 172.2 185 ARG -63.0 -47.7 -178.4 -162.8 71.6 42.5 -165.5 186 ARG -171.8 159.9 178.6 38.4 172.3 179.8 163.5 187 PHE -134.7 162.6 -178.8 54.1 87.3 188 CYS -140.2 130.3 -179.1 -165.1 189 ARG -136.3 121.8 177.6 178.3 -176.1 -175.5 -72.7 190 PHE -117.1 127.7 176.9 -73.4 1.4 191 GLU -119.5 122.9 -178.6 172.7 167.2 21.1 192 LEU -47.5 127.2 -179.7 -159.3 49.2 193 GLY 54.7 49.9 -179.1 194 ALA 179.6 49.4 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLN -26.165 41.711 -1.226 2 MET -27.060 40.979 2.400 3 GLU -23.863 39.804 4.083 4 LEU -22.425 43.359 3.916 5 ILE -24.518 44.742 6.806 6 LYS -24.838 41.466 8.768 7 LYS -21.073 41.102 8.965 8 LEU -20.320 44.847 9.324 9 ARG -23.058 45.245 11.961 10 GLU -21.879 41.977 13.539 11 ALA -18.457 43.542 14.119 12 THR -18.967 47.277 14.814 13 GLY -22.246 46.424 16.575 14 ALA -24.053 49.487 15.169 15 GLY -27.554 50.381 13.964 16 MET -29.094 47.975 11.448 17 MET -30.207 50.914 9.348 18 ASP -27.017 52.812 10.165 19 VAL -25.044 49.977 8.583 20 LYS -27.022 50.210 5.322 21 ARG -26.860 54.005 5.018 22 ALA -23.061 54.152 5.387 23 LEU -22.471 51.272 2.943 24 GLU -24.723 53.238 0.595 25 ASP -23.329 56.670 1.491 26 ALA -19.839 55.458 0.534 27 GLY -19.712 52.567 -1.950 28 TRP -20.370 49.033 -0.781 29 ASP -16.672 48.356 -0.078 30 GLU -15.895 46.216 2.988 31 GLU -13.452 48.952 4.220 32 LYS -14.615 52.488 3.276 33 ALA -17.651 51.207 5.183 34 VAL -16.432 50.860 8.790 35 GLN -14.513 54.177 8.685 36 LEU -17.742 56.001 7.979 37 LEU -19.376 54.098 10.885 38 ARG -16.641 54.922 13.349 39 GLU -16.622 58.549 12.070 40 ARG -20.381 58.925 12.654 41 GLY -20.165 57.165 16.004 42 ALA -18.284 60.271 17.134 43 MET -21.468 62.279 16.556 44 LYS -23.826 60.095 18.588 45 ALA -21.481 60.629 21.509 46 ALA -21.633 64.438 21.329 47 LYS -25.454 64.120 21.315 48 LYS -25.830 62.053 24.481 49 ALA -22.859 64.053 25.741 50 ASP -25.157 66.077 27.953 51 ARG -27.552 63.402 29.227 52 GLU -27.328 62.753 32.993 53 ALA -25.414 59.636 33.963 54 ARG -25.327 58.740 37.626 55 GLU -25.361 54.974 37.235 56 GLY -22.291 52.851 36.591 57 ILE -19.556 51.367 38.732 58 ILE -16.187 51.867 40.322 59 GLY -13.504 50.329 38.169 60 HIS -10.148 49.294 39.588 61 TYR -6.759 47.942 38.702 62 ILE -4.234 46.553 41.118 63 HIS -0.852 45.846 39.546 64 HIS 0.375 42.284 39.913 65 ASN 3.110 43.462 42.324 66 GLN 0.690 45.604 44.383 67 ARG 2.837 48.712 43.903 68 VAL 0.265 50.621 41.865 69 GLY -3.477 50.852 42.303 70 VAL -6.219 52.748 40.534 71 LEU -9.827 53.652 41.232 72 VAL -12.136 54.999 38.532 73 GLU -15.773 56.116 38.561 74 LEU -17.456 55.210 35.308 75 ASN -21.050 56.395 34.955 76 CYS -23.711 55.288 32.494 77 GLU -27.440 56.054 32.385 78 THR -29.069 52.766 33.437 79 ASP -27.705 50.169 35.828 80 PHE -28.624 47.599 33.175 81 VAL -25.821 48.942 31.059 82 ALA -23.543 49.183 34.081 83 ARG -23.852 45.388 34.460 84 ASN -23.003 44.721 30.801 85 GLU -19.809 42.897 29.925 86 LEU -18.801 45.804 27.698 87 PHE -19.104 48.447 30.381 88 GLN -17.271 46.102 32.700 89 ASN -14.373 45.648 30.313 90 LEU -14.252 49.285 29.319 91 ALA -13.894 50.073 33.014 92 LYS -11.211 47.429 33.692 93 ASP -9.308 48.724 30.658 94 LEU -9.615 52.367 31.613 95 ALA -8.288 51.614 35.138 96 MET -5.384 49.693 33.683 97 HIS -4.633 52.573 31.279 98 ILE -4.509 55.143 34.062 99 ALA -2.226 52.905 36.078 100 MET 0.303 53.170 33.247 101 MET -0.306 56.534 31.616 102 ASN -0.783 58.364 34.933 103 PRO -3.035 61.159 33.672 104 ARG -3.476 64.323 35.744 105 TYR -6.932 65.326 34.485 106 VAL -9.911 63.549 33.056 107 SER -10.877 66.107 30.429 108 ALA -9.386 69.305 29.023 109 GLU -11.995 71.726 30.445 110 GLU -10.949 70.222 33.767 111 ILE -8.057 72.668 33.418 112 PRO -8.260 76.269 34.674 113 ALA -7.138 78.760 31.998 114 GLU -4.626 80.575 34.261 115 GLU -2.956 77.195 34.507 116 LEU -2.729 77.007 30.739 117 GLU -1.398 80.575 30.807 118 LYS 1.391 79.766 33.254 119 GLU 2.345 77.144 30.670 120 ARG 1.574 78.520 27.188 121 GLN 3.848 81.467 28.022 122 ILE 6.761 79.144 28.700 123 TYR 5.885 77.884 25.220 124 ILE 6.822 81.255 23.741 125 GLN 9.789 82.012 26.026 126 ALA 12.058 79.327 24.556 127 ALA 10.465 79.713 21.096 128 LEU 10.673 83.491 20.619 129 ASN 14.074 83.005 22.265 130 GLU 16.429 81.033 20.019 131 GLY 15.085 82.331 16.710 132 LYS 11.351 82.492 15.907 133 PRO 9.573 85.802 16.689 134 GLN 6.109 85.885 18.296 135 GLN 3.872 85.565 15.239 136 ILE 5.598 82.202 14.628 137 ALA 6.496 81.231 18.230 138 GLU 2.906 81.754 19.414 139 LYS 2.062 79.546 16.393 140 ILE 4.754 76.965 17.152 141 ALA 3.507 77.055 20.758 142 GLU -0.130 76.966 19.674 143 GLY 0.725 73.481 18.401 144 ARG 3.014 72.151 21.135 145 LEU 0.218 72.362 23.710 146 LYS -1.541 69.600 21.843 147 LYS 1.360 67.360 22.898 148 TYR 0.978 68.518 26.517 149 LEU -2.708 67.602 26.669 150 GLU -1.972 64.204 25.154 151 GLU 0.183 63.647 28.210 152 VAL -1.755 65.012 31.148 153 VAL -5.327 64.587 29.930 154 LEU -6.861 61.151 30.212 155 LEU -9.234 61.621 27.283 156 GLU -6.496 62.912 24.978 157 GLN -4.076 60.162 25.891 158 PRO -3.321 57.434 23.329 159 PHE -4.992 54.215 24.487 160 VAL -2.579 51.838 26.191 161 LYS -3.854 48.804 24.219 162 ASP -3.865 50.622 20.873 163 ASP -1.708 53.747 20.593 164 LYS -3.569 54.292 17.325 165 VAL -6.725 55.516 19.103 166 LYS -7.204 58.196 21.783 167 VAL -8.954 57.267 25.009 168 LYS -11.932 59.466 24.199 169 GLU -12.386 57.474 21.009 170 LEU -12.407 54.202 22.860 171 ILE -15.215 55.635 24.939 172 GLN -17.181 57.119 22.042 173 GLN -16.955 53.729 20.372 174 ALA -18.581 52.118 23.409 175 ILE -21.308 54.745 23.648 176 ALA -22.179 53.998 20.016 177 LYS -22.742 50.278 20.569 178 ILE -24.733 50.918 23.758 179 GLY -26.770 54.077 23.277 180 GLU -26.162 55.572 26.706 181 ASN -23.931 58.541 27.484 182 ILE -20.796 57.264 29.224 183 VAL -18.699 59.522 31.400 184 VAL -15.573 59.279 33.490 185 ARG -16.418 61.050 36.759 186 ARG -13.029 60.751 38.465 187 PHE -9.994 58.562 38.947 188 CYS -7.543 57.693 41.689 189 ARG -3.988 56.485 41.378 190 PHE -1.473 55.377 44.010 191 GLU 2.087 54.323 43.154 192 LEU 4.074 53.056 46.129 193 GLY 6.427 55.742 47.393 194 ALA 5.256 58.097 44.653 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C H H H H H H H H 10 H H C C H H H H H H 20 H H H H H H H C C C 30 H H H H H H H H H H 40 H H 3 3 3 3/T T T T S 50 S S S S/S S S S/S S S S 60 S S S/T T T T S S S S 70 S S S S S S S H H H 80 H H H H/H H H H H H H 90 H H H H H H H H H H 100 H H/S S S S C T T T T 110 C H H H H H H H H H 120 H H H H H/H H H H H 3 130 3 C H H H H H H H H 140 H H H H H 3 3/H H H H 150 H H H/T T T T/S S S S/T T 160 T T C C C H H H H H 170 H H H H H H H H H/S S 180 S S S S S S/S S S S S 190 S S/S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T T T h H H H 10 H H h h H H H H H 20 H H H H H h T T t T 30 T T h H H H H H H H 40 H H H H H H H H h T 50 t E E E E 60 E E e T T t e E E E 70 E E E E E S h H H 80 H H h h H H H H H H 90 H H H H H H H H H H 100 H h S B S S t T T 110 t h H H H H H H H H 120 H H H H H h T t S S 130 S t T h H H H H 140 h T T h H H H H H H 150 H H h T T T t B t T 160 T t T T t h H H H H 170 H H H H H H H H h S 180 E E E E E E E E 190 E e T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLN 76.4 51.4 64.6 2 MET 32.4 20.3 85.2 3 GLU 69.7 50.3 59.9 4 LEU 123.9 83.8 61.1 5 ILE 122.5 85.3 44.3 6 LYS 78.1 45.0 71.4 7 LYS 83.3 48.0 65.7 8 LEU 136.5 92.4 47.7 9 ARG 116.2 55.6 65.7 10 GLU 30.8 22.2 78.7 11 ALA 22.3 30.7 77.0 12 THR 87.1 81.5 53.5 13 GLY 11.6 33.2 79.3 14 ALA 58.2 80.2 58.4 15 GLY 10.3 29.7 73.0 16 MET 58.9 37.0 71.5 17 MET 52.8 33.1 75.2 18 ASP 69.2 62.6 74.1 19 VAL 118.8 100.0 39.2 20 LYS 75.0 43.3 62.7 21 ARG 97.2 46.5 73.5 22 ALA 64.3 88.6 53.7 23 LEU 146.4 99.1 36.5 24 GLU 64.9 46.8 68.5 25 ASP 36.6 33.1 65.2 26 ALA 43.0 59.2 72.6 27 GLY 0.0 0.0 80.7 28 TRP 137.4 67.0 58.8 29 ASP 33.8 30.6 74.6 30 GLU 34.0 24.5 73.6 31 GLU 22.4 16.2 80.0 32 LYS 127.4 73.5 74.2 33 ALA 72.6 100.0 53.2 34 VAL 77.4 65.2 48.4 35 GLN 59.1 39.8 73.3 36 LEU 90.1 61.0 65.0 37 LEU 137.6 93.1 43.6 38 ARG 108.6 52.0 74.7 39 GLU 42.5 30.6 77.9 40 ARG 169.8 81.3 65.7 41 GLY 32.6 93.7 58.6 42 ALA 35.8 49.3 73.5 43 MET 44.3 27.8 75.2 44 LYS 117.1 67.5 60.5 45 ALA 65.1 89.7 50.0 46 ALA 16.3 22.4 74.7 47 LYS 43.1 24.8 83.1 48 LYS 133.9 77.2 59.8 49 ALA 40.5 55.8 76.9 50 ASP 0.0 0.0 89.7 51 ARG 100.2 48.0 76.3 52 GLU 39.2 28.3 87.2 53 ALA 72.1 99.3 63.4 54 ARG 53.6 25.6 89.7 55 GLU 73.9 53.3 71.3 56 GLY 34.8 100.0 45.8 57 ILE 97.7 68.1 63.1 58 ILE 67.4 47.0 66.0 59 GLY 34.8 100.0 57.3 60 HIS 61.3 40.8 66.9 61 TYR 133.1 73.5 52.7 62 ILE 62.7 43.7 67.7 63 HIS 95.2 63.4 69.1 64 HIS 21.2 14.1 82.3 65 ASN 63.5 52.5 59.1 66 GLN 21.5 14.5 84.9 67 ARG 82.5 39.5 74.4 68 VAL 100.3 84.4 52.2 69 GLY 25.5 73.2 55.7 70 VAL 117.8 99.2 44.2 71 LEU 54.4 36.8 63.5 72 VAL 117.9 99.3 40.1 73 GLU 108.5 78.3 65.1 74 LEU 147.8 100.0 34.6 75 ASN 115.1 95.2 59.3 76 CYS 99.2 100.0 39.0 77 GLU 115.5 83.4 54.6 78 THR 54.1 50.6 61.2 79 ASP 45.6 41.3 66.6 80 PHE 10.8 6.5 85.1 81 VAL 100.5 84.6 44.3 82 ALA 68.6 94.5 44.4 83 ARG 36.4 17.4 87.6 84 ASN 59.5 49.2 61.5 85 GLU 32.9 23.8 77.2 86 LEU 79.5 53.8 69.1 87 PHE 165.7 99.3 37.7 88 GLN 88.9 59.8 62.1 89 ASN 52.5 43.5 72.5 90 LEU 138.0 93.4 32.9 91 ALA 72.6 100.0 40.9 92 LYS 109.8 63.3 71.5 93 ASP 78.3 70.9 50.0 94 LEU 147.4 99.7 25.6 95 ALA 72.6 100.0 49.4 96 MET 95.5 59.9 60.0 97 HIS 150.2 100.0 37.4 98 ILE 143.4 100.0 32.5 99 ALA 66.2 91.2 46.5 100 MET 33.8 21.2 76.9 101 MET 109.1 68.5 58.9 102 ASN 49.7 41.1 77.9 103 PRO 124.5 100.0 50.6 104 ARG 68.4 32.7 75.7 105 TYR 160.8 88.8 50.8 106 VAL 105.6 88.9 47.2 107 SER 59.1 70.7 52.3 108 ALA 41.1 56.6 59.6 109 GLU 14.4 10.4 82.5 110 GLU 71.6 51.7 65.0 111 ILE 138.8 96.7 37.8 112 PRO 66.6 53.5 69.8 113 ALA 13.7 18.8 78.0 114 GLU 29.9 21.6 67.6 115 GLU 84.5 61.0 65.3 116 LEU 105.5 71.3 57.0 117 GLU 74.0 53.4 74.8 118 LYS 117.7 67.9 81.3 119 GLU 87.2 62.9 58.0 120 ARG 121.7 58.3 60.1 121 GLN 61.2 41.2 72.9 122 ILE 40.4 28.2 78.7 123 TYR 170.9 94.4 47.1 124 ILE 127.6 88.9 49.5 125 GLN 31.3 21.0 80.5 126 ALA 21.6 29.7 73.9 127 ALA 64.9 89.4 55.6 128 LEU 69.6 47.1 66.2 129 ASN 35.0 29.0 71.7 130 GLU 31.4 22.7 75.8 131 GLY 2.1 5.9 80.3 132 LYS 93.1 53.7 61.3 133 PRO 57.7 46.4 60.4 134 GLN 48.0 32.3 59.0 135 GLN 89.1 60.0 77.8 136 ILE 51.8 36.1 57.6 137 ALA 72.6 100.0 42.4 138 GLU 114.4 82.5 62.8 139 LYS 36.7 21.2 79.4 140 ILE 61.0 42.5 62.0 141 ALA 72.3 99.6 51.3 142 GLU 100.5 72.5 72.9 143 GLY 8.4 24.0 80.1 144 ARG 108.1 51.7 69.5 145 LEU 124.0 83.9 50.1 146 LYS 51.6 29.8 79.8 147 LYS 40.5 23.4 78.9 148 TYR 136.0 75.1 57.0 149 LEU 108.8 73.6 41.4 150 GLU 102.7 74.1 58.7 151 GLU 58.1 41.9 69.6 152 VAL 96.3 81.1 46.6 153 VAL 118.8 100.0 42.5 154 LEU 147.5 99.8 29.8 155 LEU 120.0 81.2 38.0 156 GLU 117.2 84.6 51.8 157 GLN 146.9 98.9 50.0 158 PRO 80.0 64.3 63.4 159 PHE 151.8 91.0 39.1 160 VAL 91.1 76.7 43.4 161 LYS 73.4 42.3 64.4 162 ASP 54.1 48.9 62.0 163 ASP 7.0 6.3 83.5 164 LYS 113.4 65.4 82.5 165 VAL 96.2 81.0 65.7 166 LYS 116.7 67.3 67.3 167 VAL 118.8 100.0 35.4 168 LYS 105.0 60.6 61.7 169 GLU 75.8 54.7 68.5 170 LEU 102.2 69.1 42.0 171 ILE 131.4 91.6 34.9 172 GLN 107.1 72.0 46.7 173 GLN 97.8 65.8 56.0 174 ALA 61.7 85.0 43.3 175 ILE 136.9 95.4 49.0 176 ALA 63.5 87.5 57.6 177 LYS 118.3 68.2 65.6 178 ILE 128.6 89.6 45.4 179 GLY 11.1 32.0 68.3 180 GLU 118.7 85.7 49.8 181 ASN 115.0 95.1 43.6 182 ILE 143.2 99.8 32.0 183 VAL 70.3 59.2 75.6 184 VAL 117.1 98.6 28.7 185 ARG 114.9 55.0 68.4 186 ARG 54.9 26.3 75.1 187 PHE 148.5 89.0 42.2 188 CYS 51.0 51.4 55.8 189 ARG 181.4 86.8 58.0 190 PHE 19.9 11.9 82.3 191 GLU 76.3 55.0 71.4 192 LEU 48.7 33.0 82.0 193 GLY 0.0 0.0 79.2 194 ALA 29.1 40.1 81.8