Protein Data Bank File : 1ge9 Title : RIBOSOME 19-OCT-00 1GE9 Number of Amino Acid Residues : 184 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ILE LYS GLU LEU GLU ASP ILE PHE LYS 10 GLU ALA GLU LYS ASP MET LYS LYS ALA VAL 20 GLU TYR TYR LYS ASN GLU ILE ALA GLY LEU 30 ARG THR SER ARG ALA SER THR ALA LEU VAL 40 GLU GLU ILE LYS VAL GLU TYR TYR GLY SER 50 LYS VAL PRO ILE LYS GLN LEU GLY THR ILE 60 SER VAL PRO GLU HIS ASN GLN ILE VAL ILE 70 GLN VAL TRP ASP GLN ASN ALA VAL PRO ALA 80 ILE GLU LYS ALA ILE ARG GLU GLU LEU ASN 90 LEU ASN PRO THR VAL GLN GLY ASN VAL ILE 100 ARG VAL THR LEU PRO PRO LEU THR GLU GLU 110 ARG ARG ARG GLU LEU VAL ARG LEU LEU HIS 120 LYS ILE THR GLU GLU ALA ARG VAL ARG VAL 130 ARG ASN VAL ARG ARG GLU ALA LYS GLU MET 140 ILE GLU GLU LEU GLU GLY ILE SER GLU ASP 150 GLU LYS LYS ARG ALA LEU GLU ARG LEU GLN 160 LYS LEU THR ASP LYS TYR ILE ASP GLU ILE 170 ASN LYS LEU MET GLU ALA LYS GLU LYS GLU 180 ILE MET SER VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 167.3 179.9 -129.3 -107.1 -106.3 2 ILE -113.7 93.9 -179.9 31.1 -78.3 3 LYS -130.3 -157.5 180.0 -122.3 -54.9 147.9 -139.9 4 GLU -62.8 -19.9 -179.2 -164.3 74.1 20.7 5 LEU -51.5 -44.5 -178.9 176.1 74.8 6 GLU -53.9 -39.2 179.3 -91.9 102.4 -137.5 7 ASP -68.5 -32.0 179.4 -59.1 117.3 8 ILE -69.4 -42.7 179.5 -37.8 -50.5 9 PHE -65.9 -49.3 -179.7 -152.8 -47.3 10 LYS -58.9 -42.0 179.7 -163.2 -83.7 -137.8 -158.8 11 GLU -72.1 -40.8 -179.5 69.3 175.2 -111.4 12 ALA -70.0 -34.9 -179.6 13 GLU -70.1 -53.7 -179.5 -147.8 -162.3 152.7 14 LYS -59.6 -34.2 -179.5 -177.7 -144.2 105.7 83.7 15 ASP -71.7 -49.1 -179.4 -149.0 47.0 16 MET -70.9 -45.7 -179.5 -49.8 -97.0 -123.8 17 LYS -55.1 -47.4 -179.6 -86.7 -158.6 61.9 162.7 18 LYS -67.9 -32.3 -179.3 -95.4 147.1 -150.1 61.2 19 ALA -70.2 -46.9 -179.6 20 VAL -71.7 -37.3 -179.8 -81.6 21 GLU -63.1 -49.4 179.9 -91.2 -129.8 -81.0 22 TYR -70.0 -36.4 -179.9 -88.4 -64.4 23 TYR -61.5 -49.4 179.3 154.8 -117.1 24 LYS -64.5 -31.7 179.7 65.4 168.7 -75.2 140.3 25 ASN -61.5 -33.6 179.5 -128.2 -60.6 26 GLU -75.6 -36.5 -179.3 -95.4 93.5 87.1 27 ILE -80.7 -29.9 180.0 -39.2 164.2 28 ALA -75.0 -23.5 -179.2 29 GLY -123.6 7.0 179.6 30 LEU -50.6 165.1 -179.9 -114.4 130.7 31 ARG -82.4 69.9 -179.9 18.2 -73.2 -102.8 -161.4 32 THR -69.7 129.0 180.0 -32.0 33 SER -65.8 -11.3 179.5 55.0 34 ARG -81.1 141.1 179.2 -159.8 170.7 -133.7 79.1 35 ALA -73.5 80.2 -179.2 36 SER -116.2 137.8 179.8 11.7 37 THR -72.2 -18.0 -177.4 67.3 38 ALA -69.8 -55.9 -178.1 39 LEU -33.0 -44.8 178.7 37.9 144.2 40 VAL -80.8 -106.1 179.6 -86.5 41 GLU 79.1 -21.0 179.8 -131.1 148.8 163.7 42 GLU -116.7 40.9 179.6 -146.8 -107.0 -49.9 43 ILE -66.8 65.7 -179.3 -50.1 -67.0 44 LYS -54.3 112.3 179.9 179.7 -101.9 -87.4 178.7 45 VAL -112.6 137.1 -179.9 62.5 46 GLU -78.9 129.9 179.8 -90.5 172.0 -98.2 47 TYR -128.7 94.3 179.8 -154.7 134.4 48 TYR 55.5 37.8 179.7 -75.1 -51.0 49 GLY 92.5 22.4 179.8 50 SER -131.4 131.9 -179.9 -73.8 51 LYS -99.1 111.5 179.7 -48.6 134.2 93.6 81.0 52 VAL -144.6 149.1 179.1 -116.0 53 PRO -67.6 176.8 -179.4 23.9 -31.9 54 ILE -91.8 38.0 -180.0 -34.7 -58.2 55 LYS -74.8 -40.6 179.8 -92.3 133.8 -174.9 -66.8 56 GLN -121.9 27.9 -179.9 -50.6 114.7 105.2 57 LEU -113.5 -51.5 -179.9 -88.8 -104.5 58 GLY -140.9 -127.9 -179.9 59 THR -174.1 135.1 179.8 -171.1 60 ILE -121.6 129.0 -179.6 66.0 -76.7 61 SER -143.6 151.8 179.4 71.5 62 VAL -95.4 117.7 -178.6 -176.1 63 PRO -89.6 -43.5 -178.4 34.3 -30.4 64 GLU -124.6 28.1 179.6 23.0 166.3 97.0 65 HIS 68.7 -57.5 -179.9 -98.4 -166.4 66 ASN -85.2 25.0 179.5 -84.9 -125.4 67 GLN -145.6 148.1 178.6 -162.0 -130.8 127.5 68 ILE -126.3 127.5 -178.1 -34.7 -177.5 69 VAL -118.9 119.4 179.3 -154.6 70 ILE -108.4 124.5 -179.8 -34.7 -74.8 71 GLN -117.9 107.4 -178.1 -43.6 -166.3 139.1 72 VAL -93.4 89.7 179.8 -154.8 73 TRP -37.9 -40.3 -179.7 -60.2 -7.0 74 ASP -95.3 149.1 179.1 60.1 -51.0 75 GLN -78.8 -16.2 -179.1 62.6 -143.8 -109.2 76 ASN -73.6 -34.4 -178.7 -138.1 110.7 77 ALA -91.7 -0.8 179.6 78 VAL -70.7 -47.2 -179.1 -168.4 79 PRO -67.7 -42.6 -179.2 -16.3 32.3 80 ALA -64.5 -51.7 -179.2 81 ILE -56.0 -40.5 179.7 -57.8 160.6 82 GLU -52.6 -50.2 179.2 -120.0 -139.8 -142.6 83 LYS -71.4 -35.1 -179.3 -87.1 -91.7 128.5 45.2 84 ALA -68.4 -49.8 -179.6 85 ILE -62.4 -47.5 179.9 -171.7 129.2 86 ARG -57.5 -29.0 -179.6 -173.2 -134.8 171.2 162.3 87 GLU -69.5 -49.6 -179.2 -81.9 -103.2 128.1 88 GLU -82.0 -43.7 -179.4 -65.2 -141.1 121.1 89 LEU -76.3 -23.5 179.6 -107.4 91.2 90 ASN 53.2 49.1 179.7 -94.1 51.5 91 LEU -142.4 -176.7 -179.9 -65.3 125.6 92 ASN -105.6 94.0 -180.0 -142.8 120.2 93 PRO -77.2 141.3 179.8 29.8 -33.4 94 THR -103.1 136.5 -179.8 -54.9 95 VAL -121.4 123.8 179.8 -171.7 96 GLN -130.3 125.1 -179.9 46.1 153.9 125.6 97 GLY 59.9 -85.3 179.7 98 ASN -147.5 20.1 179.9 -81.4 94.2 99 VAL -127.4 146.0 180.0 -104.8 100 ILE -118.0 117.9 179.6 -49.3 143.6 101 ARG -104.8 117.9 -179.8 172.7 146.5 98.2 76.3 102 VAL -117.5 122.9 179.0 168.4 103 THR -124.9 127.3 179.7 165.5 104 LEU -101.3 145.2 179.9 15.4 -65.2 105 PRO -50.3 134.1 -179.1 -26.1 32.3 106 PRO -46.8 116.9 179.5 6.2 -23.3 107 LEU -63.8 85.7 -178.2 66.5 -160.8 108 THR -74.6 -169.0 -179.7 79.0 109 GLU -47.8 -48.3 -179.9 -97.3 -147.4 92.8 110 GLU -71.9 -41.5 -179.4 -173.5 -131.6 -116.7 111 ARG -56.8 -47.1 179.1 -118.9 -97.6 152.1 71.4 112 ARG -59.3 -33.2 179.6 -55.1 157.4 -140.7 173.4 113 ARG -66.0 -33.6 -179.0 -102.7 60.1 -148.4 161.4 114 GLU -63.6 -53.1 -180.0 -147.7 102.0 148.1 115 LEU -68.5 -48.0 -178.9 -88.2 -34.2 116 VAL -56.1 -43.4 179.3 -57.5 117 ARG -70.6 -30.6 179.0 -96.2 59.6 157.9 71.0 118 LEU -71.0 -40.6 177.1 -133.0 95.8 119 LEU -71.6 -33.1 -178.8 -132.1 79.8 120 HIS -55.2 -42.6 178.8 -85.2 164.6 121 LYS -72.1 -33.7 179.9 -163.3 167.2 100.9 87.6 122 ILE -60.2 -51.5 -179.0 -37.5 -49.8 123 THR -57.6 -39.1 -180.0 -52.4 124 GLU -70.0 -31.9 -180.0 -140.4 136.6 62.0 125 GLU -69.7 -37.3 -179.8 -93.7 -77.0 -105.9 126 ALA -60.8 -48.1 -179.9 127 ARG -59.1 -37.8 180.0 62.5 143.6 126.0 161.1 128 VAL -59.5 -38.5 179.3 -173.7 129 ARG -70.3 -47.8 -178.8 -51.8 -124.5 126.1 -71.5 130 VAL -57.0 -47.2 179.8 -170.7 131 ARG -56.4 -48.0 -179.3 -91.1 55.8 -161.5 -80.3 132 ASN -60.2 -31.4 179.1 -86.5 -128.0 133 VAL -63.2 -51.8 179.4 173.5 134 ARG -69.4 -36.4 179.8 55.0 173.8 -102.0 176.0 135 ARG -71.4 -37.8 179.2 -147.0 -95.4 -150.0 -163.8 136 GLU -74.1 -53.0 -180.0 -171.8 -158.7 68.5 137 ALA -55.0 -44.6 179.3 138 LYS -57.6 -41.2 179.7 -92.9 -134.4 -170.1 -142.3 139 GLU -56.6 -33.0 180.0 -103.8 -129.0 -53.8 140 MET -68.0 -40.6 179.8 -98.3 -102.0 127.7 141 ILE -67.8 -50.5 178.9 -13.6 -61.5 142 GLU -64.9 -17.1 179.5 74.5 -170.0 -99.1 143 GLU -85.5 -28.6 -179.8 -179.5 138.2 -89.7 144 LEU -75.6 113.3 -178.5 -121.3 -82.1 145 GLU 58.0 8.9 -179.7 -52.9 150.4 144.9 146 GLY 75.6 -18.4 178.2 147 ILE -159.1 125.1 179.1 65.9 -58.9 148 SER -134.4 106.9 178.8 -50.1 149 GLU -75.9 -53.4 -179.8 -56.4 171.3 -80.7 150 ASP -57.6 -41.0 179.9 -136.4 -116.4 151 GLU -72.6 -48.0 -179.5 -149.4 94.7 -99.7 152 LYS -59.3 -41.3 -179.7 -79.2 170.2 178.7 -64.1 153 LYS -65.9 -52.1 -179.7 -90.1 -163.5 -72.0 -109.4 154 ARG -70.6 -33.8 179.8 -105.6 96.4 143.3 66.7 155 ALA -72.4 -33.7 -179.8 156 LEU -68.2 -51.2 179.5 -96.4 28.1 157 GLU -58.8 -41.7 178.5 57.6 -177.6 50.2 158 ARG -62.8 -42.1 179.4 -121.2 80.4 141.9 160.4 159 LEU -73.1 -34.0 179.6 -98.6 -48.6 160 GLN -71.9 -48.0 179.7 -75.5 -145.7 34.6 161 LYS -53.3 -43.0 178.9 -122.4 73.3 -132.8 69.4 162 LEU -70.1 -46.9 -179.6 -98.3 100.8 163 THR -58.0 -48.8 179.4 -144.0 164 ASP -54.5 -34.9 -179.9 -139.2 95.7 165 LYS -55.3 -48.4 179.4 -166.2 90.1 -153.4 -177.7 166 TYR -66.9 -36.6 179.9 -148.0 149.6 167 ILE -60.0 -53.2 179.5 -57.7 -64.2 168 ASP -71.5 -29.1 -179.4 -49.7 128.6 169 GLU -71.7 -42.1 -179.7 -86.5 -119.8 53.7 170 ILE -69.7 -55.5 -178.9 -176.4 -177.9 171 ASN -57.1 -32.9 179.7 55.3 24.9 172 LYS -66.4 -35.5 -180.0 -169.2 71.8 150.4 179.3 173 LEU -68.8 -47.2 -179.6 -94.9 28.4 174 MET -67.7 -44.2 -179.8 -175.5 -110.0 -128.6 175 GLU -52.7 -51.2 179.5 -113.1 -71.3 134.9 176 ALA -61.0 -54.3 -179.1 177 LYS -52.6 -43.1 -179.5 -96.9 70.2 -140.3 78.2 178 GLU -52.7 -45.1 179.2 -95.4 169.2 152.4 179 LYS -59.0 -32.5 179.4 -60.9 -111.4 72.1 152.8 180 GLU -85.9 -51.7 -179.6 -118.0 -154.9 103.7 181 ILE -57.5 -52.4 -179.7 -56.1 162.1 182 MET -82.0 1.5 -179.9 -43.1 -93.4 137.5 183 SER -53.8 -41.4 179.9 -149.5 184 VAL -67.1 -35.2 0.0 60.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 338.262 13.384 -12.121 2 ILE 337.267 10.237 -14.015 3 LYS 338.681 7.146 -12.311 4 GLU 337.475 3.907 -10.694 5 LEU 335.420 6.090 -8.339 6 GLU 332.618 6.384 -10.909 7 ASP 332.214 2.600 -10.822 8 ILE 332.067 2.719 -7.024 9 PHE 329.307 5.336 -7.055 10 LYS 327.303 3.570 -9.758 11 GLU 327.592 0.254 -7.918 12 ALA 326.912 1.809 -4.510 13 GLU 323.930 3.791 -5.805 14 LYS 322.176 0.938 -7.609 15 ASP 322.780 -1.309 -4.592 16 MET 321.487 1.112 -1.949 17 LYS 318.694 2.557 -4.101 18 LYS 317.276 -0.901 -4.814 19 ALA 317.645 -1.905 -1.159 20 VAL 315.763 1.074 0.285 21 GLU 313.146 1.058 -2.479 22 TYR 312.281 -2.612 -1.985 23 TYR 312.648 -2.304 1.786 24 LYS 310.117 0.539 2.002 25 ASN 307.922 -1.435 -0.395 26 GLU 307.603 -4.187 2.214 27 ILE 306.740 -1.753 5.003 28 ALA 304.421 0.318 2.820 29 GLY 302.389 -2.759 1.913 30 LEU 303.027 -5.109 4.852 31 ARG 300.013 -6.922 6.310 32 THR 299.237 -4.262 8.899 33 SER 296.428 -5.308 11.220 34 ARG 295.296 -1.688 11.078 35 ALA 292.516 -0.790 8.666 36 SER 294.727 1.315 6.464 37 THR 294.210 2.061 2.779 38 ALA 297.999 2.173 2.273 39 LEU 299.018 -1.482 2.907 40 VAL 297.125 -2.243 -0.268 41 GLU 297.083 0.559 -2.860 42 GLU 297.673 -2.091 -5.506 43 ILE 294.208 -3.650 -5.478 44 LYS 294.712 -4.902 -9.036 45 VAL 291.218 -5.537 -10.378 46 GLU 290.411 -7.306 -13.648 47 TYR 288.334 -5.268 -16.098 48 TYR 287.226 -7.185 -19.193 49 GLY 290.680 -8.737 -19.437 50 SER 292.607 -5.766 -18.060 51 LYS 294.527 -5.544 -14.787 52 VAL 294.321 -2.110 -13.165 53 PRO 294.152 -0.731 -9.583 54 ILE 291.010 0.867 -8.127 55 LYS 292.290 4.392 -8.800 56 GLN 289.651 5.152 -11.434 57 LEU 287.268 2.303 -10.610 58 GLY 285.941 2.959 -7.121 59 THR 287.169 4.436 -3.846 60 ILE 288.585 3.197 -0.539 61 SER 288.336 5.064 2.768 62 VAL 288.707 4.337 6.489 63 PRO 285.517 5.083 8.502 64 GLU 286.370 3.830 12.003 65 HIS 290.148 3.356 11.772 66 ASN 289.758 -0.378 12.478 67 GLN 287.762 -0.749 9.258 68 ILE 288.410 -0.494 5.522 69 VAL 285.648 0.283 3.033 70 ILE 285.998 -0.355 -0.697 71 GLN 283.279 0.980 -3.017 72 VAL 283.368 -0.304 -6.597 73 TRP 281.165 2.042 -8.641 74 ASP 281.171 -0.617 -11.374 75 GLN 279.822 -4.147 -10.978 76 ASN 282.720 -5.463 -13.080 77 ALA 285.376 -4.590 -10.497 78 VAL 283.306 -5.897 -7.592 79 PRO 284.152 -9.616 -8.130 80 ALA 287.846 -9.064 -8.885 81 ILE 288.563 -6.777 -5.934 82 GLU 286.912 -9.267 -3.584 83 LYS 289.458 -11.911 -4.574 84 ALA 292.220 -9.303 -4.860 85 ILE 291.685 -7.708 -1.447 86 ARG 291.312 -11.055 0.324 87 GLU 294.660 -12.026 -1.198 88 GLU 296.643 -9.090 0.204 89 LEU 294.495 -8.360 3.266 90 ASN 294.093 -12.085 3.962 91 LEU 290.664 -11.554 5.535 92 ASN 286.941 -12.034 4.902 93 PRO 285.566 -8.897 3.157 94 THR 281.815 -8.262 3.129 95 VAL 280.009 -6.977 0.036 96 GLN 276.588 -5.320 0.138 97 GLY 274.825 -3.765 -2.837 98 ASN 277.849 -1.935 -4.224 99 VAL 280.003 -1.329 -1.143 100 ILE 282.635 -3.489 0.545 101 ARG 283.124 -3.325 4.311 102 VAL 286.307 -4.921 5.639 103 THR 287.025 -5.275 9.342 104 LEU 290.109 -7.001 10.729 105 PRO 290.262 -8.605 14.205 106 PRO 291.391 -6.023 16.805 107 LEU 295.179 -6.015 16.712 108 THR 295.600 -7.045 20.339 109 GLU 298.727 -7.529 22.448 110 GLU 299.768 -10.512 20.324 111 ARG 298.650 -8.940 17.038 112 ARG 300.894 -5.905 17.546 113 ARG 303.695 -8.379 18.183 114 GLU 303.141 -9.949 14.756 115 LEU 303.713 -6.774 12.709 116 VAL 306.363 -5.291 15.003 117 ARG 308.381 -8.515 14.865 118 LEU 307.844 -8.672 11.106 119 LEU 309.145 -5.136 10.608 120 HIS 311.778 -6.005 13.160 121 LYS 313.373 -8.485 10.736 122 ILE 313.006 -5.979 7.897 123 THR 314.967 -3.272 9.702 124 GLU 317.771 -5.731 10.473 125 GLU 317.883 -6.822 6.831 126 ALA 318.322 -3.242 5.625 127 ARG 321.427 -2.664 7.747 128 VAL 322.928 -5.891 6.392 129 ARG 322.699 -4.500 2.860 130 VAL 324.080 -1.082 3.787 131 ARG 327.136 -2.533 5.542 132 ASN 327.916 -4.673 2.496 133 VAL 327.670 -1.575 0.304 134 ARG 330.426 0.247 2.193 135 ARG 332.309 -3.013 2.741 136 GLU 331.964 -3.978 -0.917 137 ALA 332.611 -0.521 -2.347 138 LYS 335.657 -0.128 -0.098 139 GLU 336.986 -3.418 -1.467 140 MET 336.945 -1.827 -4.923 141 ILE 339.145 1.075 -3.806 142 GLU 341.580 -1.164 -1.915 143 GLU 341.533 -3.404 -4.999 144 LEU 342.592 -0.591 -7.341 145 GLU 346.394 -0.554 -7.425 146 GLY 345.943 -2.193 -4.022 147 ILE 345.872 1.262 -2.412 148 SER 344.103 4.500 -3.334 149 GLU 344.243 7.497 -0.990 150 ASP 342.609 9.966 -3.365 151 GLU 340.069 7.321 -4.333 152 LYS 339.477 5.989 -0.806 153 LYS 338.948 9.504 0.544 154 ARG 336.570 10.592 -2.213 155 ALA 335.025 7.114 -2.400 156 LEU 334.403 6.971 1.355 157 GLU 332.552 10.284 1.551 158 ARG 330.647 9.208 -1.542 159 LEU 329.947 5.855 0.105 160 GLN 329.161 7.529 3.433 161 LYS 326.837 10.123 1.938 162 LEU 324.926 7.258 0.341 163 THR 325.098 5.019 3.423 164 ASP 323.829 7.789 5.710 165 LYS 320.912 8.094 3.308 166 TYR 319.843 4.546 4.190 167 ILE 320.558 5.171 7.878 168 ASP 318.214 8.153 8.087 169 GLU 315.861 6.499 5.606 170 ILE 315.485 3.286 7.601 171 ASN 315.140 4.811 11.084 172 LYS 312.631 7.291 9.655 173 LEU 310.468 4.414 8.424 174 MET 310.446 2.558 11.751 175 GLU 309.998 5.715 13.836 176 ALA 306.825 6.628 11.955 177 LYS 305.483 3.073 11.897 178 GLU 306.044 2.730 15.656 179 LYS 303.644 5.625 16.256 180 GLU 301.100 3.722 14.164 181 ILE 301.946 0.167 15.199 182 MET 302.145 1.097 18.885 183 SER 299.295 3.585 18.374 184 VAL 296.882 1.030 19.829 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/H H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 C C C C C C T T T T 40 C C S S S S/T T T T/S S 50 S S S S/T T T T/S S S S 60 S S/T T T T S S S S S 70 S S S C C C H H H H 80 H H H H H H H H H S 90 S S S S S/T T T T/S S S 100 S S S S S S C H H H 110 H H H H 3 3/H H H H H 120 H H H H H H H H H H 130 H H H H H H H H H H 140 H H H H/T T T T H H H 150 H H H H H H H H H H 160 H H H H H H H H H H 170 H H H H H H H H H H 180 H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t h H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H h 30 S S t T T T t 40 S E E e S S e 50 E E t T T T T t E E 60 E S S S e E E E E 70 E e S S S h H H H H 80 H H H H H H H H H h 90 S E E E T e E E 100 E E E e h H H 110 H H H H H H H H H H 120 H H H H H H H H H H 130 H H H H H H H H H H 140 H H H h T T t h H H 150 H H H H H H H H H H 160 H H H H H H H H H H 170 H H H H H H H H H H 180 H h T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 20.1 12.6 80.1 2 ILE 19.0 13.2 78.2 3 LYS 69.8 40.2 75.5 4 GLU 102.7 74.1 47.4 5 LEU 130.1 88.1 53.5 6 GLU 63.5 45.8 69.7 7 ASP 38.8 35.2 73.1 8 ILE 143.4 99.9 35.7 9 PHE 98.4 59.0 58.8 10 LYS 32.6 18.8 77.7 11 GLU 100.3 72.4 54.1 12 ALA 71.0 97.8 37.5 13 GLU 67.0 48.3 58.0 14 LYS 76.0 43.8 73.1 15 ASP 64.3 58.2 66.3 16 MET 152.8 95.8 42.8 17 LYS 63.0 36.3 73.8 18 LYS 81.2 46.8 65.6 19 ALA 64.1 88.2 52.6 20 VAL 99.7 83.9 49.2 21 GLU 39.1 28.2 69.7 22 TYR 37.8 20.9 80.6 23 TYR 170.6 94.2 44.4 24 LYS 72.9 42.0 66.1 25 ASN 35.6 29.5 72.9 26 GLU 52.6 38.0 64.4 27 ILE 141.3 98.5 32.6 28 ALA 24.6 33.9 74.8 29 GLY 20.4 58.7 76.2 30 LEU 138.4 93.6 40.4 31 ARG 47.0 22.5 76.4 32 THR 77.6 72.6 53.1 33 SER 77.2 92.3 47.3 34 ARG 176.5 84.5 61.2 35 ALA 72.6 100.0 47.0 36 SER 62.6 74.9 54.7 37 THR 67.8 63.4 53.8 38 ALA 22.4 30.8 78.1 39 LEU 138.3 93.6 58.1 40 VAL 117.7 99.1 43.2 41 GLU 36.4 26.3 75.9 42 GLU 31.8 22.9 76.9 43 ILE 138.4 96.4 33.1 44 LYS 99.3 57.3 70.9 45 VAL 118.8 100.0 45.6 46 GLU 44.8 32.3 70.1 47 TYR 114.0 63.0 54.6 48 TYR 29.3 16.2 85.4 49 GLY 1.0 2.9 82.9 50 SER 28.2 33.7 72.0 51 LYS 59.8 34.5 70.5 52 VAL 58.0 48.8 61.7 53 PRO 89.3 71.7 54.2 54 ILE 141.4 98.6 37.7 55 LYS 52.9 30.5 77.5 56 GLN 25.2 17.0 76.2 57 LEU 126.8 85.8 47.5 58 GLY 34.8 100.0 54.4 59 THR 52.9 49.5 70.1 60 ILE 104.6 72.9 50.3 61 SER 17.4 20.8 74.5 62 VAL 94.9 79.9 58.8 63 PRO 80.5 64.6 66.6 64 GLU 45.1 32.6 75.5 65 HIS 23.2 15.4 85.7 66 ASN 68.6 56.8 60.7 67 GLN 140.1 94.3 42.3 68 ILE 143.2 99.8 33.6 69 VAL 95.9 80.7 57.5 70 ILE 143.5 100.0 24.9 71 GLN 81.3 54.7 59.8 72 VAL 118.6 99.8 43.4 73 TRP 43.4 21.2 82.5 74 ASP 81.9 74.1 57.0 75 GLN 5.9 3.9 83.7 76 ASN 81.5 67.4 60.7 77 ALA 72.6 100.0 40.4 78 VAL 96.8 81.5 48.6 79 PRO 44.2 35.5 76.1 80 ALA 53.7 74.0 62.6 81 ILE 143.5 100.0 24.4 82 GLU 77.5 55.9 60.9 83 LYS 44.0 25.4 84.5 84 ALA 53.6 73.9 63.9 85 ILE 142.9 99.6 22.2 86 ARG 72.5 34.7 73.8 87 GLU 23.1 16.6 81.6 88 GLU 63.9 46.1 73.3 89 LEU 143.2 96.9 26.4 90 ASN 28.8 23.9 83.2 91 LEU 114.1 77.2 52.4 92 ASN 3.3 2.7 82.0 93 PRO 117.9 94.7 47.0 94 THR 25.5 23.8 77.1 95 VAL 98.7 83.1 49.9 96 GLN 41.0 27.6 72.9 97 GLY 0.0 0.0 85.0 98 ASN 49.0 40.5 72.1 99 VAL 74.5 62.7 66.9 100 ILE 143.4 99.9 34.2 101 ARG 92.4 44.2 70.9 102 VAL 118.0 99.3 33.4 103 THR 44.4 41.5 73.7 104 LEU 144.5 97.7 46.6 105 PRO 51.2 41.1 68.0 106 PRO 31.1 25.0 73.8 107 LEU 138.3 93.6 54.9 108 THR 37.5 35.1 71.1 109 GLU 11.7 8.4 87.9 110 GLU 17.3 12.5 81.3 111 ARG 137.0 65.6 60.7 112 ARG 148.6 71.1 59.5 113 ARG 93.3 44.7 70.7 114 GLU 41.0 29.6 75.9 115 LEU 136.7 92.5 51.1 116 VAL 113.9 95.9 38.1 117 ARG 68.4 32.8 74.9 118 LEU 70.6 47.8 62.3 119 LEU 138.2 93.5 35.7 120 HIS 72.9 48.5 66.6 121 LYS 28.5 16.4 80.5 122 ILE 114.5 79.8 43.7 123 THR 73.8 69.1 52.9 124 GLU 49.3 35.6 80.4 125 GLU 50.9 36.7 74.2 126 ALA 70.3 96.9 44.8 127 ARG 93.6 44.8 68.4 128 VAL 49.0 41.2 74.1 129 ARG 89.0 42.6 72.7 130 VAL 116.0 97.7 39.7 131 ARG 89.4 42.8 69.6 132 ASN 42.0 34.7 74.2 133 VAL 117.3 98.7 46.1 134 ARG 81.3 38.9 70.2 135 ARG 37.3 17.8 81.8 136 GLU 47.1 34.0 76.3 137 ALA 72.2 99.4 48.8 138 LYS 91.4 52.7 62.6 139 GLU 53.3 38.5 81.5 140 MET 98.2 61.6 68.7 141 ILE 143.4 99.9 35.4 142 GLU 68.9 49.7 71.7 143 GLU 32.7 23.6 75.1 144 LEU 110.0 74.4 68.4 145 GLU 31.1 22.5 77.9 146 GLY 7.1 20.5 72.3 147 ILE 27.9 19.4 79.8 148 SER 74.6 89.2 62.1 149 GLU 9.0 6.5 83.6 150 ASP 10.5 9.5 79.5 151 GLU 120.4 86.9 38.6 152 LYS 119.8 69.1 52.5 153 LYS 42.2 24.3 77.2 154 ARG 80.1 38.4 79.4 155 ALA 72.6 100.0 31.0 156 LEU 107.9 73.0 54.1 157 GLU 64.9 46.9 68.7 158 ARG 113.6 54.4 57.0 159 LEU 144.7 97.9 34.1 160 GLN 36.3 24.4 71.3 161 LYS 36.2 20.8 78.3 162 LEU 124.2 84.1 42.3 163 THR 87.6 81.9 46.1 164 ASP 47.3 42.8 74.7 165 LYS 36.3 20.9 83.4 166 TYR 179.2 99.0 32.7 167 ILE 72.1 50.3 69.6 168 ASP 38.1 34.5 81.6 169 GLU 78.3 56.5 51.6 170 ILE 125.5 87.5 42.7 171 ASN 50.2 41.5 64.7 172 LYS 25.2 14.5 83.0 173 LEU 110.1 74.5 54.9 174 MET 96.9 60.8 65.8 175 GLU 35.6 25.7 78.4 176 ALA 21.7 29.9 77.2 177 LYS 119.0 68.6 53.9 178 GLU 82.6 59.6 54.6 179 LYS 21.6 12.5 89.1 180 GLU 69.9 50.5 69.7 181 ILE 129.0 89.9 37.8 182 MET 85.2 53.5 62.4 183 SER 42.0 50.3 80.1 184 VAL 82.7 69.6 72.0