Protein Data Bank File : 1qm9 Title : RIBONUCLEOPROTEIN 22-SEP-99 1QM9 Number of Amino Acid Residues : 198 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET GLY ASN SER VAL LEU LEU VAL SER ASN 10 LEU ASN PRO GLU ARG VAL THR PRO GLN SER 20 LEU PHE ILE LEU PHE GLY VAL TYR GLY ASP 30 VAL GLN ARG VAL LYS ILE LEU PHE ASN LYS 40 LYS GLU ASN ALA LEU VAL GLN MET ALA ASP 50 GLY ASN GLN ALA GLN LEU ALA MET SER HIS 60 LEU ASN GLY HIS LYS LEU HIS GLY LYS PRO 70 ILE ARG ILE THR LEU SER LYS HIS GLN ASN 80 VAL GLN LEU PRO ARG GLU GLY GLN GLU ASP 90 GLN GLY LEU THR LYS ASP TYR GLY ASN SER 100 PRO LEU HIS ARG PHE LYS LYS PRO GLY SER 110 LYS ASN PHE GLN ASN ILE PHE PRO PRO SER 120 ALA THR LEU HIS LEU SER ASN ILE PRO PRO 130 SER VAL SER GLU GLU ASP LEU LYS VAL LEU 140 PHE SER SER ASN GLY GLY VAL VAL LYS GLY 150 PHE LYS PHE PHE GLN LYS ASP ARG LYS MET 160 ALA LEU ILE GLN MET GLY SER VAL GLU GLU 170 ALA VAL GLN ALA LEU ILE ASP LEU HIS ASN 180 HIS ASP LEU GLY GLU ASN HIS HIS LEU ARG 190 VAL SER PHE SER LYS SER THR ILE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 99.4 180.0 -68.7 139.4 167.2 2 GLY -140.2 -147.4 180.0 3 ASN -81.8 135.3 180.0 -109.8 126.9 4 SER -164.2 63.8 179.8 -140.6 5 VAL -120.6 132.3 -179.1 156.6 6 LEU -86.9 117.7 179.8 -100.2 83.5 7 LEU -87.7 131.8 -179.8 -75.5 101.4 8 VAL -101.8 130.8 -179.8 -161.5 9 SER -98.4 119.9 179.9 -46.1 10 ASN -180.0 -82.2 179.8 176.4 -138.4 11 LEU -1.7 75.4 -179.4 -60.8 -31.6 12 ASN -96.3 -65.8 -179.6 -97.0 106.4 13 PRO -71.9 -166.4 180.0 24.6 -30.1 14 GLU -98.0 -36.8 179.7 -54.5 105.0 20.2 15 ARG -67.4 -13.0 179.7 -166.2 166.9 95.4 164.0 16 VAL -96.2 80.9 -180.0 165.5 17 THR -92.8 172.7 -179.6 4.5 18 PRO -63.4 -24.8 179.5 23.4 -33.8 19 GLN -54.9 -45.2 179.2 -169.3 163.1 -75.3 20 SER -74.7 -49.5 179.3 135.9 21 LEU -60.5 -41.2 179.5 167.1 132.7 22 PHE -57.7 -37.0 179.7 -175.1 -170.8 23 ILE -58.2 -37.9 179.6 -140.7 126.2 24 LEU -58.0 -50.9 178.8 -105.1 -60.4 25 PHE -77.3 -29.1 179.9 -87.5 102.3 26 GLY -56.3 -16.7 180.0 27 VAL -38.0 -31.6 179.7 53.0 28 TYR -108.4 -3.7 180.0 44.3 -127.0 29 GLY 44.3 57.0 -179.2 30 ASP -126.2 -9.8 179.9 -93.5 -71.2 31 VAL -66.8 109.8 -179.3 119.5 32 GLN -58.9 -37.0 -179.6 -62.8 -68.4 -79.3 33 ARG -158.7 147.2 179.4 -115.0 149.7 -74.4 -178.5 34 VAL -121.1 133.3 -179.6 59.5 35 LYS -119.1 130.8 179.7 -52.0 -143.0 -75.2 103.9 36 ILE -131.1 116.2 179.9 161.2 173.8 37 LEU -175.9 -85.2 -179.9 35.3 136.2 38 PHE -58.8 -11.9 179.9 -172.8 -119.4 39 ASN -53.8 -17.7 179.9 -49.1 158.3 40 LYS 47.9 51.8 179.9 -172.8 -162.6 -141.9 -78.7 41 LYS 57.1 157.3 179.8 -48.0 -122.9 -63.9 -161.0 42 GLU 65.7 10.9 180.0 -115.0 -155.4 92.6 43 ASN -148.9 154.8 179.7 -84.1 93.6 44 ALA -157.0 163.6 -179.7 45 LEU -119.9 118.4 179.3 -111.2 -50.8 46 VAL -115.4 116.5 -178.6 135.2 47 GLN -106.3 115.3 179.2 174.0 163.9 7.1 48 MET -167.4 -39.8 -179.1 118.8 -138.3 65.3 49 ALA -53.5 -43.8 -178.1 50 ASP 39.9 19.8 -177.8 -84.4 -87.8 51 GLY 104.7 -56.2 -178.3 52 ASN -74.8 -51.9 -177.1 -81.4 95.7 53 GLN -58.7 -35.6 177.8 -59.1 -139.7 91.1 54 ALA -57.6 -32.3 178.8 55 GLN -54.4 -50.6 177.7 -143.6 74.9 79.8 56 LEU -75.3 -52.3 -179.4 172.2 116.6 57 ALA -72.7 -50.5 -178.8 58 MET -54.6 -48.3 -179.8 -151.4 -152.5 88.3 59 SER -75.0 -47.5 -178.6 -56.8 60 HIS -61.7 -40.8 -179.2 -176.7 -102.4 61 LEU -82.4 -46.2 -180.0 -120.1 124.7 62 ASN -61.4 176.2 -179.5 -65.3 30.9 63 GLY 47.7 24.2 -179.7 64 HIS -69.0 -23.4 -179.7 42.2 63.3 65 LYS 70.3 94.6 -179.7 -153.6 -179.6 171.0 -80.3 66 LEU -78.6 137.8 179.9 -58.4 158.5 67 HIS -132.8 6.7 -179.9 49.9 106.8 68 GLY -149.0 -37.5 -179.9 69 LYS -131.0 118.3 -180.0 65.6 -145.0 -68.4 110.3 70 PRO -73.8 96.7 179.9 24.8 -28.7 71 ILE -109.7 143.0 -179.7 74.7 117.9 72 ARG -108.9 140.8 179.9 -139.1 118.7 108.4 -130.1 73 ILE -126.8 128.4 -179.7 -156.0 -73.8 74 THR -123.1 163.2 -179.9 -29.1 75 LEU -119.3 118.7 -180.0 167.9 71.2 76 SER -41.4 139.0 180.0 93.4 77 LYS -101.6 -90.6 -179.9 -71.0 -147.0 70.7 -132.1 78 HIS 53.6 91.4 180.0 -131.9 113.8 79 GLN -83.4 -32.7 -179.9 -121.1 -165.4 112.1 80 ASN -53.0 -170.2 180.0 -138.7 -9.9 81 VAL -112.5 103.1 180.0 46.8 82 GLN -103.1 141.3 180.0 -157.1 82.8 -106.6 83 LEU -97.0 157.6 180.0 -49.6 172.6 84 PRO -72.8 -160.8 -180.0 24.6 -29.5 85 ARG 57.0 42.2 179.9 -178.0 158.1 55.7 154.1 86 GLU -160.0 38.5 -180.0 -95.7 -150.5 -119.9 87 GLY 179.7 60.2 179.9 88 GLN -134.5 2.3 179.9 59.4 157.2 -129.0 89 GLU 168.4 10.4 -179.8 -117.6 127.2 10.9 90 ASP -102.5 0.9 -179.8 -85.4 -160.3 91 GLN -92.5 -30.1 -180.0 -68.6 -125.7 20.2 92 GLY 145.9 -72.8 179.3 93 LEU -118.4 119.2 179.7 -124.9 155.1 94 THR -133.3 120.8 180.0 75.2 95 LYS -111.9 141.0 180.0 -105.1 49.9 171.6 140.5 96 ASP -102.1 137.0 -179.9 -47.1 -102.1 97 TYR -25.3 135.1 -180.0 61.5 112.6 98 GLY 87.4 -104.2 -180.0 99 ASN 178.2 158.9 180.0 50.5 9.9 100 SER -93.4 141.7 180.0 110.9 101 PRO -72.7 170.7 -179.8 24.6 -29.4 102 LEU -74.5 4.4 179.9 79.3 -46.1 103 HIS -115.5 15.6 -179.9 -112.5 -44.9 104 ARG -79.4 -48.1 180.0 -145.0 -62.5 168.0 81.4 105 PHE -110.5 166.5 -180.0 172.8 -115.9 106 LYS -73.7 -151.3 180.0 -56.8 -105.4 -146.1 84.7 107 LYS -51.3 107.2 -179.9 -65.2 114.3 -167.3 -167.7 108 PRO -73.4 -176.7 180.0 24.7 -29.0 109 GLY 101.1 135.2 180.0 110 SER -121.9 -179.9 180.0 -149.0 111 LYS -107.0 163.1 -179.9 -98.0 141.9 148.4 -92.8 112 ASN -105.4 -139.0 -179.9 -57.2 -4.8 113 PHE 56.1 102.0 -179.9 -116.5 -112.2 114 GLN -170.1 60.5 -179.7 77.4 -35.2 -66.1 115 ASN 75.4 107.2 -179.9 -39.3 132.4 116 ILE -94.5 131.8 -179.7 96.1 95.3 117 PHE -113.8 158.4 179.9 -60.8 -79.2 118 PRO -72.1 142.7 -179.9 24.6 -29.8 119 PRO -72.7 97.1 179.9 24.6 -29.6 120 SER -110.0 171.6 -179.3 -21.1 121 ALA -134.6 120.2 178.7 122 THR -119.9 117.3 -179.0 9.8 123 LEU -116.3 148.9 179.7 178.6 124.0 124 HIS -116.0 139.0 -179.5 -136.7 -86.9 125 LEU -99.4 130.5 -179.7 -119.2 -47.0 126 SER -87.7 156.0 -179.7 -157.3 127 ASN -15.7 131.5 179.5 -120.4 117.9 128 ILE -100.2 149.3 -179.9 -62.3 92.3 129 PRO -68.8 154.1 -179.9 24.3 -32.4 130 PRO -72.1 78.8 -180.0 24.5 -29.8 131 SER 177.7 -38.7 179.8 154.8 132 VAL -101.8 125.2 -179.9 172.2 133 SER -82.9 173.4 -179.9 -22.3 134 GLU -66.6 -29.3 -179.9 -54.7 152.5 34.2 135 GLU -61.3 -36.4 -180.0 -151.2 115.2 91.8 136 ASP -62.8 -47.6 179.9 -70.7 -142.0 137 LEU -71.8 -45.5 179.9 -123.1 122.5 138 LYS -55.0 -40.7 179.7 164.6 -168.0 -167.6 -113.4 139 VAL -67.4 -39.3 179.7 161.1 140 LEU -60.9 -48.7 -179.9 -69.0 168.4 141 PHE -54.2 -29.4 -179.5 -85.5 130.4 142 SER -82.0 -65.8 -179.2 -32.7 143 SER -74.5 -37.0 -179.7 -64.0 144 ASN -97.2 -30.4 180.0 -66.1 -110.4 145 GLY -70.7 -58.2 179.9 146 GLY 140.5 -82.2 -179.9 147 VAL -123.6 107.5 179.9 176.5 148 VAL -100.7 108.6 -180.0 172.2 149 LYS -82.0 -15.6 -179.9 -137.3 -146.6 -51.0 -148.7 150 GLY 155.1 153.1 180.0 151 PHE -136.2 134.3 179.9 84.2 -69.2 152 LYS -119.2 115.1 -180.0 -62.7 124.9 109.3 143.4 153 PHE -99.6 129.8 -179.9 -93.5 44.4 154 PHE -167.9 -164.8 -179.7 31.0 39.0 155 GLN -79.7 -7.9 -179.6 64.9 169.3 71.9 156 LYS -17.6 -98.1 -179.6 179.8 87.9 145.6 -157.3 157 ASP -76.6 46.3 179.6 -120.4 94.0 158 ARG 62.9 98.5 -179.8 -143.9 165.2 90.5 176.3 159 LYS 52.1 22.1 -179.8 -81.9 -45.1 -50.1 -99.6 160 MET -112.4 169.6 -179.5 -102.2 50.7 153.1 161 ALA -146.4 162.1 180.0 162 LEU -126.1 147.6 179.8 -148.0 168.5 163 ILE -128.7 139.4 -180.0 -32.1 101.6 164 GLN -95.9 134.2 179.6 -100.4 114.5 -10.8 165 MET -140.2 92.5 -179.5 -52.1 114.8 124.3 166 GLY -28.5 -74.7 179.8 167 SER -58.5 108.4 -179.7 -65.1 168 VAL -61.3 -44.9 179.6 -168.2 169 GLU -53.5 -32.3 179.6 -62.5 152.2 160.0 170 GLU -69.5 -38.8 -179.7 -91.5 75.2 -56.7 171 ALA -57.4 -46.1 179.4 172 VAL -67.8 -36.6 179.9 -172.5 173 GLN -53.7 -34.2 -179.9 -148.2 152.6 -41.9 174 ALA -58.3 -42.8 -179.9 175 LEU -57.5 -50.4 179.0 -171.6 97.2 176 ILE -70.1 -47.6 -178.4 -53.8 -49.1 177 ASP -71.8 -49.0 -179.3 -66.4 -117.4 178 LEU -61.1 -43.9 180.0 -56.6 -127.0 179 HIS -112.8 37.8 -179.8 -50.6 144.9 180 ASN -59.0 -39.2 180.0 171.1 -75.9 181 HIS -117.8 106.5 -180.0 -172.1 111.5 182 ASP -114.0 -162.0 -180.0 64.1 -55.3 183 LEU -126.4 -28.3 180.0 50.8 153.7 184 GLY 160.0 -78.5 179.9 185 GLU -51.9 -25.9 179.9 -160.4 -133.0 -49.3 186 ASN 65.9 11.0 179.8 -144.8 148.0 187 HIS 68.3 -173.8 179.9 -37.4 116.1 188 HIS -101.8 -1.7 179.6 -170.9 -68.5 189 LEU -76.0 120.0 -179.1 66.4 96.3 190 ARG -113.5 137.2 179.3 -137.9 -113.1 138.3 67.0 191 VAL -117.7 117.7 -179.9 160.2 192 SER -128.9 140.9 179.9 19.9 193 PHE -87.9 123.4 -179.9 85.6 90.3 194 SER -122.3 146.1 -180.0 -145.9 195 LYS -104.8 110.4 180.0 168.7 174.4 128.7 97.3 196 SER -94.8 -143.2 179.8 -145.0 197 THR -74.5 158.6 -180.0 15.1 198 ILE 70.4 -133.4 0.0 -37.6 116.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 179.708 -9.097 -5.556 2 GLY 176.167 -10.275 -6.386 3 ASN 172.569 -9.054 -5.965 4 SER 171.929 -6.929 -2.850 5 VAL 169.225 -4.258 -3.276 6 LEU 166.470 -3.604 -0.708 7 LEU 163.040 -3.327 -2.362 8 VAL 160.534 -1.071 -0.563 9 SER 156.821 -1.957 -0.712 10 ASN 154.460 1.049 -0.722 11 LEU 154.131 3.301 -3.818 12 ASN 150.336 2.800 -3.814 13 PRO 148.688 6.062 -4.894 14 GLU 150.093 8.387 -7.583 15 ARG 151.223 11.279 -5.376 16 VAL 153.406 8.703 -3.592 17 THR 156.369 8.419 -5.996 18 PRO 159.830 6.989 -5.337 19 GLN 161.125 10.554 -4.885 20 SER 159.471 10.665 -1.444 21 LEU 160.098 6.994 -0.599 22 PHE 163.677 7.333 -1.877 23 ILE 164.188 10.143 0.659 24 LEU 163.468 7.642 3.460 25 PHE 166.320 5.396 2.308 26 GLY 168.230 8.437 1.001 27 VAL 168.938 9.124 4.691 28 TYR 172.381 7.698 3.817 29 GLY 172.454 8.806 0.155 30 ASP 174.048 5.476 -0.809 31 VAL 171.559 3.951 -3.297 32 GLN 173.582 3.876 -6.536 33 ARG 170.367 3.703 -8.582 34 VAL 166.591 3.385 -8.087 35 LYS 164.236 1.651 -10.559 36 ILE 160.432 2.070 -10.567 37 LEU 158.186 0.273 -13.096 38 PHE 157.409 -3.472 -12.953 39 ASN 156.965 -2.879 -9.203 40 LYS 153.274 -2.488 -10.125 41 LYS 152.775 -0.013 -7.256 42 GLU 153.395 -1.143 -3.657 43 ASN 156.968 -1.956 -4.753 44 ALA 160.249 -0.131 -5.486 45 LEU 163.926 -0.888 -6.206 46 VAL 166.692 0.588 -4.012 47 GLN 170.285 -0.221 -5.029 48 MET 173.030 0.455 -2.457 49 ALA 173.500 -2.582 -0.180 50 ASP 175.519 -4.481 -2.785 51 GLY 175.648 -6.667 0.329 52 ASN 177.377 -4.090 2.598 53 GLN 175.039 -1.080 2.558 54 ALA 172.084 -3.301 3.507 55 GLN 174.034 -3.976 6.679 56 LEU 173.623 -0.270 7.446 57 ALA 170.401 0.321 5.406 58 MET 168.823 -3.150 5.740 59 SER 169.222 -3.105 9.546 60 HIS 168.721 0.645 10.090 61 LEU 165.565 0.765 7.944 62 ASN 164.121 -2.671 8.761 63 GLY 162.716 -3.292 12.259 64 HIS 161.641 0.364 11.916 65 LYS 158.323 -0.463 13.632 66 LEU 155.443 1.063 11.628 67 HIS 152.921 3.098 13.656 68 GLY 151.023 4.969 10.915 69 LYS 151.752 3.384 7.517 70 PRO 152.115 -0.369 7.008 71 ILE 155.085 -0.598 4.606 72 ARG 156.793 -3.853 3.570 73 ILE 160.528 -4.172 2.814 74 THR 162.134 -7.150 1.025 75 LEU 165.719 -8.019 0.022 76 SER 166.458 -9.259 -3.520 77 LYS 167.440 -12.953 -3.373 78 HIS 168.804 -14.519 -6.585 79 GLN 171.224 -17.217 -5.364 80 ASN 172.636 -17.996 -8.832 81 VAL 175.499 -15.845 -10.174 82 GLN 174.290 -12.777 -12.110 83 LEU 176.705 -10.249 -13.660 84 PRO 176.300 -6.468 -13.664 85 ARG 175.925 -4.357 -16.831 86 GLU 172.337 -5.607 -17.258 87 GLY 169.985 -3.322 -15.292 88 GLN 170.644 0.424 -15.687 89 GLU 168.042 1.460 -18.299 90 ASP 166.844 -1.681 -20.138 91 GLN 163.911 -2.405 -17.788 92 GLY 161.890 0.733 -18.581 93 LEU 162.313 3.400 -15.894 94 THR 165.677 3.761 -14.120 95 LYS 166.641 6.735 -11.921 96 ASP 170.143 7.361 -10.526 97 TYR 170.631 8.752 -6.988 98 GLY 169.904 12.505 -7.096 99 ASN 168.525 13.223 -10.589 100 SER 169.507 13.514 -14.274 101 PRO 170.282 16.904 -15.814 102 LEU 168.412 18.230 -18.875 103 HIS 171.424 17.147 -20.977 104 ARG 171.347 13.424 -20.104 105 PHE 168.952 12.282 -22.859 106 LYS 168.250 13.762 -26.315 107 LYS 164.954 15.474 -27.230 108 PRO 162.795 14.452 -24.272 109 GLY 158.986 14.161 -24.404 110 SER 156.891 11.056 -25.163 111 LYS 153.663 10.328 -27.079 112 ASN 150.199 9.461 -25.710 113 PHE 147.413 7.306 -27.204 114 GLN 147.574 3.855 -25.564 115 ASN 144.157 2.327 -24.757 116 ILE 141.639 4.742 -23.230 117 PHE 139.740 3.579 -20.131 118 PRO 136.585 4.917 -18.485 119 PRO 137.038 7.307 -15.561 120 SER 136.022 5.150 -12.571 121 ALA 136.581 5.647 -8.826 122 THR 137.695 2.975 -6.335 123 LEU 138.165 4.039 -2.698 124 HIS 139.332 1.969 0.277 125 LEU 138.199 2.499 3.884 126 SER 140.800 2.145 6.662 127 ASN 140.041 0.521 10.053 128 ILE 136.744 1.916 11.389 129 PRO 136.230 3.150 14.957 130 PRO 134.288 1.010 17.429 131 SER 130.920 2.765 16.988 132 VAL 130.154 3.270 13.276 133 SER 129.232 0.151 11.264 134 GLU 130.028 -0.337 7.555 135 GLU 126.391 0.460 6.695 136 ASP 126.874 4.025 7.978 137 LEU 129.835 4.692 5.651 138 LYS 128.407 2.674 2.745 139 VAL 125.230 4.788 2.919 140 LEU 127.279 7.998 2.973 141 PHE 129.196 7.043 -0.194 142 SER 125.788 6.704 -1.889 143 SER 123.786 9.726 -0.685 144 ASN 126.850 11.747 0.387 145 GLY 129.445 10.150 -1.918 146 GLY 127.525 10.548 -5.196 147 VAL 127.533 7.417 -7.388 148 VAL 128.159 4.057 -5.675 149 LYS 128.565 1.238 -8.226 150 GLY 129.258 -1.290 -5.443 151 PHE 131.428 -1.793 -2.339 152 LYS 133.395 -4.877 -1.230 153 PHE 134.518 -5.111 2.414 154 PHE 137.174 -7.718 3.295 155 GLN 140.773 -8.253 4.470 156 LYS 142.060 -6.757 1.173 157 ASP 144.209 -3.890 2.535 158 ARG 144.264 -5.547 5.993 159 LYS 140.878 -5.020 7.690 160 MET 140.350 -2.566 4.818 161 ALA 137.730 -2.511 2.025 162 LEU 137.273 -0.939 -1.420 163 ILE 134.219 0.697 -3.055 164 GLN 133.571 1.396 -6.755 165 MET 132.083 4.774 -7.742 166 GLY 131.771 5.394 -11.479 167 SER 131.894 9.197 -11.147 168 VAL 135.411 9.728 -9.749 169 GLU 134.572 13.253 -8.535 170 GLU 131.833 11.561 -6.481 171 ALA 134.309 9.165 -4.831 172 VAL 136.309 12.088 -3.406 173 GLN 133.082 13.868 -2.423 174 ALA 132.462 11.055 0.086 175 LEU 135.547 12.039 2.085 176 ILE 134.298 15.629 2.356 177 ASP 130.583 14.720 2.493 178 LEU 130.824 11.566 4.636 179 HIS 133.169 13.346 7.030 180 ASN 132.154 16.952 6.249 181 HIS 131.765 17.660 9.987 182 ASP 134.339 15.982 12.265 183 LEU 135.830 16.805 15.689 184 GLY 139.609 16.451 15.235 185 GLU 141.059 12.919 15.401 186 ASN 138.681 12.171 12.503 187 HIS 138.472 8.618 13.905 188 HIS 140.560 5.786 12.406 189 LEU 138.332 5.330 9.332 190 ARG 140.272 6.580 6.286 191 VAL 138.794 7.235 2.818 192 SER 141.179 7.450 -0.165 193 PHE 140.398 7.519 -3.908 194 SER 142.351 4.882 -5.873 195 LYS 142.367 4.195 -9.634 196 SER 142.297 0.468 -10.484 197 THR 141.695 -1.164 -13.884 198 ILE 139.307 0.506 -16.362 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S S S S 10 C C T T T T H H H H 20 H H H H H H H C C C 30 C S S S S S S S T T 40 T T S S S S S S C C 50 H H H H H 3/H H H H H 60 H H C C C T T T T/S S 70 S S S S S S S S S S/S 80 S S S S S C T T T T 90 C S S S S S S C S S 100 S S C S S S S/S S S S 110 S S S S S S S S S/S S 120 S S S S S S S/S S S S 130 C C H H H H H H H H 140 H H H S S S S C S S 150 S S S S S/T T T T S S 160 S S S/S S S S H H H H 170 H H H H/T T T T C C S 180 S S S S C C C S S S 190 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 E 10 S S S h H H H 20 H H H H H H h T t 30 e E E E e t T T t 40 S S E E E t T T 50 h H H H H H H H H H 60 H h T t S S 70 E E E E e S 80 S S S S S S S 90 S S e E E E e S 100 t T T t S S S 110 S 120 e E E E E e t T 130 T t h H H H H H H H 140 H H H h T t E 150 E E E e t T T t S e 160 E E E E e S h H H H 170 H H H H H H H H h t 180 S S S S e 190 E E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 0.0 0.0 97.3 2 GLY 9.1 26.1 85.2 3 ASN 73.5 60.8 67.2 4 SER 71.7 85.7 56.5 5 VAL 104.4 87.8 51.8 6 LEU 147.8 100.0 32.6 7 LEU 112.9 76.4 57.0 8 VAL 114.2 96.1 32.9 9 SER 74.9 89.6 65.2 10 ASN 85.5 70.7 43.6 11 LEU 139.2 94.2 47.2 12 ASN 61.4 50.8 63.5 13 PRO 73.8 59.3 63.8 14 GLU 59.5 42.9 70.1 15 ARG 0.0 0.0 89.0 16 VAL 76.8 64.7 66.7 17 THR 40.1 37.5 67.7 18 PRO 108.9 87.5 29.0 19 GLN 3.5 2.4 81.3 20 SER 23.7 28.4 72.2 21 LEU 136.4 92.3 38.1 22 PHE 135.1 81.0 44.3 23 ILE 29.2 20.4 72.8 24 LEU 39.4 26.6 74.1 25 PHE 166.4 99.7 25.7 26 GLY 24.4 70.0 53.7 27 VAL 50.6 42.6 67.3 28 TYR 160.9 88.9 36.2 29 GLY 3.2 9.1 68.6 30 ASP 64.9 58.7 63.6 31 VAL 118.8 100.0 37.1 32 GLN 67.8 45.6 77.3 33 ARG 133.6 64.0 67.4 34 VAL 114.2 96.1 36.9 35 LYS 150.0 86.5 49.5 36 ILE 105.9 73.8 42.5 37 LEU 115.9 78.4 61.5 38 PHE 0.0 0.0 87.3 39 ASN 104.9 86.8 53.6 40 LYS 3.9 2.3 89.3 41 LYS 87.1 50.2 77.7 42 GLU 63.4 45.7 79.3 43 ASN 67.2 55.6 67.0 44 ALA 72.3 99.6 45.2 45 LEU 114.5 77.5 54.3 46 VAL 118.8 100.0 31.3 47 GLN 91.8 61.8 57.3 48 MET 159.4 100.0 38.8 49 ALA 72.6 100.0 41.7 50 ASP 45.4 41.1 74.9 51 GLY 8.9 25.7 75.2 52 ASN 3.2 2.6 84.1 53 GLN 110.3 74.2 56.9 54 ALA 67.7 93.2 40.6 55 GLN 28.6 19.2 85.3 56 LEU 46.0 31.2 70.5 57 ALA 72.6 100.0 35.5 58 MET 101.1 63.4 57.1 59 SER 31.9 38.1 75.8 60 HIS 43.8 29.1 68.2 61 LEU 129.2 87.4 47.6 62 ASN 88.1 72.9 48.1 63 GLY 0.0 0.0 82.6 64 HIS 98.0 65.3 59.7 65 LYS 11.2 6.5 89.0 66 LEU 103.7 70.2 59.7 67 HIS 5.7 3.8 89.8 68 GLY 0.3 0.8 78.2 69 LYS 44.1 25.4 70.9 70 PRO 61.0 49.0 68.7 71 ILE 122.9 85.7 47.1 72 ARG 38.2 18.3 86.9 73 ILE 129.5 90.2 53.6 74 THR 26.3 24.6 76.8 75 LEU 83.7 56.6 60.2 76 SER 61.3 73.3 59.4 77 LYS 22.4 12.9 90.4 78 HIS 69.7 46.4 76.1 79 GLN 1.7 1.2 93.0 80 ASN 11.4 9.4 78.2 81 VAL 12.0 10.1 80.3 82 GLN 67.7 45.5 75.1 83 LEU 29.6 20.0 76.3 84 PRO 14.4 11.6 78.7 85 ARG 5.9 2.8 89.4 86 GLU 25.0 18.0 87.0 87 GLY 23.8 68.4 66.5 88 GLN 56.3 37.9 74.3 89 GLU 75.5 54.5 82.5 90 ASP 10.2 9.2 81.8 91 GLN 71.2 47.9 66.8 92 GLY 1.6 4.7 73.7 93 LEU 67.5 45.7 65.1 94 THR 106.0 99.1 53.8 95 LYS 65.9 38.0 68.7 96 ASP 85.6 77.5 65.6 97 TYR 55.5 30.7 73.6 98 GLY 0.0 0.0 80.8 99 ASN 10.6 8.8 88.2 100 SER 44.8 53.6 68.0 101 PRO 44.5 35.8 70.4 102 LEU 20.4 13.8 77.8 103 HIS 16.6 11.1 76.3 104 ARG 106.3 50.9 76.6 105 PHE 41.2 24.7 73.6 106 LYS 20.4 11.8 74.9 107 LYS 7.9 4.5 78.0 108 PRO 30.4 24.4 77.1 109 GLY 0.0 0.0 81.5 110 SER 2.6 3.1 86.4 111 LYS 0.0 0.0 92.5 112 ASN 5.8 4.8 85.6 113 PHE 0.0 0.0 88.7 114 GLN 41.6 28.0 79.0 115 ASN 18.2 15.1 72.0 116 ILE 6.9 4.8 86.0 117 PHE 73.5 44.1 72.8 118 PRO 57.5 46.2 57.6 119 PRO 19.2 15.4 76.9 120 SER 65.9 78.9 65.0 121 ALA 70.9 97.7 54.3 122 THR 99.9 93.5 46.6 123 LEU 146.7 99.3 37.1 124 HIS 131.0 87.2 43.0 125 LEU 147.6 99.9 30.8 126 SER 64.2 76.8 48.0 127 ASN 64.6 53.4 62.1 128 ILE 116.7 81.3 50.4 129 PRO 104.9 84.3 36.7 130 PRO 4.9 4.0 81.6 131 SER 14.7 17.6 75.3 132 VAL 74.8 63.0 63.0 133 SER 16.8 20.1 79.8 134 GLU 53.3 38.4 59.9 135 GLU 30.8 22.2 73.2 136 ASP 44.5 40.3 65.5 137 LEU 145.8 98.6 28.1 138 LYS 103.1 59.5 54.2 139 VAL 43.5 36.6 71.1 140 LEU 103.8 70.2 61.0 141 PHE 165.5 99.2 25.0 142 SER 47.0 56.3 67.8 143 SER 18.3 21.9 81.6 144 ASN 73.1 60.5 58.0 145 GLY 34.2 98.2 56.8 146 GLY 18.5 53.1 66.7 147 VAL 52.8 44.4 75.2 148 VAL 102.9 86.6 55.2 149 LYS 63.9 36.8 71.2 150 GLY 7.2 20.6 67.4 151 PHE 116.6 69.9 42.5 152 LYS 65.3 37.6 75.7 153 PHE 142.4 85.3 38.4 154 PHE 96.3 57.7 63.5 155 GLN 4.5 3.0 82.2 156 LYS 68.2 39.4 63.6 157 ASP 34.8 31.5 66.3 158 ARG 43.8 21.0 75.5 159 LYS 40.4 23.3 83.1 160 MET 127.2 79.8 67.5 161 ALA 69.3 95.5 42.9 162 LEU 122.9 83.1 46.4 163 ILE 142.6 99.4 31.1 164 GLN 98.8 66.5 55.2 165 MET 157.9 99.0 43.1 166 GLY 16.6 47.8 58.4 167 SER 47.8 57.2 68.1 168 VAL 75.4 63.4 58.1 169 GLU 7.8 5.6 83.1 170 GLU 104.6 75.5 63.6 171 ALA 72.5 99.8 38.7 172 VAL 54.3 45.7 59.8 173 GLN 65.2 43.8 78.5 174 ALA 72.6 100.0 42.0 175 LEU 91.5 61.9 65.9 176 ILE 44.6 31.1 75.3 177 ASP 73.0 66.1 57.1 178 LEU 147.8 100.0 38.2 179 HIS 126.9 84.5 53.2 180 ASN 34.1 28.2 73.3 181 HIS 5.5 3.7 93.0 182 ASP 63.6 57.6 67.0 183 LEU 47.8 32.3 74.3 184 GLY 3.0 8.6 82.1 185 GLU 22.2 16.0 79.2 186 ASN 62.4 51.6 69.1 187 HIS 95.8 63.8 53.2 188 HIS 46.6 31.0 76.5 189 LEU 142.0 96.1 45.4 190 ARG 58.4 28.0 79.5 191 VAL 118.8 100.0 33.2 192 SER 32.7 39.2 69.1 193 PHE 77.1 46.3 63.8 194 SER 43.1 51.6 71.1 195 LYS 49.9 28.8 87.7 196 SER 29.9 35.8 76.4 197 THR 8.1 7.6 76.5 198 ILE 46.8 32.6 70.6