Protein Data Bank File : 1rl6a Title : RNA-BINDING PROTEIN 14-JAN-99 1RL6 Number of Amino Acid Residues : 164 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PRO ILE GLU ILE PRO ALA GLY VAL THR VAL 10 THR VAL ASN GLY ASN THR VAL THR VAL LYS 20 GLY PRO LYS GLY GLU LEU THR ARG THR PHE 30 HIS PRO ASP MET THR ILE THR VAL GLU GLY 40 ASN VAL ILE THR VAL THR ARG PRO SER ASP 50 GLU LYS HIS HIS ARG ALA LEU HIS GLY THR 60 THR ARG SER LEU LEU ALA ASN MET VAL GLU 70 GLY VAL SER LYS GLY TYR GLU LYS ALA LEU 80 GLU LEU VAL GLY VAL GLY TYR ARG ALA SER 90 LYS GLN GLY LYS LYS LEU VAL LEU SER VAL 100 GLY TYR SER HIS PRO VAL GLU ILE GLU PRO 110 GLU GLU GLY LEU GLU ILE GLU VAL PRO SER 120 GLN THR LYS ILE ILE VAL LYS GLY ALA ASP 130 LYS GLN ARG VAL GLY GLU LEU ALA ALA ASN 140 ILE ARG ALA VAL ARG PRO PRO GLU PRO TYR 150 LYS GLY LYS GLY ILE ARG TYR GLU GLY GLU 160 LEU VAL ARG LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PRO 0.0 166.3 178.1 40.4 -37.6 2 ILE -104.7 124.4 179.7 -64.7 85.4 3 GLU -71.9 130.9 177.5 -127.3 -146.1 68.8 4 ILE -90.4 106.4 -179.9 -60.8 -178.8 5 PRO -67.6 174.4 -179.8 30.1 -42.9 6 ALA -70.3 147.5 -179.6 7 GLY 83.5 -11.9 -179.2 8 VAL -96.5 129.6 177.1 172.8 9 THR -112.4 125.3 178.7 -56.2 10 VAL -112.5 131.6 -179.7 176.6 11 THR -127.6 132.8 180.0 -72.4 12 VAL -122.4 135.0 -179.5 -175.6 13 ASN -143.8 90.6 -179.3 166.3 56.8 14 GLY 72.7 -121.2 -179.9 15 ASN -102.0 8.3 -179.3 66.3 -33.8 16 THR -104.9 128.5 178.8 -40.8 17 VAL -118.2 129.7 176.6 177.0 18 THR -114.0 127.0 179.1 -63.0 19 VAL -122.6 129.2 179.7 -175.5 20 LYS -121.2 152.0 178.8 -36.9 161.8 61.4 168.1 21 GLY -166.9 -178.0 179.7 22 PRO -59.1 -35.2 -178.2 18.5 -38.2 23 LYS -87.3 -3.2 179.9 -58.0 -53.3 -153.9 -58.1 24 GLY 151.3 -173.5 -179.3 25 GLU -136.3 136.3 -178.7 -170.2 176.3 -25.5 26 LEU -138.0 137.2 179.0 -57.0 171.6 27 THR -119.5 131.1 -179.0 -66.7 28 ARG -142.3 144.0 177.3 -149.5 179.8 -172.3 -59.8 29 THR -102.4 144.5 -179.6 -74.1 30 PHE -122.4 167.1 -180.0 -61.2 81.9 31 HIS -54.5 123.6 -180.0 -166.1 -72.9 32 PRO -41.6 -41.9 -178.6 -38.6 45.4 33 ASP -63.9 -16.9 179.9 -74.3 14.5 34 MET -89.9 136.7 177.2 -61.9 -66.5 111.9 35 THR -108.1 126.0 -179.0 -61.0 36 ILE -116.1 129.3 -178.9 -59.9 167.0 37 THR -140.2 141.9 176.8 68.3 38 VAL -91.0 103.8 -179.8 174.8 39 GLU -90.6 80.3 -178.7 -131.1 76.4 82.1 40 GLY 65.2 -94.5 -179.0 41 ASN -102.4 -1.0 179.4 49.0 6.5 42 VAL -135.4 153.3 179.5 -67.2 43 ILE -97.9 129.9 180.0 -45.3 162.3 44 THR -115.8 143.6 177.0 -57.8 45 VAL -116.5 126.0 -178.6 -172.1 46 THR -119.2 122.0 177.1 -66.7 47 ARG -88.2 153.2 -179.0 58.1 175.7 -179.8 -113.1 48 PRO -70.5 -30.8 -179.8 30.9 -40.5 49 SER -143.8 -175.3 -179.6 83.4 50 ASP -109.5 15.7 178.4 -73.3 -66.3 51 GLU -67.5 175.9 -179.9 -79.8 -168.4 70.7 52 LYS -68.1 -52.6 -178.1 -176.5 -173.1 -178.2 -176.3 53 HIS -52.7 -33.7 178.9 62.8 -94.7 54 HIS -75.0 -42.8 179.2 -77.5 132.7 55 ARG -59.2 -37.6 -179.9 -175.0 162.1 -66.5 95.1 56 ALA -73.2 -39.3 178.2 57 LEU -63.3 -41.6 -179.1 -96.2 169.3 58 HIS -57.7 -51.1 178.9 -163.6 -161.2 59 GLY -68.5 -36.0 178.5 60 THR -66.9 -43.2 178.1 -64.8 61 THR -63.4 -44.6 179.3 -62.6 62 ARG -59.3 -46.3 179.6 -124.9 150.9 53.5 -149.3 63 SER -60.8 -50.0 179.2 -54.5 64 LEU -53.0 -42.8 179.8 -90.9 52.1 65 LEU -65.8 -46.4 -180.0 -78.3 159.5 66 ALA -53.0 -51.0 179.4 67 ASN -64.3 -28.6 178.3 -66.3 -6.4 68 MET -71.4 -38.9 179.2 -78.7 -179.6 91.0 69 VAL -69.3 -37.5 179.2 175.6 70 GLU -67.9 -40.5 179.6 -163.3 -176.5 -31.1 71 GLY -60.9 -46.8 -179.8 72 VAL -80.8 -12.4 179.5 -54.4 73 SER -101.2 -52.0 -179.7 67.3 74 LYS -96.5 -26.2 -179.3 -61.0 166.4 -171.5 -179.7 75 GLY 69.4 165.6 178.3 76 TYR -126.3 157.9 178.0 -62.3 -82.3 77 GLU -151.9 156.1 179.6 56.4 179.2 64.9 78 LYS -140.1 127.4 179.0 -171.1 68.2 -158.3 63.3 79 ALA -101.3 148.5 179.3 80 LEU -132.1 155.9 178.4 -63.3 147.2 81 GLU -133.1 145.7 179.4 35.7 -162.6 40.8 82 LEU -96.8 134.6 178.6 -65.5 -154.0 83 VAL -129.7 118.4 -179.9 180.0 84 GLY 148.1 138.4 -178.8 85 VAL -66.9 127.5 -178.6 -59.0 86 GLY 91.6 -11.6 179.6 87 TYR -77.3 118.3 179.2 -75.3 18.1 88 ARG -152.3 155.3 -180.0 46.5 171.6 -170.0 -84.5 89 ALA -120.1 148.7 177.6 90 SER -149.0 162.1 179.4 71.9 91 LYS -108.9 116.7 178.8 -154.1 72.8 -165.0 -51.9 92 GLN -119.6 89.5 -178.4 -56.0 -69.0 100.1 93 GLY 81.3 -142.1 179.0 94 LYS -80.5 -10.4 -178.3 -162.6 99.0 177.8 59.2 95 LYS -82.1 140.9 174.9 -96.1 175.9 -58.2 166.4 96 LEU -92.0 127.0 -179.9 166.6 64.5 97 VAL -114.1 121.7 -178.7 -176.4 98 LEU -110.6 132.7 176.6 -63.6 165.5 99 SER -116.9 98.5 -178.3 -78.6 100 VAL -126.6 44.3 176.6 -67.3 101 GLY 79.7 22.0 177.0 102 TYR -108.5 172.6 -179.4 -64.9 -44.1 103 SER -63.2 -36.9 -179.2 77.4 104 HIS -126.7 162.6 179.9 -66.9 83.0 105 PRO -71.5 156.9 178.2 35.3 -45.9 106 VAL -106.3 125.5 -179.7 -176.3 107 GLU -110.6 128.6 -179.9 -61.0 176.3 -27.8 108 ILE -123.2 131.8 179.7 -70.0 168.6 109 GLU -114.8 121.8 -179.9 -165.1 -178.2 -41.4 110 PRO -68.9 153.9 177.8 32.0 -43.4 111 GLU -77.9 -179.9 178.8 -109.0 64.5 -46.9 112 GLU -65.1 136.5 179.8 177.4 167.7 21.7 113 GLY 91.9 -4.7 -179.5 114 LEU -120.5 142.1 178.7 -66.0 172.2 115 GLU -125.7 153.5 179.1 -71.3 -168.1 57.4 116 ILE -134.4 125.7 179.2 -62.1 164.3 117 GLU -117.3 147.5 -179.3 -64.1 -178.5 -10.0 118 VAL -128.5 84.1 -179.6 -176.1 119 PRO -68.1 -25.7 177.1 28.1 -40.8 120 SER -146.0 157.4 -178.8 75.8 121 GLN -60.8 -8.0 -179.8 50.6 -173.5 14.6 122 THR -121.3 13.9 179.8 60.5 123 LYS -130.9 132.2 179.2 179.3 122.7 57.7 -179.3 124 ILE -124.2 132.4 177.2 -51.3 168.8 125 ILE -120.7 125.4 178.0 -61.0 173.9 126 VAL -104.5 134.8 179.6 -178.5 127 LYS -144.4 154.0 -179.8 44.2 -133.6 -78.8 -175.2 128 GLY 176.1 -179.0 -178.2 129 ALA -84.5 -25.3 -179.8 130 ASP -96.3 109.7 179.7 -167.7 -55.9 131 LYS -55.5 -35.7 -180.0 -165.0 39.6 177.2 168.8 132 GLN -70.0 -49.1 -178.7 178.7 70.7 18.4 133 ARG -64.0 -30.1 178.8 -69.8 -173.0 72.3 -143.7 134 VAL -69.9 -45.4 -179.6 173.1 135 GLY -61.0 -44.5 -179.9 136 GLU -64.6 -43.0 177.9 178.6 -141.2 -31.3 137 LEU -68.4 -39.7 177.9 174.1 61.5 138 ALA -63.7 -33.1 178.0 139 ALA -71.9 -33.4 178.2 140 ASN -72.2 -34.6 177.0 -70.7 148.1 141 ILE -68.7 -50.2 178.4 -65.0 -177.4 142 ARG -54.7 -38.3 179.4 169.7 -179.1 -174.3 -78.6 143 ALA -64.5 -14.6 178.2 144 VAL -62.8 -41.1 177.2 164.3 145 ARG -160.1 84.3 179.8 -175.7 148.6 -168.9 172.7 146 PRO -64.2 162.6 -179.3 -18.1 36.4 147 PRO -58.9 129.4 178.1 -22.6 38.4 148 GLU -90.3 139.8 -178.8 49.6 82.6 24.0 149 PRO -54.1 -30.2 -175.9 33.7 -45.7 150 TYR -81.1 -33.6 -177.6 -51.4 -67.3 151 LYS -133.5 -3.7 178.9 -142.0 67.1 -88.1 -56.5 152 GLY 74.8 18.7 179.1 153 LYS -76.0 150.0 179.8 -71.9 -162.9 -53.5 179.8 154 GLY 129.6 -157.8 -179.7 155 ILE -109.9 134.7 179.0 -49.4 170.4 156 ARG -135.9 159.4 176.2 72.3 -175.7 51.1 172.9 157 TYR -66.6 157.7 -178.2 -66.5 -56.7 158 GLU -47.7 -53.3 179.1 -172.2 -179.4 52.3 159 GLY -98.6 30.5 -177.6 160 GLU -72.8 116.8 179.8 -170.5 167.3 -16.9 161 LEU -78.1 97.8 178.6 -143.4 173.0 162 VAL -128.7 86.1 179.2 48.0 163 ARG -72.5 132.2 -177.5 -112.3 142.6 157.7 117.7 164 LEU -73.1 -84.6 0.0 -58.0 -29.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PRO 64.061 13.461 81.186 2 ILE 66.808 16.104 81.571 3 GLU 67.714 17.139 85.065 4 ILE 67.621 20.918 85.662 5 PRO 70.641 21.635 87.861 6 ALA 70.628 24.408 90.419 7 GLY 70.890 27.981 89.251 8 VAL 69.406 26.943 85.924 9 THR 66.064 28.355 84.717 10 VAL 64.298 26.606 81.771 11 THR 61.460 28.270 79.869 12 VAL 59.349 26.636 77.149 13 ASN 56.996 28.414 74.774 14 GLY 55.709 26.214 71.997 15 ASN 58.763 24.923 70.165 16 THR 61.220 27.499 71.491 17 VAL 63.223 26.712 74.619 18 THR 65.218 29.215 76.682 19 VAL 67.778 27.993 79.235 20 LYS 69.645 30.429 81.504 21 GLY 72.447 29.707 83.927 22 PRO 75.659 31.081 85.449 23 LYS 77.623 30.529 82.251 24 GLY 75.116 32.090 79.843 25 GLU 71.639 32.006 78.261 26 LEU 70.607 30.063 75.132 27 THR 67.371 29.972 73.141 28 ARG 66.669 27.182 70.717 29 THR 63.766 26.031 68.555 30 PHE 62.993 22.326 68.083 31 HIS 61.075 20.149 65.651 32 PRO 57.318 20.947 65.887 33 ASP 56.399 17.288 66.330 34 MET 58.273 17.121 69.626 35 THR 56.560 18.217 72.873 36 ILE 58.873 19.667 75.497 37 THR 57.710 20.254 79.067 38 VAL 59.322 21.311 82.344 39 GLU 57.997 18.646 84.731 40 GLY 58.858 20.438 87.983 41 ASN 62.591 19.691 88.280 42 VAL 63.176 17.875 84.916 43 ILE 62.643 18.590 81.226 44 THR 60.700 15.878 79.498 45 VAL 60.488 15.263 75.689 46 THR 57.379 13.446 74.311 47 ARG 57.297 12.242 70.701 48 PRO 53.885 11.892 68.929 49 SER 54.348 8.263 67.803 50 ASP 56.637 5.230 67.897 51 GLU 57.672 5.208 64.278 52 LYS 61.398 5.403 63.530 53 HIS 61.723 9.027 62.436 54 HIS 60.125 10.092 65.697 55 ARG 62.283 7.815 67.813 56 ALA 65.311 9.394 66.094 57 LEU 63.908 12.908 66.505 58 HIS 63.274 12.177 70.202 59 GLY 66.881 11.208 71.020 60 THR 68.278 14.082 68.904 61 THR 66.006 16.658 70.683 62 ARG 66.986 15.188 74.065 63 SER 70.704 15.504 73.331 64 LEU 70.422 19.142 72.211 65 LEU 68.635 19.995 75.431 66 ALA 71.186 18.142 77.534 67 ASN 74.007 20.115 75.885 68 MET 72.089 23.413 76.300 69 VAL 71.849 22.571 79.998 70 GLU 75.576 21.660 80.124 71 GLY 76.603 24.923 78.399 72 VAL 74.909 27.392 80.756 73 SER 75.857 25.417 83.825 74 LYS 79.315 24.106 83.072 75 GLY 80.108 26.250 80.026 76 TYR 82.562 25.362 77.229 77 GLU 86.056 26.575 76.395 78 LYS 88.832 26.354 73.839 79 ALA 92.456 27.421 74.506 80 LEU 95.040 28.830 72.035 81 GLU 98.735 29.596 72.533 82 LEU 101.099 32.178 70.992 83 VAL 104.496 31.007 69.798 84 GLY 107.083 33.505 68.733 85 VAL 109.369 36.052 70.293 86 GLY 107.481 39.316 70.911 87 TYR 104.145 37.582 70.321 88 ARG 101.755 38.475 73.096 89 ALA 98.100 38.929 73.999 90 SER 96.439 41.269 76.498 91 LYS 92.958 42.233 77.568 92 GLN 91.973 45.888 77.041 93 GLY 88.329 46.094 78.035 94 LYS 86.161 43.432 76.438 95 LYS 88.754 43.460 73.648 96 LEU 91.538 40.961 72.958 97 VAL 94.676 42.804 71.746 98 LEU 97.144 40.707 69.754 99 SER 100.758 41.597 68.988 100 VAL 101.685 38.922 66.416 101 GLY 104.393 40.308 64.161 102 TYR 102.490 42.855 62.038 103 SER 103.292 46.564 62.116 104 HIS 100.296 47.154 64.436 105 PRO 98.181 45.085 66.870 106 VAL 95.040 43.130 65.973 107 GLU 92.025 43.815 68.225 108 ILE 89.146 41.349 68.513 109 GLU 85.941 41.955 70.333 110 PRO 83.790 38.925 71.123 111 GLU 80.143 38.960 70.233 112 GLU 77.358 38.646 72.746 113 GLY 77.465 35.433 74.739 114 LEU 81.283 34.983 74.259 115 GLU 84.238 35.721 76.546 116 ILE 87.953 35.707 75.938 117 GLU 90.366 35.398 78.807 118 VAL 94.144 35.924 78.676 119 PRO 95.640 34.308 81.841 120 SER 99.240 34.711 80.641 121 GLN 100.572 36.681 77.669 122 THR 100.875 33.609 75.513 123 LYS 97.585 31.891 76.340 124 ILE 94.099 32.828 75.166 125 ILE 90.898 31.087 76.388 126 VAL 87.560 31.484 74.582 127 LYS 84.456 30.530 76.526 128 GLY 80.722 30.548 76.366 129 ALA 77.578 28.421 76.499 130 ASP 77.399 27.554 72.835 131 LYS 80.088 24.935 71.973 132 GLN 79.824 25.834 68.306 133 ARG 80.212 29.575 68.692 134 VAL 83.181 28.947 70.987 135 GLY 84.758 26.699 68.361 136 GLU 84.133 29.291 65.627 137 LEU 85.620 32.324 67.444 138 ALA 88.751 30.349 68.448 139 ALA 89.221 29.322 64.760 140 ASN 88.877 32.952 63.735 141 ILE 91.484 34.075 66.266 142 ARG 93.950 31.392 65.144 143 ALA 93.309 32.477 61.521 144 VAL 94.705 35.970 62.303 145 ARG 98.123 34.383 62.127 146 PRO 98.249 30.575 61.935 147 PRO 101.554 28.638 62.685 148 GLU 104.290 29.013 60.036 149 PRO 106.089 25.830 58.906 150 TYR 109.710 26.714 59.437 151 LYS 109.573 27.644 63.083 152 GLY 105.982 27.175 64.226 153 LYS 105.407 30.854 64.990 154 GLY 101.870 32.157 65.041 155 ILE 98.758 31.162 66.965 156 ARG 97.917 27.470 67.456 157 TYR 95.282 25.600 69.404 158 GLU 96.581 24.517 72.845 159 GLY 97.365 20.939 71.819 160 GLU 98.160 21.647 68.143 161 LEU 100.723 19.292 66.643 162 VAL 102.714 21.517 64.337 163 ARG 106.095 19.975 63.812 164 LEU 108.610 22.381 62.294 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 10 S S S/T T T T/S S S S S 20 S/T T T T/S S S S S S S 30 S S S S S S S S/T T T 40 T/S S S S S S S S S C 50 H H H H H H H H H H 60 H H H H H H H H H H 70 H H H H/S S S S S S S 80 S S S S S S S S S S 90 S S/T T T T/S S S S S S 100 S C S S S S S S S S 110 S S S S S S S S S S/T 120 T T T/S S S S S S S H 130 H H H H H H H H H H 140 H H H H/S S S S T T T 150 T C C S S S S S/S S S 160 S/S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E e t T T t E E 10 E E E T e E E E E E 20 E T T E E E E E E e 30 t T T t E E E E E T 40 e E E E E E S 50 h H H H H H H H H H 60 H H H H H H H H H H 70 H H H h t E E E E E 80 E E E t T T t E E E 90 E E T T E E E E E S 100 S S S S E E E 110 t T e E E E E E E E 120 T e E E E E E E e h 130 H H H H H H H H H H 140 H H h T t t T T 150 T t E E E E e T t 160 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PRO 49.0 39.4 69.7 2 ILE 125.7 87.6 42.8 3 GLU 18.2 13.1 77.7 4 ILE 126.7 88.3 51.1 5 PRO 81.2 65.2 61.9 6 ALA 0.0 0.0 88.9 7 GLY 0.0 0.0 74.6 8 VAL 118.8 100.0 41.8 9 THR 35.6 33.3 75.0 10 VAL 118.8 100.0 28.6 11 THR 34.0 31.8 67.6 12 VAL 104.2 87.7 53.4 13 ASN 11.0 9.1 81.9 14 GLY 0.0 0.0 87.2 15 ASN 69.6 57.6 66.8 16 THR 67.2 62.9 72.2 17 VAL 118.8 100.0 34.1 18 THR 79.2 74.1 57.0 19 VAL 118.8 100.0 31.6 20 LYS 76.7 44.2 71.3 21 GLY 32.5 93.5 54.4 22 PRO 55.3 44.4 72.9 23 LYS 82.4 47.5 74.4 24 GLY 10.2 29.2 67.0 25 GLU 57.3 41.4 61.3 26 LEU 113.2 76.6 56.9 27 THR 53.0 49.6 63.5 28 ARG 99.9 47.8 61.2 29 THR 49.2 46.1 72.1 30 PHE 159.0 95.3 41.5 31 HIS 78.8 52.5 55.4 32 PRO 42.6 34.2 79.2 33 ASP 51.5 46.6 62.8 34 MET 159.4 100.0 40.6 35 THR 33.8 31.7 71.0 36 ILE 141.9 98.9 30.0 37 THR 56.2 52.6 68.0 38 VAL 86.5 72.8 58.6 39 GLU 45.6 32.9 78.9 40 GLY 0.0 0.0 80.7 41 ASN 9.8 8.1 77.2 42 VAL 89.0 74.9 55.6 43 ILE 143.5 100.0 28.4 44 THR 68.0 63.6 67.8 45 VAL 118.8 100.0 38.5 46 THR 29.5 27.6 73.3 47 ARG 157.7 75.5 59.7 48 PRO 74.3 59.7 62.8 49 SER 43.5 52.0 68.9 50 ASP 27.6 25.0 86.8 51 GLU 34.1 24.6 83.8 52 LYS 4.2 2.4 86.3 53 HIS 53.5 35.6 71.3 54 HIS 136.1 90.6 51.9 55 ARG 100.4 48.1 75.5 56 ALA 15.9 21.9 77.9 57 LEU 105.4 71.3 52.4 58 HIS 127.1 84.6 59.3 59 GLY 17.1 49.3 79.0 60 THR 33.0 30.9 72.5 61 THR 102.3 95.7 31.6 62 ARG 107.6 51.5 64.6 63 SER 27.6 33.0 74.0 64 LEU 96.6 65.4 63.2 65 LEU 147.8 100.0 24.8 66 ALA 33.5 46.1 64.5 67 ASN 39.8 33.0 78.7 68 MET 149.8 94.0 42.3 69 VAL 108.5 91.3 40.6 70 GLU 73.8 53.3 71.1 71 GLY 34.8 100.0 58.5 72 VAL 118.8 100.0 43.9 73 SER 69.7 83.4 42.1 74 LYS 37.6 21.7 84.3 75 GLY 30.3 87.2 55.3 76 TYR 147.3 81.4 57.7 77 GLU 61.5 44.4 63.0 78 LYS 108.7 62.7 60.0 79 ALA 61.4 84.5 57.0 80 LEU 147.8 100.0 35.2 81 GLU 94.1 67.9 61.4 82 LEU 147.7 100.0 39.9 83 VAL 68.6 57.7 75.5 84 GLY 29.2 84.0 46.3 85 VAL 0.0 0.0 88.7 86 GLY 4.0 11.6 81.3 87 TYR 173.2 95.7 56.3 88 ARG 83.9 40.2 74.6 89 ALA 72.2 99.5 41.6 90 SER 35.8 42.8 65.2 91 LYS 119.0 68.6 69.1 92 GLN 41.8 28.1 77.6 93 GLY 0.0 0.0 86.9 94 LYS 70.5 40.7 74.5 95 LYS 100.4 57.9 70.6 96 LEU 147.8 100.0 28.6 97 VAL 97.9 82.4 55.7 98 LEU 147.8 100.0 29.2 99 SER 46.3 55.4 68.3 100 VAL 118.6 99.9 26.0 101 GLY 11.9 34.2 75.3 102 TYR 95.7 52.9 71.4 103 SER 11.1 13.3 80.5 104 HIS 20.6 13.7 81.8 105 PRO 71.4 57.3 62.3 106 VAL 80.9 68.1 49.2 107 GLU 69.1 49.9 65.0 108 ILE 113.8 79.3 43.3 109 GLU 45.8 33.0 64.6 110 PRO 124.0 99.6 49.6 111 GLU 28.7 20.7 87.2 112 GLU 0.0 0.0 89.3 113 GLY 0.8 2.2 78.8 114 LEU 139.9 94.6 52.2 115 GLU 51.5 37.1 74.5 116 ILE 143.5 100.0 30.7 117 GLU 71.4 51.5 66.9 118 VAL 114.4 96.3 47.1 119 PRO 70.0 56.2 61.3 120 SER 30.5 36.5 74.5 121 GLN 38.0 25.6 71.3 122 THR 47.8 44.7 76.9 123 LYS 99.5 57.4 70.6 124 ILE 143.5 100.0 25.5 125 ILE 115.1 80.2 52.5 126 VAL 118.8 100.0 35.0 127 LYS 119.9 69.1 63.2 128 GLY 27.5 79.1 66.7 129 ALA 69.4 95.5 47.2 130 ASP 66.0 59.7 54.6 131 LYS 82.2 47.4 63.2 132 GLN 11.5 7.7 85.7 133 ARG 126.7 60.7 62.8 134 VAL 118.8 100.0 50.6 135 GLY 11.1 31.9 70.4 136 GLU 42.2 30.4 80.3 137 LEU 126.5 85.6 40.5 138 ALA 72.5 99.8 40.8 139 ALA 36.1 49.7 77.4 140 ASN 47.2 39.0 70.2 141 ILE 143.5 100.0 23.0 142 ARG 148.1 70.9 55.7 143 ALA 30.0 41.4 75.0 144 VAL 91.6 77.1 44.0 145 ARG 149.1 71.4 56.0 146 PRO 68.7 55.2 73.8 147 PRO 121.0 97.2 55.4 148 GLU 97.8 70.5 54.8 149 PRO 44.1 35.4 69.4 150 TYR 10.4 5.8 82.4 151 LYS 48.4 27.9 73.4 152 GLY 34.8 99.9 60.7 153 LYS 103.9 59.9 64.4 154 GLY 34.8 100.0 51.8 155 ILE 143.5 100.0 36.6 156 ARG 171.2 82.0 52.8 157 TYR 119.9 66.2 55.0 158 GLU 63.4 45.7 73.3 159 GLY 0.0 0.0 80.6 160 GLU 105.7 76.2 58.4 161 LEU 29.3 19.8 83.1 162 VAL 94.9 79.9 64.6 163 ARG 18.8 9.0 80.0 164 LEU 93.8 63.5 73.3