Protein Data Bank File : 1sfe Title : DNA-BINDING PROTEIN 21-JUN-96 1SFE Number of Amino Acid Residues : 165 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU ALA VAL ARG TYR ALA LEU ALA ASP CYS 10 GLU LEU GLY ARG CYS LEU VAL ALA GLU SER 20 GLU ARG GLY ILE CYS ALA ILE LEU LEU GLY 30 ASP ASP ASP ALA THR LEU ILE SER GLU LEU 40 GLN GLN MET PHE PRO ALA ALA ASP ASN ALA 50 PRO ALA ASP LEU MET PHE GLN GLN HIS VAL 60 ARG GLU VAL ILE ALA SER LEU ASN GLN ARG 70 ASP THR PRO LEU THR LEU PRO LEU ASP ILE 80 ARG GLY THR ALA PHE GLN GLN GLN VAL TRP 90 GLN ALA LEU ARG THR ILE PRO CYS GLY GLU 100 THR VAL SER TYR GLN GLN LEU ALA ASN ALA 110 ILE GLY LYS PRO LYS ALA VAL ARG ALA VAL 120 ALA SER ALA CYS ALA ALA ASN LYS LEU ALA 130 ILE VAL ILE PRO CYS HIS ARG VAL VAL ARG 140 GLY ASP GLY SER LEU SER GLY TYR ARG TRP 150 GLY VAL SER ARG LYS ALA GLN LEU LEU ARG 160 ARG GLU ALA GLU ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 6.7 -178.0 -66.3 135.5 2 ALA -52.7 131.0 179.3 3 VAL -134.3 127.7 179.8 170.2 4 ARG -109.3 149.3 178.3 -64.7 -179.1 -78.6 -44.2 5 TYR -144.4 157.3 176.3 79.9 79.5 6 ALA -141.3 154.3 176.3 7 LEU -115.5 135.0 -178.4 -86.1 108.0 8 ALA -145.2 163.4 177.6 9 ASP -92.5 149.8 177.0 -74.4 -46.5 10 CYS -154.7 172.8 179.2 76.5 11 GLU -54.0 -32.1 -179.7 -108.3 137.7 48.9 12 LEU -87.7 2.8 178.7 -67.3 -57.8 13 GLY 112.7 -143.1 179.1 14 ARG -80.5 134.3 175.8 -156.2 81.2 -164.4 137.4 15 CYS -132.0 155.1 175.8 69.5 16 LEU -119.3 125.7 178.8 177.5 138.8 17 VAL -110.1 137.7 -176.4 162.9 18 ALA -135.2 145.2 -175.1 19 GLU -141.9 129.8 175.8 -171.6 -164.2 -81.0 20 SER -99.4 -162.5 175.1 61.8 21 GLU -81.4 -11.0 179.2 -147.2 78.6 -74.8 22 ARG -89.9 -31.8 -179.8 -83.4 146.6 126.2 133.9 23 GLY 159.2 -173.1 173.6 24 ILE -56.1 119.6 -178.6 -52.0 -59.1 25 CYS -111.9 -3.2 173.8 69.3 26 ALA -168.9 139.0 176.1 27 ILE -136.9 107.9 -175.0 -63.3 162.3 28 LEU -118.3 143.5 -176.5 -50.8 168.6 29 LEU -116.7 150.4 -176.5 -48.7 160.8 30 GLY 179.8 -177.7 -177.7 31 ASP -105.4 -26.3 -179.0 -60.6 -86.3 32 ASP -136.9 142.6 -176.1 83.0 -66.1 33 ASP -57.8 -44.8 -179.2 -63.5 -9.5 34 ALA -49.0 -48.7 -179.3 35 THR -69.8 -44.7 175.6 57.1 36 LEU -55.5 -47.1 -178.3 -66.7 -174.1 37 ILE -65.9 -38.5 176.2 -53.5 167.2 38 SER -73.7 -38.5 175.6 15.7 39 GLU -55.2 -47.1 177.2 -151.8 175.0 -49.7 40 LEU -66.6 -43.7 176.7 -166.7 -85.6 41 GLN -58.5 -33.4 175.2 -124.3 143.4 -173.1 42 GLN -57.3 -41.7 179.8 -125.6 147.2 -51.4 43 MET -94.4 -35.9 178.1 26.6 -156.7 170.0 44 PHE -131.2 88.8 -169.6 -49.9 -73.3 45 PRO -66.7 -36.4 176.5 -17.0 32.5 46 ALA -103.8 20.2 177.6 47 ALA -52.1 141.2 179.5 48 ASP -132.1 158.2 179.3 -150.7 -16.6 49 ASN -77.2 159.9 -176.5 44.9 162.8 50 ALA -148.1 67.4 -177.6 51 PRO -57.9 -33.7 -177.3 22.0 -36.7 52 ALA -93.0 -7.3 177.3 53 ASP -67.9 99.0 -177.8 -173.4 -50.3 54 LEU -55.8 -42.7 -174.6 -66.1 165.6 55 MET -73.0 -32.5 172.0 169.1 -161.5 168.9 56 PHE -71.0 -44.9 -178.2 168.9 58.0 57 GLN -61.7 -31.7 173.0 -55.8 -73.1 -22.0 58 GLN -62.1 -53.1 175.5 -90.0 -68.1 0.1 59 HIS -51.7 -42.4 175.1 -73.3 -177.9 60 VAL -59.6 -38.5 177.6 164.4 61 ARG -69.6 -35.8 172.2 -84.5 -173.9 -87.5 119.1 62 GLU -63.4 -51.9 176.1 -85.4 -138.0 78.1 63 VAL -56.7 -47.8 -179.0 172.1 64 ILE -56.1 -47.9 178.0 -70.1 -78.5 65 ALA -47.1 -51.0 175.2 66 SER -53.7 -55.1 178.8 -97.2 67 LEU -50.2 -41.7 179.5 -92.2 30.7 68 ASN -84.2 -14.6 -178.8 -58.4 -45.2 69 GLN -95.3 150.1 -179.9 -72.6 172.7 -44.0 70 ARG -56.9 -45.7 -177.0 -178.9 174.2 172.4 -61.0 71 ASP -145.3 41.2 178.2 -162.5 5.9 72 THR -94.5 108.0 178.3 -47.5 73 PRO -57.5 145.7 177.1 13.3 -21.1 74 LEU -93.4 114.3 179.9 -149.2 -145.8 75 THR -76.8 -36.6 -173.9 -94.8 76 LEU -51.0 154.2 178.1 -69.2 163.1 77 PRO -61.7 137.5 179.5 -3.7 5.2 78 LEU -103.0 138.8 174.3 -58.3 -166.0 79 ASP -106.4 81.2 -176.1 -178.4 15.1 80 ILE -83.9 118.5 179.8 -53.3 -175.0 81 ARG -115.0 127.0 -179.8 -55.3 -136.1 -166.6 -137.7 82 GLY 169.4 -179.7 179.6 83 THR -74.3 164.4 179.1 69.8 84 ALA -52.9 -48.9 177.4 85 PHE -57.0 -50.5 175.7 -172.2 65.7 86 GLN -58.8 -44.2 178.9 -89.8 158.4 -8.3 87 GLN -62.0 -41.5 174.8 -64.1 -126.5 17.5 88 GLN -62.4 -45.3 -178.2 -60.8 -178.1 -2.3 89 VAL -62.4 -49.9 -178.2 175.9 90 TRP -61.1 -39.9 174.4 -60.1 -27.3 91 GLN -59.3 -44.8 -179.7 -172.8 41.5 58.0 92 ALA -70.1 -30.5 168.6 93 LEU -52.1 -43.1 -177.3 -62.8 171.3 94 ARG -64.3 -13.1 177.7 -57.3 177.9 67.8 172.5 95 THR -98.4 -2.6 172.1 64.5 96 ILE -69.0 124.2 -177.7 -59.6 156.0 97 PRO -65.3 146.0 176.8 10.7 -14.5 98 CYS -61.7 127.1 175.3 170.9 99 GLY 106.6 -1.1 177.1 100 GLU -124.6 158.9 171.3 -78.5 -157.8 39.7 101 THR -123.6 147.2 174.1 45.6 102 VAL -122.0 152.1 179.0 -55.2 103 SER -86.0 163.0 177.1 76.6 104 TYR -53.5 -46.9 -177.1 -63.9 -63.5 105 GLN -60.7 -43.6 174.6 -178.6 73.4 -108.7 106 GLN -57.8 -45.0 176.7 -74.6 169.2 -15.5 107 LEU -60.0 -42.6 179.9 -144.9 -142.0 108 ALA -65.8 -39.7 178.2 109 ASN -63.2 -47.3 178.0 -77.3 156.5 110 ALA -59.2 -31.1 -177.8 111 ILE -93.2 3.7 176.0 59.2 -178.4 112 GLY 95.1 10.8 178.8 113 LYS -135.2 79.6 -178.8 8.5 -94.5 -108.3 163.2 114 PRO -53.5 -38.2 178.3 -23.8 29.7 115 LYS -64.8 -31.4 -171.5 27.5 126.4 159.3 -136.3 116 ALA -91.4 40.3 -179.7 117 VAL -55.7 -45.5 179.9 177.7 118 ARG -58.8 -51.4 179.5 -170.3 75.2 -93.9 -177.4 119 ALA -63.5 -34.7 177.1 120 VAL -65.7 -45.7 176.5 -35.9 121 ALA -51.2 -46.6 176.3 122 SER -66.3 -35.1 -177.6 -57.7 123 ALA -67.1 -40.5 179.4 124 CYS -63.9 -39.7 -178.7 -62.1 125 ALA -77.5 -11.6 175.1 126 ALA -92.4 3.4 -180.0 127 ASN -62.8 135.8 178.1 -179.2 29.4 128 LYS -107.6 4.5 -176.3 -55.7 161.5 -176.4 110.1 129 LEU -125.3 77.0 -174.3 -66.2 176.3 130 ALA -52.7 141.8 172.6 131 ILE 69.2 -50.4 178.1 -58.0 -168.1 132 VAL -59.9 -37.2 175.2 169.2 133 ILE -111.7 103.3 -161.7 -70.7 -175.0 134 PRO -80.1 62.4 179.1 14.5 -8.6 135 CYS -68.1 -7.4 174.4 68.5 136 HIS -73.2 -17.9 -175.2 49.7 -70.0 137 ARG -82.5 -14.9 175.9 -68.5 -178.9 -167.5 152.1 138 VAL -92.8 137.8 -177.0 -167.5 139 VAL -129.6 154.8 175.2 -66.2 140 ARG -72.9 155.4 -177.8 50.1 -162.8 -28.0 -105.0 141 GLY -71.6 -9.6 -170.5 142 ASP -79.6 6.7 179.8 76.4 -12.9 143 GLY 99.5 -11.8 179.6 144 SER -91.7 153.4 179.6 96.7 145 LEU -103.1 33.9 179.0 -62.6 173.8 146 SER -82.6 175.2 179.0 52.1 147 GLY 91.9 -15.7 177.2 148 TYR -67.6 140.6 -177.4 -158.3 42.3 149 ARG -67.8 -32.1 -177.7 161.7 151.5 -169.0 -173.7 150 TRP -111.9 28.6 171.1 -55.8 -78.9 151 GLY 92.8 160.3 -172.2 152 VAL -73.6 -37.2 179.1 69.4 153 SER -63.9 -37.6 179.6 -177.3 154 ARG -79.7 -41.6 177.5 -86.4 174.8 -145.4 99.5 155 LYS -55.9 -49.7 -178.6 169.7 161.5 -175.4 156.7 156 ALA -61.5 -43.5 176.7 157 GLN -60.1 -43.6 179.7 -159.5 170.4 -26.4 158 LEU -64.9 -49.3 -179.7 -77.1 169.2 159 LEU -61.4 -32.4 -178.2 -69.0 169.8 160 ARG -72.0 -37.9 178.5 167.9 -146.8 -45.2 149.4 161 ARG -72.9 -28.5 -178.1 84.7 168.4 175.3 -153.5 162 GLU -85.4 -23.5 176.1 -54.7 -174.5 -22.5 163 ALA -100.4 72.8 -173.6 164 GLU -111.1 146.8 176.9 -134.9 -107.8 -23.0 165 ASN 66.9 69.7 0.0 -67.0 -46.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU -23.078 -12.360 -8.620 2 ALA -19.736 -13.518 -10.047 3 VAL -17.278 -14.108 -7.192 4 ARG -13.653 -15.000 -7.705 5 TYR -11.303 -16.451 -5.092 6 ALA -7.691 -17.400 -4.470 7 LEU -5.879 -19.185 -1.670 8 ALA -2.613 -17.849 -0.312 9 ASP -0.304 -18.120 2.667 10 CYS 0.068 -15.275 5.140 11 GLU 1.401 -14.663 8.653 12 LEU -1.942 -15.737 10.131 13 GLY -1.839 -18.975 8.132 14 ARG -3.972 -19.942 5.168 15 CYS -6.310 -17.255 3.854 16 LEU -8.927 -17.071 1.156 17 VAL -9.440 -13.763 -0.653 18 ALA -12.617 -13.306 -2.674 19 GLU -13.671 -10.531 -5.012 20 SER -16.968 -9.679 -6.686 21 GLU -17.334 -6.885 -9.266 22 ARG -17.729 -4.292 -6.450 23 GLY -14.569 -5.137 -4.513 24 ILE -13.049 -7.544 -1.975 25 CYS -16.113 -9.340 -0.607 26 ALA -14.450 -11.866 1.710 27 ILE -11.152 -12.396 3.504 28 LEU -11.224 -15.665 5.451 29 LEU -8.494 -17.214 7.626 30 GLY -7.890 -20.894 8.363 31 ASP -5.642 -23.921 8.334 32 ASP -7.038 -25.960 5.438 33 ASP -8.386 -25.195 1.977 34 ALA -11.385 -27.538 2.109 35 THR -12.909 -25.647 5.036 36 LEU -12.116 -22.144 3.705 37 ILE -13.741 -23.040 0.386 38 SER -16.916 -24.482 1.963 39 GLU -17.051 -21.518 4.376 40 LEU -16.883 -19.248 1.297 41 GLN -19.261 -21.476 -0.692 42 GLN -21.781 -21.068 2.166 43 MET -21.947 -17.295 1.541 44 PHE -20.928 -17.198 -2.180 45 PRO -21.891 -20.612 -3.586 46 ALA -20.698 -20.799 -7.230 47 ALA -17.576 -18.793 -6.435 48 ASP -14.682 -20.138 -8.561 49 ASN -10.886 -19.826 -8.542 50 ALA -9.350 -17.589 -11.249 51 PRO -5.626 -18.308 -11.558 52 ALA -5.272 -16.675 -14.954 53 ASP -7.193 -13.454 -14.109 54 LEU -4.038 -11.286 -14.088 55 MET -5.897 -8.319 -12.564 56 PHE -7.509 -10.375 -9.757 57 GLN -4.199 -12.001 -8.873 58 GLN -2.639 -8.527 -8.434 59 HIS -5.451 -7.449 -6.081 60 VAL -4.880 -10.642 -4.036 61 ARG -1.210 -9.703 -3.646 62 GLU -2.324 -6.225 -2.513 63 VAL -4.761 -7.744 -0.006 64 ILE -2.080 -10.166 1.283 65 ALA 0.354 -7.252 1.855 66 SER -2.179 -5.519 4.161 67 LEU -2.774 -8.836 5.929 68 ASN 0.883 -9.445 6.779 69 GLN 1.585 -5.850 7.930 70 ARG 0.804 -4.344 11.336 71 ASP -0.985 -1.216 10.121 72 THR -1.142 -1.133 6.322 73 PRO -4.607 -0.019 5.253 74 LEU -6.264 -1.944 2.422 75 THR -6.884 0.613 -0.313 76 LEU -8.737 -1.594 -2.771 77 PRO -12.510 -1.177 -2.885 78 LEU -14.506 -3.190 -0.334 79 ASP -17.739 -5.011 -1.109 80 ILE -19.293 -4.942 2.364 81 ARG -22.574 -6.903 2.537 82 GLY -24.960 -6.849 5.497 83 THR -27.786 -5.208 7.439 84 ALA -27.764 -1.550 8.502 85 PHE -26.904 -2.634 12.055 86 GLN -24.057 -4.909 10.898 87 GLN -22.821 -2.125 8.622 88 GLN -22.997 0.330 11.502 89 VAL -21.079 -2.096 13.698 90 TRP -18.405 -2.794 11.024 91 GLN -18.005 0.876 10.145 92 ALA -17.348 1.625 13.842 93 LEU -14.797 -1.238 14.100 94 ARG -12.894 0.516 11.340 95 THR -12.457 3.626 13.514 96 ILE -10.817 1.591 16.323 97 PRO -7.164 2.684 16.235 98 CYS -4.478 0.111 15.539 99 GLY -3.254 -0.884 18.987 100 GLU -6.418 -0.465 21.024 101 THR -9.339 -2.642 22.077 102 VAL -12.892 -1.654 23.001 103 SER -15.335 -3.939 24.847 104 TYR -18.671 -4.941 23.286 105 GLN -20.542 -2.585 25.675 106 GLN -18.361 0.411 24.784 107 LEU -18.989 -0.338 21.110 108 ALA -22.735 -0.625 21.798 109 ASN -22.505 2.649 23.764 110 ALA -20.581 4.391 20.960 111 ILE -23.180 3.588 18.273 112 GLY -26.118 4.794 20.349 113 LYS -27.587 1.487 21.585 114 PRO -26.250 0.737 25.071 115 LYS -28.822 -2.024 25.301 116 ALA -27.829 -4.043 22.209 117 VAL -24.624 -5.690 23.508 118 ARG -25.679 -9.183 22.367 119 ALA -26.473 -8.120 18.778 120 VAL -23.233 -6.116 18.596 121 ALA -21.369 -9.267 19.698 122 SER -23.050 -11.261 16.952 123 ALA -22.307 -8.542 14.366 124 CYS -18.620 -8.881 15.116 125 ALA -18.611 -12.683 14.740 126 ALA -20.478 -12.378 11.404 127 ASN -17.722 -10.191 9.813 128 LYS -16.590 -11.660 6.446 129 LEU -13.563 -9.389 5.950 130 ALA -10.928 -10.499 8.361 131 ILE -8.474 -7.877 9.551 132 VAL -9.619 -5.118 7.078 133 ILE -12.693 -4.754 9.280 134 PRO -10.816 -5.016 12.544 135 CYS -13.153 -7.286 14.504 136 HIS -10.181 -8.647 16.457 137 ARG -10.159 -5.298 18.291 138 VAL -13.434 -5.842 20.154 139 VAL -13.280 -7.883 23.340 140 ARG -15.804 -9.192 25.856 141 GLY -14.899 -7.066 28.916 142 ASP -13.802 -9.997 31.134 143 GLY -10.149 -10.543 30.063 144 SER -10.862 -13.374 27.630 145 LEU -10.086 -13.408 23.909 146 SER -13.164 -15.450 22.968 147 GLY -15.647 -14.458 20.276 148 TYR -13.304 -14.269 17.229 149 ARG -14.736 -15.825 14.037 150 TRP -11.377 -17.387 13.137 151 GLY -10.255 -18.543 16.538 152 VAL -8.449 -17.447 19.662 153 SER -4.950 -18.103 18.352 154 ARG -5.418 -15.678 15.438 155 LYS -7.273 -13.038 17.533 156 ALA -4.495 -13.233 20.140 157 GLN -1.835 -13.115 17.426 158 LEU -3.407 -10.043 15.834 159 LEU -3.767 -8.109 19.120 160 ARG -0.177 -8.951 20.075 161 ARG 1.250 -7.570 16.841 162 GLU -0.713 -4.263 17.070 163 ALA 0.127 -3.686 20.733 164 GLU 3.865 -3.657 20.096 165 ASN 6.963 -2.409 21.876 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/T 10 T T T/S S S S S S S S/T 20 T T T/S S S S/S S S S S 30 S H H H H H H H H H 40 H H H H C S S S S S 50 S C H H H H H H H H 60 H H H H H H H H H S 70 S S S S C S S S S S 80 S S S/H H H H H H H H 90 H H H H H H C C S S 100 S S S/H H H H H H H H 110 H H C C C H H H H H 120 H H H H H H H C T T 130 T T C C C C S S S S/T 140 T T T C C S S S S C 150 H H H H H H H H H H 160 H H H H/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E E E E 10 T T E E E E E E E e 20 S S e E E E E E E E 30 S h H H H H H H H H 40 H H H h T T t E E e 50 T T h H H H H H H H 60 H H H H H H H H h S 70 S S B 80 S h H H H H H H H 90 H H H h T t t T T t 100 E E H H H H H H H 110 h T t T T h H H H H 120 H H H H H h t B B 130 T T B g G G e E E t 140 T T t t T T t T T 150 h H H H H H H H H H 160 H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 0.0 0.0 96.7 2 ALA 6.7 9.2 86.9 3 VAL 113.3 95.4 41.8 4 ARG 165.7 79.3 60.9 5 TYR 158.8 87.8 37.3 6 ALA 61.3 84.4 53.8 7 LEU 133.5 90.3 46.6 8 ALA 48.8 67.2 61.1 9 ASP 24.4 22.1 79.5 10 CYS 94.2 94.9 48.6 11 GLU 49.1 35.4 77.1 12 LEU 146.9 99.4 45.4 13 GLY 6.3 18.1 83.2 14 ARG 149.6 71.6 70.6 15 CYS 99.1 99.9 37.4 16 LEU 147.8 100.0 30.4 17 VAL 118.2 99.5 31.2 18 ALA 72.6 100.0 33.6 19 GLU 131.1 94.6 48.2 20 SER 79.8 95.4 63.2 21 GLU 11.2 8.1 90.8 22 ARG 45.6 21.9 90.3 23 GLY 28.3 81.4 59.0 24 ILE 142.3 99.2 36.6 25 CYS 99.2 100.0 44.7 26 ALA 72.6 100.0 33.7 27 ILE 143.5 100.0 29.1 28 LEU 147.8 100.0 41.4 29 LEU 147.8 100.0 29.0 30 GLY 26.7 76.7 66.4 31 ASP 16.8 15.2 83.9 32 ASP 39.4 35.7 73.1 33 ASP 60.6 54.8 58.6 34 ALA 37.1 51.1 75.2 35 THR 34.6 32.3 86.1 36 LEU 146.0 98.8 51.9 37 ILE 100.9 70.3 55.5 38 SER 29.4 35.2 79.4 39 GLU 94.2 68.0 65.6 40 LEU 147.0 99.4 27.0 41 GLN 73.3 49.3 70.9 42 GLN 22.4 15.1 82.2 43 MET 131.5 82.5 47.5 44 PHE 143.4 86.0 37.6 45 PRO 39.5 31.8 79.5 46 ALA 0.0 0.0 89.0 47 ALA 71.8 98.8 48.1 48 ASP 23.3 21.1 86.1 49 ASN 46.9 38.8 72.9 50 ALA 53.4 73.5 51.0 51 PRO 36.3 29.2 77.9 52 ALA 0.0 0.0 82.4 53 ASP 63.7 57.6 62.5 54 LEU 0.0 0.0 89.6 55 MET 23.1 14.5 82.3 56 PHE 166.0 99.5 54.3 57 GLN 104.0 70.0 62.8 58 GLN 57.8 38.9 81.0 59 HIS 110.0 73.3 50.5 60 VAL 110.2 92.7 38.2 61 ARG 77.0 36.8 79.8 62 GLU 62.3 45.0 61.1 63 VAL 118.8 100.0 24.9 64 ILE 119.6 83.3 49.8 65 ALA 25.4 35.0 80.3 66 SER 79.4 95.0 55.8 67 LEU 147.8 100.0 31.9 68 ASN 83.7 69.2 62.7 69 GLN 52.9 35.6 78.4 70 ARG 119.8 57.3 67.4 71 ASP 40.6 36.7 74.6 72 THR 57.8 54.1 68.6 73 PRO 23.7 19.0 83.0 74 LEU 145.0 98.1 42.8 75 THR 9.2 8.6 83.3 76 LEU 134.6 91.1 43.3 77 PRO 41.5 33.3 73.4 78 LEU 138.9 94.0 49.0 79 ASP 104.6 94.7 56.2 80 ILE 113.9 79.4 50.3 81 ARG 116.7 55.9 69.2 82 GLY 22.6 65.0 64.9 83 THR 22.8 21.3 77.3 84 ALA 7.7 10.6 80.1 85 PHE 120.1 72.0 49.2 86 GLN 103.7 69.8 48.2 87 GLN 74.6 50.2 68.3 88 GLN 64.7 43.6 64.8 89 VAL 118.8 100.0 31.4 90 TRP 199.7 97.4 46.2 91 GLN 51.0 34.3 72.2 92 ALA 53.2 73.2 59.1 93 LEU 147.8 100.0 33.2 94 ARG 133.7 64.0 62.4 95 THR 27.9 26.1 84.8 96 ILE 134.7 93.9 45.1 97 PRO 52.6 42.3 76.3 98 CYS 94.9 95.6 71.8 99 GLY 26.6 76.4 67.2 100 GLU 41.0 29.6 73.7 101 THR 68.5 64.1 49.4 102 VAL 82.8 69.7 52.8 103 SER 64.2 76.8 57.1 104 TYR 156.0 86.2 47.8 105 GLN 67.8 45.6 72.1 106 GLN 47.6 32.0 76.3 107 LEU 142.4 96.4 33.1 108 ALA 72.6 100.0 53.6 109 ASN 63.0 52.1 64.3 110 ALA 17.0 23.4 76.5 111 ILE 125.1 87.2 47.9 112 GLY 2.0 5.6 75.8 113 LYS 103.7 59.8 57.5 114 PRO 56.5 45.3 75.0 115 LYS 33.1 19.1 75.6 116 ALA 49.7 68.5 50.8 117 VAL 74.6 62.8 64.4 118 ARG 20.9 10.0 84.3 119 ALA 29.5 40.6 63.2 120 VAL 118.8 100.0 32.8 121 ALA 68.3 94.1 59.3 122 SER 24.1 28.9 75.0 123 ALA 69.9 96.3 46.5 124 CYS 93.6 94.4 43.1 125 ALA 37.5 51.7 78.6 126 ALA 42.1 57.9 78.3 127 ASN 119.9 99.2 47.3 128 LYS 132.1 76.2 52.9 129 LEU 143.8 97.3 41.7 130 ALA 72.6 100.0 43.0 131 ILE 128.7 89.7 48.5 132 VAL 105.6 88.9 39.0 133 ILE 142.6 99.4 33.1 134 PRO 118.1 94.8 62.1 135 CYS 97.4 98.2 47.1 136 HIS 150.1 100.0 45.4 137 ARG 184.6 88.4 56.8 138 VAL 118.3 99.6 37.4 139 VAL 92.7 78.1 56.9 140 ARG 96.6 46.2 80.9 141 GLY 11.9 34.2 70.4 142 ASP 49.3 44.6 77.9 143 GLY 0.0 0.0 86.7 144 SER 43.1 51.6 77.2 145 LEU 97.3 65.8 53.6 146 SER 32.0 38.3 78.8 147 GLY 8.4 24.0 85.2 148 TYR 177.0 97.8 44.2 149 ARG 158.7 76.0 54.0 150 TRP 195.6 95.4 51.6 151 GLY 4.9 14.0 78.3 152 VAL 30.0 25.2 68.7 153 SER 5.2 6.2 76.2 154 ARG 177.3 84.9 58.9 155 LYS 171.2 98.7 48.4 156 ALA 52.0 71.7 59.9 157 GLN 96.8 65.1 68.0 158 LEU 147.8 100.0 45.5 159 LEU 124.2 84.0 48.6 160 ARG 52.0 24.9 79.0 161 ARG 166.8 79.9 56.1 162 GLU 136.2 98.3 57.6 163 ALA 21.4 29.5 82.0 164 GLU 63.7 46.0 83.2 165 ASN 10.0 8.3 84.1