Protein Data Bank File : 1qsta Title : TRANSFERASE 23-JUN-99 1QST Number of Amino Acid Residues : 160 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU ASP PHE ASP ILE LEU THR ASN ASP GLY 10 THR HIS ARG ASN MET LYS LEU LEU ILE ASP 20 LEU LYS ASN ILE PHE SER ARG GLN LEU PRO 30 LYS MET PRO LYS GLU TYR ILE VAL LYS LEU 40 VAL PHE ASP ARG HIS HIS GLU SER MET VAL 50 ILE LEU LYS ASN LYS GLN LYS VAL ILE GLY 60 GLY ILE CYS PHE ARG GLN TYR LYS PRO GLN 70 ARG PHE ALA GLU VAL ALA PHE LEU ALA VAL 80 THR ALA ASN GLU GLN VAL ARG GLY TYR GLY 90 THR ARG LEU MET ASN LYS PHE LYS ASP HIS 100 MET GLN LYS GLN ASN ILE GLU TYR LEU LEU 110 THR TYR ALA ASP ASN PHE ALA ILE GLY TYR 120 PHE LYS LYS GLN GLY PHE THR LYS GLU HIS 130 ARG MET PRO GLN GLU LYS TRP LYS GLY TYR 140 ILE LYS ASP TYR ASP GLY GLY THR LEU MET 150 GLU CYS TYR ILE HIS PRO TYR VAL ASP TYR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 119.1 179.1 -108.5 -127.6 2 ASP -119.8 144.4 178.8 -79.0 125.4 3 PHE -118.8 91.7 -177.4 -63.2 86.4 4 ASP -111.0 143.4 177.1 -50.5 155.6 5 ILE -77.2 121.8 -178.1 -79.5 -61.0 6 LEU -96.9 116.9 -179.7 -145.3 35.3 7 THR -95.3 137.5 178.5 72.1 8 ASN -85.1 88.5 -177.6 161.7 10.3 9 ASP -106.5 11.5 179.7 61.3 177.7 10 GLY 75.4 8.9 179.4 11 THR -90.7 151.6 -179.5 56.8 12 HIS -57.6 -46.0 -179.0 -70.4 -74.9 13 ARG -58.4 -54.3 -179.0 155.8 130.1 -165.9 110.4 14 ASN -66.9 -45.4 -179.2 -84.3 31.8 15 MET -65.4 -25.4 178.2 -48.1 -71.4 -52.7 16 LYS -69.9 -40.5 180.0 -169.2 -135.9 176.4 -111.2 17 LEU -71.7 -31.1 179.5 -62.3 171.1 18 LEU -72.6 -37.5 178.0 -77.7 165.6 19 ILE -66.3 -44.0 179.1 -69.0 176.5 20 ASP -55.9 -44.4 179.5 -73.6 -11.8 21 LEU -66.2 -43.4 179.4 177.8 66.9 22 LYS -57.1 -40.6 -179.7 172.0 -93.9 -54.9 -171.9 23 ASN -68.6 -30.7 178.4 -78.1 151.3 24 ILE -71.9 -43.4 179.7 -76.0 170.2 25 PHE -57.4 -47.5 -179.0 -77.9 152.0 26 SER -56.8 -43.5 179.9 -153.8 27 ARG -72.3 -36.2 -179.6 -88.0 156.9 -118.1 -91.7 28 GLN -81.5 -14.9 178.7 -76.7 -61.3 122.2 29 LEU -130.1 72.0 -179.5 -43.9 167.1 30 PRO -55.5 -31.4 -179.4 -20.2 32.9 31 LYS -82.5 -20.1 179.9 -67.3 -59.2 -111.1 164.3 32 MET -72.9 126.5 -180.0 179.8 77.3 69.6 33 PRO -59.3 119.9 -178.3 -18.7 31.0 34 LYS -54.2 -40.8 -179.8 -171.0 147.2 156.3 169.8 35 GLU -63.7 -27.9 179.6 114.5 -96.1 -22.6 36 TYR -74.7 -36.8 179.0 -178.9 66.9 37 ILE -64.4 -42.8 -180.0 -62.1 176.8 38 VAL -62.7 -43.7 -179.5 169.1 39 LYS -55.5 -50.1 -179.0 -171.7 170.2 149.2 -134.5 40 LEU -71.4 -44.4 -179.0 -97.4 42.0 41 VAL -57.6 -41.0 -179.1 167.5 42 PHE -97.0 14.3 178.9 -59.8 91.7 43 ASP -70.9 153.3 -179.4 -173.9 -130.2 44 ARG -75.5 -17.0 -179.4 71.5 -162.6 -164.7 100.9 45 HIS -97.8 -12.8 -178.1 -60.2 -66.7 46 HIS -97.8 148.7 178.9 -72.5 73.4 47 GLU -132.9 157.4 179.5 -48.0 173.0 -122.7 48 SER -134.6 132.4 175.2 -60.3 49 MET -102.9 125.4 179.8 172.9 177.7 -82.3 50 VAL -111.3 155.4 176.5 -67.8 51 ILE -97.3 104.5 -178.8 -59.2 171.1 52 LEU -94.2 121.2 179.8 -146.1 53.3 53 LYS -102.9 123.2 179.1 -155.5 -161.8 158.8 136.5 54 ASN 60.5 34.2 178.2 -90.5 -61.9 55 LYS 70.6 -3.8 -179.6 -42.7 -100.0 71.6 167.8 56 GLN -150.6 -10.0 -179.6 15.9 -136.6 56.9 57 LYS -103.1 106.1 178.8 -169.9 116.5 159.2 -141.7 58 VAL -77.5 131.9 -179.6 7.8 59 ILE -121.7 7.4 179.6 59.3 175.7 60 GLY 168.7 176.8 179.7 61 GLY 170.6 176.3 179.6 62 ILE -131.8 128.4 177.7 -70.9 176.3 63 CYS -107.3 122.8 -176.7 178.3 64 PHE -134.7 164.1 -179.7 58.9 100.5 65 ARG -132.3 111.6 -179.8 -152.4 -90.8 -146.1 -138.2 66 GLN -82.5 138.2 174.8 -62.4 -169.6 -113.6 67 TYR -115.0 76.1 -176.5 -70.1 89.8 68 LYS -44.1 -59.1 179.9 -54.5 -170.0 -153.9 -137.9 69 PRO -63.3 -27.6 -179.6 -17.8 32.0 70 GLN -82.1 -14.9 178.7 -66.8 67.8 43.0 71 ARG 67.4 28.9 175.6 -53.5 -157.2 76.8 -145.7 72 PHE -137.9 159.6 -179.6 57.6 69.9 73 ALA -138.0 151.3 178.3 74 GLU -108.2 133.8 177.3 -169.3 -168.4 -29.2 75 VAL -91.1 105.8 -179.4 166.8 76 ALA -73.7 -53.2 180.0 77 PHE -136.3 147.1 179.0 -48.9 116.2 78 LEU -149.4 131.3 179.1 -177.0 153.5 79 ALA -167.3 161.2 177.6 80 VAL -131.8 133.0 -178.9 176.2 81 THR -57.6 143.3 -177.9 -160.6 82 ALA -44.7 -47.6 -178.4 83 ASN -78.5 9.4 178.9 60.7 24.6 84 GLU -126.5 13.7 -179.4 -66.9 -71.6 8.8 85 GLN -81.8 168.3 -179.6 -60.0 -165.3 177.2 86 VAL 53.5 34.2 179.5 -139.9 87 ARG -122.8 12.5 179.3 -72.4 177.9 172.2 66.9 88 GLY 85.9 -1.8 -178.5 89 TYR -68.3 -38.3 -179.6 -58.5 145.9 90 GLY -58.6 -44.5 180.0 91 THR -70.5 -44.7 -180.0 -68.5 92 ARG -59.9 -37.9 179.6 -75.7 166.6 69.4 -173.3 93 LEU -64.6 -48.6 -179.1 167.6 67.3 94 MET -63.4 -35.3 179.5 175.0 65.7 79.5 95 ASN -65.7 -45.5 178.0 -79.6 -23.8 96 LYS -62.7 -36.0 179.5 -68.7 -92.8 162.8 151.2 97 PHE -69.2 -42.1 179.3 -178.9 60.4 98 LYS -63.3 -40.1 179.3 -79.1 175.1 171.8 -169.8 99 ASP -61.9 -41.9 179.1 179.9 77.3 100 HIS -65.3 -44.3 179.9 -173.8 -117.9 101 MET -64.8 -35.6 178.8 -64.3 -76.3 103.5 102 GLN -61.0 -45.3 179.3 179.2 -178.1 70.4 103 LYS -68.3 -19.8 -179.8 -75.2 171.9 172.4 49.1 104 GLN -92.7 5.0 -179.5 -70.8 -64.3 -69.7 105 ASN 61.5 39.6 176.9 -54.7 147.2 106 ILE -103.7 126.3 -179.0 -69.7 -66.7 107 GLU -103.5 -10.4 178.9 66.1 -175.3 127.1 108 TYR -140.5 141.1 177.2 -75.9 102.4 109 LEU -116.2 138.1 179.0 -65.8 -176.1 110 LEU -129.5 146.3 179.7 -77.2 168.8 111 THR -160.1 144.0 177.0 -160.0 112 TYR -93.5 103.6 -177.5 -84.3 100.5 113 ALA -63.3 134.3 -179.6 114 ASP -61.9 -1.2 -179.4 168.3 -131.8 115 ASN 72.9 -35.2 177.6 -136.6 -78.4 116 PHE -94.1 -1.4 -179.1 -151.9 107.5 117 ALA -118.7 -6.2 -179.5 118 ILE -55.0 -46.0 179.7 -69.0 -169.2 119 GLY -57.2 -35.7 -179.6 120 TYR -68.9 -49.3 -179.5 166.1 79.2 121 PHE -65.2 -33.5 178.4 -74.3 111.2 122 LYS -65.7 -38.2 179.4 -93.7 -162.6 -164.0 145.9 123 LYS -67.2 -32.9 179.9 176.5 -159.9 -129.5 -145.3 124 GLN -87.2 9.7 178.1 -63.7 -41.3 -40.6 125 GLY 92.8 5.5 179.3 126 PHE -81.1 153.3 -179.8 -76.8 70.6 127 THR -134.3 155.3 179.3 56.5 128 LYS -76.5 -27.7 179.3 -97.3 115.1 -179.9 59.7 129 GLU -87.2 135.5 -178.2 -102.5 72.9 34.0 130 HIS -97.2 146.5 178.2 -64.5 2.9 131 ARG -104.5 -21.7 179.2 -141.8 19.2 63.4 -155.9 132 MET -100.4 125.9 -179.8 147.7 163.8 69.9 133 PRO -62.9 136.8 -179.9 -15.1 29.7 134 GLN -48.6 -38.4 179.3 51.0 -131.1 -151.5 135 GLU -53.6 -29.1 -179.4 -58.0 -135.3 -40.6 136 LYS -67.7 -44.9 -179.5 -116.1 -104.6 -120.4 141.4 137 TRP -97.7 -1.5 179.8 52.4 -93.5 138 LYS -66.1 127.0 -179.7 -112.2 69.3 -165.8 -122.7 139 GLY 93.8 -1.3 179.8 140 TYR -121.9 -54.3 179.6 -66.5 103.0 141 ILE -106.6 131.3 -179.1 -73.6 179.2 142 LYS -61.2 145.8 -179.6 -97.7 -155.3 96.9 126.3 143 ASP -104.9 96.7 180.0 -175.0 -167.7 144 TYR -98.5 142.3 178.9 -57.2 102.9 145 ASP -77.1 -39.8 178.3 -87.1 35.1 146 GLY -75.3 176.2 -179.9 147 GLY 59.8 151.2 -179.8 148 THR -99.5 116.7 178.7 -24.2 149 LEU -82.7 116.4 -179.4 -178.6 64.5 150 MET -115.7 144.7 -177.8 -67.2 170.0 87.8 151 GLU -120.6 149.1 177.6 169.4 -155.4 -87.8 152 CYS -138.4 127.6 179.4 -173.9 153 TYR -86.9 139.4 179.1 174.2 64.6 154 ILE -110.6 104.1 -179.3 -55.6 -62.3 155 HIS -69.8 135.2 -179.5 -167.4 109.8 156 PRO -58.8 -26.2 178.5 22.2 -33.0 157 TYR -135.7 44.5 176.0 40.1 94.5 158 VAL -104.4 141.0 -179.1 155.4 159 ASP -85.3 110.4 -179.7 -172.3 176.0 160 TYR -100.6 7.6 0.0 -67.5 111.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 54.282 13.773 -0.895 2 ASP 51.597 11.098 -1.081 3 PHE 47.911 11.460 -0.230 4 ASP 46.777 7.960 0.716 5 ILE 43.582 6.575 2.209 6 LEU 44.738 4.822 5.373 7 THR 42.900 1.634 6.216 8 ASN 42.737 0.288 9.756 9 ASP 43.697 -3.260 8.816 10 GLY 45.367 -4.318 12.047 11 THR 48.887 -4.239 10.557 12 HIS 51.827 -2.684 12.395 13 ARG 52.603 -0.319 9.501 14 ASN 49.088 1.043 9.044 15 MET 48.143 1.227 12.689 16 LYS 51.406 3.130 13.296 17 LEU 50.493 5.782 10.738 18 LEU 46.976 6.043 12.157 19 ILE 48.319 6.611 15.674 20 ASP 50.698 9.232 14.234 21 LEU 47.715 10.978 12.611 22 LYS 45.660 10.683 15.797 23 ASN 48.493 12.400 17.669 24 ILE 48.580 15.216 15.124 25 PHE 44.823 15.678 15.446 26 SER 45.216 15.788 19.229 27 ARG 47.890 18.501 19.115 28 GLN 46.077 20.649 16.528 29 LEU 42.760 20.314 18.401 30 PRO 43.772 20.739 22.088 31 LYS 40.178 21.001 23.354 32 MET 38.984 17.835 21.583 33 PRO 39.106 14.866 24.010 34 LYS 41.968 12.595 22.928 35 GLU 40.114 9.411 23.818 36 TYR 37.313 10.608 21.533 37 ILE 39.746 11.182 18.670 38 VAL 41.029 7.628 19.155 39 LYS 37.467 6.316 19.229 40 LEU 36.539 7.837 15.868 41 VAL 39.850 7.248 14.076 42 PHE 39.789 3.497 14.787 43 ASP 36.020 3.314 14.273 44 ARG 34.630 0.890 11.672 45 HIS 32.763 3.680 9.872 46 HIS 35.654 6.152 9.697 47 GLU 38.447 6.459 7.139 48 SER 41.517 8.693 6.984 49 MET 43.429 10.193 4.041 50 VAL 46.924 11.063 5.238 51 ILE 49.597 13.368 3.826 52 LEU 52.564 11.001 3.708 53 LYS 56.008 12.601 3.546 54 ASN 58.852 10.457 2.217 55 LYS 56.765 7.270 2.338 56 GLN 56.569 7.140 6.135 57 LYS 56.120 10.503 7.849 58 VAL 52.509 11.561 8.223 59 ILE 52.304 15.350 8.429 60 GLY 48.556 15.771 8.246 61 GLY 45.288 14.203 7.239 62 ILE 41.505 14.107 7.181 63 CYS 39.381 11.651 9.171 64 PHE 35.967 11.247 7.585 65 ARG 32.785 9.205 7.701 66 GLN 30.891 8.409 4.499 67 TYR 27.114 8.004 4.457 68 LYS 27.292 6.227 1.097 69 PRO 23.631 5.687 0.162 70 GLN 22.893 9.250 1.297 71 ARG 25.748 10.583 -0.830 72 PHE 27.256 12.878 1.805 73 ALA 30.232 12.569 4.148 74 GLU 31.272 14.197 7.397 75 VAL 34.798 15.476 7.923 76 ALA 35.389 14.549 11.566 77 PHE 38.968 15.821 11.904 78 LEU 41.363 17.725 9.644 79 ALA 44.855 19.010 10.382 80 VAL 48.410 19.609 9.233 81 THR 51.221 19.384 11.764 82 ALA 52.436 22.788 12.961 83 ASN 55.891 22.660 11.360 84 GLU 54.451 21.812 7.933 85 GLN 51.855 24.569 7.685 86 VAL 51.694 27.434 5.152 87 ARG 53.395 25.176 2.580 88 GLY 50.340 24.487 0.416 89 TYR 49.558 21.098 1.960 90 GLY 46.182 21.977 3.445 91 THR 44.702 22.917 0.089 92 ARG 46.307 20.024 -1.768 93 LEU 44.902 17.630 0.824 94 MET 41.334 18.894 0.538 95 ASN 41.616 18.797 -3.263 96 LYS 42.812 15.193 -3.258 97 PHE 39.994 14.423 -0.816 98 LYS 37.368 16.126 -2.994 99 ASP 38.656 14.150 -5.961 100 HIS 38.287 10.949 -3.940 101 MET 34.775 11.816 -2.756 102 GLN 33.815 12.663 -6.351 103 LYS 34.933 9.171 -7.417 104 GLN 32.973 7.775 -4.466 105 ASN 29.755 9.375 -5.685 106 ILE 29.588 11.610 -2.603 107 GLU 27.991 14.959 -3.445 108 TYR 28.191 16.801 -0.108 109 LEU 30.759 17.234 2.649 110 LEU 29.706 18.439 6.095 111 THR 31.855 19.527 9.028 112 TYR 31.597 21.292 12.372 113 ALA 34.305 23.943 11.989 114 ASP 36.940 24.388 14.698 115 ASN 36.288 28.172 14.633 116 PHE 40.059 28.458 14.287 117 ALA 39.452 26.540 11.067 118 ILE 36.458 28.427 9.657 119 GLY 38.708 30.615 7.548 120 TYR 40.271 27.467 6.097 121 PHE 37.000 25.751 5.205 122 LYS 35.629 28.992 3.731 123 LYS 38.824 29.046 1.679 124 GLN 38.215 25.436 0.593 125 GLY 34.739 26.313 -0.649 126 PHE 32.658 25.381 2.401 127 THR 29.774 27.626 3.429 128 LYS 27.746 28.395 6.547 129 GLU 24.603 28.373 4.414 130 HIS 23.341 24.945 3.381 131 ARG 22.199 23.710 -0.007 132 MET 21.265 20.341 1.496 133 PRO 18.161 20.359 3.797 134 GLN 18.705 19.465 7.460 135 GLU 16.079 16.758 6.980 136 LYS 18.613 15.130 4.638 137 TRP 21.402 14.646 7.196 138 LYS 19.099 14.382 10.203 139 GLY 19.586 11.037 11.903 140 TYR 22.988 10.532 10.300 141 ILE 25.095 13.501 11.291 142 LYS 24.683 14.884 14.818 143 ASP 23.001 18.271 15.308 144 TYR 25.045 20.434 17.704 145 ASP 24.045 23.949 18.744 146 GLY 27.653 24.906 19.388 147 GLY 30.207 24.866 16.579 148 THR 29.563 25.988 12.997 149 LEU 28.235 23.345 10.598 150 MET 29.679 24.119 7.175 151 GLU 28.848 22.416 3.873 152 CYS 30.652 21.876 0.564 153 TYR 29.130 20.570 -2.668 154 ILE 31.173 18.150 -4.779 155 HIS 30.290 18.698 -8.444 156 PRO 30.223 15.472 -10.561 157 TYR 32.426 16.879 -13.306 158 VAL 34.647 19.568 -11.816 159 ASP 38.378 18.826 -11.947 160 TYR 39.718 18.515 -8.400 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 C C 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 H H H H H H H H 40 H H H C S S S S S S 50 S S/T T T T S S S S S 60 S S S S S S S/T T T T 70 S S S S S S S/S S S S 80 S/T T T T C C C H H H 90 H H H H H H H H H H 100 H H H H H/S S S S/S S S 110 S S S S C C H H H H 120 H H H H H/S S S S/S S S 130 S C T T T T T T T T/S 140 S S S S S S S S S S 150 S S S 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 S 10 h H H H H H H H H H 20 H H H H H H H H h T 30 T t h H H H H H H H 40 H h t S e E E E E E 50 E E E T T T E E E E 60 E E E E E E E T T T 70 e E E E E E E E E E 80 e G G G g S S h H H 90 H H H H H H H H H H 100 H H H h T t e E E E 110 E E E S S h H H H 120 H H H h T t B S S 130 S S h H H H H h T T 140 t S S S E E E 150 E E E e t T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 134.0 90.7 53.2 2 ASP 67.4 61.0 70.5 3 PHE 164.4 98.5 45.0 4 ASP 52.9 47.8 65.2 5 ILE 112.2 78.2 52.4 6 LEU 137.1 92.7 44.4 7 THR 32.3 30.2 76.1 8 ASN 79.3 65.6 60.9 9 ASP 56.1 50.8 75.5 10 GLY 5.9 16.9 72.6 11 THR 43.5 40.7 79.1 12 HIS 0.0 0.0 90.2 13 ARG 92.0 44.0 69.2 14 ASN 95.7 79.1 65.1 15 MET 109.2 68.5 58.7 16 LYS 55.1 31.8 81.3 17 LEU 144.3 97.7 50.5 18 LEU 145.5 98.4 43.8 19 ILE 64.9 45.2 68.4 20 ASP 72.6 65.7 63.5 21 LEU 147.8 100.0 40.5 22 LYS 150.5 86.8 40.7 23 ASN 90.2 74.6 69.4 24 ILE 125.5 87.4 52.3 25 PHE 166.8 100.0 35.4 26 SER 71.4 85.4 56.5 27 ARG 45.5 21.8 84.1 28 GLN 100.8 67.8 63.2 29 LEU 127.1 86.0 47.5 30 PRO 39.0 31.3 83.8 31 LYS 0.0 0.0 90.4 32 MET 100.1 62.8 49.5 33 PRO 52.6 42.3 73.6 34 LYS 85.8 49.5 75.9 35 GLU 18.5 13.3 70.8 36 TYR 111.6 61.7 56.6 37 ILE 143.5 100.0 38.6 38 VAL 63.0 53.1 54.0 39 LYS 41.7 24.0 73.4 40 LEU 122.2 82.7 47.7 41 VAL 118.8 100.0 36.5 42 PHE 134.3 80.5 48.2 43 ASP 70.4 63.7 62.9 44 ARG 26.6 12.8 86.8 45 HIS 88.2 58.7 81.3 46 HIS 132.2 88.0 46.7 47 GLU 91.3 65.9 63.2 48 SER 82.9 99.2 37.5 49 MET 150.9 94.7 41.8 50 VAL 118.7 99.9 35.5 51 ILE 143.5 100.0 33.7 52 LEU 138.9 94.0 54.7 53 LYS 101.9 58.7 69.1 54 ASN 16.2 13.4 74.0 55 LYS 46.2 26.6 80.7 56 GLN 37.4 25.2 80.7 57 LYS 31.7 18.3 78.2 58 VAL 118.2 99.5 44.5 59 ILE 140.6 98.0 31.2 60 GLY 34.8 100.0 43.4 61 GLY 34.8 100.0 44.0 62 ILE 143.5 100.0 28.3 63 CYS 99.1 99.9 39.5 64 PHE 166.8 100.0 38.3 65 ARG 152.1 72.8 59.7 66 GLN 145.6 98.0 43.3 67 TYR 158.4 87.5 54.1 68 LYS 54.7 31.6 77.4 69 PRO 31.0 24.9 81.1 70 GLN 104.1 70.1 49.7 71 ARG 110.7 53.0 73.1 72 PHE 166.8 100.0 33.0 73 ALA 72.6 100.0 36.9 74 GLU 103.8 74.9 51.2 75 VAL 117.7 99.1 35.8 76 ALA 64.7 89.1 51.9 77 PHE 161.2 96.7 28.3 78 LEU 133.6 90.4 33.8 79 ALA 66.3 91.3 44.6 80 VAL 106.0 89.2 43.2 81 THR 75.3 70.5 53.1 82 ALA 14.5 19.9 85.5 83 ASN 12.0 10.0 80.8 84 GLU 122.1 88.1 55.0 85 GLN 82.0 55.2 72.6 86 VAL 0.0 0.0 87.3 87 ARG 89.3 42.8 83.4 88 GLY 0.7 1.9 77.7 89 TYR 151.6 83.8 48.7 90 GLY 25.1 72.2 53.2 91 THR 60.2 56.3 80.4 92 ARG 99.0 47.4 61.4 93 LEU 147.8 100.0 40.0 94 MET 159.4 100.0 33.8 95 ASN 65.2 53.9 57.5 96 LYS 66.8 38.5 64.6 97 PHE 166.8 100.0 22.4 98 LYS 153.4 88.5 40.2 99 ASP 72.3 65.5 65.2 100 HIS 109.7 73.0 52.1 101 MET 159.4 100.0 31.9 102 GLN 122.2 82.2 67.5 103 LYS 53.0 30.5 86.7 104 GLN 88.4 59.5 71.7 105 ASN 28.8 23.8 90.2 106 ILE 143.2 99.8 51.5 107 GLU 93.6 67.6 64.0 108 TYR 157.2 86.8 45.0 109 LEU 147.8 100.0 27.3 110 LEU 147.8 100.0 31.1 111 THR 102.8 96.1 39.2 112 TYR 153.5 84.8 56.8 113 ALA 72.4 99.7 48.3 114 ASP 51.7 46.8 60.7 115 ASN 28.0 23.1 78.9 116 PHE 0.0 0.0 91.2 117 ALA 53.0 73.0 57.4 118 ILE 118.3 82.4 56.4 119 GLY 0.0 0.0 72.1 120 TYR 139.3 77.0 44.2 121 PHE 158.8 95.2 28.1 122 LYS 71.8 41.4 68.3 123 LYS 41.3 23.8 85.5 124 GLN 139.3 93.7 47.0 125 GLY 4.7 13.5 78.7 126 PHE 166.8 100.0 32.0 127 THR 39.5 37.0 79.9 128 LYS 120.7 69.6 51.8 129 GLU 15.5 11.2 85.6 130 HIS 118.5 78.9 68.4 131 ARG 53.8 25.8 81.9 132 MET 157.7 98.9 33.4 133 PRO 42.2 33.9 70.1 134 GLN 47.3 31.8 70.4 135 GLU 8.5 6.2 74.3 136 LYS 102.8 59.3 59.5 137 TRP 196.4 95.8 38.8 138 LYS 100.5 58.0 63.9 139 GLY 0.0 0.0 80.3 140 TYR 101.1 55.8 66.4 141 ILE 142.7 99.5 39.8 142 LYS 38.5 22.2 77.9 143 ASP 48.1 43.5 71.4 144 TYR 89.8 49.6 67.7 145 ASP 0.0 0.0 91.2 146 GLY 0.0 0.0 81.6 147 GLY 15.1 43.4 73.2 148 THR 71.7 67.1 57.1 149 LEU 132.4 89.6 42.6 150 MET 159.4 100.0 38.7 151 GLU 133.7 96.5 45.0 152 CYS 93.2 94.0 51.3 153 TYR 102.3 56.5 64.8 154 ILE 142.9 99.6 41.6 155 HIS 92.1 61.3 53.1 156 PRO 57.2 45.9 68.0 157 TYR 22.1 12.2 81.8 158 VAL 57.1 48.0 69.8 159 ASP 0.9 0.8 87.3 160 TYR 155.0 85.6 56.7