Protein Data Bank File : 1b55a Title : TRANSFERASE 12-JAN-99 1B55 Number of Amino Acid Residues : 163 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA ALA VAL ILE LEU GLU SER ILE PHE LEU 10 LYS ARG SER GLN GLN LYS LYS LYS THR SER 20 PRO LEU ASN PHE LYS LYS ARG LEU PHE LEU 30 LEU THR VAL HIS LYS LEU SER TYR TYR GLU 40 TYR ASP PHE GLU ARG GLY ARG ARG GLY SER 50 LYS LYS GLY SER ILE ASP VAL GLU LYS ILE 60 THR CYS VAL GLU THR VAL VAL PRO GLU LYS 70 ASN PRO PRO PRO GLU ARG GLN ILE PRO ARG 80 ARG MET GLU GLN ILE SER ILE ILE GLU ARG 90 PHE PRO TYR PRO PHE GLN VAL VAL TYR ASP 100 GLU GLY PRO LEU TYR VAL PHE SER PRO THR 110 GLU GLU LEU ARG LYS ARG TRP ILE HIS GLN 120 LEU LYS ASN VAL ILE ARG TYR ASN SER ASP 130 LEU VAL GLN LYS TYR HIS PRO CYS PHE TRP 140 ILE ASP GLY GLN TYR LEU CYS CYS SER GLN 150 THR ALA LYS ASN ALA MET GLY CYS GLN ILE 160 LEU GLU ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 -142.9 178.0 2 ALA -84.2 157.9 173.3 3 VAL -97.9 127.5 179.3 167.5 4 ILE -85.7 -37.4 -176.5 -54.4 130.5 5 LEU -155.0 155.3 177.3 -77.6 173.7 6 GLU -154.3 123.5 -171.7 171.7 -175.6 72.1 7 SER -151.9 171.5 179.0 -50.2 8 ILE -114.4 126.1 177.9 -85.3 128.8 9 PHE -130.7 174.9 177.6 -60.3 -72.3 10 LEU -115.5 112.9 -175.9 174.4 77.4 11 LYS -102.8 149.0 176.6 78.3 139.7 -122.1 -37.2 12 ARG -98.5 154.0 -171.0 -177.6 -166.7 102.8 -176.2 13 SER -64.0 131.8 -180.0 -179.4 14 GLN -72.4 -18.4 179.8 -83.8 -164.5 104.0 15 GLN 52.2 43.0 175.9 -110.3 179.2 -29.7 16 LYS -61.8 -39.9 173.6 -113.2 108.2 143.1 -142.9 17 LYS -93.3 138.0 176.2 -22.6 -167.7 -61.0 -125.5 18 LYS -42.6 -47.4 -170.5 -13.4 -163.0 96.3 -172.7 19 THR -77.4 0.5 -173.4 -130.8 20 SER -83.4 137.2 -176.6 -74.9 21 PRO -77.3 157.7 174.7 21.1 -32.9 22 LEU -93.0 105.4 -177.4 -159.9 52.4 23 ASN -147.7 169.8 -178.2 67.3 9.9 24 PHE -114.1 146.2 -178.9 -44.7 62.9 25 LYS -132.1 141.0 176.9 -61.2 -79.4 165.7 178.2 26 LYS -81.5 130.0 179.5 -91.4 177.6 -150.4 -177.7 27 ARG -139.9 148.9 177.0 -61.3 -78.6 -173.7 -106.3 28 LEU -88.5 116.1 178.7 175.4 57.0 29 PHE -95.0 135.4 173.4 -78.6 72.3 30 LEU -119.0 168.2 172.3 -72.6 -152.6 31 LEU -150.2 116.3 165.3 171.9 69.4 32 THR -109.2 168.6 173.7 58.9 33 VAL -56.4 -19.9 179.5 -64.6 34 HIS -84.9 -56.5 -178.2 -81.9 -115.3 35 LYS -141.1 172.9 175.1 -3.1 -175.3 -173.8 154.5 36 LEU -120.4 119.5 -168.5 175.3 80.8 37 SER -135.5 151.4 175.9 18.3 38 TYR -137.2 141.1 -170.6 57.4 -88.7 39 TYR -127.5 155.5 172.1 -59.6 89.9 40 GLU -64.3 148.2 177.0 -137.7 175.0 -19.0 41 TYR -105.7 129.2 178.3 -169.3 55.6 42 ASP -95.3 85.0 -177.1 -174.7 167.6 43 PHE -67.1 -44.1 178.5 158.7 113.0 44 GLU -45.5 -70.0 -178.3 -75.9 -66.7 -58.6 45 ARG -66.4 -13.7 -172.8 -67.5 178.7 163.0 -162.1 46 GLY 70.4 43.5 177.5 47 ARG -146.2 166.0 -177.4 46.8 -147.1 -70.2 -134.9 48 ARG -69.9 147.2 -176.8 116.9 174.4 114.1 60.5 49 GLY -105.6 -144.6 178.7 50 SER -67.4 134.7 179.0 1.6 51 LYS -69.5 143.7 -176.1 176.0 154.2 128.4 -171.4 52 LYS -126.3 2.5 176.7 -79.0 -62.3 165.9 138.3 53 GLY 159.8 158.1 168.4 54 SER -144.7 167.1 171.4 35.6 55 ILE -135.9 125.7 -176.0 -74.8 179.8 56 ASP -69.9 128.9 -175.4 -74.9 -16.1 57 VAL -54.5 -14.0 -174.8 169.9 58 GLU -101.1 -25.5 173.9 44.3 173.6 43.8 59 LYS -71.9 3.8 -175.2 -66.0 -168.9 154.3 62.5 60 ILE -83.3 109.3 -175.9 -64.1 177.4 61 THR -79.8 -24.7 -167.9 58.1 62 CYS -170.2 151.1 175.3 180.0 63 VAL -145.8 127.2 -179.1 170.3 64 GLU -161.2 176.9 172.0 -55.3 -83.5 -13.0 65 THR -70.9 169.1 -179.8 55.2 66 VAL -133.1 151.1 178.8 -167.2 67 VAL -75.7 127.1 -173.4 144.9 68 PRO -64.0 145.4 179.3 22.6 -10.5 69 GLU -66.4 155.1 -170.5 69.5 -112.9 88.5 70 LYS -73.5 -34.1 -178.9 -70.4 -179.7 -152.3 -172.1 71 ASN -140.0 71.4 179.4 -67.6 -44.4 72 PRO -75.7 142.4 174.8 33.2 -41.2 73 PRO -70.8 161.2 -172.4 41.1 -32.8 74 PRO -49.3 -27.4 -179.2 22.2 -35.6 75 GLU -66.7 -13.9 178.1 68.3 165.2 150.9 76 ARG -137.1 46.0 180.0 -9.9 -155.3 -116.1 -79.3 77 GLN -114.9 159.5 174.6 -104.6 177.5 31.7 78 ILE -90.9 126.7 -178.0 30.5 107.7 79 PRO -65.5 -166.9 167.6 17.6 -6.4 80 ARG -103.2 -50.6 -179.0 -122.6 -131.1 -104.8 -82.4 81 ARG 173.4 135.4 -51.3 -113.1 102.8 -165.3 -114.3 82 MET -9.9 116.8 -167.1 -18.9 141.3 -65.3 83 GLU -91.6 -52.9 174.5 120.5 141.9 -10.9 84 GLN -30.2 -27.2 179.3 170.2 -149.7 48.6 85 ILE -93.4 -52.8 -176.9 -66.9 -54.6 86 SER -48.2 -35.5 -177.3 59.7 87 ILE -74.7 0.2 174.7 -156.0 -154.0 88 ILE -134.1 12.6 172.6 63.3 161.1 89 GLU -135.4 -17.7 -177.2 -7.7 -171.2 -74.4 90 ARG -119.2 115.6 -178.3 -171.6 -160.2 -134.3 5.5 91 PHE -126.6 88.0 -174.4 -57.4 83.8 92 PRO -100.3 4.9 -172.9 31.4 -14.2 93 TYR -115.7 97.3 -172.6 -61.1 -70.3 94 PRO -91.5 164.9 177.8 31.3 -22.3 95 PHE -154.1 167.8 -168.2 77.8 -99.4 96 GLN -133.3 132.5 179.1 73.9 -167.2 112.3 97 VAL -116.8 106.4 -172.9 177.6 98 VAL -106.6 148.0 -179.7 -151.1 99 TYR -157.8 -177.0 -174.4 65.0 -65.7 100 ASP -48.1 -43.6 -178.1 27.4 -65.3 101 GLU -74.6 -18.2 177.5 -51.4 164.6 55.6 102 GLY 146.2 -145.2 178.4 103 PRO -114.4 137.8 170.2 30.3 -26.5 104 LEU -97.2 128.5 178.9 173.8 51.1 105 TYR -100.4 128.8 -168.0 -68.2 -58.7 106 VAL -138.6 122.4 177.2 -176.0 107 PHE -97.0 137.3 179.5 -58.3 72.1 108 SER -114.3 147.2 -174.3 154.7 109 PRO -77.1 -32.4 171.4 33.8 -30.2 110 THR -122.6 164.5 -178.8 55.4 111 GLU -72.2 -42.5 -172.8 -156.6 115.6 -155.5 112 GLU -60.9 -39.7 -178.6 153.8 -149.0 60.9 113 LEU -59.5 -41.8 -173.9 -151.0 21.4 114 ARG -69.9 -40.8 178.5 171.4 175.3 68.3 176.9 115 LYS -57.2 -56.1 -174.7 -129.0 -143.4 145.8 -175.5 116 ARG -48.3 -48.7 -174.2 -64.8 177.3 81.0 -143.0 117 TRP -66.6 -46.3 -173.6 -84.9 75.3 118 ILE -59.6 -39.1 176.7 -78.5 175.0 119 HIS -63.6 -58.1 177.8 -172.6 -57.8 120 GLN -54.5 -40.8 -178.0 -65.7 -57.3 -40.6 121 LEU -59.8 -45.5 171.4 -86.1 168.7 122 LYS -50.2 -67.6 177.5 -64.4 -165.7 167.7 -122.3 123 ASN -40.3 -51.6 -172.9 -63.1 16.3 124 VAL -57.3 -33.5 -173.8 177.9 125 ILE -100.9 -5.3 178.8 57.4 167.1 126 ARG -31.4 -40.5 -174.5 -148.0 120.4 166.0 -93.7 127 TYR -115.3 26.7 179.0 -46.8 -95.6 128 ASN -68.4 163.2 -177.4 -94.6 43.8 129 SER -89.8 -14.9 -178.1 61.4 130 ASP -123.8 29.7 178.8 -57.8 -105.2 131 LEU -61.3 95.6 168.1 -61.2 -152.7 132 VAL -48.9 155.7 -176.6 -41.8 133 GLN -118.2 -11.7 172.3 -134.0 134.5 40.9 134 LYS -117.0 136.8 -178.8 -77.8 172.1 -100.0 -171.4 135 TYR -136.5 176.7 171.1 87.0 -52.9 136 HIS -107.7 112.9 -175.8 -56.7 -73.0 137 PRO -78.6 -9.5 176.2 19.5 -23.3 138 CYS -106.9 167.1 -177.5 -62.9 139 PHE -75.2 162.9 168.6 -75.1 -73.8 140 TRP -91.1 126.1 -176.4 -169.5 95.2 141 ILE -159.5 137.7 176.9 -142.2 140.6 142 ASP 56.8 32.7 170.2 -87.4 -16.9 143 GLY 115.7 -16.0 -178.0 144 GLN -167.0 175.9 -178.8 31.5 160.4 80.0 145 TYR -85.8 126.3 176.0 -80.3 -81.0 146 LEU -56.2 -42.4 -167.5 -46.9 155.5 147 CYS -64.2 -38.0 -174.7 36.8 148 CYS -133.9 14.3 175.2 54.2 149 SER 55.3 4.0 174.8 -82.6 150 GLN -67.5 151.1 -174.4 -24.4 -177.9 13.7 151 THR -100.0 -28.1 178.7 48.5 152 ALA -62.9 100.5 176.1 153 LYS -32.3 -36.6 177.5 -155.8 175.7 -102.7 115.1 154 ASN -111.5 44.0 170.3 70.9 -16.1 155 ALA -66.9 160.9 172.2 156 MET -67.6 132.4 178.1 -153.5 -144.8 -159.9 157 GLY -53.9 150.7 -175.3 158 CYS -100.6 5.4 179.0 34.9 159 GLN -139.6 143.1 -176.9 -166.8 -165.5 -1.5 160 ILE -110.4 123.6 177.2 -78.0 -167.5 161 LEU -98.9 106.3 178.7 -91.5 172.4 162 GLU -126.7 116.8 -171.5 86.0 -98.9 -77.3 163 ASN 20.2 134.0 0.0 70.6 118.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 25.260 2.167 39.090 2 ALA 25.682 5.378 41.119 3 VAL 22.816 7.475 42.177 4 ILE 23.142 10.931 40.668 5 LEU 20.073 12.126 42.411 6 GLU 17.358 10.969 44.675 7 SER 14.294 13.040 45.759 8 ILE 10.668 12.583 46.584 9 PHE 8.301 14.011 44.041 10 LEU 4.734 13.904 43.123 11 LYS 4.355 12.400 39.671 12 ARG 1.137 12.302 37.556 13 SER -0.329 9.122 36.084 14 GLN 1.104 8.295 32.788 15 GLN -2.091 6.708 31.980 16 LYS -0.402 4.196 29.663 17 LYS -3.373 2.102 30.091 18 LYS -6.881 3.013 29.052 19 THR -8.527 2.096 32.310 20 SER -6.104 4.352 34.305 21 PRO -7.043 7.375 36.330 22 LEU -5.384 10.640 35.993 23 ASN -3.849 10.872 39.419 24 PHE -0.792 11.755 41.480 25 LYS 1.539 9.619 43.544 26 LYS 4.275 10.449 45.887 27 ARG 7.266 8.510 44.624 28 LEU 10.844 8.183 45.465 29 PHE 12.681 9.028 42.128 30 LEU 16.220 7.927 41.391 31 LEU 18.615 8.702 38.682 32 THR 21.523 6.803 37.271 33 VAL 23.174 7.238 33.941 34 HIS 20.988 4.396 33.011 35 LYS 17.495 5.231 33.980 36 LEU 15.129 7.444 35.725 37 SER 13.069 5.319 37.951 38 TYR 10.491 5.744 40.564 39 TYR 9.436 3.602 43.561 40 GLU 6.793 3.590 46.158 41 TYR 8.150 5.123 49.280 42 ASP 8.199 3.251 52.485 43 PHE 8.277 6.053 54.969 44 GLU 7.755 4.087 58.192 45 ARG 10.732 1.926 57.675 46 GLY 12.427 4.745 55.771 47 ARG 13.251 2.923 52.525 48 ARG 12.635 2.709 48.938 49 GLY 9.881 0.470 48.058 50 SER 8.507 -1.355 45.087 51 LYS 9.507 0.070 41.756 52 LYS 6.671 1.571 39.871 53 GLY 8.369 2.556 36.579 54 SER 11.434 3.703 34.745 55 ILE 12.404 5.518 31.750 56 ASP 15.672 4.586 30.055 57 VAL 17.947 7.608 29.972 58 GLU 18.622 7.209 26.327 59 LYS 15.109 7.031 25.129 60 ILE 14.713 10.647 26.438 61 THR 14.057 13.223 23.739 62 CYS 13.564 16.120 26.094 63 VAL 13.332 17.541 29.641 64 GLU 11.968 20.921 30.734 65 THR 9.728 22.898 32.997 66 VAL 5.948 22.745 32.209 67 VAL 3.612 25.705 32.601 68 PRO 1.987 25.336 35.928 69 GLU -1.652 24.589 35.911 70 LYS -3.909 27.477 36.574 71 ASN -5.776 26.249 39.626 72 PRO -3.782 23.533 41.255 73 PRO -5.208 22.158 44.386 74 PRO -3.118 22.810 47.556 75 GLU -0.878 19.830 47.275 76 ARG 0.722 21.659 44.379 77 GLN 0.052 25.253 45.185 78 ILE 2.539 27.882 46.141 79 PRO 2.053 28.882 49.719 80 ARG 2.241 32.356 51.305 81 ARG 4.664 31.469 54.270 82 MET 7.959 23.731 58.917 83 GLU 9.590 22.639 56.007 84 GLN 10.657 19.222 56.669 85 ILE 7.031 18.346 56.334 86 SER 5.966 20.691 53.525 87 ILE 8.778 19.438 51.326 88 ILE 7.063 16.074 51.337 89 GLU 3.575 17.139 51.019 90 ARG 3.541 20.204 48.873 91 PHE 4.975 19.851 45.365 92 PRO 4.243 22.761 43.235 93 TYR 7.077 22.970 40.567 94 PRO 6.589 20.557 37.701 95 PHE 8.691 19.400 34.994 96 GLN 8.551 17.092 32.149 97 VAL 10.650 14.144 31.114 98 VAL 9.640 13.264 27.652 99 TYR 10.333 10.158 25.708 100 ASP 8.908 7.897 23.010 101 GLU 5.754 7.023 24.917 102 GLY 5.035 10.650 25.844 103 PRO 5.829 12.824 28.824 104 LEU 6.243 11.924 32.416 105 TYR 5.157 14.854 34.659 106 VAL 6.948 15.389 37.870 107 PHE 6.374 17.894 40.522 108 SER 8.966 19.180 42.754 109 PRO 8.429 20.702 46.106 110 THR 11.143 23.361 45.556 111 GLU 12.550 25.184 42.568 112 GLU 16.105 24.416 43.366 113 LEU 15.312 20.847 43.488 114 ARG 13.641 21.096 40.079 115 LYS 16.556 23.017 38.851 116 ARG 18.886 20.430 40.138 117 TRP 17.151 17.649 38.415 118 ILE 16.596 19.258 35.054 119 HIS 20.148 20.020 34.826 120 GLN 21.532 16.636 35.618 121 LEU 18.928 15.100 33.416 122 LYS 20.226 17.391 30.815 123 ASN 23.833 16.317 31.332 124 VAL 22.595 12.917 31.315 125 ILE 20.870 13.259 27.985 126 ARG 23.266 15.648 26.183 127 TYR 24.392 13.115 23.515 128 ASN 21.191 11.300 23.122 129 SER 20.211 10.525 19.602 130 ASP 16.676 12.000 19.663 131 LEU 16.806 15.138 21.443 132 VAL 13.778 16.897 20.075 133 GLN 13.889 20.616 19.502 134 LYS 10.163 21.311 19.755 135 TYR 8.218 20.498 22.999 136 HIS 4.848 21.326 24.654 137 PRO 5.382 23.791 27.442 138 CYS 1.860 23.166 28.812 139 PHE 0.319 19.979 30.123 140 TRP -1.391 17.288 28.208 141 ILE -4.796 17.175 29.722 142 ASP -8.201 15.961 29.017 143 GLY -7.378 14.627 25.596 144 GLN -4.936 17.013 24.266 145 TYR -2.355 19.536 24.878 146 LEU -3.290 22.943 26.096 147 CYS -0.558 24.668 24.322 148 CYS -1.561 23.511 20.885 149 SER -4.636 21.491 21.388 150 GLN -3.104 18.564 19.652 151 THR -4.417 15.307 20.878 152 ALA -1.627 12.752 20.240 153 LYS -0.109 12.475 23.670 154 ASN 3.215 12.140 21.850 155 ALA 2.491 14.831 19.381 156 MET 5.227 17.099 18.176 157 GLY 5.808 20.044 20.496 158 CYS 4.345 23.191 19.308 159 GLN 7.284 25.203 20.454 160 ILE 10.942 25.527 19.781 161 LEU 12.967 26.841 22.493 162 GLU 16.073 27.947 20.875 163 ASN 18.385 29.747 23.224 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 S/S 10 S S S C C C C C S S 20 S S S S S S S S/S S S 30 S S/T T T T/S S S S S S 40 S S/T T T T S S S S S/S 50 S S S/S S S S/T T T T/S S 60 S S/S S S S S S C C S 70 S S S/T T T T/S S S S S 80 C/X X/C H H H H H H H H/S 90 S S S/S S S S S S S/T T 100 T T/S S S S S S S S H 110 H H H H H H H H H H 120 H H H H H H C C C C 130 S S S S/S S S S/S S S S/T 140 T T T C T T T T S S 150 S S C C C C C S S S 160 S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S E E E E E E 10 E E e t T T t 20 e E E E E E E E 30 E e S e E E E E E E 40 E E T T T T E E E E 50 E E E E E E e T e E 60 E E E E E e S 70 S g G G G g 80 h H H H H h T T t 90 E E E E E E E e 100 T E E E E E E E S h 110 H H H H H H H H H H 120 H H H H H h T t S 130 e E E S S e E 140 E T T E E e T T t 150 t T T t S E E 160 e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 23.9 33.0 74.6 2 ALA 5.3 7.3 78.3 3 VAL 75.5 63.5 59.4 4 ILE 108.0 75.2 52.1 5 LEU 132.3 89.5 47.3 6 GLU 64.7 46.7 56.9 7 SER 71.2 85.1 46.6 8 ILE 104.5 72.8 45.5 9 PHE 166.5 99.8 31.3 10 LEU 143.3 96.9 44.1 11 LYS 155.8 89.8 47.7 12 ARG 196.3 94.0 31.5 13 SER 71.0 85.0 66.4 14 GLN 128.3 86.4 62.4 15 GLN 108.3 72.9 66.8 16 LYS 86.2 49.7 75.9 17 LYS 35.6 20.5 79.0 18 LYS 0.0 0.0 89.5 19 THR 5.9 5.6 79.7 20 SER 64.5 77.1 56.0 21 PRO 41.9 33.7 84.3 22 LEU 106.9 72.3 66.5 23 ASN 73.8 61.1 55.1 24 PHE 137.8 82.6 54.5 25 LYS 92.3 53.2 80.3 26 LYS 94.8 54.7 62.1 27 ARG 177.1 84.8 44.1 28 LEU 133.9 90.6 40.4 29 PHE 165.4 99.1 31.0 30 LEU 132.1 89.3 51.6 31 LEU 147.8 100.0 30.8 32 THR 86.2 80.7 51.0 33 VAL 43.7 36.8 55.3 34 HIS 33.4 22.2 68.8 35 LYS 99.1 57.1 77.6 36 LEU 145.4 98.4 26.5 37 SER 74.3 88.8 46.8 38 TYR 169.6 93.7 40.5 39 TYR 157.9 87.2 52.4 40 GLU 66.5 48.0 75.8 41 TYR 129.7 71.7 53.1 42 ASP 69.7 63.1 56.5 43 PHE 44.1 26.4 73.6 44 GLU 9.3 6.7 79.0 45 ARG 49.1 23.5 84.2 46 GLY 14.1 40.4 79.1 47 ARG 82.1 39.3 80.3 48 ARG 103.4 49.5 61.8 49 GLY 20.1 57.6 67.6 50 SER 24.3 29.0 75.9 51 LYS 98.6 56.9 70.9 52 LYS 87.3 50.4 71.7 53 GLY 15.4 44.3 64.8 54 SER 67.8 81.0 50.9 55 ILE 139.5 97.2 40.0 56 ASP 59.0 53.4 65.1 57 VAL 111.3 93.7 50.6 58 GLU 27.6 19.9 82.6 59 LYS 75.6 43.6 80.4 60 ILE 143.5 100.0 37.5 61 THR 88.4 82.7 45.7 62 CYS 86.7 87.4 42.0 63 VAL 118.7 100.0 26.1 64 GLU 108.1 78.0 50.9 65 THR 50.2 47.0 69.7 66 VAL 118.3 99.5 49.5 67 VAL 49.2 41.4 60.1 68 PRO 48.2 38.7 70.1 69 GLU 99.5 71.8 52.9 70 LYS 6.3 3.6 87.7 71 ASN 3.8 3.2 79.9 72 PRO 101.4 81.5 60.8 73 PRO 70.8 56.8 69.6 74 PRO 35.9 28.8 77.3 75 GLU 74.3 53.6 60.1 76 ARG 185.3 88.7 44.5 77 GLN 80.2 54.0 66.4 78 ILE 36.1 25.2 72.3 79 PRO 67.4 54.1 68.8 80 ARG 0.0 0.0 90.6 81 ARG 0.0 0.0 85.3 82 MET 28.0 17.6 80.1 83 GLU 28.6 20.7 75.5 84 GLN 14.2 9.5 71.5 85 ILE 78.8 54.9 62.9 86 SER 46.1 55.2 56.4 87 ILE 89.8 62.5 59.7 88 ILE 94.5 65.9 50.6 89 GLU 57.2 41.3 63.1 90 ARG 151.8 72.7 55.4 91 PHE 166.8 100.0 43.2 92 PRO 120.4 96.7 50.8 93 TYR 133.0 73.5 56.8 94 PRO 122.7 98.5 45.8 95 PHE 164.2 98.4 28.0 96 GLN 145.2 97.7 40.6 97 VAL 118.8 100.0 23.4 98 VAL 92.4 77.8 54.5 99 TYR 175.5 97.0 53.2 100 ASP 46.9 42.4 59.9 101 GLU 59.5 42.9 68.8 102 GLY 32.5 93.3 50.5 103 PRO 121.3 97.4 46.4 104 LEU 147.7 99.9 37.8 105 TYR 176.0 97.2 42.9 106 VAL 118.0 99.3 28.6 107 PHE 164.3 98.5 41.8 108 SER 83.6 100.0 35.6 109 PRO 122.6 98.5 43.3 110 THR 54.8 51.3 60.1 111 GLU 51.7 37.3 71.8 112 GLU 34.1 24.6 68.2 113 LEU 121.4 82.2 59.6 114 ARG 180.6 86.5 44.7 115 LYS 25.3 14.6 75.8 116 ARG 84.3 40.3 65.7 117 TRP 203.8 99.4 32.3 118 ILE 121.9 84.9 39.5 119 HIS 51.5 34.3 77.2 120 GLN 97.9 65.9 56.2 121 LEU 147.6 99.8 23.4 122 LYS 85.1 49.1 67.7 123 ASN 58.3 48.2 66.9 124 VAL 99.0 83.3 47.2 125 ILE 135.1 94.1 48.2 126 ARG 65.8 31.5 76.3 127 TYR 26.6 14.7 86.2 128 ASN 106.4 88.0 63.4 129 SER 8.4 10.1 89.8 130 ASP 23.0 20.8 74.7 131 LEU 103.6 70.1 68.6 132 VAL 65.1 54.8 69.4 133 GLN 18.7 12.6 81.3 134 LYS 105.9 61.0 56.9 135 TYR 157.2 86.9 47.0 136 HIS 143.1 95.3 43.7 137 PRO 101.4 81.5 51.9 138 CYS 76.8 77.4 43.1 139 PHE 162.8 97.6 36.1 140 TRP 180.4 88.0 55.1 141 ILE 89.9 62.7 56.7 142 ASP 4.1 3.7 75.4 143 GLY 8.1 23.3 59.0 144 GLN 80.5 54.2 67.7 145 TYR 176.5 97.5 50.2 146 LEU 78.2 52.9 61.5 147 CYS 84.9 85.6 44.2 148 CYS 77.6 78.3 52.9 149 SER 28.5 34.1 81.0 150 GLN 80.9 54.4 59.8 151 THR 30.9 28.9 81.3 152 ALA 19.1 26.3 76.9 153 LYS 109.7 63.2 63.9 154 ASN 42.6 35.3 79.8 155 ALA 64.1 88.3 59.5 156 MET 42.1 26.4 81.6 157 GLY 34.8 100.0 58.0 158 CYS 72.6 73.2 56.5 159 GLN 65.2 43.9 63.3 160 ILE 81.9 57.1 62.4 161 LEU 73.5 49.8 76.6 162 GLU 37.4 27.0 78.0 163 ASN 0.0 0.0 83.2