Protein Data Bank File : 1d6ja Title : TRANSFERASE 13-OCT-99 1D6J Number of Amino Acid Residues : 177 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 HIS ALA SER ALA LEU THR ARG SER GLU ARG 10 THR GLU LEU ARG ASN GLN ARG GLY LEU THR 20 ILE TRP LEU THR GLY LEU SER ALA SER GLY 30 LYS SER THR LEU ALA VAL GLU LEU GLU HIS 40 GLN LEU VAL ARG ASP ARG ARG VAL HIS ALA 50 TYR ARG LEU ASP GLY ASP ASN ILE ARG PHE 60 GLY LEU ASN LYS ASP LEU GLY PHE SER GLU 70 ALA ASP ARG ASN GLU ASN ILE ARG ARG ILE 80 ALA GLU VAL ALA LYS LEU PHE ALA ASP SER 90 ASN SER ILE ALA ILE THR SER PHE ILE SER 100 PRO TYR ARG LYS ASP ARG ASP THR ALA ARG 110 GLN LEU HIS GLU VAL ALA THR PRO GLY GLU 120 GLU THR GLY LEU PRO PHE VAL GLU VAL TYR 130 VAL ASP VAL PRO VAL GLU ALA PRO TYR GLU 140 ALA PRO ALA ASN PRO GLU VAL HIS VAL LYS 150 ASN TYR GLU LEU PRO VAL GLN ASP ALA VAL 160 LYS GLN ILE ILE ASP TYR LEU ASP THR LYS 170 GLY TYR LEU PRO ALA LYS LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 HIS 0.0 -68.7 -177.1 171.9 -67.5 2 ALA -53.6 -70.8 -179.6 3 SER -101.8 159.4 -178.1 81.9 4 ALA -65.2 156.8 177.6 5 LEU -45.3 134.7 178.1 -139.7 34.8 6 THR -88.9 166.7 177.8 65.6 7 ARG -58.6 -40.5 179.7 -174.4 -175.4 -61.6 173.9 8 SER -56.7 -50.6 -178.9 -51.1 9 GLU -61.2 -48.5 -176.7 -25.9 -175.5 -150.1 10 ARG -61.2 -50.0 -180.0 -163.7 -173.3 -69.6 -81.8 11 THR -54.9 -49.5 178.0 -60.1 12 GLU -50.7 -58.4 -177.3 164.6 128.3 54.2 13 LEU -66.5 -34.0 -178.6 -55.6 152.9 14 ARG -83.8 -20.0 174.9 -69.0 -84.8 76.6 -131.6 15 ASN 64.1 36.8 177.6 -168.6 -145.7 16 GLN -169.0 157.3 177.6 76.7 173.0 85.7 17 ARG -91.5 167.1 178.2 -71.7 -165.1 57.3 -176.5 18 GLY -107.2 140.0 179.5 19 LEU -165.5 177.8 179.5 56.9 138.0 20 THR -128.5 134.1 178.8 -70.8 21 ILE -114.3 119.8 -177.9 -64.0 166.8 22 TRP -114.4 107.6 -178.7 -166.0 -68.0 23 LEU -87.2 121.3 -176.9 -65.6 91.8 24 THR -121.1 145.9 -179.3 -179.0 25 GLY 165.7 176.0 177.7 26 LEU -58.7 157.8 -178.8 -65.9 167.2 27 SER -57.2 -33.1 -178.9 62.4 28 ALA -91.5 3.3 -178.6 29 SER -62.2 -16.5 -176.5 67.3 30 GLY 86.0 8.9 -178.9 31 LYS -56.4 -37.1 179.7 54.9 -174.7 172.7 67.8 32 SER -64.5 -42.8 -179.5 178.6 33 THR -62.6 -38.1 179.8 -65.5 34 LEU -67.6 -40.2 -179.8 -98.1 55.6 35 ALA -58.2 -43.7 -178.2 36 VAL -62.7 -49.6 -179.6 169.7 37 GLU -66.1 -38.2 178.1 175.4 65.7 -171.2 38 LEU -60.0 -47.4 179.5 170.2 65.1 39 GLU -62.6 -47.1 -179.8 174.2 -170.8 43.8 40 HIS -53.2 -51.2 179.7 -153.5 147.9 41 GLN -68.5 -33.2 -179.4 -78.4 -177.3 39.5 42 LEU -67.3 -41.3 -177.7 -80.0 167.3 43 VAL -77.2 -46.3 -178.2 175.4 44 ARG -77.8 -62.3 -177.1 -174.7 -170.4 61.9 -155.7 45 ASP -74.1 -26.9 -179.9 -40.8 -33.6 46 ARG -108.8 1.7 178.0 -61.6 -67.2 -60.0 -101.2 47 ARG 59.1 22.9 179.6 0.0 0.0 0.0 0.0 48 VAL -101.5 170.3 178.3 -62.7 49 HIS -92.3 123.4 177.1 178.4 -66.5 50 ALA -140.8 152.5 -179.6 51 TYR -150.3 127.4 178.2 -174.1 65.0 52 ARG -88.1 120.2 179.1 -164.4 178.6 60.1 85.3 53 LEU -84.3 101.7 -178.0 -64.9 168.9 54 ASP -78.8 135.2 -179.3 175.3 83.8 55 GLY -48.8 -50.6 178.9 56 ASP -72.3 -39.0 175.6 -68.0 -10.9 57 ASN -59.3 -37.3 -179.7 -70.7 -26.4 58 ILE -69.2 -49.9 -179.0 -69.9 -66.4 59 ARG -61.4 -39.5 -178.8 -83.0 -166.3 -88.9 -89.5 60 PHE -82.6 -9.3 -179.4 -69.9 94.1 61 GLY -118.9 -97.6 -178.4 62 LEU -50.1 -43.9 -173.0 177.4 62.1 63 ASN -102.8 22.2 -175.3 -73.0 -173.6 64 LYS -67.0 -20.6 -179.8 80.7 -175.0 179.3 -172.1 65 ASP -79.0 -9.2 -174.0 59.4 -49.8 66 LEU -91.8 137.2 178.2 -64.1 179.3 67 GLY -107.3 -128.7 -171.7 68 PHE -128.8 14.8 174.3 -65.5 92.3 69 SER -67.2 167.3 178.7 60.8 70 GLU -66.1 -34.7 -179.9 176.3 63.1 -169.6 71 ALA -64.7 -37.9 179.2 72 ASP -69.7 -36.2 177.9 -80.5 3.3 73 ARG -62.5 -45.1 177.1 -169.3 -168.4 66.9 87.1 74 ASN -63.9 -40.6 -178.0 -72.2 -27.7 75 GLU -66.6 -37.3 178.9 176.3 66.2 4.7 76 ASN -57.4 -47.0 -176.4 -97.3 -75.6 77 ILE -66.9 -38.5 -177.9 -69.1 156.7 78 ARG -63.3 -48.7 180.0 -172.4 -164.4 74.3 77.9 79 ARG -62.9 -42.1 -179.3 -61.3 -164.2 -164.2 160.3 80 ILE -63.4 -37.8 179.7 -69.8 159.6 81 ALA -65.8 -40.9 -178.2 82 GLU -68.3 -33.3 -179.1 -68.9 -76.2 3.2 83 VAL -70.2 -43.4 178.0 168.6 84 ALA -57.3 -44.5 -178.0 85 LYS -62.2 -35.5 176.1 -177.5 -170.7 -167.7 -157.7 86 LEU -66.2 -42.7 177.1 -68.1 168.3 87 PHE -61.7 -42.7 -179.6 -87.7 84.8 88 ALA -61.9 -43.1 176.7 89 ASP -58.5 -31.6 -178.7 -169.3 59.7 90 SER -85.8 9.6 -175.5 74.5 91 ASN 65.2 45.3 176.2 -73.7 75.5 92 SER -118.2 160.9 175.8 170.8 93 ILE -100.6 107.6 179.2 -61.5 173.2 94 ALA -81.0 137.4 -179.9 95 ILE -130.3 138.4 178.8 -63.3 159.4 96 THR -155.7 149.1 177.6 -171.7 97 SER -128.5 31.5 -177.8 55.8 98 PHE -58.7 137.9 179.7 -163.9 74.6 99 ILE -48.2 131.0 -177.2 -175.3 150.4 100 SER -170.1 75.6 -178.4 36.4 101 PRO -59.4 -30.2 -174.5 22.4 -31.2 102 TYR -97.0 150.3 179.2 -46.4 101.7 103 ARG -60.8 -39.4 -178.4 -95.7 178.0 -81.1 -147.0 104 LYS -60.9 -29.1 178.8 53.7 106.2 141.1 -174.5 105 ASP -63.0 -54.4 179.4 -62.2 -24.1 106 ARG -67.5 -37.2 178.4 -69.6 103.3 54.8 -176.1 107 ASP -59.5 -39.4 176.3 -67.7 167.6 108 THR -62.8 -44.6 179.1 -68.2 109 ALA -63.4 -41.8 -179.0 110 ARG -57.5 -49.3 -179.3 -174.4 177.9 -73.3 -78.9 111 GLN -58.5 -37.6 179.3 -176.9 177.7 -51.5 112 LEU -66.9 -36.2 177.6 -49.8 178.9 113 HIS -68.7 -39.4 179.6 -80.5 71.9 114 GLU -68.9 -32.3 177.2 -66.1 166.1 -21.1 115 VAL -57.8 123.6 -178.3 134.2 116 ALA -61.8 169.1 176.1 117 THR -134.6 157.3 179.8 65.1 118 PRO -59.7 3.8 177.8 -34.1 45.3 119 GLY -83.2 -2.3 179.8 120 GLU 173.2 -160.7 177.5 0.0 0.0 0.0 121 GLU -115.5 9.3 -179.2 0.0 0.0 0.0 122 THR -126.5 160.6 178.6 -164.9 123 GLY -86.2 -159.7 -179.4 124 LEU -122.9 144.2 -178.9 -72.2 169.5 125 PRO -57.0 134.5 176.3 -21.3 38.8 126 PHE -119.8 119.3 -178.2 -176.4 79.1 127 VAL -114.9 103.0 -179.6 178.4 128 GLU -88.0 121.0 -179.1 -176.5 169.9 14.0 129 VAL -108.5 111.9 179.4 -179.0 130 TYR -83.8 111.3 178.6 178.3 25.3 131 VAL -94.3 96.1 -174.4 -170.4 132 ASP -95.5 129.7 179.2 -176.7 12.2 133 VAL -127.5 157.5 -179.0 -62.5 134 PRO -63.6 122.4 176.2 -17.4 35.6 135 VAL -87.6 85.1 -177.8 -73.2 136 GLU -170.3 37.9 -88.1 0.0 0.0 0.0 137 ALA 25.3 76.2 179.8 138 PRO -86.6 112.3 179.5 35.2 -41.4 139 TYR -45.7 134.2 176.6 -179.2 72.5 140 GLU -113.2 120.1 -175.9 -63.8 164.6 4.9 141 ALA -72.8 151.2 180.0 142 PRO -73.1 155.5 -178.6 33.0 -43.5 143 ALA -80.0 -31.3 -174.5 144 ASN -150.3 60.8 -179.2 -171.2 44.2 145 PRO -64.0 151.5 176.7 35.4 -40.0 146 GLU -68.0 -32.8 -178.0 -77.1 63.4 -151.5 147 VAL -136.3 135.8 178.8 -175.0 148 HIS -121.3 111.7 -177.3 -172.9 174.3 149 VAL -108.8 119.8 -179.5 174.3 150 LYS -95.3 91.5 -174.9 -83.0 172.6 172.3 -168.8 151 ASN -79.9 63.9 177.5 -154.9 16.2 152 TYR -128.0 119.7 -177.9 -177.2 65.8 153 GLU 48.3 49.7 -179.3 -66.3 -65.3 -36.6 154 LEU -124.6 120.7 -179.9 170.6 71.1 155 PRO -55.9 138.6 177.6 -34.2 44.5 156 VAL -54.6 -37.1 179.8 175.3 157 GLN -62.2 -32.1 -179.4 0.0 0.0 0.0 158 ASP -79.5 -34.5 178.1 -55.3 -40.3 159 ALA -58.4 -51.1 -179.7 160 VAL -65.0 -38.6 177.8 169.9 161 LYS -60.2 -33.0 -178.9 172.6 178.4 -179.5 56.1 162 GLN -64.4 -45.2 179.4 -164.3 -173.7 -29.7 163 ILE -63.2 -49.3 -177.2 -63.0 166.3 164 ILE -62.4 -44.4 178.4 -66.0 -174.8 165 ASP -56.2 -40.2 178.3 -64.4 -13.0 166 TYR -61.1 -36.1 -179.9 167.6 80.1 167 LEU -62.1 -45.0 178.5 -61.9 -173.3 168 ASP -60.7 -38.2 176.4 -77.0 -44.8 169 THR -60.2 -22.4 -178.8 75.5 170 LYS -98.8 -4.4 -179.2 -54.6 -58.8 -68.6 -166.3 171 GLY 76.8 21.6 -178.3 172 TYR -72.7 -20.3 -177.5 -61.8 152.2 173 LEU -115.9 161.2 178.2 -54.8 166.7 174 PRO -87.1 151.0 -179.3 32.9 -43.3 175 ALA -56.5 151.5 -179.1 176 LYS -73.9 -172.5 -179.8 0.0 0.0 0.0 0.0 177 LYS -154.2 -1.0 0.0 0.0 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 HIS 9.283 18.633 64.267 2 ALA 8.411 16.017 61.633 3 SER 8.714 17.734 58.256 4 ALA 10.825 20.733 57.305 5 LEU 9.784 24.394 57.514 6 THR 7.373 25.245 54.592 7 ARG 7.959 28.403 52.480 8 SER 4.927 30.066 54.266 9 GLU 6.337 29.464 57.663 10 ARG 9.826 30.556 56.805 11 THR 8.615 33.666 55.024 12 GLU 6.347 34.342 57.940 13 LEU 9.196 33.891 60.474 14 ARG 11.874 35.538 58.378 15 ASN 9.666 38.539 57.545 16 GLN 10.915 39.026 53.948 17 ARG 10.545 37.157 50.729 18 GLY 13.367 35.235 49.110 19 LEU 14.512 36.086 45.602 20 THR 17.460 36.625 43.376 21 ILE 18.599 39.850 41.859 22 TRP 20.848 39.457 38.850 23 LEU 22.611 42.618 37.693 24 THR 23.541 42.407 34.019 25 GLY 25.472 44.823 31.826 26 LEU 28.842 45.498 30.186 27 SER 31.915 44.768 32.354 28 ALA 32.390 48.469 32.681 29 SER 28.745 49.178 33.461 30 GLY 29.407 49.552 37.196 31 LYS 27.040 46.616 37.962 32 SER 29.404 45.236 40.566 33 THR 29.474 48.541 42.448 34 LEU 25.726 48.686 42.434 35 ALA 25.476 45.117 43.766 36 VAL 27.695 46.040 46.739 37 GLU 25.773 49.198 47.644 38 LEU 22.506 47.332 47.028 39 GLU 23.411 44.537 49.487 40 HIS 24.609 47.135 52.014 41 GLN 21.391 49.152 51.991 42 LEU 19.232 46.094 52.042 43 VAL 20.914 44.709 55.120 44 ARG 21.602 47.983 56.902 45 ASP 18.788 50.275 55.861 46 ARG 16.077 47.681 55.328 47 ARG 17.098 45.156 57.976 48 VAL 16.732 42.087 55.750 49 HIS 19.002 39.192 55.109 50 ALA 20.604 39.771 51.627 51 TYR 23.895 38.346 50.291 52 ARG 26.091 39.239 47.343 53 LEU 27.578 36.172 45.654 54 ASP 30.950 37.649 44.836 55 GLY 32.701 36.527 41.652 56 ASP 35.995 35.775 43.301 57 ASN 34.573 34.086 46.436 58 ILE 32.708 31.850 43.932 59 ARG 35.647 31.225 41.599 60 PHE 38.106 30.447 44.386 61 GLY 35.702 28.265 46.276 62 LEU 32.640 26.463 44.932 63 ASN 33.675 26.890 41.227 64 LYS 37.447 26.513 41.568 65 ASP 37.433 23.344 39.544 66 LEU 36.062 25.180 36.491 67 GLY 38.143 26.583 33.693 68 PHE 37.231 28.337 30.457 69 SER 35.878 25.863 27.896 70 GLU 32.320 26.779 26.875 71 ALA 30.960 23.896 28.993 72 ASP 32.774 25.305 32.039 73 ARG 31.546 28.822 31.286 74 ASN 27.941 27.438 31.265 75 GLU 28.597 25.370 34.397 76 ASN 29.872 28.418 36.313 77 ILE 26.567 30.177 35.630 78 ARG 24.562 27.117 36.444 79 ARG 26.092 26.581 39.858 80 ILE 25.874 30.265 40.818 81 ALA 22.202 30.264 39.774 82 GLU 21.484 27.156 41.870 83 VAL 23.264 28.740 44.818 84 ALA 21.258 32.005 44.448 85 LYS 18.121 29.837 44.342 86 LEU 19.133 28.183 47.609 87 PHE 19.577 31.595 49.234 88 ALA 16.186 32.641 47.825 89 ASP 14.713 29.395 49.234 90 SER 16.065 30.351 52.686 91 ASN 14.220 33.709 52.365 92 SER 17.336 35.706 51.641 93 ILE 17.838 38.149 48.783 94 ALA 20.689 36.678 46.712 95 ILE 22.497 39.298 44.683 96 THR 24.985 38.836 41.838 97 SER 26.643 40.603 39.020 98 PHE 28.505 37.488 37.823 99 ILE 29.812 37.740 34.275 100 SER 27.052 36.517 31.847 101 PRO 27.079 38.326 28.486 102 TYR 24.364 36.418 26.804 103 ARG 20.694 36.491 27.210 104 LYS 20.783 32.754 27.328 105 ASP 23.070 32.934 30.428 106 ARG 20.532 34.938 32.434 107 ASP 17.545 33.049 30.865 108 THR 19.052 29.828 32.100 109 ALA 19.359 31.211 35.645 110 ARG 15.806 32.652 35.330 111 GLN 14.438 29.294 34.245 112 LEU 15.943 27.465 37.282 113 HIS 14.298 29.989 39.579 114 GLU 10.873 29.612 37.863 115 VAL 11.120 25.803 38.144 116 ALA 9.133 25.038 41.264 117 THR 10.386 23.423 44.450 118 PRO 8.701 21.114 46.962 119 GLY 8.602 24.373 48.926 120 GLU 5.483 25.155 46.840 121 GLU 3.870 24.946 43.376 122 THR 5.713 28.104 42.518 123 GLY 9.255 29.182 41.743 124 LEU 11.212 32.027 43.314 125 PRO 11.498 35.544 41.947 126 PHE 14.309 36.294 39.550 127 VAL 14.903 40.055 39.133 128 GLU 17.134 40.889 36.260 129 VAL 18.552 44.416 36.590 130 TYR 19.955 45.920 33.438 131 VAL 22.759 48.325 34.381 132 ASP 22.853 50.286 31.089 133 VAL 25.626 52.714 30.209 134 PRO 26.264 54.856 27.079 135 VAL 28.217 52.858 24.549 136 GLU 29.925 56.165 24.044 137 ALA 31.898 37.813 23.723 138 PRO 29.531 40.589 22.543 139 TYR 27.297 41.568 25.428 140 GLU 23.531 40.993 24.848 141 ALA 21.228 43.414 26.668 142 PRO 18.223 41.809 28.168 143 ALA 14.924 42.020 26.241 144 ASN 12.694 42.625 29.222 145 PRO 14.502 43.317 32.494 146 GLU 12.501 43.782 35.675 147 VAL 14.629 46.868 36.340 148 HIS 16.390 49.175 33.962 149 VAL 19.040 51.455 35.448 150 LYS 20.603 54.039 33.113 151 ASN 23.878 54.347 34.977 152 TYR 25.150 57.593 33.517 153 GLU 25.890 60.459 35.911 154 LEU 23.643 58.667 38.399 155 PRO 24.565 58.610 42.113 156 VAL 25.030 54.973 43.185 157 GLN 22.579 55.660 46.033 158 ASP 19.896 56.630 43.487 159 ALA 20.645 53.652 41.289 160 VAL 20.095 51.368 44.265 161 LYS 16.939 53.189 45.412 162 GLN 15.579 52.503 41.999 163 ILE 16.195 48.813 42.488 164 ILE 14.798 48.706 46.035 165 ASP 11.716 50.725 45.139 166 TYR 10.995 48.134 42.460 167 LEU 11.312 45.436 45.172 168 ASP 8.736 47.371 47.267 169 THR 6.339 47.501 44.329 170 LYS 6.314 43.661 44.379 171 GLY 5.995 43.434 48.152 172 TYR 9.306 41.556 48.602 173 LEU 10.405 43.561 51.567 174 PRO 9.010 44.449 54.972 175 ALA 8.223 48.206 55.384 176 LYS 11.124 50.362 56.694 177 LYS 11.496 52.091 60.058 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S H H H H H 10 H H H H H/S S S S S S/S 20 S S S S S S/T T T T H 30 H H H H H H H H H H 40 H H H H H C S S S S 50 S S S H H H H H H H 60 H C C C S S S S H H 70 H H H H H H H H H H 80 H H H H H H H H H H 90 H/S S S S S S S S S S 100 S H H H H H H H H H 110 H H H H H C T T T T 120 S S S S S S S S S S 130 S S S S C C/X X/S S S S 140 S S S S S S/S S S S S 150 C C C C H H H H H H 160 H H H H H H H H H H 170 H S S S S/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S h H H H H 10 H H H H h t E E 20 E E E E S g G G G h 30 H H H H H H H H H H 40 H H H h T t e E 50 E E e h H H H H H H 60 h T T T T t S h H 70 H H H H H H H H H H 80 H H H H H H H H H h 90 T e E E E E 100 h H H H H H H H H 110 H H H H h t T T t 120 S S e E E E E E 130 E E 140 S S S E E E E 150 e S S h H H H H H 160 H H H H H H H H H h 170 T t S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 HIS 0.0 0.0 91.8 2 ALA 5.1 7.0 82.8 3 SER 6.0 7.2 85.6 4 ALA 0.7 1.0 88.8 5 LEU 85.0 57.5 71.2 6 THR 39.4 36.9 79.2 7 ARG 172.0 82.3 64.7 8 SER 2.8 3.4 82.0 9 GLU 71.0 51.2 58.7 10 ARG 139.9 67.0 58.7 11 THR 68.2 63.8 64.1 12 GLU 14.5 10.5 79.5 13 LEU 49.6 33.5 68.7 14 ARG 94.8 45.4 73.4 15 ASN 26.5 21.9 79.8 16 GLN 141.5 95.2 52.2 17 ARG 119.4 57.2 62.2 18 GLY 34.7 99.7 56.8 19 LEU 147.8 100.0 30.2 20 THR 106.8 99.9 38.1 21 ILE 143.5 100.0 24.3 22 TRP 205.0 100.0 34.1 23 LEU 147.8 100.0 34.4 24 THR 105.1 98.4 50.5 25 GLY 34.8 99.9 54.1 26 LEU 85.9 58.1 53.7 27 SER 9.7 11.6 77.2 28 ALA 2.8 3.9 84.6 29 SER 83.5 99.9 48.4 30 GLY 8.8 25.2 83.3 31 LYS 150.4 86.7 57.3 32 SER 26.7 31.9 75.8 33 THR 32.8 30.7 64.0 34 LEU 146.7 99.3 35.9 35 ALA 72.6 100.0 44.3 36 VAL 50.5 42.5 79.5 37 GLU 95.3 68.7 59.2 38 LEU 147.8 100.0 26.3 39 GLU 100.2 72.3 54.2 40 HIS 63.3 42.1 74.6 41 GLN 124.1 83.5 58.8 42 LEU 147.8 100.0 23.8 43 VAL 54.5 45.8 75.3 44 ARG 90.5 43.3 78.2 45 ASP 53.6 48.5 70.7 46 ARG 180.3 86.3 52.1 47 ARG 179.6 86.0 84.7 48 VAL 114.6 96.5 45.0 49 HIS 65.0 43.3 71.0 50 ALA 72.6 100.0 44.9 51 TYR 96.3 53.2 63.5 52 ARG 164.3 78.7 59.5 53 LEU 142.5 96.4 37.4 54 ASP 81.7 74.0 76.2 55 GLY 26.7 76.6 63.6 56 ASP 32.6 29.5 77.5 57 ASN 33.9 28.0 81.8 58 ILE 129.4 90.2 42.8 59 ARG 118.3 56.6 61.1 60 PHE 28.6 17.1 79.2 61 GLY 7.7 22.1 79.3 62 LEU 72.1 48.8 64.3 63 ASN 120.9 100.0 46.5 64 LYS 37.5 21.6 87.5 65 ASP 40.5 36.6 77.7 66 LEU 139.2 94.2 68.1 67 GLY 10.4 30.0 68.3 68 PHE 7.9 4.7 85.2 69 SER 22.8 27.2 81.3 70 GLU 54.4 39.2 84.5 71 ALA 7.2 10.0 84.9 72 ASP 72.8 65.9 66.0 73 ARG 153.6 73.5 64.7 74 ASN 63.5 52.5 73.1 75 GLU 99.5 71.8 65.3 76 ASN 104.8 86.7 48.0 77 ILE 139.0 96.9 48.8 78 ARG 98.3 47.0 68.7 79 ARG 160.9 77.0 63.5 80 ILE 143.1 99.7 32.4 81 ALA 72.6 100.0 41.6 82 GLU 79.1 57.1 61.9 83 VAL 89.7 75.5 38.7 84 ALA 72.6 100.0 40.6 85 LYS 148.1 85.4 56.7 86 LEU 31.5 21.3 76.5 87 PHE 109.9 65.9 52.3 88 ALA 72.6 100.0 58.4 89 ASP 59.2 53.6 68.7 90 SER 43.9 52.5 70.5 91 ASN 117.6 97.2 55.2 92 SER 81.9 98.0 54.4 93 ILE 143.5 100.0 39.1 94 ALA 72.5 99.8 51.1 95 ILE 143.5 100.0 35.4 96 THR 106.6 99.7 35.5 97 SER 74.7 89.3 59.6 98 PHE 158.0 94.7 50.2 99 ILE 44.9 31.3 73.9 100 SER 81.9 98.0 52.5 101 PRO 108.3 87.0 49.4 102 TYR 142.5 78.7 59.2 103 ARG 100.2 48.0 74.7 104 LYS 77.7 44.8 78.9 105 ASP 108.0 97.7 45.5 106 ARG 208.5 99.8 50.6 107 ASP 42.4 38.4 69.0 108 THR 48.6 45.4 63.5 109 ALA 72.6 100.0 36.1 110 ARG 158.8 76.0 68.3 111 GLN 31.0 20.8 78.8 112 LEU 112.6 76.2 57.4 113 HIS 150.2 100.0 45.7 114 GLU 48.4 34.9 71.9 115 VAL 35.8 30.1 83.7 116 ALA 42.5 58.6 73.0 117 THR 85.5 80.0 61.7 118 PRO 2.0 1.6 84.3 119 GLY 18.0 51.8 78.3 120 GLU 106.8 77.0 76.0 121 GLU 62.2 44.8 77.5 122 THR 34.5 32.3 77.8 123 GLY 32.9 94.4 67.7 124 LEU 143.5 97.1 53.5 125 PRO 103.6 83.3 59.1 126 PHE 165.4 99.2 44.5 127 VAL 117.5 98.9 34.0 128 GLU 132.4 95.5 48.8 129 VAL 118.8 100.0 31.1 130 TYR 149.1 82.4 47.3 131 VAL 118.8 100.0 41.6 132 ASP 80.0 72.4 57.1 133 VAL 96.0 80.8 57.4 134 PRO 71.7 57.6 53.8 135 VAL 12.6 10.6 78.1 136 GLU 70.4 50.8 70.3 137 ALA 24.7 34.0 72.8 138 PRO 22.4 18.0 86.9 139 TYR 161.2 89.1 53.0 140 GLU 85.5 61.7 68.1 141 ALA 41.2 56.7 63.6 142 PRO 121.7 97.8 49.0 143 ALA 17.5 24.1 76.5 144 ASN 3.2 2.7 81.3 145 PRO 108.3 87.0 58.6 146 GLU 101.1 73.0 69.1 147 VAL 112.3 94.5 40.2 148 HIS 88.2 58.7 56.0 149 VAL 118.8 100.0 39.8 150 LYS 36.8 21.2 82.0 151 ASN 103.3 85.4 49.2 152 TYR 53.8 29.7 71.6 153 GLU 17.5 12.6 80.4 154 LEU 111.7 75.6 64.0 155 PRO 42.7 34.3 78.2 156 VAL 71.0 59.8 53.7 157 GLN 97.9 65.9 77.1 158 ASP 49.6 44.9 57.6 159 ALA 72.6 100.0 42.9 160 VAL 118.8 100.0 44.1 161 LYS 46.3 26.7 83.9 162 GLN 75.8 51.0 68.3 163 ILE 143.5 100.0 24.6 164 ILE 133.3 92.9 46.9 165 ASP 58.2 52.6 67.7 166 TYR 135.2 74.7 50.9 167 LEU 147.8 100.0 23.4 168 ASP 67.5 61.1 73.9 169 THR 30.7 28.7 71.2 170 LYS 85.7 49.4 74.4 171 GLY 3.4 9.7 84.1 172 TYR 165.8 91.6 36.7 173 LEU 147.8 100.0 40.4 174 PRO 93.6 75.2 70.0 175 ALA 0.5 0.7 91.1 176 LYS 134.1 77.4 78.6 177 LYS 91.5 52.8 77.0