Protein Data Bank File : 1i12a Title : TRANSFERASE 30-JAN-01 1I12 Number of Amino Acid Residues : 154 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU PRO ASP GLY PHE TYR ILE ARG ARG MET 10 GLU GLU GLY ASP LEU GLU GLN VAL THR GLU 20 THR LEU LYS VAL LEU THR THR VAL GLY THR 30 ILE THR PRO GLU SER PHE CYS LYS LEU ILE 40 LYS TYR TRP ASN GLU ALA THR VAL TRP ASN 50 ASP LYS LYS ILE MET GLN TYR ASN PRO MET 60 VAL ILE VAL ASP LYS ARG THR GLU THR VAL 70 ALA ALA THR GLY ASN ILE ILE ILE GLU ARG 80 LYS ILE ILE HIS GLU LEU GLY LEU CYS GLY 90 HIS ILE GLU ASP ILE ALA VAL ASN SER LYS 100 TYR GLN GLY GLN GLY LEU GLY LYS LEU LEU 110 ILE ASP GLN LEU VAL THR ILE GLY PHE ASP 120 TYR GLY CYS TYR LYS ILE ILE LEU ASP CYS 130 ASP GLU LYS ASN VAL LYS PHE TYR GLU LYS 140 CYS GLY PHE SER ASN ALA GLY VAL GLU MET 150 GLN ILE ARG LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 163.0 179.7 -97.6 73.6 2 PRO -69.7 174.7 -178.5 32.4 -43.7 3 ASP -67.8 131.8 177.9 -72.6 68.5 4 GLY 90.6 2.4 179.5 5 PHE -129.9 156.4 172.2 -68.4 87.0 6 TYR -144.6 167.6 177.3 69.2 -81.5 7 ILE -123.0 142.9 178.4 -173.2 162.7 8 ARG -156.1 167.4 174.0 59.7 164.4 165.8 83.3 9 ARG -65.2 147.3 177.5 -163.3 166.4 172.7 93.7 10 MET -64.5 149.6 -178.9 -169.3 -179.4 -68.2 11 GLU -131.0 165.6 -177.2 -62.4 173.9 10.0 12 GLU -58.8 -31.6 -178.2 50.3 -176.2 42.2 13 GLY -75.1 -6.7 -179.6 14 ASP -77.9 -1.9 -174.4 -69.2 -24.9 15 LEU -50.1 -51.1 -175.4 179.6 55.0 16 GLU -63.6 -45.4 -177.5 -179.7 153.8 -54.5 17 GLN -75.1 -35.8 176.8 -69.2 178.7 -4.5 18 VAL -66.2 -35.8 176.7 163.4 19 THR -60.1 -44.2 -179.8 -69.4 20 GLU -64.5 -43.9 -180.0 171.9 67.0 21.5 21 THR -63.0 -47.6 -177.5 -59.0 22 LEU -65.9 -15.8 179.4 -73.0 165.1 23 LYS -63.4 -18.9 178.7 -52.5 -60.7 -178.0 58.1 24 VAL -75.9 -12.3 -179.0 -55.4 25 LEU -99.7 -49.6 -177.7 178.8 62.7 26 THR -168.2 -174.4 -179.3 -167.0 27 THR -74.8 124.8 176.3 -53.4 28 VAL -95.5 -44.9 -177.5 -179.8 29 GLY 79.4 -162.4 -178.5 30 THR -100.8 134.7 179.5 -59.5 31 ILE -130.7 131.9 179.9 -60.6 167.7 32 THR -79.4 149.0 178.2 68.7 33 PRO -58.2 -38.3 -178.3 -32.8 38.7 34 GLU -61.8 -45.1 -179.5 -172.2 170.8 66.2 35 SER -67.4 -37.5 179.3 71.7 36 PHE -67.3 -39.0 179.2 -168.1 70.1 37 CYS -61.4 -39.1 178.0 -72.7 38 LYS -68.3 -35.4 178.4 -69.5 175.8 -175.3 -175.9 39 LEU -68.7 -43.1 -179.3 176.6 65.2 40 ILE -65.1 -35.0 176.7 -67.1 -66.3 41 LYS -63.0 -43.2 179.0 -175.6 171.8 -175.5 162.7 42 TYR -61.9 -46.0 -179.4 168.1 56.6 43 TRP -68.8 -22.7 179.7 -70.1 -9.9 44 ASN -90.7 -2.7 -178.5 -73.5 -17.7 45 GLU -119.1 -28.1 -177.6 -73.3 169.9 14.1 46 ALA -66.6 116.8 178.8 47 THR -116.4 157.7 -178.8 61.9 48 VAL -98.8 134.0 178.0 178.3 49 TRP -59.8 140.6 178.2 170.2 76.1 50 ASN -159.0 -93.2 25.7 65.4 97.5 51 ASP -107.2 146.4 177.1 -53.1 -77.5 52 LYS -123.6 122.5 -178.9 -144.1 -167.9 -170.9 169.7 53 LYS -94.3 102.4 -176.3 -60.4 156.8 -173.8 -68.1 54 ILE -108.0 117.5 175.9 -57.4 179.0 55 MET -79.8 132.3 177.0 -51.1 -56.7 -55.2 56 GLN -63.5 -41.8 -179.9 -172.4 -165.5 -22.5 57 TYR -111.0 139.8 -178.6 -68.2 81.6 58 ASN -137.2 68.5 -179.5 -59.8 -88.7 59 PRO -75.9 125.2 -177.7 31.5 -35.4 60 MET -121.2 152.1 171.2 -53.1 -65.5 -72.4 61 VAL -130.0 142.7 170.1 -69.5 62 ILE -99.9 127.8 -175.0 -78.0 172.1 63 VAL -119.8 131.8 176.1 -179.8 64 ASP -80.5 113.4 -178.5 174.9 -5.5 65 LYS -64.3 -21.9 -178.4 -65.7 171.6 59.5 64.7 66 ARG -55.4 -44.6 -179.1 -66.2 176.9 -76.3 177.0 67 THR -126.1 6.6 -173.6 50.9 68 GLU 52.1 54.7 178.6 -77.3 -70.6 -40.5 69 THR -108.4 129.1 174.1 -61.1 70 VAL -63.8 124.1 -179.7 173.1 71 ALA -104.1 -20.5 -179.2 72 ALA -163.6 156.0 177.5 73 THR -145.1 152.0 175.8 -172.3 74 GLY -164.7 165.2 -177.7 75 ASN -139.6 153.4 170.2 -162.4 -16.3 76 ILE -130.7 126.2 -179.0 -178.4 171.9 77 ILE -106.4 133.5 -175.8 -67.8 172.9 78 ILE -103.7 125.2 -177.2 -50.6 -61.3 79 GLU -114.8 131.3 174.9 176.6 -158.1 -3.1 80 ARG -94.9 128.7 179.5 176.8 68.0 73.7 -170.9 81 LYS -114.6 177.1 172.7 -63.0 179.9 169.8 -64.5 82 ILE -93.4 -43.9 -179.5 -66.7 177.7 83 ILE -58.2 159.7 -179.1 58.7 173.9 84 HIS 59.1 45.6 179.1 -149.4 -79.0 85 GLU 54.1 55.8 -177.4 -71.4 84.1 41.4 86 LEU 55.8 53.5 -178.5 -55.9 -172.7 87 GLY -73.7 163.8 177.1 88 LEU -109.4 133.0 177.5 -71.1 168.7 89 CYS -119.0 132.6 177.9 -174.7 90 GLY -97.2 141.5 -179.2 91 HIS -125.2 109.6 177.6 -64.4 84.8 92 ILE -82.9 133.8 -174.6 -75.1 179.1 93 GLU -143.6 157.4 168.6 -48.6 -91.7 -2.2 94 ASP 53.5 56.3 -179.6 -60.0 -28.4 95 ILE -91.4 125.6 -178.1 -58.4 -56.5 96 ALA -153.3 135.1 175.3 97 VAL -118.9 129.3 179.5 177.4 98 ASN -55.0 144.4 -178.9 -71.1 -133.7 99 SER -48.4 -44.3 -177.3 -173.0 100 LYS -69.1 -14.9 -179.7 62.8 -175.5 160.6 -62.2 101 TYR -107.9 1.5 -179.4 -71.1 -79.2 102 GLN -70.5 156.4 175.9 -75.9 174.4 14.6 103 GLY 68.5 25.4 178.6 104 GLN -121.1 9.9 179.1 -56.9 174.0 13.7 105 GLY 92.0 -1.1 -178.1 106 LEU -71.2 -36.1 177.8 -60.2 177.5 107 GLY -60.9 -46.3 179.3 108 LYS -63.9 -40.6 178.4 -179.5 170.2 176.1 -54.3 109 LEU -60.3 -43.7 178.5 -71.0 166.9 110 LEU -60.6 -49.6 -179.9 170.6 64.6 111 ILE -59.9 -45.2 178.8 -64.6 -57.0 112 ASP -56.7 -40.9 180.0 -70.9 -10.5 113 GLN -67.8 -40.1 178.4 -66.8 -78.6 -44.6 114 LEU -65.5 -39.9 178.1 -64.4 170.4 115 VAL -61.8 -43.1 179.1 167.8 116 THR -62.2 -42.1 178.9 -65.6 117 ILE -60.6 -43.9 -179.8 -70.6 167.5 118 GLY -65.5 -48.8 -179.1 119 PHE -69.9 -31.0 176.3 -74.5 -40.6 120 ASP -64.7 -27.9 178.4 -78.2 -8.3 121 TYR -80.0 -10.7 179.8 -75.0 -45.8 122 GLY 101.4 13.6 178.1 123 CYS -60.7 141.5 177.6 -69.5 124 TYR -85.0 -20.2 175.3 68.2 -86.1 125 LYS -155.7 161.2 174.4 69.9 179.4 -175.0 -175.7 126 ILE -130.9 132.6 -177.4 -66.0 173.4 127 ILE -128.9 160.4 174.3 59.8 173.5 128 LEU -155.2 160.8 173.9 59.7 86.8 129 ASP -112.6 145.5 177.9 -63.9 -51.2 130 CYS -151.2 160.0 173.8 66.3 131 ASP -72.0 156.4 -179.4 -74.2 -8.0 132 GLU -50.7 -34.5 -177.9 179.9 59.2 41.9 133 LYS -58.8 -26.1 -176.8 69.8 -179.6 -176.9 174.1 134 ASN -92.3 -5.5 -173.8 -63.4 -37.5 135 VAL -55.6 -46.2 -178.2 170.1 136 LYS -66.0 -34.3 173.8 -69.4 177.5 -175.5 177.8 137 PHE -60.6 -47.8 -178.3 162.3 70.4 138 TYR -66.7 -32.0 176.2 -76.4 -63.4 139 GLU -65.4 -38.6 176.0 -74.1 172.3 -24.6 140 LYS -64.8 -20.4 175.9 -73.1 -70.9 -179.9 74.5 141 CYS -92.0 6.9 177.3 -65.8 142 GLY 93.7 3.5 -179.5 143 PHE -87.9 159.5 175.9 -75.2 69.0 144 SER -134.3 158.7 -179.5 47.0 145 ASN -59.6 133.2 -177.6 -144.4 104.9 146 ALA -125.5 -16.0 -176.8 147 GLY 164.2 -162.5 -177.1 148 VAL -118.1 133.6 175.3 179.9 149 GLU -85.9 130.9 177.6 179.5 -162.2 3.1 150 MET -120.9 150.6 -179.2 -57.1 -68.0 -69.4 151 GLN -143.7 157.3 173.5 77.9 175.2 -29.8 152 ILE -137.8 136.5 -178.0 -168.1 177.2 153 ARG -108.1 148.3 -178.2 -62.7 -106.8 167.2 178.2 154 LYS -69.2 -33.5 0.0 -174.2 177.7 -74.0 172.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 87.626 29.376 20.321 2 PRO 85.724 28.910 17.031 3 ASP 83.604 31.568 15.438 4 GLY 80.658 32.709 17.362 5 PHE 81.608 31.326 20.814 6 TYR 83.538 32.508 23.845 7 ILE 84.462 31.128 27.283 8 ARG 84.197 32.888 30.656 9 ARG 83.728 32.224 34.335 10 MET 80.178 31.344 35.373 11 GLU 78.071 34.217 36.798 12 GLU 74.921 34.481 38.922 13 GLY 72.715 35.142 35.962 14 ASP 73.675 31.818 34.406 15 LEU 71.398 29.751 36.625 16 GLU 68.647 29.018 34.162 17 GLN 70.869 28.120 31.233 18 VAL 73.434 26.172 33.301 19 THR 70.506 24.100 34.762 20 GLU 69.452 23.238 31.228 21 THR 72.982 22.349 30.118 22 LEU 73.712 20.097 33.142 23 LYS 70.578 18.001 32.545 24 VAL 72.447 15.953 29.898 25 LEU 74.693 14.809 32.716 26 THR 72.369 14.221 35.682 27 THR 69.485 15.578 37.774 28 VAL 69.887 19.263 38.691 29 GLY 66.489 19.933 40.232 30 THR 65.322 23.367 41.364 31 ILE 67.698 25.996 42.711 32 THR 66.638 29.417 43.968 33 PRO 68.299 32.555 42.547 34 GLU 69.204 33.714 46.065 35 SER 71.038 30.477 46.804 36 PHE 72.808 30.447 43.459 37 CYS 74.021 34.051 43.994 38 LYS 75.465 32.901 47.340 39 LEU 77.123 29.902 45.726 40 ILE 78.761 32.027 43.012 41 LYS 79.974 34.433 45.772 42 TYR 81.528 31.423 47.583 43 TRP 83.139 30.254 44.353 44 ASN 84.484 33.764 43.638 45 GLU 86.110 34.116 47.056 46 ALA 87.416 30.685 48.078 47 THR 91.178 30.622 47.505 48 VAL 93.733 27.844 48.005 49 TRP 96.694 28.316 50.368 50 ASN 100.098 28.739 48.648 51 ASP 101.346 35.522 46.396 52 LYS 99.742 33.250 43.846 53 LYS 95.951 33.796 43.803 54 ILE 94.538 30.362 43.257 55 MET 90.751 29.974 43.129 56 GLN 89.535 26.659 44.587 57 TYR 86.599 26.599 42.152 58 ASN 86.844 27.547 38.453 59 PRO 83.384 27.137 36.931 60 MET 83.375 27.970 33.243 61 VAL 80.785 28.324 30.543 62 ILE 81.131 28.323 26.739 63 VAL 78.586 30.765 25.292 64 ASP 77.071 30.962 21.795 65 LYS 77.276 34.710 20.943 66 ARG 74.308 34.592 18.565 67 THR 71.888 34.593 21.487 68 GLU 74.255 34.654 24.509 69 THR 73.172 31.057 25.322 70 VAL 75.335 28.758 27.482 71 ALA 76.370 25.839 25.234 72 ALA 78.617 23.954 27.656 73 THR 79.861 24.082 31.217 74 GLY 82.610 22.484 33.264 75 ASN 84.601 23.119 36.430 76 ILE 88.101 22.403 37.733 77 ILE 88.539 22.281 41.506 78 ILE 91.989 22.754 42.999 79 GLU 93.087 20.588 45.980 80 ARG 96.189 21.118 48.147 81 LYS 97.770 17.826 49.306 82 ILE 100.730 16.833 51.462 83 ILE 102.140 14.321 48.928 84 HIS 104.328 15.583 46.067 85 GLU 105.905 18.338 48.210 86 LEU 102.559 19.861 49.252 87 GLY 101.354 19.394 45.698 88 LEU 98.288 20.676 43.917 89 CYS 95.874 18.324 42.218 90 GLY 93.217 19.493 39.769 91 HIS 89.815 17.743 39.651 92 ILE 87.702 18.298 36.534 93 GLU 83.997 17.930 37.290 94 ASP 80.506 18.432 35.937 95 ILE 81.220 18.531 32.267 96 ALA 78.186 18.936 30.013 97 VAL 77.544 20.176 26.460 98 ASN 73.859 20.828 25.495 99 SER 72.573 18.140 23.095 100 LYS 72.169 20.601 20.237 101 TYR 75.756 21.764 20.556 102 GLN 77.415 18.306 20.923 103 GLY 79.889 16.947 18.417 104 GLN 81.129 20.335 17.221 105 GLY 84.375 20.438 19.261 106 LEU 83.077 22.439 22.190 107 GLY 83.635 19.656 24.789 108 LYS 87.304 19.350 23.774 109 LEU 87.715 23.155 23.816 110 LEU 86.251 23.298 27.315 111 ILE 88.483 20.503 28.639 112 ASP 91.555 22.117 27.063 113 GLN 90.735 25.393 28.811 114 LEU 90.213 23.684 32.192 115 VAL 93.499 21.775 31.796 116 THR 95.289 25.075 31.075 117 ILE 93.817 26.687 34.185 118 GLY 94.956 23.747 36.339 119 PHE 98.496 23.483 34.992 120 ASP 98.924 27.294 35.059 121 TYR 98.178 27.077 38.791 122 GLY 100.926 24.486 39.197 123 CYS 98.971 21.210 39.479 124 TYR 101.146 18.158 39.102 125 LYS 98.237 16.168 37.577 126 ILE 94.596 16.758 36.665 127 ILE 92.127 13.917 37.125 128 LEU 88.475 13.233 36.486 129 ASP 86.012 10.371 36.730 130 CYS 83.741 9.402 33.881 131 ASP 81.468 6.630 32.702 132 GLU 82.956 4.134 30.229 133 LYS 80.995 5.793 27.430 134 ASN 83.166 8.971 27.725 135 VAL 86.583 7.317 27.680 136 LYS 87.353 7.804 23.991 137 PHE 86.354 11.509 24.162 138 TYR 88.754 12.029 27.068 139 GLU 91.516 10.147 25.204 140 LYS 90.974 12.621 22.292 141 CYS 91.539 15.383 24.916 142 GLY 94.867 13.847 25.933 143 PHE 93.803 11.927 29.039 144 SER 94.676 8.305 29.842 145 ASN 93.194 5.622 32.055 146 ALA 94.396 6.024 35.661 147 GLY 92.195 3.801 37.765 148 VAL 88.676 2.951 38.837 149 GLU 86.058 5.280 40.363 150 MET 84.234 3.751 43.387 151 GLN 81.237 5.196 45.186 152 ILE 78.963 4.793 48.213 153 ARG 75.534 6.449 48.494 154 LYS 73.793 7.618 51.649 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C S S S S S S/S S 10 S S C H H H H H H H 20 H H H/T T T T/S S S S S 30 C H H H H H H H H H 40 H H H H H H/S S S S S/X 50 X/S S S S S S/S S S S S 60 S S S S/T T T T S S S 70 S S/S S S S S S S S S 80 S S/T T T T S S S S S 90 S S S S/S S S S S/T T T 100 T C C C H H H H H H 110 H H H H H H H H H H 120 H H C S S S S S S S 130 S C C H H H H H H H 140 H H/S S S S S S/S S S S 150 S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T e E E E E E e 10 g G G h H H H H H H 20 H H h T T t 30 h H H H H H H H H 40 H H H H H h B 50 B S B e E 60 E E E E e T T T E E 70 E E E E E E E E E E 80 e h H H H H h E E E 90 E E E E E E E e G G 100 G g T t h H H H H H 110 H H H H H H H H H H 120 h T t S E E E 130 g G G h H H H H H H 140 h T t 150 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 133.8 90.5 48.0 2 PRO 71.9 57.7 52.1 3 ASP 0.0 0.0 88.6 4 GLY 13.3 38.3 61.0 5 PHE 148.0 88.8 46.6 6 TYR 118.4 65.4 62.4 7 ILE 125.0 87.1 40.1 8 ARG 152.9 73.2 61.9 9 ARG 149.0 71.3 60.4 10 MET 148.5 93.1 40.8 11 GLU 47.6 34.3 74.6 12 GLU 48.1 34.7 60.7 13 GLY 0.0 0.0 79.3 14 ASP 99.4 90.0 53.3 15 LEU 122.7 83.0 48.6 16 GLU 0.0 0.0 82.7 17 GLN 81.9 55.1 67.4 18 VAL 111.8 94.1 34.2 19 THR 81.6 76.3 57.3 20 GLU 39.2 28.3 82.3 21 THR 106.8 99.9 56.0 22 LEU 113.5 76.8 44.0 23 LYS 94.8 54.7 73.1 24 VAL 75.8 63.8 71.2 25 LEU 89.0 60.2 68.1 26 THR 22.9 21.4 78.4 27 THR 3.4 3.2 80.2 28 VAL 104.0 87.5 52.0 29 GLY 2.6 7.5 71.8 30 THR 1.8 1.7 83.9 31 ILE 87.2 60.7 64.9 32 THR 31.1 29.1 66.1 33 PRO 26.8 21.5 71.1 34 GLU 21.1 15.2 79.0 35 SER 36.8 44.0 70.3 36 PHE 156.8 94.0 38.0 37 CYS 55.4 55.9 68.7 38 LYS 43.2 24.9 77.5 39 LEU 81.3 55.0 55.4 40 ILE 134.7 93.9 48.5 41 LYS 42.0 24.2 84.1 42 TYR 76.0 42.0 71.6 43 TRP 167.9 81.9 41.3 44 ASN 66.1 54.7 66.5 45 GLU 45.5 32.8 70.5 46 ALA 53.8 74.2 62.7 47 THR 47.1 44.1 70.3 48 VAL 107.0 90.1 53.5 49 TRP 46.8 22.8 72.9 50 ASN 94.9 78.5 56.1 51 ASP 1.1 1.0 89.7 52 LYS 72.9 42.0 71.0 53 LYS 17.2 9.9 80.9 54 ILE 143.1 99.8 41.0 55 MET 121.6 76.3 71.9 56 GLN 98.1 66.0 59.1 57 TYR 143.8 79.5 55.2 58 ASN 115.9 95.9 49.5 59 PRO 123.1 98.9 44.3 60 MET 137.1 86.0 44.6 61 VAL 118.8 100.0 43.4 62 ILE 143.5 100.0 30.0 63 VAL 117.9 99.3 52.9 64 ASP 107.6 97.4 56.7 65 LYS 72.1 41.6 74.7 66 ARG 42.5 20.3 81.5 67 THR 26.7 25.0 81.8 68 GLU 60.1 43.3 74.0 69 THR 77.9 72.9 70.6 70 VAL 117.7 99.1 50.3 71 ALA 72.6 100.0 40.5 72 ALA 72.6 100.0 38.8 73 THR 104.2 97.5 38.0 74 GLY 34.2 98.4 50.4 75 ASN 110.2 91.2 41.0 76 ILE 143.5 100.0 34.5 77 ILE 100.6 70.1 59.3 78 ILE 143.5 100.0 35.3 79 GLU 80.6 58.1 70.1 80 ARG 160.2 76.7 47.7 81 LYS 121.2 69.9 65.7 82 ILE 4.3 3.0 77.7 83 ILE 31.9 22.2 76.0 84 HIS 60.3 40.2 65.2 85 GLU 1.0 0.7 85.7 86 LEU 65.8 44.5 64.8 87 GLY 26.9 77.3 66.5 88 LEU 140.3 94.9 50.2 89 CYS 99.2 100.0 42.9 90 GLY 34.8 100.0 41.4 91 HIS 110.7 73.7 57.4 92 ILE 143.3 99.8 30.0 93 GLU 69.8 50.4 63.6 94 ASP 36.8 33.3 62.0 95 ILE 125.8 87.7 47.9 96 ALA 68.8 94.8 44.4 97 VAL 105.2 88.6 45.8 98 ASN 115.3 95.4 54.1 99 SER 14.5 17.4 78.5 100 LYS 59.1 34.1 75.7 101 TYR 168.0 92.8 50.9 102 GLN 71.4 48.1 70.4 103 GLY 0.0 0.0 82.2 104 GLN 66.6 44.8 73.9 105 GLY 4.3 12.4 76.9 106 LEU 146.6 99.2 33.9 107 GLY 30.0 86.1 44.3 108 LYS 81.0 46.7 70.2 109 LEU 99.4 67.2 53.0 110 LEU 147.8 100.0 37.8 111 ILE 143.4 99.9 30.4 112 ASP 63.1 57.1 67.7 113 GLN 80.6 54.2 56.0 114 LEU 147.8 100.0 37.4 115 VAL 84.8 71.4 44.5 116 THR 32.2 30.1 79.5 117 ILE 104.3 72.7 48.8 118 GLY 34.8 100.0 40.4 119 PHE 82.1 49.2 69.1 120 ASP 24.2 21.9 76.4 121 TYR 148.9 82.3 53.4 122 GLY 12.1 34.8 80.7 123 CYS 99.2 100.0 43.1 124 TYR 141.0 77.9 51.3 125 LYS 85.9 49.5 55.1 126 ILE 141.1 98.3 34.0 127 ILE 82.8 57.7 58.7 128 LEU 132.6 89.7 42.6 129 ASP 41.6 37.6 73.3 130 CYS 78.5 79.1 57.6 131 ASP 20.6 18.6 78.4 132 GLU 11.3 8.2 79.1 133 LYS 28.2 16.3 86.7 134 ASN 76.4 63.2 52.9 135 VAL 86.0 72.4 68.7 136 LYS 7.3 4.2 87.4 137 PHE 99.8 59.9 53.5 138 TYR 165.2 91.3 29.0 139 GLU 64.8 46.7 70.4 140 LYS 19.3 11.2 85.3 141 CYS 98.4 99.2 43.0 142 GLY 0.0 0.1 82.7 143 PHE 134.1 80.4 47.7 144 SER 9.1 10.9 83.8 145 ASN 26.3 21.7 80.7 146 ALA 11.8 16.3 84.1 147 GLY 4.0 11.6 78.0 148 VAL 18.3 15.4 78.3 149 GLU 63.7 45.9 76.4 150 MET 19.7 12.3 82.0 151 GLN 46.9 31.6 83.8 152 ILE 0.0 0.0 87.1 153 ARG 35.9 17.2 90.0 154 LYS 0.0 0.0 94.5