Protein Data Bank File : 1qmya Title : HYDROLASE 08-OCT-99 1QMY Number of Amino Acid Residues : 156 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET GLU LEU THR LEU TYR ASN GLY GLU LYS 10 LYS THR PHE TYR SER ARG PRO ASN ASN HIS 20 ASP ASN ALA TRP LEU ASN ALA ILE LEU GLN 30 LEU PHE ARG TYR VAL GLU GLU PRO PHE PHE 40 ASP TRP VAL TYR SER SER PRO GLU ASN LEU 50 THR LEU GLU ALA ILE LYS GLN LEU GLU ASP 60 LEU THR GLY LEU GLU LEU HIS GLU GLY GLY 70 PRO PRO ALA LEU VAL ILE TRP ASN ILE LYS 80 HIS LEU LEU HIS THR GLY ILE GLY THR ALA 90 SER ARG PRO SER GLU VAL CYS VAL VAL ASP 100 GLY THR ASP MET SER LEU ALA ASP PHE HIS 110 ALA GLY ILE PHE LEU LYS GLY GLN GLU HIS 120 ALA VAL PHE ALA CYS VAL THR SER ASN GLY 130 TRP TYR ALA ILE ASP ASP GLU ASP PHE TYR 140 PRO TRP THR PRO ASP PRO SER ASP VAL LEU 150 VAL PHE VAL PRO TYR ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 135.3 177.6 -177.2 -177.8 -62.1 2 GLU -85.1 132.2 179.6 -172.6 169.7 76.7 3 LEU -117.4 147.3 176.0 -57.3 -178.9 4 THR -106.6 116.5 -172.4 -60.7 5 LEU -78.4 -176.8 -176.6 -55.3 178.4 6 TYR -58.0 -29.3 -179.5 84.3 90.4 7 ASN -99.6 18.0 179.5 65.4 -9.1 8 GLY 82.3 -8.5 -178.7 9 GLU -73.1 136.9 177.9 -174.5 -177.1 -28.6 10 LYS -94.7 145.3 176.3 -61.7 177.2 -171.7 178.3 11 LYS -151.8 135.4 178.7 -176.4 174.0 -65.2 -58.4 12 THR -91.9 134.9 177.1 -57.6 13 PHE -118.8 152.9 -177.4 -63.6 78.2 14 TYR -115.6 145.8 174.1 -50.9 -54.0 15 SER -66.4 138.2 179.1 -69.1 16 ARG -123.1 135.6 -179.7 -69.7 -152.7 56.5 88.2 17 PRO -79.6 158.5 179.1 35.3 -43.8 18 ASN -124.2 89.3 -178.9 -175.7 -16.5 19 ASN -113.2 -2.0 178.8 -65.8 -65.9 20 HIS -133.7 38.0 179.8 -53.5 90.0 21 ASP 51.1 47.4 -174.4 -161.0 -10.2 22 ASN -110.9 30.8 177.7 58.1 -87.3 23 ALA -58.5 -36.1 -179.2 24 TRP -61.0 -39.2 -178.6 60.9 -85.9 25 LEU -74.7 -41.1 179.3 173.6 57.5 26 ASN -61.1 -35.1 -179.0 -73.1 -19.7 27 ALA -68.9 -43.7 176.9 28 ILE -59.7 -43.6 -176.6 -70.2 170.2 29 LEU -62.9 -39.6 177.8 -65.1 169.4 30 GLN -67.4 -40.3 178.8 -58.7 -65.0 -3.9 31 LEU -62.1 -46.1 -179.2 171.4 58.4 32 PHE -61.8 -38.7 177.4 -80.5 8.8 33 ARG -60.5 -46.2 -178.8 170.4 61.1 166.4 -170.6 34 TYR -59.5 -44.6 180.0 -174.4 -87.0 35 VAL -93.8 6.1 -179.7 -57.1 36 GLU 60.3 43.7 177.8 -70.9 -173.3 17.6 37 GLU -79.9 124.1 179.9 168.2 57.5 44.1 38 PRO -74.0 -23.3 -174.4 -5.0 11.9 39 PHE -37.8 -52.7 178.9 -168.3 78.9 40 PHE -113.4 34.2 -177.2 -89.9 -39.3 41 ASP -63.6 -26.4 177.4 57.8 11.8 42 TRP -67.2 -25.0 178.0 55.7 -82.1 43 VAL -78.5 -48.9 -177.6 174.0 44 TYR -63.1 -40.6 179.3 -160.7 74.5 45 SER -88.7 7.1 -177.3 -73.1 46 SER -79.3 137.6 178.7 -179.8 47 PRO -72.4 -6.2 -180.0 -26.3 38.6 48 GLU -110.9 162.6 179.2 -61.9 -166.5 -66.2 49 ASN -85.5 102.9 -179.3 -175.7 165.4 50 LEU -97.5 19.3 179.0 -58.7 -172.4 51 THR -48.5 -49.9 -179.0 -65.4 52 LEU -60.7 -38.4 179.9 -71.9 177.9 53 GLU -68.9 -39.6 179.9 -49.0 -173.2 -12.3 54 ALA -62.9 -44.5 179.2 55 ILE -59.6 -46.9 -179.4 -75.1 169.7 56 LYS -59.1 -44.3 -179.0 164.2 97.9 -177.4 94.9 57 GLN -66.9 -41.0 180.0 170.7 178.4 -76.7 58 LEU -65.8 -36.8 178.4 -75.7 175.5 59 GLU -61.2 -42.7 -178.6 -68.5 -174.7 -27.0 60 ASP -63.7 -35.1 -178.0 -78.5 -8.1 61 LEU -84.3 -26.4 -175.9 -67.1 170.9 62 THR -108.0 -19.1 -179.9 66.4 63 GLY 77.5 12.5 179.0 64 LEU -103.4 154.1 177.4 -57.0 171.2 65 GLU -95.4 124.3 -174.2 -156.3 -63.3 -51.9 66 LEU -126.9 25.0 179.4 -58.2 168.3 67 HIS -88.4 -12.7 -179.2 -81.9 87.5 68 GLU -133.9 54.8 -179.8 -49.2 -169.2 -34.9 69 GLY 99.7 166.1 179.8 70 GLY -169.4 163.9 -179.7 71 PRO -96.6 103.8 -178.7 36.1 -35.1 72 PRO -55.6 -40.0 -180.0 30.7 -40.8 73 ALA -65.9 -38.7 179.5 74 LEU -68.8 -46.7 176.4 -180.0 55.9 75 VAL -52.6 -51.0 -179.4 172.0 76 ILE -61.1 -43.4 178.5 -76.3 162.0 77 TRP -60.7 -45.4 -176.5 -168.1 -105.1 78 ASN -70.1 -17.1 177.9 -71.4 -5.5 79 ILE -113.0 7.4 -175.4 68.6 171.9 80 LYS -49.3 -37.8 -179.7 68.1 -172.9 171.2 -62.4 81 HIS -68.8 -11.6 179.1 53.2 -72.9 82 LEU -97.8 -1.4 -177.9 -60.5 176.4 83 LEU -100.1 148.4 176.3 -51.6 176.3 84 HIS -70.8 -40.6 -178.9 169.2 76.6 85 THR -69.3 136.4 178.2 -49.9 86 GLY -74.4 132.1 -177.9 87 ILE -116.3 130.1 179.9 -54.3 -58.0 88 GLY -134.9 -159.0 179.3 89 THR -126.5 170.4 179.2 61.5 90 ALA -60.5 -35.5 -178.1 91 SER -74.6 -36.7 177.9 -48.1 92 ARG -129.3 79.9 -179.0 -59.0 -157.6 -122.9 139.8 93 PRO -64.2 153.5 174.5 -11.8 32.7 94 SER -144.7 -162.0 -178.7 -174.9 95 GLU -60.1 -41.9 178.4 -168.2 174.5 -17.5 96 VAL -121.2 140.2 -178.0 172.6 97 CYS -124.9 138.6 175.6 -60.4 98 VAL -95.0 142.6 -178.8 -61.4 99 VAL -70.1 142.8 -177.3 -57.5 100 ASP -127.6 17.3 -179.3 62.2 0.2 101 GLY 97.4 -4.3 177.5 102 THR -68.0 157.4 -179.1 -67.1 103 ASP -76.6 116.6 -178.3 -176.8 -77.1 104 MET -106.8 144.8 178.2 -60.8 -48.3 -49.3 105 SER -127.9 148.5 -179.8 153.3 106 LEU -50.1 -39.8 -179.8 -166.7 70.8 107 ALA -67.0 -10.0 -179.8 108 ASP -75.5 -14.4 -175.3 -64.4 -23.6 109 PHE -154.5 160.0 179.2 45.7 74.9 110 HIS -108.3 -2.8 178.8 45.6 94.5 111 ALA -164.8 163.0 177.0 112 GLY 172.9 179.9 177.3 113 ILE -107.3 131.9 -176.5 -67.3 178.2 114 PHE -128.9 151.5 176.7 -53.4 80.7 115 LEU -85.1 127.3 177.0 -142.0 46.5 116 LYS -123.9 106.3 -179.1 -174.2 158.7 -179.9 -71.0 117 GLY 95.3 5.2 -179.5 118 GLN 65.5 -3.9 -176.1 -59.3 -44.6 -59.4 119 GLU -121.0 -14.8 -172.1 51.4 175.0 55.2 120 HIS -135.9 117.2 -179.6 179.7 77.3 121 ALA -89.1 145.5 179.2 122 VAL -138.1 164.7 175.0 -61.1 123 PHE -102.2 148.6 176.9 170.8 75.0 124 ALA -149.5 148.2 176.9 125 CYS -154.8 165.3 176.8 59.7 126 VAL -70.9 138.3 174.9 174.2 127 THR -141.4 166.6 -179.4 78.9 128 SER -63.3 -14.0 177.5 60.1 129 ASN -102.8 19.5 -178.0 -64.7 -47.0 130 GLY 97.6 167.9 176.2 131 TRP -51.3 133.6 -178.4 -91.3 88.3 132 TYR -126.9 144.4 177.0 -116.4 68.3 133 ALA -106.4 141.8 172.1 134 ILE -110.0 108.3 -173.8 -54.5 -171.2 135 ASP -120.8 92.8 -175.1 179.7 0.7 136 ASP 55.4 -114.6 -178.6 -69.6 -20.4 137 GLU -84.5 -14.3 -175.6 -65.2 176.0 -53.2 138 ASP -100.2 140.0 176.4 -51.4 -51.1 139 PHE -115.5 134.9 179.2 -69.9 70.2 140 TYR -164.1 154.0 179.7 55.8 78.5 141 PRO -61.2 135.1 -179.2 -19.9 37.9 142 TRP -169.1 118.8 179.3 -177.4 69.4 143 THR -104.3 113.7 -179.1 -55.2 144 PRO -71.0 158.0 175.8 33.9 -40.8 145 ASP -89.5 123.3 -179.4 174.7 -36.2 146 PRO -57.8 -22.3 179.5 -23.3 39.5 147 SER -64.5 -13.3 -178.1 168.8 148 ASP -102.4 4.4 -178.7 -65.7 -22.6 149 VAL -75.3 140.4 179.6 70.7 150 LEU -116.9 -32.2 -178.9 -56.0 168.4 151 VAL -143.5 138.1 -178.8 -175.1 152 PHE -143.4 163.5 -179.2 60.3 -84.7 153 VAL -117.9 101.4 -179.4 -174.2 154 PRO -67.5 160.6 177.1 35.5 -44.5 155 TYR -72.8 160.7 177.5 -69.8 80.9 156 ASP -69.7 147.5 0.0 -62.6 -34.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 31.717 -6.136 5.730 2 GLU 33.630 -3.403 3.962 3 LEU 32.462 -2.937 0.352 4 THR 34.178 -1.044 -2.451 5 LEU 31.333 0.683 -4.238 6 TYR 30.877 1.488 -7.952 7 ASN 33.081 4.553 -7.693 8 GLY 35.878 2.845 -5.724 9 GLU 34.761 4.358 -2.360 10 LYS 34.915 2.019 0.587 11 LYS 32.101 1.862 3.110 12 THR 31.440 -0.603 5.860 13 PHE 27.991 -2.132 6.137 14 TYR 26.825 -4.301 8.996 15 SER 24.975 -7.573 9.174 16 ARG 21.540 -6.996 10.695 17 PRO 19.405 -9.690 12.359 18 ASN 15.821 -10.443 11.376 19 ASN 13.872 -11.383 14.525 20 HIS 10.847 -9.311 13.800 21 ASP 10.107 -10.081 10.144 22 ASN 12.131 -6.977 9.412 23 ALA 14.007 -7.568 6.142 24 TRP 12.119 -4.533 4.817 25 LEU 13.597 -2.379 7.596 26 ASN 17.084 -3.852 7.266 27 ALA 16.884 -3.019 3.585 28 ILE 15.910 0.598 4.307 29 LEU 18.761 0.851 6.882 30 GLN 21.364 -0.414 4.401 31 LEU 20.057 2.014 1.765 32 PHE 20.281 4.844 4.322 33 ARG 23.818 3.713 5.193 34 TYR 24.688 3.779 1.494 35 VAL 23.488 7.307 0.818 36 GLU 24.580 8.539 4.296 37 GLU 21.074 9.383 5.432 38 PRO 21.244 10.406 9.090 39 PHE 17.631 9.517 9.979 40 PHE 18.137 6.143 11.573 41 ASP 21.826 6.274 12.166 42 TRP 21.270 5.643 15.886 43 VAL 19.555 2.385 14.926 44 TYR 22.214 1.300 12.439 45 SER 25.177 2.150 14.684 46 SER 23.774 0.720 17.898 47 PRO 25.637 -2.163 19.591 48 GLU 22.119 -3.338 20.500 49 ASN 19.265 -4.501 18.263 50 LEU 16.954 -1.455 18.071 51 THR 14.543 -2.909 15.530 52 LEU 11.508 -2.723 17.850 53 GLU 12.019 0.924 18.650 54 ALA 12.523 1.763 14.956 55 ILE 9.318 -0.114 14.027 56 LYS 7.344 1.730 16.692 57 GLN 8.599 5.063 15.489 58 LEU 7.906 4.209 11.875 59 GLU 4.383 3.048 12.688 60 ASP 3.738 6.394 14.351 61 LEU 5.065 8.297 11.357 62 THR 3.462 6.150 8.639 63 GLY 0.079 4.826 9.838 64 LEU 1.193 1.366 8.783 65 GLU 1.297 -1.804 10.881 66 LEU 4.917 -2.896 10.671 67 HIS 5.382 -5.767 13.135 68 GLU 4.942 -8.503 10.512 69 GLY 6.618 -7.160 7.448 70 GLY 6.234 -3.826 5.721 71 PRO 6.477 -2.093 2.327 72 PRO 9.884 -0.351 2.201 73 ALA 9.122 1.991 -0.672 74 LEU 5.906 3.193 0.967 75 VAL 7.611 3.601 4.322 76 ILE 10.329 5.780 2.731 77 TRP 7.748 7.805 0.798 78 ASN 5.575 8.488 3.874 79 ILE 8.613 9.810 5.853 80 LYS 10.468 11.546 2.991 81 HIS 10.049 15.074 4.416 82 LEU 11.961 13.931 7.513 83 LEU 14.941 12.763 5.526 84 HIS 18.049 14.634 4.522 85 THR 18.114 12.652 1.275 86 GLY 15.870 13.903 -1.544 87 ILE 13.284 11.266 -2.420 88 GLY 11.644 11.260 -5.839 89 THR 10.092 8.886 -8.386 90 ALA 11.451 7.379 -11.606 91 SER 9.417 10.062 -13.429 92 ARG 10.524 12.957 -11.204 93 PRO 13.929 11.732 -9.875 94 SER 15.881 12.847 -6.872 95 GLU 18.799 11.207 -5.059 96 VAL 16.743 8.152 -4.109 97 CYS 13.759 7.097 -6.183 98 VAL 10.721 5.036 -5.406 99 VAL 9.481 3.036 -8.382 100 ASP 6.307 4.393 -9.943 101 GLY 5.597 1.945 -12.758 102 THR 8.109 3.542 -15.099 103 ASP 10.091 0.913 -17.043 104 MET 13.321 0.118 -15.084 105 SER 16.660 -1.363 -16.152 106 LEU 19.741 -2.571 -14.124 107 ALA 21.869 0.138 -15.797 108 ASP 19.557 2.818 -14.348 109 PHE 21.035 2.525 -10.840 110 HIS 23.970 1.502 -8.672 111 ALA 21.973 0.539 -5.597 112 GLY 18.419 -0.045 -4.338 113 ILE 16.029 -2.067 -2.322 114 PHE 14.800 -5.145 -4.155 115 LEU 12.207 -7.780 -3.799 116 LYS 13.885 -11.203 -3.630 117 GLY 11.311 -14.006 -3.711 118 GLN 8.455 -11.452 -3.991 119 GLU 8.261 -11.885 -0.220 120 HIS 11.611 -10.620 1.022 121 ALA 13.293 -7.276 0.483 122 VAL 17.077 -6.924 0.464 123 PHE 19.436 -4.065 -0.277 124 ALA 21.822 -4.628 -3.161 125 CYS 24.433 -2.446 -4.742 126 VAL 27.337 -2.532 -7.130 127 THR 30.604 -3.574 -5.519 128 SER 33.990 -4.438 -6.930 129 ASN 32.981 -8.151 -6.559 130 GLY 29.844 -7.628 -8.596 131 TRP 26.343 -6.663 -7.608 132 TYR 26.037 -7.700 -3.974 133 ALA 23.067 -8.196 -1.754 134 ILE 23.028 -7.228 1.882 135 ASP 20.313 -9.619 3.033 136 ASP 19.630 -9.298 6.736 137 GLU 22.778 -10.874 8.192 138 ASP 24.215 -12.149 4.927 139 PHE 26.329 -10.523 2.224 140 TYR 26.624 -12.363 -1.099 141 PRO 27.005 -11.828 -4.865 142 TRP 23.550 -11.249 -6.289 143 THR 22.499 -9.323 -9.388 144 PRO 18.898 -8.278 -9.097 145 ASP 16.273 -8.506 -11.775 146 PRO 15.228 -4.820 -12.166 147 SER 11.607 -5.887 -12.253 148 ASP 12.154 -6.385 -8.551 149 VAL 13.455 -2.938 -7.626 150 LEU 11.286 -0.937 -5.206 151 VAL 13.682 1.934 -4.419 152 PHE 16.794 2.837 -6.342 153 VAL 19.715 5.212 -6.432 154 PRO 20.281 6.560 -9.952 155 TYR 23.689 7.551 -11.220 156 ASP 24.474 11.299 -11.218 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S/T T T T/S S S 10 S S S S S S S S/T T T 20 T H H H H H H H H H 30 H H H H H H C C C H 40 H H H H H H C C C H 50 H H H H H H H H H H 60 H H H/S S S S/T T T T C 70 H H H H H H H H H H 80 C C C S S S S S S/T T 90 T T T T T T/S S S S S 100 S S S S S/T T T T C C 110 C S S S S/T T T T S S 120 S S S S S S S/T T T T/S 130 S S S S S/T T T T/S S S 140 S/S S S S S/T T T T/S S S 150 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 T T t e E 10 E E e S S 20 S h H H H H H H H H 30 H H H H H h t t T h 40 H H H H h t S S h 50 H H H H H H H H H H 60 H H h S S 70 h H H H H H H H H h 80 G G g S S e E E E e 90 S S S E E E e 100 S g G G e E E 110 E E E E E E T T T E 120 E E E E E e t T T t 130 e E E E E T T E E E 140 E e g G G e E E 150 E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 74.6 46.8 65.8 2 GLU 58.8 42.5 71.3 3 LEU 142.0 96.1 33.4 4 THR 69.7 65.2 59.5 5 LEU 138.9 94.0 48.3 6 TYR 120.8 66.8 58.9 7 ASN 57.7 47.7 68.6 8 GLY 8.3 23.7 74.6 9 GLU 58.2 42.0 80.2 10 LYS 58.2 33.6 82.9 11 LYS 146.7 84.6 59.5 12 THR 62.7 58.6 65.2 13 PHE 166.8 100.0 34.1 14 TYR 92.1 50.9 70.6 15 SER 45.3 54.2 62.8 16 ARG 196.6 94.1 53.8 17 PRO 87.1 69.9 76.4 18 ASN 94.9 78.5 70.3 19 ASN 40.1 33.2 78.6 20 HIS 94.6 63.0 58.7 21 ASP 36.1 32.6 79.5 22 ASN 120.7 99.8 60.9 23 ALA 66.3 91.3 75.6 24 TRP 199.0 97.0 35.8 25 LEU 147.7 99.9 30.3 26 ASN 118.9 98.4 59.5 27 ALA 71.5 98.5 49.3 28 ILE 143.0 99.7 25.8 29 LEU 147.1 99.5 38.3 30 GLN 147.3 99.1 41.3 31 LEU 147.5 99.8 24.0 32 PHE 159.3 95.5 32.7 33 ARG 140.1 67.0 60.9 34 TYR 172.2 95.1 30.5 35 VAL 110.4 92.9 45.3 36 GLU 39.7 28.6 87.8 37 GLU 137.2 99.0 40.5 38 PRO 60.1 48.3 74.1 39 PHE 135.6 81.3 43.9 40 PHE 166.3 99.7 31.3 41 ASP 35.1 31.7 70.6 42 TRP 104.1 50.8 69.8 43 VAL 118.8 100.0 37.3 44 TYR 172.8 95.5 50.3 45 SER 33.3 39.8 75.6 46 SER 70.9 84.8 57.3 47 PRO 12.5 10.1 86.1 48 GLU 18.5 13.4 80.0 49 ASN 82.3 68.1 69.2 50 LEU 118.0 79.8 65.1 51 THR 106.3 99.5 53.9 52 LEU 63.4 42.9 64.9 53 GLU 47.6 34.3 62.3 54 ALA 72.6 100.0 36.5 55 ILE 143.5 100.0 39.9 56 LYS 49.7 28.7 83.0 57 GLN 89.1 59.9 53.2 58 LEU 147.5 99.8 25.0 59 GLU 110.0 79.4 62.5 60 ASP 39.1 35.4 78.5 61 LEU 96.7 65.5 52.3 62 THR 105.9 99.1 45.5 63 GLY 0.0 0.0 86.2 64 LEU 108.9 73.7 55.5 65 GLU 43.3 31.2 75.5 66 LEU 147.8 100.0 41.6 67 HIS 81.9 54.5 67.8 68 GLU 15.8 11.4 86.2 69 GLY 20.8 59.7 77.9 70 GLY 29.3 84.2 41.2 71 PRO 68.5 55.0 46.6 72 PRO 117.6 94.5 32.3 73 ALA 53.4 73.5 49.2 74 LEU 74.7 50.5 61.6 75 VAL 118.7 99.9 25.9 76 ILE 143.4 100.0 23.1 77 TRP 119.7 58.4 57.7 78 ASN 81.2 67.1 58.3 79 ILE 143.0 99.6 29.3 80 LYS 110.5 63.7 58.5 81 HIS 38.9 25.9 74.7 82 LEU 86.6 58.6 54.6 83 LEU 147.8 100.0 41.5 84 HIS 23.0 15.3 80.5 85 THR 103.4 96.8 46.3 86 GLY 6.2 17.8 74.7 87 ILE 142.5 99.3 36.1 88 GLY 27.6 79.3 55.9 89 THR 80.3 75.2 48.4 90 ALA 68.5 94.4 46.0 91 SER 29.5 35.2 80.3 92 ARG 6.3 3.0 87.1 93 PRO 59.8 48.0 71.1 94 SER 47.4 56.7 67.1 95 GLU 54.6 39.4 67.7 96 VAL 116.9 98.4 29.6 97 CYS 99.1 99.9 45.6 98 VAL 106.0 89.2 41.1 99 VAL 87.4 73.5 54.1 100 ASP 76.4 69.1 70.9 101 GLY 0.0 0.0 88.3 102 THR 53.0 49.6 73.8 103 ASP 0.0 0.0 85.0 104 MET 144.0 90.3 42.7 105 SER 32.4 38.7 69.9 106 LEU 97.0 65.6 52.5 107 ALA 2.1 2.9 87.3 108 ASP 61.2 55.3 60.5 109 PHE 166.8 100.0 34.2 110 HIS 137.4 91.5 41.1 111 ALA 72.6 100.0 37.4 112 GLY 34.8 100.0 36.1 113 ILE 143.5 100.0 30.0 114 PHE 166.8 100.0 36.8 115 LEU 106.9 72.3 60.1 116 LYS 109.4 63.1 62.6 117 GLY 1.2 3.4 74.9 118 GLN 47.8 32.2 75.5 119 GLU 17.5 12.6 81.0 120 HIS 103.3 68.8 71.5 121 ALA 70.4 97.0 39.5 122 VAL 117.4 98.8 44.9 123 PHE 166.8 100.0 32.2 124 ALA 72.6 100.0 35.8 125 CYS 99.2 100.0 32.9 126 VAL 87.8 73.9 55.4 127 THR 105.9 99.0 47.5 128 SER 27.6 33.0 80.5 129 ASN 30.0 24.8 82.6 130 GLY 2.4 6.8 85.1 131 TRP 183.2 89.4 46.0 132 TYR 154.4 85.3 53.3 133 ALA 72.6 100.0 41.5 134 ILE 143.4 100.0 39.8 135 ASP 93.7 84.8 57.1 136 ASP 93.3 84.4 63.4 137 GLU 52.0 37.5 71.5 138 ASP 25.6 23.2 72.6 139 PHE 161.4 96.8 45.0 140 TYR 126.7 70.0 52.7 141 PRO 47.7 38.3 69.8 142 TRP 158.9 77.5 46.1 143 THR 49.0 45.8 59.6 144 PRO 124.2 99.8 30.0 145 ASP 33.4 30.2 70.1 146 PRO 95.5 76.7 55.8 147 SER 9.7 11.7 87.4 148 ASP 84.7 76.6 70.5 149 VAL 116.6 98.1 36.1 150 LEU 111.9 75.7 41.5 151 VAL 118.8 100.0 31.1 152 PHE 160.3 96.1 28.8 153 VAL 112.2 94.4 38.1 154 PRO 97.1 78.0 60.2 155 TYR 103.9 57.4 67.8 156 ASP 0.0 0.0 94.1