Protein Data Bank File : 1g9za Title : HYDROLASE/DNA 28-NOV-00 1G9Z Number of Amino Acid Residues : 152 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASN THR LYS TYR ASN LYS GLU PHE LEU LEU 10 TYR LEU ALA GLY PHE VAL ASP GLY ASP GLY 20 SER ILE ILE ALA GLN ILE LYS PRO ASN GLN 30 SER TYR LYS PHE LYS HIS GLN LEU SER LEU 40 THR PHE GLN VAL THR GLN LYS THR GLN ARG 50 ARG TRP PHE LEU ASP LYS LEU VAL ASP GLU 60 ILE GLY VAL GLY TYR VAL ARG ASP ARG GLY 70 SER VAL SER ASP TYR ILE LEU SER GLU ILE 80 LYS PRO LEU HIS ASN PHE LEU THR GLN LEU 90 GLN PRO PHE LEU LYS LEU LYS GLN LYS GLN 100 ALA ASN LEU VAL LEU LYS ILE ILE GLU GLN 110 LEU PRO SER ALA LYS GLU SER PRO ASP LYS 120 PHE LEU GLU VAL CYS THR TRP VAL ASP GLN 130 ILE ALA ALA LEU ASN ASP SER LYS THR ARG 140 LYS THR THR SER GLU THR VAL ARG ALA VAL 150 LEU ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASN 0.0 143.4 -179.1 -79.3 -59.5 2 THR -72.1 138.5 179.5 171.8 3 LYS -100.1 122.0 -179.1 -118.5 -65.6 -176.7 -178.6 4 TYR -92.5 146.4 178.9 -58.8 -71.4 5 ASN -61.4 140.0 -179.2 178.8 67.3 6 LYS -61.9 -41.9 -179.5 -177.4 -175.7 178.0 -172.0 7 GLU -68.4 -33.1 177.7 -52.8 -163.6 -42.9 8 PHE -63.9 -46.7 179.8 166.1 66.3 9 LEU -65.3 -37.0 179.5 -65.9 169.0 10 LEU -61.6 -50.4 179.6 -80.7 166.9 11 TYR -63.2 -47.9 -179.2 170.3 -82.4 12 LEU -61.8 -39.8 179.2 -173.5 55.7 13 ALA -57.4 -42.6 179.4 14 GLY -65.5 -42.6 -179.5 15 PHE -65.8 -40.7 178.7 -160.8 96.0 16 VAL -63.8 -45.5 178.9 169.1 17 ASP -57.8 -31.5 179.7 -86.6 -19.8 18 GLY -82.3 -58.0 -176.7 19 ASP -116.7 4.5 179.8 -76.8 -22.1 20 GLY -94.0 179.1 -179.4 21 SER -153.9 134.5 178.1 -168.7 22 ILE -112.5 108.7 -174.5 -64.2 -176.4 23 ILE -114.9 143.6 178.2 -46.7 159.2 24 ALA -132.0 132.2 -179.8 25 GLN -141.4 154.2 178.1 -54.7 177.8 70.3 26 ILE -117.5 106.2 -177.7 -61.8 166.7 27 LYS -101.2 122.9 179.5 -56.2 177.1 177.4 -64.2 28 PRO -66.6 124.1 -179.5 26.6 -40.3 29 ASN -155.3 117.3 -178.1 -169.3 -50.8 30 GLN -63.4 -20.9 -178.7 -62.2 -64.8 71.2 31 SER -75.4 -5.4 179.9 69.1 32 TYR -94.9 151.2 -179.7 -66.8 67.1 33 LYS -50.9 -52.4 -179.5 -173.2 177.0 -176.3 -179.8 34 PHE -93.4 22.2 178.1 -63.0 -55.9 35 LYS 60.5 10.7 179.2 -50.3 -56.7 177.0 -179.4 36 HIS -144.0 146.8 178.0 -61.5 71.9 37 GLN -105.1 137.3 176.6 166.7 -177.8 26.6 38 LEU -91.9 111.7 -178.8 -67.7 -174.9 39 SER -112.5 131.4 179.3 172.1 40 LEU -119.6 133.9 -179.6 -64.2 -57.7 41 THR -140.8 135.3 173.5 -55.4 42 PHE -113.3 129.3 -179.7 163.0 77.3 43 GLN -144.9 158.2 176.4 68.0 168.6 -147.3 44 VAL -133.6 124.2 -178.7 179.1 45 THR -101.4 143.4 177.6 -57.2 46 GLN -160.3 150.0 179.2 -159.5 71.8 -172.9 47 LYS -53.9 138.0 -177.7 -171.9 172.1 178.1 175.8 48 THR -56.7 -30.5 179.3 -59.3 49 GLN -62.7 -17.9 178.3 74.1 178.1 -172.6 50 ARG -107.8 23.6 -179.9 -71.4 -167.4 -78.6 -76.6 51 ARG -57.3 -27.3 -179.7 176.8 172.1 168.6 150.6 52 TRP -54.2 -37.7 179.9 65.1 -89.9 53 PHE -62.4 -40.0 179.3 175.9 -82.7 54 LEU -70.7 -39.8 179.1 -93.6 20.7 55 ASP -61.3 -43.1 178.7 -72.1 -22.0 56 LYS -60.5 -34.0 179.5 165.5 164.4 -70.8 -61.3 57 LEU -65.1 -36.0 179.2 -81.0 -175.9 58 VAL -61.0 -41.1 -179.5 173.5 59 ASP -71.3 -43.0 -179.4 178.9 55.9 60 GLU -70.9 -40.6 179.0 -69.2 167.2 164.6 61 ILE -78.9 -29.6 177.5 -64.8 178.5 62 GLY 85.6 -1.1 -179.8 63 VAL -149.9 168.9 179.8 54.0 64 GLY 93.6 -177.4 -179.6 65 TYR -156.9 171.8 -180.0 60.8 95.5 66 VAL -115.3 132.3 178.7 177.8 67 ARG -115.8 152.8 -179.1 68.3 91.4 166.6 -121.1 68 ASP -106.8 134.5 176.9 179.4 106.1 69 ARG -139.5 58.2 179.2 53.1 159.7 157.9 149.2 70 GLY 87.9 -125.4 -179.1 71 SER -78.3 -1.2 -179.4 68.5 72 VAL -130.0 148.2 177.8 172.2 73 SER -129.3 164.6 -180.0 -65.2 74 ASP -142.2 137.0 173.2 -49.9 86.0 75 TYR -90.7 128.4 -179.4 163.4 76.4 76 ILE -123.2 137.0 178.3 -56.8 -75.5 77 LEU -136.2 112.0 180.0 175.1 56.2 78 SER -121.6 -20.3 178.9 -69.0 79 GLU -50.7 114.6 -176.5 -65.6 -165.8 65.1 80 ILE -52.8 -45.5 -179.0 -168.4 -179.3 81 LYS -66.4 -51.7 179.8 -167.1 67.7 -75.4 177.1 82 PRO -67.0 -29.3 179.8 -25.9 40.9 83 LEU -64.3 -46.6 179.4 177.0 57.6 84 HIS -59.6 -47.1 179.7 -168.6 -78.4 85 ASN -60.3 -45.8 -178.9 174.9 55.4 86 PHE -63.0 -56.3 -179.3 174.1 67.4 87 LEU -59.7 -31.3 179.5 -71.2 -176.0 88 THR -62.1 -39.8 -179.8 -69.5 89 GLN -83.3 -25.4 -178.6 -64.1 -179.7 59.6 90 LEU -81.6 -45.5 -178.2 -175.6 68.8 91 GLN -36.4 -42.8 -179.8 175.2 -79.7 -57.7 92 PRO -67.3 -13.9 -179.2 26.0 -40.4 93 PHE -105.5 -5.2 178.9 -52.8 -53.5 94 LEU -77.1 147.1 179.9 -69.1 170.2 95 LYS -119.7 -33.5 -179.5 -59.8 -174.3 -175.3 -174.9 96 LEU -101.4 -28.1 -178.1 -57.4 -173.6 97 LYS -121.7 22.3 179.9 -55.9 164.2 -171.4 -67.4 98 GLN -64.5 -39.4 -179.9 -167.8 -178.9 69.1 99 LYS -65.8 -43.7 179.7 -69.1 -179.7 179.5 179.2 100 GLN -58.2 -43.4 -179.7 -70.2 91.8 139.3 101 ALA -60.1 -49.1 -179.5 102 ASN -62.6 -33.1 178.5 -73.2 147.7 103 LEU -70.5 -35.2 178.4 -75.3 173.8 104 VAL -66.0 -44.8 179.8 166.1 105 LEU -60.6 -34.9 180.0 -81.0 45.2 106 LYS -70.0 -43.0 179.4 -179.5 178.9 179.8 -176.7 107 ILE -63.3 -47.9 179.7 -69.3 177.4 108 ILE -55.9 -44.6 -179.3 -71.2 -179.7 109 GLU -67.3 -25.1 -179.4 -59.0 172.4 -48.4 110 GLN -101.7 6.5 179.8 -60.3 -54.9 -52.6 111 LEU -62.8 -44.2 -179.9 -75.4 -170.5 112 PRO -61.0 -39.6 180.0 30.7 -43.8 113 SER -79.3 -18.1 179.8 66.6 114 ALA -81.3 -18.8 -179.9 115 LYS -72.7 -3.9 179.9 -126.7 71.5 69.2 64.0 116 GLU -109.8 -95.9 -179.4 -86.5 74.4 61.9 117 SER -46.6 112.8 179.8 -177.7 118 PRO -57.8 -20.2 179.4 -30.9 43.6 119 ASP -89.4 -15.3 178.5 -72.2 56.7 120 LYS -85.3 -25.6 179.1 175.4 59.5 175.3 -177.9 121 PHE -72.1 -40.3 179.3 -172.3 73.2 122 LEU -69.0 -32.4 179.6 -85.4 -175.0 123 GLU -70.9 -29.3 179.1 -174.3 -172.2 -179.7 124 VAL -77.7 -37.3 178.7 -179.2 125 CYS -64.7 -10.1 178.5 -76.6 126 THR -81.6 -42.9 178.7 -70.9 127 TRP -57.6 -34.7 -179.6 -57.5 166.8 128 VAL -69.6 -35.0 178.9 -177.8 129 ASP -64.0 -41.8 -179.2 -69.6 -50.4 130 GLN -62.3 -42.7 179.9 -69.1 -175.2 59.4 131 ILE -63.2 -48.4 179.9 -65.8 174.6 132 ALA -59.5 -34.8 -179.9 133 ALA -67.0 -34.3 179.5 134 LEU -76.2 -26.9 179.5 -66.3 168.6 135 ASN -85.7 171.3 178.6 -63.6 -29.4 136 ASP -85.9 61.4 -179.1 -65.3 -37.8 137 SER -70.5 127.7 -179.2 177.4 138 LYS -133.5 -12.6 -178.9 -59.8 -177.1 -67.0 -71.8 139 THR -130.2 21.4 -179.3 65.8 140 ARG -64.3 133.6 -179.6 -169.8 174.6 163.2 75.3 141 LYS -118.8 -50.0 -179.4 -58.1 -61.5 179.5 -176.2 142 THR -91.2 113.7 -179.9 -61.3 143 THR -120.6 175.2 179.8 179.4 144 SER -57.9 -37.9 179.3 68.3 145 GLU -56.2 -32.5 179.0 -173.4 55.7 42.9 146 THR -69.6 -48.3 179.7 -61.8 147 VAL -59.0 -22.1 -179.9 178.2 148 ARG -62.9 8.1 178.5 -160.9 166.1 -59.4 -176.5 149 ALA -89.0 17.2 178.2 150 VAL -80.0 -5.2 179.8 170.5 151 LEU -73.7 110.1 -180.0 -51.8 178.5 152 ASP -127.3 4.9 0.0 -60.9 -54.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASN -17.966 56.821 48.227 2 THR -17.589 53.157 49.187 3 LYS -19.353 51.829 52.301 4 TYR -17.262 49.454 54.411 5 ASN -18.594 46.508 56.406 6 LYS -18.923 47.196 60.157 7 GLU -17.110 44.037 61.264 8 PHE -14.290 44.841 58.833 9 LEU -13.953 48.289 60.395 10 LEU -14.114 46.846 63.916 11 TYR -11.229 44.468 63.270 12 LEU -9.200 47.030 61.311 13 ALA -9.639 49.728 63.966 14 GLY -8.065 47.362 66.461 15 PHE -5.228 46.490 64.074 16 VAL -4.687 50.169 63.300 17 ASP -4.583 51.091 66.975 18 GLY -1.872 48.462 67.294 19 ASP 0.317 48.664 64.171 20 GLY -1.168 51.496 62.138 21 SER -0.364 55.180 62.089 22 ILE -2.416 58.306 61.375 23 ILE 0.079 60.914 60.216 24 ALA 0.032 64.635 59.429 25 GLN 3.088 66.431 58.084 26 ILE 4.221 69.833 56.891 27 LYS 6.799 69.131 54.198 28 PRO 9.190 71.864 53.051 29 ASN 8.853 72.208 49.292 30 GLN 9.642 75.421 47.415 31 SER 7.084 74.814 44.656 32 TYR 4.206 75.539 47.048 33 LYS 2.761 78.988 47.717 34 PHE 3.601 78.842 51.418 35 LYS 6.788 76.853 50.788 36 HIS 5.268 73.824 52.538 37 GLN 2.981 70.918 51.663 38 LEU 0.271 69.696 54.012 39 SER 0.620 65.916 53.779 40 LEU -1.824 63.413 55.323 41 THR -1.170 59.694 55.567 42 PHE -2.956 56.614 56.860 43 GLN -0.705 53.578 57.007 44 VAL -0.426 50.057 58.375 45 THR 3.044 48.575 58.829 46 GLN 3.892 44.878 58.761 47 LYS 6.839 42.527 58.279 48 THR 7.248 41.853 54.564 49 GLN 6.749 38.103 54.981 50 ARG 3.195 39.130 55.906 51 ARG 2.780 41.510 52.958 52 TRP -0.209 39.455 51.803 53 PHE -2.180 40.998 54.662 54 LEU -1.325 44.500 53.373 55 ASP -2.128 43.546 49.767 56 LYS -5.517 42.318 50.928 57 LEU -6.114 45.729 52.560 58 VAL -5.640 47.401 49.212 59 ASP -8.429 45.206 47.838 60 GLU -10.717 45.591 50.850 61 ILE -10.275 49.348 51.255 62 GLY -10.311 49.652 47.468 63 VAL -7.709 52.396 47.266 64 GLY -4.105 52.888 48.374 65 TYR -1.012 50.783 47.783 66 VAL 1.721 48.801 49.498 67 ARG 5.325 49.887 49.522 68 ASP 8.392 47.841 50.341 69 ARG 11.201 49.063 52.591 70 GLY 13.317 45.992 53.227 71 SER 12.205 43.556 55.901 72 VAL 9.133 45.726 56.442 73 SER 6.267 46.891 54.190 74 ASP 3.480 49.494 54.517 75 TYR -0.033 49.971 53.254 76 ILE -0.434 53.724 52.482 77 LEU -3.468 55.803 51.788 78 SER -2.892 59.486 51.096 79 GLU -5.521 60.311 48.441 80 ILE -7.420 63.000 50.345 81 LYS -10.952 62.133 49.219 82 PRO -10.793 58.367 49.826 83 LEU -8.826 59.057 53.024 84 HIS -11.643 61.242 54.317 85 ASN -14.278 58.650 53.450 86 PHE -12.255 55.864 55.046 87 LEU -11.299 57.629 58.277 88 THR -14.877 58.854 58.661 89 GLN -16.048 55.244 58.866 90 LEU -13.089 53.923 60.871 91 GLN -12.941 56.699 63.471 92 PRO -15.894 55.575 65.604 93 PHE -14.163 52.277 66.405 94 LEU -10.683 53.611 67.181 95 LYS -9.588 53.802 70.830 96 LEU -5.963 54.951 70.713 97 LYS -5.921 57.004 67.527 98 GLN -9.505 58.257 67.375 99 LYS -8.368 61.809 68.147 100 GLN -5.657 61.730 65.491 101 ALA -8.228 60.565 62.933 102 ASN -10.687 63.327 63.767 103 LEU -7.942 65.938 63.503 104 VAL -7.089 64.598 60.049 105 LEU -10.721 64.839 58.912 106 LYS -10.697 68.389 60.259 107 ILE -7.480 69.257 58.414 108 ILE -8.827 67.780 55.174 109 GLU -12.047 69.791 55.440 110 GLN -10.090 73.013 55.975 111 LEU -7.487 72.512 53.232 112 PRO -9.303 74.605 50.593 113 SER -9.644 77.573 52.954 114 ALA -6.068 77.050 54.142 115 LYS -4.789 77.562 50.598 116 GLU -5.580 81.271 51.067 117 SER -5.151 83.111 54.369 118 PRO -1.464 82.637 55.333 119 ASP -2.742 82.729 58.911 120 LYS -5.272 80.016 58.112 121 PHE -2.390 77.872 56.889 122 LEU -0.660 78.326 60.242 123 GLU -3.828 77.439 62.127 124 VAL -3.997 74.196 60.159 125 CYS -0.311 73.584 60.811 126 THR -1.562 73.765 64.398 127 TRP -3.903 70.808 63.896 128 VAL -0.751 69.030 62.720 129 ASP 1.133 69.883 65.912 130 GLN -1.713 68.267 67.841 131 ILE -1.619 65.035 65.850 132 ALA 2.130 64.689 66.295 133 ALA 1.690 65.335 70.023 134 LEU -0.789 62.452 70.258 135 ASN 1.495 60.021 68.374 136 ASP 4.771 58.578 69.686 137 SER 6.661 61.264 67.751 138 LYS 10.451 61.129 68.122 139 THR 12.051 62.510 64.934 140 ARG 9.799 65.399 63.940 141 LYS 11.755 68.286 62.405 142 THR 9.334 70.534 60.528 143 THR 6.662 72.114 62.744 144 SER 4.288 75.080 62.469 145 GLU 6.915 77.143 64.290 146 THR 9.071 76.327 61.279 147 VAL 6.318 77.444 58.903 148 ARG 6.295 80.673 60.905 149 ALA 9.085 81.568 58.464 150 VAL 6.272 82.939 56.317 151 LEU 7.341 86.232 57.896 152 ASP 8.789 88.333 55.064 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S/H H H H H H 10 H H H H H H H H H/S S 20 S S S S S S/S S S S S 30 C T T T T/S S S S S S 40 S S S S/S S S S C C H 50 H H H 3 3/H H H H H H 60 H H/S S S S S S S S/T T 70 T T/S S S S S S S S/H H 80 H H H H H H H H H H 90 H C S S S S H H H H 100 H H H H H H H H H H 110 H/H H H H H 3 H H H H 120 H H H H H H H H H H 130 H H H H H S S S S/S S 140 S S H H H H H H 3 S 150 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H 10 H H H H H H H H H E 20 E E E E E E E E e T 30 T t T T e E E E E E 40 E E E E E E E e T h 50 H H H H H H H H H H 60 H h S E E E E E T 70 e E E E E E E h H 80 H H H H H H H H H H 90 h G G g S S h H H H 100 H H H H H H H H H h 110 H H H H h T h H H H 120 H H H H H H H H H H 130 H H H H h T t S 140 h H H H H h G G 150 g Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASN 47.6 39.4 78.2 2 THR 40.3 37.7 78.4 3 LYS 23.6 13.6 87.9 4 TYR 170.9 94.4 51.5 5 ASN 35.2 29.2 73.2 6 LYS 44.8 25.8 66.7 7 GLU 15.6 11.2 80.3 8 PHE 129.3 77.5 47.6 9 LEU 140.7 95.2 42.3 10 LEU 73.2 49.5 59.0 11 TYR 52.5 29.0 69.6 12 LEU 146.8 99.3 23.6 13 ALA 71.8 98.9 51.7 14 GLY 1.6 4.5 80.5 15 PHE 124.2 74.5 55.3 16 VAL 118.8 100.0 30.7 17 ASP 99.4 89.9 46.1 18 GLY 1.6 4.6 82.9 19 ASP 43.4 39.3 79.5 20 GLY 34.8 99.9 54.9 21 SER 55.0 65.8 60.6 22 ILE 143.0 99.6 33.9 23 ILE 105.0 73.1 68.4 24 ALA 72.6 100.0 34.4 25 GLN 87.1 58.6 66.7 26 ILE 143.5 100.0 36.9 27 LYS 95.1 54.8 71.6 28 PRO 52.6 42.3 74.4 29 ASN 57.6 47.7 75.4 30 GLN 20.5 13.8 83.0 31 SER 14.5 17.4 79.8 32 TYR 106.5 58.8 78.8 33 LYS 41.6 24.0 78.0 34 PHE 148.5 89.0 43.4 35 LYS 70.0 40.3 81.5 36 HIS 134.7 89.7 41.4 37 GLN 87.9 59.2 61.0 38 LEU 138.9 94.0 31.3 39 SER 69.3 82.9 60.2 40 LEU 139.6 94.5 42.0 41 THR 93.2 87.2 60.6 42 PHE 166.6 99.9 24.5 43 GLN 121.1 81.5 51.0 44 VAL 118.8 100.0 30.4 45 THR 74.7 69.9 68.0 46 GLN 126.7 85.2 51.3 47 LYS 77.3 44.6 77.3 48 THR 70.8 66.3 73.1 49 GLN 46.2 31.1 77.0 50 ARG 107.3 51.4 71.6 51 ARG 125.6 60.1 69.3 52 TRP 56.5 27.6 69.6 53 PHE 136.4 81.8 37.0 54 LEU 147.8 100.0 39.1 55 ASP 55.3 50.1 66.4 56 LYS 72.5 41.8 74.4 57 LEU 142.7 96.5 32.2 58 VAL 76.8 64.6 65.8 59 ASP 13.0 11.8 80.6 60 GLU 82.3 59.4 60.6 61 ILE 143.5 100.0 34.3 62 GLY 9.3 26.7 80.9 63 VAL 93.6 78.8 55.4 64 GLY 30.2 86.7 49.6 65 TYR 55.7 30.7 66.2 66 VAL 117.6 99.0 50.6 67 ARG 102.2 48.9 67.6 68 ASP 53.2 48.1 75.7 69 ARG 106.1 50.8 76.7 70 GLY 0.0 0.0 87.1 71 SER 6.4 7.6 76.3 72 VAL 76.2 64.1 73.4 73 SER 83.6 100.0 49.7 74 ASP 110.5 100.0 54.0 75 TYR 181.0 100.0 33.1 76 ILE 125.8 87.7 54.8 77 LEU 147.3 99.7 37.2 78 SER 44.3 53.0 67.7 79 GLU 37.4 27.0 68.6 80 ILE 73.4 51.1 53.5 81 LYS 57.4 33.1 72.8 82 PRO 90.3 72.5 54.6 83 LEU 147.2 99.6 36.0 84 HIS 115.7 77.0 57.6 85 ASN 103.3 85.4 66.2 86 PHE 166.8 100.0 27.6 87 LEU 147.1 99.5 28.0 88 THR 48.9 45.7 64.9 89 GLN 128.8 86.7 57.9 90 LEU 147.8 100.0 28.3 91 GLN 112.6 75.8 58.3 92 PRO 74.4 59.8 73.5 93 PHE 124.3 74.5 51.9 94 LEU 147.8 100.0 43.3 95 LYS 15.0 8.7 87.1 96 LEU 38.3 25.9 78.8 97 LYS 138.8 80.0 63.2 98 GLN 88.3 59.4 71.0 99 LYS 30.2 17.4 76.5 100 GLN 143.5 96.5 49.0 101 ALA 72.6 100.0 38.1 102 ASN 65.9 54.5 65.0 103 LEU 126.7 85.7 52.2 104 VAL 117.6 99.0 31.5 105 LEU 128.1 86.7 54.8 106 LYS 91.0 52.5 63.9 107 ILE 143.2 99.8 30.1 108 ILE 137.9 96.1 33.8 109 GLU 53.6 38.7 73.9 110 GLN 87.6 59.0 72.5 111 LEU 125.4 84.8 37.1 112 PRO 44.2 35.5 77.8 113 SER 38.4 46.0 69.5 114 ALA 72.3 99.6 48.9 115 LYS 55.1 31.8 75.2 116 GLU 36.9 26.6 81.8 117 SER 32.9 39.4 59.6 118 PRO 64.8 52.1 63.5 119 ASP 10.8 9.8 79.5 120 LYS 127.6 73.6 66.5 121 PHE 158.9 95.2 37.6 122 LEU 107.3 72.6 57.3 123 GLU 65.0 46.9 68.0 124 VAL 118.8 100.0 39.0 125 CYS 99.2 100.0 30.3 126 THR 55.5 51.9 68.3 127 TRP 176.6 86.2 50.6 128 VAL 117.1 98.6 47.8 129 ASP 72.4 65.5 77.9 130 GLN 74.8 50.4 56.9 131 ILE 143.0 99.7 44.5 132 ALA 62.0 85.3 68.2 133 ALA 13.1 18.1 81.3 134 LEU 93.9 63.5 63.8 135 ASN 94.9 78.5 66.9 136 ASP 0.0 0.0 87.7 137 SER 54.3 64.9 62.5 138 LYS 28.1 16.2 83.7 139 THR 8.0 7.5 83.3 140 ARG 153.9 73.7 68.3 141 LYS 19.3 11.1 86.5 142 THR 86.3 80.7 53.1 143 THR 67.5 63.1 71.8 144 SER 72.6 86.8 61.8 145 GLU 48.6 35.1 77.6 146 THR 51.6 48.2 73.8 147 VAL 118.8 100.0 33.5 148 ARG 95.5 45.7 71.9 149 ALA 13.5 18.6 82.8 150 VAL 82.6 69.5 57.1 151 LEU 26.1 17.7 80.5 152 ASP 10.5 9.5 89.3