Protein Data Bank File : 1hzta Title : ISOMERASE 26-JAN-01 1HZT Number of Amino Acid Residues : 153 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU HIS LEU ALA PHE SER SER TRP LEU PHE 10 ASN ALA LYS GLY GLN LEU LEU VAL THR ARG 20 ARG ALA LEU SER LYS LYS ALA TRP PRO GLY 30 VAL TRP THR ASN SER VAL CYS GLY HIS PRO 40 GLN LEU GLY GLU SER ASN GLU ASP ALA VAL 50 ILE ARG ARG CYS ARG TYR GLU LEU GLY VAL 60 GLU ILE THR PRO PRO GLU SER ILE TYR PRO 70 ASP PHE ARG TYR ARG ALA THR ASP PRO SER 80 GLY ILE VAL GLU ASN GLU VAL CYS PRO VAL 90 PHE ALA ALA ARG THR THR SER ALA LEU GLN 100 ILE ASN ASP ASP GLU VAL MET ASP TYR GLN 110 TRP CYS ASP LEU ALA ASP VAL LEU HIS GLY 120 ILE ASP ALA THR PRO TRP ALA PHE SER PRO 130 TRP MET VAL MET GLN ALA THR ASN ARG GLU 140 ALA ARG LYS ARG LEU SER ALA PHE THR GLN 150 LEU LYS LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 145.1 179.8 -54.5 177.6 2 HIS -127.4 151.2 179.8 -70.1 -62.3 3 LEU -92.1 135.4 -179.8 -63.3 177.5 4 ALA -152.7 -175.9 179.1 5 PHE -156.8 161.5 178.4 71.7 79.5 6 SER -138.8 146.1 179.4 -75.0 7 SER -138.3 144.3 178.7 -169.5 8 TRP -115.1 119.4 -178.7 -66.1 65.0 9 LEU -106.4 138.1 179.7 -58.0 179.4 10 PHE -125.9 152.8 177.0 -62.3 74.7 11 ASN -93.7 -178.5 -179.1 59.9 6.4 12 ALA -60.9 -32.2 -179.7 13 LYS -73.4 -10.8 178.9 -68.8 177.4 176.9 -61.5 14 GLY 95.2 5.8 178.7 15 GLN -78.5 146.3 179.3 -62.7 173.3 -77.4 16 LEU -95.0 139.9 178.4 170.8 68.3 17 LEU -95.3 115.4 177.6 174.7 61.1 18 VAL -107.3 143.6 -178.0 176.8 19 THR -128.4 159.9 178.5 59.9 20 ARG -116.9 122.6 -179.1 -167.0 179.8 174.2 -150.4 21 ARG -63.2 139.8 -179.6 -64.3 167.1 67.3 79.2 22 ALA -62.0 153.2 -179.5 23 LEU -64.4 -20.9 -179.2 -58.2 175.5 24 SER -86.3 -5.9 179.8 61.4 25 LYS -63.2 140.1 -179.4 -68.1 -58.9 -61.0 -179.0 26 LYS -63.7 -45.9 -179.7 -179.6 62.0 179.5 -59.7 27 ALA -113.0 140.3 179.9 28 TRP 47.5 49.7 179.6 -76.0 -80.7 29 PRO -68.9 145.7 178.8 32.2 -44.1 30 GLY 67.4 17.3 -179.1 31 VAL -100.0 139.0 177.8 170.9 32 TRP -76.8 137.9 -175.7 -80.2 103.0 33 THR -156.0 -176.7 178.6 -175.6 34 ASN -72.7 168.9 -176.1 56.8 100.6 35 SER -37.5 -62.8 -178.8 -46.4 36 VAL -150.7 161.5 179.3 -172.5 37 CYS -164.7 149.8 -179.7 67.5 38 GLY -174.6 -159.0 -173.6 39 HIS -130.8 136.4 179.9 -58.1 79.0 40 PRO -74.6 158.8 178.7 34.1 -44.2 41 GLN -89.6 153.8 -178.4 -71.1 167.6 167.3 42 LEU -23.1 -63.8 -179.3 -68.9 -179.7 43 GLY -111.6 36.0 -179.2 44 GLU -109.3 143.9 179.5 172.5 -172.1 49.2 45 SER -76.1 159.6 179.8 70.3 46 ASN -63.9 -39.6 -179.9 -70.7 147.2 47 GLU -60.3 -45.1 -179.9 -64.0 60.3 50.7 48 ASP -69.1 -29.8 178.9 -73.3 -28.5 49 ALA -67.3 -40.8 179.0 50 VAL -60.8 -49.4 179.9 170.8 51 ILE -57.7 -44.5 -179.9 -69.0 168.7 52 ARG -62.7 -45.8 -179.5 172.6 173.6 55.3 79.3 53 ARG -72.3 -31.9 177.6 -66.2 -53.6 -63.0 -174.5 54 CYS -63.9 -37.9 178.1 -77.3 55 ARG -70.9 -41.3 -178.4 -75.1 166.7 173.3 166.9 56 TYR -68.8 -47.5 -177.8 -173.1 76.3 57 GLU -87.4 -33.2 -176.3 -49.6 -160.3 -37.0 58 LEU -118.2 0.1 -179.8 -55.1 171.8 59 GLY 50.8 31.8 -176.9 60 VAL -117.0 150.7 177.4 74.7 61 GLU -96.1 150.6 -178.4 -67.4 -60.2 -50.4 62 ILE -138.7 165.4 177.5 61.4 177.5 63 THR -79.2 170.1 -179.7 53.3 64 PRO -55.7 121.8 -179.8 -30.7 44.4 65 PRO -59.7 131.9 178.9 -28.5 41.8 66 GLU -99.2 135.7 178.9 -179.4 -167.8 -54.9 67 SER -80.7 117.7 -178.6 170.4 68 ILE -115.0 -8.8 -179.5 67.8 172.1 69 TYR -162.6 72.5 -179.2 -163.5 -12.4 70 PRO -63.4 -33.5 -177.8 33.5 -43.7 71 ASP -91.9 14.5 180.0 55.1 -49.0 72 PHE -68.6 125.0 178.2 178.6 63.8 73 ARG -131.4 148.3 179.7 -60.6 -159.8 -163.9 72.1 74 TYR -156.1 147.1 177.7 86.3 87.8 75 ARG -132.0 104.5 178.3 -177.1 173.3 -177.9 176.7 76 ALA -126.1 155.8 -178.3 77 THR -123.1 120.3 -178.9 -57.5 78 ASP -71.0 168.0 -174.0 99.8 161.8 79 PRO -53.9 -14.9 178.7 -1.0 0.5 80 SER -118.0 25.8 176.7 56.0 81 GLY 89.3 -2.8 178.6 82 ILE -64.9 127.8 -178.0 -63.5 -70.9 83 VAL -110.5 139.7 -180.0 -173.7 84 GLU -129.9 129.7 178.8 -66.8 -167.8 -178.7 85 ASN -128.6 116.3 -178.0 -162.4 -44.5 86 GLU -149.4 158.0 175.8 -47.4 172.4 -55.7 87 VAL -94.2 121.8 -175.7 -179.1 88 CYS -133.2 77.9 179.6 -174.6 89 PRO -58.4 141.9 -177.8 25.7 -41.3 90 VAL -107.8 140.4 -179.5 -171.4 91 PHE -129.4 162.9 177.3 -58.1 80.3 92 ALA -136.8 145.8 178.6 93 ALA -158.9 168.8 178.7 94 ARG -107.8 142.8 177.6 -58.2 -102.5 -173.0 171.8 95 THR -79.0 149.7 179.9 54.9 96 THR -124.2 4.0 179.4 60.6 97 SER -147.1 173.1 -179.9 71.9 98 ALA -76.2 152.7 178.3 99 LEU -74.8 148.6 175.5 -59.0 175.1 100 GLN -138.5 96.6 -175.9 -166.4 -169.9 -37.3 101 ILE -68.0 133.2 177.0 -51.3 -60.4 102 ASN -98.7 103.0 -177.9 177.3 -14.5 103 ASP -68.8 -0.4 177.0 62.6 20.4 104 ASP -83.6 -13.6 -178.4 -72.7 -43.2 105 GLU -118.8 -38.4 -177.1 -57.5 -64.0 -41.5 106 VAL -122.7 125.6 -179.3 179.0 107 MET -100.9 -11.2 -179.4 65.2 -179.7 -63.9 108 ASP -169.6 163.8 177.9 -160.7 -6.3 109 TYR -162.6 164.6 -178.5 71.9 84.7 110 GLN -151.7 136.7 176.0 -175.5 89.0 -12.6 111 TRP -94.7 120.6 -178.0 -76.1 106.4 112 CYS -134.8 172.4 176.9 -23.2 113 ASP -86.6 132.2 -179.1 -65.2 -40.9 114 LEU -54.1 -42.0 -179.1 178.9 65.5 115 ALA -53.6 -41.2 179.9 116 ASP -70.3 -41.4 -180.0 -62.4 -37.0 117 VAL -62.5 -40.8 179.3 176.6 118 LEU -66.2 -35.9 178.9 -64.4 -179.8 119 HIS -66.6 -37.2 179.6 -70.3 -35.1 120 GLY -69.1 -42.4 179.1 121 ILE -63.0 -38.1 -179.6 -74.4 172.8 122 ASP -73.9 -34.0 -178.9 -65.7 -23.8 123 ALA -82.3 -44.6 -178.1 124 THR -133.5 67.6 -179.5 55.7 125 PRO -56.2 -27.4 180.0 26.6 -40.9 126 TRP -65.7 -14.5 -179.3 42.6 -96.4 127 ALA -87.6 3.3 -178.3 128 PHE -132.7 167.9 179.1 -51.6 -79.1 129 SER -64.2 144.8 -179.8 68.3 130 PRO -61.3 -34.7 -179.7 28.7 -41.6 131 TRP -71.7 -32.4 177.8 62.7 88.7 132 MET -62.5 -44.9 -179.7 171.8 -169.7 -143.4 133 VAL -64.4 -49.7 -179.6 176.6 134 MET -60.8 -39.8 179.7 -60.1 179.4 -84.4 135 GLN -68.1 -45.5 -179.2 -73.0 164.1 24.2 136 ALA -69.0 -19.2 -179.5 137 THR -89.7 -10.1 177.7 54.4 138 ASN -74.2 123.5 -177.9 174.4 -90.9 139 ARG -51.8 -48.5 -179.1 -163.7 -173.2 74.1 65.6 140 GLU -65.8 -43.5 179.9 -62.4 56.4 58.9 141 ALA -64.7 -41.2 -179.3 142 ARG -61.5 -37.6 179.1 -174.4 171.7 -70.7 -143.4 143 LYS -64.4 -37.4 179.3 -73.2 -177.9 60.3 59.0 144 ARG -69.6 -38.9 178.8 -61.6 -45.7 -54.3 167.1 145 LEU -61.3 -40.8 180.0 -64.2 177.3 146 SER -61.0 -37.7 -180.0 -178.9 147 ALA -62.7 -30.5 -180.0 148 PHE -79.3 1.1 179.5 -83.2 76.1 149 THR -89.1 -5.6 179.3 64.2 150 GLN -66.0 141.8 178.0 -173.6 -164.0 -38.0 151 LEU -69.8 128.5 179.4 -172.8 179.1 152 LYS -115.1 111.1 179.7 -80.2 -52.8 -51.2 174.9 153 LEU -95.3 -31.1 0.0 -60.8 172.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 63.812 23.699 -5.462 2 HIS 61.232 21.259 -4.084 3 LEU 57.454 21.016 -4.457 4 ALA 55.283 21.234 -1.348 5 PHE 51.985 22.546 -0.013 6 SER 50.500 23.942 3.180 7 SER 46.913 23.839 4.360 8 TRP 44.851 25.658 6.967 9 LEU 41.838 23.674 8.214 10 PHE 38.706 25.077 9.847 11 ASN 35.679 23.301 11.280 12 ALA 32.050 24.170 10.510 13 LYS 31.992 26.593 13.447 14 GLY 34.820 28.567 11.886 15 GLN 37.529 27.599 14.374 16 LEU 41.058 27.106 13.061 17 LEU 42.995 23.898 13.710 18 VAL 46.576 24.575 14.814 19 THR 48.931 21.620 15.278 20 ARG 52.229 20.857 16.951 21 ARG 54.763 18.778 15.014 22 ALA 55.908 15.571 16.705 23 LEU 59.302 15.478 18.433 24 SER 60.425 12.778 15.997 25 LYS 59.968 14.967 12.915 26 LYS 63.171 15.555 10.958 27 ALA 62.551 19.263 10.433 28 TRP 61.056 21.705 12.944 29 PRO 60.133 19.033 15.508 30 GLY 57.896 20.147 18.377 31 VAL 56.963 23.398 16.625 32 TRP 53.462 24.882 16.529 33 THR 52.223 25.417 12.978 34 ASN 49.247 25.512 10.628 35 SER 47.117 22.404 10.124 36 VAL 49.058 20.366 7.571 37 CYS 51.797 20.595 5.000 38 GLY 53.606 18.127 2.779 39 HIS 54.800 17.254 -0.536 40 PRO 52.887 16.025 -3.582 41 GLN 53.744 12.727 -5.251 42 LEU 55.255 12.607 -8.758 43 GLY 52.008 12.650 -10.739 44 GLU 49.620 13.858 -8.043 45 SER 47.799 17.201 -7.931 46 ASN 48.380 19.580 -5.021 47 GLU 44.701 19.300 -4.112 48 ASP 44.860 15.512 -3.880 49 ALA 48.068 15.733 -1.851 50 VAL 46.296 17.951 0.698 51 ILE 43.437 15.453 0.931 52 ARG 45.896 12.562 1.311 53 ARG 47.957 14.178 4.073 54 CYS 44.898 15.387 5.989 55 ARG 43.815 11.748 6.092 56 TYR 47.305 10.508 6.977 57 GLU 48.261 12.942 9.744 58 LEU 44.851 13.931 11.083 59 GLY 42.595 11.104 9.908 60 VAL 40.125 13.719 8.710 61 GLU 37.928 14.317 5.657 62 ILE 37.717 17.818 4.177 63 THR 35.781 20.008 1.738 64 PRO 37.382 20.868 -1.634 65 PRO 40.668 22.692 -0.879 66 GLU 40.640 26.348 -1.908 67 SER 43.840 27.913 -3.272 68 ILE 44.608 30.989 -1.143 69 TYR 48.308 31.737 -1.856 70 PRO 49.451 29.951 -5.054 71 ASP 52.712 31.855 -5.491 72 PHE 54.065 31.280 -1.990 73 ARG 57.739 30.322 -2.070 74 TYR 60.073 30.050 0.882 75 ARG 63.618 29.256 1.913 76 ALA 63.892 28.770 5.713 77 THR 66.511 27.040 7.925 78 ASP 65.541 24.907 10.974 79 PRO 67.349 25.040 14.428 80 SER 70.209 22.610 13.425 81 GLY 71.042 24.160 10.029 82 ILE 68.682 22.021 7.884 83 VAL 67.661 24.277 4.958 84 GLU 64.451 24.102 2.922 85 ASN 63.726 25.821 -0.367 86 GLU 60.307 25.070 -1.818 87 VAL 57.432 26.163 -4.021 88 CYS 54.598 25.923 -1.519 89 PRO 51.050 26.721 -2.686 90 VAL 48.721 27.308 0.265 91 PHE 45.187 25.968 0.701 92 ALA 42.267 26.269 3.115 93 ALA 39.425 23.813 3.688 94 ARG 36.785 22.766 6.201 95 THR 36.876 19.462 8.062 96 THR 33.846 17.212 7.544 97 SER 34.646 14.483 10.071 98 ALA 36.238 14.107 13.505 99 LEU 40.007 14.163 13.882 100 GLN 41.912 10.916 14.453 101 ILE 45.457 11.933 15.346 102 ASN 48.545 10.168 13.989 103 ASP 51.052 10.676 16.816 104 ASP 53.990 9.930 14.520 105 GLU 53.266 13.314 12.940 106 VAL 51.289 15.414 15.452 107 MET 51.986 15.683 19.195 108 ASP 49.319 18.255 20.134 109 TYR 46.655 20.463 18.554 110 GLN 44.197 23.205 19.370 111 TRP 40.947 24.493 17.908 112 CYS 41.173 28.277 18.178 113 ASP 39.700 31.515 16.982 114 LEU 41.659 32.831 14.003 115 ALA 41.715 36.350 15.435 116 ASP 43.687 35.116 18.439 117 VAL 46.105 33.069 16.334 118 LEU 46.813 36.092 14.159 119 HIS 47.440 38.224 17.256 120 GLY 49.884 35.610 18.514 121 ILE 51.648 35.367 15.168 122 ASP 52.018 39.143 15.024 123 ALA 53.269 39.463 18.616 124 THR 55.552 36.425 18.962 125 PRO 56.305 34.999 15.485 126 TRP 59.247 33.035 16.902 127 ALA 56.848 30.701 18.723 128 PHE 55.561 29.317 15.411 129 SER 56.834 27.707 12.210 130 PRO 58.256 30.285 9.808 131 TRP 55.943 29.279 6.954 132 MET 52.840 29.617 9.144 133 VAL 53.938 33.182 9.938 134 MET 54.872 34.139 6.374 135 GLN 51.606 32.734 5.020 136 ALA 49.413 34.406 7.646 137 THR 51.112 37.773 7.101 138 ASN 50.325 37.893 3.373 139 ARG 47.395 40.309 3.020 140 GLU 45.523 38.287 0.386 141 ALA 45.999 34.963 2.164 142 ARG 44.902 36.458 5.491 143 LYS 41.660 37.666 3.911 144 ARG 40.870 34.139 2.723 145 LEU 41.587 32.708 6.175 146 SER 39.166 35.267 7.591 147 ALA 36.487 34.074 5.161 148 PHE 36.741 30.538 6.581 149 THR 35.800 31.730 10.082 150 GLN 32.174 32.119 9.009 151 LEU 29.737 29.717 10.648 152 LYS 28.726 27.109 8.064 153 LEU 25.421 25.323 8.573 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 10 S/T T T T/S S S S S S S 20 S S S C T T T T C S 30 S S S S S S S S/S S S 40 S S C C H H H H H H 50 H H H H H H H H S S 60 S S S S/S S S S S S C 70 S S S S S S S S/T T T 80 T/S S S S S S S/S S S S 90 S S S S S S/S S S S S 100 S T T T T/S S S S/S S S 110 S S S/H H H H H H H H 120 H H H H C C C C H H 130 H H H H H H H H/H H H 140 H H H H H H H H H S 150 S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E e E E E E E E 10 t T T t E E E E E 20 E e T T t S S t T T 30 e E E E e E E E 40 t T T t h H H H H H 50 H H H H H H H H h 60 B S E E E E T 70 T e E E E E E e T T 80 t e E E E E E e e E 90 E E E E e S 100 t T T e E E E E E 110 E E h H H H H H H H 120 H H H h G G G B h H 130 H H H H H H H h H H 140 H H H H H H H h T t 150 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 49.1 33.2 79.0 2 HIS 27.6 18.4 82.0 3 LEU 40.2 27.2 69.6 4 ALA 68.8 94.8 52.6 5 PHE 166.8 100.0 40.4 6 SER 82.7 98.9 49.9 7 SER 83.6 100.0 36.2 8 TRP 204.7 99.8 31.1 9 LEU 147.8 100.0 31.9 10 PHE 166.8 100.0 40.6 11 ASN 94.3 78.0 58.8 12 ALA 23.6 32.5 74.5 13 LYS 33.9 19.6 81.2 14 GLY 34.7 99.6 74.2 15 GLN 92.7 62.4 66.9 16 LEU 147.8 100.0 33.2 17 LEU 147.8 100.0 28.4 18 VAL 110.4 93.0 36.6 19 THR 103.0 96.3 39.3 20 ARG 138.5 66.3 55.4 21 ARG 173.6 83.1 45.1 22 ALA 68.1 93.8 63.9 23 LEU 41.2 27.9 71.9 24 SER 16.0 19.1 81.1 25 LYS 123.3 71.1 78.8 26 LYS 23.3 13.4 80.0 27 ALA 64.0 88.1 58.9 28 TRP 191.0 93.2 34.2 29 PRO 85.9 69.0 69.6 30 GLY 32.2 92.5 55.4 31 VAL 86.6 72.9 54.7 32 TRP 134.6 65.7 58.8 33 THR 102.7 96.0 54.5 34 ASN 120.7 99.8 52.2 35 SER 83.6 100.0 47.6 36 VAL 115.6 97.3 42.4 37 CYS 75.2 75.8 64.3 38 GLY 26.1 74.9 56.1 39 HIS 59.2 39.4 70.4 40 PRO 118.3 95.1 59.7 41 GLN 48.9 32.9 81.0 42 LEU 0.0 0.0 92.1 43 GLY 0.0 0.0 82.0 44 GLU 115.1 83.0 62.8 45 SER 36.8 44.1 78.3 46 ASN 80.1 66.3 52.3 47 GLU 67.8 48.9 60.2 48 ASP 37.3 33.7 72.8 49 ALA 72.6 100.0 55.6 50 VAL 118.8 100.0 32.9 51 ILE 96.0 66.9 62.3 52 ARG 144.2 69.0 68.9 53 ARG 163.8 78.4 57.8 54 CYS 99.1 99.9 39.0 55 ARG 90.6 43.4 77.6 56 TYR 73.6 40.7 80.7 57 GLU 121.2 87.4 54.7 58 LEU 147.8 100.0 32.0 59 GLY 21.3 61.3 74.0 60 VAL 118.8 100.0 46.5 61 GLU 67.0 48.3 75.5 62 ILE 142.3 99.2 37.1 63 THR 61.7 57.7 51.4 64 PRO 15.1 12.1 75.1 65 PRO 119.6 96.1 38.5 66 GLU 83.5 60.3 67.5 67 SER 44.5 53.2 57.8 68 ILE 140.6 98.0 42.1 69 TYR 146.7 81.0 53.2 70 PRO 49.3 39.6 78.5 71 ASP 23.4 21.2 70.1 72 PHE 160.0 95.9 43.7 73 ARG 60.4 28.9 74.6 74 TYR 164.1 90.7 44.6 75 ARG 58.8 28.1 77.5 76 ALA 58.2 80.2 48.2 77 THR 56.0 52.4 63.1 78 ASP 106.6 96.5 50.3 79 PRO 39.1 31.4 76.0 80 SER 16.1 19.3 82.9 81 GLY 6.7 19.3 74.5 82 ILE 77.5 54.0 71.9 83 VAL 65.2 54.9 74.0 84 GLU 97.9 70.6 56.6 85 ASN 75.8 62.7 56.4 86 GLU 129.5 93.4 54.1 87 VAL 76.4 64.3 51.9 88 CYS 96.4 97.1 51.7 89 PRO 108.0 86.8 59.7 90 VAL 118.7 99.9 43.4 91 PHE 162.0 97.1 46.3 92 ALA 72.6 100.0 40.7 93 ALA 72.4 99.7 47.6 94 ARG 183.0 87.6 52.4 95 THR 100.7 94.2 39.0 96 THR 53.1 49.6 65.8 97 SER 44.1 52.7 72.7 98 ALA 0.0 0.0 87.9 99 LEU 139.6 94.5 39.7 100 GLN 10.2 6.9 85.8 101 ILE 109.5 76.3 52.1 102 ASN 87.4 72.3 65.6 103 ASP 14.8 13.4 87.1 104 ASP 20.7 18.8 88.6 105 GLU 120.3 86.8 59.6 106 VAL 114.3 96.2 52.1 107 MET 116.6 73.2 58.6 108 ASP 44.8 40.5 61.9 109 TYR 112.3 62.0 47.7 110 GLN 42.8 28.8 68.5 111 TRP 151.4 73.9 54.5 112 CYS 71.1 71.7 55.6 113 ASP 29.7 26.9 77.8 114 LEU 142.5 96.4 32.7 115 ALA 15.6 21.5 71.7 116 ASP 31.6 28.6 72.1 117 VAL 104.4 87.8 34.9 118 LEU 128.9 87.2 48.9 119 HIS 29.5 19.7 80.9 120 GLY 12.3 35.4 69.0 121 ILE 143.5 100.0 34.9 122 ASP 54.1 49.0 77.4 123 ALA 17.4 23.9 76.1 124 THR 59.7 55.9 53.8 125 PRO 72.4 58.2 64.7 126 TRP 29.6 14.4 75.3 127 ALA 39.2 54.0 61.2 128 PHE 133.8 80.2 51.2 129 SER 83.5 99.9 37.4 130 PRO 84.6 68.0 47.1 131 TRP 196.5 95.8 42.7 132 MET 159.4 100.0 37.1 133 VAL 96.3 81.1 46.5 134 MET 95.0 59.6 56.1 135 GLN 147.8 99.5 38.4 136 ALA 72.6 100.0 42.6 137 THR 58.7 55.0 71.2 138 ASN 83.4 69.0 69.6 139 ARG 53.9 25.8 76.4 140 GLU 54.8 39.5 82.1 141 ALA 72.1 99.3 53.4 142 ARG 146.0 69.9 58.8 143 LYS 55.5 32.0 80.5 144 ARG 108.4 51.9 69.7 145 LEU 147.2 99.6 28.7 146 SER 28.8 34.4 70.9 147 ALA 34.4 47.4 81.6 148 PHE 144.9 86.9 56.8 149 THR 70.0 65.5 65.0 150 GLN 34.8 23.4 88.5 151 LEU 59.6 40.4 69.1 152 LYS 76.2 43.9 80.7 153 LEU 12.8 8.7 74.2