Protein Data Bank File : 1a6m Title : OXYGEN TRANSPORT 26-FEB-98 1A6M Number of Amino Acid Residues : 151 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 VAL LEU SER GLU GLY GLU TRP GLN LEU VAL 10 LEU HIS VAL TRP ALA LYS VAL GLU ALA ASP 20 VAL ALA GLY HIS GLY GLN ASP ILE LEU ILE 30 ARG LEU PHE LYS SER HIS PRO GLU THR LEU 40 GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS 50 THR GLU ALA GLU MET LYS ALA SER GLU ASP 60 LEU LYS LYS HIS GLY VAL THR VAL LEU THR 70 ALA LEU GLY ALA ILE LEU LYS LYS LYS GLY 80 HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA 90 GLN SER HIS ALA THR LYS HIS LYS ILE PRO 100 ILE LYS TYR LEU GLU PHE ILE SER GLU ALA 110 ILE ILE HIS VAL LEU HIS SER ARG HIS PRO 120 GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA 130 MET ASN LYS ALA LEU GLU LEU PHE ARG LYS 140 ASP ILE ALA ALA LYS TYR LYS GLU LEU GLY 150 TYR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 VAL 0.0 132.3 177.4 158.8 2 LEU -76.0 145.3 172.6 -77.9 70.1 3 SER -77.5 166.8 173.5 65.7 4 GLU -59.4 -39.4 -179.6 -77.4 -68.7 -11.2 5 GLY -64.1 -39.1 178.9 6 GLU -66.2 -44.2 178.3 -71.6 161.5 -19.4 7 TRP -61.8 -37.1 178.3 -76.6 120.4 8 GLN -59.8 -43.5 -180.0 178.6 -77.0 -29.3 9 LEU -63.2 -42.0 179.6 -69.7 170.1 10 VAL -61.5 -50.2 -173.6 167.9 11 LEU -76.5 -22.6 176.7 -65.2 178.0 12 HIS -66.5 -45.6 177.1 -175.8 73.7 13 VAL -71.6 -34.7 179.5 71.2 14 TRP -62.9 -34.8 179.8 -163.0 -96.1 15 ALA -63.6 -28.4 175.3 16 LYS -70.5 -36.7 177.4 -54.5 -61.5 -177.3 172.6 17 VAL -62.6 -44.5 -176.8 168.4 18 GLU -65.7 -6.9 170.3 -79.2 -168.6 -19.2 19 ALA -76.1 -16.7 -179.7 20 ASP -155.0 67.3 -177.5 175.6 21.4 21 VAL -56.4 -48.3 -172.1 175.5 22 ALA -64.9 -41.0 179.8 23 GLY -65.8 -38.8 174.0 24 HIS -63.9 -42.3 -175.9 -74.2 80.0 25 GLY -62.1 -36.1 176.8 26 GLN -64.6 -50.6 -176.4 -73.3 165.0 -50.4 27 ASP -59.5 -43.8 -174.4 -67.0 -9.1 28 ILE -69.0 -48.1 179.5 -70.6 163.0 29 LEU -64.7 -38.5 179.0 -68.3 174.2 30 ILE -65.3 -41.7 176.8 -66.3 170.3 31 ARG -61.6 -45.0 177.6 169.4 68.5 -178.6 -156.8 32 LEU -54.7 -51.7 -174.3 178.4 67.3 33 PHE -67.7 -36.5 -179.1 -65.6 -22.2 34 LYS -74.4 -43.7 -177.2 -70.3 176.6 56.2 105.7 35 SER -75.0 -26.0 -176.1 -66.7 36 HIS -141.8 77.9 -172.2 -53.1 -81.7 37 PRO -59.4 -22.6 174.6 -25.6 36.0 38 GLU -57.8 -28.6 -178.8 63.9 -87.4 41.9 39 THR -69.6 -36.7 179.9 65.7 40 LEU -62.2 -37.0 -176.3 176.1 57.4 41 GLU -63.6 -21.5 175.9 -173.4 66.1 -12.1 42 LYS -71.3 -10.9 -175.6 -64.6 -75.1 179.4 172.7 43 PHE -108.4 99.0 170.3 -68.4 89.4 44 ASP -52.8 -34.4 -179.2 -74.4 -4.3 45 ARG -63.8 -30.5 -164.2 -87.2 157.5 89.0 -179.8 46 PHE -120.4 -12.3 -171.9 -55.0 -50.2 47 LYS -67.9 -10.7 171.1 75.5 -177.9 -165.1 171.7 48 HIS -69.9 -18.3 -177.9 69.7 -83.1 49 LEU -75.5 125.8 -170.2 -60.4 166.0 50 LYS -118.6 -14.0 179.3 -58.0 -48.5 172.4 -166.0 51 THR -133.5 159.3 174.7 73.0 52 GLU -61.0 -40.3 177.9 -179.9 167.1 3.8 53 ALA -61.5 -39.6 176.9 54 GLU -64.1 -41.4 177.4 -73.3 169.9 -0.2 55 MET -59.8 -46.0 -177.8 -64.8 171.5 -169.9 56 LYS -66.6 -25.2 -179.6 -85.9 167.9 -179.4 53.5 57 ALA -87.7 -4.5 -176.7 58 SER -87.5 113.4 178.5 170.8 59 GLU -67.5 -35.0 179.6 -168.9 65.7 9.5 60 ASP -62.4 -41.1 177.8 -161.5 46.6 61 LEU -62.5 -43.6 177.9 -176.6 60.8 62 LYS -58.9 -43.4 177.3 -171.4 173.5 -178.5 175.0 63 LYS -60.6 -45.7 179.5 -83.0 172.2 54.8 77.2 64 HIS -62.7 -38.5 176.8 -173.7 67.0 65 GLY -59.9 -35.7 173.3 66 VAL -63.3 -44.5 177.6 172.9 67 THR -56.0 -47.4 -177.5 -63.1 68 VAL -62.7 -50.4 -175.2 174.2 69 LEU -71.3 -30.4 175.6 -64.0 -171.6 70 THR -63.4 -44.9 178.5 -63.3 71 ALA -63.1 -46.1 -178.2 72 LEU -62.7 -42.3 -179.7 -178.6 58.8 73 GLY -60.8 -41.1 179.4 74 ALA -61.8 -38.9 175.6 75 ILE -65.6 -50.8 -176.0 -72.7 161.5 76 LEU -57.8 -40.6 -176.3 -64.1 173.6 77 LYS -68.8 -13.0 172.2 -69.6 169.6 -168.5 178.8 78 LYS -79.1 -9.7 175.2 -64.3 -54.3 -87.3 -117.4 79 LYS 49.5 50.7 176.6 -59.6 166.7 65.4 -172.8 80 GLY 94.4 -23.3 -178.0 81 HIS -89.2 57.9 -167.5 -60.7 -101.3 82 HIS -113.8 23.0 -176.2 53.0 -142.3 83 GLU -56.6 -45.2 -175.1 -21.0 61.8 13.9 84 ALA -67.2 -36.3 179.8 85 GLU -71.4 -34.1 -177.3 -62.9 66.2 24.9 86 LEU -77.0 -23.6 -176.2 -67.1 -173.0 87 LYS -53.2 -56.0 -176.8 -150.4 163.8 144.7 117.6 88 PRO -67.9 -34.6 -176.5 23.2 -35.4 89 LEU -65.9 -48.8 177.5 -176.9 72.3 90 ALA -62.2 -39.8 -179.5 91 GLN -61.9 -47.7 -177.5 -61.9 178.7 -32.0 92 SER -66.4 -42.3 -175.3 71.3 93 HIS -71.0 -32.7 175.1 -73.8 63.5 94 ALA -73.8 -51.1 -163.6 95 THR -97.1 -27.0 -178.4 74.7 96 LYS -105.6 -51.8 -175.4 -165.1 -149.3 -59.7 -120.4 97 HIS -86.0 -18.7 176.0 -50.3 -44.0 98 LYS 57.2 59.9 -178.5 -55.6 -143.8 166.9 18.2 99 ILE -103.1 114.1 173.6 -53.2 -52.5 100 PRO -62.6 150.5 173.3 -19.2 30.7 101 ILE -50.5 -37.4 179.5 -61.0 -62.9 102 LYS -55.6 -35.5 -179.3 -170.9 69.6 175.9 177.7 103 TYR -70.2 -27.7 170.8 -69.3 22.6 104 LEU -66.1 -34.6 172.1 -56.4 -178.1 105 GLU -61.3 -43.5 -179.7 -176.3 -175.0 0.8 106 PHE -62.2 -45.2 -179.3 -62.8 -26.1 107 ILE -66.7 -33.8 176.1 -158.1 173.9 108 SER -60.4 -41.9 175.9 -62.8 109 GLU -62.1 -39.6 178.1 -178.7 -70.8 -28.2 110 ALA -66.2 -40.1 175.4 111 ILE -58.0 -51.3 -178.1 -67.6 158.7 112 ILE -60.0 -43.3 -179.9 -66.6 167.1 113 HIS -61.1 -46.5 -178.8 -175.6 -79.4 114 VAL -66.5 -38.5 176.7 168.4 115 LEU -62.3 -38.5 179.3 -87.8 53.0 116 HIS -64.8 -42.7 179.4 -179.6 -98.3 117 SER -65.4 -41.4 -172.9 -64.5 118 ARG -84.5 -28.5 -167.7 -81.6 179.9 178.1 -111.2 119 HIS -135.9 50.9 -171.9 -49.6 -62.7 120 PRO -58.4 -39.8 -178.8 20.9 -34.4 121 GLY -65.6 -18.9 177.6 122 ASP -115.5 18.5 -175.2 -66.2 -69.6 123 PHE -146.0 44.0 168.8 -152.5 62.6 124 GLY -70.0 -175.4 -170.5 125 ALA -59.3 -39.7 -179.1 126 ASP -60.0 -47.8 179.7 52.5 -12.8 127 ALA -66.2 -37.3 176.1 128 GLN -61.1 -45.3 178.2 -73.6 166.6 42.0 129 GLY -61.6 -42.1 179.7 130 ALA -64.8 -42.7 177.5 131 MET -64.9 -38.9 174.7 -175.7 59.0 75.2 132 ASN -58.9 -44.0 179.7 -176.8 62.8 133 LYS -62.7 -40.7 179.6 -73.4 -175.1 172.4 -169.0 134 ALA -65.0 -40.8 -178.8 135 LEU -74.9 -30.9 170.7 -62.9 174.0 136 GLU -61.3 -45.0 179.6 -75.1 174.2 -19.0 137 LEU -60.4 -43.2 174.7 177.7 62.7 138 PHE -53.6 -52.0 -178.8 171.4 78.3 139 ARG -63.6 -42.8 -180.0 -69.4 -160.6 -56.0 -77.1 140 LYS -55.9 -48.6 -174.6 172.7 -172.0 171.1 178.6 141 ASP -72.7 -36.9 171.2 -69.9 -9.9 142 ILE -62.3 -44.2 -177.3 -65.9 -69.9 143 ALA -59.3 -36.7 179.2 144 ALA -65.3 -37.5 176.8 145 LYS -68.4 -42.0 174.2 -62.1 -69.5 151.1 -84.3 146 TYR -55.4 -45.4 -175.6 -86.3 21.6 147 LYS -62.5 -45.7 177.4 -177.0 -178.1 173.7 96.7 148 GLU -51.4 -46.4 -175.2 171.3 -173.1 -13.6 149 LEU -79.7 -5.9 179.3 -69.8 171.8 150 GLY 83.9 19.7 173.9 151 TYR -113.5 -174.9 0.0 -171.5 68.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 VAL -3.526 15.758 14.900 2 LEU -0.689 14.190 16.862 3 SER -1.487 12.495 20.143 4 GLU 0.324 13.366 23.335 5 GLY 2.196 10.084 23.022 6 GLU 3.317 10.981 19.508 7 TRP 4.502 14.431 20.597 8 GLN 6.475 12.812 23.418 9 LEU 8.296 10.604 20.915 10 VAL 9.019 13.628 18.670 11 LEU 10.311 15.860 21.464 12 HIS 12.315 13.068 23.090 13 VAL 14.421 12.632 19.976 14 TRP 14.480 16.388 19.359 15 ALA 16.044 16.935 22.798 16 LYS 18.881 14.660 21.558 17 VAL 19.269 16.901 18.449 18 GLU 19.557 19.981 20.499 19 ALA 22.712 18.601 22.014 20 ASP 24.546 19.223 18.625 21 VAL 22.306 21.550 16.647 22 ALA 25.042 22.516 14.185 23 GLY 26.217 19.010 13.295 24 HIS 22.696 17.908 12.638 25 GLY 22.074 20.968 10.503 26 GLN 25.151 20.160 8.384 27 ASP 24.193 16.513 7.883 28 ILE 20.655 17.495 6.980 29 LEU 21.463 20.254 4.476 30 ILE 24.167 18.158 2.856 31 ARG 21.812 15.200 2.466 32 LEU 19.184 17.558 1.045 33 PHE 21.599 19.119 -1.465 34 LYS 23.095 15.772 -2.549 35 SER 19.778 13.935 -2.820 36 HIS 17.931 16.835 -4.470 37 PRO 20.320 19.174 -6.246 38 GLU 17.529 21.507 -7.322 39 THR 17.322 22.578 -3.685 40 LEU 20.928 23.813 -3.598 41 GLU 20.239 26.028 -6.564 42 LYS 17.728 28.019 -4.446 43 PHE 20.573 29.297 -2.236 44 ASP 22.672 32.102 -3.726 45 ARG 24.855 31.645 -0.546 46 PHE 25.554 28.009 -1.284 47 LYS 25.246 27.211 -4.946 48 HIS 29.042 27.646 -5.398 49 LEU 29.487 24.404 -3.403 50 LYS 30.184 21.492 -5.800 51 THR 31.347 18.646 -3.495 52 GLU 30.343 17.167 -0.195 53 ALA 33.737 18.078 1.267 54 GLU 33.209 21.712 0.266 55 MET 29.783 21.655 1.892 56 LYS 31.173 20.193 5.111 57 ALA 33.926 22.865 5.171 58 SER 31.540 25.829 4.823 59 GLU 31.010 27.703 8.081 60 ASP 28.253 29.741 6.460 61 LEU 26.379 26.516 5.654 62 LYS 26.833 25.354 9.250 63 LYS 25.434 28.671 10.530 64 HIS 22.424 28.365 8.264 65 GLY 21.755 24.840 9.442 66 VAL 21.554 26.207 12.989 67 THR 19.055 28.848 11.830 68 VAL 16.871 26.185 10.188 69 LEU 16.889 23.715 13.063 70 THR 16.389 26.446 15.680 71 ALA 13.215 27.552 13.842 72 LEU 12.016 23.940 13.482 73 GLY 12.641 23.149 17.132 74 ALA 10.619 26.205 18.214 75 ILE 7.759 24.959 16.029 76 LEU 7.911 21.336 17.288 77 LYS 7.831 22.452 20.926 78 LYS 4.499 24.207 20.246 79 LYS 2.992 20.719 19.615 80 GLY 0.825 21.934 16.771 81 HIS -0.013 25.350 18.278 82 HIS 2.472 26.958 15.867 83 GLU 0.448 29.457 13.878 84 ALA 2.482 32.453 14.914 85 GLU 5.765 30.762 14.068 86 LEU 4.644 29.656 10.641 87 LYS 3.351 32.956 9.384 88 PRO 6.673 34.597 8.717 89 LEU 8.268 31.360 7.577 90 ALA 5.574 30.545 5.033 91 GLN 5.560 34.119 3.825 92 SER 9.306 34.227 3.218 93 HIS 9.514 30.786 1.728 94 ALA 6.586 31.332 -0.638 95 THR 7.192 34.892 -1.699 96 LYS 10.872 35.642 -1.314 97 HIS 12.824 32.363 -1.384 98 LYS 10.342 30.603 -3.756 99 ILE 10.462 27.191 -2.191 100 PRO 7.889 24.626 -3.368 101 ILE 6.116 22.468 -0.829 102 LYS 7.758 19.461 -2.429 103 TYR 11.138 20.809 -1.329 104 LEU 9.785 20.849 2.244 105 GLU 9.008 17.144 1.745 106 PHE 12.613 16.629 0.659 107 ILE 14.057 18.362 3.765 108 SER 11.687 16.345 5.936 109 GLU 13.115 13.145 4.470 110 ALA 16.627 14.390 5.174 111 ILE 15.709 15.246 8.776 112 ILE 14.260 11.788 9.333 113 HIS 17.275 10.093 7.795 114 VAL 19.775 12.019 9.928 115 LEU 17.789 11.469 13.102 116 HIS 17.791 7.733 12.402 117 SER 21.547 7.695 11.850 118 ARG 22.379 9.795 14.916 119 HIS 19.746 8.538 17.398 120 PRO 18.711 4.970 16.538 121 GLY 17.835 4.026 20.120 122 ASP 15.404 6.957 20.340 123 PHE 14.257 6.723 16.762 124 GLY 12.716 3.308 16.306 125 ALA 9.677 2.882 14.124 126 ASP 7.233 4.374 16.546 127 ALA 9.304 7.565 16.861 128 GLN 9.949 7.650 13.096 129 GLY 6.217 7.508 12.465 130 ALA 5.547 10.263 14.986 131 MET 8.242 12.520 13.528 132 ASN 6.863 11.899 10.049 133 LYS 3.438 12.982 11.347 134 ALA 4.895 16.149 12.919 135 LEU 6.692 17.097 9.700 136 GLU 3.559 16.304 7.698 137 LEU 1.616 18.702 9.956 138 PHE 4.269 21.352 9.382 139 ARG 3.948 20.902 5.620 140 LYS 0.136 20.841 5.720 141 ASP 0.017 24.122 7.544 142 ILE 2.632 25.820 5.403 143 ALA 0.809 24.596 2.290 144 ALA -2.420 26.238 3.433 145 LYS -0.593 29.539 3.774 146 TYR 1.041 29.069 0.360 147 LYS -2.455 28.490 -1.105 148 GLU -3.772 31.712 0.449 149 LEU -0.870 33.550 -1.190 150 GLY -1.223 31.968 -4.522 151 TYR 1.894 29.853 -4.417 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C H H H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H H H H H H/H H H H 40 H H 3/T T T T C S S S 50 S/H H H H H H H H/H H H 60 H H H H H H H H H H 70 H H H H H H H H H C 80 C H H H H H H/H H H H 90 H H H H H C S S S S/H 100 H H H H H H H H H H 110 H H H H H H H H H H/T 120 T T T H H H H H H H 130 H H H H H H H H H H 140 H H H H H H H H H H/S 150 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H H 10 H H H H H H H h T h 20 H H H H H H H H H H 30 H H H H H h H H H H 40 h T t T T T T T t 50 h H H H H H h h H H 60 H H H H H H H H H H 70 H H H H H H h T T T 80 t h H H H H H H H H 90 H H H H H h t h 100 H H H H H H H H H H 110 H H H H H H H H h G 120 G G g h H H H H H H 130 H H H H H H H H H H 140 H H H H H H H H H h 150 t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 VAL 2.0 1.7 87.7 2 LEU 143.8 97.3 41.7 3 SER 26.9 32.1 75.5 4 GLU 25.8 18.6 81.5 5 GLY 0.0 0.0 77.4 6 GLU 101.4 73.2 57.2 7 TRP 191.1 93.2 43.6 8 GLN 48.1 32.4 70.4 9 LEU 100.8 68.2 65.7 10 VAL 118.8 100.0 32.4 11 LEU 108.8 73.6 50.3 12 HIS 74.3 49.5 77.0 13 VAL 118.8 100.0 36.3 14 TRP 203.0 99.0 31.1 15 ALA 20.4 28.1 80.5 16 LYS 88.4 51.0 71.5 17 VAL 118.7 99.9 33.6 18 GLU 92.9 67.0 62.7 19 ALA 10.0 13.8 85.6 20 ASP 49.2 44.5 79.7 21 VAL 87.9 74.0 57.5 22 ALA 52.1 71.8 55.6 23 GLY 27.0 77.5 79.4 24 HIS 148.1 98.6 41.0 25 GLY 33.9 97.5 53.4 26 GLN 117.4 79.0 58.7 27 ASP 65.7 59.5 65.8 28 ILE 142.1 99.0 30.8 29 LEU 144.7 97.9 33.1 30 ILE 138.5 96.5 41.6 31 ARG 124.0 59.3 70.0 32 LEU 138.9 94.0 37.7 33 PHE 166.7 99.9 30.5 34 LYS 81.2 46.8 69.8 35 SER 53.2 63.6 70.5 36 HIS 109.7 73.1 52.5 37 PRO 42.9 34.5 85.2 38 GLU 69.3 50.0 58.8 39 THR 102.9 96.2 35.9 40 LEU 126.1 85.3 49.9 41 GLU 34.2 24.7 77.3 42 LYS 113.8 65.6 62.8 43 PHE 118.8 71.2 56.4 44 ASP 12.6 11.4 83.4 45 ARG 101.9 48.8 69.3 46 PHE 166.2 99.6 36.8 47 LYS 85.9 49.5 81.1 48 HIS 43.4 28.9 75.0 49 LEU 141.4 95.7 44.7 50 LYS 47.0 27.1 82.9 51 THR 40.7 38.0 72.5 52 GLU 86.0 62.1 59.4 53 ALA 6.3 8.7 77.7 54 GLU 65.4 47.2 66.5 55 MET 149.4 93.7 35.6 56 LYS 85.4 49.3 69.3 57 ALA 12.0 16.5 83.4 58 SER 66.6 79.7 59.7 59 GLU 31.6 22.8 75.0 60 ASP 58.0 52.5 66.5 61 LEU 147.6 99.9 31.4 62 LYS 103.0 59.4 73.8 63 LYS 50.1 28.9 81.5 64 HIS 118.0 78.6 49.8 65 GLY 34.5 99.0 53.8 66 VAL 63.9 53.8 66.8 67 THR 25.6 24.0 75.3 68 VAL 81.1 68.3 48.9 69 LEU 146.4 99.0 33.5 70 THR 26.3 24.6 73.4 71 ALA 32.4 44.6 66.9 72 LEU 139.0 94.0 26.3 73 GLY 34.1 97.9 59.9 74 ALA 25.0 34.5 70.6 75 ILE 138.6 96.6 34.3 76 LEU 145.0 98.1 29.0 77 LYS 83.0 47.9 69.7 78 LYS 86.3 49.8 77.8 79 LYS 108.4 62.5 62.9 80 GLY 26.4 75.8 53.4 81 HIS 26.0 17.3 83.0 82 HIS 144.5 96.2 45.6 83 GLU 29.4 21.2 79.2 84 ALA 6.2 8.6 82.5 85 GLU 94.2 67.9 57.0 86 LEU 143.6 97.2 39.4 87 LYS 54.6 31.5 75.4 88 PRO 47.2 37.9 78.6 89 LEU 105.1 71.1 52.0 90 ALA 72.6 99.9 41.2 91 GLN 73.5 49.5 59.4 92 SER 56.9 68.1 63.7 93 HIS 101.9 67.9 55.7 94 ALA 72.6 100.0 40.2 95 THR 42.9 40.2 65.3 96 LYS 43.4 25.0 82.2 97 HIS 81.1 54.0 60.9 98 LYS 69.5 40.1 80.6 99 ILE 123.9 86.3 39.9 100 PRO 79.6 63.9 58.9 101 ILE 99.6 69.4 50.3 102 LYS 62.5 36.0 67.1 103 TYR 146.6 81.0 38.9 104 LEU 130.2 88.1 37.5 105 GLU 73.3 52.9 73.0 106 PHE 138.3 82.9 45.7 107 ILE 119.3 83.2 36.3 108 SER 80.2 95.9 49.7 109 GLU 64.8 46.7 71.0 110 ALA 72.0 99.1 51.4 111 ILE 139.1 96.9 25.0 112 ILE 105.0 73.2 51.5 113 HIS 79.1 52.7 76.4 114 VAL 111.0 93.4 50.9 115 LEU 147.8 100.0 25.1 116 HIS 61.3 40.8 72.1 117 SER 34.1 40.8 74.0 118 ARG 141.8 67.9 64.3 119 HIS 122.5 81.6 45.9 120 PRO 49.6 39.8 82.1 121 GLY 0.0 0.0 82.8 122 ASP 68.0 61.5 62.4 123 PHE 166.8 100.0 37.4 124 GLY 6.2 17.9 87.1 125 ALA 5.7 7.8 84.1 126 ASP 23.8 21.6 69.6 127 ALA 70.2 96.7 54.1 128 GLN 92.3 62.1 58.0 129 GLY 1.8 5.2 77.2 130 ALA 71.9 99.0 45.7 131 MET 159.4 100.0 27.5 132 ASN 67.5 55.8 66.8 133 LYS 78.1 45.0 77.0 134 ALA 72.6 100.0 34.6 135 LEU 146.9 99.4 37.9 136 GLU 67.5 48.7 80.5 137 LEU 117.8 79.7 55.0 138 PHE 148.2 88.8 32.6 139 ARG 169.9 81.4 52.5 140 LYS 30.0 17.3 81.0 141 ASP 71.3 64.5 56.4 142 ILE 141.8 98.8 32.0 143 ALA 42.0 57.9 58.2 144 ALA 24.9 34.4 79.2 145 LYS 95.8 55.2 65.1 146 TYR 178.4 98.5 40.3 147 LYS 11.6 6.7 89.8 148 GLU 33.2 23.9 77.4 149 LEU 95.1 64.4 58.9 150 GLY 1.4 4.2 85.5 151 TYR 125.0 69.1 59.3