Protein Data Bank File : 1qtna Title : APOPTOSIS 28-JUN-99 1QTN Number of Amino Acid Residues : 152 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP LYS VAL TYR GLN MET LYS SER LYS PRO 10 ARG GLY TYR CYS LEU ILE ILE ASN ASN HIS 20 ASN PHE ALA LYS ALA ARG GLU LYS VAL PRO 30 LYS LEU HIS SER ILE ARG ASP ARG ASN GLY 40 THR HIS LEU ASP ALA GLY ALA LEU THR THR 50 THR PHE GLU GLU LEU HIS PHE GLU ILE LYS 60 PRO HIS ASP ASP CYS THR VAL GLU GLN ILE 70 TYR GLU ILE LEU LYS ILE TYR GLN LEU MET 80 ASP HIS SER ASN MET ASP CYS PHE ILE CYS 90 CYS ILE LEU SER HIS GLY ASP LYS GLY ILE 100 ILE TYR GLY THR ASP GLY GLN GLU ALA PRO 110 ILE TYR GLU LEU THR SER GLN PHE THR GLY 120 LEU LYS CYS PRO SER LEU ALA GLY LYS PRO 130 LYS VAL PHE PHE ILE GLN ALA CYS GLN GLY 140 ASP ASN TYR GLN LYS GLY ILE PRO VAL GLU 150 THR ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 135.0 171.6 -80.7 -13.7 2 LYS -73.7 143.0 -177.0 -47.4 169.4 -92.2 -72.5 3 VAL -131.1 135.0 175.5 -179.4 4 TYR -59.9 140.6 171.7 -68.9 -77.7 5 GLN -59.6 132.6 -177.2 176.4 172.0 -74.8 6 MET -151.3 67.8 -172.5 -164.4 66.8 56.5 7 LYS -124.0 -16.5 -176.4 -56.0 159.0 -175.9 140.8 8 SER -65.5 153.3 178.7 66.2 9 LYS -134.3 98.7 10.3 -70.5 -142.5 176.3 152.2 10 PRO -76.7 160.0 177.1 28.6 -38.5 11 ARG -62.2 -35.5 -174.2 -61.6 -60.1 -172.9 -132.5 12 GLY 164.3 -175.8 174.4 13 TYR -84.1 143.2 170.6 -61.3 -67.6 14 CYS -121.5 98.2 177.9 175.3 15 LEU -75.3 139.5 171.7 -52.6 -167.5 16 ILE -127.9 114.3 174.5 -56.9 172.1 17 ILE -99.2 109.2 -168.4 -58.1 175.2 18 ASN -114.9 97.1 -173.3 178.6 -143.1 19 ASN -96.8 115.7 179.9 -77.0 -4.1 20 HIS -108.3 -53.7 -165.9 172.7 -95.6 21 ASN -94.9 109.6 -177.5 -178.2 -4.6 22 PHE -106.8 26.4 175.3 -74.3 79.8 23 ALA -59.5 -40.8 -178.2 24 LYS -60.8 -40.9 177.7 -64.6 163.9 -171.4 -158.9 25 ALA -63.6 -45.2 179.1 26 ARG -60.1 -36.0 179.2 -69.9 -170.1 -70.3 -84.7 27 GLU -77.2 -34.0 -170.3 -164.2 -110.4 -89.0 28 LYS -102.6 -30.7 -170.7 -52.1 156.0 86.4 -129.2 29 VAL -112.2 104.8 -173.2 -174.9 30 PRO -46.3 -42.8 -176.7 -33.5 40.4 31 LYS -72.7 -15.8 -177.5 63.7 165.2 179.0 -159.2 32 LEU -101.6 24.9 178.3 -58.3 -178.5 33 HIS -51.9 -32.2 -177.8 56.1 84.3 34 SER -115.7 15.8 175.7 -71.7 35 ILE -60.4 133.3 -172.6 -159.1 173.8 36 ARG -93.1 155.1 170.3 -68.1 -178.6 -176.4 176.0 37 ASP -66.5 149.3 -171.4 -68.6 -12.9 38 ARG -92.9 61.7 -176.1 -60.9 -177.1 58.0 -96.2 39 ASN -53.7 133.4 -178.3 -68.3 -34.3 40 GLY 97.6 -13.0 -175.7 41 THR -58.0 -28.2 178.0 -172.5 42 HIS -63.5 -25.2 177.9 67.6 -75.9 43 LEU -67.0 -31.1 175.6 -62.8 178.3 44 ASP -75.5 -43.4 178.6 -79.9 -6.1 45 ALA -58.0 -42.9 -179.5 46 GLY -65.6 -44.1 178.7 47 ALA -60.7 -42.6 179.5 48 LEU -66.6 -37.6 178.3 -74.0 163.4 49 THR -62.0 -51.8 179.9 -63.5 50 THR -54.9 -49.2 -174.1 -69.7 51 THR -63.7 -50.1 -176.0 -60.6 52 PHE -80.0 -22.5 170.4 -73.9 -68.2 53 GLU -71.0 -39.1 174.9 -82.0 -167.2 -20.4 54 GLU -59.0 -31.8 178.0 -172.6 165.3 -76.3 55 LEU -90.1 7.8 170.7 -61.9 167.1 56 HIS 82.6 22.8 173.5 -50.6 -70.6 57 PHE -90.8 154.0 173.4 -73.3 77.1 58 GLU -95.4 111.8 -172.9 -171.0 176.0 -48.4 59 ILE -84.7 134.4 -177.3 -43.8 -53.9 60 LYS -129.6 89.8 -178.0 -58.7 -68.0 -160.1 -174.4 61 PRO -85.4 146.4 176.0 34.2 -37.7 62 HIS -144.2 119.8 -175.1 -64.8 -83.9 63 ASP -99.2 144.3 166.9 -66.8 -18.1 64 ASP 57.3 68.4 -174.1 -72.6 -27.9 65 CYS -104.8 126.8 169.4 -56.9 66 THR -74.2 168.8 178.3 64.1 67 VAL -58.2 -46.2 179.8 172.0 68 GLU -61.4 -37.7 177.3 -79.5 175.5 57.7 69 GLN -65.4 -39.1 174.0 -68.6 157.5 -171.4 70 ILE -59.9 -44.8 177.7 -65.9 174.4 71 TYR -63.4 -37.1 178.8 -68.7 -29.7 72 GLU -62.9 -45.9 180.0 -172.1 -152.1 0.0 73 ILE -61.3 -44.6 178.7 -66.0 158.2 74 LEU -62.0 -41.7 178.7 -60.7 -178.3 75 LYS -58.0 -42.8 175.8 -177.8 173.1 -168.2 -97.0 76 ILE -55.9 -46.4 177.3 -70.4 169.8 77 TYR -74.3 -29.5 174.5 -75.0 -82.7 78 GLN -61.6 -36.2 -176.2 166.4 -170.6 -92.0 79 LEU -86.1 -11.6 -178.6 -67.4 170.7 80 MET -70.7 158.2 177.3 -155.1 153.1 -58.6 81 ASP -90.8 109.3 -179.1 174.1 28.7 82 HIS -101.6 16.4 -174.7 -60.9 -105.8 83 SER -56.1 -33.3 -180.0 60.8 84 ASN -92.2 7.1 177.2 -58.7 -46.7 85 MET -104.3 155.2 177.2 -52.8 -54.3 -159.5 86 ASP -104.2 -11.4 -172.6 -76.6 -21.5 87 CYS -159.4 164.1 172.7 -171.3 88 PHE -141.5 134.0 177.5 173.7 69.2 89 ILE -125.0 140.2 173.2 -56.5 -179.0 90 CYS -133.5 120.5 179.0 179.0 91 CYS -110.3 128.7 177.9 -58.4 92 ILE -117.6 122.1 178.8 -54.0 -176.2 93 LEU -115.0 107.1 -173.8 -43.1 175.4 94 SER -164.0 178.9 163.7 -161.3 95 HIS -76.3 161.0 174.7 -77.0 -59.5 96 GLY -162.1 -179.0 179.6 97 ASP -148.8 -173.9 -173.4 -155.1 -24.0 98 LYS -54.7 115.7 176.9 -62.2 176.4 -118.2 -147.7 99 GLY 73.7 3.4 -171.1 100 ILE -134.2 162.6 162.9 69.4 95.5 101 ILE -121.0 152.1 178.6 63.0 92.1 102 TYR -96.2 142.0 161.9 -78.1 -65.3 103 GLY -76.8 168.9 175.9 104 THR -60.6 -20.7 177.3 52.5 105 ASP -84.6 -3.6 179.5 57.9 -17.6 106 GLY 81.6 3.8 170.3 107 GLN -77.4 157.0 -174.6 -66.5 -60.5 122.1 108 GLU -100.5 142.8 169.6 -57.5 -175.6 0.5 109 ALA -125.1 108.9 175.3 110 PRO -58.1 140.6 178.9 -26.6 37.5 111 ILE -57.1 -38.9 179.5 -63.2 158.0 112 TYR -64.0 -32.8 175.8 176.8 74.8 113 GLU -65.4 -23.3 177.1 -63.5 -62.5 -33.1 114 LEU -83.2 -50.6 -176.5 -54.2 171.9 115 THR -67.8 -34.6 -175.5 57.9 116 SER -65.1 -13.7 176.2 72.8 117 GLN -71.9 -7.7 -175.6 -53.6 -44.7 131.5 118 PHE -121.0 18.3 174.4 -59.4 -89.4 119 THR -61.7 166.3 -177.7 63.2 120 GLY -63.2 -32.3 178.1 121 LEU -70.8 -40.3 -173.5 -64.8 167.9 122 LYS -81.0 -26.6 177.9 -65.2 -145.8 167.3 -92.2 123 CYS -138.1 78.6 -174.5 -170.2 124 PRO -61.7 -28.7 177.7 -23.9 35.5 125 SER -72.1 -6.0 168.4 63.6 126 LEU -105.8 6.9 179.7 -69.8 169.0 127 ALA -61.1 132.0 -177.4 128 GLY 80.1 -2.1 -178.3 129 LYS -108.7 147.0 180.0 -54.3 175.1 -176.2 171.8 130 PRO -66.8 136.9 175.9 20.2 -27.1 131 LYS -123.7 117.6 -171.4 -60.5 160.4 -82.2 -87.9 132 VAL -117.6 125.8 177.8 -177.3 133 PHE -118.6 127.1 173.4 -70.7 75.9 134 PHE -112.8 122.2 -177.7 -65.6 -67.6 135 ILE -117.9 109.3 176.5 -52.6 -67.0 136 GLN -103.1 96.9 -178.8 169.2 47.3 56.5 137 ALA -159.5 160.4 166.1 138 CYS -72.8 158.8 175.4 -65.7 139 GLN -123.6 26.4 -178.3 -67.8 -71.3 -75.7 140 GLY 147.0 -174.7 -172.6 141 ASP -112.7 6.9 179.3 61.1 16.7 142 ASN -82.1 146.2 170.0 -60.9 112.3 143 TYR -85.9 125.9 172.8 -68.0 -70.3 144 GLN -65.6 129.4 -179.6 176.1 75.3 8.8 145 LYS -82.0 161.9 177.3 -66.3 169.3 178.9 75.2 146 GLY -103.9 158.0 177.8 147 ILE -131.7 140.3 -177.9 55.9 176.6 148 PRO -80.9 135.8 176.8 29.6 -35.0 149 VAL -141.0 162.2 179.6 -69.5 150 GLU -73.1 148.5 -177.1 -100.0 166.5 -21.3 151 THR -75.1 135.2 178.4 -46.9 152 ASP -66.5 -28.7 0.0 -75.9 146.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP -2.314 8.225 12.660 2 LYS -0.807 11.327 11.061 3 VAL 1.286 13.396 13.474 4 TYR 2.528 16.977 13.127 5 GLN 6.243 17.276 12.454 6 MET 7.964 18.241 15.708 7 LYS 11.709 17.909 15.234 8 SER 13.047 21.474 15.048 9 LYS 15.329 22.783 17.809 10 PRO 13.927 25.034 19.058 11 ARG 10.423 23.752 18.341 12 GLY 9.189 27.321 18.117 13 TYR 8.462 30.377 20.251 14 CYS 6.401 30.093 23.420 15 LEU 5.052 33.557 24.312 16 ILE 3.955 34.190 27.890 17 ILE 1.858 37.287 28.603 18 ASN 1.838 37.532 32.372 19 ASN -0.536 40.143 33.764 20 HIS -0.248 40.980 37.449 21 ASN -0.847 44.667 38.128 22 PHE -4.354 45.971 37.447 23 ALA -3.989 49.404 39.033 24 LYS -4.605 51.056 35.624 25 ALA -7.897 49.169 35.290 26 ARG -8.978 50.120 38.786 27 GLU -8.201 53.744 37.963 28 LYS -9.680 54.024 34.474 29 VAL -12.615 51.632 34.150 30 PRO -15.491 52.332 36.516 31 LYS -16.863 48.823 36.654 32 LEU -13.401 47.480 37.412 33 HIS -12.943 49.652 40.470 34 SER -12.208 46.584 42.582 35 ILE -10.496 44.220 40.141 36 ARG -7.615 42.643 42.017 37 ASP -3.966 42.209 41.217 38 ARG -3.170 38.634 40.210 39 ASN -0.935 37.633 43.081 40 GLY 0.881 34.412 42.364 41 THR 0.784 34.647 38.576 42 HIS 4.573 34.519 38.372 43 LEU 4.382 30.925 39.656 44 ASP 2.456 30.021 36.478 45 ALA 4.867 31.936 34.226 46 GLY 7.716 30.052 35.853 47 ALA 6.018 26.678 35.553 48 LEU 5.286 27.287 31.859 49 THR 8.885 28.392 31.298 50 THR 10.293 25.271 32.936 51 THR 7.854 23.006 31.114 52 PHE 8.211 24.441 27.654 53 GLU 11.976 24.908 27.840 54 GLU 12.216 21.215 28.743 55 LEU 10.147 20.610 25.603 56 HIS 12.571 22.603 23.479 57 PHE 10.663 25.834 23.017 58 GLU 12.205 29.331 23.095 59 ILE 10.377 31.256 25.793 60 LYS 9.435 34.928 25.304 61 PRO 7.968 36.437 28.459 62 HIS 6.195 39.805 28.737 63 ASP 4.857 41.086 32.063 64 ASP 2.016 43.534 32.753 65 CYS 0.578 44.175 29.344 66 THR -2.239 46.547 28.313 67 VAL -4.435 45.490 25.408 68 GLU -2.549 47.663 22.931 69 GLN 0.718 46.206 24.197 70 ILE -0.620 42.688 23.703 71 TYR -1.583 43.471 20.131 72 GLU 1.849 44.929 19.496 73 ILE 3.605 41.784 20.774 74 LEU 1.391 39.547 18.692 75 LYS 1.987 41.690 15.604 76 ILE 5.743 41.245 16.070 77 TYR 5.377 37.506 16.088 78 GLN 2.863 37.435 13.253 79 LEU 5.425 39.226 11.056 80 MET 8.319 37.047 12.187 81 ASP 9.790 34.241 10.108 82 HIS 8.762 30.915 11.616 83 SER 10.033 28.895 8.658 84 ASN 12.537 27.014 10.788 85 MET 9.997 26.319 13.551 86 ASP 7.557 23.430 13.805 87 CYS 5.067 25.025 16.259 88 PHE 4.029 28.283 17.968 89 ILE 2.589 28.642 21.512 90 CYS 1.053 31.687 23.177 91 CYS 0.064 31.650 26.859 92 ILE -2.047 34.441 28.328 93 LEU -2.335 34.851 32.100 94 SER -4.836 37.572 32.958 95 HIS -8.287 38.589 34.067 96 GLY -11.135 38.095 31.613 97 ASP -14.872 37.986 30.978 98 LYS -17.121 36.238 28.434 99 GLY -15.090 35.702 25.290 100 ILE -12.432 38.218 26.253 101 ILE -9.242 38.814 28.197 102 TYR -8.427 42.092 29.932 103 GLY -5.262 44.096 29.559 104 THR -3.779 45.568 32.739 105 ASP -5.577 48.773 31.693 106 GLY -8.971 47.100 31.822 107 GLN -9.533 47.294 28.068 108 GLU -10.910 44.147 26.423 109 ALA -9.332 41.872 23.819 110 PRO -11.712 39.311 22.270 111 ILE -9.989 35.952 22.222 112 TYR -10.631 35.591 18.512 113 GLU -8.757 38.848 17.844 114 LEU -5.700 37.247 19.469 115 THR -5.777 33.848 17.774 116 SER -6.748 35.282 14.387 117 GLN -3.380 37.031 14.121 118 PHE -1.866 33.626 13.390 119 THR -4.067 32.230 10.655 120 GLY -2.292 30.827 7.638 121 LEU -2.905 34.002 5.620 122 LYS -1.646 36.346 8.340 123 CYS 1.341 34.187 9.239 124 PRO 2.268 32.066 6.255 125 SER 5.426 30.681 7.791 126 LEU 3.234 28.836 10.329 127 ALA 0.879 27.472 7.641 128 GLY 0.242 23.783 8.236 129 LYS 1.906 24.012 11.660 130 PRO 0.194 23.790 15.055 131 LYS -0.612 27.010 16.828 132 VAL -1.442 26.555 20.494 133 PHE -3.022 29.139 22.777 134 PHE -3.453 28.607 26.547 135 ILE -5.726 31.151 28.236 136 GLN -5.716 31.331 32.012 137 ALA -8.396 33.929 32.773 138 CYS -11.953 34.092 34.071 139 GLN -14.719 34.030 31.439 140 GLY -17.320 35.681 33.669 141 ASP -18.128 36.029 37.348 142 ASN -20.236 32.948 38.026 143 TYR -19.041 30.082 40.190 144 GLN -19.420 26.778 38.319 145 LYS -21.587 24.484 40.425 146 GLY -20.801 20.915 41.351 147 ILE -22.731 17.691 40.764 148 PRO -22.466 14.449 42.736 149 VAL -21.095 11.353 41.036 150 GLU -19.829 7.930 42.073 151 THR -16.109 7.621 42.798 152 ASP -13.969 6.001 40.099 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S C C T T/P T 10 T/S S S S S S S S S S 20 S H H H H H H H H/T T 30 T T S S S S S/S S S S/H 40 H H H 3 3/H H H H H H 50 H H H H H H/S S S S S 60 S S S S C H H H H H 70 H H H H H H H H H H 80 C T T T T C S S S S 90 S S S S S C T T T T/S 100 S S S/T T T T/S S S S S/H 110 H H H H H H H C T T 120 T T T T T T/T T T T/S S 130 S S S S S S S S C C 140 S S S S S S S S S S/S 150 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S 10 e E E E E E E e 20 h H H H H H H h G 30 G G g T t t T h 40 H H H H H H H H H H 50 H H H H h T t E E E 60 E E E e h H H H H 70 H H H H H H H H H h 80 t T T t S E E E 90 E E E e e E E T e E 100 E E e T T t e E E E 110 H H H H H h G G g T 120 T T g G G G g T t e 130 E E E E E E S S S 140 S 150 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 0.0 0.0 93.0 2 LYS 0.0 0.0 90.6 3 VAL 15.9 13.3 87.1 4 TYR 54.1 29.9 74.3 5 GLN 47.2 31.8 83.2 6 MET 106.2 66.6 55.4 7 LYS 33.8 19.5 85.5 8 SER 60.4 72.2 72.7 9 LYS 59.8 34.5 80.3 10 PRO 75.2 60.4 68.0 11 ARG 168.0 80.4 50.1 12 GLY 34.8 100.0 48.9 13 TYR 152.8 84.4 42.9 14 CYS 99.2 100.0 33.6 15 LEU 147.8 100.0 30.7 16 ILE 143.2 99.8 39.6 17 ILE 143.5 100.0 34.0 18 ASN 112.2 92.8 52.0 19 ASN 120.9 100.0 52.0 20 HIS 88.2 58.7 66.4 21 ASN 55.9 46.2 72.8 22 PHE 166.8 100.0 52.7 23 ALA 29.8 41.0 82.9 24 LYS 66.4 38.3 69.0 25 ALA 72.6 100.0 48.1 26 ARG 142.2 68.1 68.8 27 GLU 14.4 10.4 81.8 28 LYS 83.8 48.3 73.0 29 VAL 93.3 78.5 57.0 30 PRO 13.5 10.8 83.6 31 LYS 56.2 32.4 75.0 32 LEU 130.7 88.5 43.3 33 HIS 39.8 26.5 83.6 34 SER 19.5 23.3 76.6 35 ILE 121.5 84.7 41.8 36 ARG 12.5 6.0 92.5 37 ASP 78.7 71.2 70.4 38 ARG 173.8 83.2 60.7 39 ASN 20.2 16.7 82.4 40 GLY 16.5 47.3 68.8 41 THR 100.5 94.0 61.5 42 HIS 36.4 24.2 73.6 43 LEU 30.0 20.3 81.4 44 ASP 51.0 46.1 62.4 45 ALA 57.8 79.6 52.6 46 GLY 3.0 8.5 79.0 47 ALA 17.1 23.6 80.7 48 LEU 111.5 75.5 39.5 49 THR 66.7 62.4 60.5 50 THR 21.2 19.8 82.8 51 THR 46.7 43.7 61.5 52 PHE 142.7 85.6 30.6 53 GLU 56.3 40.6 72.8 54 GLU 23.2 16.7 79.5 55 LEU 57.0 38.5 63.3 56 HIS 75.6 50.3 75.3 57 PHE 154.9 92.9 40.1 58 GLU 70.8 51.1 61.2 59 ILE 138.7 96.7 47.5 60 LYS 107.8 62.2 61.4 61 PRO 54.7 44.0 70.0 62 HIS 90.7 60.4 56.6 63 ASP 35.0 31.7 77.7 64 ASP 65.9 59.7 64.6 65 CYS 94.3 95.0 51.7 66 THR 94.4 88.3 66.9 67 VAL 108.9 91.7 49.0 68 GLU 2.2 1.6 82.5 69 GLN 76.3 51.3 71.6 70 ILE 143.5 100.0 31.7 71 TYR 110.1 60.8 54.5 72 GLU 36.9 26.7 70.5 73 ILE 128.7 89.7 37.9 74 LEU 147.7 99.9 30.0 75 LYS 52.9 30.5 76.1 76 ILE 60.1 41.9 63.2 77 TYR 166.1 91.7 32.0 78 GLN 127.5 85.8 49.4 79 LEU 50.3 34.0 82.2 80 MET 108.9 68.3 61.4 81 ASP 33.0 29.8 77.7 82 HIS 150.2 100.0 39.2 83 SER 37.9 45.4 82.3 84 ASN 4.8 4.0 87.3 85 MET 141.6 88.8 61.1 86 ASP 102.4 92.6 55.7 87 CYS 93.6 94.3 35.9 88 PHE 166.8 100.0 28.9 89 ILE 137.3 95.7 28.9 90 CYS 99.2 100.0 29.7 91 CYS 99.0 99.8 32.5 92 ILE 143.5 100.0 26.9 93 LEU 142.5 96.4 52.4 94 SER 83.6 100.0 54.7 95 HIS 112.6 74.9 46.4 96 GLY 34.8 100.0 49.2 97 ASP 67.0 60.7 59.3 98 LYS 15.7 9.0 86.3 99 GLY 2.3 6.6 75.0 100 ILE 127.6 88.9 52.6 101 ILE 143.5 100.0 28.4 102 TYR 171.9 95.0 45.3 103 GLY 34.8 100.0 62.2 104 THR 103.7 97.0 52.7 105 ASP 99.0 89.6 48.3 106 GLY 34.8 100.0 45.4 107 GLN 54.4 36.6 75.7 108 GLU 70.9 51.1 62.9 109 ALA 72.6 100.0 37.2 110 PRO 68.1 54.7 67.6 111 ILE 102.7 71.6 53.7 112 TYR 31.2 17.2 82.2 113 GLU 63.8 46.0 68.4 114 LEU 147.5 99.8 29.2 115 THR 68.3 63.8 49.2 116 SER 67.9 81.2 63.6 117 GLN 105.9 71.3 64.4 118 PHE 166.0 99.5 35.9 119 THR 47.7 44.6 68.9 120 GLY 19.1 54.8 70.7 121 LEU 0.0 0.0 87.1 122 LYS 61.6 35.5 83.6 123 CYS 98.4 99.2 55.4 124 PRO 41.5 33.4 82.7 125 SER 57.3 68.6 65.8 126 LEU 147.8 100.0 43.9 127 ALA 33.1 45.6 76.4 128 GLY 0.0 0.0 81.9 129 LYS 132.2 76.2 67.9 130 PRO 100.4 80.6 44.2 131 LYS 134.3 77.5 58.6 132 VAL 71.1 59.8 50.9 133 PHE 149.1 89.4 40.1 134 PHE 71.4 42.8 58.5 135 ILE 121.6 84.7 45.4 136 GLN 54.8 36.9 78.2 137 ALA 71.7 98.8 65.0 138 CYS 29.1 29.3 86.9 139 GLN 84.7 57.0 65.6 140 GLY 23.4 67.1 70.1 141 ASP 2.2 2.0 89.3 142 ASN 7.6 6.3 91.4 143 TYR 0.0 0.0 92.9 144 GLN 0.0 0.0 92.5 145 LYS 5.5 3.2 92.4 146 GLY 0.0 0.0 77.9 147 ILE 17.3 12.1 75.8 148 PRO 7.3 5.9 83.1 149 VAL 21.6 18.2 82.4 150 GLU 0.0 0.0 91.2 151 THR 0.0 0.0 91.5 152 ASP 0.0 0.0 93.3