Protein Data Bank File : 1g2ia Title : HYDROLASE 19-OCT-00 1G2I Number of Amino Acid Residues : 162 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS VAL LEU PHE LEU THR ALA ASN GLU PHE 10 GLU ASP VAL GLU LEU ILE TYR PRO TYR HIS 20 ARG LEU LYS GLU GLU GLY HIS GLU VAL TYR 30 ILE ALA SER PHE GLU ARG GLY THR ILE THR 40 GLY LYS HIS GLY TYR SER VAL LYS VAL ASP 50 LEU THR PHE ASP LYS VAL ASN PRO GLU GLU 60 PHE ASP ALA LEU VAL LEU PRO GLY GLY ARG 70 ALA PRO GLU ARG VAL ARG LEU ASN GLU LYS 80 ALA VAL SER ILE ALA ARG LYS PHE SER GLU 90 GLY LYS PRO VAL ALA SER ILE CYS HIS GLY 100 PRO GLN ILE LEU ILE SER ALA GLY VAL LEU 110 ARG GLY ARG LYS GLY THR SER TYR PRO GLY 120 ILE LYS ASP ASP ILE ASN ALA GLY VAL GLU 130 TRP VAL ASP ALA GLU VAL VAL VAL ASP GLY 140 ASN TRP VAL SER SER ARG VAL PRO ALA ASP 150 LEU TYR ALA TRP ARG GLU PHE VAL LYS LEU 160 LEU LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 117.9 -178.7 -65.1 -169.7 -67.7 -60.9 2 VAL -105.5 127.0 -179.6 -172.2 3 LEU -102.4 140.6 177.8 -179.3 69.4 4 PHE -115.7 130.9 177.4 -72.8 66.5 5 LEU -109.5 112.9 -177.9 -65.1 178.1 6 THR -155.6 -170.6 -179.5 -175.3 7 ALA -170.6 -175.7 178.6 8 ASN -52.2 146.5 179.2 -79.7 146.1 9 GLU 74.8 24.0 177.1 -62.8 -72.0 64.5 10 PHE -74.4 155.6 178.0 59.1 84.7 11 GLU -75.2 110.2 -176.5 172.7 59.6 -159.0 12 ASP -38.8 -60.3 -178.4 -50.0 60.2 13 VAL -67.8 -25.3 -179.9 -63.6 14 GLU -73.4 -11.3 177.4 -58.7 -176.6 -17.8 15 LEU -104.2 -50.3 -178.8 166.5 47.0 16 ILE -63.3 -39.9 -179.5 -64.5 172.4 17 TYR -61.2 -56.8 -180.0 -173.3 77.8 18 PRO -63.8 -31.0 179.7 29.6 -42.8 19 TYR -57.6 -53.6 179.9 -178.3 -85.5 20 HIS -74.3 -39.1 -179.4 -77.6 92.0 21 ARG -57.6 -38.3 179.9 -179.5 68.5 -170.8 79.5 22 LEU -77.9 -34.5 178.4 -64.1 174.7 23 LYS -63.6 -32.5 179.5 -78.2 -165.7 62.4 172.3 24 GLU -56.7 -40.9 -179.1 167.8 -176.8 164.8 25 GLU -73.1 -11.9 -179.9 -62.5 -61.1 155.5 26 GLY 101.9 3.7 179.3 27 HIS -76.9 145.7 178.1 -64.8 127.0 28 GLU -88.7 131.5 -179.0 -59.1 178.6 66.2 29 VAL -113.3 138.0 -179.5 -69.3 30 TYR -130.0 136.4 179.7 -56.1 74.3 31 ILE -104.5 118.0 179.1 -57.9 -61.1 32 ALA -111.0 140.0 179.6 33 SER -153.0 -173.5 -179.3 -166.9 34 PHE -59.7 -46.7 -178.5 -64.6 93.6 35 GLU -136.1 165.9 178.8 -52.8 179.5 -56.0 36 ARG -70.0 174.6 -179.5 -79.3 -60.3 -168.5 65.9 37 GLY 101.1 -130.8 -179.7 38 THR -135.3 163.0 177.7 66.3 39 ILE -128.4 157.1 -177.9 44.6 177.2 40 THR -124.9 133.1 -179.7 -50.9 41 GLY -72.3 169.8 -179.7 42 LYS -63.9 -24.4 179.9 66.2 163.7 66.2 -64.1 43 HIS -95.0 3.0 177.9 -73.1 -84.5 44 GLY 100.8 -6.4 178.8 45 TYR -71.8 136.5 179.9 -80.4 94.3 46 SER -108.3 133.9 179.2 169.7 47 VAL -131.8 149.7 -179.5 -52.0 48 LYS -86.8 142.4 178.9 54.3 -179.1 173.1 -62.1 49 VAL -86.9 131.1 -179.9 175.3 50 ASP -85.5 -36.1 178.8 -68.3 -62.6 51 LEU -159.9 158.9 -179.7 69.7 172.2 52 THR -85.9 162.3 179.0 61.9 53 PHE -56.3 -43.4 -179.0 -64.5 142.1 54 ASP -60.3 -30.8 -179.0 -64.4 -55.5 55 LYS -89.0 -3.0 -179.4 -57.5 169.2 -174.6 177.3 56 VAL -80.6 132.9 176.8 173.1 57 ASN -114.8 107.6 -179.6 -174.2 -38.0 58 PRO -47.7 -33.8 -178.8 -30.1 43.4 59 GLU -69.2 -17.4 -179.8 -53.0 -57.4 175.0 60 GLU -88.3 -1.0 179.8 -63.3 -174.7 -58.9 61 PHE -122.2 151.9 -177.3 -61.0 86.2 62 ASP -105.6 -21.3 -179.5 -44.3 -59.1 63 ALA -145.7 158.7 -178.0 64 LEU -131.8 138.4 178.7 179.4 68.6 65 VAL -125.2 131.9 -179.1 178.6 66 LEU -119.6 93.4 179.6 -54.5 172.5 67 PRO -65.8 165.8 179.5 -27.8 41.5 68 GLY -95.5 -149.7 -179.0 69 GLY 99.0 -156.7 179.3 70 ARG -91.8 -15.2 -178.9 -66.6 179.6 172.7 -179.4 71 ALA -54.4 -42.0 -179.8 72 PRO -54.2 -37.3 -180.0 -32.8 44.4 73 GLU -65.7 -20.9 177.9 -97.8 -175.5 39.1 74 ARG -94.9 -39.7 179.3 -71.1 -153.6 167.3 -172.7 75 VAL -63.6 -37.9 -178.6 176.1 76 ARG -66.7 -8.9 178.9 75.6 -171.2 -55.6 -164.4 77 LEU -98.5 -3.9 179.5 -73.2 177.8 78 ASN -94.2 113.7 -179.2 -177.8 -83.2 79 GLU -52.8 -45.1 -179.4 177.1 -78.0 -57.4 80 LYS -63.2 -47.2 -179.8 -175.0 62.5 174.5 64.4 81 ALA -61.8 -43.8 -180.0 82 VAL -63.7 -40.0 179.8 175.2 83 SER -66.2 -34.6 178.7 66.7 84 ILE -60.2 -50.3 179.9 -68.4 172.6 85 ALA -64.3 -41.6 -179.6 86 ARG -60.6 -48.4 -179.9 -177.4 163.4 49.0 -128.1 87 LYS -62.9 17.8 77.9 -66.3 178.9 -177.7 178.8 88 PHE 22.6 -46.6 -179.0 -171.2 92.0 89 SER -67.6 -27.6 179.0 64.3 90 GLU -74.1 -5.9 179.4 -70.3 179.9 -57.1 91 GLY 84.9 8.8 179.3 92 LYS -70.2 152.2 179.9 -67.1 176.5 177.9 176.6 93 PRO -57.6 130.8 179.4 -31.5 44.1 94 VAL -134.3 122.4 179.8 179.3 95 ALA -111.6 128.7 179.6 96 SER -132.3 149.0 178.9 73.2 97 ILE -149.0 149.0 178.2 -172.7 168.3 98 CYS 59.7 -115.1 179.0 -164.4 99 HIS -91.0 -6.7 -179.8 -74.1 78.8 100 GLY -47.8 -41.8 -179.9 101 PRO -66.0 -8.2 177.9 30.1 -42.5 102 GLN -59.6 -30.8 179.4 -68.7 -178.2 -49.0 103 ILE -66.4 -38.2 179.0 -67.1 166.2 104 LEU -72.0 -36.3 177.8 -65.4 177.2 105 ILE -56.3 -50.7 -179.3 -74.1 -179.0 106 SER -64.0 -26.5 178.8 -65.7 107 ALA -73.8 -18.7 179.1 108 GLY 72.6 28.8 -178.0 109 VAL -108.6 3.6 -176.1 -58.1 110 LEU -91.0 -6.2 -177.9 -61.1 -179.4 111 ARG -59.3 124.4 179.6 177.3 147.3 -73.9 100.9 112 GLY 87.7 -8.0 -179.7 113 ARG -82.4 158.3 -178.6 -59.4 -53.6 -68.8 -93.9 114 LYS -113.6 126.6 -179.3 -169.2 170.6 -173.3 175.7 115 GLY -172.6 -168.3 -179.4 116 THR -140.8 -176.5 -178.9 -169.6 117 SER -175.2 -172.8 176.6 67.8 118 TYR -58.6 127.3 -179.7 173.2 62.1 119 PRO -50.5 -31.5 -179.5 -32.4 44.6 120 GLY -59.3 -22.5 179.8 121 ILE -116.6 20.2 179.9 62.9 172.7 122 LYS -57.8 -36.9 -179.6 69.7 174.3 -176.2 60.7 123 ASP -66.6 -29.7 179.5 -73.0 -21.6 124 ASP -76.7 29.5 73.5 -56.0 -40.6 125 ILE 24.6 -46.2 179.9 -68.0 171.8 126 ASN -62.7 -18.9 178.9 -79.5 155.7 127 ALA -90.0 1.4 178.9 128 GLY 95.8 10.7 180.0 129 VAL -85.2 137.5 175.3 171.7 130 GLU -90.8 99.9 -176.9 48.8 -179.4 -59.2 131 TRP -74.5 130.9 179.7 -158.5 83.9 132 VAL -120.4 136.0 179.2 -179.0 133 ASP -94.5 81.8 180.0 -174.1 11.0 134 ALA -140.0 151.9 -179.6 135 GLU -56.8 -29.0 178.2 51.1 -178.9 11.3 136 VAL -157.2 137.7 179.2 70.4 137 VAL -126.4 136.0 179.5 -178.9 138 VAL -118.5 115.0 -179.8 178.2 139 ASP -127.8 82.7 -179.0 173.9 35.0 140 GLY 68.4 -118.9 -179.4 141 ASN -84.2 -4.9 -178.0 65.8 -47.4 142 TRP -104.8 111.5 179.3 -176.7 34.7 143 VAL -109.3 117.5 -178.4 178.5 144 SER -127.1 149.2 178.7 58.6 145 SER -135.4 173.3 -176.2 -70.3 146 ARG -101.0 -55.3 -176.8 -45.5 160.3 -61.0 -174.2 147 VAL -137.8 174.0 179.9 -63.7 148 PRO -52.8 -31.5 -179.8 -34.5 44.8 149 ALA -63.8 -18.9 -179.5 150 ASP -90.5 -4.1 -178.0 -55.4 -35.0 151 LEU -43.3 -49.0 -178.9 -72.3 177.3 152 TYR -57.3 -48.6 -179.4 75.9 101.4 153 ALA -69.4 -37.2 -179.7 154 TRP -56.0 9.1 76.4 -176.3 44.9 155 ARG 43.3 -45.2 -179.9 179.2 -136.9 -62.2 139.9 156 GLU -74.6 -43.2 -179.0 -65.6 -51.0 -36.4 157 PHE -63.5 -38.4 179.1 -161.9 58.6 158 VAL -59.8 -43.8 179.6 165.8 159 LYS -57.8 -42.8 -179.3 -63.0 178.1 -178.1 175.6 160 LEU -62.9 -36.2 -179.2 -157.3 -176.6 161 LEU -78.2 -20.8 -179.7 -76.3 -89.8 162 LYS -61.7 -10.8 0.0 -60.8 174.8 -176.3 175.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 108.372 61.462 11.970 2 VAL 104.674 62.009 12.656 3 LEU 101.993 60.410 10.495 4 PHE 98.462 61.742 10.056 5 LEU 95.617 59.433 8.994 6 THR 92.807 61.513 7.519 7 ALA 90.680 62.242 4.431 8 ASN 88.181 64.651 2.845 9 GLU 85.908 66.344 5.401 10 PHE 88.489 66.389 8.190 11 GLU 87.936 69.083 10.832 12 ASP 90.249 71.736 9.381 13 VAL 91.863 73.090 12.553 14 GLU 92.217 69.643 14.133 15 LEU 94.574 68.763 11.303 16 ILE 96.278 72.107 10.643 17 TYR 96.985 72.986 14.291 18 PRO 98.923 69.825 15.238 19 TYR 100.591 69.843 11.830 20 HIS 102.252 73.198 12.464 21 ARG 102.627 72.805 16.227 22 LEU 104.734 69.694 15.657 23 LYS 106.696 71.215 12.764 24 GLU 107.663 73.983 15.175 25 GLU 109.483 71.369 17.259 26 GLY 111.398 70.111 14.239 27 HIS 109.319 66.984 13.703 28 GLU 108.646 65.851 10.150 29 VAL 104.916 65.635 9.438 30 TYR 103.242 63.455 6.803 31 ILE 99.652 63.392 5.559 32 ALA 98.303 59.985 4.532 33 SER 94.918 59.459 2.888 34 PHE 93.101 57.269 0.351 35 GLU 94.677 58.806 -2.752 36 ARG 97.382 61.210 -3.878 37 GLY 96.606 64.826 -4.661 38 THR 94.732 66.888 -2.095 39 ILE 91.917 66.573 0.426 40 THR 89.566 69.298 1.633 41 GLY 88.370 70.014 5.156 42 LYS 84.753 70.575 6.098 43 HIS 85.534 74.305 6.217 44 GLY 87.239 74.439 2.833 45 TYR 90.940 74.292 3.667 46 SER 92.886 72.228 1.153 47 VAL 95.946 70.183 2.092 48 LYS 98.206 67.959 0.017 49 VAL 98.426 64.216 0.601 50 ASP 102.000 62.994 1.052 51 LEU 101.255 59.297 0.597 52 THR 98.381 56.832 0.368 53 PHE 97.367 54.379 3.085 54 ASP 98.606 51.518 0.889 55 LYS 102.113 52.981 0.612 56 VAL 102.482 53.522 4.361 57 ASN 104.856 51.335 6.363 58 PRO 103.974 51.748 10.079 59 GLU 107.581 50.944 10.966 60 GLU 108.817 54.046 9.149 61 PHE 106.917 56.414 11.446 62 ASP 107.316 57.269 15.130 63 ALA 104.056 58.979 16.080 64 LEU 100.441 59.135 14.924 65 VAL 97.852 61.913 14.876 66 LEU 94.138 61.368 14.292 67 PRO 92.197 64.570 13.446 68 GLY 88.419 64.658 13.763 69 GLY 85.613 65.622 11.404 70 ARG 83.659 63.228 9.177 71 ALA 86.832 61.664 7.767 72 PRO 87.247 59.064 10.565 73 GLU 83.987 57.326 9.624 74 ARG 85.378 56.678 6.152 75 VAL 88.951 55.980 7.253 76 ARG 87.802 53.425 9.850 77 LEU 86.380 51.280 7.026 78 ASN 89.748 51.052 5.284 79 GLU 91.569 47.887 6.348 80 LYS 94.999 49.341 5.568 81 ALA 94.438 52.585 7.498 82 VAL 93.041 50.727 10.501 83 SER 95.984 48.297 10.548 84 ILE 98.395 51.239 10.490 85 ALA 96.737 52.662 13.596 86 ARG 96.444 49.252 15.266 87 LYS 100.153 48.507 14.824 88 PHE 99.162 52.163 18.844 89 SER 99.925 48.624 20.032 90 GLU 103.665 49.195 19.561 91 GLY 103.322 51.895 22.200 92 LYS 104.159 54.747 19.837 93 PRO 102.729 58.202 20.647 94 VAL 99.157 58.553 19.370 95 ALA 97.135 61.772 19.515 96 SER 93.392 61.770 18.881 97 ILE 90.687 64.419 19.001 98 CYS 86.941 64.653 18.289 99 HIS 85.907 61.740 16.029 100 GLY 89.524 60.737 15.434 101 PRO 89.416 57.890 17.990 102 GLN 86.703 56.102 15.976 103 ILE 89.686 54.782 14.012 104 LEU 91.202 53.335 17.197 105 ILE 87.846 51.812 18.157 106 SER 87.880 49.962 14.832 107 ALA 91.498 48.929 15.378 108 GLY 90.241 47.165 18.519 109 VAL 92.973 48.478 20.817 110 LEU 91.030 50.608 23.308 111 ARG 89.664 48.158 25.876 112 GLY 90.753 49.277 29.332 113 ARG 92.319 52.510 28.096 114 LYS 91.502 55.936 29.524 115 GLY 90.644 58.854 27.269 116 THR 88.070 61.190 25.787 117 SER 86.530 62.203 22.459 118 TYR 83.715 64.195 20.909 119 PRO 80.994 63.858 23.592 120 GLY 78.577 62.679 20.915 121 ILE 80.340 59.319 20.640 122 LYS 81.208 58.784 24.300 123 ASP 78.847 55.797 24.406 124 ASP 80.677 54.160 21.516 125 ILE 82.551 53.224 26.417 126 ASN 81.158 50.216 24.497 127 ALA 84.681 49.689 23.158 128 GLY 85.980 49.354 26.719 129 VAL 87.207 52.913 27.212 130 GLU 86.872 54.563 30.603 131 TRP 85.639 57.856 29.172 132 VAL 86.653 61.124 30.824 133 ASP 85.130 64.533 30.127 134 ALA 88.303 66.640 30.154 135 GLU 89.989 68.973 27.650 136 VAL 92.874 66.515 27.507 137 VAL 93.591 63.043 28.843 138 VAL 97.008 61.407 28.930 139 ASP 97.054 57.614 29.184 140 GLY 100.559 56.407 28.496 141 ASN 101.151 56.748 24.762 142 TRP 97.574 57.929 24.132 143 VAL 96.811 61.650 24.329 144 SER 93.180 62.529 23.602 145 SER 90.992 65.630 23.475 146 ARG 87.359 66.432 22.648 147 VAL 86.840 69.518 20.481 148 PRO 88.696 72.405 18.768 149 ALA 88.494 74.421 21.989 150 ASP 90.850 71.833 23.534 151 LEU 93.599 72.299 20.924 152 TYR 95.995 74.193 23.204 153 ALA 95.867 71.541 25.939 154 TRP 95.860 68.683 23.430 155 ARG 100.657 70.822 25.065 156 GLU 100.579 67.232 26.328 157 PHE 101.417 65.496 23.047 158 VAL 104.472 67.696 22.515 159 LYS 105.768 66.656 25.950 160 LEU 105.364 62.987 25.032 161 LEU 107.373 63.528 21.839 162 LYS 110.196 65.384 23.613 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S C C 10 H H H H H H H 3 3/H H 20 H H H H H H/S S S S S 30 S S S S/S S S S/S S S S 40 S/T T T T/S S S S S S S 50 C T T T T C T T T T/S 60 S S S/S S S S S S S S/H 70 H H H 3 3 C C H H H 80 H H H H H H H/X X/T T T 90 T S S S S S S/T T T T 100 H H H H H H H H S S 110 S S/S S S S S S T T T 120 T C C C/X X/T T T T C S 130 S S S S S S S S S/T T 140 T T/S S S S S S/T T T T/T 150 T T T C/X X/H H H H H H 160 H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E e t T T B 10 h H H H H H H H H H 20 H H H H h T t e E E 30 E E E S S S E E E E 40 e T T t e E E E E 50 E E e G G g g G G G 60 g S E E E E B h 70 H H H H H h T h H H 80 H H H H H H h t T T 90 t e E E E E e T T 100 h H H H H H H h t t 110 T T e E E g G G 120 G g T t t T T t E 130 E e S S E E E T 140 e E E E E g G G G 150 g T T t h H H H H H 160 H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 101.9 58.8 74.1 2 VAL 118.5 99.7 34.8 3 LEU 145.1 98.1 27.4 4 PHE 166.8 100.0 31.8 5 LEU 147.8 100.0 28.1 6 THR 104.3 97.6 30.4 7 ALA 68.1 93.8 44.3 8 ASN 46.6 38.6 66.6 9 GLU 75.9 54.8 68.0 10 PHE 166.8 100.0 49.9 11 GLU 118.1 85.2 48.1 12 ASP 108.8 98.5 39.3 13 VAL 55.1 46.4 54.8 14 GLU 138.5 99.9 30.4 15 LEU 145.9 98.7 24.9 16 ILE 93.9 65.4 45.6 17 TYR 97.3 53.7 56.3 18 PRO 114.1 91.7 37.7 19 TYR 134.2 74.2 50.6 20 HIS 45.3 30.1 69.0 21 ARG 140.9 67.5 59.9 22 LEU 144.2 97.5 32.7 23 LYS 80.3 46.3 71.5 24 GLU 35.6 25.7 82.4 25 GLU 90.4 65.2 68.2 26 GLY 1.0 2.9 85.7 27 HIS 109.6 72.9 52.5 28 GLU 40.9 29.5 73.5 29 VAL 115.0 96.8 41.9 30 TYR 126.2 69.7 49.7 31 ILE 138.5 96.5 34.8 32 ALA 72.6 100.0 39.7 33 SER 82.4 98.6 36.2 34 PHE 103.0 61.8 56.0 35 GLU 13.5 9.7 81.6 36 ARG 90.5 43.3 74.7 37 GLY 0.0 0.0 73.7 38 THR 45.2 42.3 73.3 39 ILE 133.4 92.9 51.4 40 THR 50.8 47.6 70.9 41 GLY 34.8 100.0 60.1 42 LYS 119.7 69.0 71.2 43 HIS 50.7 33.7 76.0 44 GLY 9.6 27.6 73.9 45 TYR 53.9 29.8 68.5 46 SER 38.8 46.5 73.7 47 VAL 91.1 76.7 47.4 48 LYS 34.6 19.9 83.1 49 VAL 118.7 99.9 51.3 50 ASP 68.2 61.7 58.6 51 LEU 121.5 82.2 44.5 52 THR 94.3 88.3 58.2 53 PHE 164.5 98.6 38.9 54 ASP 21.8 19.7 71.9 55 LYS 71.3 41.1 76.3 56 VAL 118.8 100.0 36.0 57 ASN 51.3 42.5 61.5 58 PRO 110.1 88.4 57.1 59 GLU 51.3 37.0 82.4 60 GLU 39.3 28.3 76.6 61 PHE 151.4 90.8 45.9 62 ASP 40.0 36.2 75.1 63 ALA 72.1 99.3 39.4 64 LEU 135.5 91.7 37.6 65 VAL 118.5 99.7 27.4 66 LEU 147.8 100.0 32.9 67 PRO 124.4 99.9 48.9 68 GLY 34.8 100.0 55.4 69 GLY 31.0 89.0 55.6 70 ARG 42.6 20.4 84.7 71 ALA 70.9 97.7 52.7 72 PRO 122.8 98.6 55.2 73 GLU 44.6 32.2 80.2 74 ARG 29.0 13.9 80.8 75 VAL 118.6 99.9 34.4 76 ARG 155.5 74.5 54.2 77 LEU 21.5 14.6 85.1 78 ASN 80.9 66.9 54.8 79 GLU 18.1 13.1 78.9 80 LYS 126.9 73.2 70.8 81 ALA 72.6 100.0 38.6 82 VAL 108.0 90.9 60.6 83 SER 72.1 86.3 64.9 84 ILE 139.8 97.4 38.2 85 ALA 72.6 100.0 42.0 86 ARG 112.6 53.9 64.0 87 LYS 69.9 40.3 71.8 88 PHE 163.8 98.2 47.6 89 SER 32.9 39.4 67.3 90 GLU 83.5 60.2 71.4 91 GLY 9.9 28.6 81.4 92 LYS 121.7 70.2 72.5 93 PRO 101.0 81.1 44.4 94 VAL 118.3 99.6 40.9 95 ALA 71.0 97.8 39.3 96 SER 83.5 99.9 42.6 97 ILE 143.4 100.0 44.8 98 CYS 85.6 86.3 57.2 99 HIS 111.5 74.3 47.9 100 GLY 34.8 100.0 50.1 101 PRO 119.3 95.8 48.5 102 GLN 139.7 94.0 46.0 103 ILE 142.9 99.6 37.6 104 LEU 147.8 100.0 28.0 105 ILE 112.3 78.2 54.4 106 SER 59.2 70.8 68.8 107 ALA 72.6 100.0 52.1 108 GLY 3.0 8.6 85.3 109 VAL 98.7 83.1 46.6 110 LEU 145.0 98.1 32.8 111 ARG 53.0 25.4 85.3 112 GLY 0.0 0.1 79.9 113 ARG 149.9 71.8 66.1 114 LYS 79.5 45.8 65.7 115 GLY 34.8 100.0 42.8 116 THR 106.7 99.8 54.3 117 SER 76.8 91.8 54.7 118 TYR 95.1 52.6 57.3 119 PRO 70.1 56.3 54.8 120 GLY 8.4 24.1 63.9 121 ILE 128.0 89.2 62.1 122 LYS 89.6 51.7 67.6 123 ASP 31.1 28.2 76.2 124 ASP 40.0 36.2 66.0 125 ILE 69.1 48.2 78.3 126 ASN 20.1 16.6 83.0 127 ALA 55.9 77.0 60.5 128 GLY 20.7 59.5 74.7 129 VAL 108.9 91.7 51.8 130 GLU 48.3 34.9 72.6 131 TRP 180.4 88.0 52.6 132 VAL 73.8 62.1 54.3 133 ASP 42.3 38.3 66.3 134 ALA 40.5 55.7 67.8 135 GLU 82.0 59.2 68.4 136 VAL 106.3 89.5 53.5 137 VAL 105.6 88.9 52.7 138 VAL 68.5 57.6 64.4 139 ASP 77.0 69.7 65.6 140 GLY 0.0 0.0 86.6 141 ASN 105.2 87.1 58.8 142 TRP 202.5 98.8 46.1 143 VAL 118.6 99.8 40.9 144 SER 83.4 99.8 59.8 145 SER 83.6 100.0 40.4 146 ARG 156.0 74.7 61.1 147 VAL 75.4 63.5 52.0 148 PRO 77.7 62.4 53.0 149 ALA 5.7 7.9 79.3 150 ASP 107.3 97.1 57.9 151 LEU 125.3 84.8 38.9 152 TYR 64.9 35.9 85.1 153 ALA 72.6 100.0 53.9 154 TRP 198.8 97.0 40.3 155 ARG 112.2 53.7 70.8 156 GLU 110.7 79.9 52.7 157 PHE 156.4 93.8 38.4 158 VAL 113.2 95.3 50.3 159 LYS 82.4 47.5 73.3 160 LEU 103.0 69.7 56.5 161 LEU 133.1 90.0 41.1 162 LYS 58.1 33.5 76.0