Protein Data Bank File : 1bvh Title : HYDROLASE 03-MAY-94 1BVH Number of Amino Acid Residues : 157 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA GLU GLN VAL THR LYS SER VAL LEU PHE 10 VAL CYS LEU GLY ASN ILE CYS ARG SER PRO 20 ILE ALA GLU ALA VAL PHE ARG LYS LEU VAL 30 THR ASP GLN ASN ILE SER ASP ASN TRP VAL 40 ILE ASP SER GLY ALA VAL SER ASP TRP ASN 50 VAL GLY ARG SER PRO ASP PRO ARG ALA VAL 60 SER CYS LEU ARG ASN HIS GLY ILE ASN THR 70 ALA HIS LYS ALA ARG GLN VAL THR LYS GLU 80 ASP PHE VAL THR PHE ASP TYR ILE LEU CYS 90 MET ASP GLU SER ASN LEU ARG ASP LEU ASN 100 ARG LYS SER ASN GLN VAL LYS ASN CYS ARG 110 ALA LYS ILE GLU LEU LEU GLY SER TYR ASP 120 PRO GLN LYS GLN LEU ILE ILE GLU ASP PRO 130 TYR TYR GLY ASN ASP ALA ASP PHE GLU THR 140 VAL TYR GLN GLN CYS VAL ARG CYS CYS ARG 150 ALA PHE LEU GLU LYS VAL ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 -51.6 179.9 2 GLU -98.7 113.6 -180.0 -38.7 -163.4 23.4 3 GLN -67.3 172.6 -180.0 -80.2 156.9 -107.5 4 VAL -124.7 150.2 179.9 -157.7 5 THR -85.0 71.0 -180.0 23.6 6 LYS -41.9 162.9 -179.5 -143.0 155.6 -67.5 -156.4 7 SER -139.2 136.0 180.0 -58.3 8 VAL -141.7 155.5 -179.7 32.5 9 LEU -150.1 116.0 -179.7 161.6 127.4 10 PHE -86.8 151.6 -179.9 -95.6 -51.1 11 VAL -143.8 157.9 179.9 -165.6 12 CYS 173.1 128.0 179.8 147.2 13 LEU -44.9 150.1 -179.8 -149.1 96.8 14 GLY 58.0 88.3 -179.9 15 ASN -85.5 15.2 -180.0 -176.0 -87.2 16 ILE -119.2 131.8 179.8 61.6 104.2 17 CYS 66.8 128.1 179.8 -171.0 18 ARG 43.1 78.6 179.9 172.9 -132.0 165.2 -74.1 19 SER 163.6 -61.5 -179.6 141.8 20 PRO -71.2 -1.2 -179.9 25.2 -31.5 21 ILE -74.6 -48.1 -179.9 -37.4 -48.6 22 ALA -57.3 -27.9 179.9 23 GLU -73.3 -71.8 179.6 -96.4 121.2 -23.7 24 ALA -44.9 -27.0 179.8 25 VAL -70.2 -54.4 179.6 173.2 26 PHE -45.6 -35.8 179.5 -158.4 -61.5 27 ARG -63.8 -57.7 -179.9 -155.5 112.6 -139.8 150.4 28 LYS -56.0 -21.1 -179.9 179.3 78.1 -127.3 -120.8 29 LEU -85.6 -30.8 179.8 -60.4 164.3 30 VAL -90.7 -6.2 -179.6 80.5 31 THR -105.1 5.9 179.8 -26.8 32 ASP -128.0 59.7 -179.6 -140.9 -4.9 33 GLN 171.3 31.0 -178.7 -133.0 68.2 87.3 34 ASN 45.1 32.0 -178.0 -140.5 -81.2 35 ILE -112.8 -7.3 -179.5 165.7 158.1 36 SER -73.1 -25.1 -179.8 -136.4 37 ASP -84.5 16.3 179.9 -160.3 -25.1 38 ASN -144.5 36.1 -179.4 -95.0 -70.9 39 TRP -150.2 150.4 178.5 -95.3 106.8 40 VAL -128.3 70.9 -178.2 174.5 41 ILE -89.6 140.2 179.6 -53.1 118.9 42 ASP -146.2 171.6 -179.8 -96.3 40.8 43 SER -105.1 162.4 -179.9 57.4 44 GLY -143.1 122.8 180.0 45 ALA -87.1 -41.3 -179.9 46 VAL 80.2 -5.2 179.9 101.4 47 SER -126.5 179.6 -180.0 -98.0 48 ASP -120.4 7.9 -179.9 171.9 76.6 49 TRP -91.6 -33.0 -180.0 -25.2 -40.2 50 ASN -101.9 31.2 180.0 -49.5 -99.6 51 VAL -76.3 96.8 -179.9 174.0 52 GLY 98.4 4.2 -180.0 53 ARG -79.4 86.6 -180.0 -92.8 -167.2 99.2 -42.4 54 SER -45.4 159.6 180.0 -82.5 55 PRO -50.5 152.4 180.0 -25.3 31.6 56 ASP -68.2 152.4 -180.0 -112.0 -29.0 57 PRO -51.2 -20.0 -179.8 -24.9 31.3 58 ARG -81.9 -47.8 -179.7 -81.7 -142.6 116.0 -144.5 59 ALA -89.9 4.6 -180.0 60 VAL -89.9 -43.9 -179.9 74.3 61 SER -76.8 -17.8 -179.9 41.1 62 CYS -78.3 -62.3 -179.9 -59.1 63 LEU -60.7 -28.0 -179.9 92.3 173.3 64 ARG -96.9 33.4 179.9 -173.9 133.4 72.0 100.8 65 ASN -131.5 -43.1 180.0 167.2 -81.6 66 HIS -82.9 -22.2 -179.9 -67.8 -125.5 67 GLY 113.2 83.3 -179.8 68 ILE -122.2 -24.5 -180.0 -156.5 93.8 69 ASN 63.5 98.3 180.0 -60.2 -101.3 70 THR -124.2 91.4 180.0 156.1 71 ALA -119.8 53.5 180.0 72 HIS -143.9 155.9 -179.9 178.3 104.1 73 LYS -104.7 130.8 180.0 -145.0 77.9 64.0 36.1 74 ALA -44.0 -69.9 -179.9 75 ARG 61.1 159.0 -179.9 -87.8 -78.2 -127.9 -47.6 76 GLN -88.4 123.8 -180.0 175.1 -162.0 -67.7 77 VAL -47.6 151.5 -179.9 -171.7 78 THR -141.1 165.2 179.8 -6.7 79 LYS -43.2 -41.7 -179.9 166.6 -103.0 144.8 172.9 80 GLU -56.1 -48.4 -179.9 179.5 80.6 32.6 81 ASP -62.3 -34.0 -179.5 -63.0 57.0 82 PHE -65.7 -79.1 -179.7 -71.3 -81.7 83 VAL -48.1 -46.9 179.8 69.7 84 THR -45.8 -82.9 180.0 -72.0 85 PHE -57.1 166.5 -179.7 -47.7 -57.6 86 ASP -121.3 -25.6 -179.8 -120.5 62.1 87 TYR -109.4 72.5 -180.0 -49.9 -22.8 88 ILE -82.8 96.6 179.8 -82.8 -154.4 89 LEU -109.9 180.0 180.0 -31.4 116.8 90 CYS -147.6 172.5 179.9 21.8 91 MET -85.5 46.6 -179.9 -71.9 -60.8 118.2 92 ASP 56.9 -93.8 -179.9 170.0 48.8 93 GLU 43.5 -94.7 179.4 174.6 -165.7 65.9 94 SER -85.7 88.2 -179.2 42.3 95 ASN -31.9 85.9 179.6 52.7 -11.2 96 LEU 29.5 57.0 180.0 -106.4 179.8 97 ARG -91.3 -51.0 -179.7 -164.5 -165.4 142.5 -173.6 98 ASP -92.8 -64.1 -179.8 -114.8 -66.2 99 LEU -44.0 -40.1 179.8 -80.3 -175.3 100 ASN -61.6 -49.3 179.5 -144.4 66.1 101 ARG -89.8 14.6 -180.0 -122.0 -83.9 -158.9 48.4 102 LYS -86.2 -40.4 179.9 169.0 47.7 69.1 -140.8 103 SER -65.9 -11.8 180.0 95.6 104 ASN -72.4 -36.8 180.0 -111.0 -112.5 105 GLN -99.2 8.6 179.8 60.4 149.7 -100.5 106 VAL -83.5 129.2 179.3 168.1 107 LYS -62.5 89.0 -179.5 173.0 81.9 148.2 86.0 108 ASN 74.0 71.1 -179.4 -154.8 66.5 109 CYS -85.0 143.7 179.9 -133.0 110 ARG -143.8 13.6 -179.8 108.4 -168.9 -93.3 156.6 111 ALA -89.8 97.2 179.0 112 LYS -46.7 123.6 -179.1 -95.4 -178.8 165.1 -131.3 113 ILE -99.4 139.6 179.7 -28.4 -74.9 114 GLU -167.1 -177.4 180.0 -114.0 138.3 -35.4 115 LEU -134.0 145.7 180.0 47.0 155.1 116 LEU -43.2 152.5 180.0 -122.4 107.2 117 GLY -158.4 -143.8 -180.0 118 SER -87.2 109.2 180.0 35.7 119 TYR -112.3 -82.0 180.0 -81.1 -53.8 120 ASP -61.6 -61.5 -180.0 -103.6 61.6 121 PRO -71.8 -161.7 -180.0 25.2 -31.2 122 GLN -144.4 36.6 -179.9 -63.7 -157.4 -91.2 123 LYS -111.5 159.1 180.0 34.3 178.7 63.0 174.2 124 GLN -87.7 81.9 179.9 50.6 -100.9 111.8 125 LEU -109.5 112.8 -179.9 -152.9 114.3 126 ILE -124.8 152.4 179.8 -80.6 -70.4 127 ILE -92.3 64.7 -179.7 -32.2 -56.8 128 GLU -85.6 46.7 179.8 -95.7 -149.7 47.9 129 ASP -127.2 144.8 -179.9 -91.1 -60.7 130 PRO -71.7 -42.9 180.0 25.4 -31.5 131 TYR -169.0 178.4 180.0 -111.8 -51.8 132 TYR -125.0 12.7 180.0 -52.4 -49.0 133 GLY 96.5 -115.7 179.9 134 ASN -169.7 -48.2 179.9 -128.7 -57.6 135 ASP -102.3 159.7 -179.9 -55.4 32.9 136 ALA 74.2 5.9 -180.0 137 ASP -177.4 120.9 180.0 43.0 64.8 138 PHE -170.8 -50.3 179.9 -144.4 79.9 139 GLU -66.7 -28.6 180.0 50.5 148.7 -8.8 140 THR -62.2 -43.9 179.8 -53.3 141 VAL -61.6 -57.2 179.8 166.2 142 TYR -46.5 -38.2 -179.8 160.4 -76.0 143 GLN -68.9 -39.3 180.0 -105.7 128.2 96.7 144 GLN -68.7 -13.1 179.9 -103.6 -88.9 -43.3 145 CYS -88.1 -12.6 180.0 -95.4 146 VAL -58.5 -60.4 179.9 176.0 147 ARG -74.4 -18.5 179.9 -45.6 107.7 118.9 130.6 148 CYS -46.7 -32.2 179.7 -96.5 149 CYS -114.1 -30.0 179.6 35.1 150 ARG -75.2 -57.7 179.7 -159.7 -161.9 179.2 -122.2 151 ALA -51.8 -31.5 180.0 152 PHE -83.4 -29.4 179.9 153.0 -84.0 153 LEU -66.0 -18.1 179.5 157.8 66.0 154 GLU -70.1 -45.4 179.5 -61.0 -98.8 72.2 155 LYS -64.9 -46.4 179.6 -110.5 -63.9 121.3 140.9 156 VAL -95.3 25.2 -179.9 -74.0 157 ARG -57.0 148.1 0.0 -141.2 -99.0 -72.5 -169.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA -16.897 23.085 1.781 2 GLU -16.353 20.159 4.179 3 GLN -13.541 17.852 3.001 4 VAL -13.774 14.095 3.663 5 THR -11.293 11.719 5.334 6 LYS -10.816 9.437 2.302 7 SER -9.497 5.966 3.227 8 VAL -7.026 3.675 1.429 9 LEU -5.180 0.448 2.316 10 PHE -2.343 -1.142 0.312 11 VAL -1.786 -4.916 0.423 12 CYS 0.752 -7.413 -0.962 13 LEU 2.183 -10.778 0.140 14 GLY 5.394 -10.298 2.154 15 ASN 4.919 -6.873 3.782 16 ILE 8.683 -6.729 4.435 17 CYS 11.228 -5.461 1.877 18 ARG 9.892 -4.252 -1.496 19 SER 6.253 -3.773 -0.428 20 PRO 5.916 -1.743 2.763 21 ILE 7.559 1.184 0.926 22 ALA 4.436 2.254 -1.006 23 GLU 2.663 2.316 2.383 24 ALA 5.011 4.464 4.499 25 VAL 5.113 6.559 1.310 26 PHE 1.354 7.226 1.135 27 ARG 1.889 8.615 4.651 28 LYS 4.659 11.062 3.662 29 LEU 2.300 12.047 0.824 30 VAL -0.674 12.641 3.142 31 THR 1.537 14.432 5.706 32 ASP 2.846 17.060 3.259 33 GLN -0.278 18.928 2.093 34 ASN -2.673 19.496 5.038 35 ILE -4.048 16.238 3.638 36 SER -3.049 13.953 6.536 37 ASP -6.078 15.145 8.540 38 ASN -8.353 13.740 5.809 39 TRP -7.049 10.225 5.092 40 VAL -7.080 6.741 6.637 41 ILE -4.177 4.934 4.942 42 ASP -2.947 1.595 6.327 43 SER -0.851 -1.404 5.216 44 GLY -2.050 -4.959 4.480 45 ALA 0.046 -8.153 4.529 46 VAL -2.732 -10.581 3.509 47 SER -0.727 -13.355 5.220 48 ASP -0.096 -14.476 8.817 49 TRP 3.675 -15.065 8.567 50 ASN 4.683 -11.381 8.426 51 VAL 2.194 -10.329 11.127 52 GLY 4.262 -7.777 13.080 53 ARG 7.426 -8.406 11.030 54 SER 8.774 -4.832 10.917 55 PRO 10.509 -3.876 7.684 56 ASP 13.878 -5.586 7.096 57 PRO 16.980 -3.810 8.364 58 ARG 17.644 -3.022 4.681 59 ALA 14.333 -1.291 3.880 60 VAL 14.073 0.023 7.461 61 SER 17.015 2.463 7.435 62 CYS 16.048 3.546 3.901 63 LEU 12.408 4.588 4.412 64 ARG 13.461 5.935 7.836 65 ASN 16.281 8.045 6.352 66 HIS 14.817 10.216 3.569 67 GLY 11.669 10.929 5.617 68 ILE 8.771 8.473 5.203 69 ASN 7.339 8.239 8.744 70 THR 6.514 4.579 9.477 71 ALA 4.533 4.176 12.721 72 HIS 2.275 1.210 11.877 73 LYS 2.462 -2.594 12.201 74 ALA 1.997 -4.758 9.084 75 ARG -0.374 -7.229 10.783 76 GLN -2.627 -9.450 8.638 77 VAL -5.432 -7.486 6.936 78 THR -8.878 -8.385 8.330 79 LYS -12.550 -7.842 7.415 80 GLU -12.329 -4.659 9.517 81 ASP -9.532 -3.295 7.299 82 PHE -11.587 -4.211 4.215 83 VAL -14.967 -2.544 4.844 84 THR -13.138 0.117 6.882 85 PHE -10.802 1.428 4.163 86 ASP -12.362 2.017 0.727 87 TYR -9.369 1.862 -1.645 88 ILE -7.867 -1.564 -0.910 89 LEU -5.227 -1.946 -3.647 90 CYS -2.113 -4.146 -3.837 91 MET 1.313 -4.286 -5.521 92 ASP -0.089 -6.476 -8.321 93 GLU 2.053 -9.563 -7.590 94 SER -0.925 -11.939 -7.267 95 ASN -3.201 -10.443 -9.973 96 LEU -6.122 -9.825 -7.561 97 ARG -6.283 -13.571 -6.836 98 ASP -6.951 -13.600 -3.072 99 LEU -7.757 -9.988 -2.120 100 ASN -10.195 -10.029 -5.061 101 ARG -11.980 -13.129 -3.721 102 LYS -11.239 -11.938 -0.169 103 SER -14.119 -9.439 0.087 104 ASN -16.371 -12.409 -0.751 105 GLN -15.802 -14.002 2.675 106 VAL -15.543 -10.608 4.417 107 LYS -18.465 -9.908 6.780 108 ASN -19.810 -6.942 4.779 109 CYS -16.775 -5.992 2.660 110 ARG -16.616 -2.470 1.181 111 ALA -12.905 -2.092 0.321 112 LYS -12.768 -1.677 -3.472 113 ILE -9.992 -4.108 -4.437 114 GLU -7.547 -3.317 -7.258 115 LEU -3.815 -3.131 -8.051 116 LEU -1.522 -0.177 -8.827 117 GLY -1.508 0.667 -12.555 118 SER -1.097 3.670 -14.880 119 TYR -1.997 6.809 -12.893 120 ASP 0.225 9.861 -13.480 121 PRO 1.955 8.495 -16.571 122 GLN 0.177 6.433 -19.256 123 LYS 2.264 3.253 -19.624 124 GLN 1.356 -0.334 -18.668 125 LEU 3.733 -0.822 -15.716 126 ILE 2.693 -3.576 -13.282 127 ILE 4.657 -5.332 -10.512 128 GLU 4.049 -8.881 -11.793 129 ASP 7.251 -10.134 -10.132 130 PRO 7.719 -12.325 -7.069 131 TYR 10.874 -10.521 -5.885 132 TYR 14.110 -8.879 -7.081 133 GLY 16.613 -10.772 -4.899 134 ASN 18.229 -8.515 -2.274 135 ASP 21.589 -7.109 -3.428 136 ALA 22.238 -5.203 -6.676 137 ASP 18.680 -3.839 -6.359 138 PHE 16.714 -2.318 -3.454 139 GLU 16.593 1.500 -3.578 140 THR 14.912 1.249 -7.001 141 VAL 11.883 -0.512 -5.472 142 TYR 11.501 1.979 -2.603 143 GLN 11.509 4.666 -5.327 144 GLN 8.787 2.872 -7.323 145 CYS 6.716 2.954 -4.114 146 VAL 6.802 6.772 -4.031 147 ARG 4.067 7.217 -6.659 148 CYS 2.593 3.859 -5.590 149 CYS 0.583 5.978 -3.128 150 ARG 1.117 9.492 -4.548 151 ALA 0.280 8.739 -8.196 152 PHE -2.799 6.970 -6.788 153 LEU -3.608 9.800 -4.352 154 GLU -4.186 11.923 -7.477 155 LYS -7.184 9.839 -8.595 156 VAL -8.589 9.732 -5.047 157 ARG -7.231 13.228 -4.338 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 S 10 S S S S C T T T T H 20 H H H H H H H H H H 30 H H/T T T T/T T T T/S S S 40 S S S S S S/S S S S C 50 C S S S S H H H H H 60 H H H H H 3 3/S S S S 70 S/S S S S S S S S/H H H 80 H H H H H S S S S S 90 S T T T T C H H H H 100 H H/T T T T C S S S S 110 S S S S S S C T T T 120 T/S S S S/S S S S C C C 130 C C C T T T T H H H 140 H H H H H H C H H H 150 H H H H 3 3/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E 10 E e S S S S h H 20 H H H H H H H H H H 30 h S S S g G G e E E 40 E E E E S S S t 50 T T t h H H H H 60 H H H H H H h t 70 h H H 80 H H H H h e E E E E 90 e S S t T T h H H H 100 H H h T t t T T t 110 E E E E e S S S 120 S S S 130 S S S h H H 140 H H H H H H H H H H 150 H H H H H h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 86.8 2 GLU 0.9 0.7 88.3 3 GLN 32.7 22.0 85.5 4 VAL 12.3 10.4 86.1 5 THR 44.5 41.6 73.2 6 LYS 115.3 66.5 64.1 7 SER 66.5 79.5 52.3 8 VAL 118.8 100.0 26.1 9 LEU 147.8 100.0 36.3 10 PHE 164.9 98.9 37.6 11 VAL 118.6 99.8 36.4 12 CYS 92.6 93.3 61.6 13 LEU 76.4 51.7 67.9 14 GLY 22.6 64.9 75.0 15 ASN 113.8 94.2 53.1 16 ILE 116.9 81.5 66.1 17 CYS 90.5 91.3 39.9 18 ARG 196.5 94.0 34.7 19 SER 82.9 99.2 55.9 20 PRO 117.1 94.0 57.9 21 ILE 141.4 98.5 36.4 22 ALA 72.5 99.9 35.3 23 GLU 125.3 90.4 59.1 24 ALA 64.2 88.4 48.8 25 VAL 115.9 97.6 38.3 26 PHE 166.8 100.0 24.5 27 ARG 107.9 51.6 74.2 28 LYS 100.6 58.0 70.3 29 LEU 126.1 85.3 49.6 30 VAL 116.9 98.4 45.3 31 THR 56.3 52.7 64.3 32 ASP 30.9 27.9 83.3 33 GLN 21.5 14.5 82.7 34 ASN 0.0 0.0 89.2 35 ILE 124.8 87.0 53.0 36 SER 53.6 64.1 60.4 37 ASP 2.1 1.9 88.4 38 ASN 90.9 75.2 61.6 39 TRP 200.9 98.0 34.6 40 VAL 60.4 50.8 63.2 41 ILE 139.8 97.4 41.8 42 ASP 77.1 69.8 58.1 43 SER 74.9 89.6 60.5 44 GLY 34.8 99.9 54.0 45 ALA 72.6 100.0 59.9 46 VAL 100.7 84.7 41.5 47 SER 74.5 89.1 53.6 48 ASP 26.8 24.2 73.1 49 TRP 48.3 23.6 81.1 50 ASN 107.1 88.6 41.7 51 VAL 85.4 71.9 66.0 52 GLY 22.0 63.2 63.2 53 ARG 100.8 48.2 77.3 54 SER 24.5 29.3 67.4 55 PRO 101.0 81.1 52.9 56 ASP 67.2 60.8 55.9 57 PRO 27.7 22.3 75.0 58 ARG 84.2 40.3 72.0 59 ALA 69.9 96.2 43.4 60 VAL 74.9 63.1 59.9 61 SER 19.7 23.6 76.1 62 CYS 53.1 53.5 63.3 63 LEU 146.7 99.2 34.6 64 ARG 52.6 25.2 75.2 65 ASN 35.6 29.4 82.6 66 HIS 34.7 23.1 86.3 67 GLY 7.6 21.8 83.2 68 ILE 138.8 96.7 42.8 69 ASN 43.7 36.2 65.2 70 THR 82.6 77.3 52.1 71 ALA 0.0 0.0 88.1 72 HIS 76.0 50.6 84.3 73 LYS 75.5 43.5 78.5 74 ALA 70.1 96.5 71.5 75 ARG 71.9 34.4 74.9 76 GLN 81.9 55.1 66.8 77 VAL 115.5 97.2 41.8 78 THR 32.2 30.1 78.4 79 LYS 104.3 60.1 55.9 80 GLU 34.9 25.2 80.4 81 ASP 80.3 72.7 50.1 82 PHE 162.6 97.5 32.3 83 VAL 96.8 81.5 61.6 84 THR 62.4 58.4 54.9 85 PHE 158.3 94.9 45.8 86 ASP 62.5 56.6 66.9 87 TYR 137.7 76.1 42.8 88 ILE 143.5 100.0 34.9 89 LEU 139.5 94.4 44.0 90 CYS 92.6 93.3 44.8 91 MET 155.7 97.7 33.0 92 ASP 109.1 98.7 38.7 93 GLU 110.7 79.9 64.6 94 SER 34.1 40.7 75.0 95 ASN 24.9 20.6 76.3 96 LEU 122.4 82.8 52.5 97 ARG 30.4 14.6 88.2 98 ASP 35.3 32.0 76.0 99 LEU 139.5 94.4 26.1 100 ASN 55.5 45.9 64.0 101 ARG 42.1 20.2 88.6 102 LYS 130.4 75.2 59.4 103 SER 58.2 69.6 55.5 104 ASN 35.4 29.3 83.9 105 GLN 35.3 23.7 82.6 106 VAL 115.3 97.0 44.0 107 LYS 8.8 5.1 80.8 108 ASN 19.7 16.3 78.7 109 CYS 95.4 96.2 48.4 110 ARG 60.8 29.1 82.3 111 ALA 72.6 100.0 48.0 112 LYS 25.7 14.8 86.2 113 ILE 132.4 92.3 48.0 114 GLU 52.5 37.9 60.5 115 LEU 107.7 72.9 52.8 116 LEU 128.6 87.0 45.4 117 GLY 17.7 51.0 68.1 118 SER 44.9 53.7 73.3 119 TYR 139.0 76.8 51.9 120 ASP 49.6 44.9 63.9 121 PRO 59.1 47.5 61.0 122 GLN 4.2 2.8 83.8 123 LYS 53.2 30.7 71.9 124 GLN 0.0 0.0 85.1 125 LEU 64.4 43.6 75.3 126 ILE 100.5 70.1 58.5 127 ILE 122.0 85.0 63.5 128 GLU 36.6 26.4 79.2 129 ASP 44.4 40.1 69.9 130 PRO 23.8 19.1 83.5 131 TYR 96.8 53.5 65.5 132 TYR 116.8 64.5 54.2 133 GLY 0.0 0.0 79.8 134 ASN 46.6 38.5 72.3 135 ASP 16.5 14.9 84.9 136 ALA 0.0 0.0 84.6 137 ASP 66.9 60.5 71.0 138 PHE 142.5 85.4 55.7 139 GLU 23.8 17.2 84.2 140 THR 21.0 19.7 71.9 141 VAL 99.5 83.8 42.0 142 TYR 152.6 84.3 39.6 143 GLN 61.1 41.1 67.5 144 GLN 87.7 59.0 60.7 145 CYS 95.1 95.8 45.5 146 VAL 69.5 58.5 50.8 147 ARG 71.3 34.1 73.8 148 CYS 97.2 98.0 37.0 149 CYS 99.2 100.0 40.0 150 ARG 87.6 41.9 65.5 151 ALA 66.4 91.5 44.2 152 PHE 161.1 96.6 29.2 153 LEU 133.4 90.2 41.1 154 GLU 70.3 50.8 78.6 155 LYS 33.8 19.5 78.1 156 VAL 97.3 81.9 43.6 157 ARG 50.8 24.3 82.7