Protein Data Bank File : 1fsib Title : HYDROLASE 10-SEP-00 1FSI Number of Amino Acid Residues : 170 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET GLU GLU VAL LYS LYS ASP VAL TYR SER 10 VAL TRP ALA LEU PRO ASP GLU GLU SER GLU 20 PRO ARG PHE LYS LYS LEU MET GLU ALA LEU 30 ARG SER GLU PHE THR GLY PRO ARG PHE VAL 40 PRO HIS VAL THR VAL ALA VAL SER ALA TYR 50 LEU THR ALA ASP GLU ALA LYS LYS MET PHE 60 GLU SER ALA CYS ASP GLY LEU LYS ALA TYR 70 THR ALA THR VAL ASP ARG VAL SER THR GLY 80 THR PHE PHE PHE GLN CYS VAL PHE LEU LEU 90 LEU GLN THR THR PRO GLU VAL MET GLU ALA 100 GLY GLU THR PRO TYR MET PRO HIS LEU SER 110 LEU LEU TYR ALA GLU LEU THR GLU GLU GLU 120 LYS LYS ASN ALA GLN GLU LYS ALA TYR THR 130 LEU ASP SER SER LEU ASP GLY LEU SER PHE 140 ARG LEU ASN ARG LEU ALA LEU CYS LYS THR 150 ASP THR GLU ASP LYS THR LEU GLU THR TRP 160 GLU THR VAL ALA VAL CYS ASN LEU ASN PRO Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 128.5 -178.2 -166.7 -123.8 90.7 2 GLU -124.1 122.2 177.9 -171.7 173.6 -15.7 3 GLU -79.2 125.7 -173.5 -59.1 -157.8 -35.3 4 VAL -108.5 -23.4 176.3 89.6 5 LYS -80.5 131.6 177.3 179.2 -178.0 163.3 52.4 6 LYS -130.6 139.4 178.8 -59.4 -162.1 -167.1 -174.0 7 ASP -135.3 167.3 178.1 -55.4 82.2 8 VAL -92.3 123.6 179.4 165.1 9 TYR -107.7 162.3 178.5 -68.1 77.2 10 SER -136.3 139.9 179.3 -49.7 11 VAL -105.5 130.1 -178.1 170.5 12 TRP -117.0 131.1 175.4 -72.2 -5.2 13 ALA -91.6 129.1 -179.1 14 LEU -103.5 144.0 179.1 -48.0 -174.0 15 PRO -72.4 157.4 -179.5 32.4 -43.5 16 ASP -62.0 172.4 179.6 57.4 48.9 17 GLU -70.9 -20.4 -178.9 -87.9 -56.0 -46.8 18 GLU -79.3 -34.2 -177.8 -51.5 82.2 78.6 19 SER -91.6 -21.4 -178.7 73.8 20 GLU -55.2 -53.5 -179.5 179.6 165.2 -58.5 21 PRO -47.6 -49.0 -178.6 -26.0 38.8 22 ARG -55.4 -52.4 -179.2 -172.3 179.9 -173.9 159.5 23 PHE -62.5 -39.0 -179.5 -64.3 131.3 24 LYS -66.5 -45.3 178.9 -74.7 -175.4 -171.8 -156.3 25 LYS -52.9 -51.1 177.7 168.7 -164.9 145.6 -59.7 26 LEU -56.5 -44.6 -177.4 -132.5 -164.4 27 MET -70.5 -26.1 -178.6 -74.7 170.5 -113.5 28 GLU -81.8 -35.5 -179.7 -146.0 -108.6 58.8 29 ALA -75.1 -33.4 -179.5 30 LEU -67.1 -40.2 -178.1 -74.0 174.7 31 ARG -69.0 -18.8 178.5 -177.0 180.0 81.0 83.5 32 SER -89.8 -46.7 -179.5 -168.9 33 GLU -66.9 -37.2 176.7 157.6 168.5 19.3 34 PHE -98.9 -144.4 177.4 -64.9 80.0 35 THR -130.4 -165.7 177.1 172.0 36 GLY 131.7 139.5 180.0 37 PRO -60.2 156.5 179.3 33.2 -38.5 38 ARG -96.5 136.2 175.8 149.5 91.4 89.2 -129.6 39 PHE -154.4 156.5 180.0 62.6 -76.2 40 VAL -78.5 150.7 -179.6 -54.2 41 PRO -65.7 140.4 -178.4 27.0 -40.9 42 HIS -161.6 160.6 177.1 62.0 -69.3 43 VAL -125.7 109.4 -176.7 -177.9 44 THR -70.3 121.3 -179.8 -53.7 45 VAL -103.1 -25.3 177.3 -68.3 46 ALA -156.2 154.6 174.4 47 VAL -131.5 133.4 -179.1 169.4 48 SER -95.0 -179.6 176.2 69.7 49 ALA -89.9 -155.6 -179.6 50 TYR -87.3 120.2 -179.6 -89.9 91.1 51 LEU -121.1 145.1 176.5 -54.2 -175.4 52 THR -83.2 171.5 -178.7 82.8 53 ALA -56.0 -49.1 177.5 54 ASP -52.0 -52.3 177.2 -92.2 169.8 55 GLU -55.6 -48.9 -177.6 -76.1 155.6 178.2 56 ALA -55.2 -47.1 -179.7 57 LYS -58.8 -50.2 -179.7 174.6 -171.0 -158.0 -172.7 58 LYS -59.3 -38.8 178.3 -70.6 -179.9 178.1 -177.0 59 MET -65.2 -37.6 -178.4 -174.0 -105.7 -30.4 60 PHE -66.7 -51.2 178.3 -164.6 -138.9 61 GLU -51.3 -45.3 -179.8 -78.8 168.4 160.6 62 SER -61.1 -37.9 178.2 173.3 63 ALA -79.1 -35.9 178.1 64 CYS -65.8 -42.8 -178.5 -69.2 65 ASP -67.0 -39.5 -176.8 -77.2 164.8 66 GLY -97.4 -4.6 -179.3 67 LEU -104.6 135.7 -176.9 -167.8 -73.1 68 LYS -96.2 138.1 176.0 69.2 -57.5 172.5 167.4 69 ALA -47.3 140.3 -178.8 70 TYR -139.3 172.4 -179.6 68.6 107.9 71 THR -114.1 128.4 178.0 -83.2 72 ALA -112.9 151.3 178.1 73 THR -129.6 135.4 -177.9 -53.6 74 VAL -71.9 112.2 174.9 173.7 75 ASP -71.2 -59.7 -180.0 162.9 38.6 76 ARG -165.9 179.3 178.2 67.3 -164.1 -137.6 -96.1 77 VAL -97.0 117.6 -177.5 178.7 78 SER -114.0 173.1 -176.4 -137.1 79 THR -128.5 157.2 -177.8 -102.0 80 GLY -133.6 -172.6 -177.8 81 THR -110.1 1.8 175.3 74.0 82 PHE -142.0 175.3 -174.4 68.9 -77.7 83 PHE -48.1 -43.9 -177.8 176.9 -91.2 84 PHE -83.8 -3.1 178.5 -69.8 110.8 85 GLN -135.7 69.3 179.4 -76.7 177.7 29.2 86 CYS -95.1 -73.8 178.2 -177.3 87 VAL -128.4 128.2 -177.1 -178.6 88 PHE -155.3 152.6 178.7 55.7 -84.2 89 LEU -87.8 109.6 177.5 -57.3 169.3 90 LEU -71.8 125.7 179.5 -166.3 62.2 91 LEU -95.7 162.8 178.8 -43.8 171.8 92 GLN -65.4 126.6 178.5 -56.0 -85.9 -162.5 93 THR -73.0 49.8 178.9 68.3 94 THR -74.7 155.5 179.8 73.3 95 PRO -48.5 -65.9 -179.4 26.6 -44.6 96 GLU -42.9 -49.9 177.8 -111.7 -166.6 -42.3 97 VAL -61.6 -61.2 -179.7 158.7 98 MET -59.2 -30.4 -178.2 -59.9 -65.7 -53.1 99 GLU -61.6 -63.0 178.8 -80.3 -149.7 73.0 100 ALA -32.9 -33.6 179.5 101 GLY -95.0 24.1 178.9 102 GLU -144.0 149.6 -4.3 0.0 0.0 0.0 103 THR 20.6 143.1 179.9 -55.6 104 PRO -78.3 122.6 178.9 34.1 -44.2 105 TYR -52.6 106.6 179.1 -176.3 -145.6 106 MET -104.2 82.6 -179.4 170.8 -152.5 -105.2 107 PRO -51.7 128.3 -177.1 31.5 -39.9 108 HIS -160.8 156.8 178.2 61.0 -91.0 109 LEU -117.1 102.2 -178.0 -176.2 157.7 110 SER -61.9 137.1 180.0 -61.8 111 LEU -100.8 -38.0 -178.3 -70.9 -177.5 112 LEU -144.0 145.9 176.4 170.7 66.9 113 TYR -118.8 125.4 -178.0 -67.5 147.5 114 ALA -173.2 158.2 177.0 115 GLU -110.3 102.5 -175.3 -81.6 162.0 -27.1 116 LEU -117.4 155.4 177.1 -89.3 25.5 117 THR -71.7 167.5 -179.2 62.4 118 GLU -57.9 -39.3 179.8 -162.0 57.8 -78.6 119 GLU -67.5 -54.7 178.2 -166.4 -177.7 -157.3 120 GLU -59.3 -34.1 179.2 -66.3 176.6 122.1 121 LYS -60.9 -50.1 178.8 -156.1 -177.4 -59.3 156.1 122 LYS -55.0 -40.8 178.0 -82.1 -41.8 87.8 170.3 123 ASN -58.9 -52.0 -178.0 -86.9 141.2 124 ALA -58.8 -43.2 177.7 125 GLN -58.9 -45.2 -178.7 171.2 169.4 49.2 126 GLU -69.3 -39.9 -179.2 -119.2 -48.8 -77.3 127 LYS -57.5 -26.1 -179.5 -169.5 53.0 -179.2 174.6 128 ALA -67.4 -49.9 -179.3 129 TYR -65.7 -29.8 -179.8 -75.8 113.9 130 THR -66.5 -41.5 179.7 -78.0 131 LEU -78.4 -25.8 -179.7 -66.8 178.9 132 ASP -152.7 86.3 -174.8 -168.4 -37.4 133 SER -73.0 -16.2 178.7 41.1 134 SER -97.1 23.9 179.7 50.0 135 LEU -61.0 -48.6 178.6 -112.4 18.2 136 ASP -57.6 130.9 -178.1 -72.7 15.9 137 GLY 86.9 -10.9 -179.4 138 LEU -63.4 128.1 179.5 -162.6 -171.7 139 SER -109.7 139.7 179.5 -88.7 140 PHE -148.5 155.5 -179.2 60.6 102.3 141 ARG -89.2 132.7 177.6 -150.4 68.4 179.2 134.5 142 LEU -110.4 97.6 -177.3 -74.0 160.6 143 ASN -114.3 25.0 179.7 54.9 51.6 144 ARG -160.2 153.4 176.1 -70.0 -166.5 -69.8 163.8 145 LEU -121.2 154.7 175.4 -71.3 -178.7 146 ALA -130.9 136.1 176.4 147 LEU -94.9 120.7 -177.2 -151.8 -143.4 148 CYS -133.9 159.8 174.9 -42.3 149 LYS -108.0 124.1 178.6 -81.4 -174.8 176.0 101.8 150 THR -145.9 95.0 178.6 53.2 151 ASP -67.7 97.7 -179.8 159.8 14.1 152 THR -56.8 4.1 -179.5 28.9 153 GLU -112.8 14.0 177.4 -59.9 179.8 23.9 154 ASP -107.5 95.0 -177.4 167.8 -161.6 155 LYS -77.0 7.2 177.1 -31.7 -177.0 175.8 159.4 156 THR -97.4 -18.0 -178.2 43.0 157 LEU 59.9 10.5 179.6 -48.5 -178.7 158 GLU -63.6 -32.9 179.8 -66.3 -176.7 79.3 159 THR -72.3 -24.1 -175.4 -92.1 160 TRP -71.8 138.0 177.0 -68.7 18.0 161 GLU -150.2 144.5 179.4 28.8 -140.5 50.2 162 THR -92.5 116.2 -179.2 -50.8 163 VAL -87.0 -46.7 178.5 38.8 164 ALA -151.7 161.7 178.4 165 VAL -136.4 149.1 -179.4 -45.0 166 CYS -140.3 142.2 178.1 75.7 167 ASN -75.8 143.1 177.7 -68.3 -57.1 168 LEU -95.4 153.5 178.6 -70.1 176.5 169 ASN -91.1 141.7 -179.5 -78.1 -40.1 170 PRO -43.9 -42.0 0.0 26.3 -43.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 71.911 51.942 65.643 2 GLU 69.287 49.945 67.588 3 GLU 69.402 48.793 71.271 4 VAL 67.944 45.345 71.161 5 LYS 68.399 44.197 74.763 6 LYS 65.580 45.058 77.260 7 ASP 65.391 44.429 81.027 8 VAL 63.047 45.208 83.881 9 TYR 64.321 48.014 86.104 10 SER 63.469 49.101 89.665 11 VAL 64.072 52.479 91.195 12 TRP 65.213 52.576 94.763 13 ALA 65.116 55.509 97.158 14 LEU 68.115 55.253 99.497 15 PRO 68.385 56.426 103.109 16 ASP 70.759 59.312 104.195 17 GLU 74.224 58.687 105.569 18 GLU 73.140 59.073 109.152 19 SER 70.518 56.376 108.907 20 GLU 72.245 53.957 106.538 21 PRO 74.616 52.463 109.160 22 ARG 71.713 51.773 111.500 23 PHE 69.513 49.914 109.048 24 LYS 72.539 47.869 107.945 25 LYS 73.538 46.836 111.467 26 LEU 69.907 45.603 111.968 27 MET 69.858 43.863 108.594 28 GLU 73.066 42.123 109.267 29 ALA 72.105 40.790 112.616 30 LEU 68.656 39.660 111.457 31 ARG 70.301 38.050 108.487 32 SER 72.679 36.178 110.721 33 GLU 70.238 34.771 113.311 34 PHE 67.720 33.849 110.675 35 THR 69.208 33.329 107.354 36 GLY 69.262 35.447 104.229 37 PRO 70.969 37.176 101.284 38 ARG 72.792 40.392 101.899 39 PHE 71.399 43.587 100.360 40 VAL 71.446 47.401 101.019 41 PRO 68.576 49.256 102.727 42 HIS 66.148 50.762 100.306 43 VAL 62.573 51.927 99.697 44 THR 61.389 50.823 96.288 45 VAL 59.604 53.610 94.395 46 ALA 59.116 52.085 90.909 47 VAL 59.390 48.990 88.733 48 SER 59.432 49.329 84.926 49 ALA 58.229 47.391 81.932 50 TYR 60.913 46.192 79.571 51 LEU 63.362 49.019 78.817 52 THR 66.441 49.271 76.736 53 ALA 69.392 50.920 78.503 54 ASP 68.659 54.286 76.844 55 GLU 64.969 54.264 77.902 56 ALA 66.002 53.218 81.361 57 LYS 68.425 56.106 81.591 58 LYS 65.942 58.690 80.370 59 MET 63.421 57.273 82.807 60 PHE 66.068 57.497 85.542 61 GLU 67.044 61.088 84.754 62 SER 63.406 62.038 84.761 63 ALA 62.882 60.613 88.234 64 CYS 66.148 62.079 89.501 65 ASP 65.312 65.460 88.050 66 GLY 61.751 65.621 89.297 67 LEU 61.839 63.946 92.714 68 LYS 62.656 65.889 95.802 69 ALA 64.601 64.544 98.776 70 TYR 61.991 63.403 101.242 71 THR 61.249 62.159 104.759 72 ALA 59.861 58.770 105.673 73 THR 58.693 57.722 109.080 74 VAL 58.539 54.276 110.496 75 ASP 55.012 53.302 111.379 76 ARG 56.163 49.884 112.655 77 VAL 57.985 46.606 112.048 78 SER 55.768 44.310 110.058 79 THR 55.734 40.817 108.658 80 GLY 54.658 39.354 105.362 81 THR 53.782 36.133 103.545 82 PHE 56.521 35.542 101.012 83 PHE 60.301 35.840 100.679 84 PHE 60.559 39.499 99.775 85 GLN 58.207 40.542 102.527 86 CYS 59.490 38.668 105.510 87 VAL 60.438 41.381 107.985 88 PHE 60.242 45.039 107.056 89 LEU 59.725 48.511 108.384 90 LEU 56.262 49.602 107.205 91 LEU 56.328 53.401 106.558 92 GLN 53.810 56.168 107.213 93 THR 51.532 56.559 104.225 94 THR 52.371 60.304 104.140 95 PRO 51.957 62.352 100.937 96 GLU 55.666 62.961 100.041 97 VAL 56.327 59.219 100.582 98 MET 53.285 57.771 98.755 99 GLU 53.880 60.296 96.035 100 ALA 57.427 59.181 95.361 101 GLY 55.789 55.815 94.553 102 GLU 53.204 56.601 91.772 103 THR 48.085 47.002 93.317 104 PRO 48.265 49.682 96.073 105 TYR 51.766 51.033 96.857 106 MET 52.852 49.807 100.374 107 PRO 56.061 51.856 101.100 108 HIS 58.550 49.881 103.204 109 LEU 62.204 49.346 103.903 110 SER 62.787 45.566 103.923 111 LEU 64.950 44.248 106.726 112 LEU 65.174 40.573 105.837 113 TYR 64.307 38.322 102.851 114 ALA 63.612 34.726 103.905 115 GLU 61.124 31.836 103.865 116 LEU 60.298 31.287 107.494 117 THR 57.644 29.367 109.374 118 GLU 55.040 31.571 111.080 119 GLU 56.807 31.105 114.417 120 GLU 60.359 31.976 113.262 121 LYS 58.696 34.943 111.536 122 LYS 57.238 36.157 114.856 123 ASN 60.702 35.694 116.365 124 ALA 62.424 37.721 113.729 125 GLN 59.950 40.539 114.151 126 GLU 60.584 40.570 117.887 127 LYS 64.278 40.177 117.440 128 ALA 64.036 43.394 115.491 129 TYR 62.699 45.472 118.386 130 THR 65.178 43.761 120.596 131 LEU 68.011 44.933 118.420 132 ASP 66.693 48.492 117.830 133 SER 63.861 49.403 120.198 134 SER 63.321 52.980 119.186 135 LEU 62.337 51.949 115.626 136 ASP 58.603 52.948 115.749 137 GLY 58.442 56.670 114.966 138 LEU 61.946 56.746 113.475 139 SER 62.225 59.405 110.758 140 PHE 64.796 59.411 108.103 141 ARG 65.785 61.226 104.988 142 LEU 65.727 59.581 101.502 143 ASN 68.107 61.729 99.450 144 ARG 69.217 59.513 96.587 145 LEU 67.915 57.131 94.017 146 ALA 69.430 54.013 92.476 147 LEU 68.488 52.515 89.076 148 CYS 68.665 48.674 89.333 149 LYS 67.979 45.446 87.419 150 THR 66.349 42.977 89.859 151 ASP 64.700 39.791 88.732 152 THR 62.367 39.411 91.757 153 GLU 62.121 35.738 91.319 154 ASP 65.801 35.375 91.967 155 LYS 66.024 34.832 95.687 156 THR 69.764 34.700 95.498 157 LEU 69.903 38.316 94.434 158 GLU 73.092 37.074 92.624 159 THR 71.296 38.619 89.656 160 TRP 70.679 42.017 91.189 161 GLU 72.702 45.018 90.106 162 THR 72.864 48.728 90.558 163 VAL 73.440 50.448 87.241 164 ALA 73.495 54.056 88.443 165 VAL 72.721 56.335 91.370 166 CYS 71.758 60.022 91.651 167 ASN 71.520 62.569 94.484 168 LEU 68.104 64.121 95.073 169 ASN 67.736 67.905 95.528 170 PRO 66.455 69.200 98.929 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 S S S C H H 20 H H H H H H H H H H 30 H H H H H S S S S S/S 40 S S S S S S S S S S 50 C H H H H H H H H H 60 H H H H H H H S S S 70 S S S S S S S S S S 80 C T T T T S S S S/S S 90 S S S H H H H H H H 100 H 3PX X/S S S S S S S/S S 110 S S/S S S S C H H H H 120 H H H H H H H H H H 130 H H H C C C S S S S 140 S S S S/S S S S S S/S S 150 S S C T T T T C S S 160 S S S S/S S S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E 10 E E E E E e T T h H 20 H H H H H H H H H H 30 H H H h 40 E E E E E E E E 50 E h H H H H H H H H 60 H H H H H H h B E 70 E E E E E E E E E E 80 E E T T E E E E E E 90 E e h H H H H H H 100 h t e E E E 110 E E h H H H 120 H H H H H H H H H H 130 H h T T t T T e E E 140 E E E E E E E E E e 150 t T T t T T t T T t 160 E E E E E E E e B Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 32.0 20.1 87.2 2 GLU 16.6 12.0 80.4 3 GLU 88.9 64.2 64.2 4 VAL 8.7 7.4 83.8 5 LYS 42.2 24.3 85.2 6 LYS 85.5 49.3 73.1 7 ASP 81.3 73.5 55.2 8 VAL 73.4 61.8 64.3 9 TYR 176.1 97.3 44.4 10 SER 77.6 92.9 56.4 11 VAL 115.7 97.4 30.3 12 TRP 187.4 91.4 38.5 13 ALA 72.6 100.0 40.1 14 LEU 131.0 88.7 50.2 15 PRO 124.1 99.7 44.7 16 ASP 101.5 91.9 66.8 17 GLU 34.1 24.6 85.0 18 GLU 14.1 10.2 81.0 19 SER 74.1 88.7 44.9 20 GLU 107.6 77.6 60.0 21 PRO 50.9 40.9 75.0 22 ARG 125.4 60.0 65.7 23 PHE 166.8 100.0 23.8 24 LYS 89.2 51.5 61.9 25 LYS 58.3 33.6 73.8 26 LEU 147.7 99.9 36.9 27 MET 151.4 95.0 47.4 28 GLU 66.4 47.9 80.4 29 ALA 41.0 56.5 65.7 30 LEU 147.8 100.0 34.6 31 ARG 147.3 70.5 68.5 32 SER 20.4 24.4 86.0 33 GLU 62.9 45.4 62.1 34 PHE 148.8 89.2 44.9 35 THR 21.0 19.6 75.2 36 GLY 29.5 84.6 56.6 37 PRO 97.6 78.4 54.6 38 ARG 91.6 43.8 75.5 39 PHE 149.8 89.8 50.4 40 VAL 52.5 44.2 59.8 41 PRO 123.9 99.5 31.3 42 HIS 142.5 94.9 46.5 43 VAL 118.3 99.6 44.4 44 THR 66.6 62.3 65.6 45 VAL 111.0 93.5 49.0 46 ALA 28.0 38.5 63.3 47 VAL 49.1 41.3 70.1 48 SER 68.7 82.2 52.4 49 ALA 2.9 4.0 74.6 50 TYR 50.1 27.7 69.7 51 LEU 119.5 80.8 49.3 52 THR 95.8 89.6 59.3 53 ALA 18.7 25.8 84.8 54 ASP 35.9 32.5 73.1 55 GLU 62.9 45.4 66.3 56 ALA 71.4 98.3 40.3 57 LYS 53.7 31.0 79.0 58 LYS 29.5 17.0 82.6 59 MET 103.5 65.0 48.1 60 PHE 154.7 92.7 39.1 61 GLU 60.1 43.4 65.2 62 SER 17.7 21.2 79.9 63 ALA 40.4 55.6 63.1 64 CYS 87.4 88.1 42.4 65 ASP 16.3 14.8 79.5 66 GLY 2.3 6.7 82.6 67 LEU 124.0 83.9 49.2 68 LYS 112.1 64.7 59.5 69 ALA 68.5 94.4 50.8 70 TYR 180.1 99.5 39.9 71 THR 60.5 56.6 73.0 72 ALA 72.6 100.0 34.4 73 THR 82.4 77.1 59.6 74 VAL 118.8 100.0 39.4 75 ASP 60.3 54.6 67.6 76 ARG 94.8 45.4 77.4 77 VAL 118.8 100.0 34.4 78 SER 74.8 89.4 59.8 79 THR 90.5 84.6 61.5 80 GLY 26.4 75.9 57.6 81 THR 9.1 8.5 82.3 82 PHE 64.9 38.9 75.6 83 PHE 150.3 90.1 40.0 84 PHE 144.2 86.5 36.3 85 GLN 98.8 66.5 51.6 86 CYS 97.3 98.1 49.8 87 VAL 118.8 100.0 36.4 88 PHE 165.0 98.9 43.5 89 LEU 147.8 100.0 24.5 90 LEU 121.0 81.9 57.2 91 LEU 147.7 99.9 38.3 92 GLN 81.4 54.8 63.8 93 THR 25.4 23.8 70.3 94 THR 58.9 55.1 59.3 95 PRO 21.8 17.5 77.0 96 GLU 75.4 54.4 66.1 97 VAL 118.1 99.4 46.4 98 MET 103.6 65.0 58.0 99 GLU 29.5 21.3 78.8 100 ALA 69.6 95.8 52.8 101 GLY 34.8 100.0 62.1 102 GLU 73.0 52.6 82.3 103 THR 4.1 3.8 83.4 104 PRO 12.6 10.1 80.3 105 TYR 135.8 75.0 61.3 106 MET 72.9 45.7 63.4 107 PRO 121.6 97.7 38.6 108 HIS 113.6 75.7 57.6 109 LEU 147.8 100.0 29.6 110 SER 79.1 94.6 55.2 111 LEU 147.8 100.0 26.3 112 LEU 146.3 99.0 37.1 113 TYR 173.8 96.0 30.9 114 ALA 70.0 96.4 35.9 115 GLU 52.5 37.8 72.7 116 LEU 140.6 95.1 42.8 117 THR 23.3 21.8 78.8 118 GLU 33.2 24.0 77.2 119 GLU 3.7 2.6 86.2 120 GLU 58.0 41.8 66.2 121 LYS 150.7 86.9 59.9 122 LYS 78.1 45.0 76.4 123 ASN 40.2 33.2 68.2 124 ALA 72.6 100.0 35.0 125 GLN 110.9 74.7 60.4 126 GLU 35.0 25.3 77.6 127 LYS 106.2 61.2 58.4 128 ALA 72.6 100.0 38.1 129 TYR 131.2 72.5 67.4 130 THR 45.5 42.6 75.6 131 LEU 109.4 74.0 57.9 132 ASP 94.4 85.4 61.8 133 SER 15.4 18.4 84.4 134 SER 13.5 16.2 91.6 135 LEU 147.8 100.0 39.7 136 ASP 50.5 45.7 69.1 137 GLY 5.5 15.9 75.7 138 LEU 127.1 86.0 53.5 139 SER 41.4 49.5 66.0 140 PHE 160.1 96.0 34.8 141 ARG 120.2 57.6 69.1 142 LEU 147.8 100.0 41.3 143 ASN 78.0 64.5 55.7 144 ARG 146.5 70.1 67.8 145 LEU 146.3 99.0 30.4 146 ALA 70.4 97.0 34.9 147 LEU 142.3 96.3 31.4 148 CYS 97.9 98.7 45.3 149 LYS 118.2 68.2 64.5 150 THR 101.9 95.3 46.2 151 ASP 37.7 34.1 67.2 152 THR 33.3 31.1 67.3 153 GLU 7.2 5.2 87.6 154 ASP 87.9 79.6 70.7 155 LYS 78.5 45.3 68.7 156 THR 40.8 38.1 76.0 157 LEU 141.0 95.4 43.0 158 GLU 11.0 7.9 84.9 159 THR 52.8 49.4 69.3 160 TRP 184.4 89.9 44.5 161 GLU 41.4 29.9 79.9 162 THR 52.6 49.2 58.5 163 VAL 60.9 51.3 59.4 164 ALA 30.4 41.8 58.1 165 VAL 66.5 56.0 57.3 166 CYS 73.3 73.9 50.1 167 ASN 17.9 14.8 76.3 168 LEU 147.8 100.0 51.4 169 ASN 10.1 8.3 79.9 170 PRO 24.4 19.6 79.0