Protein Data Bank File : 2scpa Title : BINDING PROTEIN 22-AUG-91 2SCP Number of Amino Acid Residues : 174 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER ASP LEU TRP VAL GLN LYS MET LYS THR 10 TYR PHE ASN ARG ILE ASP PHE ASP LYS ASP 20 GLY ALA ILE THR ARG MET ASP PHE GLU SER 30 MET ALA GLU ARG PHE ALA LYS GLU SER GLU 40 MET LYS ALA GLU HIS ALA LYS VAL LEU MET 50 ASP SER LEU THR GLY VAL TRP ASP ASN PHE 60 LEU THR ALA VAL ALA GLY GLY LYS GLY ILE 70 ASP GLU THR THR PHE ILE ASN SER MET LYS 80 GLU MET VAL LYS ASN PRO GLU ALA LYS SER 90 VAL VAL GLU GLY PRO LEU PRO LEU PHE PHE 100 ARG ALA VAL ASP THR ASN GLU ASP ASN ASN 110 ILE SER ARG ASP GLU TYR GLY ILE PHE PHE 120 GLY MET LEU GLY LEU ASP LYS THR MET ALA 130 PRO ALA SER PHE ASP ALA ILE ASP THR ASN 140 ASN ASP GLY LEU LEU SER LEU GLU GLU PHE 150 VAL ILE ALA GLY SER ASP PHE PHE MET ASN 160 ASP GLY ASP SER THR ASN LYS VAL PHE TRP 170 GLY PRO LEU VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 109.9 -175.2 9.7 2 ASP -35.9 -77.5 179.4 41.6 90.8 3 LEU -54.3 -40.0 -177.6 -150.6 -145.0 4 TRP -64.3 -41.4 178.3 -178.0 88.6 5 VAL -63.2 -40.7 -178.9 171.6 6 GLN -62.6 -38.4 177.4 -164.1 -163.4 -1.7 7 LYS -66.0 -42.7 -177.9 -70.6 -163.5 -75.4 173.9 8 MET -64.3 -43.5 178.3 -56.9 -64.3 117.9 9 LYS -58.6 -38.0 -178.9 -83.7 174.2 167.5 175.9 10 THR -66.1 -51.0 178.2 -58.6 11 TYR -54.6 -47.9 -179.4 -179.6 52.0 12 PHE -53.4 -46.9 -179.3 -177.4 -87.8 13 ASN -57.2 -53.9 -175.1 178.2 83.8 14 ARG -63.3 -37.4 179.3 -48.6 -66.6 136.3 86.8 15 ILE -83.2 -18.3 176.5 -116.8 70.6 16 ASP -81.3 67.9 -177.5 174.8 23.5 17 PHE -47.6 -51.2 -179.2 -173.0 80.2 18 ASP -82.4 2.3 178.1 61.1 31.4 19 LYS 54.8 31.7 -177.5 -58.1 -57.0 159.7 171.8 20 ASP -93.4 13.3 178.2 71.1 -5.7 21 GLY 86.4 -2.3 179.6 22 ALA -140.0 137.6 179.1 23 ILE -81.8 131.6 177.9 -51.2 -45.9 24 THR -142.0 168.7 178.3 66.9 25 ARG -63.1 -28.0 -179.9 -174.3 178.0 -158.7 -80.8 26 MET -56.3 -36.4 180.0 -64.5 -176.7 -90.5 27 ASP -59.7 -46.1 -179.5 -74.6 -47.3 28 PHE -72.2 -36.4 176.9 -68.7 -78.0 29 GLU -60.8 -49.2 178.9 -58.2 170.5 1.7 30 SER -67.4 -41.8 -178.7 -64.7 31 MET -59.2 -46.7 -179.1 171.9 -173.4 -165.4 32 ALA -56.5 -49.7 -177.0 33 GLU -59.4 -42.5 179.0 -146.5 112.7 -80.8 34 ARG -66.9 -45.2 -179.3 -174.4 -164.6 167.0 -174.3 35 PHE -57.6 -46.1 -179.7 -152.8 -26.5 36 ALA -64.2 -29.6 -176.4 37 LYS -79.8 -50.8 -174.7 178.6 171.5 67.7 -142.9 38 GLU -88.6 -4.5 180.0 -73.2 171.3 47.0 39 SER -107.9 157.7 170.5 -177.5 40 GLU -83.1 142.5 -178.5 -67.4 -174.4 -39.1 41 MET -171.2 169.1 172.8 64.3 -172.2 59.6 42 LYS -74.1 136.5 -177.1 -72.0 150.3 146.4 98.0 43 ALA -45.2 -45.4 -177.5 44 GLU -70.0 -20.7 -179.8 32.8 -98.9 87.0 45 HIS -61.8 -18.7 -178.5 -161.2 75.5 46 ALA -65.0 -38.9 176.4 47 LYS -68.2 -44.6 -178.0 11.6 145.1 -111.7 137.2 48 VAL -52.0 -47.7 -178.1 162.2 49 LEU -53.1 -51.3 -179.1 -150.5 32.8 50 MET -63.9 -46.9 -178.8 171.4 72.5 59.3 51 ASP -63.7 -46.3 -178.2 -67.9 -22.9 52 SER -68.1 -39.9 -178.8 -63.6 53 LEU -76.1 -42.2 177.1 -76.0 -171.6 54 THR -68.4 -31.3 175.7 61.6 55 GLY -63.7 -22.1 176.0 56 VAL -60.8 -45.9 178.7 175.5 57 TRP -71.6 -57.6 -176.8 169.9 -90.6 58 ASP -50.3 -43.6 -174.1 -67.3 -27.5 59 ASN -99.5 -18.1 -175.3 -61.6 109.0 60 PHE -120.2 -72.5 -175.1 -60.6 -82.7 61 LEU -60.8 -26.6 179.3 -56.1 -176.5 62 THR -59.3 -28.5 179.2 -154.3 63 ALA -75.9 -8.9 -178.2 64 VAL -74.0 -52.1 -179.4 -177.6 65 ALA -123.0 27.6 -179.3 66 GLY 46.8 62.6 175.7 67 GLY 110.7 -31.5 -179.0 68 LYS -125.0 178.7 -175.9 -33.6 136.9 -33.4 -57.2 69 GLY -32.3 134.0 179.2 70 ILE -111.6 119.7 180.0 -53.0 167.3 71 ASP -84.8 165.6 -179.0 68.0 75.9 72 GLU -59.6 -35.6 -178.4 -164.8 -175.8 75.0 73 THR -70.9 -46.3 179.6 -70.0 74 THR -60.4 -36.7 -179.1 -57.2 75 PHE -58.5 -56.6 -178.3 179.0 73.8 76 ILE -61.2 -43.3 178.4 -67.3 147.2 77 ASN -60.6 -47.6 -179.5 -73.1 -22.1 78 SER -61.9 -58.3 178.6 -52.7 79 MET -52.3 -37.4 -178.2 -65.9 -71.3 -48.7 80 LYS -55.1 -44.2 179.1 -147.1 164.8 -105.2 -143.0 81 GLU -70.6 -44.0 -179.3 -46.1 156.7 -62.1 82 MET -62.5 -31.1 -177.1 -82.3 169.8 -142.7 83 VAL -85.6 -9.0 -179.3 -56.7 84 LYS -63.3 -38.6 -179.5 -107.9 167.8 -174.1 -83.3 85 ASN -94.7 103.7 -179.1 -170.0 -14.8 86 PRO -60.6 -21.1 -178.2 20.5 -31.0 87 GLU -86.8 -10.9 179.1 -59.1 -71.8 -6.9 88 ALA -115.7 29.4 -176.3 89 LYS -55.7 -32.7 -177.4 -80.1 -168.4 -115.1 61.2 90 SER -63.7 -14.5 177.9 53.8 91 VAL -75.8 -28.1 179.3 -12.8 92 VAL -91.6 -37.3 -176.5 175.7 93 GLU -82.8 -24.5 179.2 -74.2 166.4 16.3 94 GLY -39.6 -43.8 178.9 95 PRO -67.6 -18.2 -175.2 -23.2 37.4 96 LEU -56.3 -49.3 -179.7 -58.1 173.5 97 PRO -60.3 -32.4 176.6 -36.5 52.6 98 LEU -70.0 -42.7 179.7 -81.2 61.2 99 PHE -60.9 -41.7 -179.5 -84.0 -63.7 100 PHE -59.4 -50.2 -177.6 -173.4 -84.8 101 ARG -58.2 -44.1 -179.5 -174.9 73.2 -146.5 -55.3 102 ALA -63.7 -43.5 -176.4 103 VAL -70.1 -25.8 178.7 174.0 104 ASP -77.8 72.0 -174.6 -172.4 14.4 105 THR -67.1 -22.6 178.0 58.2 106 ASN -96.4 4.3 179.6 74.0 -13.5 107 GLU 47.4 42.4 179.7 -40.4 -163.6 -24.2 108 ASP -96.2 4.3 179.4 65.4 0.8 109 ASN 76.8 11.7 178.8 -69.2 -58.1 110 ASN -136.2 152.2 173.3 -71.8 122.0 111 ILE -105.0 124.4 178.4 -67.2 176.2 112 SER -91.3 166.0 178.1 63.6 113 ARG -52.7 -46.9 179.3 -73.0 -145.7 -162.3 -108.2 114 ASP -60.7 -46.3 179.8 -66.1 7.3 115 GLU -61.3 -41.1 179.3 -72.7 170.4 -17.5 116 TYR -64.9 -44.0 178.4 -162.7 77.6 117 GLY -56.9 -43.4 179.4 118 ILE -64.3 -38.1 178.8 -81.8 53.7 119 PHE -61.8 -50.2 -179.2 174.4 46.8 120 PHE -57.5 -42.9 177.3 -97.1 35.7 121 GLY -61.3 -32.4 -179.2 122 MET -71.9 -35.2 177.2 -65.6 -65.3 141.6 123 LEU -74.3 3.7 179.3 -54.4 165.3 124 GLY 82.5 3.3 -180.0 125 LEU -84.7 151.8 177.0 -92.1 33.0 126 ASP -68.5 123.1 -175.6 170.5 25.1 127 LYS -57.8 -20.2 -179.9 -99.8 128.0 148.6 -40.5 128 THR -74.6 -8.7 177.2 79.8 129 MET -90.8 -9.4 -177.6 41.2 -108.3 -143.3 130 ALA -63.2 -45.5 -174.6 131 PRO -52.6 -46.7 -178.8 -25.3 38.4 132 ALA -60.1 -37.8 -179.5 133 SER -75.2 -43.5 179.9 -56.7 134 PHE -55.3 -52.0 -177.4 -172.3 -86.0 135 ASP -55.8 -37.9 177.1 -76.5 -0.4 136 ALA -68.1 -34.5 -178.0 137 ILE -82.2 -35.1 -178.1 -56.3 167.7 138 ASP -74.5 72.0 -177.3 -171.3 12.9 139 THR -66.5 -24.2 -179.7 56.9 140 ASN -97.4 0.7 173.6 75.8 -17.9 141 ASN 60.1 26.7 -179.1 -57.4 -55.5 142 ASP -86.7 1.3 176.6 71.8 -0.8 143 GLY 77.4 16.9 177.2 144 LEU -136.8 157.8 172.3 -98.2 8.9 145 LEU -106.4 119.5 175.5 -54.0 -171.2 146 SER -84.2 164.1 178.2 61.6 147 LEU -58.6 -41.8 -178.7 -176.1 58.0 148 GLU -59.5 -53.9 179.5 -166.2 -172.5 88.7 149 GLU -57.8 -41.7 -178.1 -64.7 179.4 -37.8 150 PHE -62.4 -50.3 180.0 -168.2 81.0 151 VAL -69.2 -36.8 -179.6 -54.6 152 ILE -62.8 -47.5 179.5 -73.1 164.1 153 ALA -63.9 -42.9 -178.1 154 GLY -62.5 -39.1 -179.3 155 SER -64.5 -44.1 178.1 158.2 156 ASP -60.5 -42.9 179.8 -169.5 56.3 157 PHE -57.2 -48.2 -176.6 169.8 87.1 158 PHE -70.7 -37.7 -172.5 -75.8 -57.3 159 MET -97.8 -26.7 -177.6 -45.2 -88.6 172.4 160 ASN -72.9 128.2 177.8 -154.8 -33.6 161 ASP -84.4 -20.2 179.5 -139.2 44.0 162 GLY -106.9 177.1 -178.1 163 ASP -74.8 135.1 178.3 -171.3 -18.4 164 SER -149.5 174.7 179.1 53.4 165 THR -73.9 -21.9 -178.8 50.2 166 ASN -78.8 3.2 176.4 -54.4 111.5 167 LYS -60.7 -24.7 -180.0 60.2 -165.4 -171.6 -147.8 168 VAL -95.3 20.4 178.2 -56.0 169 PHE -48.3 -40.5 -177.3 -166.2 81.6 170 TRP -105.4 26.6 179.3 -62.0 92.8 171 GLY 96.0 -167.6 -178.9 172 PRO -61.6 140.2 -178.8 5.5 -5.5 173 LEU -74.2 140.1 176.8 -59.8 163.7 174 VAL -81.6 173.0 0.0 -59.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER 22.470 4.255 2.107 2 ASP 25.202 2.473 0.131 3 LEU 27.745 5.168 -0.629 4 TRP 26.942 6.781 2.758 5 VAL 27.779 3.565 4.614 6 GLN 30.946 3.367 2.533 7 LYS 32.018 6.889 3.522 8 MET 31.484 6.110 7.224 9 LYS 33.503 2.934 6.865 10 THR 36.260 4.991 5.248 11 TYR 36.258 7.661 7.960 12 PHE 36.335 4.898 10.611 13 ASN 39.407 3.388 8.957 14 ARG 41.333 6.679 8.705 15 ILE 40.636 7.724 12.319 16 ASP 41.354 4.247 13.726 17 PHE 45.013 5.338 13.773 18 ASP 46.453 2.289 15.592 19 LYS 44.223 0.012 13.454 20 ASP 42.897 -2.147 16.329 21 GLY 39.277 -2.028 15.142 22 ALA 38.082 0.494 17.729 23 ILE 38.148 4.300 17.927 24 THR 39.620 5.293 21.290 25 ARG 41.248 8.431 22.699 26 MET 44.463 6.447 22.143 27 ASP 44.073 6.856 18.354 28 PHE 44.006 10.652 18.714 29 GLU 46.778 10.640 21.331 30 SER 49.068 8.648 18.994 31 MET 48.081 10.551 15.842 32 ALA 48.976 13.787 17.634 33 GLU 52.325 12.494 18.903 34 ARG 53.379 11.318 15.437 35 PHE 52.186 14.573 13.878 36 ALA 54.192 16.590 16.427 37 LYS 57.409 14.654 15.731 38 GLU 57.358 14.480 11.977 39 SER 55.868 17.771 10.810 40 GLU 57.417 21.195 10.395 41 MET 55.459 23.629 12.560 42 LYS 55.696 26.584 14.892 43 ALA 57.154 25.186 18.137 44 GLU 54.072 26.069 20.164 45 HIS 51.837 24.214 17.698 46 ALA 52.793 20.856 19.285 47 LYS 50.571 21.558 22.242 48 VAL 47.763 22.810 19.960 49 LEU 47.927 19.575 18.004 50 MET 47.569 17.386 21.060 51 ASP 44.721 19.460 22.526 52 SER 42.777 19.732 19.260 53 LEU 43.079 16.080 18.148 54 THR 42.368 14.750 21.633 55 GLY 39.518 17.294 21.824 56 VAL 37.880 15.377 18.886 57 TRP 37.456 12.393 21.245 58 ASP 36.920 14.342 24.469 59 ASN 34.128 16.639 23.188 60 PHE 32.546 14.551 20.449 61 LEU 33.288 10.821 20.072 62 THR 33.187 10.228 23.845 63 ALA 29.419 10.681 23.571 64 VAL 29.089 7.669 21.218 65 ALA 29.618 4.674 23.536 66 GLY 29.872 6.861 26.592 67 GLY 33.617 6.766 27.287 68 LYS 35.022 3.749 25.525 69 GLY 36.048 2.130 22.332 70 ILE 33.863 2.455 19.295 71 ASP 33.685 -0.594 16.993 72 GLU 32.827 -0.107 13.343 73 THR 29.258 -1.302 13.829 74 THR 28.512 1.027 16.741 75 PHE 30.127 3.904 14.809 76 ILE 27.842 3.507 11.785 77 ASN 24.788 2.820 13.927 78 SER 25.568 5.902 16.010 79 MET 26.281 8.267 13.089 80 LYS 23.141 6.964 11.363 81 GLU 21.045 8.308 14.266 82 MET 23.037 11.538 14.576 83 VAL 22.469 12.619 10.986 84 LYS 18.710 12.213 11.392 85 ASN 18.190 15.595 13.081 86 PRO 18.975 18.420 10.665 87 GLU 18.956 20.803 13.608 88 ALA 21.774 19.123 15.540 89 LYS 24.362 18.800 12.722 90 SER 27.066 20.554 14.718 91 VAL 27.328 17.472 16.913 92 VAL 28.603 15.612 13.809 93 GLU 30.282 18.640 12.219 94 GLY 31.883 19.987 15.411 95 PRO 35.209 18.168 15.027 96 LEU 36.032 19.775 11.622 97 PRO 37.413 23.018 13.109 98 LEU 39.527 20.999 15.539 99 PHE 40.976 18.952 12.634 100 PHE 41.552 22.231 10.827 101 ARG 43.400 23.806 13.777 102 ALA 45.724 20.787 14.147 103 VAL 46.528 20.713 10.410 104 ASP 47.355 24.471 10.165 105 THR 50.886 23.970 11.462 106 ASN 52.110 27.467 10.568 107 GLU 48.891 28.855 12.141 108 ASP 48.155 31.267 9.315 109 ASN 44.501 30.176 9.343 110 ASN 44.606 28.512 5.911 111 ILE 45.688 24.968 5.005 112 SER 48.309 24.912 2.254 113 ARG 49.035 22.042 -0.112 114 ASP 52.110 21.073 1.942 115 GLU 50.124 21.066 5.213 116 TYR 47.384 18.977 3.596 117 GLY 49.914 16.500 2.146 118 ILE 51.434 16.079 5.620 119 PHE 47.952 15.473 7.020 120 PHE 47.308 12.642 4.492 121 GLY 50.708 11.258 5.423 122 MET 49.828 11.261 9.131 123 LEU 46.735 9.153 8.290 124 GLY 49.108 6.597 6.642 125 LEU 47.958 7.606 3.125 126 ASP 50.107 8.027 0.036 127 LYS 50.772 11.753 -0.409 128 THR 50.040 11.345 -4.076 129 MET 46.350 10.924 -3.160 130 ALA 46.187 14.388 -1.548 131 PRO 45.723 16.570 -4.618 132 ALA 42.372 15.071 -5.678 133 SER 40.964 15.606 -2.162 134 PHE 42.562 19.089 -1.779 135 ASP 41.156 20.129 -5.177 136 ALA 37.627 19.131 -4.170 137 ILE 37.756 21.308 -1.051 138 ASP 39.451 24.311 -2.722 139 THR 36.329 25.728 -4.416 140 ASN 37.804 29.177 -5.155 141 ASN 40.991 27.675 -6.555 142 ASP 43.274 30.068 -4.624 143 GLY 45.452 27.071 -3.659 144 LEU 44.628 27.171 0.049 145 LEU 41.895 25.673 2.258 146 SER 39.988 28.278 4.349 147 LEU 38.127 27.071 7.504 148 GLU 34.897 27.727 5.638 149 GLU 35.808 25.516 2.611 150 PHE 37.039 22.751 4.916 151 VAL 33.922 22.615 7.065 152 ILE 31.571 22.895 4.050 153 ALA 33.264 19.978 2.290 154 GLY 33.538 17.944 5.531 155 SER 29.865 18.632 6.205 156 ASP 29.002 17.310 2.741 157 PHE 31.103 14.173 3.389 158 PHE 29.214 13.378 6.589 159 MET 25.758 14.379 5.462 160 ASN 25.299 13.581 1.772 161 ASP 23.406 10.363 1.079 162 GLY 24.358 10.694 -2.560 163 ASP 27.599 10.942 -4.518 164 SER 29.530 14.241 -4.502 165 THR 33.153 15.297 -5.016 166 ASN 33.620 15.492 -1.219 167 LYS 33.184 11.730 -0.842 168 VAL 36.992 11.603 -0.868 169 PHE 37.375 14.073 2.023 170 TRP 39.243 11.364 3.976 171 GLY 41.114 9.840 1.031 172 PRO 40.103 6.912 -1.165 173 LEU 36.946 4.994 -0.233 174 VAL 37.124 1.459 1.185 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H H H H H/T T T T C 20 S S S S/H H H H H H H 30 H H H H H H H H H/S S 40 S S C H H H H H H H 50 H H H H H H H H H H/T 60 T T T/T T T T S S S S 70 S/H H H H H H H H H H 80 H H H H T T T T H H 90 H H H H H H H H H H 100 H H H H/T T T T C S S 110 S S/H H H H H H H H H 120 H H H H C T T T T H 130 H H H H H H H H/T T T 140 T C S S S S/H H H H H 150 H H H H H H H H H H 160 S S S S S C C T T T 170 T/S S S 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 H H 10 H H H H H h T T t S 20 e E E h H H H H H H 30 H H H H H H H H h 40 t T h H H H H H H 50 H H H H H H H H H h 60 G G G g T T T t E 70 E H H H H H H H H H 80 H H h t g G G G h H 90 H H H h H H H H H H 100 H H H h T T t S S S 110 E E H H H H H H H H 120 H H h T t g G G h H 130 H H H H H H H h T T 140 t S e E E h H H H H 150 H H H H H H H H H h 160 S S g G G G G g T 170 t S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 48.5 58.0 77.5 2 ASP 0.0 0.0 77.9 3 LEU 124.3 84.1 57.1 4 TRP 198.8 97.0 43.9 5 VAL 85.6 72.0 58.0 6 GLN 84.8 57.1 61.2 7 LYS 173.2 99.9 44.7 8 MET 159.4 100.0 32.4 9 LYS 93.5 53.9 60.9 10 THR 106.8 99.9 51.1 11 TYR 175.6 97.0 22.9 12 PHE 156.7 93.9 45.3 13 ASN 72.3 59.8 64.8 14 ARG 193.1 92.4 46.3 15 ILE 142.0 98.9 30.7 16 ASP 103.8 94.0 59.7 17 PHE 132.8 79.6 56.2 18 ASP 66.5 60.2 70.6 19 LYS 84.6 48.8 87.6 20 ASP 49.5 44.8 81.5 21 GLY 4.4 12.7 76.3 22 ALA 47.2 65.1 61.2 23 ILE 143.3 99.9 32.4 24 THR 87.2 81.6 51.2 25 ARG 121.5 58.2 66.3 26 MET 49.4 31.0 81.6 27 ASP 110.2 99.8 63.1 28 PHE 165.6 99.3 34.0 29 GLU 80.6 58.2 60.4 30 SER 42.4 50.8 63.3 31 MET 156.0 97.9 27.7 32 ALA 72.4 99.8 46.4 33 GLU 35.7 25.7 74.0 34 ARG 132.2 63.3 67.9 35 PHE 165.9 99.4 31.6 36 ALA 53.1 73.1 56.8 37 LYS 45.4 26.2 80.9 38 GLU 76.7 55.3 68.7 39 SER 80.0 95.7 51.1 40 GLU 0.0 0.0 90.5 41 MET 144.3 90.5 52.0 42 LYS 75.8 43.7 70.9 43 ALA 0.0 0.0 87.2 44 GLU 34.3 24.8 71.0 45 HIS 150.2 100.0 47.1 46 ALA 38.5 53.0 62.8 47 LYS 41.4 23.9 76.7 48 VAL 105.8 89.1 68.8 49 LEU 147.7 99.9 37.0 50 MET 99.5 62.4 69.0 51 ASP 26.1 23.6 80.2 52 SER 68.9 82.4 52.7 53 LEU 146.8 99.3 33.8 54 THR 101.1 94.6 54.6 55 GLY 27.1 77.9 73.0 56 VAL 118.8 100.0 35.3 57 TRP 191.5 93.4 50.6 58 ASP 64.4 58.3 71.4 59 ASN 38.2 31.6 66.2 60 PHE 127.3 76.3 58.0 61 LEU 134.5 91.0 32.4 62 THR 65.7 61.4 65.1 63 ALA 16.3 22.4 76.9 64 VAL 113.1 95.2 41.8 65 ALA 49.1 67.6 69.1 66 GLY 2.1 6.1 81.2 67 GLY 13.6 39.1 74.6 68 LYS 39.6 22.8 84.2 69 GLY 23.8 68.4 49.1 70 ILE 143.4 100.0 37.6 71 ASP 50.5 45.7 69.5 72 GLU 74.4 53.7 51.2 73 THR 18.4 17.2 85.6 74 THR 62.5 58.4 67.1 75 PHE 165.7 99.3 25.5 76 ILE 128.6 89.6 42.5 77 ASN 47.2 39.1 63.7 78 SER 75.3 90.0 52.8 79 MET 147.9 92.8 28.7 80 LYS 89.8 51.8 62.0 81 GLU 39.2 28.3 74.1 82 MET 109.0 68.4 51.8 83 VAL 93.6 78.8 55.7 84 LYS 23.3 13.4 85.5 85 ASN 39.7 32.9 66.4 86 PRO 38.6 31.0 77.3 87 GLU 8.9 6.5 87.2 88 ALA 38.3 52.8 74.0 89 LYS 85.4 49.2 72.5 90 SER 10.6 12.7 77.7 91 VAL 47.6 40.1 63.1 92 VAL 113.2 95.2 37.6 93 GLU 103.2 74.5 46.1 94 GLY 21.0 60.3 51.8 95 PRO 117.7 94.5 41.0 96 LEU 147.3 99.7 32.9 97 PRO 79.2 63.6 54.2 98 LEU 103.9 70.3 58.4 99 PHE 166.2 99.7 27.0 100 PHE 156.1 93.6 43.0 101 ARG 103.3 49.5 69.3 102 ALA 72.6 99.9 45.0 103 VAL 117.9 99.3 34.2 104 ASP 106.5 96.4 64.9 105 THR 98.6 92.2 53.0 106 ASN 61.4 50.8 78.5 107 GLU 106.0 76.5 63.8 108 ASP 48.5 43.9 86.4 109 ASN 10.1 8.3 85.9 110 ASN 75.3 62.3 60.2 111 ILE 143.5 100.0 35.4 112 SER 46.7 55.9 59.2 113 ARG 103.6 49.6 68.2 114 ASP 1.7 1.6 80.1 115 GLU 121.5 87.7 67.7 116 TYR 179.2 99.0 31.7 117 GLY 27.0 77.7 59.5 118 ILE 99.7 69.5 56.7 119 PHE 164.8 98.8 23.5 120 PHE 166.7 100.0 44.0 121 GLY 26.8 76.9 67.9 122 MET 150.6 94.5 49.0 123 LEU 146.9 99.4 36.1 124 GLY 4.9 14.0 83.4 125 LEU 132.7 89.8 48.3 126 ASP 36.7 33.2 69.5 127 LYS 83.6 48.2 64.9 128 THR 15.0 14.0 83.3 129 MET 101.4 63.6 53.7 130 ALA 66.6 91.8 43.0 131 PRO 59.4 47.7 77.2 132 ALA 8.6 11.8 80.4 133 SER 81.4 97.4 51.9 134 PHE 164.5 98.6 47.2 135 ASP 48.4 43.8 74.2 136 ALA 58.1 80.0 70.5 137 ILE 142.8 99.5 42.0 138 ASP 106.5 96.4 65.4 139 THR 21.0 19.6 86.2 140 ASN 41.4 34.2 86.4 141 ASN 14.7 12.2 92.1 142 ASP 49.4 44.7 81.9 143 GLY 16.8 48.3 75.3 144 LEU 84.2 56.9 70.1 145 LEU 147.8 100.0 34.9 146 SER 47.7 57.0 67.1 147 LEU 71.3 48.2 55.8 148 GLU 20.2 14.6 73.0 149 GLU 119.1 85.9 67.2 150 PHE 166.1 99.6 26.4 151 VAL 79.3 66.8 48.1 152 ILE 38.0 26.5 72.0 153 ALA 68.7 94.6 52.6 154 GLY 34.8 100.0 42.5 155 SER 58.9 70.4 62.1 156 ASP 73.6 66.6 72.9 157 PHE 166.8 100.0 44.1 158 PHE 162.6 97.5 35.9 159 MET 132.2 82.9 52.9 160 ASN 72.5 59.9 78.5 161 ASP 35.5 32.2 73.4 162 GLY 3.5 10.0 79.1 163 ASP 45.8 41.5 70.6 164 SER 58.3 69.7 83.3 165 THR 8.8 8.3 81.0 166 ASN 103.0 85.2 57.1 167 LYS 116.4 67.1 56.8 168 VAL 82.0 69.0 62.9 169 PHE 164.1 98.4 36.4 170 TRP 204.7 99.9 19.3 171 GLY 34.3 98.5 48.7 172 PRO 68.6 55.1 56.3 173 LEU 129.3 87.5 50.8 174 VAL 68.0 57.2 73.3