Protein Data Bank File : 1fjra Title : SIGNALING PROTEIN 08-AUG-00 1FJR Number of Amino Acid Residues : 188 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP ILE LEU GLU CYS ASP TYR PHE ASP THR 10 VAL ASP ILE SER ALA ALA GLN LYS LEU GLN 20 ASN GLY SER TYR LEU PHE GLU GLY LEU LEU 30 VAL PRO ALA ILE LEU THR GLY GLU TYR ASP 40 PHE ARG ILE LEU PRO ASP ASP SER LYS GLN 50 LYS VAL ALA ARG HIS ILE ARG GLY CYS VAL 60 CYS LYS LEU LYS PRO CYS VAL ARG PHE CYS 70 CYS PRO HIS ASP HIS ILE MET ASP ASN GLY 80 VAL CYS TYR ASP ASN MET SER ASP GLU GLU 90 LEU ALA GLU LEU ASP PRO PHE LEU ASN VAL 100 THR LEU ASP ASP GLY SER VAL SER ARG ARG 110 HIS PHE LYS ASN GLU LEU ILE VAL GLN TRP 120 ASP LEU PRO MET PRO CYS ASP GLY MET PHE 130 TYR LEU ASP ASN ARG GLU GLU GLN ASP LYS 140 TYR THR LEU PHE GLU ASN GLY THR PHE PHE 150 ARG HIS PHE ASP ARG VAL THR LEU ARG LYS 160 ARG GLU TYR CYS LEU GLN HIS LEU THR PHE 170 ALA ASP GLY ASN ALA THR SER ILE ARG ILE 180 ALA PRO HIS ASN CYS LEU ILE VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 -48.3 178.4 -160.5 79.1 2 ILE -65.2 132.2 -177.2 -66.1 174.0 3 LEU -55.8 124.1 -179.8 114.2 153.1 4 GLU 53.4 35.1 179.7 -60.2 -157.1 -43.0 5 CYS -123.0 118.6 177.6 -175.8 6 ASP -64.8 145.5 -179.3 -175.5 68.7 7 TYR -54.8 -38.1 -179.1 179.5 74.8 8 PHE -74.8 7.8 176.5 -69.3 71.6 9 ASP -112.6 13.9 -180.0 -84.3 164.6 10 THR -112.1 163.3 -179.1 71.3 11 VAL -139.3 155.5 178.9 127.4 12 ASP -78.8 121.1 -179.6 179.5 -24.7 13 ILE -113.9 13.0 -179.3 62.0 168.1 14 SER -52.3 -22.8 180.0 60.6 15 ALA -94.4 3.9 -179.5 16 ALA -81.7 157.2 179.6 17 GLN -80.0 118.1 179.1 -60.3 78.2 66.6 18 LYS -84.4 114.1 -178.8 179.0 175.5 179.4 -59.5 19 LEU -78.6 174.4 -179.0 -57.6 -173.9 20 GLN -61.2 -57.4 -179.7 -36.3 73.5 -167.0 21 ASN -64.9 4.7 178.7 50.7 59.4 22 GLY 93.2 -12.6 179.5 23 SER -82.3 172.6 -179.1 68.6 24 TYR -121.9 157.8 178.5 -65.0 72.6 25 LEU -115.8 99.0 -178.6 -162.2 56.3 26 PHE -102.2 110.4 179.7 175.1 70.9 27 GLU 40.9 54.7 179.0 -75.0 170.1 39.8 28 GLY 80.3 -2.8 -179.8 29 LEU -105.1 134.2 178.9 178.8 67.8 30 LEU -83.5 116.8 179.8 176.4 68.8 31 VAL -111.1 110.7 -180.0 -176.1 32 PRO -60.3 146.3 -179.9 -28.7 42.9 33 ALA -53.2 -40.3 -179.9 34 ILE -59.1 -27.8 179.5 -163.9 59.9 35 LEU -89.6 11.4 179.9 -69.6 -177.6 36 THR -120.7 159.2 -179.5 68.6 37 GLY -175.5 156.0 -179.9 38 GLU -85.2 139.0 179.0 -173.0 -175.6 72.9 39 TYR -127.3 137.8 179.0 -74.1 69.9 40 ASP -122.9 28.8 -179.9 62.5 -26.9 41 PHE -161.0 158.1 178.8 70.6 86.1 42 ARG -141.1 126.5 -179.9 61.9 -170.8 167.4 -158.4 43 ILE -63.4 149.5 -179.2 -62.6 -165.9 44 LEU -114.3 174.5 179.9 -54.7 170.9 45 PRO -47.1 -38.3 -179.0 -37.4 46.1 46 ASP -84.1 7.5 179.2 57.7 44.2 47 ASP 70.2 21.6 178.5 -49.8 -52.3 48 SER -98.7 176.5 179.9 71.1 49 LYS -111.1 143.9 178.6 -61.3 -173.6 -179.0 -177.0 50 GLN -128.4 160.8 -177.7 171.0 147.5 51.1 51 LYS -91.4 152.2 179.5 -45.1 71.0 -170.6 175.7 52 VAL -153.2 162.8 179.7 -170.6 53 ALA -58.1 134.2 179.3 54 ARG -45.7 99.2 179.1 -113.9 72.4 174.7 55.8 55 HIS -124.7 158.3 -179.3 71.1 -72.9 56 ILE -92.7 123.4 178.9 178.9 68.9 57 ARG -112.5 156.2 -179.3 -63.2 -174.3 75.9 72.0 58 GLY -130.9 143.9 -178.4 59 CYS -89.3 62.0 -177.3 -163.4 60 VAL -65.8 -26.1 -179.1 -53.6 61 CYS -63.2 -14.4 177.5 -53.0 62 LYS -88.1 -12.5 -179.5 -82.5 -177.4 169.4 72.0 63 LEU -99.6 -41.1 179.2 -59.2 172.3 64 LYS -139.4 148.6 180.0 -107.1 -58.5 170.7 -168.3 65 PRO -62.4 146.2 179.3 23.6 -39.1 66 CYS -112.6 157.8 175.2 -75.1 67 VAL -120.6 128.8 -179.3 -144.7 68 ARG -83.2 98.2 -179.8 -133.8 -114.8 85.8 146.6 69 PHE -94.4 161.8 -179.3 -105.2 46.0 70 CYS -90.8 -26.1 -176.8 -50.2 71 CYS -148.3 179.6 179.3 -31.5 72 PRO -53.9 153.9 -176.4 -36.7 46.2 73 HIS -52.9 -26.7 -177.9 78.0 -88.7 74 ASP -104.4 10.6 179.5 60.3 -8.1 75 HIS -91.8 163.2 176.8 -81.9 45.3 76 ILE -119.3 148.6 178.1 -161.5 157.0 77 MET -94.1 124.9 179.9 -175.2 92.6 -48.7 78 ASP -121.8 105.9 -179.9 -164.2 -21.9 79 ASN 46.8 56.0 178.4 -172.9 42.1 80 GLY 77.2 1.3 179.7 81 VAL -119.2 133.0 179.5 -177.7 82 CYS -67.8 126.0 -176.2 -66.3 83 TYR -134.0 112.1 -179.9 -178.1 51.1 84 ASP -85.3 78.2 179.5 172.8 14.9 85 ASN -139.6 23.3 -179.5 -157.2 50.5 86 MET -74.7 121.3 179.9 -77.0 -156.2 -85.8 87 SER -70.4 160.2 -179.8 61.9 88 ASP -56.8 -30.3 179.6 -56.5 -41.5 89 GLU -66.5 -51.0 179.3 -175.1 179.1 64.1 90 GLU -59.8 -38.4 -179.8 -67.1 171.1 -48.8 91 LEU -62.5 -30.5 -178.7 -69.5 179.6 92 ALA -84.4 -36.8 -178.7 93 GLU -88.1 -11.5 -178.2 -81.9 152.5 46.4 94 LEU -70.6 149.6 179.4 102.8 -141.5 95 ASP -85.7 107.0 -179.6 177.4 -8.5 96 PRO -84.2 4.6 -177.0 40.8 -45.8 97 PHE -99.0 139.4 178.2 -60.5 98.7 98 LEU -116.4 143.5 178.0 -77.8 173.4 99 ASN -95.8 108.4 -179.8 -60.0 -50.8 100 VAL -110.1 130.3 179.8 -43.6 101 THR -87.1 127.0 -177.3 -59.6 102 LEU -89.0 173.7 179.2 -50.5 -179.9 103 ASP -62.8 -24.7 179.0 -65.6 -52.6 104 ASP -83.5 4.8 179.5 65.9 4.3 105 GLY 88.4 -5.6 -179.0 106 SER -84.3 168.0 -179.1 73.2 107 VAL -112.0 137.2 179.5 173.2 108 SER -130.1 136.0 177.9 -179.9 109 ARG -85.8 122.9 -177.3 166.0 177.7 -69.0 160.6 110 ARG -126.7 134.6 177.9 -59.2 -70.3 175.6 69.7 111 HIS -70.4 120.6 -177.2 -176.2 100.9 112 PHE -50.5 -35.7 -178.0 90.6 97.1 113 LYS -99.9 -41.2 -177.6 177.7 -175.8 -179.2 -173.8 114 ASN -84.1 -29.9 -178.8 -51.6 -38.5 115 GLU -104.6 -4.3 -179.7 -60.2 179.6 71.6 116 LEU -137.2 157.2 177.8 -53.8 162.0 117 ILE -95.1 117.7 -179.0 -63.1 172.5 118 VAL -78.4 123.2 178.4 175.1 119 GLN -101.7 118.8 -177.9 -61.5 -177.2 89.7 120 TRP -125.6 -9.7 -178.5 55.5 -94.4 121 ASP -92.7 6.7 179.2 81.1 173.4 122 LEU -74.4 153.3 179.8 -55.9 171.1 123 PRO -63.9 145.3 178.7 26.4 -41.5 124 MET -60.4 135.7 180.0 -159.4 67.5 88.3 125 PRO -57.4 -28.8 177.6 19.6 -35.0 126 CYS 179.2 171.6 179.4 67.1 127 ASP -85.1 140.8 179.4 -164.0 64.1 128 GLY 62.1 58.2 179.6 129 MET -80.4 157.2 176.6 -60.4 177.4 -70.6 130 PHE -108.7 158.3 -179.9 66.8 94.3 131 TYR -114.6 155.4 179.4 69.0 89.3 132 LEU -101.1 136.8 176.8 -62.2 172.5 133 ASP -115.3 96.1 -177.3 178.7 -19.9 134 ASN -65.1 7.7 175.8 63.4 -9.5 135 ARG -81.5 -21.2 178.6 -71.3 177.7 -57.0 -178.9 136 GLU -91.2 138.4 -177.8 -51.9 -73.3 165.1 137 GLU -57.5 -28.9 -179.0 70.8 -179.5 -170.7 138 GLN -84.5 -14.6 -178.6 -23.1 86.1 79.4 139 ASP -94.1 7.0 -178.6 -81.3 23.8 140 LYS -63.1 147.0 179.8 -55.4 -70.1 -165.3 179.1 141 TYR -152.9 164.6 177.4 69.3 90.7 142 THR -125.0 133.9 179.7 -60.5 143 LEU -118.9 111.4 -179.6 170.8 65.8 144 PHE -83.8 149.3 -179.7 -65.3 95.6 145 GLU -58.0 -29.5 -179.0 -170.9 -172.3 60.5 146 ASN -79.8 4.5 178.6 69.7 11.4 147 GLY 104.1 -19.4 179.3 148 THR -69.5 139.4 -179.7 -66.0 149 PHE -119.3 132.1 -179.1 -179.0 86.9 150 PHE -123.3 119.9 -179.9 -174.8 64.5 151 ARG -94.4 115.9 -176.5 -171.0 166.5 58.2 -145.7 152 HIS -64.6 -44.4 -178.5 -53.9 173.9 153 PHE -41.5 -55.3 -179.5 -178.3 64.7 154 ASP -112.9 14.8 179.5 51.8 -5.2 155 ARG 45.1 47.9 178.5 -62.1 -168.8 70.9 88.0 156 VAL -106.2 144.3 -179.9 -39.8 157 THR -99.0 127.3 179.1 -68.9 158 LEU -114.6 139.5 178.0 -57.1 -176.9 159 ARG -96.2 173.7 -176.9 -81.5 173.1 175.4 60.4 160 LYS -56.9 -16.6 178.1 -62.0 -151.6 -82.2 -172.8 161 ARG -80.0 -16.5 -174.8 -74.2 176.7 167.0 70.8 162 GLU -113.5 5.8 178.1 -48.8 160.1 -73.4 163 TYR -154.2 166.1 176.4 79.0 88.2 164 CYS -162.0 149.0 -178.3 65.5 165 LEU -106.5 149.9 177.5 -59.4 146.5 166 GLN -162.4 147.8 176.3 -161.3 69.0 -143.4 167 HIS -54.9 144.7 -180.0 -62.1 117.6 168 LEU -153.7 145.9 -179.6 178.6 138.7 169 THR -87.3 122.9 178.4 -60.8 170 PHE -110.4 155.1 177.9 -69.0 84.3 171 ALA -90.0 135.0 178.6 172 ASP -107.9 67.7 -178.4 -103.8 -55.9 173 GLY 73.7 -87.5 179.9 174 ASN -127.5 24.4 178.7 -53.1 -57.3 175 ALA -132.5 -159.4 -179.7 176 THR -155.5 144.7 179.6 -157.3 177 SER -147.0 154.4 -179.7 71.0 178 ILE -112.7 130.6 -179.5 -55.2 173.9 179 ARG -142.2 161.0 179.7 164.4 170.2 47.9 106.7 180 ILE -84.3 127.4 -179.0 -61.0 177.6 181 ALA -127.4 145.1 179.5 182 PRO -81.0 149.8 179.3 30.5 -40.5 183 HIS -120.9 133.6 179.9 -67.8 -106.2 184 ASN -125.1 166.1 177.4 -65.5 -4.8 185 CYS -99.5 125.6 -179.0 -67.1 186 LEU -60.4 -45.1 179.8 -177.1 50.7 187 ILE -118.5 -29.2 -179.7 70.3 174.7 188 VAL -35.9 134.5 0.0 177.4 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP -2.988 49.690 41.163 2 ILE -0.798 51.793 38.828 3 LEU -3.181 53.728 36.565 4 GLU -3.974 51.836 33.367 5 CYS -1.100 49.373 33.776 6 ASP -1.563 45.615 33.609 7 TYR 0.331 43.886 36.429 8 PHE 2.426 41.940 33.917 9 ASP 3.787 45.213 32.534 10 THR 5.336 46.006 35.913 11 VAL 8.669 45.465 37.576 12 ASP 9.761 45.784 41.232 13 ILE 11.417 49.200 41.606 14 SER 11.957 49.228 45.366 15 ALA 15.708 49.348 44.694 16 ALA 15.447 52.388 42.419 17 GLN 16.600 55.878 43.392 18 LYS 13.586 57.975 44.377 19 LEU 14.149 61.498 43.077 20 GLN 13.119 64.917 44.362 21 ASN 10.265 65.629 41.934 22 GLY 8.851 62.251 42.964 23 SER 9.885 60.284 39.874 24 TYR 12.337 57.351 39.964 25 LEU 15.620 56.357 38.384 26 PHE 15.407 52.640 37.633 27 GLU 18.621 51.189 36.242 28 GLY 19.297 54.344 34.245 29 LEU 15.657 54.812 33.277 30 LEU 13.587 57.800 34.433 31 VAL 10.266 56.493 35.742 32 PRO 7.576 59.158 36.312 33 ALA 5.660 58.989 39.589 34 ILE 2.363 58.436 37.763 35 LEU 3.801 55.182 36.391 36 THR 4.641 54.039 39.922 37 GLY 2.565 52.664 42.786 38 GLU 2.583 50.573 45.951 39 TYR 1.524 46.935 45.751 40 ASP 0.594 44.582 48.575 41 PHE -0.192 41.730 46.233 42 ARG 1.240 39.755 43.321 43 ILE -0.862 37.909 40.778 44 LEU -0.372 34.148 40.661 45 PRO -0.663 31.539 37.860 46 ASP -4.439 31.283 38.435 47 ASP -4.888 35.068 38.158 48 SER -5.753 35.398 41.850 49 LYS -4.057 37.724 44.325 50 GLN -1.564 36.886 47.062 51 LYS 0.018 39.088 49.704 52 VAL 3.566 40.440 49.715 53 ALA 5.475 43.090 51.643 54 ARG 4.204 46.581 50.768 55 HIS 6.559 47.264 47.850 56 ILE 6.824 49.846 45.088 57 ARG 6.386 48.665 41.463 58 GLY 6.833 50.577 38.203 59 CYS 5.175 50.282 34.802 60 VAL 8.481 50.359 32.947 61 CYS 7.235 48.391 29.918 62 LYS 5.406 51.516 28.742 63 LEU 8.729 53.409 28.770 64 LYS 11.157 50.812 27.321 65 PRO 10.415 47.431 25.794 66 CYS 10.300 44.480 28.182 67 VAL 11.109 40.790 27.640 68 ARG 8.917 38.334 29.563 69 PHE 11.392 35.995 31.249 70 CYS 10.649 32.892 33.355 71 CYS 13.523 33.499 35.776 72 PRO 16.338 35.954 36.625 73 HIS 18.354 37.080 33.594 74 ASP 21.297 34.746 34.320 75 HIS 19.379 31.543 35.105 76 ILE 18.825 28.693 32.722 77 MET 15.563 26.801 32.400 78 ASP 16.191 23.103 32.905 79 ASN 13.155 21.000 32.136 80 GLY 10.786 23.641 33.479 81 VAL 12.830 24.667 36.556 82 CYS 14.751 27.893 37.068 83 TYR 18.344 26.852 37.669 84 ASP 21.156 29.275 38.603 85 ASN 24.088 27.216 37.365 86 MET 25.470 28.863 34.273 87 SER 29.240 28.575 34.196 88 ASP 31.268 31.567 33.061 89 GLU 31.820 29.641 29.832 90 GLU 28.105 29.218 29.132 91 LEU 27.565 32.873 29.980 92 ALA 30.090 33.754 27.302 93 GLU 28.957 31.344 24.559 94 LEU 25.230 31.803 24.954 95 ASP 23.237 33.678 22.299 96 PRO 21.867 36.829 24.068 97 PHE 19.830 37.982 21.094 98 LEU 16.081 37.885 20.563 99 ASN 14.301 38.478 17.286 100 VAL 11.523 40.958 18.053 101 THR 8.912 41.929 15.516 102 LEU 8.126 45.641 15.661 103 ASP 4.873 47.494 15.061 104 ASP 5.799 48.308 11.446 105 GLY 6.006 44.555 10.888 106 SER 9.799 44.463 10.569 107 VAL 12.195 42.312 12.604 108 SER 14.907 43.644 14.875 109 ARG 17.676 41.738 16.692 110 ARG 17.719 42.868 20.356 111 HIS 20.099 42.038 23.191 112 PHE 17.833 40.434 25.866 113 LYS 19.435 42.290 28.772 114 ASN 20.874 45.530 27.340 115 GLU 18.157 46.537 24.877 116 LEU 15.159 45.225 26.788 117 ILE 13.994 45.268 30.410 118 VAL 13.963 41.704 31.693 119 GLN 10.901 40.868 33.743 120 TRP 11.698 37.933 35.970 121 ASP 9.594 38.246 39.100 122 LEU 6.298 37.412 37.415 123 PRO 4.605 34.106 38.374 124 MET 5.505 31.039 36.307 125 PRO 2.719 30.565 33.735 126 CYS 2.170 26.945 34.909 127 ASP 3.830 23.782 36.106 128 GLY 5.547 21.589 33.492 129 MET 5.786 23.967 30.537 130 PHE 7.083 22.781 27.180 131 TYR 9.546 24.796 25.110 132 LEU 9.642 25.713 21.430 133 ASP 12.709 25.065 19.283 134 ASN 12.065 27.342 16.302 135 ARG 14.582 25.356 14.250 136 GLU 11.738 22.818 13.806 137 GLU 8.988 23.825 11.365 138 GLN 6.132 23.246 13.852 139 ASP 7.786 25.344 16.563 140 LYS 7.901 28.705 14.764 141 TYR 6.723 31.774 16.635 142 THR 6.644 35.567 16.505 143 LEU 7.525 37.749 19.502 144 PHE 6.276 41.311 19.251 145 GLU 8.056 44.182 20.934 146 ASN 4.853 45.020 22.812 147 GLY 4.830 41.697 24.645 148 THR 2.389 39.752 22.468 149 PHE 3.472 36.194 21.566 150 PHE 2.129 34.373 18.499 151 ARG 2.470 30.581 18.089 152 HIS 2.371 29.684 14.401 153 PHE 1.426 25.987 14.545 154 ASP -2.098 26.674 15.799 155 ARG -1.971 30.433 15.272 156 VAL -2.780 31.247 18.897 157 THR -1.864 34.521 20.600 158 LEU -0.481 34.311 24.134 159 ARG -0.209 37.229 26.549 160 LYS 2.461 37.660 29.215 161 ARG 0.481 35.592 31.709 162 GLU 0.794 32.564 29.412 163 TYR 4.386 32.367 28.227 164 CYS 7.901 33.186 29.304 165 LEU 11.324 33.106 27.683 166 GLN 14.516 31.688 29.119 167 HIS 18.029 30.648 28.214 168 LEU 18.013 26.939 27.458 169 THR 20.522 24.302 26.421 170 PHE 19.918 22.820 22.979 171 ALA 21.756 19.905 21.400 172 ASP 23.835 20.783 18.316 173 GLY 23.855 17.357 16.722 174 ASN 26.656 16.042 18.923 175 ALA 27.529 19.316 20.655 176 THR 25.561 21.854 22.709 177 SER 24.576 25.551 22.583 178 ILE 22.475 27.965 24.612 179 ARG 19.787 30.160 23.102 180 ILE 16.655 31.870 24.454 181 ALA 13.493 29.811 23.951 182 PRO 9.823 30.432 24.695 183 HIS 7.959 28.195 27.116 184 ASN 4.201 27.628 26.828 185 CYS 1.583 25.725 28.845 186 LEU 0.312 22.602 27.135 187 ILE -3.220 22.672 28.565 188 VAL -3.627 25.747 30.803 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C C C T T T T/S S 10 S S S S S S S S S/T T 20 T T/S S S S/T T T T/S S S 30 S S/T T T T C S S S S/S 40 S S S S/T T T T/S S S S 50 S S S/S S S S S S S T 60 T T T/S S S S S S C C 70 C C C S S S S/T T T T/S 80 S S S S/S S S S/H H H H 90 H H H H C S S S S S 100 S S/T T T T/S S S S S S 110 S/T T T T S S S S S S 120 S C C C C C S S S S 130 S S S S C T T T T/S S 140 S S S S/T T T T/S S S S 150 S/T T T T S S S S S/T T 160 T T/S S S S S S/S S S S 170 S/T T T T/S S S S/S S S S 180 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 t T T t g G G G g 10 E E e T T t E E e T 20 T t e E E E T T E E 30 E g G G e E E E E E 40 E E E e T T t e E E 50 E E E E E E E E e G 60 G G g t e E E E e S 70 S t T T t E E E T T 80 E E E h H H H 90 H H H h e E E E E 100 E e T T t e E E E E 110 E e T T T t E E E 120 S S S S S E 130 E e t T T g G G G e 140 E E E e T T t e E E 150 E e T T T E E E t T 160 T e E E E E E E E E 170 E e S S e E E E E E 180 E E E E e S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 38.8 35.1 75.8 2 ILE 140.4 97.9 53.0 3 LEU 54.3 36.7 68.1 4 GLU 2.6 1.9 83.6 5 CYS 99.2 100.0 52.3 6 ASP 52.7 47.7 76.2 7 TYR 171.2 94.6 45.7 8 PHE 162.1 97.2 45.4 9 ASP 80.0 72.4 57.9 10 THR 106.9 100.0 52.4 11 VAL 107.8 90.8 47.6 12 ASP 67.7 61.3 68.4 13 ILE 143.2 99.8 32.9 14 SER 43.5 52.1 70.5 15 ALA 0.0 0.0 89.7 16 ALA 70.3 96.9 52.6 17 GLN 46.7 31.4 74.9 18 LYS 64.3 37.1 77.7 19 LEU 106.1 71.8 67.1 20 GLN 21.0 14.1 79.2 21 ASN 29.8 24.6 80.2 22 GLY 19.1 54.8 75.6 23 SER 72.5 86.7 54.0 24 TYR 157.0 86.8 45.7 25 LEU 84.3 57.0 62.9 26 PHE 145.2 87.0 42.2 27 GLU 15.9 11.5 76.8 28 GLY 1.6 4.7 72.9 29 LEU 109.5 74.1 50.6 30 LEU 57.0 38.5 65.7 31 VAL 118.8 100.0 31.4 32 PRO 75.9 61.0 50.0 33 ALA 31.6 43.6 74.6 34 ILE 36.8 25.6 64.9 35 LEU 125.5 84.9 38.2 36 THR 99.3 92.9 42.1 37 GLY 21.4 61.5 61.2 38 GLU 60.4 43.6 68.6 39 TYR 178.7 98.8 46.4 40 ASP 57.4 51.9 70.2 41 PHE 136.5 81.8 53.5 42 ARG 99.7 47.7 65.8 43 ILE 126.6 88.2 48.4 44 LEU 105.0 71.0 64.4 45 PRO 68.3 54.9 65.0 46 ASP 28.2 25.5 75.8 47 ASP 46.3 41.9 76.0 48 SER 34.2 40.9 73.7 49 LYS 58.8 33.9 67.1 50 GLN 75.7 50.9 65.5 51 LYS 20.0 11.5 84.3 52 VAL 86.1 72.5 65.7 53 ALA 0.0 0.0 80.9 54 ARG 84.0 40.2 83.2 55 HIS 123.0 81.9 62.1 56 ILE 106.8 74.4 54.7 57 ARG 205.4 98.3 50.3 58 GLY 34.8 100.0 40.2 59 CYS 99.2 100.0 37.3 60 VAL 118.8 100.0 26.4 61 CYS 92.4 93.2 60.6 62 LYS 90.9 52.4 70.3 63 LEU 110.2 74.6 50.7 64 LYS 63.5 36.6 67.0 65 PRO 100.4 80.6 66.3 66 CYS 97.9 98.7 50.2 67 VAL 115.0 96.8 37.4 68 ARG 208.7 99.9 44.8 69 PHE 166.8 100.0 45.6 70 CYS 99.2 100.0 39.3 71 CYS 97.8 98.6 35.8 72 PRO 81.6 65.6 55.0 73 HIS 85.4 56.9 54.0 74 ASP 60.4 54.7 62.1 75 HIS 117.7 78.4 57.0 76 ILE 128.9 89.8 48.5 77 MET 159.4 100.0 40.6 78 ASP 35.8 32.4 67.2 79 ASN 0.0 0.0 93.3 80 GLY 31.8 91.4 60.5 81 VAL 19.4 16.3 83.1 82 CYS 74.9 75.5 43.7 83 TYR 79.7 44.0 73.6 84 ASP 37.7 34.1 77.1 85 ASN 38.5 31.9 76.8 86 MET 157.4 98.8 46.1 87 SER 28.4 34.0 76.9 88 ASP 0.0 0.0 80.9 89 GLU 26.0 18.8 83.3 90 GLU 82.1 59.3 64.0 91 LEU 85.3 57.7 63.1 92 ALA 14.2 19.6 83.3 93 GLU 30.7 22.2 81.0 94 LEU 135.7 91.8 47.3 95 ASP 53.2 48.1 61.6 96 PRO 98.0 78.7 48.6 97 PHE 92.6 55.5 69.1 98 LEU 143.0 96.7 37.6 99 ASN 41.3 34.2 72.3 100 VAL 115.5 97.3 44.2 101 THR 88.5 82.8 47.4 102 LEU 110.3 74.6 71.8 103 ASP 13.2 11.9 85.9 104 ASP 25.2 22.8 79.2 105 GLY 5.8 16.5 79.9 106 SER 33.0 39.4 73.2 107 VAL 46.4 39.1 75.4 108 SER 57.2 68.4 63.8 109 ARG 53.0 25.4 78.6 110 ARG 170.2 81.5 50.6 111 HIS 116.5 77.6 49.9 112 PHE 155.4 93.2 33.2 113 LYS 78.2 45.1 67.8 114 ASN 39.8 32.9 69.3 115 GLU 66.8 48.2 65.8 116 LEU 144.1 97.5 44.2 117 ILE 116.1 80.9 43.2 118 VAL 109.9 92.5 44.4 119 GLN 148.2 99.7 43.6 120 TRP 88.1 43.0 67.6 121 ASP 81.6 73.9 60.8 122 LEU 147.8 100.0 57.3 123 PRO 102.5 82.3 53.0 124 MET 110.7 69.4 60.6 125 PRO 122.9 98.7 51.0 126 CYS 84.5 85.1 46.9 127 ASP 0.0 0.0 87.2 128 GLY 0.0 0.0 82.3 129 MET 158.6 99.5 44.7 130 PHE 99.4 59.6 63.1 131 TYR 90.6 50.0 59.1 132 LEU 141.0 95.4 45.9 133 ASP 93.7 84.8 59.1 134 ASN 83.4 69.0 70.5 135 ARG 110.2 52.7 82.7 136 GLU 50.7 36.6 83.3 137 GLU 12.6 9.1 79.1 138 GLN 63.1 42.4 70.3 139 ASP 84.1 76.2 58.8 140 LYS 81.1 46.8 71.9 141 TYR 162.0 89.5 48.0 142 THR 80.1 75.0 52.5 143 LEU 140.0 94.7 40.6 144 PHE 103.5 62.0 61.3 145 GLU 94.1 67.9 61.5 146 ASN 40.6 33.6 80.3 147 GLY 29.6 85.2 72.4 148 THR 68.4 64.0 61.9 149 PHE 166.8 100.0 34.4 150 PHE 128.9 77.3 62.6 151 ARG 172.8 82.7 47.7 152 HIS 92.0 61.3 64.5 153 PHE 37.7 22.6 76.8 154 ASP 60.2 54.5 63.0 155 ARG 45.3 21.7 78.0 156 VAL 73.4 61.8 69.7 157 THR 61.4 57.4 63.4 158 LEU 129.1 87.3 58.3 159 ARG 47.0 22.5 81.5 160 LYS 156.8 90.4 50.7 161 ARG 140.0 67.0 58.4 162 GLU 67.6 48.8 60.2 163 TYR 180.1 99.5 40.7 164 CYS 99.2 100.0 36.5 165 LEU 147.8 100.0 30.1 166 GLN 148.6 100.0 43.0 167 HIS 149.2 99.3 33.3 168 LEU 138.2 93.5 46.1 169 THR 59.3 55.5 60.5 170 PHE 160.0 95.9 62.0 171 ALA 14.7 20.2 85.0 172 ASP 58.1 52.6 74.3 173 GLY 0.0 0.0 84.2 174 ASN 0.0 0.0 87.7 175 ALA 15.0 20.6 78.2 176 THR 37.1 34.7 69.0 177 SER 40.0 47.8 75.9 178 ILE 135.8 94.6 42.4 179 ARG 161.0 77.1 64.0 180 ILE 143.2 99.8 39.3 181 ALA 71.9 99.0 49.8 182 PRO 123.4 99.1 38.7 183 HIS 147.9 98.5 41.7 184 ASN 120.9 100.0 35.9 185 CYS 94.3 95.1 43.7 186 LEU 29.8 20.1 72.7 187 ILE 6.3 4.4 79.9 188 VAL 47.8 40.2 59.4