Protein Data Bank File : 1nskl Title : PHOSPHOTRANSFERASE (PO4 AS ACCEPTOR) 04-JUL-95 1NSK Number of Amino Acid Residues : 151 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ALA ASN LEU GLU ARG THR PHE ILE ALA 10 ILE LYS PRO ASP GLY VAL GLN ARG GLY LEU 20 VAL GLY GLU ILE ILE LYS ARG PHE GLU GLN 30 LYS GLY PHE ARG LEU VAL ALA MET LYS PHE 40 LEU ARG ALA SER GLU GLU HIS LEU LYS GLN 50 HIS TYR ILE ASP LEU LYS ASP ARG PRO PHE 60 PHE PRO GLY LEU VAL LYS TYR MET ASN SER 70 GLY PRO VAL VAL ALA MET VAL TRP GLU GLY 80 LEU ASN VAL VAL LYS THR GLY ARG VAL MET 90 LEU GLY GLU THR ASN PRO ALA ASP SER LYS 100 PRO GLY THR ILE ARG GLY ASP PHE CYS ILE 110 GLN VAL GLY ARG ASN ILE ILE HIS GLY SER 120 ASP SER VAL LYS SER ALA GLU LYS GLU ILE 130 SER LEU TRP PHE LYS PRO GLU GLU LEU VAL 140 ASP TYR LYS SER CYS ALA HIS ASP TRP VAL 150 TYR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 0.0 0.0 0.0 0.0 0.0 2 ALA 0.0 -36.0 -179.9 3 ASN -178.1 159.6 179.6 175.7 40.4 4 LEU -69.4 -127.9 -180.0 -67.3 -155.1 5 GLU 165.5 -159.4 -179.2 -108.0 179.0 59.8 6 ARG -179.4 141.5 -178.4 -177.3 175.9 63.2 -161.5 7 THR -140.8 162.2 179.2 -163.3 8 PHE -102.0 119.8 179.9 175.4 72.9 9 ILE -117.2 127.8 179.7 -62.1 -61.6 10 ALA -128.2 127.6 178.8 11 ILE -93.8 106.7 -178.0 -62.5 178.3 12 LYS -59.5 161.2 -179.7 -60.3 175.3 171.6 170.0 13 PRO -44.6 -44.4 -179.8 -31.5 44.3 14 ASP -66.3 -35.3 178.1 56.4 -50.1 15 GLY -65.2 -42.7 179.3 16 VAL -66.6 -49.8 -179.3 168.7 17 GLN -58.5 -36.0 -179.8 -79.9 -81.3 -3.1 18 ARG -88.9 8.3 178.3 -68.8 173.3 60.4 -143.4 19 GLY 63.7 55.1 179.3 20 LEU -119.2 16.8 -179.6 -59.7 169.1 21 VAL -65.1 -53.5 -179.6 -176.9 22 GLY -58.2 -44.7 179.9 23 GLU -60.6 -45.6 -179.6 -103.4 -47.7 -41.6 24 ILE -67.3 -45.5 179.1 -60.7 165.0 25 ILE -62.2 -49.2 -179.2 -63.8 175.3 26 LYS -49.2 -47.4 -179.9 -177.3 -177.8 -176.8 64.7 27 ARG -57.4 -41.0 179.2 -61.1 -159.9 172.8 -166.1 28 PHE -70.4 -35.7 178.9 -79.0 82.1 29 GLU -62.8 -54.1 -178.8 -74.3 -173.4 -65.6 30 GLN -60.5 -18.8 -179.7 63.5 -167.9 -166.4 31 LYS -79.3 -27.3 -179.7 177.7 68.0 179.5 -179.1 32 GLY 110.6 6.3 179.2 33 PHE -83.1 147.3 -178.7 -67.9 -41.2 34 ARG -110.1 131.2 -179.8 43.1 165.4 -76.8 110.9 35 LEU -68.6 106.9 179.0 -141.2 -154.2 36 VAL -83.6 -40.1 180.0 177.7 37 ALA -155.9 154.7 179.5 38 MET -161.1 132.2 179.6 175.6 175.1 85.8 39 LYS -144.8 150.9 179.9 63.6 163.9 73.1 -179.9 40 PHE -110.3 124.8 -178.3 -173.3 65.4 41 LEU -163.4 159.3 177.7 74.3 160.9 42 ARG -99.9 99.2 -178.4 179.7 -178.0 -134.5 111.2 43 ALA -59.3 122.5 179.5 44 SER -65.5 150.7 179.3 68.9 45 GLU -54.3 -38.0 179.8 -67.2 178.2 87.5 46 GLU -61.7 -49.8 179.0 -176.9 -178.2 -61.0 47 HIS -61.4 -42.2 -179.1 -172.0 -125.6 48 LEU -65.0 -38.4 178.9 -68.2 163.4 49 LYS -62.5 -36.9 178.8 -67.4 173.9 -173.1 173.0 50 GLN -66.1 -42.8 179.2 -72.6 -166.0 -112.2 51 HIS -63.2 -34.9 -178.9 -179.5 -84.1 52 TYR -106.0 29.0 179.9 -65.1 -69.4 53 ILE -52.7 -41.8 -180.0 -77.1 179.1 54 ASP -66.3 -4.3 179.6 -67.1 11.4 55 LEU -125.8 17.1 179.9 -57.0 178.2 56 LYS -73.0 -10.5 178.6 67.0 164.7 168.3 -74.0 57 ASP -110.6 26.3 179.6 -77.6 4.2 58 ARG -120.8 134.9 -179.7 -81.6 71.5 -177.8 174.7 59 PRO -35.2 -54.2 -178.4 -28.8 43.4 60 PHE -67.1 -24.6 -178.1 56.6 70.9 61 PHE -34.6 -57.4 -179.8 -175.4 72.0 62 PRO -53.1 -45.6 -179.6 -33.4 45.2 63 GLY -65.3 -46.5 179.8 64 LEU -50.8 -41.8 179.2 173.2 55.5 65 VAL -70.2 -47.0 179.5 179.1 66 LYS -58.4 -37.2 -179.8 158.6 81.1 80.9 62.8 67 TYR -60.5 -66.8 -178.6 -147.2 -67.0 68 MET -58.6 -9.4 179.9 -69.7 -67.2 -85.2 69 ASN -103.3 -10.5 -178.3 175.2 70.3 70 SER -62.1 -24.1 179.7 68.1 71 GLY -157.2 168.9 179.7 72 PRO -68.5 153.9 179.1 29.7 -43.8 73 VAL -125.3 169.7 177.9 -59.8 74 VAL -120.3 106.6 -179.6 172.0 75 ALA -93.2 134.5 -178.3 76 MET -145.3 163.4 178.6 -49.5 163.6 -75.0 77 VAL -129.3 128.5 -179.6 -176.8 78 TRP -122.8 128.3 -179.5 -73.4 89.9 79 GLU -101.5 149.7 179.4 164.8 170.1 75.4 80 GLY 161.5 161.9 178.5 81 LEU -63.8 113.6 178.4 162.7 68.9 82 ASN 67.3 27.4 -179.5 -120.6 -50.6 83 VAL -46.8 -44.9 -178.9 -128.3 84 VAL -56.8 -54.6 -179.1 174.7 85 LYS -64.1 -57.2 -178.9 -178.6 173.5 -65.8 177.5 86 THR -66.6 -37.1 179.3 68.9 87 GLY -56.3 -44.2 179.1 88 ARG -65.4 -39.5 178.9 -58.9 -158.9 94.3 -143.4 89 VAL -60.6 -39.8 178.9 177.2 90 MET -65.5 -32.0 179.8 -71.6 175.4 59.0 91 LEU -73.2 -37.0 -178.3 -96.7 53.2 92 GLY 95.9 178.3 -179.9 93 GLU -59.7 155.5 179.4 -59.5 -59.3 -27.1 94 THR -66.9 -26.7 178.3 -48.3 95 ASN -95.6 103.8 -179.9 -179.1 -11.7 96 PRO -44.1 -27.6 179.8 -35.5 45.5 97 ALA -60.5 -29.9 -179.4 98 ASP -104.6 -6.5 179.9 -58.3 -26.1 99 SER -67.9 126.8 -179.0 -59.9 100 LYS -80.4 145.4 179.6 -58.5 -69.9 -179.5 48.6 101 PRO -53.7 138.6 -179.1 -36.9 45.0 102 GLY 110.4 -21.1 178.3 103 THR -94.5 157.0 179.8 61.6 104 ILE -49.1 -59.3 -179.7 -69.5 179.1 105 ARG -62.7 -40.7 -179.2 -72.4 -168.6 -177.5 102.9 106 GLY -62.0 -28.7 -179.6 107 ASP -95.6 -27.8 -175.2 -58.9 -45.1 108 PHE -114.8 -10.8 -179.6 -48.1 -67.3 109 CYS -137.8 167.2 -177.1 57.4 110 ILE -118.0 -52.1 -177.1 -51.6 170.7 111 GLN -98.1 148.5 179.5 -163.1 -175.7 75.5 112 VAL -64.9 -32.2 178.9 -154.6 113 GLY -57.1 -46.6 179.6 114 ARG -112.3 75.9 -179.6 -41.9 -105.9 156.3 -157.7 115 ASN -99.2 29.7 177.9 62.4 -13.8 116 ILE 40.6 -17.3 -175.9 60.3 171.9 117 ILE -153.4 162.7 178.7 -168.5 173.0 118 HIS -137.5 136.6 178.4 154.9 73.3 119 GLY -132.7 144.6 179.9 120 SER -59.7 140.3 -179.9 -55.4 121 ASP -81.4 -15.1 -179.4 51.6 -69.7 122 SER -164.5 164.7 179.0 64.4 123 VAL -59.8 -37.8 179.9 -78.1 124 LYS -63.9 -45.9 179.3 -154.9 169.6 -60.9 174.4 125 SER -69.1 -36.4 -179.7 -49.0 126 ALA -54.3 -59.1 -180.0 127 GLU -56.8 -39.4 178.3 -65.6 -61.7 -47.8 128 LYS -60.1 -56.3 -179.4 -79.6 179.4 162.7 55.7 129 GLU -57.9 -42.4 179.6 -68.0 175.0 -0.9 130 ILE -58.9 -43.4 179.3 -57.7 170.1 131 SER -68.2 -41.9 -179.5 -55.2 132 LEU -67.3 -34.4 -178.8 -173.5 -102.9 133 TRP -97.1 -28.6 -178.9 -72.4 81.9 134 PHE -121.6 153.4 177.9 -63.9 -83.7 135 LYS -95.0 143.0 -179.6 -60.7 -177.2 179.9 179.6 136 PRO -51.1 -28.3 179.0 33.5 -45.2 137 GLU -81.8 -2.4 -179.6 -161.3 174.3 -46.6 138 GLU -92.3 -17.6 178.4 -62.2 -177.9 -32.8 139 LEU -83.1 103.4 -179.0 -57.6 -148.2 140 VAL -78.2 135.3 179.1 -168.8 141 ASP -112.8 115.1 179.3 -65.0 -23.5 142 TYR -146.6 -178.3 179.5 59.5 -79.7 143 LYS -130.3 122.3 179.9 -176.3 168.1 177.8 168.8 144 SER -62.0 131.3 -178.5 24.4 145 CYS -59.4 -21.5 179.6 64.4 146 ALA -103.7 16.0 -178.8 147 HIS -54.7 -42.6 -179.4 -179.5 -91.7 148 ASP -74.4 -10.8 178.3 -62.3 -36.8 149 TRP -95.8 -12.6 178.7 -72.0 114.4 150 VAL -98.0 -35.5 -179.5 -177.0 151 TYR -124.4 179.7 0.0 -53.5 -74.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 33.782 47.570 3.933 2 ALA 30.149 48.380 5.060 3 ASN 29.919 50.976 7.840 4 LEU 30.883 51.396 11.496 5 GLU 28.214 51.336 14.256 6 ARG 27.680 52.093 17.953 7 THR 26.250 50.070 20.866 8 PHE 24.953 50.382 24.403 9 ILE 27.023 48.528 26.991 10 ALA 25.838 48.501 30.621 11 ILE 27.710 47.099 33.621 12 LYS 25.094 45.698 36.018 13 PRO 25.098 46.171 39.834 14 ASP 26.934 42.875 40.447 15 GLY 29.651 43.769 37.940 16 VAL 30.218 47.072 39.728 17 GLN 30.022 45.494 43.197 18 ARG 32.528 42.766 42.341 19 GLY 34.962 45.302 40.924 20 LEU 34.933 44.453 37.222 21 VAL 34.491 47.976 35.820 22 GLY 38.134 48.483 34.878 23 GLU 38.473 45.008 33.373 24 ILE 35.400 45.374 31.199 25 ILE 36.243 48.877 29.944 26 LYS 39.855 47.823 29.347 27 ARG 38.759 44.937 27.138 28 PHE 36.767 47.251 24.868 29 GLU 39.668 49.699 24.737 30 GLN 42.259 47.106 23.671 31 LYS 39.934 45.900 20.917 32 GLY 39.933 49.291 19.203 33 PHE 36.391 50.382 20.056 34 ARG 35.889 53.989 21.119 35 LEU 34.103 55.242 24.200 36 VAL 31.468 57.651 22.911 37 ALA 29.778 58.171 26.295 38 MET 29.833 56.835 29.864 39 LYS 27.955 57.549 33.102 40 PHE 27.623 55.987 36.566 41 LEU 24.067 55.925 37.995 42 ARG 21.461 53.875 39.894 43 ALA 18.774 53.256 37.277 44 SER 15.326 53.952 38.693 45 GLU 12.748 51.172 38.518 46 GLU 10.737 53.464 36.220 47 HIS 13.653 53.912 33.825 48 LEU 14.366 50.171 34.016 49 LYS 10.791 49.145 33.195 50 GLN 11.188 51.251 30.058 51 HIS 14.442 49.491 29.268 52 TYR 12.726 46.130 29.726 53 ILE 9.349 46.920 28.091 54 ASP 9.643 43.931 25.731 55 LEU 9.757 41.737 28.855 56 LYS 7.011 43.404 30.938 57 ASP 4.757 40.412 30.223 58 ARG 7.384 37.929 31.457 59 PRO 7.486 36.318 34.980 60 PHE 10.944 37.587 35.965 61 PHE 10.281 41.203 34.975 62 PRO 9.360 42.420 38.451 63 GLY 12.496 40.909 39.966 64 LEU 14.640 42.031 37.051 65 VAL 13.587 45.630 37.709 66 LYS 14.096 45.342 41.494 67 TYR 17.455 43.784 40.626 68 MET 18.843 46.420 38.284 69 ASN 17.866 49.102 40.794 70 SER 19.642 47.421 43.744 71 GLY 22.910 49.160 42.947 72 PRO 24.574 51.627 40.542 73 VAL 25.431 50.601 36.986 74 VAL 27.882 51.944 34.406 75 ALA 26.095 52.880 31.183 76 MET 28.277 53.367 28.095 77 VAL 28.239 53.757 24.324 78 TRP 30.980 52.173 22.185 79 GLU 31.559 52.997 18.540 80 GLY 33.220 50.740 15.992 81 LEU 32.809 48.590 12.905 82 ASN 30.175 46.049 13.997 83 VAL 30.289 46.983 17.710 84 VAL 26.860 45.461 18.388 85 LYS 27.691 42.010 16.983 86 THR 31.294 41.733 18.159 87 GLY 30.555 43.509 21.435 88 ARG 28.093 40.768 22.316 89 VAL 30.624 38.106 21.312 90 MET 33.078 39.789 23.700 91 LEU 30.358 39.636 26.351 92 GLY 29.702 35.948 25.813 93 GLU 26.345 34.198 25.956 94 THR 23.731 35.925 28.090 95 ASN 23.702 32.722 30.127 96 PRO 27.133 32.574 31.843 97 ALA 26.699 28.804 31.649 98 ASP 27.273 28.953 27.886 99 SER 29.740 31.848 27.851 100 LYS 33.070 30.565 26.599 101 PRO 36.309 31.241 28.524 102 GLY 37.927 34.423 27.269 103 THR 34.681 36.356 27.251 104 ILE 33.690 38.819 29.950 105 ARG 30.870 36.604 31.252 106 GLY 32.877 33.434 30.656 107 ASP 35.693 34.716 32.831 108 PHE 33.788 36.601 35.526 109 CYS 30.329 35.191 36.291 110 ILE 28.362 31.978 36.889 111 GLN 24.562 32.479 37.023 112 VAL 22.252 34.153 34.464 113 GLY 20.616 36.029 37.308 114 ARG 23.939 37.725 37.955 115 ASN 25.517 37.953 34.508 116 ILE 27.397 41.217 35.299 117 ILE 26.830 43.029 31.985 118 HIS 24.423 43.977 29.161 119 GLY 24.967 44.591 25.467 120 SER 22.443 45.601 22.810 121 ASP 21.088 42.670 20.817 122 SER 20.912 44.705 17.605 123 VAL 21.581 48.099 16.011 124 LYS 17.862 48.876 16.263 125 SER 17.826 48.091 20.013 126 ALA 21.172 49.876 20.373 127 GLU 19.832 53.203 19.157 128 LYS 16.705 52.792 21.322 129 GLU 18.771 52.083 24.450 130 ILE 21.277 54.840 23.687 131 SER 18.396 57.342 23.522 132 LEU 16.730 55.915 26.639 133 TRP 19.953 56.015 28.674 134 PHE 21.816 58.979 27.202 135 LYS 21.075 62.573 26.262 136 PRO 22.359 63.619 22.787 137 GLU 24.801 66.091 24.358 138 GLU 26.356 63.218 26.330 139 LEU 27.695 61.365 23.296 140 VAL 31.178 62.856 22.881 141 ASP 32.616 63.009 19.379 142 TYR 36.395 62.852 19.057 143 LYS 38.915 60.803 17.107 144 SER 41.148 58.089 18.523 145 CYS 44.830 58.679 17.678 146 ALA 45.183 55.063 16.525 147 HIS 42.048 55.159 14.357 148 ASP 43.927 54.735 11.073 149 TRP 45.774 51.747 12.549 150 VAL 42.498 50.044 13.493 151 TYR 40.750 50.875 10.233 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C/P S S S S S S/S S S S 10 S S/H H H H H H H H H 20 H H H H H H H H H H 30 H H/S S S S S/S S S S/S S 40 S S C H H H H H H H 50 H H H C C C C C C H 60 H H H H H H H H H H/S 70 S S S S S S S S S S 80 S H H H H H H H H H 90 H H C C T T T T/S S S 100 S C H H H H H H C C 110 T T T T C C S S S S 120 S H H H H H H H H H 130 H H H H T T T T/S S S 140 S S S C C H H H H H 150 H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E E 10 E h H H H H H h T h 20 H H H H H H H H H H 30 H h t E E E E E E E 40 E h H H H H H H 50 H h G G G g T t T h 60 H H H H H H H H h t 70 S E E E E E E E e 80 T h H H H H H H H H 90 H h S g G G G g t 100 T T h H H H H H h 110 t T T t e E E E e 120 S h H H H H H H H H 130 H H H h g G G G g 140 t T h H H H H 150 h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 60.2 37.7 88.6 2 ALA 0.0 0.0 80.1 3 ASN 9.4 7.7 80.7 4 LEU 92.6 62.7 63.9 5 GLU 98.8 71.3 60.5 6 ARG 137.6 65.9 55.1 7 THR 105.8 99.0 40.4 8 PHE 166.6 99.9 41.0 9 ILE 142.4 99.3 32.2 10 ALA 71.2 98.1 34.7 11 ILE 143.5 100.0 37.5 12 LYS 146.8 84.7 58.0 13 PRO 119.6 96.0 54.4 14 ASP 99.4 89.9 42.8 15 GLY 34.8 100.0 48.9 16 VAL 99.5 83.8 48.0 17 GLN 34.0 22.9 73.8 18 ARG 93.3 44.7 68.7 19 GLY 2.6 7.5 81.5 20 LEU 129.7 87.8 45.7 21 VAL 78.8 66.3 46.4 22 GLY 0.0 0.0 73.4 23 GLU 74.6 53.8 58.0 24 ILE 143.5 100.0 25.9 25 ILE 114.4 79.7 40.5 26 LYS 59.2 34.1 84.4 27 ARG 162.0 77.6 57.1 28 PHE 166.7 100.0 27.1 29 GLU 45.4 32.8 71.4 30 GLN 46.3 31.1 72.9 31 LYS 76.4 44.1 65.7 32 GLY 20.9 60.1 66.6 33 PHE 158.0 94.7 46.7 34 ARG 186.0 89.1 56.7 35 LEU 107.6 72.8 51.4 36 VAL 114.8 96.6 51.9 37 ALA 67.1 92.4 42.8 38 MET 96.1 60.3 47.0 39 LYS 119.2 68.7 59.3 40 PHE 69.5 41.7 59.2 41 LEU 97.5 65.9 56.5 42 ARG 89.2 42.7 77.8 43 ALA 71.6 98.7 47.9 44 SER 29.8 35.7 74.3 45 GLU 64.4 46.5 65.1 46 GLU 12.7 9.2 83.5 47 HIS 115.4 76.8 53.4 48 LEU 147.8 100.0 40.2 49 LYS 67.3 38.8 64.4 50 GLN 64.2 43.2 62.6 51 HIS 137.4 91.5 43.9 52 TYR 158.8 87.7 39.1 53 ILE 64.6 45.0 78.4 54 ASP 0.0 0.0 78.7 55 LEU 87.4 59.1 53.2 56 LYS 73.2 42.2 67.0 57 ASP 21.0 19.0 77.4 58 ARG 95.6 45.8 64.7 59 PRO 13.6 10.9 79.1 60 PHE 60.1 36.0 59.0 61 PHE 145.9 87.5 41.1 62 PRO 37.9 30.5 76.0 63 GLY 0.2 0.6 74.8 64 LEU 114.9 77.8 41.7 65 VAL 114.5 96.4 40.2 66 LYS 32.3 18.6 83.8 67 TYR 136.0 75.1 62.6 68 MET 154.7 97.1 31.4 69 ASN 85.1 70.4 64.3 70 SER 36.0 43.1 76.0 71 GLY 31.9 91.7 57.5 72 PRO 92.2 74.0 51.6 73 VAL 118.8 100.0 42.3 74 VAL 110.9 93.3 29.4 75 ALA 72.6 100.0 32.2 76 MET 159.3 99.9 31.2 77 VAL 118.8 100.0 30.2 78 TRP 203.9 99.5 30.3 79 GLU 91.0 65.7 50.5 80 GLY 34.3 98.5 45.1 81 LEU 71.8 48.6 68.4 82 ASN 70.5 58.3 62.6 83 VAL 118.8 100.0 45.0 84 VAL 110.2 92.8 58.5 85 LYS 36.1 20.8 79.0 86 THR 67.2 62.8 52.0 87 GLY 34.5 99.0 51.5 88 ARG 124.8 59.7 71.8 89 VAL 18.0 15.2 77.3 90 MET 127.1 79.7 43.0 91 LEU 146.4 99.0 42.6 92 GLY 29.3 84.2 65.9 93 GLU 43.7 31.5 80.0 94 THR 44.5 41.7 83.2 95 ASN 67.2 55.6 56.8 96 PRO 124.5 100.0 56.0 97 ALA 21.3 29.4 87.2 98 ASP 33.4 30.2 72.5 99 SER 83.6 100.0 57.2 100 LYS 26.0 15.0 81.0 101 PRO 27.5 22.1 80.6 102 GLY 0.5 1.5 82.1 103 THR 86.0 80.5 69.6 104 ILE 143.3 99.8 28.9 105 ARG 202.8 97.1 50.8 106 GLY 32.9 94.7 72.0 107 ASP 77.5 70.1 67.9 108 PHE 131.1 78.6 52.4 109 CYS 97.4 98.2 49.7 110 ILE 0.0 0.0 82.1 111 GLN 30.6 20.6 73.6 112 VAL 54.9 46.3 66.8 113 GLY 8.5 24.3 71.3 114 ARG 86.6 41.4 73.4 115 ASN 117.9 97.5 55.5 116 ILE 143.5 100.0 41.5 117 ILE 143.5 100.0 31.1 118 HIS 123.2 82.0 58.6 119 GLY 34.6 99.5 52.4 120 SER 83.6 100.0 63.3 121 ASP 44.8 40.6 77.3 122 SER 45.1 54.0 67.4 123 VAL 43.6 36.7 64.9 124 LYS 19.4 11.2 86.2 125 SER 61.4 73.4 69.8 126 ALA 72.4 99.7 54.7 127 GLU 62.0 44.8 77.7 128 LYS 37.5 21.6 77.3 129 GLU 119.4 86.1 51.2 130 ILE 136.4 95.1 45.6 131 SER 15.8 18.8 85.3 132 LEU 110.2 74.6 61.5 133 TRP 203.3 99.2 29.1 134 PHE 165.2 99.0 40.9 135 LYS 32.7 18.9 77.7 136 PRO 13.1 10.5 78.5 137 GLU 0.0 0.0 84.8 138 GLU 87.8 63.3 57.7 139 LEU 128.9 87.2 48.5 140 VAL 30.3 25.5 77.7 141 ASP 13.5 12.2 79.9 142 TYR 86.3 47.7 71.7 143 LYS 58.0 33.5 79.4 144 SER 46.2 55.2 56.5 145 CYS 0.0 0.0 88.0 146 ALA 26.3 36.2 60.1 147 HIS 108.5 72.2 54.8 148 ASP 21.8 19.7 79.6 149 TRP 11.9 5.8 85.0 150 VAL 76.5 64.4 61.8 151 TYR 136.6 75.5 55.2