Protein Data Bank File : 1cnt1 Title : CYTOKINE 06-JUN-96 1CNT Number of Amino Acid Residues : 150 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PRO HIS ARG ARG ASP LEU CYS SER ARG SER 10 ILE TRP LEU ALA ARG LYS ILE ARG SER ASP 20 LEU THR ALA LEU THR GLU SER TYR VAL LYS 30 HIS GLN GLY LEU TRP SER GLU LEU THR GLU 40 ALA GLU ARG LEU GLN GLU ASN LEU GLN ALA 50 TYR ARG THR PHE HIS VAL LEU LEU ALA ARG 60 LEU LEU GLU ASP GLN GLN VAL HIS PHE THR 70 PRO THR GLU GLY ASP PHE HIS GLN ALA ILE 80 HIS THR LEU LEU LEU GLN VAL ALA ALA PHE 90 ALA TYR GLN ILE GLU GLU LEU MET ILE LEU 100 LEU GLU TYR LYS ILE PRO ARG ASN GLU ALA 110 ASP GLY MET LEU PHE GLU LYS LYS LEU TRP 120 GLY LEU LYS VAL LEU GLN GLU LEU SER GLN 130 TRP THR VAL ARG SER ILE HIS ASP LEU ARG 140 PHE ILE SER SER HIS GLN THR GLY ILE PRO Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PRO 0.0 95.3 -178.7 -29.1 43.7 2 HIS -130.9 149.3 -179.3 -54.9 -73.7 3 ARG -53.4 -61.8 179.5 -66.6 159.3 -53.1 -170.9 4 ARG -51.9 -48.3 179.8 -71.3 173.0 -80.2 -169.3 5 ASP -55.2 -52.2 -179.7 -150.6 -40.7 6 LEU -59.5 -39.7 179.4 -143.9 27.4 7 CYS -62.2 -52.3 -179.8 -84.7 8 SER -66.5 -33.8 179.3 36.8 9 ARG -68.9 -35.0 178.1 -80.7 -168.1 -68.0 120.7 10 SER -70.5 -35.3 178.5 -66.4 11 ILE -68.7 -49.3 178.6 -73.1 161.9 12 TRP -54.2 -49.4 -179.2 178.7 93.9 13 LEU -62.6 -31.5 179.4 -176.1 54.5 14 ALA -70.9 -41.1 178.6 15 ARG -64.0 -43.5 179.1 -63.0 -153.7 159.7 163.9 16 LYS -59.5 -39.8 179.1 168.1 86.1 168.5 -59.2 17 ILE -66.3 -42.1 179.4 -62.6 174.9 18 ARG -57.9 -45.5 178.9 172.4 110.5 137.6 138.3 19 SER -63.6 -52.7 -179.8 -64.1 20 ASP -53.4 -40.7 -179.5 -73.2 11.5 21 LEU -59.2 -31.5 178.6 -79.0 177.5 22 THR -55.2 -61.5 -179.8 -57.0 23 ALA -61.0 -52.8 -179.2 24 LEU -58.0 -32.7 179.3 176.5 59.2 25 THR -72.6 -41.2 178.3 -57.3 26 GLU -59.1 -53.5 178.9 -104.1 73.8 -60.6 27 SER -53.1 -42.7 -179.3 -66.7 28 TYR -64.0 -51.4 -179.3 -178.8 86.0 29 VAL -56.6 -40.8 179.1 -60.1 30 LYS -66.9 -42.9 -179.5 -100.6 162.8 171.4 -85.9 31 HIS -60.8 -41.9 -179.4 -78.8 -121.7 32 GLN -88.1 2.4 179.8 -56.6 -55.9 -46.2 33 GLY 63.1 62.9 -179.8 34 LEU -129.3 -129.4 -62.4 -64.6 166.7 35 TRP 78.2 25.7 -179.5 -50.5 131.6 36 SER -75.9 139.9 179.6 177.8 37 GLU -120.5 39.3 179.4 -63.2 178.9 23.4 38 LEU -101.7 152.8 179.5 -56.6 174.0 39 THR -78.7 171.5 178.0 48.0 40 GLU -52.1 -48.8 -179.2 -65.8 -173.1 -51.0 41 ALA -55.7 -53.3 -179.4 42 GLU -60.7 -34.4 179.3 -62.6 172.2 -49.8 43 ARG -68.8 -45.8 179.3 -62.4 -177.9 -172.6 -122.4 44 LEU -62.0 -43.1 179.4 -74.8 166.5 45 GLN -60.4 -53.3 -179.5 -65.6 165.5 -169.6 46 GLU -58.8 -40.8 178.6 -67.2 174.0 -23.3 47 ASN -64.0 -45.4 -179.4 -90.9 57.3 48 LEU -58.3 -54.8 -179.4 -170.8 51.4 49 GLN -62.6 -26.1 179.7 -111.3 49.4 67.6 50 ALA -73.7 -53.1 -179.4 51 TYR -67.3 -29.0 177.0 -70.6 71.2 52 ARG -64.2 -42.0 179.3 -81.7 173.1 169.9 172.1 53 THR -72.3 -39.1 178.5 -61.2 54 PHE -59.6 -38.9 -179.2 -87.0 -35.6 55 HIS -61.6 -45.5 179.8 -156.3 -89.6 56 VAL -62.0 -41.1 179.5 174.3 57 LEU -65.5 -44.6 179.4 -91.4 48.8 58 LEU -68.5 -35.7 179.2 -87.1 -34.9 59 ALA -59.1 -39.8 179.1 60 ARG -72.2 -38.6 179.4 179.0 51.5 136.7 49.4 61 LEU -61.9 -43.2 179.5 -173.5 159.1 62 LEU -63.0 -50.0 -179.2 170.0 77.2 63 GLU -50.8 -40.9 179.8 -151.3 -121.3 64.6 64 ASP -70.8 -17.7 -179.8 -75.0 -14.7 65 GLN -84.8 -68.2 -178.9 -57.8 -55.3 -63.2 66 GLN -51.5 -33.1 -178.3 52.5 -158.2 26.3 67 VAL -103.7 1.8 -178.0 -173.8 68 HIS -148.5 -77.0 -176.6 -166.5 -41.4 69 PHE -63.1 -53.7 -179.4 -61.4 -45.4 70 THR -138.5 67.7 -179.8 52.5 71 PRO -46.7 -84.0 178.5 -35.0 46.3 72 THR -85.3 109.0 -178.2 -39.7 73 GLU -132.1 -74.1 179.8 -165.3 56.2 59.9 74 GLY 153.6 -129.9 -179.3 75 ASP -61.2 -12.5 -179.8 -107.1 -88.6 76 PHE -69.2 -51.7 179.8 -170.5 49.2 77 HIS -59.9 -32.6 179.4 -78.4 -4.2 78 GLN -69.7 -41.4 178.9 179.4 160.3 -32.9 79 ALA -60.7 -36.9 178.3 80 ILE -68.9 -41.3 179.1 -59.7 179.0 81 HIS -59.8 -39.6 -180.0 -77.9 -41.9 82 THR -69.6 -34.1 179.3 -44.1 83 LEU -64.9 -50.7 179.0 -172.5 58.9 84 LEU -49.9 -42.3 -179.6 -75.1 161.7 85 LEU -71.1 -35.3 178.6 -61.3 174.3 86 GLN -70.2 -41.7 -179.9 -67.5 176.6 143.1 87 VAL -63.9 -45.0 179.1 171.9 88 ALA -66.3 -40.1 180.0 89 ALA -67.7 -29.9 179.6 90 PHE -70.5 -47.4 178.8 -170.9 80.0 91 ALA -62.8 -37.1 178.0 92 TYR -64.3 -44.5 178.3 -65.2 -24.5 93 GLN -61.5 -38.1 178.4 -70.1 177.6 159.2 94 ILE -66.7 -37.3 178.9 -76.8 -52.8 95 GLU -62.8 -50.1 -179.5 -83.9 176.7 57.5 96 GLU -60.2 -34.8 179.0 -63.2 174.2 36.4 97 LEU -67.0 -48.7 179.7 -167.5 38.5 98 MET -53.6 -39.9 178.8 -65.0 -171.7 87.9 99 ILE -61.0 -52.7 179.9 -75.7 -62.1 100 LEU -63.4 -28.0 180.0 -94.1 50.1 101 LEU -91.9 -0.6 179.1 -97.3 34.6 102 GLU 61.6 43.9 177.9 -57.4 -171.8 41.4 103 TYR -109.7 137.2 -179.3 -67.5 -47.1 104 LYS -70.1 115.3 179.3 -178.1 48.4 -164.6 155.6 105 ILE -66.1 128.0 179.7 -63.5 176.5 106 PRO -67.3 154.0 178.4 -26.0 41.5 107 ARG -80.0 146.8 -177.7 0.0 0.0 0.0 0.0 108 ASN -65.9 122.2 179.6 -155.0 -36.2 109 GLU -113.8 16.9 -178.3 -54.8 170.0 -44.2 110 ALA -107.7 -42.3 -179.4 111 ASP -66.9 79.4 -179.9 -81.3 -51.5 112 GLY 167.5 -71.2 179.3 113 MET -177.5 157.8 -96.5 172.4 44.9 111.6 114 LEU -62.2 -82.8 -179.9 -73.4 149.7 115 PHE -63.9 -39.6 179.0 -163.5 42.8 116 GLU -55.1 -49.0 179.6 -173.6 178.5 -18.9 117 LYS -58.8 -57.1 179.8 -71.2 171.4 171.6 176.1 118 LYS -45.3 -47.4 -179.7 -57.8 169.6 -177.0 -64.4 119 LEU -67.0 -50.2 179.8 -70.8 174.3 120 TRP -50.9 -52.4 -179.7 165.0 69.3 121 GLY -58.2 -34.5 178.9 122 LEU -70.6 -37.9 179.2 177.4 64.9 123 LYS -63.5 -48.9 179.5 -169.7 48.2 173.6 162.8 124 VAL -52.9 -53.6 180.0 -178.2 125 LEU -60.0 -36.1 180.0 -72.4 -178.4 126 GLN -71.9 -42.3 179.5 -65.4 -179.5 124.2 127 GLU -67.1 -39.7 178.6 -65.7 -66.4 68.5 128 LEU -59.3 -38.3 -179.5 172.6 45.8 129 SER -66.3 -45.0 179.4 -160.6 130 GLN -60.8 -38.3 -180.0 -80.0 -69.6 61.8 131 TRP -62.0 -37.1 -179.6 -110.2 107.2 132 THR -61.9 -31.9 178.7 63.4 133 VAL -65.0 -50.9 178.9 178.8 134 ARG -53.2 -52.7 179.9 156.2 104.2 123.9 105.0 135 SER -51.2 -49.1 179.9 -61.1 136 ILE -59.8 -37.9 178.2 -66.0 159.1 137 HIS -67.6 -49.1 178.9 -80.5 153.4 138 ASP -55.9 -47.1 -178.9 -71.1 -20.8 139 LEU -64.3 -37.6 179.2 -69.5 178.7 140 ARG -63.2 -42.6 179.1 -64.6 -145.0 -159.2 156.5 141 PHE -58.7 -51.5 179.9 165.9 61.0 142 ILE -64.4 -37.0 -179.3 -59.6 169.7 143 SER -61.5 -33.6 -179.2 -171.0 144 SER -60.0 -28.0 -178.9 -72.1 145 HIS -91.0 0.2 -177.8 -45.4 172.2 146 GLN -94.8 95.1 176.7 -52.6 -47.7 -47.1 147 THR -108.3 179.2 179.8 41.8 148 GLY -76.3 13.3 -178.2 149 ILE -75.4 123.0 179.7 -59.8 177.5 150 PRO -62.4 137.4 0.0 -30.8 43.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PRO 49.334 14.467 108.356 2 HIS 50.872 13.137 105.142 3 ARG 51.628 14.716 101.753 4 ARG 49.614 12.402 99.482 5 ASP 46.747 12.471 101.997 6 LEU 46.747 16.279 102.261 7 CYS 46.731 16.709 98.466 8 SER 43.652 14.599 97.862 9 ARG 41.881 16.126 100.897 10 SER 42.619 19.645 99.608 11 ILE 41.341 18.644 96.160 12 TRP 38.192 17.127 97.646 13 LEU 37.625 20.303 99.678 14 ALA 38.096 22.549 96.647 15 ARG 35.460 20.574 94.705 16 LYS 33.124 20.702 97.723 17 ILE 33.496 24.532 97.838 18 ARG 32.712 24.851 94.092 19 SER 29.431 22.889 94.469 20 ASP 28.182 24.763 97.547 21 LEU 28.736 28.059 95.756 22 THR 26.244 27.039 93.064 23 ALA 23.346 26.921 95.548 24 LEU 24.711 29.701 97.790 25 THR 25.257 32.135 94.897 26 GLU 21.684 31.574 93.698 27 SER 20.436 32.153 97.235 28 TYR 22.559 35.310 97.401 29 VAL 21.396 36.906 94.120 30 LYS 17.735 36.403 95.058 31 HIS 18.207 37.819 98.569 32 GLN 19.843 41.005 97.300 33 GLY 17.405 41.367 94.394 34 LEU 19.744 40.873 91.434 35 TRP 49.382 26.493 80.936 36 SER 50.912 27.476 84.278 37 GLU 54.683 27.526 84.678 38 LEU 54.816 28.063 88.434 39 THR 56.611 25.750 90.834 40 GLU 54.883 23.771 93.593 41 ALA 55.984 26.604 95.898 42 GLU 54.702 29.542 93.854 43 ARG 51.332 27.791 93.444 44 LEU 50.918 27.074 97.188 45 GLN 51.817 30.648 98.108 46 GLU 49.321 32.208 95.666 47 ASN 46.605 29.770 96.792 48 LEU 47.318 30.537 100.452 49 GLN 47.167 34.284 99.970 50 ALA 44.010 33.943 97.873 51 TYR 41.968 31.996 100.388 52 ARG 43.267 34.124 103.268 53 THR 41.874 37.157 101.420 54 PHE 38.665 35.378 100.447 55 HIS 38.160 34.706 104.130 56 VAL 38.481 38.386 105.054 57 LEU 36.074 39.240 102.220 58 LEU 33.422 36.648 103.165 59 ALA 33.641 37.658 106.826 60 ARG 32.695 41.125 105.609 61 LEU 30.043 39.703 103.269 62 LEU 28.446 37.844 106.198 63 GLU 28.734 40.936 108.323 64 ASP 26.723 42.951 105.761 65 GLN 23.913 40.398 105.887 66 GLN 23.283 39.797 109.572 67 VAL 23.701 43.519 110.387 68 HIS 22.097 45.020 107.271 69 PHE 20.588 43.162 104.299 70 THR 18.927 40.060 105.785 71 PRO 19.236 40.102 109.635 72 THR 16.686 37.489 110.781 73 GLU 16.575 35.089 107.836 74 GLY 17.463 31.422 108.260 75 ASP 19.564 28.781 106.487 76 PHE 21.263 31.546 104.502 77 HIS 23.444 32.953 107.312 78 GLN 24.314 29.317 108.090 79 ALA 25.341 28.557 104.487 80 ILE 27.738 31.528 104.691 81 HIS 29.151 30.262 108.030 82 THR 29.842 26.956 106.323 83 LEU 31.592 28.642 103.381 84 LEU 33.858 30.558 105.773 85 LEU 34.865 27.282 107.503 86 GLN 35.603 25.511 104.229 87 VAL 37.690 28.511 103.108 88 ALA 39.623 28.686 106.393 89 ALA 40.124 24.920 106.378 90 PHE 41.489 25.033 102.796 91 ALA 44.121 27.660 103.632 92 TYR 45.067 25.654 106.742 93 GLN 45.516 22.507 104.599 94 ILE 47.672 24.477 102.138 95 GLU 49.694 25.699 105.130 96 GLU 50.216 22.171 106.442 97 LEU 51.282 21.034 102.978 98 MET 53.874 23.817 102.715 99 ILE 55.284 22.624 106.047 100 LEU 55.566 19.014 104.839 101 LEU 57.044 20.121 101.514 102 GLU 59.465 22.361 103.385 103 TYR 58.351 25.592 101.742 104 LYS 58.429 28.809 103.762 105 ILE 54.863 29.845 104.581 106 PRO 54.210 33.518 103.712 107 ARG 53.209 35.892 106.524 108 ASN 49.541 36.977 106.544 109 GLU 48.876 40.190 104.599 110 ALA 45.108 39.818 104.832 111 ASP 44.153 40.102 108.516 112 GLY 43.858 43.884 108.613 113 MET 43.087 45.307 105.189 114 LEU 23.940 49.276 99.248 115 PHE 24.115 48.373 95.553 116 GLU 27.929 48.597 95.585 117 LYS 27.913 45.981 98.357 118 LYS 25.359 43.748 96.606 119 LEU 27.562 43.800 93.502 120 TRP 30.819 43.427 95.434 121 GLY 29.526 40.359 97.280 122 LEU 28.480 38.704 94.018 123 LYS 31.949 39.360 92.607 124 VAL 33.619 37.809 95.674 125 LEU 31.517 34.634 95.365 126 GLN 32.198 34.463 91.625 127 GLU 35.977 34.897 91.908 128 LEU 36.085 32.350 94.730 129 SER 34.362 29.866 92.441 130 GLN 36.888 30.493 89.677 131 TRP 39.644 30.040 92.222 132 THR 38.588 26.516 93.209 133 VAL 39.131 25.457 89.591 134 ARG 42.627 26.963 89.672 135 SER 43.288 25.256 93.013 136 ILE 42.307 21.796 91.721 137 HIS 44.706 22.109 88.782 138 ASP 47.570 23.263 91.022 139 LEU 46.886 20.463 93.484 140 ARG 46.728 17.822 90.775 141 PHE 50.151 18.989 89.525 142 ILE 51.656 18.868 93.027 143 SER 50.011 15.506 93.850 144 SER 51.848 13.810 90.961 145 HIS 55.199 14.292 92.643 146 GLN 54.083 12.770 95.914 147 THR 55.406 9.233 96.178 148 GLY 56.446 7.729 99.512 149 ILE 59.973 9.118 99.034 150 PRO 61.209 11.195 102.027 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C H H H H H H H H H 10 H H H H H H H H H H 20 H H/H H H H H H H H H 30 H H H C/X X/S S S S S/H H 40 H H H H H H H H H H 50 H H H H H H H H H H 60 H H H H H H H H S S 70 S S/S S S S/H H H H H H 80 H H H H H H H H H H 90 H H H H H H H H H H 100 H H/S S S S S S S C C 110 C C C/X X/H H H H H H H 120 H H H H H H H H H H 130 H H H H H H H H H H 140 H H H H H H C 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 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H h T t h H 40 H H H H H H H H H H 50 H H H H H H H H H H 60 H H H H H H h T T t 70 S S h H H H H H H 80 H H H H H H H H H H 90 H H H H H H H H H H 100 h T t S S 110 S h H H H H H H 120 H H H H H H H H H H 130 H H H H H H H H H H 140 H H H h T t S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PRO 22.5 18.1 82.9 2 HIS 28.1 18.7 81.5 3 ARG 153.4 73.5 61.0 4 ARG 73.9 35.4 74.0 5 ASP 45.5 41.1 73.1 6 LEU 147.7 100.0 55.0 7 CYS 99.2 100.0 47.1 8 SER 23.3 27.9 73.4 9 ARG 103.9 49.7 73.8 10 SER 83.6 100.0 44.7 11 ILE 115.1 80.2 49.6 12 TRP 56.6 27.6 71.5 13 LEU 133.4 90.3 47.0 14 ALA 72.6 100.0 43.8 15 ARG 87.2 41.7 70.2 16 LYS 90.4 52.2 65.7 17 ILE 143.5 100.0 34.8 18 ARG 95.3 45.6 73.4 19 SER 18.1 21.7 83.7 20 ASP 64.2 58.1 65.4 21 LEU 145.7 98.6 45.0 22 THR 21.5 20.1 85.3 23 ALA 5.7 7.9 80.2 24 LEU 138.3 93.6 37.3 25 THR 82.4 77.1 48.9 26 GLU 41.9 30.3 69.2 27 SER 41.2 49.3 59.7 28 TYR 177.9 98.3 38.8 29 VAL 81.6 68.7 48.4 30 LYS 17.5 10.1 83.3 31 HIS 106.9 71.2 55.8 32 GLN 147.0 98.9 47.0 33 GLY 0.0 0.0 82.4 34 LEU 118.7 80.3 39.9 35 TRP 0.0 0.0 97.6 36 SER 48.8 58.4 74.5 37 GLU 0.0 0.0 91.4 38 LEU 97.4 65.9 78.9 39 THR 26.6 24.9 72.7 40 GLU 114.8 82.8 49.1 41 ALA 51.5 70.9 54.3 42 GLU 66.8 48.2 70.1 43 ARG 190.8 91.3 55.0 44 LEU 146.3 99.0 28.5 45 GLN 81.3 54.7 58.0 46 GLU 76.2 54.9 66.9 47 ASN 119.4 98.8 42.5 48 LEU 147.7 100.0 46.2 49 GLN 110.4 74.3 64.3 50 ALA 59.0 81.3 52.8 51 TYR 180.9 100.0 34.1 52 ARG 181.8 87.0 56.4 53 THR 48.7 45.5 60.8 54 PHE 153.6 92.1 35.3 55 HIS 91.8 61.1 52.7 56 VAL 72.3 60.9 66.4 57 LEU 98.1 66.4 48.9 58 LEU 147.4 99.8 26.4 59 ALA 33.1 45.6 66.7 60 ARG 88.9 42.6 73.1 61 LEU 143.7 97.3 34.2 62 LEU 131.3 88.8 53.4 63 GLU 57.5 41.5 72.3 64 ASP 101.6 92.0 54.7 65 GLN 147.0 98.9 49.5 66 GLN 91.8 61.8 54.4 67 VAL 26.7 22.5 77.9 68 HIS 82.5 54.9 62.5 69 PHE 154.6 92.7 56.4 70 THR 90.0 84.2 60.0 71 PRO 62.5 50.2 80.2 72 THR 0.0 0.0 86.9 73 GLU 81.0 58.4 65.6 74 GLY 2.4 6.8 81.0 75 ASP 3.5 3.2 84.5 76 PHE 158.7 95.1 46.7 77 HIS 124.5 82.9 58.1 78 GLN 34.0 22.9 80.0 79 ALA 37.8 52.1 63.6 80 ILE 141.8 98.8 34.1 81 HIS 66.0 43.9 63.1 82 THR 48.4 45.3 68.0 83 LEU 146.4 99.1 35.2 84 LEU 130.6 88.3 46.3 85 LEU 27.0 18.3 78.6 86 GLN 137.6 92.6 43.8 87 VAL 118.7 99.9 31.7 88 ALA 56.4 77.7 57.9 89 ALA 34.7 47.9 63.4 90 PHE 166.7 99.9 40.8 91 ALA 67.1 92.4 49.2 92 TYR 56.5 31.2 77.0 93 GLN 127.9 86.0 58.0 94 ILE 143.0 99.7 35.7 95 GLU 94.3 68.0 52.0 96 GLU 64.5 46.5 59.5 97 LEU 147.8 100.0 32.9 98 MET 159.4 100.0 39.1 99 ILE 43.1 30.0 69.6 100 LEU 103.1 69.8 57.0 101 LEU 134.6 91.1 44.5 102 GLU 6.9 5.0 90.3 103 TYR 124.3 68.7 56.5 104 LYS 8.3 4.8 88.6 105 ILE 116.5 81.2 52.1 106 PRO 89.6 72.0 61.0 107 ARG 132.4 63.4 89.5 108 ASN 82.2 68.0 69.6 109 GLU 18.9 13.6 85.0 110 ALA 64.5 88.8 65.8 111 ASP 24.2 21.9 78.4 112 GLY 0.0 0.0 82.5 113 MET 0.0 0.0 88.5 114 LEU 37.5 25.4 73.7 115 PHE 54.0 32.4 60.8 116 GLU 0.1 0.1 81.9 117 LYS 110.0 63.5 64.3 118 LYS 131.5 75.8 52.4 119 LEU 66.0 44.7 59.4 120 TRP 132.4 64.6 54.3 121 GLY 34.3 98.6 48.6 122 LEU 112.1 75.9 49.7 123 LYS 62.7 36.2 79.4 124 VAL 113.3 95.4 36.4 125 LEU 145.8 98.6 33.9 126 GLN 69.4 46.7 63.9 127 GLU 67.5 48.7 61.9 128 LEU 147.8 100.0 23.9 129 SER 58.8 70.4 61.7 130 GLN 34.4 23.1 84.3 131 TRP 154.7 75.5 57.9 132 THR 106.9 100.0 46.3 133 VAL 73.7 62.1 76.7 134 ARG 128.5 61.5 63.5 135 SER 83.6 100.0 49.0 136 ILE 126.6 88.2 53.6 137 HIS 39.1 26.1 75.9 138 ASP 106.7 96.6 57.2 139 LEU 146.9 99.4 36.2 140 ARG 87.1 41.7 71.0 141 PHE 96.5 57.9 71.2 142 ILE 142.8 99.5 35.7 143 SER 53.6 64.1 58.5 144 SER 18.8 22.5 82.7 145 HIS 72.3 48.1 68.9 146 GLN 137.5 92.5 51.3 147 THR 34.3 32.1 74.8 148 GLY 19.1 55.0 80.9 149 ILE 20.4 14.2 82.0 150 PRO 20.4 16.4 86.9