Protein Data Bank File : 1dv9 Title : TRANSPORT PROTEIN 20-JAN-00 1DV9 Number of Amino Acid Residues : 162 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA TYR VAL THR GLN THR MET LYS GLY LEU 10 ASP ILE GLN LYS VAL ALA GLY THR TRP TYR 20 SER LEU ALA MET ALA ALA SER ASP ILE SER 30 LEU LEU ASP ALA GLN SER ALA PRO LEU ARG 40 VAL TYR VAL GLU GLU LEU LYS PRO THR PRO 50 GLU GLY ASP LEU GLU ILE LEU LEU GLN LYS 60 TRP GLU ASN ASP GLU CYS ALA GLN LYS LYS 70 ILE ILE ALA GLU LYS THR LYS ILE PRO ALA 80 VAL PHE LYS ILE ASP ALA LEU ASN GLU ASN 90 LYS VAL LEU VAL LEU ASP THR ASP TYR LYS 100 LYS TYR LEU LEU PHE CYS MET GLU ASN SER 110 ALA GLU PRO GLU GLN SER LEU VAL CYS GLN 120 CYS LEU VAL ARG THR PRO GLU VAL ASP ASP 130 GLU ALA LEU GLU LYS PHE ASP LYS ALA LEU 140 LYS ALA LEU PRO MET HIS ILE ARG LEU SER 150 PHE ASN PRO THR GLN LEU GLU GLU GLN CYS 160 HIS ILE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 124.8 -180.0 2 TYR -85.2 162.1 -179.9 60.7 -111.1 3 VAL -131.3 104.1 180.0 -171.9 4 THR -161.2 81.9 180.0 -13.9 5 GLN -148.7 -62.6 179.9 -81.0 -76.3 78.3 6 THR -108.3 99.8 -179.9 23.5 7 MET -50.2 -55.9 -179.9 -176.7 48.8 -175.7 8 LYS 59.6 154.3 -179.9 178.8 179.4 -91.1 161.2 9 GLY 50.0 47.0 -179.9 10 LEU -112.9 129.7 179.8 170.2 135.3 11 ASP -70.9 113.2 -179.8 -83.8 104.8 12 ILE -59.3 -53.6 -179.6 -59.3 -73.6 13 GLN -62.3 -16.3 -179.8 -83.3 -85.2 -17.3 14 LYS -65.9 -23.6 180.0 -118.7 -63.0 -153.1 -86.2 15 VAL -94.4 25.6 180.0 -64.1 16 ALA -93.9 114.8 -180.0 17 GLY 153.7 -152.8 -180.0 18 THR -98.2 141.2 179.9 33.0 19 TRP -132.3 177.1 -180.0 -76.8 83.5 20 TYR -154.6 160.9 180.0 -52.5 -89.5 21 SER -91.5 147.1 -180.0 63.2 22 LEU -126.1 -43.5 180.0 175.6 123.3 23 ALA -162.3 156.6 -180.0 24 MET -140.1 135.6 -180.0 -57.5 165.8 150.4 25 ALA -132.7 100.3 180.0 26 ALA -106.2 153.7 -180.0 27 SER -82.1 -29.1 180.0 166.7 28 ASP -103.9 121.2 180.0 -120.3 -26.0 29 ILE -59.7 -49.8 -179.9 -47.4 120.6 30 SER -58.9 -23.9 -179.9 -139.8 31 LEU -74.5 -32.6 179.9 -91.1 46.4 32 LEU -147.5 77.2 -180.0 -178.3 50.0 33 ASP -145.9 -70.3 -180.0 177.0 -90.4 34 ALA -155.1 175.5 180.0 35 GLN 70.0 37.6 -180.0 -129.9 175.8 0.1 36 SER 54.6 59.3 -180.0 -170.0 37 ALA -58.5 142.3 -180.0 38 PRO -49.6 -50.6 179.9 -26.9 33.3 39 LEU -66.7 -32.0 179.9 -92.2 -50.5 40 ARG -58.8 88.5 -180.0 -154.2 -97.3 -160.4 170.6 41 VAL -131.9 132.6 -179.9 -70.7 42 TYR -94.5 74.8 179.9 174.5 -145.6 43 VAL -47.5 149.3 -179.8 58.2 44 GLU -140.8 -44.2 -179.7 64.3 -176.0 13.7 45 GLU -126.6 152.1 179.8 -152.9 -144.3 -45.8 46 LEU -154.3 118.5 -179.8 -136.5 81.5 47 LYS -159.9 117.6 -179.8 177.2 165.4 156.2 -148.5 48 PRO -85.0 172.8 179.9 32.4 -30.4 49 THR -102.7 160.3 179.9 37.4 50 PRO -58.9 -17.5 179.9 17.8 -30.7 51 GLU -72.4 -40.8 180.0 -79.1 -173.0 -69.5 52 GLY 142.2 -20.5 -180.0 53 ASP -64.6 169.2 -179.9 -54.9 -165.3 54 LEU -131.4 123.2 180.0 178.1 75.6 55 GLU -86.9 99.1 -180.0 -156.3 132.9 -124.4 56 ILE -93.8 94.3 180.0 -42.3 -176.2 57 LEU -86.4 107.8 -180.0 -118.9 77.6 58 LEU -118.8 154.6 179.9 45.1 123.7 59 GLN -114.1 113.2 -179.9 -106.0 -142.1 -8.5 60 LYS -140.1 143.8 -180.0 177.8 -148.5 -77.2 -167.1 61 TRP -57.1 110.2 180.0 -167.2 -15.0 62 GLU -109.8 -37.0 180.0 -132.7 -116.9 140.7 63 ASN 174.1 -36.0 -179.9 47.4 14.4 64 ASP -93.1 39.2 179.9 -50.0 -23.5 65 GLU 50.0 99.1 179.9 -143.2 139.5 -84.0 66 CYS 61.6 79.3 179.9 -57.9 67 ALA -96.6 148.0 -179.9 68 GLN -101.9 121.6 179.9 70.9 -158.4 -79.0 69 LYS -110.5 179.0 -180.0 -56.3 -69.8 160.1 -126.3 70 LYS -154.0 127.2 180.0 51.1 -134.7 65.4 111.4 71 ILE -108.2 124.8 -179.9 -49.2 176.0 72 ILE -89.9 77.1 180.0 -43.2 120.6 73 ALA -58.2 124.1 179.9 74 GLU -85.8 162.5 179.9 -99.6 122.4 -20.7 75 LYS -90.1 156.5 -180.0 -177.4 165.9 -82.5 -90.7 76 THR -121.5 -61.5 -180.0 52.9 77 LYS -169.8 -42.5 -179.9 -173.9 65.0 146.9 141.5 78 ILE -107.0 133.0 180.0 -39.5 -58.9 79 PRO -53.7 -21.4 -180.0 -24.4 33.1 80 ALA -94.3 24.8 180.0 81 VAL -154.9 122.5 -179.9 -168.6 82 PHE -128.3 164.8 179.9 -53.2 -83.8 83 LYS -124.1 120.8 -179.9 -94.4 -66.8 -91.8 -139.7 84 ILE -118.1 169.0 -179.9 63.2 178.0 85 ASP -147.2 69.1 -180.0 -143.3 15.6 86 ALA -145.2 -80.3 -180.0 87 LEU -70.3 -171.6 179.9 -104.2 47.6 88 ASN -81.1 57.2 -180.0 -96.1 90.7 89 GLU -179.3 113.2 -180.0 36.8 -106.0 -60.0 90 ASN -91.3 -29.0 -180.0 46.6 -109.8 91 LYS -88.1 139.8 180.0 -112.3 128.8 125.1 109.9 92 VAL -136.8 108.6 180.0 -166.6 93 LEU -101.3 143.8 180.0 35.0 154.2 94 VAL -99.9 108.6 179.9 -178.5 95 LEU -66.7 -76.4 -180.0 -94.1 -76.9 96 ASP -151.7 179.6 179.9 -112.6 47.6 97 THR -179.3 171.1 179.8 176.5 98 ASP -131.1 21.7 -180.0 -98.3 -108.0 99 TYR 61.0 -80.7 -179.9 -77.2 -45.6 100 LYS -100.2 56.7 180.0 -38.2 162.1 -110.0 149.4 101 LYS -158.6 -64.0 179.9 -138.8 121.7 -131.2 103.1 102 TYR -163.4 175.2 180.0 50.3 -117.2 103 LEU -143.9 139.0 179.9 180.0 121.0 104 LEU -123.4 119.7 -180.0 -97.4 75.4 105 PHE -133.9 166.5 -179.9 68.8 -70.2 106 CYS -137.4 153.0 180.0 -123.1 107 MET -128.4 138.2 -180.0 -90.9 154.1 -173.0 108 GLU -157.6 165.4 -180.0 71.5 -152.3 -169.9 109 ASN -119.9 126.6 180.0 -148.3 -85.8 110 SER -50.4 -25.3 180.0 87.7 111 ALA -76.4 -39.8 179.9 112 GLU -150.0 72.5 -180.0 -108.2 155.6 -161.6 113 PRO -55.6 -64.4 -179.9 -23.1 32.6 114 GLU -50.3 -33.0 -180.0 -61.0 -136.9 170.3 115 GLN -81.3 -25.2 -180.0 -112.6 -69.4 3.0 116 SER -113.6 22.5 179.9 -90.9 117 LEU -76.1 120.9 -180.0 -123.9 177.3 118 VAL -152.4 137.6 180.0 58.6 119 CYS -133.5 145.3 -180.0 -110.4 120 GLN -147.1 160.8 180.0 -47.9 174.8 -46.9 121 CYS -126.8 132.7 179.9 40.8 122 LEU -112.7 131.3 -180.0 -39.4 -168.5 123 VAL -102.3 144.9 -179.9 67.3 124 ARG -82.4 -26.2 179.9 -107.4 -146.4 126.3 158.9 125 THR -83.7 130.0 180.0 26.2 126 PRO -65.1 61.3 -180.0 -15.7 29.3 127 GLU 167.6 154.7 179.9 44.0 -127.7 124.4 128 VAL -54.8 155.5 179.8 -165.7 129 ASP -145.6 116.4 -179.8 -157.7 -28.3 130 ASP -46.7 -18.3 -179.4 48.5 -0.1 131 GLU -75.8 -50.3 -179.9 65.2 -161.2 -156.8 132 ALA -66.3 -25.3 -179.5 133 LEU -72.7 -57.4 -179.4 -130.1 60.7 134 GLU -58.1 -57.5 -179.9 -101.0 -60.3 -16.4 135 LYS -51.3 -54.4 -179.8 -89.7 43.9 77.7 131.2 136 PHE -57.7 -30.9 179.8 179.1 87.8 137 ASP -79.2 -33.1 179.9 -111.0 -81.3 138 LYS -75.5 -29.3 -179.8 -92.9 -179.7 155.7 -89.6 139 ALA -84.5 -25.8 179.5 140 LEU -90.7 -17.1 -179.9 -102.1 -70.9 141 LYS -63.8 -14.0 -179.4 -110.0 -172.5 152.2 -105.5 142 ALA -101.0 -21.5 180.0 143 LEU -98.2 173.9 180.0 -108.5 97.9 144 PRO -70.1 179.0 179.9 26.3 -34.3 145 MET -164.8 -176.1 -180.0 40.8 -91.1 -149.0 146 HIS -177.2 -39.7 179.9 -117.1 -76.8 147 ILE -148.4 123.9 180.0 -174.3 105.5 148 ARG -110.3 162.9 180.0 -134.3 99.6 77.0 -168.3 149 LEU -147.5 131.9 -180.0 -76.4 151.7 150 SER -128.9 98.0 179.9 -152.2 151 PHE -56.5 151.9 179.9 -69.1 -96.0 152 ASN -124.3 151.8 180.0 -54.2 72.1 153 PRO -51.1 -29.3 180.0 -26.0 33.2 154 THR -74.0 -43.2 -180.0 53.9 155 GLN -77.3 -33.6 180.0 -129.2 165.1 83.2 156 LEU -75.6 -24.8 -180.0 -168.9 74.0 157 GLU -50.1 -63.5 -180.0 -164.0 129.8 -148.2 158 GLU -132.9 169.1 -179.9 -44.7 -164.7 156.1 159 GLN -152.6 120.0 179.9 -179.8 143.5 32.5 160 CYS 42.6 43.4 -180.0 74.2 161 HIS -78.0 164.3 -179.9 -156.6 88.8 162 ILE -97.0 77.4 0.0 -54.1 106.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 8.103 -6.352 6.351 2 TYR 6.880 -7.071 2.821 3 VAL 8.778 -6.260 -0.373 4 THR 6.833 -5.044 -3.407 5 GLN 7.819 -1.702 -4.934 6 THR 10.931 -1.777 -7.119 7 MET 11.075 -4.963 -9.191 8 LYS 14.633 -4.274 -10.347 9 GLY 16.587 -6.739 -12.463 10 LEU 13.678 -7.073 -14.878 11 ASP 14.133 -8.001 -18.537 12 ILE 12.613 -5.185 -20.591 13 GLN 12.325 -7.249 -23.780 14 LYS 10.720 -9.971 -21.645 15 VAL 7.512 -7.925 -21.690 16 ALA 7.412 -8.009 -25.490 17 GLY 4.212 -9.517 -26.852 18 THR 0.462 -9.564 -26.265 19 TRP -1.099 -8.727 -22.899 20 TYR -4.527 -8.364 -21.290 21 SER -6.293 -6.713 -18.355 22 LEU -7.397 -8.629 -15.262 23 ALA -8.136 -6.053 -12.565 24 MET -7.638 -2.386 -11.691 25 ALA -7.399 -0.597 -8.343 26 ALA -7.273 3.203 -8.369 27 SER -7.369 5.603 -5.421 28 ASP -9.484 8.152 -7.291 29 ILE -12.955 7.071 -8.410 30 SER -13.171 9.753 -11.094 31 LEU -9.815 8.453 -12.330 32 LEU -11.229 4.974 -12.940 33 ASP -15.026 4.820 -12.779 34 ALA -16.973 6.313 -15.685 35 GLN -16.978 9.053 -18.323 36 SER -13.886 7.623 -20.016 37 ALA -11.667 7.940 -16.945 38 PRO -7.960 8.609 -17.692 39 LEU -6.866 5.435 -15.905 40 ARG -9.729 3.537 -17.538 41 VAL -7.667 1.883 -20.274 42 TYR -8.196 -1.492 -21.944 43 VAL -4.577 -2.549 -22.466 44 GLU -4.006 -5.052 -25.275 45 GLU -0.356 -4.993 -26.357 46 LEU 2.918 -4.296 -24.551 47 LYS 6.450 -4.311 -25.962 48 PRO 9.457 -2.072 -25.123 49 THR 12.398 -1.089 -27.323 50 PRO 16.083 -2.141 -27.048 51 GLU 16.768 1.423 -25.900 52 GLY 14.798 1.042 -22.682 53 ASP 11.441 2.650 -23.435 54 LEU 8.162 0.745 -23.119 55 GLU 5.420 0.620 -25.757 56 ILE 2.140 0.626 -23.832 57 LEU -0.579 -0.107 -26.390 58 LEU -3.962 0.590 -24.798 59 GLN -7.474 0.782 -26.246 60 LYS -9.669 3.665 -25.092 61 TRP -12.605 5.543 -26.616 62 GLU -10.998 8.521 -28.354 63 ASN -13.477 9.251 -31.146 64 ASP -13.462 6.325 -33.579 65 GLU -15.286 4.077 -31.109 66 CYS -12.649 2.212 -29.100 67 ALA -9.376 3.699 -30.339 68 GLN -5.952 2.143 -29.773 69 LYS -3.219 4.412 -28.415 70 LYS 0.439 3.938 -27.487 71 ILE 2.621 5.552 -24.823 72 ILE 6.393 5.688 -25.284 73 ALA 7.485 5.420 -21.651 74 GLU 10.996 6.837 -21.297 75 LYS 13.742 5.422 -19.078 76 THR 15.015 7.029 -15.875 77 LYS 17.606 4.842 -14.150 78 ILE 15.966 1.749 -12.662 79 PRO 14.163 -0.869 -14.830 80 ALA 11.402 -0.717 -12.218 81 VAL 10.799 2.966 -12.954 82 PHE 9.696 4.703 -16.152 83 LYS 8.618 8.201 -17.186 84 ILE 5.524 8.839 -19.304 85 ASP 3.685 11.925 -20.555 86 ALA 0.059 11.139 -21.396 87 LEU -2.404 10.131 -18.678 88 ASN -2.577 11.629 -15.186 89 GLU 0.712 10.010 -14.172 90 ASN 4.267 10.546 -15.417 91 LYS 5.881 8.119 -12.972 92 VAL 5.555 4.370 -13.527 93 LEU 6.728 1.855 -10.927 94 VAL 6.884 -1.903 -11.495 95 LEU 5.385 -3.864 -8.601 96 ASP 5.809 -7.493 -9.658 97 THR 5.326 -9.947 -12.524 98 ASP 5.913 -13.487 -13.775 99 TYR 7.081 -12.752 -17.325 100 LYS 4.878 -15.409 -18.927 101 LYS 1.935 -15.047 -16.544 102 TYR 1.038 -11.495 -15.519 103 LEU 2.402 -8.034 -14.730 104 LEU 1.844 -5.580 -11.880 105 PHE 2.613 -1.873 -12.236 106 CYS 1.640 1.414 -10.588 107 MET 1.232 5.027 -11.702 108 GLU 1.660 8.240 -9.712 109 ASN 2.642 11.900 -10.019 110 SER 5.519 13.472 -8.091 111 ALA 3.155 16.423 -7.684 112 GLU 0.362 14.366 -6.124 113 PRO 1.292 10.667 -5.659 114 GLU -1.395 9.758 -3.126 115 GLN -3.811 11.640 -5.382 116 SER -2.483 9.907 -8.497 117 LEU -1.894 6.520 -6.860 118 VAL -3.110 3.702 -9.107 119 CYS -2.187 0.043 -9.592 120 GLN -3.254 -2.585 -12.125 121 CYS -2.424 -6.143 -13.182 122 LEU -2.115 -7.487 -16.725 123 VAL -2.465 -11.174 -17.588 124 ARG -0.791 -12.889 -20.544 125 THR -3.561 -15.479 -20.846 126 PRO -6.693 -14.324 -22.774 127 GLU -8.870 -14.851 -19.689 128 VAL -9.016 -14.321 -15.925 129 ASP -6.619 -16.333 -13.773 130 ASP -7.067 -17.085 -10.074 131 GLU -3.293 -16.481 -9.836 132 ALA -3.264 -12.832 -10.919 133 LEU -6.312 -12.235 -8.716 134 GLU -4.993 -13.534 -5.384 135 LYS -1.475 -12.128 -5.781 136 PHE -2.744 -8.734 -6.940 137 ASP -5.132 -8.787 -3.976 138 LYS -2.411 -9.802 -1.525 139 ALA -0.100 -7.061 -2.798 140 LEU -2.852 -4.395 -2.769 141 LYS -4.149 -5.431 0.670 142 ALA -1.262 -3.402 2.125 143 LEU -1.668 -0.251 0.014 144 PRO -4.612 2.230 -0.168 145 MET -7.687 1.867 -2.377 146 HIS -11.023 3.375 -3.407 147 ILE -12.297 1.607 -6.523 148 ARG -11.610 -1.919 -7.774 149 LEU -12.397 -3.635 -11.078 150 SER -12.618 -7.303 -12.060 151 PHE -13.055 -8.005 -15.773 152 ASN -15.246 -10.965 -16.731 153 PRO -15.081 -13.489 -19.621 154 THR -18.343 -11.975 -20.859 155 GLN -17.044 -8.400 -20.883 156 LEU -13.587 -9.446 -22.079 157 GLU -15.132 -11.495 -24.888 158 GLU -16.021 -8.494 -27.051 159 GLN -16.013 -4.697 -26.819 160 CYS -18.112 -2.155 -28.734 161 HIS -18.344 -4.687 -31.566 162 ILE -20.555 -4.269 -34.632 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S C C C C C 10 H H H H 3 3/S S S S S 20 S S S/S S S S S H H H 30 H H H C C C T T T T/S 40 S S S S S/S S S S S/T T 50 T T/S S S S S S S S S 60 S/T T T T S S S S S S 70 S S S S S S S T T T 80 T/S S S S S S C S S S 90 S/S S S S S S C T T T 100 T S S S S S S S C C 110 C H H H H H H/S S S S/S 120 S S S S C C C C H H 130 H H H H H H H H H H 140 H 3 3/S S S S S/S S S S 150 S S/H H H H H H 3 C S 160 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S 10 g G G G g E E e E 20 E E E E E E e t T T 30 T t S S S S S S 40 E E E E E E E e T 50 T t e E E E E E E E 60 S S S S S E E E E 70 E E E E E e S t T e 80 E E E e S S S e 90 E E E E E E E e S S 100 e E E E E E E E t T 110 T t T T T t e E E E 120 E E E e S S S h H 130 H H H H H H H H H H 140 h T t S E E E E 150 e h H H H H H h S S 160 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 94.5 2 TYR 56.9 31.4 74.4 3 VAL 1.6 1.4 88.8 4 THR 80.8 75.6 53.8 5 GLN 54.3 36.6 67.5 6 THR 45.8 42.9 63.1 7 MET 110.3 69.2 60.4 8 LYS 41.2 23.7 69.6 9 GLY 0.0 0.0 70.5 10 LEU 143.4 97.0 38.2 11 ASP 25.9 23.5 72.6 12 ILE 119.3 83.2 51.9 13 GLN 62.7 42.2 63.0 14 LYS 98.7 56.9 56.5 15 VAL 113.7 95.7 36.2 16 ALA 61.8 85.1 59.1 17 GLY 13.8 39.8 75.7 18 THR 30.7 28.8 73.9 19 TRP 203.7 99.4 46.1 20 TYR 128.9 71.2 58.4 21 SER 83.4 99.8 36.0 22 LEU 147.3 99.7 37.5 23 ALA 66.7 91.8 44.1 24 MET 156.0 97.9 41.5 25 ALA 72.2 99.5 46.9 26 ALA 72.6 100.0 47.4 27 SER 65.3 78.1 62.0 28 ASP 75.7 68.5 65.0 29 ILE 65.5 45.6 69.1 30 SER 5.7 6.8 76.3 31 LEU 121.1 81.9 51.7 32 LEU 147.3 99.7 38.8 33 ASP 59.6 53.9 55.2 34 ALA 16.2 22.3 83.6 35 GLN 0.0 0.0 88.7 36 SER 46.5 55.6 69.1 37 ALA 70.7 97.3 61.7 38 PRO 82.9 66.6 66.4 39 LEU 147.1 99.5 34.3 40 ARG 101.3 48.5 69.2 41 VAL 105.9 89.1 49.2 42 TYR 139.0 76.8 65.4 43 VAL 113.1 95.2 38.1 44 GLU 95.4 68.8 56.5 45 GLU 82.5 59.5 52.2 46 LEU 143.6 97.1 33.4 47 LYS 71.8 41.4 75.7 48 PRO 124.5 100.0 46.4 49 THR 51.1 47.8 68.6 50 PRO 32.1 25.8 75.6 51 GLU 13.1 9.4 85.2 52 GLY 30.7 88.2 59.7 53 ASP 83.2 75.3 59.0 54 LEU 130.4 88.3 34.9 55 GLU 73.6 53.1 56.6 56 ILE 130.3 90.8 31.9 57 LEU 122.7 83.0 58.6 58 LEU 140.3 94.9 34.2 59 GLN 109.1 73.4 62.2 60 LYS 139.7 80.5 63.1 61 TRP 63.4 30.9 79.4 62 GLU 65.6 47.4 72.2 63 ASN 43.0 35.6 82.2 64 ASP 12.6 11.4 81.9 65 GLU 39.8 28.7 68.9 66 CYS 80.3 80.9 54.3 67 ALA 62.4 86.0 71.3 68 GLN 59.0 39.7 76.1 69 LYS 99.4 57.3 65.0 70 LYS 84.6 48.8 64.9 71 ILE 127.9 89.1 39.4 72 ILE 38.8 27.1 80.8 73 ALA 72.5 99.8 44.6 74 GLU 38.8 28.0 84.2 75 LYS 112.1 64.7 62.2 76 THR 71.2 66.6 58.2 77 LYS 17.5 10.1 80.3 78 ILE 82.7 57.6 49.0 79 PRO 89.6 72.0 63.8 80 ALA 72.6 100.0 42.7 81 VAL 83.8 70.6 54.2 82 PHE 161.1 96.6 42.9 83 LYS 89.0 51.3 62.7 84 ILE 142.7 99.4 38.1 85 ASP 2.1 1.9 83.5 86 ALA 40.0 55.1 60.4 87 LEU 124.1 84.0 47.3 88 ASN 33.8 27.9 69.2 89 GLU 138.6 100.0 41.4 90 ASN 97.1 80.4 65.0 91 LYS 96.4 55.6 66.2 92 VAL 115.2 97.0 37.4 93 LEU 127.0 85.9 60.7 94 VAL 111.0 93.5 39.9 95 LEU 144.7 97.9 41.3 96 ASP 52.6 47.6 54.3 97 THR 105.6 98.8 34.9 98 ASP 52.5 47.5 65.9 99 TYR 126.6 70.0 56.4 100 LYS 44.7 25.8 79.0 101 LYS 76.9 44.4 73.4 102 TYR 162.4 89.7 40.2 103 LEU 135.5 91.7 29.7 104 LEU 143.8 97.3 34.2 105 PHE 145.3 87.1 41.3 106 CYS 98.1 98.9 35.2 107 MET 149.2 93.6 32.8 108 GLU 105.2 75.9 38.7 109 ASN 85.0 70.3 64.6 110 SER 28.3 33.8 69.5 111 ALA 10.7 14.7 84.0 112 GLU 35.3 25.5 69.5 113 PRO 68.8 55.2 65.6 114 GLU 3.5 2.6 77.8 115 GLN 53.7 36.1 80.5 116 SER 74.0 88.5 59.7 117 LEU 121.9 82.5 47.1 118 VAL 116.1 97.7 45.5 119 CYS 95.1 95.9 33.1 120 GLN 144.6 97.3 31.3 121 CYS 99.2 100.0 33.9 122 LEU 144.0 97.4 33.2 123 VAL 118.4 99.6 53.3 124 ARG 137.5 65.8 64.2 125 THR 44.2 41.3 66.5 126 PRO 57.1 45.9 66.7 127 GLU 46.8 33.8 67.2 128 VAL 87.4 73.6 51.0 129 ASP 79.4 71.8 68.5 130 ASP 6.9 6.2 81.3 131 GLU 102.6 74.0 56.2 132 ALA 72.6 100.0 31.6 133 LEU 86.6 58.6 65.1 134 GLU 42.3 30.5 70.8 135 LYS 79.8 46.0 65.3 136 PHE 162.7 97.5 39.1 137 ASP 47.9 43.4 71.7 138 LYS 39.6 22.8 79.9 139 ALA 54.1 74.5 58.4 140 LEU 140.0 94.7 46.8 141 LYS 29.8 17.2 84.1 142 ALA 43.7 60.2 69.8 143 LEU 112.7 76.2 53.9 144 PRO 58.6 47.1 54.9 145 MET 82.2 51.6 78.5 146 HIS 55.2 36.7 72.6 147 ILE 103.7 72.3 66.1 148 ARG 112.9 54.0 60.7 149 LEU 81.7 55.3 61.2 150 SER 34.9 41.7 69.0 151 PHE 126.8 76.0 55.9 152 ASN 45.8 37.9 73.7 153 PRO 42.5 34.1 65.5 154 THR 10.8 10.1 76.3 155 GLN 26.1 17.5 84.7 156 LEU 130.1 88.0 57.1 157 GLU 28.8 20.8 81.5 158 GLU 42.0 30.3 73.0 159 GLN 88.7 59.7 62.1 160 CYS 55.3 55.7 61.0 161 HIS 44.7 29.8 79.6 162 ILE 0.0 0.0 88.8