Protein Data Bank File : 1e30a Title : RUSTICYANIN 01-JUN-00 1E30 Number of Amino Acid Residues : 153 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU ASP THR THR TRP LYS GLU ALA THR LEU 10 PRO GLN VAL LYS ALA MET LEU GLU LYS ASP 20 THR GLY LYS VAL SER GLY ASP THR VAL THR 30 TYR SER GLY LYS THR VAL HIS VAL VAL ALA 40 ALA ALA VAL LEU PRO GLY PHE PRO PHE PRO 50 SER PHE GLU VAL HIS ASP LYS LYS ASN PRO 60 THR LEU GLU ILE PRO ALA GLY ALA THR VAL 70 ASP VAL THR PHE ILE ASN THR ASN LYS GLY 80 PHE GLY HIS SER PHE ASP ILE THR LYS LYS 90 GLY PRO PRO TYR ALA VAL MET PRO VAL ILE 100 ASP PRO ILE VAL ALA GLY THR GLY PHE SER 110 PRO VAL PRO LYS ASP GLY LYS PHE GLY TYR 120 THR ASN PHE THR TRP HIS PRO THR ALA GLY 130 THR TYR TYR TYR VAL CYS GLN ILE PRO GLY 140 HIS ALA ALA THR GLY GLN PHE GLY LYS ILE 150 VAL VAL LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 157.0 177.1 -62.0 173.1 2 ASP -76.8 120.9 -178.7 173.0 3.9 3 THR -128.5 28.6 -177.7 57.8 4 THR -110.9 106.8 -175.7 -62.5 5 TRP -107.1 129.0 179.3 -59.9 92.8 6 LYS -104.6 154.9 -179.9 -67.3 172.7 152.6 -179.5 7 GLU -94.1 145.1 176.5 -59.1 -175.0 3.4 8 ALA -144.2 141.4 174.6 9 THR -79.6 174.7 178.5 60.3 10 LEU -58.9 -51.3 178.8 -178.9 165.2 11 PRO -53.9 -38.7 178.8 -19.0 24.7 12 GLN -68.5 -41.5 175.7 -73.6 169.9 -40.3 13 VAL -56.5 -49.1 -177.5 165.0 14 LYS -60.6 -48.2 177.7 -69.4 -59.4 157.4 -177.3 15 ALA -52.4 -44.9 179.6 16 MET -68.8 -42.5 179.5 -70.9 -164.0 -78.1 17 LEU -60.7 -29.3 178.6 -68.3 163.9 18 GLU -75.6 -10.4 -179.8 -21.8 -60.0 12.6 19 LYS -83.1 -5.1 177.6 -167.5 107.1 -90.6 162.8 20 ASP -60.1 131.9 -174.7 -179.5 -86.4 21 THR -97.0 6.7 179.9 60.6 22 GLY -81.5 164.9 175.8 23 LYS -115.5 127.9 -177.5 56.3 -165.6 164.4 -177.5 24 VAL -85.6 139.9 171.2 -179.5 25 SER -142.0 123.3 -177.9 -72.7 26 GLY 63.9 -127.9 177.3 27 ASP -113.3 32.7 -178.5 -71.7 -80.1 28 THR -126.8 131.3 176.8 -64.9 29 VAL -100.5 115.6 -179.3 -174.3 30 THR -101.8 124.5 -180.0 -60.4 31 TYR -103.3 151.7 176.7 -61.7 85.4 32 SER -147.9 155.8 -180.0 51.5 33 GLY 112.3 167.9 -179.1 34 LYS -67.1 -39.2 178.5 -47.3 158.4 178.8 54.9 35 THR -123.3 128.6 -179.1 47.8 36 VAL -121.6 151.8 -179.9 -51.1 37 HIS -122.7 108.8 178.7 -169.2 -171.4 38 VAL -91.9 126.7 175.1 171.7 39 VAL -118.5 108.8 -176.8 -172.6 40 ALA -111.6 146.4 177.3 41 ALA -128.9 147.7 177.4 42 ALA -94.6 114.3 177.2 43 VAL 51.7 79.5 172.8 -167.8 44 LEU -72.0 151.3 177.6 -70.6 179.4 45 PRO -55.8 133.6 179.2 9.2 -18.4 46 GLY 96.0 -6.5 -179.0 47 PHE -111.5 155.6 -174.8 -73.2 83.3 48 PRO -74.9 150.3 175.7 4.9 1.8 49 PHE -95.3 137.1 -8.4 174.0 -84.5 50 PRO -98.0 136.1 -178.0 31.5 -16.4 51 SER -153.7 164.1 173.3 60.9 52 PHE -108.5 139.1 175.1 -69.0 -69.7 53 GLU -112.9 136.4 177.5 -83.2 65.6 60.9 54 VAL -136.9 122.4 177.9 -178.3 55 HIS 53.8 41.9 177.3 -146.6 -66.0 56 ASP 66.6 19.0 178.5 -147.5 28.2 57 LYS -119.2 148.7 179.5 -64.0 -63.2 -70.0 176.2 58 LYS -86.2 120.8 -179.8 -172.1 -157.2 -45.4 155.7 59 ASN 41.9 49.8 -177.9 -63.8 -33.9 60 PRO -71.3 157.7 174.1 34.7 -42.7 61 THR -78.5 133.8 -179.8 -63.1 62 LEU -102.1 124.0 -179.9 -48.5 178.6 63 GLU -106.1 116.9 -174.4 -66.6 -164.6 26.0 64 ILE -121.9 139.8 179.5 -65.1 168.2 65 PRO -67.5 136.0 177.0 -14.2 27.3 66 ALA -63.2 134.8 -178.0 67 GLY 96.2 -9.5 -178.0 68 ALA -76.5 150.9 170.9 69 THR -90.8 124.3 -178.4 -68.9 70 VAL -107.2 113.2 175.5 -176.2 71 ASP -93.1 113.4 -179.5 -68.7 -19.4 72 VAL -104.7 132.4 171.2 -179.8 73 THR -114.6 122.2 178.9 -62.6 74 PHE -114.5 121.8 -177.9 172.8 54.5 75 ILE -116.1 127.0 176.8 -50.3 166.4 76 ASN -94.3 101.7 179.0 177.7 -163.8 77 THR -96.1 7.7 -174.0 45.2 78 ASN -96.9 99.0 -178.3 -168.9 29.1 79 LYS -52.8 129.4 177.0 -64.1 -177.3 -48.3 -44.0 80 GLY 89.3 -3.6 -176.2 81 PHE -134.1 143.1 173.0 -72.0 -85.7 82 GLY -93.5 152.1 177.0 83 HIS -144.9 157.9 175.2 -72.5 -68.8 84 SER -125.9 170.1 177.1 79.0 85 PHE -140.6 105.3 -173.5 -176.3 -77.0 86 ASP -130.7 125.4 -176.1 -63.0 -63.5 87 ILE -93.4 136.1 -175.1 -59.3 177.8 88 THR -153.5 160.2 176.9 171.9 89 LYS -87.0 -13.5 -178.8 -69.0 157.0 -122.3 104.2 90 LYS -71.0 123.7 -178.9 -97.1 29.5 -155.6 -59.4 91 GLY -96.7 172.6 179.9 92 PRO -69.5 166.5 -0.7 31.6 -40.7 93 PRO -76.7 144.7 -177.8 29.0 -31.0 94 TYR -94.5 141.9 176.8 -58.7 -78.9 95 ALA -70.4 164.9 174.4 96 VAL -53.6 -42.4 170.1 179.4 97 MET -108.3 98.0 -172.2 -77.8 -170.7 -68.5 98 PRO -57.1 137.0 -178.8 -22.1 30.4 99 VAL -100.7 82.0 -168.6 177.6 100 ILE -113.4 9.2 177.6 65.6 172.5 101 ASP -69.5 151.1 -3.5 -71.4 -7.8 102 PRO -77.0 143.0 173.5 1.1 8.0 103 ILE -85.7 115.5 -175.6 -67.9 165.3 104 VAL -78.1 -21.6 178.1 -58.7 105 ALA -172.0 146.7 178.3 106 GLY 155.0 -171.3 -171.5 107 THR -115.4 167.1 169.8 79.0 108 GLY -87.8 -166.0 179.1 109 PHE -73.1 133.2 178.3 -71.6 10.9 110 SER -81.0 165.4 168.8 74.2 111 PRO -72.7 162.1 174.6 32.1 -37.8 112 VAL -80.7 147.4 177.4 -42.3 113 PRO -55.8 130.9 -176.8 -23.8 39.8 114 LYS -137.6 150.8 178.2 179.9 -149.6 -166.7 -167.2 115 ASP 44.9 44.7 -177.6 -52.8 -33.2 116 GLY 71.2 18.6 -177.5 117 LYS -126.3 164.7 -176.8 -80.2 -153.6 -152.9 168.2 118 PHE -130.6 145.2 178.2 -58.4 -82.1 119 GLY -91.5 144.7 179.1 120 TYR -147.7 163.4 178.1 77.9 -83.3 121 THR -153.2 162.4 -178.3 -168.2 122 ASN -128.7 137.5 175.4 -59.4 101.5 123 PHE -143.8 161.2 -178.5 60.3 90.1 124 THR -116.5 138.9 -179.1 66.9 125 TRP -128.8 139.0 177.7 177.7 38.7 126 HIS -118.8 81.0 -174.2 -72.1 92.1 127 PRO -66.3 150.2 167.4 24.6 -35.5 128 THR -95.4 148.5 179.6 45.7 129 ALA -51.1 136.9 178.0 130 GLY 154.6 -177.9 178.6 131 THR -106.7 130.7 -178.2 178.9 132 TYR -131.4 170.6 179.9 -55.5 80.4 133 TYR -133.3 143.3 173.1 -64.2 -87.1 134 TYR -106.8 123.2 -171.3 56.6 -85.9 135 VAL -135.1 149.5 173.5 -3.8 136 CYS -90.8 140.0 -178.2 178.3 137 GLN -99.7 0.0 178.6 -67.9 -158.6 -75.1 138 ILE -63.5 127.9 -175.5 -66.0 -66.5 139 PRO -46.7 128.3 177.2 -33.7 43.3 140 GLY 89.9 -20.0 -175.6 141 HIS -67.5 -46.0 178.3 -69.8 -164.0 142 ALA -67.7 -35.3 178.5 143 ALA -64.2 -24.5 179.5 144 THR -105.4 18.5 170.6 55.4 145 GLY 106.8 3.9 -179.3 146 GLN -85.8 83.0 177.1 -169.8 173.8 12.1 147 PHE -167.2 160.7 174.2 64.0 89.4 148 GLY -146.7 174.6 -178.8 149 LYS -105.0 148.0 175.0 -171.9 -179.8 -76.8 170.6 150 ILE -124.8 124.8 176.7 -56.6 179.5 151 VAL -113.5 110.8 178.0 176.9 152 VAL -99.4 117.1 176.9 176.9 153 LYS -168.7 23.2 0.0 42.8 45.2 143.7 159.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 1.096 -3.561 1.028 2 ASP -2.520 -3.032 2.049 3 THR -3.783 0.054 0.212 4 THR -7.518 -0.505 0.641 5 TRP -9.136 2.028 2.946 6 LYS -12.701 1.802 4.258 7 GLU -14.655 4.681 5.796 8 ALA -15.967 4.666 9.326 9 THR -17.893 7.242 11.332 10 LEU -16.783 7.952 14.928 11 PRO -19.225 5.454 16.484 12 GLN -17.925 2.818 14.058 13 VAL -14.341 3.716 14.995 14 LYS -15.160 3.371 18.684 15 ALA -16.905 0.074 18.112 16 MET -13.782 -1.213 16.350 17 LEU -11.236 0.001 18.938 18 GLU -13.246 -1.902 21.564 19 LYS -12.780 -5.130 19.515 20 ASP -9.058 -5.390 20.404 21 THR -8.694 -8.806 22.048 22 GLY -5.561 -8.177 24.119 23 LYS -5.232 -7.792 27.879 24 VAL -3.134 -4.886 29.178 25 SER -0.484 -5.287 31.848 26 GLY 1.920 -2.365 32.386 27 ASP 2.526 -0.997 28.895 28 THR 2.101 -4.347 27.158 29 VAL -1.013 -5.690 25.411 30 THR -0.938 -9.490 25.591 31 TYR -2.903 -11.467 23.074 32 SER -3.846 -15.152 23.332 33 GLY -5.752 -17.701 21.264 34 LYS -5.431 -19.092 17.741 35 THR -6.704 -15.893 16.147 36 VAL -6.064 -12.495 17.794 37 HIS -7.376 -9.066 16.796 38 VAL -5.132 -6.050 17.208 39 VAL -7.000 -2.742 16.763 40 ALA -4.650 0.200 16.406 41 ALA -5.366 3.886 15.878 42 ALA -3.055 6.721 14.879 43 VAL -3.401 9.518 17.471 44 LEU -6.660 9.104 19.355 45 PRO -7.889 12.333 20.956 46 GLY -6.075 12.990 24.237 47 PHE -2.952 11.127 23.133 48 PRO 0.242 12.666 21.807 49 PHE 1.188 13.251 18.213 50 PRO 2.451 11.253 16.518 51 SER 1.661 7.922 18.245 52 PHE -0.280 4.736 17.871 53 GLU -2.915 3.730 20.420 54 VAL -3.785 0.076 20.991 55 HIS -6.265 -0.949 23.731 56 ASP -6.200 2.606 25.088 57 LYS -2.410 2.582 25.563 58 LYS 0.186 4.713 23.792 59 ASN 2.590 2.737 21.594 60 PRO 2.282 -0.387 23.750 61 THR 4.336 -3.506 23.241 62 LEU 2.140 -6.180 21.682 63 GLU 2.841 -9.729 22.942 64 ILE 1.462 -12.272 20.488 65 PRO 1.593 -16.068 20.646 66 ALA 3.906 -17.778 18.170 67 GLY 1.667 -19.542 15.663 68 ALA -1.244 -17.123 16.005 69 THR -3.129 -15.588 13.090 70 VAL -3.028 -11.827 13.698 71 ASP -5.922 -9.808 12.330 72 VAL -4.866 -6.142 12.452 73 THR -7.312 -3.268 12.080 74 PHE -5.550 0.117 11.634 75 ILE -7.686 3.236 11.965 76 ASN -6.420 6.739 11.151 77 THR -8.230 8.922 13.676 78 ASN -5.837 11.874 13.235 79 LYS -7.533 14.795 11.545 80 GLY -5.287 16.425 8.961 81 PHE -2.645 13.741 8.746 82 GLY -2.044 10.561 6.820 83 HIS -0.410 7.734 8.768 84 SER 0.672 4.211 7.909 85 PHE 1.062 1.029 9.973 86 ASP 3.930 -1.195 8.869 87 ILE 5.423 -4.156 10.691 88 THR 9.156 -4.705 10.356 89 LYS 12.100 -6.275 12.156 90 LYS 14.042 -3.001 11.905 91 GLY 14.133 -1.236 15.266 92 PRO 14.569 2.407 16.306 93 PRO 15.932 4.917 16.042 94 TYR 14.213 5.599 12.715 95 ALA 15.453 7.876 9.993 96 VAL 13.070 10.627 8.762 97 MET 12.276 8.262 5.863 98 PRO 12.493 4.960 7.780 99 VAL 14.631 2.250 6.199 100 ILE 12.382 -0.622 7.235 101 ASP 12.300 -3.188 4.477 102 PRO 11.364 -5.808 4.424 103 ILE 7.887 -4.783 5.591 104 VAL 6.478 -8.142 6.724 105 ALA 2.901 -6.902 6.835 106 GLY 1.302 -3.506 6.738 107 THR -0.309 -0.662 4.989 108 GLY 0.428 2.116 2.585 109 PHE -0.224 5.751 3.524 110 SER -3.806 6.314 4.655 111 PRO -6.125 9.064 3.520 112 VAL -6.669 12.038 5.898 113 PRO -9.980 12.074 7.852 114 LYS -12.750 13.603 5.759 115 ASP -16.424 14.594 5.990 116 GLY -16.719 13.486 9.632 117 LYS -15.230 10.115 8.684 118 PHE -12.003 8.225 9.251 119 GLY -10.163 5.747 7.055 120 TYR -9.345 2.292 8.350 121 THR -8.125 -1.004 6.977 122 ASN -7.710 -4.641 7.964 123 PHE -4.894 -7.038 7.116 124 THR -3.847 -10.481 8.332 125 TRP -0.372 -11.449 9.474 126 HIS 1.023 -14.895 10.283 127 PRO 4.113 -14.039 12.270 128 THR 7.175 -16.134 12.908 129 ALA 8.592 -15.888 16.451 130 GLY 10.790 -12.843 16.996 131 THR 10.788 -9.154 17.834 132 TYR 9.173 -6.726 15.444 133 TYR 8.147 -3.086 15.388 134 TYR 4.975 -1.421 14.066 135 VAL 5.946 1.885 12.541 136 CYS 4.494 4.787 10.591 137 GLN 6.301 5.623 7.344 138 ILE 5.024 9.189 6.874 139 PRO 8.286 11.135 6.847 140 GLY 9.359 12.172 10.326 141 HIS 6.690 10.319 12.317 142 ALA 8.721 7.289 13.353 143 ALA 11.679 9.584 14.032 144 THR 9.445 11.473 16.476 145 GLY 8.152 8.345 18.171 146 GLN 5.333 6.794 16.210 147 PHE 6.243 3.165 16.634 148 GLY 5.859 0.345 19.104 149 LYS 7.306 -3.134 19.640 150 ILE 5.785 -6.541 18.899 151 VAL 7.138 -9.640 20.645 152 VAL 5.945 -12.838 19.002 153 LYS 6.890 -15.930 21.046 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/S S S S S S/H H 10 H H H H H H H H H/S S 20 S S C T T T T/S S S S 30 S S S S/S S S S S S S 40 S S S C C S S S S/P S 50 S S S/T T T T/S S S S/S S 60 S S S S S C S S S S 70 S S S S S S S/S S S S/S 80 S S S S S S S S S/S S 90 S S/P S C T T T T C C 100 C/P C C S S S S S S/S S 110 S S S T T T T/S S S S 120 S S S S S S S S S/S S 130 S S S S S S C C C H 140 H H H H H S S S S S 150 S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B E E E E H 10 H H H H H H H h T t 20 E E E T e E E E 30 e S e E E E E E E 40 E E e t T T t S S 50 e E E E e T E E e 60 E E E E E e T t E E 70 E E E E E E e t T T 80 t e E E E e 90 S S S S 100 e E E E E e 110 B T e E E E E 120 E E E E E S E 130 E E E E E e t T T 140 T T T T T e E E E E 150 E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 87.0 58.9 70.7 2 ASP 87.6 79.3 57.5 3 THR 32.2 30.1 78.6 4 THR 17.1 16.0 81.9 5 TRP 180.5 88.1 53.8 6 LYS 55.1 31.8 79.1 7 GLU 42.7 30.8 74.0 8 ALA 71.7 98.7 43.3 9 THR 59.5 55.7 56.4 10 LEU 49.9 33.8 54.6 11 PRO 38.5 30.9 68.0 12 GLN 52.0 35.0 70.9 13 VAL 116.6 98.2 28.4 14 LYS 97.3 56.1 55.9 15 ALA 19.1 26.3 73.9 16 MET 120.7 75.7 43.9 17 LEU 132.6 89.7 48.8 18 GLU 34.4 24.8 77.6 19 LYS 42.0 24.2 80.7 20 ASP 109.8 99.4 53.3 21 THR 49.9 46.7 73.0 22 GLY 34.8 100.0 53.6 23 LYS 38.2 22.0 79.5 24 VAL 92.5 77.9 59.3 25 SER 9.9 11.9 83.5 26 GLY 0.0 0.0 86.4 27 ASP 25.3 22.9 77.1 28 THR 80.0 74.8 66.5 29 VAL 118.8 100.0 39.2 30 THR 65.4 61.2 58.8 31 TYR 181.0 100.0 41.1 32 SER 28.0 33.5 69.3 33 GLY 1.3 3.7 79.2 34 LYS 0.0 0.0 87.0 35 THR 33.0 30.9 76.3 36 VAL 118.0 99.3 45.2 37 HIS 111.1 74.0 54.7 38 VAL 117.4 98.8 29.8 39 VAL 118.8 100.0 47.2 40 ALA 72.6 100.0 37.1 41 ALA 72.6 100.0 45.0 42 ALA 72.6 100.0 48.5 43 VAL 106.5 89.6 66.6 44 LEU 134.4 90.9 43.3 45 PRO 32.8 26.3 81.3 46 GLY 0.0 0.0 80.7 47 PHE 128.9 77.3 61.8 48 PRO 60.7 48.8 68.7 49 PHE 98.2 58.8 54.6 50 PRO 117.5 94.4 49.3 51 SER 81.6 97.6 55.6 52 PHE 166.8 100.0 46.5 53 GLU 138.5 99.9 43.5 54 VAL 118.7 99.9 45.2 55 HIS 88.5 58.9 66.0 56 ASP 21.3 19.3 70.7 57 LYS 110.3 63.6 64.5 58 LYS 82.7 47.7 62.8 59 ASN 96.3 79.7 59.2 60 PRO 123.7 99.3 55.4 61 THR 74.5 69.7 58.0 62 LEU 146.6 99.2 29.4 63 GLU 90.4 65.2 64.4 64 ILE 143.0 99.6 26.4 65 PRO 87.6 70.3 64.7 66 ALA 43.3 59.6 66.6 67 GLY 0.0 0.0 85.8 68 ALA 70.8 97.6 57.0 69 THR 73.1 68.3 61.5 70 VAL 118.1 99.4 34.4 71 ASP 59.9 54.2 55.5 72 VAL 116.9 98.4 36.1 73 THR 105.5 98.7 45.8 74 PHE 166.8 100.0 36.2 75 ILE 143.5 100.0 31.0 76 ASN 120.9 100.0 53.1 77 THR 101.0 94.5 38.4 78 ASN 105.3 87.1 49.3 79 LYS 30.9 17.8 79.2 80 GLY 3.0 8.6 65.4 81 PHE 83.8 50.3 69.9 82 GLY 29.0 83.3 63.7 83 HIS 150.2 100.0 42.0 84 SER 83.4 99.8 50.8 85 PHE 166.0 99.5 23.0 86 ASP 110.5 100.0 49.5 87 ILE 142.5 99.3 26.4 88 THR 106.8 99.9 47.6 89 LYS 86.5 49.9 60.8 90 LYS 70.1 40.4 76.9 91 GLY 26.4 75.9 57.2 92 PRO 89.5 71.9 46.0 93 PRO 6.4 5.1 81.9 94 TYR 175.5 97.0 36.9 95 ALA 23.0 31.6 76.8 96 VAL 27.0 22.7 65.9 97 MET 24.2 15.2 75.0 98 PRO 122.6 98.4 49.6 99 VAL 8.5 7.2 85.2 100 ILE 143.2 99.8 40.7 101 ASP 17.8 16.1 75.5 102 PRO 39.9 32.0 80.2 103 ILE 132.8 92.5 56.9 104 VAL 90.1 75.8 55.7 105 ALA 57.6 79.3 47.6 106 GLY 34.8 100.0 47.4 107 THR 106.9 100.0 41.5 108 GLY 22.5 64.8 51.8 109 PHE 75.1 45.0 65.7 110 SER 83.6 100.0 49.0 111 PRO 63.9 51.3 62.2 112 VAL 44.4 37.4 74.3 113 PRO 120.5 96.8 62.5 114 LYS 31.6 18.2 90.0 115 ASP 22.7 20.5 76.0 116 GLY 0.0 0.0 82.7 117 LYS 99.1 57.2 68.6 118 PHE 139.6 83.7 47.0 119 GLY 30.9 88.7 54.8 120 TYR 150.6 83.2 47.1 121 THR 103.8 97.1 48.9 122 ASN 63.7 52.7 68.0 123 PHE 145.8 87.4 44.5 124 THR 40.6 38.0 70.5 125 TRP 191.2 93.3 30.6 126 HIS 44.6 29.7 76.4 127 PRO 123.6 99.3 48.5 128 THR 4.8 4.5 90.0 129 ALA 31.7 43.7 60.7 130 GLY 4.4 12.6 74.3 131 THR 42.9 40.1 66.0 132 TYR 172.8 95.5 45.7 133 TYR 151.6 83.8 51.2 134 TYR 181.0 100.0 32.1 135 VAL 118.8 100.0 38.2 136 CYS 99.2 100.0 55.2 137 GLN 113.8 76.6 50.5 138 ILE 113.1 78.8 48.0 139 PRO 68.0 54.6 56.9 140 GLY 18.9 54.4 57.7 141 HIS 134.8 89.7 50.0 142 ALA 72.6 100.0 47.6 143 ALA 54.5 75.0 65.8 144 THR 30.9 28.9 73.4 145 GLY 13.3 38.2 71.0 146 GLN 148.6 100.0 40.5 147 PHE 120.0 72.0 49.1 148 GLY 30.4 87.3 55.7 149 LYS 88.0 50.7 66.2 150 ILE 141.6 98.7 29.0 151 VAL 82.1 69.1 49.9 152 VAL 118.8 100.0 42.8 153 LYS 68.7 39.6 72.9