Protein Data Bank File : 1amx Title : BACTERIAL ADHESIN 19-JUN-97 1AMX Number of Amino Acid Residues : 150 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR SER SER VAL PHE TYR TYR LYS THR GLY 10 ASP MET LEU PRO GLU ASP THR THR HIS VAL 20 ARG TRP PHE LEU ASN ILE ASN ASN GLU LYS 30 SER TYR VAL SER LYS ASP ILE THR ILE LYS 40 ASP GLN ILE GLN GLY GLY GLN GLN LEU ASP 50 LEU SER THR LEU ASN ILE ASN VAL THR GLY 60 THR HIS SER ASN TYR TYR SER GLY GLN SER 70 ALA ILE THR ASP PHE GLU LYS ALA PHE PRO 80 GLY SER LYS ILE THR VAL ASP ASN THR LYS 90 ASN THR ILE ASP VAL THR ILE PRO GLN GLY 100 TYR GLY SER TYR ASN SER PHE SER ILE ASN 110 TYR LYS THR LYS ILE THR ASN GLU GLN GLN 120 LYS GLU PHE VAL ASN ASN SER GLN ALA TRP 130 TYR GLN GLU HIS GLY LYS GLU GLU VAL ASN 140 GLY LYS SER PHE ASN HIS THR VAL HIS ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 -27.6 178.5 133.4 2 SER -80.9 149.7 -179.2 38.1 3 SER 178.2 111.3 173.6 169.3 4 VAL -135.9 111.6 -176.9 148.3 5 PHE -54.4 -48.2 -179.0 -175.8 86.2 6 TYR -143.9 141.4 175.7 165.0 69.1 7 TYR -160.3 153.5 -177.5 76.1 -89.0 8 LYS -112.4 132.1 177.6 -125.9 -148.1 75.3 59.3 9 THR -141.4 173.2 -179.3 -166.3 10 GLY -171.5 166.5 179.8 11 ASP -160.9 176.8 178.1 66.9 14.5 12 MET -129.6 120.9 177.3 -79.5 -170.4 38.8 13 LEU -71.5 131.5 -179.9 -94.2 27.4 14 PRO -64.5 -20.6 179.1 32.1 -44.3 15 GLU -88.2 2.6 179.6 51.4 -99.9 -67.8 16 ASP -147.8 81.6 -178.7 -176.4 5.2 17 THR -78.9 8.5 -179.4 64.4 18 THR -110.8 -2.1 -180.0 54.5 19 HIS -130.1 149.6 174.4 -70.0 87.7 20 VAL -116.1 132.0 179.2 -178.4 21 ARG -96.9 135.7 179.4 -58.0 158.9 69.4 -134.9 22 TRP -122.0 143.6 -179.9 -65.4 103.6 23 PHE -134.3 122.7 174.9 -55.2 88.3 24 LEU -102.7 108.6 -177.1 -90.5 45.8 25 ASN -106.3 105.1 -176.0 -66.4 -50.6 26 ILE -105.3 134.4 -180.0 -39.6 166.8 27 ASN 52.6 56.5 -179.3 -162.1 -2.4 28 ASN -56.8 -23.6 -179.8 -62.2 -65.0 29 GLU -107.6 5.4 178.2 -60.4 -58.6 -44.0 30 LYS 54.9 48.4 179.2 -57.9 163.3 -162.9 53.7 31 SER -78.2 164.0 171.9 -47.5 32 TYR -75.3 147.3 -175.3 177.3 83.9 33 VAL -123.5 135.0 -175.2 127.8 34 SER -91.1 -21.4 178.4 -61.2 35 LYS -137.1 167.7 178.6 56.5 179.9 -88.0 -163.1 36 ASP -64.2 156.5 179.2 -70.2 -1.6 37 ILE -101.2 126.5 179.3 -53.4 164.6 38 THR -127.1 125.4 179.3 -63.8 39 ILE -121.0 132.1 179.4 -51.0 -74.0 40 LYS -117.2 120.7 -177.8 -79.6 -168.0 176.5 178.7 41 ASP -121.1 130.7 178.5 -167.0 -55.8 42 GLN -124.7 107.0 179.8 -53.6 86.4 43.1 43 ILE -72.8 137.4 -177.5 -65.7 153.3 44 GLN -92.2 177.0 -172.5 -54.0 -67.8 114.6 45 GLY -55.6 151.4 176.2 46 GLY 84.1 20.3 -178.9 47 GLN -155.8 150.8 -179.9 59.0 -167.4 137.8 48 GLN -125.3 128.4 177.8 175.8 58.3 41.6 49 LEU -60.6 132.1 175.9 170.0 69.0 50 ASP -104.7 92.1 -175.6 -170.6 -14.1 51 LEU -56.9 -29.4 179.7 -159.0 57.6 52 SER -66.8 -16.0 179.5 68.7 53 THR -92.9 1.3 -177.5 55.9 54 LEU -70.9 119.8 176.1 -166.9 -75.9 55 ASN -136.9 151.5 -177.4 67.5 -110.7 56 ILE -130.2 126.3 178.9 -46.9 156.2 57 ASN -111.8 119.2 179.5 -169.5 24.1 58 VAL -110.7 126.5 177.0 -178.0 59 THR -127.7 138.9 -179.8 67.0 60 GLY 140.7 -123.6 179.2 61 THR -73.4 -34.8 -178.9 -66.6 62 HIS -117.8 59.8 -179.9 -60.4 -49.5 63 SER -63.0 116.1 178.7 -85.0 64 ASN -157.3 155.3 179.3 -104.7 101.9 65 TYR -120.6 121.3 -179.3 -177.7 76.5 66 TYR -107.3 127.6 -178.2 -56.0 -84.4 67 SER -151.4 174.0 178.5 -159.1 68 GLY 90.8 -161.1 -178.8 69 GLN -85.4 -15.1 178.6 -138.8 41.6 75.6 70 SER -103.5 4.6 -178.7 53.2 71 ALA -38.2 -57.1 179.7 72 ILE -58.4 -51.6 179.6 -71.0 -173.5 73 THR -62.8 -38.5 178.7 -66.5 74 ASP -68.3 -33.7 178.2 -69.5 -2.4 75 PHE -73.0 -47.8 179.9 169.8 80.0 76 GLU -65.3 -24.2 -179.7 -61.5 -167.3 -12.1 77 LYS -79.5 -45.1 179.8 -163.1 179.9 -59.1 -178.4 78 ALA -67.6 -31.4 -177.9 79 PHE -119.6 70.6 180.0 -64.2 -79.2 80 PRO -46.4 125.6 -177.7 18.8 -37.7 81 GLY 108.3 -27.3 178.6 82 SER -68.1 154.6 -179.1 -59.8 83 LYS -155.2 131.4 175.3 -141.7 60.2 174.8 172.2 84 ILE -127.9 113.7 -177.3 -59.1 -175.0 85 THR -112.5 117.3 179.7 -51.9 86 VAL -112.9 138.2 174.3 -178.3 87 ASP -124.1 100.8 -175.8 -172.5 -7.3 88 ASN -64.3 -26.9 178.7 -81.9 -99.2 89 THR -75.9 -47.1 -180.0 -62.2 90 LYS -80.4 -17.8 -179.6 -70.1 -169.0 72.8 170.5 91 ASN 67.1 42.3 -179.9 -100.3 -38.5 92 THR -118.7 150.1 175.3 58.5 93 ILE -137.0 128.8 179.6 -50.4 179.3 94 ASP -123.1 129.2 -177.8 -69.1 -36.0 95 VAL -122.2 130.9 177.2 -179.8 96 THR -129.8 127.3 -179.5 -66.6 97 ILE -126.5 119.9 179.8 -56.2 178.5 98 PRO -57.8 144.0 -177.8 28.1 -41.6 99 GLN -57.0 -34.2 179.7 73.0 84.6 -138.1 100 GLY -63.9 -35.7 179.3 101 TYR -89.3 -28.4 178.2 -72.9 -56.3 102 GLY -65.2 -33.8 -179.8 103 SER -64.0 130.7 176.5 -61.1 104 TYR 68.3 20.1 -179.8 -50.7 -60.4 105 ASN -139.8 137.6 173.5 -71.4 -58.2 106 SER -97.2 138.2 178.3 -40.5 107 PHE -120.6 126.5 176.3 -58.4 87.2 108 SER -118.8 108.2 179.9 179.6 109 ILE -100.3 122.3 -179.7 -61.5 177.9 110 ASN -125.0 146.5 177.9 165.8 -118.4 111 TYR -159.1 168.3 179.2 57.7 85.6 112 LYS -124.0 156.1 174.5 -78.1 -178.9 170.2 64.9 113 THR -120.9 137.3 177.5 57.0 114 LYS -85.3 131.4 178.1 170.1 71.2 -168.8 -38.8 115 ILE -74.8 129.5 -178.6 -63.6 -179.6 116 THR -111.7 -6.7 177.4 57.9 117 ASN -126.8 94.9 -176.5 -166.1 -31.5 118 GLU -63.6 -17.5 -177.8 -44.4 -96.6 -30.8 119 GLN -86.6 -24.3 -179.3 -70.7 70.1 26.1 120 GLN -62.7 143.4 -179.4 -165.2 165.4 -48.2 121 LYS -107.1 -22.9 -179.8 -84.6 -67.7 -178.0 -72.5 122 GLU -126.8 135.1 179.4 -76.7 174.6 -6.0 123 PHE -122.8 125.3 -177.8 -58.8 -84.0 124 VAL -120.0 150.5 178.3 -1.6 125 ASN -130.2 124.7 179.2 -172.9 -133.0 126 ASN -107.2 151.0 176.4 -64.5 -20.1 127 SER -152.2 153.7 177.4 67.0 128 GLN -129.7 141.2 -179.0 -58.7 81.0 43.2 129 ALA -122.6 147.2 177.3 130 TRP -133.5 114.4 -179.5 -69.8 -95.6 131 TYR -164.9 173.7 176.4 58.1 87.5 132 GLN -156.2 115.8 178.2 176.0 174.7 38.7 133 GLU -79.7 158.9 179.1 -64.3 179.8 75.9 134 HIS -57.8 121.2 178.8 -170.5 -149.7 135 GLY 77.1 4.9 -179.8 136 LYS -115.2 172.0 -179.4 -61.5 -167.7 174.0 -178.3 137 GLU -73.0 140.4 178.7 -63.7 160.0 -69.8 138 GLU -61.1 139.9 177.5 -175.9 -175.1 42.6 139 VAL -110.3 126.4 -179.1 165.3 140 ASN -135.9 116.7 177.9 -80.0 -17.1 141 GLY 71.3 4.9 -179.8 142 LYS -59.3 142.6 -179.8 -168.3 176.3 -170.6 -60.2 143 SER -94.6 133.6 176.3 -78.6 144 PHE -132.4 88.6 -178.7 -58.4 88.5 145 ASN -102.9 165.3 176.6 -47.6 148.1 146 HIS -151.5 141.8 179.0 -163.1 -102.4 147 THR -121.2 122.1 177.4 -60.8 148 VAL -93.8 129.5 -178.7 165.6 149 HIS -95.7 163.2 -178.9 -61.3 94.4 150 ASN -149.7 4.3 0.0 -166.5 51.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR -2.085 44.337 62.841 2 SER -0.180 42.714 59.921 3 SER 3.327 43.955 58.965 4 VAL 6.286 42.606 57.071 5 PHE 8.508 45.310 55.715 6 TYR 9.814 43.157 52.895 7 TYR 9.068 39.745 51.454 8 LYS 9.487 37.837 48.237 9 THR 6.767 35.735 46.653 10 GLY 5.928 34.105 43.353 11 ASP 3.578 31.868 41.387 12 MET 2.780 30.147 38.113 13 LEU -0.335 31.021 36.206 14 PRO -1.929 27.727 35.143 15 GLU -2.660 29.339 31.752 16 ASP 1.047 29.987 31.281 17 THR 3.114 26.971 32.242 18 THR 6.346 28.340 30.761 19 HIS 6.814 31.379 33.047 20 VAL 7.157 31.961 36.771 21 ARG 6.032 35.266 38.097 22 TRP 8.135 36.841 40.860 23 PHE 7.249 39.693 43.268 24 LEU 9.544 41.737 45.469 25 ASN 7.287 43.587 47.865 26 ILE 9.123 46.446 49.609 27 ASN 7.975 48.682 52.502 28 ASN 4.539 47.147 52.619 29 GLU 3.315 49.391 55.426 30 LYS 4.823 52.555 53.964 31 SER 6.906 53.251 57.048 32 TYR 9.453 55.953 57.385 33 VAL 12.851 54.482 56.650 34 SER 16.110 55.408 58.465 35 LYS 18.614 53.986 55.948 36 ASP 18.604 53.168 52.222 37 ILE 16.891 49.976 51.146 38 THR 19.109 47.447 49.393 39 ILE 17.795 44.213 47.960 40 LYS 20.043 41.584 46.419 41 ASP 18.333 39.005 44.273 42 GLN 19.802 35.865 42.694 43 ILE 17.395 33.918 40.490 44 GLN 18.231 30.238 40.653 45 GLY 18.788 27.550 37.987 46 GLY 16.456 26.380 35.233 47 GLN 14.948 29.753 34.423 48 GLN 15.905 32.898 32.576 49 LEU 14.948 36.425 33.531 50 ASP 12.782 38.096 30.897 51 LEU 13.805 41.713 31.296 52 SER 11.007 42.906 29.077 53 THR 8.504 41.779 31.776 54 LEU 10.044 43.939 34.546 55 ASN 7.528 46.389 36.047 56 ILE 7.507 48.466 39.239 57 ASN 4.412 49.642 41.037 58 VAL 4.936 52.427 43.568 59 THR 2.075 53.356 45.911 60 GLY 2.021 56.004 48.628 61 THR 3.356 59.526 48.430 62 HIS 4.703 58.994 44.875 63 SER 2.138 56.705 43.254 64 ASN 3.219 55.685 39.729 65 TYR 3.390 52.550 37.579 66 TYR 6.523 51.815 35.541 67 SER 6.336 49.341 32.685 68 GLY 7.619 48.760 29.174 69 GLN 11.141 48.854 27.870 70 SER 12.167 52.059 29.653 71 ALA 10.748 51.024 33.097 72 ILE 14.099 50.895 34.942 73 THR 15.270 54.174 33.410 74 ASP 11.921 55.966 34.009 75 PHE 12.016 54.768 37.621 76 GLU 15.650 55.727 38.260 77 LYS 14.820 59.071 36.731 78 ALA 11.748 59.601 38.892 79 PHE 13.598 58.443 41.994 80 PRO 17.034 60.094 41.813 81 GLY 19.589 58.025 43.726 82 SER 17.679 54.807 42.974 83 LYS 19.349 52.006 41.068 84 ILE 18.155 48.733 39.640 85 THR 20.934 46.634 38.254 86 VAL 20.066 43.618 36.182 87 ASP 22.564 41.133 34.814 88 ASN 20.784 39.017 32.262 89 THR 23.642 36.539 31.997 90 LYS 23.932 35.990 35.754 91 ASN 20.184 36.318 36.462 92 THR 20.754 38.751 39.306 93 ILE 18.831 41.889 40.188 94 ASP 20.057 44.432 42.664 95 VAL 17.841 47.276 43.912 96 THR 18.875 50.354 45.882 97 ILE 16.305 52.922 46.978 98 PRO 17.415 56.091 48.795 99 GLN 15.842 56.463 52.247 100 GLY 14.098 59.718 51.364 101 TYR 12.207 58.038 48.554 102 GLY 11.893 54.699 50.333 103 SER 9.941 56.483 53.051 104 TYR 6.125 56.366 52.860 105 ASN 5.985 54.333 49.656 106 SER 5.481 50.670 48.917 107 PHE 7.360 49.269 45.969 108 SER 6.252 46.114 44.227 109 ILE 8.784 44.918 41.679 110 ASN 7.518 42.127 39.419 111 TYR 9.158 40.190 36.596 112 LYS 8.947 36.800 34.983 113 THR 11.441 34.134 34.259 114 LYS 11.120 31.859 31.300 115 ILE 11.450 28.184 32.301 116 THR 14.378 26.616 30.362 117 ASN 14.159 23.186 31.945 118 GLU 10.720 21.779 31.235 119 GLN 11.521 18.844 33.515 120 GLN 12.229 20.867 36.697 121 LYS 9.511 20.948 39.393 122 GLU 10.770 23.695 41.703 123 PHE 12.006 27.146 40.845 124 VAL 13.625 29.189 43.560 125 ASN 14.545 32.782 43.919 126 ASN 16.854 33.882 46.728 127 SER 17.213 37.482 48.006 128 GLN 18.962 39.329 50.847 129 ALA 17.810 42.609 52.410 130 TRP 19.407 45.550 54.196 131 TYR 17.068 48.188 55.652 132 GLN 15.850 49.897 58.824 133 GLU 12.368 51.123 59.618 134 HIS 12.018 54.113 61.895 135 GLY 12.556 53.035 65.526 136 LYS 13.177 49.380 64.783 137 GLU 16.248 47.207 64.629 138 GLU 18.372 47.422 61.545 139 VAL 18.039 44.511 59.180 140 ASN 21.233 43.365 57.467 141 GLY 21.715 40.528 55.007 142 LYS 18.609 38.728 56.111 143 SER 17.395 36.137 53.607 144 PHE 13.988 36.181 52.011 145 ASN 13.891 33.314 49.560 146 HIS 10.961 31.734 47.789 147 THR 10.358 28.460 45.961 148 VAL 7.577 28.151 43.397 149 HIS 6.321 24.596 43.173 150 ASN 5.031 22.673 40.209 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 S 10 C C T T T T C S S S 20 S S S S S S S/T T T T 30 S S S S S/S S S S S S 40 S S S S S S/S S S S S/T 50 T T T/S S S S S S S/T T 60 T T/S S S S S S S S H 70 H H H H H H H H H H 80 S S S S S S S/T T T T 90 S S S S S S S S/H H H 100 H H H S S S S S S S 110 S S S S S S C C S S 120 S S/S S S S S S S S S 130 S S S/T T T T/S S S S S 140 S/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 e E E E E E 10 E t T T t T e E E 20 E E E E E E e T T t 30 B S S E E E E 40 E E E e S e E E E E 50 E E E E E E E E E E 60 e T t E E E S S h 70 H H H H H H H H h T 80 T t E E E E E T T T 90 e E E E E E E h H H 100 H H h e E E E E E E 110 E E E E E e t T T t 120 e E E E E E E E E E 130 E B T T t E E 140 E E E e E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 0.0 0.0 97.4 2 SER 0.0 0.0 91.6 3 SER 52.3 62.5 74.9 4 VAL 40.9 34.4 76.7 5 PHE 161.5 96.8 44.0 6 TYR 181.0 100.0 31.4 7 TYR 90.4 49.9 61.8 8 LYS 173.2 99.9 50.0 9 THR 63.7 59.6 61.0 10 GLY 34.6 99.4 46.4 11 ASP 56.2 50.9 60.8 12 MET 143.5 90.0 54.2 13 LEU 95.7 64.7 66.6 14 PRO 27.2 21.8 81.1 15 GLU 27.2 19.6 69.0 16 ASP 71.2 64.4 66.7 17 THR 30.1 28.1 75.9 18 THR 58.3 54.6 70.4 19 HIS 113.9 75.8 59.3 20 VAL 118.8 100.0 38.8 21 ARG 151.5 72.5 58.0 22 TRP 205.0 100.0 49.3 23 PHE 126.4 75.8 68.8 24 LEU 147.7 100.0 41.8 25 ASN 99.6 82.4 59.9 26 ILE 143.5 100.0 27.0 27 ASN 120.8 99.9 50.0 28 ASN 93.6 77.4 62.3 29 GLU 67.8 49.0 80.8 30 LYS 99.3 57.3 79.0 31 SER 58.1 69.5 69.8 32 TYR 102.5 56.6 68.5 33 VAL 118.8 100.0 48.8 34 SER 56.5 67.6 61.2 35 LYS 121.9 70.3 69.1 36 ASP 52.6 47.6 62.9 37 ILE 143.5 100.0 34.3 38 THR 69.0 64.6 55.5 39 ILE 143.3 99.9 33.0 40 LYS 78.4 45.2 70.2 41 ASP 110.3 99.8 53.1 42 GLN 95.0 63.9 72.6 43 ILE 143.5 100.0 52.8 44 GLN 84.0 56.5 72.1 45 GLY 0.0 0.0 82.1 46 GLY 27.4 78.7 71.4 47 GLN 148.6 100.0 51.2 48 GLN 85.8 57.7 69.7 49 LEU 147.8 100.0 39.0 50 ASP 65.5 59.2 71.3 51 LEU 100.6 68.0 59.6 52 SER 38.3 45.8 85.9 53 THR 73.0 68.3 70.1 54 LEU 145.3 98.3 34.8 55 ASN 96.2 79.6 64.6 56 ILE 143.4 99.9 30.9 57 ASN 64.1 53.0 57.7 58 VAL 118.8 100.0 41.5 59 THR 54.4 50.9 76.7 60 GLY 23.4 67.1 68.5 61 THR 38.7 36.2 74.7 62 HIS 69.6 46.4 63.5 63 SER 36.0 43.1 75.9 64 ASN 36.6 30.3 78.5 65 TYR 80.9 44.7 74.9 66 TYR 160.1 88.5 44.2 67 SER 42.6 51.0 64.0 68 GLY 0.0 0.0 84.0 69 GLN 44.1 29.7 76.4 70 SER 28.5 34.0 83.0 71 ALA 69.8 96.1 60.7 72 ILE 109.4 76.2 46.3 73 THR 32.2 30.1 72.5 74 ASP 60.1 54.4 64.8 75 PHE 166.5 99.8 27.4 76 GLU 110.4 79.7 60.5 77 LYS 38.6 22.2 83.1 78 ALA 39.1 53.9 67.3 79 PHE 162.8 97.6 36.4 80 PRO 57.7 46.3 81.3 81 GLY 0.9 2.5 75.9 82 SER 83.6 100.0 43.8 83 LYS 53.4 30.8 82.4 84 ILE 143.5 100.0 27.5 85 THR 32.3 30.2 73.3 86 VAL 115.2 97.0 40.4 87 ASP 57.0 51.6 68.9 88 ASN 65.9 54.5 66.0 89 THR 0.2 0.2 86.3 90 LYS 37.4 21.6 81.2 91 ASN 103.1 85.3 67.4 92 THR 80.1 74.9 58.6 93 ILE 143.5 100.0 30.8 94 ASP 58.6 53.1 66.2 95 VAL 118.5 99.7 34.9 96 THR 61.7 57.7 69.2 97 ILE 143.3 99.9 29.2 98 PRO 99.6 80.0 62.9 99 GLN 93.3 62.8 68.8 100 GLY 3.7 10.7 75.8 101 TYR 116.8 64.5 60.4 102 GLY 34.8 100.0 45.1 103 SER 80.2 95.9 56.6 104 TYR 68.0 37.6 71.4 105 ASN 119.8 99.1 48.1 106 SER 67.9 81.2 66.5 107 PHE 166.5 99.8 33.6 108 SER 52.8 63.2 69.0 109 ILE 143.1 99.7 28.6 110 ASN 102.2 84.5 58.4 111 TYR 180.9 100.0 38.8 112 LYS 125.5 72.4 53.3 113 THR 106.9 100.0 43.9 114 LYS 90.1 52.0 69.4 115 ILE 134.6 93.8 49.2 116 THR 48.1 45.0 67.4 117 ASN 56.6 46.8 72.9 118 GLU 40.8 29.4 78.6 119 GLN 15.6 10.5 86.4 120 GLN 105.5 71.0 68.8 121 LYS 55.7 32.1 82.4 122 GLU 56.8 41.0 63.6 123 PHE 166.0 99.5 47.2 124 VAL 74.2 62.5 64.8 125 ASN 120.9 100.0 50.7 126 ASN 81.1 67.1 70.1 127 SER 83.6 100.0 56.0 128 GLN 111.0 74.7 64.6 129 ALA 72.6 100.0 31.8 130 TRP 138.9 67.7 55.3 131 TYR 165.3 91.4 34.0 132 GLN 99.6 67.0 61.6 133 GLU 117.2 84.6 51.4 134 HIS 40.1 26.7 77.4 135 GLY 0.0 0.0 79.1 136 LYS 60.3 34.8 87.5 137 GLU 0.0 0.0 90.4 138 GLU 70.3 50.7 75.7 139 VAL 87.7 73.8 58.3 140 ASN 64.6 53.4 75.2 141 GLY 22.3 63.9 60.3 142 LYS 57.5 33.2 72.5 143 SER 38.6 46.2 74.5 144 PHE 135.1 81.0 61.1 145 ASN 69.9 57.8 71.4 146 HIS 93.6 62.3 68.8 147 THR 71.1 66.5 57.6 148 VAL 111.4 93.8 48.4 149 HIS 47.0 31.3 76.7 150 ASN 71.4 59.1 62.6