Protein Data Bank File : 1j97a Title : HYDROLASE 24-MAY-01 1J97 Number of Amino Acid Residues : 209 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU LYS LYS LYS LYS LEU ILE LEU PHE PHE 10 ASP SER THR LEU VAL ASN ASN GLU THR ILE 20 ASP GLU ILE ALA ARG GLU ALA GLY VAL GLU 30 GLU GLU VAL LYS LYS ILE THR LYS GLU ALA 40 MET GLU GLY LYS LEU ASN PHE GLU GLN SER 50 LEU ARG LYS ARG VAL SER LEU LEU LYS ASP 60 LEU PRO ILE GLU LYS VAL GLU LYS ALA ILE 70 LYS ARG ILE THR PRO THR GLU GLY ALA GLU 80 GLU THR ILE LYS GLU LEU LYS ASN ARG GLY 90 TYR VAL VAL ALA VAL VAL SER GLY GLY PHE 100 ASP ILE ALA VAL ASN LYS ILE LYS GLU LYS 110 LEU GLY LEU ASP TYR ALA PHE ALA ASN ARG 120 LEU ILE VAL LYS ASP GLY LYS LEU THR GLY 130 ASP VAL GLU GLY GLU VAL LEU LYS GLU ASN 140 ALA LYS GLY GLU ILE LEU GLU LYS ILE ALA 150 LYS ILE GLU GLY ILE ASN LEU GLU ASP THR 160 VAL ALA VAL GLY ASP GLY ALA ASN ASP ILE 170 SER MET PHE LYS LYS ALA GLY LEU LYS ILE 180 ALA PHE CYS ALA LYS PRO ILE LEU LYS GLU 190 LYS ALA ASP ILE CYS ILE GLU LYS ARG ASP 200 LEU ARG GLU ILE LEU LYS TYR ILE LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 -151.7 179.4 -37.9 -165.0 -43.9 2 LYS 136.7 141.0 -178.2 -177.0 -168.0 81.3 174.2 3 LYS -78.4 148.0 175.6 53.8 -173.3 45.0 175.3 4 LYS -85.0 156.0 173.8 -64.4 -178.0 178.7 -56.4 5 LYS -120.5 159.8 178.0 -69.7 -177.8 170.0 175.4 6 LEU -116.9 126.6 -179.4 169.1 66.4 7 ILE -119.3 123.6 178.5 -44.6 -66.4 8 LEU -109.4 126.9 176.9 -95.5 66.8 9 PHE -112.3 -150.1 37.4 -70.8 -88.6 10 PHE -127.9 -73.9 -175.8 -175.7 68.9 11 ASP -60.5 125.1 -178.1 -66.4 116.3 12 SER 69.4 -0.4 177.7 -65.1 13 THR -114.4 -75.0 176.6 -66.0 14 LEU -67.4 -29.6 177.5 -83.1 175.5 15 VAL -122.3 161.2 -176.7 -62.6 16 ASN -78.3 -19.3 -172.5 -62.9 -59.2 17 ASN -103.6 172.1 173.1 -32.2 61.2 18 GLU -110.3 109.6 -178.8 -75.6 -71.5 -25.3 19 THR -50.9 -49.8 -179.3 -56.6 20 ILE -57.6 -37.7 -179.9 -177.7 60.2 21 ASP -71.7 -36.3 177.8 -66.3 -11.6 22 GLU -63.4 -42.9 -178.6 -65.4 -74.1 0.6 23 ILE -67.5 -38.4 178.6 -61.7 171.8 24 ALA -57.2 -37.0 176.7 25 ARG -58.9 -43.5 -179.3 163.9 65.6 -178.1 79.6 26 GLU -66.8 -28.5 180.0 -63.1 -57.7 -44.2 27 ALA -85.8 -1.8 179.3 28 GLY 74.9 21.3 -178.4 29 VAL -129.6 33.2 -178.0 -67.0 30 GLU -56.8 -49.7 -177.9 -175.1 171.8 37.6 31 GLU -59.8 -49.4 -178.5 -173.7 178.1 -40.6 32 GLU -62.8 -45.9 -179.3 -178.1 171.2 23.2 33 VAL -69.3 -40.4 179.3 169.4 34 LYS -57.5 -42.2 -180.0 -160.6 160.1 -179.5 -177.0 35 LYS -63.0 -43.8 178.2 178.3 165.1 -61.0 -177.3 36 ILE -66.0 -41.5 179.0 -62.1 163.1 37 THR -59.3 -45.6 179.3 -62.7 38 LYS -61.0 -46.0 178.1 178.3 173.6 -173.7 -63.3 39 GLU -62.2 -41.6 179.7 -62.1 176.0 -51.8 40 ALA -63.2 -45.4 -179.0 41 MET -72.6 -22.6 176.3 -67.3 -58.8 93.1 42 GLU -84.3 -4.1 177.6 -60.8 173.9 -34.7 43 GLY 86.3 14.8 -178.5 44 LYS -87.5 -2.0 179.8 -50.4 -179.3 171.8 175.2 45 LEU -142.4 153.2 175.8 -58.5 174.2 46 ASN -65.4 132.3 -177.0 168.8 -85.4 47 PHE -61.0 -53.4 -178.8 -176.6 70.8 48 GLU -58.8 -44.0 179.0 -177.3 169.1 -2.2 49 GLN -60.6 -43.0 -177.9 -66.6 177.7 38.5 50 SER -68.1 -34.5 -179.3 77.5 51 LEU -72.6 -44.5 178.0 -171.3 64.6 52 ARG -61.9 -37.8 178.1 -71.2 -176.5 -179.9 -79.7 53 LYS -61.9 -44.9 179.6 -177.6 178.6 173.0 64.4 54 ARG -66.9 -44.1 180.0 -72.2 171.8 -78.7 162.0 55 VAL -65.2 -32.2 178.6 174.4 56 SER -61.8 -30.1 179.4 68.9 57 LEU -71.4 -9.4 -179.9 -63.8 172.7 58 LEU -96.3 4.7 -178.4 -48.0 178.1 59 LYS -53.3 137.7 178.5 -178.7 173.9 -175.8 174.4 60 ASP 77.1 1.7 -179.6 -65.7 -36.6 61 LEU -70.3 126.9 179.5 -176.7 72.3 62 PRO -62.2 147.1 -178.7 -28.9 47.0 63 ILE -60.8 -29.4 179.6 -164.4 75.6 64 GLU -64.0 -33.4 178.7 -67.2 62.9 37.7 65 LYS -75.7 -34.0 176.0 -68.0 -54.1 -175.8 54.6 66 VAL -61.6 -41.9 179.3 177.8 67 GLU -64.5 -36.0 179.8 -68.7 -55.6 -26.9 68 LYS -64.1 -39.1 178.9 178.1 177.7 -177.5 176.5 69 ALA -67.1 -44.6 -179.8 70 ILE -59.7 -36.2 -178.9 -63.2 -57.1 71 LYS -60.1 -30.7 -179.9 80.0 -174.3 173.9 71.8 72 ARG -73.2 -11.7 -179.3 -64.6 -164.5 -68.6 -89.5 73 ILE -69.9 130.7 -179.4 -65.3 176.7 74 THR -123.4 142.9 179.6 54.4 75 PRO -68.8 144.0 178.0 -26.5 46.9 76 THR -66.0 146.6 177.3 -64.3 77 GLU -47.9 134.0 176.3 -172.3 -179.9 -29.7 78 GLY 78.6 1.0 -177.7 79 ALA -54.1 -56.0 -176.2 80 GLU -65.9 -42.5 -179.4 -174.3 159.2 14.5 81 GLU -60.0 -39.3 179.7 -174.4 177.7 -32.5 82 THR -66.1 -48.5 179.3 -63.2 83 ILE -59.9 -44.9 179.4 -64.5 -59.6 84 LYS -62.8 -37.1 179.2 -69.3 -71.4 -179.2 -78.4 85 GLU -67.9 -42.4 177.0 172.6 53.3 19.1 86 LEU -61.1 -40.6 178.7 -64.9 169.6 87 LYS -68.4 -31.4 179.6 -67.9 -172.7 -62.5 178.8 88 ASN -62.5 -30.5 -180.0 179.2 43.5 89 ARG -82.7 -1.7 -178.7 -62.6 179.7 -168.5 -173.9 90 GLY 88.7 12.6 -177.3 91 TYR -81.9 158.5 179.8 -59.6 -14.4 92 VAL -99.0 135.4 -177.4 179.9 93 VAL -126.6 134.6 -178.2 -56.0 94 ALA -131.4 152.8 171.5 95 VAL -115.5 129.4 -178.1 57.3 96 VAL -131.3 118.2 -171.4 -175.3 97 SER -136.4 142.0 173.1 179.8 98 GLY -82.0 4.0 177.9 99 GLY -86.5 -143.3 -169.5 100 PHE -127.7 139.9 178.4 -47.8 -59.6 101 ASP -50.9 -37.9 -176.7 -73.0 -23.1 102 ILE -58.0 -26.5 176.2 -164.9 172.3 103 ALA -97.8 -45.9 -177.4 104 VAL -67.0 -29.0 -179.9 -178.2 105 ASN -60.1 -45.1 -179.6 -74.9 -29.6 106 LYS -58.5 -47.8 -176.2 -68.0 -153.5 177.5 70.7 107 ILE -68.7 -30.9 177.7 71.9 149.9 108 LYS -56.3 -45.4 -178.7 -177.3 -160.3 -178.9 -176.1 109 GLU -78.4 -43.5 -178.8 -53.9 -56.3 171.2 110 LYS -59.0 -46.5 -178.5 178.3 -168.5 171.6 -179.9 111 LEU -92.0 -5.9 178.1 -53.7 171.9 112 GLY 75.8 47.6 179.2 113 LEU -84.5 153.7 -179.9 -52.3 -177.9 114 ASP -85.2 -23.4 -177.9 -55.6 -53.9 115 TYR -146.9 147.0 176.4 -70.7 -89.8 116 ALA -145.1 129.5 179.0 117 PHE -133.6 128.9 177.2 -70.8 -95.5 118 ALA -157.6 174.0 176.7 119 ASN -90.1 -176.0 -179.5 -60.4 -51.7 120 ARG -139.6 140.4 176.0 55.4 -166.3 167.7 -82.1 121 LEU -83.3 131.1 178.3 -66.8 166.6 122 ILE -82.0 136.1 -176.9 -56.7 -50.9 123 VAL -126.7 145.0 -179.8 -172.3 124 LYS -148.9 130.6 -179.7 177.8 177.3 57.5 178.5 125 ASP 48.5 41.2 177.5 -68.1 -53.0 126 GLY 75.7 14.0 -178.5 127 LYS -137.3 153.1 176.7 -62.4 178.7 168.6 56.8 128 LEU -67.9 139.3 178.1 -62.1 -173.7 129 THR -87.5 -14.6 -176.8 68.9 130 GLY 99.6 -1.5 178.2 131 ASP -103.4 157.6 176.7 -171.7 40.6 132 VAL -137.3 143.5 175.9 48.2 133 GLU -140.9 158.9 179.1 -58.7 -65.3 160.6 134 GLY 156.9 -179.7 -179.1 135 GLU -111.2 22.2 175.9 -48.5 -50.6 -51.7 136 VAL -126.6 53.7 -177.4 -159.1 137 LEU -121.6 -45.0 -178.1 -67.4 173.6 138 LYS -64.2 160.2 -177.9 -61.8 168.6 63.2 -177.9 139 GLU -57.2 -37.2 -180.0 -177.2 179.8 49.7 140 ASN -100.0 21.1 -175.7 -157.5 -60.8 141 ALA -57.7 -48.2 -178.5 142 LYS -67.2 -34.2 178.5 -60.2 -162.1 -172.8 -174.6 143 GLY -66.7 -37.2 179.0 144 GLU -63.3 -41.0 180.0 173.0 175.5 -26.6 145 ILE -69.1 -40.8 177.9 -72.0 165.3 146 LEU -58.2 -47.9 -179.7 -176.6 157.2 147 GLU -60.8 -41.4 -179.0 -73.5 -177.4 166.6 148 LYS -63.8 -45.3 -177.8 166.8 -174.3 167.2 177.7 149 ILE -66.6 -43.1 179.6 -61.0 170.8 150 ALA -58.8 -38.1 179.7 151 LYS -66.9 -43.8 178.9 -82.8 -67.8 -172.9 59.6 152 ILE -60.1 -40.8 -176.9 -68.9 168.3 153 GLU -85.6 -4.5 -178.4 -62.5 -66.2 -21.3 154 GLY 69.3 23.4 -177.2 155 ILE -102.1 126.2 179.5 -64.0 172.5 156 ASN -65.4 146.2 179.6 -168.7 -77.2 157 LEU -57.3 -25.8 179.9 -67.5 -175.6 158 GLU -68.9 -16.3 -178.5 76.4 178.9 -26.4 159 ASP -103.6 28.0 177.0 -62.8 -49.3 160 THR -112.8 153.7 -178.9 64.1 161 VAL -135.6 132.2 177.6 176.9 162 ALA -117.1 134.0 -178.7 163 VAL -128.8 119.1 -178.2 -173.6 164 GLY -158.2 180.0 -176.5 165 ASP -127.5 -19.8 -171.2 70.6 -71.5 166 GLY -122.4 174.1 -178.8 167 ALA -59.1 -25.5 -179.5 168 ASN -79.7 1.6 174.9 66.8 -32.4 169 ASP -95.1 -7.3 -179.1 -62.4 -42.8 170 ILE -59.7 -43.5 -177.7 -71.3 170.9 171 SER -66.2 -28.1 177.7 72.7 172 MET -70.7 -45.5 177.1 -175.7 165.7 71.5 173 PHE -57.4 -41.4 -176.7 -92.9 24.5 174 LYS -54.5 -34.9 -177.8 -71.2 -173.8 -178.1 179.3 175 LYS -97.5 -15.5 -175.4 -59.1 -55.2 -178.2 -172.1 176 ALA -74.4 149.1 176.2 177 GLY -72.7 -35.6 178.8 178 LEU -133.0 130.7 -176.0 179.4 61.2 179 LYS -114.7 112.8 179.6 -59.0 159.9 176.7 52.3 180 ILE -114.7 118.2 177.2 -57.7 175.2 181 ALA -93.1 117.3 -178.2 182 PHE -101.7 109.4 -178.3 -175.2 71.4 183 CYS 40.9 51.9 -170.5 -59.5 184 ALA -90.6 166.7 176.8 185 LYS -74.2 151.5 179.9 -71.9 -61.9 179.4 -178.5 186 PRO -50.3 -40.0 -178.0 -35.9 49.2 187 ILE -62.6 -32.0 -180.0 -167.7 176.6 188 LEU -84.8 -37.7 179.7 -170.8 71.3 189 LYS -56.7 -35.1 -179.5 -65.2 -170.1 -69.9 -175.7 190 GLU -62.4 -28.3 -177.3 -165.7 -173.9 -44.5 191 LYS -99.6 -8.0 -177.3 -67.7 166.4 173.0 -58.6 192 ALA -77.2 155.5 172.3 193 ASP -80.9 -47.4 -177.6 -71.5 -49.6 194 ILE -123.3 137.3 176.5 -58.0 -59.8 195 CYS -116.9 123.9 177.2 -68.8 196 ILE -106.9 129.1 179.2 -65.3 178.3 197 GLU -114.2 -8.0 176.5 -56.4 -52.4 -33.1 198 LYS -86.6 128.0 -177.2 175.4 158.8 -68.5 -177.9 199 ARG -80.9 73.7 -179.5 -162.0 168.0 -175.8 85.0 200 ASP -153.1 112.6 -178.3 -176.6 -17.6 201 LEU -60.0 -21.4 179.1 -78.0 164.8 202 ARG -63.9 -18.6 177.3 -65.9 170.7 -70.5 -172.5 203 GLU -60.7 -24.6 179.8 -64.7 -70.3 -40.6 204 ILE -72.3 -22.6 -173.9 74.2 178.3 205 LEU -58.9 -37.9 179.3 -65.8 169.9 206 LYS -56.2 -27.9 -175.4 -49.8 -171.2 -65.7 -66.2 207 TYR -94.4 -2.3 -176.8 -58.7 -78.1 208 ILE -122.4 122.2 176.7 -57.6 163.0 209 LYS -76.2 138.0 0.0 178.4 178.6 -177.7 174.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 59.141 25.792 17.526 2 LYS 61.523 24.483 20.293 3 LYS 61.505 21.393 22.456 4 LYS 59.765 20.900 25.708 5 LYS 61.545 19.591 28.764 6 LEU 60.064 17.587 31.613 7 ILE 60.973 18.637 35.174 8 LEU 60.246 16.338 38.109 9 PHE 60.311 17.630 41.649 10 PHE 57.843 16.934 47.412 11 ASP 59.019 16.471 51.040 12 SER 61.982 18.721 51.891 13 THR 62.176 19.815 48.188 14 LEU 58.947 21.573 47.028 15 VAL 58.038 22.101 50.679 16 ASN 60.235 22.757 53.703 17 ASN 58.830 19.921 55.793 18 GLU 58.595 16.168 55.969 19 THR 54.871 15.352 55.847 20 ILE 55.374 12.049 57.684 21 ASP 57.287 13.774 60.521 22 GLU 54.607 16.451 60.907 23 ILE 51.894 13.796 61.196 24 ALA 54.085 11.826 63.656 25 ARG 54.020 14.813 66.003 26 GLU 50.205 14.645 66.216 27 ALA 50.456 10.892 66.837 28 GLY 52.972 11.383 69.657 29 VAL 55.802 9.534 67.947 30 GLU 57.743 12.500 66.547 31 GLU 61.164 11.481 67.858 32 GLU 60.985 7.888 66.669 33 VAL 59.605 8.748 63.212 34 LYS 62.004 11.682 62.630 35 LYS 64.934 9.309 63.242 36 ILE 63.661 6.715 60.754 37 THR 62.915 9.431 58.184 38 LYS 66.454 10.783 58.468 39 GLU 67.997 7.292 58.068 40 ALA 65.708 6.586 55.089 41 MET 66.601 9.845 53.318 42 GLU 70.324 9.336 54.023 43 GLY 69.982 5.916 52.301 44 LYS 70.596 3.766 55.385 45 LEU 67.266 1.928 55.110 46 ASN 65.078 0.311 52.426 47 PHE 62.510 2.990 51.616 48 GLU 59.330 0.930 51.589 49 GLN 60.228 -0.926 54.739 50 SER 61.030 2.364 56.497 51 LEU 57.827 4.018 55.347 52 ARG 55.598 1.136 56.421 53 LYS 57.390 1.098 59.791 54 ARG 56.710 4.808 60.256 55 VAL 53.111 4.760 59.092 56 SER 52.311 1.842 61.401 57 LEU 53.210 4.146 64.355 58 LEU 50.384 6.462 63.193 59 LYS 47.619 3.911 63.714 60 ASP 44.347 5.322 65.121 61 LEU 45.213 8.971 64.548 62 PRO 42.011 10.907 63.689 63 ILE 41.876 12.452 60.255 64 GLU 41.345 15.901 61.854 65 LYS 44.831 15.612 63.422 66 VAL 46.346 14.551 60.100 67 GLU 44.852 17.749 58.627 68 LYS 46.316 19.849 61.466 69 ALA 49.745 18.434 60.623 70 ILE 49.298 19.052 56.864 71 LYS 48.359 22.681 57.542 72 ARG 51.849 23.274 58.952 73 ILE 53.452 22.384 55.624 74 THR 54.930 25.456 53.899 75 PRO 56.183 25.796 50.296 76 THR 59.915 26.214 49.831 77 GLU 61.063 29.736 48.950 78 GLY 60.598 30.431 45.256 79 ALA 58.459 27.400 44.492 80 GLU 55.579 28.995 42.563 81 GLU 57.780 31.458 40.728 82 THR 60.061 28.629 39.623 83 ILE 57.167 26.426 38.442 84 LYS 55.544 29.304 36.556 85 GLU 58.815 30.178 34.825 86 LEU 59.302 26.539 33.738 87 LYS 55.712 26.489 32.382 88 ASN 56.377 29.824 30.695 89 ARG 59.079 28.079 28.648 90 GLY 56.480 25.486 27.586 91 TYR 57.843 22.809 29.929 92 VAL 55.965 19.963 31.652 93 VAL 56.233 19.836 35.455 94 ALA 55.581 16.955 37.819 95 VAL 55.745 16.207 41.519 96 VAL 56.809 12.632 42.473 97 SER 56.799 11.793 46.171 98 GLY 57.258 8.920 48.568 99 GLY 54.775 10.889 50.698 100 PHE 50.997 11.135 50.628 101 ASP 48.258 12.305 48.314 102 ILE 46.494 14.135 51.140 103 ALA 49.418 16.575 51.145 104 VAL 50.634 16.339 47.541 105 ASN 47.134 16.818 46.013 106 LYS 46.977 20.274 47.420 107 ILE 50.303 21.460 46.016 108 LYS 49.563 20.021 42.602 109 GLU 46.611 22.418 42.371 110 LYS 48.186 25.272 44.312 111 LEU 51.388 25.462 42.245 112 GLY 49.835 24.329 38.982 113 LEU 51.591 21.028 38.269 114 ASP 50.865 18.756 35.328 115 TYR 51.396 15.460 37.143 116 ALA 51.403 14.279 40.725 117 PHE 52.377 10.852 42.048 118 ALA 52.437 9.912 45.743 119 ASN 51.405 7.119 48.071 120 ARG 48.260 7.040 50.208 121 LEU 47.387 6.687 53.851 122 ILE 44.646 4.109 54.464 123 VAL 41.708 5.397 56.546 124 LYS 38.871 3.621 58.379 125 ASP 36.137 5.176 60.523 126 GLY 37.822 8.552 60.366 127 LYS 41.211 7.366 61.621 128 LEU 44.417 6.140 60.061 129 THR 44.684 2.377 60.018 130 GLY 48.453 2.403 60.023 131 ASP 48.759 1.125 56.418 132 VAL 50.132 2.885 53.350 133 GLU 49.798 1.800 49.723 134 GLY 50.968 3.192 46.417 135 GLU 53.350 3.122 43.465 136 VAL 56.108 5.349 44.877 137 LEU 57.502 2.749 47.261 138 LYS 59.917 0.396 45.507 139 GLU 63.542 1.371 45.148 140 ASN 63.275 2.235 41.437 141 ALA 59.785 3.750 41.693 142 LYS 60.590 7.316 40.793 143 GLY 62.729 6.345 37.831 144 GLU 59.880 4.184 36.522 145 ILE 57.498 7.155 36.815 146 LEU 59.937 9.533 35.120 147 GLU 60.209 7.137 32.191 148 LYS 56.427 6.694 32.000 149 ILE 55.710 10.452 31.988 150 ALA 58.441 11.143 29.413 151 LYS 56.890 8.495 27.130 152 ILE 53.412 9.984 27.404 153 GLU 54.806 13.430 26.558 154 GLY 57.089 12.361 23.705 155 ILE 60.050 13.881 25.577 156 ASN 63.461 12.209 25.270 157 LEU 65.108 11.298 28.564 158 GLU 67.952 13.686 27.781 159 ASP 65.405 16.500 28.079 160 THR 64.323 15.598 31.594 161 VAL 65.429 17.204 34.875 162 ALA 65.096 15.677 38.367 163 VAL 65.195 17.815 41.542 164 GLY 65.267 16.169 44.980 165 ASP 66.901 15.942 48.382 166 GLY 66.831 12.310 49.485 167 ALA 67.849 8.765 48.788 168 ASN 64.480 7.910 47.246 169 ASP 65.298 10.423 44.463 170 ILE 68.271 8.312 43.316 171 SER 66.225 6.192 40.865 172 MET 64.843 9.442 39.322 173 PHE 68.393 10.812 38.935 174 LYS 69.409 7.566 37.158 175 LYS 67.081 8.240 34.243 176 ALA 67.250 12.049 34.211 177 GLY 69.071 14.265 31.760 178 LEU 70.039 16.795 34.496 179 LYS 70.295 15.805 38.187 180 ILE 69.854 18.570 40.736 181 ALA 70.333 17.862 44.459 182 PHE 68.471 20.564 46.395 183 CYS 69.880 21.181 49.937 184 ALA 70.333 17.416 49.784 185 LYS 71.597 14.492 51.802 186 PRO 75.150 13.346 51.013 187 ILE 74.060 10.150 49.249 188 LEU 72.133 12.159 46.664 189 LYS 74.729 14.949 46.375 190 GLU 77.266 12.317 45.343 191 LYS 75.125 11.415 42.372 192 ALA 74.022 14.892 41.368 193 ASP 75.176 17.000 38.488 194 ILE 74.466 20.223 40.437 195 CYS 74.187 20.738 44.198 196 ILE 72.253 23.746 45.396 197 GLU 72.678 24.734 49.063 198 LYS 70.820 28.061 49.105 199 ARG 67.212 27.242 50.007 200 ASP 65.437 28.941 47.071 201 LEU 64.064 26.861 44.248 202 ARG 64.684 29.694 41.804 203 GLU 68.362 28.706 42.009 204 ILE 67.710 25.753 39.694 205 LEU 66.675 28.042 36.822 206 LYS 70.277 29.078 36.010 207 TYR 71.127 25.469 35.129 208 ILE 68.231 24.852 32.763 209 LYS 67.901 26.365 29.332 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/X X/T 10 T T T C C C C H H H 20 H H H H H H H H H H 30 H H H H H H H H H H 40 H H H C C H H H H H 50 H H H H H H H H 3 C 60 C H H H H H H H H H 70 H H 3/S S S S S H H H 80 H H H H H H H H H H/S 90 S S S S S S S S C H 100 H H H H H H H H H H 110 H H/S S S S/S S S S S S 120 S S S/T T T T/S S S S S 130 S S S S C C C C C H 140 H H H H H H H H H H 150 H H H H C T T T T/S S 160 S S S S S S C C H H 170 H H H H H H S S S S 180 S S S C H H H H H H 190 H H S S S S S S C C 200 C T T T T/T T T T/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E t 10 T T T T B S S h H H 20 H H H H H H h T h H 30 H H H H H H H H H H 40 H h T t S h H H H H 50 H H H H H H h T T T 60 t h H H H H H H H H 70 H h t B t T h H H 80 H H H H H H H H h T 90 t E E E E E E E E E 100 H H H H H H H H H H 110 H h t S E E E E E E 120 E E E E T T E E E E 130 E E E S S t T h 140 H H H H H H H H H H 150 H H H h t g G G e E 160 E E E E S g G G h H 170 H H H H H h S E E E 180 E E e h H H H H h 190 T t S E E E S S g 200 G G G G G G G g Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 0.0 0.0 96.5 2 LYS 70.9 40.9 76.1 3 LYS 48.0 27.7 84.5 4 LYS 72.1 41.6 66.3 5 LYS 133.3 76.9 49.2 6 LEU 147.8 100.0 29.5 7 ILE 143.5 100.0 27.4 8 LEU 147.8 100.0 32.1 9 PHE 166.5 99.8 25.0 10 PHE 166.0 99.5 37.8 11 ASP 94.7 85.7 65.0 12 SER 61.2 73.2 75.7 13 THR 105.1 98.4 51.4 14 LEU 147.6 99.8 24.8 15 VAL 118.1 99.4 48.0 16 ASN 76.9 63.6 73.3 17 ASN 94.6 78.2 64.7 18 GLU 111.1 80.2 56.3 19 THR 106.6 99.7 33.3 20 ILE 136.0 94.8 39.4 21 ASP 93.1 84.2 45.5 22 GLU 107.1 77.3 62.7 23 ILE 143.5 100.0 26.5 24 ALA 72.6 100.0 45.4 25 ARG 78.9 37.8 83.5 26 GLU 128.3 92.6 56.9 27 ALA 64.4 88.8 52.1 28 GLY 1.8 5.2 82.5 29 VAL 87.8 73.9 59.2 30 GLU 69.2 49.9 64.3 31 GLU 4.6 3.3 84.1 32 GLU 56.7 40.9 58.7 33 VAL 118.8 100.0 40.2 34 LYS 46.3 26.7 80.8 35 LYS 42.3 24.4 80.9 36 ILE 132.6 92.4 41.9 37 THR 101.7 95.2 55.0 38 LYS 65.8 38.0 80.2 39 GLU 81.1 58.5 54.1 40 ALA 72.6 100.0 58.5 41 MET 142.1 89.2 58.5 42 GLU 118.4 85.4 53.6 43 GLY 30.4 87.4 58.5 44 LYS 55.3 31.9 77.9 45 LEU 87.7 59.3 66.2 46 ASN 56.2 46.5 73.4 47 PHE 146.7 87.9 57.2 48 GLU 94.0 67.8 57.8 49 GLN 24.2 16.3 80.2 50 SER 80.7 96.6 46.7 51 LEU 144.3 97.6 44.8 52 ARG 132.3 63.3 70.4 53 LYS 55.1 31.8 74.2 54 ARG 204.5 97.9 34.2 55 VAL 118.5 99.7 37.8 56 SER 34.4 41.2 75.2 57 LEU 100.3 67.9 63.0 58 LEU 147.8 100.0 34.5 59 LYS 57.1 32.9 84.8 60 ASP 32.3 29.3 67.5 61 LEU 135.5 91.7 43.5 62 PRO 78.5 63.0 64.1 63 ILE 99.7 69.5 51.5 64 GLU 26.1 18.9 69.6 65 LYS 87.4 50.4 63.9 66 VAL 118.8 100.0 29.0 67 GLU 74.1 53.5 62.9 68 LYS 72.8 42.0 72.4 69 ALA 72.6 100.0 54.3 70 ILE 136.4 95.0 43.9 71 LYS 63.8 36.8 68.9 72 ARG 146.7 70.2 67.6 73 ILE 133.7 93.2 43.4 74 THR 38.8 36.3 75.2 75 PRO 86.9 69.8 59.2 76 THR 106.9 100.0 58.2 77 GLU 46.2 33.3 84.7 78 GLY 28.6 82.1 67.6 79 ALA 71.6 98.6 48.4 80 GLU 69.4 50.1 64.6 81 GLU 44.9 32.4 72.3 82 THR 106.4 99.6 35.0 83 ILE 143.1 99.7 34.2 84 LYS 90.3 52.1 73.0 85 GLU 87.6 63.2 68.4 86 LEU 147.8 100.0 27.5 87 LYS 124.7 71.9 67.1 88 ASN 26.7 22.1 85.8 89 ARG 160.3 76.8 63.4 90 GLY 11.0 31.5 80.3 91 TYR 177.1 97.8 46.1 92 VAL 104.4 87.9 44.2 93 VAL 118.8 100.0 40.0 94 ALA 72.6 100.0 38.3 95 VAL 118.8 100.0 35.2 96 VAL 118.8 100.0 30.7 97 SER 82.2 98.3 52.5 98 GLY 33.5 96.4 63.5 99 GLY 29.9 85.9 63.2 100 PHE 166.3 99.7 29.3 101 ASP 64.2 58.1 71.2 102 ILE 101.5 70.7 51.3 103 ALA 71.7 98.8 42.7 104 VAL 117.6 99.0 40.5 105 ASN 39.6 32.8 69.5 106 LYS 62.2 35.9 77.7 107 ILE 132.2 92.1 28.7 108 LYS 107.9 62.2 67.8 109 GLU 26.8 19.3 83.5 110 LYS 68.8 39.7 65.6 111 LEU 146.3 99.0 37.0 112 GLY 14.6 42.0 82.3 113 LEU 147.8 100.0 39.1 114 ASP 59.5 53.9 60.9 115 TYR 140.2 77.5 42.9 116 ALA 65.1 89.7 48.7 117 PHE 126.7 76.0 46.2 118 ALA 72.5 99.9 57.4 119 ASN 120.9 100.0 47.2 120 ARG 99.4 47.6 68.8 121 LEU 142.8 96.6 25.5 122 ILE 86.5 60.3 66.2 123 VAL 78.2 65.8 55.8 124 LYS 37.8 21.8 78.3 125 ASP 1.8 1.7 80.8 126 GLY 9.6 27.7 62.0 127 LYS 81.8 47.2 74.9 128 LEU 146.8 99.3 34.4 129 THR 84.7 79.3 53.5 130 GLY 32.5 93.4 59.3 131 ASP 62.4 56.5 67.7 132 VAL 118.4 99.6 35.0 133 GLU 76.5 55.2 73.5 134 GLY 34.8 100.0 67.6 135 GLU 12.6 9.1 84.5 136 VAL 116.0 97.7 46.5 137 LEU 140.1 94.8 53.4 138 LYS 22.3 12.9 87.1 139 GLU 3.0 2.2 89.5 140 ASN 57.1 47.2 66.8 141 ALA 65.1 89.6 63.1 142 LYS 163.9 94.5 55.2 143 GLY 34.8 100.0 61.3 144 GLU 28.4 20.5 80.5 145 ILE 135.5 94.4 32.2 146 LEU 147.8 100.0 35.4 147 GLU 77.4 55.8 58.6 148 LYS 62.7 36.1 62.8 149 ILE 143.4 100.0 24.6 150 ALA 70.3 96.8 48.3 151 LYS 16.8 9.7 87.4 152 ILE 59.0 41.1 70.3 153 GLU 96.9 69.9 53.6 154 GLY 0.0 0.0 83.4 155 ILE 133.6 93.1 50.7 156 ASN 30.6 25.3 79.9 157 LEU 87.1 59.0 64.1 158 GLU 30.9 22.3 81.5 159 ASP 93.9 85.0 50.8 160 THR 106.9 100.0 44.8 161 VAL 115.0 96.8 34.6 162 ALA 72.6 100.0 38.2 163 VAL 118.8 100.0 28.7 164 GLY 33.2 95.3 52.7 165 ASP 98.8 89.5 62.7 166 GLY 34.8 100.0 58.0 167 ALA 63.5 87.4 48.8 168 ASN 96.2 79.6 51.4 169 ASP 105.3 95.3 55.2 170 ILE 117.4 81.8 42.1 171 SER 81.1 97.0 63.3 172 MET 158.9 99.7 42.4 173 PHE 165.0 98.9 41.8 174 LYS 67.6 39.0 72.9 175 LYS 104.2 60.1 69.2 176 ALA 72.6 100.0 58.6 177 GLY 24.9 71.6 77.2 178 LEU 109.8 74.3 48.3 179 LYS 126.0 72.7 61.8 180 ILE 143.5 100.0 30.1 181 ALA 72.6 100.0 40.0 182 PHE 166.8 100.0 45.1 183 CYS 82.2 82.8 67.1 184 ALA 72.5 99.8 53.7 185 LYS 111.7 64.4 55.6 186 PRO 38.0 30.5 69.5 187 ILE 91.5 63.8 58.7 188 LEU 147.8 100.0 43.1 189 LYS 107.5 62.0 62.9 190 GLU 14.5 10.4 83.8 191 LYS 84.9 48.9 63.4 192 ALA 72.6 100.0 51.1 193 ASP 55.3 50.0 63.6 194 ILE 100.5 70.0 48.5 195 CYS 65.6 66.1 61.0 196 ILE 135.2 94.2 45.7 197 GLU 59.8 43.2 69.0 198 LYS 33.7 19.4 81.4 199 ARG 136.6 65.4 64.5 200 ASP 94.1 85.1 58.6 201 LEU 147.3 99.7 36.8 202 ARG 127.2 60.9 72.5 203 GLU 92.7 66.9 60.8 204 ILE 143.5 100.0 22.0 205 LEU 122.1 82.6 53.7 206 LYS 67.4 38.8 77.5 207 TYR 116.3 64.3 52.8 208 ILE 142.2 99.1 39.0 209 LYS 0.0 0.0 92.5