Protein Data Bank File : 1cmxc Title : HYDROLASE 12-MAY-99 1CMX Number of Amino Acid Residues : 210 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA VAL VAL PRO ILE GLU SER ASN PRO GLU 10 VAL PHE THR ASN PHE ALA HIS LYS LEU GLY 20 LEU LYS ASN GLU TRP ALA TYR PHE ASP ILE 30 TYR SER LEU THR GLU PRO GLU LEU LEU ALA 40 PHE LEU PRO ARG PRO VAL LYS ALA ILE VAL 50 LEU LEU PHE PRO VAL ILE TRP PHE LYS GLN 60 SER VAL LYS ASN ALA CYS GLY LEU TYR ALA 70 ILE LEU HIS SER LEU SER ASN ASN GLN SER 80 LEU LEU GLU PRO GLY SER ASP LEU ASP ASN 90 PHE LEU LYS SER GLN SER ASP THR SER SER 100 SER LYS ASN ARG PHE ASP ASP VAL THR THR 110 ASP GLN PHE VAL LEU ASN VAL ILE LYS GLU 120 ASN VAL GLN THR PHE SER THR GLY GLN SER 130 GLU ALA PRO GLU ALA THR ALA ASP THR ASN 140 LEU HIS TYR ILE THR TYR VAL GLU GLU ASN 150 GLY GLY ILE PHE GLU LEU ASP GLY ARG ASN 160 LEU SER GLY PRO LEU TYR LEU GLY LYS SER 170 ASP PRO THR ALA THR ASP LEU ILE GLU GLN 180 GLU LEU VAL ARG VAL ARG VAL ALA SER TYR 190 MET GLU ASN ALA ASN GLU GLU ASP VAL LEU 200 ASN PHE ALA MET LEU GLY LEU GLY PRO ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 131.3 179.8 2 VAL -118.4 164.6 179.0 -162.9 3 VAL -76.3 127.4 179.7 175.5 4 PRO -59.1 124.1 -177.3 23.8 -40.9 5 ILE -68.7 139.1 -179.5 -46.8 166.9 6 GLU -79.5 141.7 179.1 165.2 178.1 126.6 7 SER -72.8 61.8 -179.3 76.9 8 ASN -112.9 125.8 179.7 -174.8 -35.0 9 PRO -58.9 -31.1 -179.6 20.1 -33.8 10 GLU -70.2 -40.7 178.6 -66.0 -67.5 -24.8 11 VAL -68.2 -39.6 177.8 -175.2 12 PHE -66.0 -45.7 179.1 -92.2 68.0 13 THR -61.6 -40.3 179.1 -56.7 14 ASN -63.4 -51.4 176.9 -83.2 170.5 15 PHE -56.6 -50.0 -177.2 -86.9 114.6 16 ALA -57.0 -46.0 177.9 17 HIS -62.1 -37.5 179.5 -75.6 -21.3 18 LYS -68.4 -28.4 179.9 -64.5 -179.2 178.8 -176.3 19 LEU -79.9 -26.6 -177.1 -73.3 166.5 20 GLY 140.7 -5.3 179.6 21 LEU -60.9 128.9 179.2 176.0 68.6 22 LYS -55.5 152.3 180.0 -86.0 178.8 176.7 53.9 23 ASN -68.2 -21.8 179.7 -65.7 -30.4 24 GLU -72.4 -4.3 -179.4 -51.8 71.9 30.3 25 TRP -121.7 153.7 178.9 -62.7 88.3 26 ALA -162.8 166.0 177.3 27 TYR -90.4 148.2 179.4 -79.6 100.4 28 PHE -142.6 161.9 -179.0 54.9 75.1 29 ASP -73.0 136.0 175.7 -96.2 -42.2 30 ILE -115.8 114.8 -178.8 -59.5 174.1 31 TYR -107.5 -13.8 178.2 41.2 90.6 32 SER -150.1 122.3 -179.8 -108.1 33 LEU -113.5 65.3 166.9 -79.9 -173.1 34 THR 159.7 33.5 -175.1 86.7 35 GLU -128.9 117.8 -178.1 -176.1 62.1 27.4 36 PRO -41.0 -69.4 -179.4 34.3 -40.5 37 GLU -50.8 -50.5 -179.3 -96.6 -55.8 -24.7 38 LEU -64.4 -12.4 179.2 -46.3 177.0 39 LEU -92.4 -11.6 178.6 -64.7 -172.9 40 ALA -81.4 -20.6 179.2 41 PHE -87.5 -24.2 179.8 -72.1 119.2 42 LEU -83.8 129.0 -179.8 -72.3 -170.8 43 PRO -61.9 134.7 -179.3 -22.9 38.4 44 ARG -124.4 150.7 1.2 -38.6 -71.4 -63.0 -71.7 45 PRO -78.0 143.2 177.2 34.7 -43.1 46 VAL -88.0 114.9 -177.7 173.1 47 LYS -92.8 -14.7 176.8 -56.3 -61.4 -157.2 170.4 48 ALA -158.8 155.7 179.2 49 ILE -136.6 129.8 -180.0 -80.3 164.7 50 VAL -109.2 137.6 -177.8 177.2 51 LEU -125.0 132.4 176.1 169.6 73.7 52 LEU -113.5 128.0 -176.6 169.3 56.6 53 PHE -162.6 170.9 -179.7 70.1 110.1 54 PRO -66.2 26.5 26.6 -27.5 42.0 55 VAL 90.2 105.7 -179.0 -154.1 56 ILE -80.9 130.0 179.8 -58.4 160.4 57 TRP -128.0 147.2 179.5 176.7 76.9 58 PHE -130.5 132.8 176.0 -70.3 80.2 59 LYS -78.9 135.4 178.6 141.6 134.4 -68.9 -173.2 60 GLN -77.1 127.2 -179.6 168.1 154.6 -31.9 61 SER -119.9 -14.3 -178.1 -59.6 62 VAL -113.1 129.6 179.5 -178.0 63 LYS -56.9 137.2 179.4 -103.3 177.8 -167.0 167.4 64 ASN 62.6 11.4 -178.9 -67.6 -38.8 65 ALA -90.2 3.4 -178.5 66 CYS -46.3 -40.2 178.5 57.9 67 GLY -61.2 -38.6 180.0 68 LEU -69.4 -44.8 177.0 174.8 63.0 69 TYR -59.2 -32.0 178.7 -75.8 106.3 70 ALA -66.8 -41.5 177.1 71 ILE -66.4 -41.9 177.1 -66.9 148.2 72 LEU -59.1 -44.6 179.1 -71.4 -170.7 73 HIS -65.3 -44.7 177.7 -72.3 139.0 74 SER -59.9 -45.3 -178.0 -48.6 75 LEU -76.5 -45.3 -177.4 -64.3 -170.7 76 SER -62.4 -23.6 179.3 -58.3 77 ASN -101.1 12.2 179.0 -75.7 -66.9 78 ASN -138.0 37.1 -178.5 -83.6 -75.0 79 GLN -41.3 -26.4 179.7 -55.4 -156.0 28.9 80 SER -72.0 -11.3 178.9 156.1 81 LEU -97.6 -3.9 179.1 -51.2 -169.2 82 LEU -84.6 151.6 179.0 -65.6 -178.3 83 GLU -79.0 124.6 179.3 -85.9 -66.2 -6.9 84 PRO -62.8 127.9 -178.5 12.8 -26.4 85 GLY 102.4 -20.8 -179.7 86 SER -57.1 172.6 -179.4 61.8 87 ASP -64.2 -48.0 -178.0 -67.2 -34.3 88 LEU -67.2 -42.1 -179.7 -175.9 59.4 89 ASP -57.5 -41.6 178.3 -169.1 -113.1 90 ASN -64.2 -46.5 -179.0 -77.2 -9.1 91 PHE -59.1 -44.7 -179.0 172.6 77.8 92 LEU -62.6 -50.2 -179.9 -65.3 179.1 93 LYS -63.9 -37.1 179.4 -55.4 -131.2 172.2 -171.9 94 SER -53.8 -50.8 -178.7 161.1 95 GLN -69.2 -21.1 177.4 -59.6 -123.5 -82.7 96 SER -77.6 -44.5 179.8 -71.7 97 ASP -59.0 -52.2 -179.7 -65.8 -25.8 98 THR -79.9 -14.2 179.4 63.7 99 SER 58.8 33.5 179.7 78.8 100 SER -55.0 -78.6 177.4 42.6 101 SER -126.1 94.5 -178.7 -70.8 102 LYS -47.6 -20.3 -180.0 -115.6 -136.3 138.5 160.2 103 ASN -170.6 3.8 178.7 55.7 9.1 104 ARG -128.6 90.7 -177.8 56.9 155.7 109.0 169.9 105 PHE -81.6 96.1 -179.8 -62.8 -51.6 106 ASP -135.3 20.0 -176.8 44.7 20.6 107 ASP -78.4 -158.0 178.3 -33.0 -47.1 108 VAL -95.4 -45.5 180.0 169.6 109 THR -57.3 -37.7 -179.5 -50.7 110 THR -81.8 -39.5 178.8 76.3 111 ASP -66.3 -26.1 179.5 -175.0 19.9 112 GLN -79.7 -46.7 179.0 -118.3 -83.0 -93.9 113 PHE -55.0 -39.6 -178.9 162.1 70.8 114 VAL -73.8 -46.5 -179.9 168.5 115 LEU -62.7 -26.3 177.0 -171.2 68.5 116 ASN -73.6 -35.4 178.6 -121.8 68.8 117 VAL -71.9 -43.8 -179.3 173.5 118 ILE -59.7 -45.3 -178.9 -56.1 -168.9 119 LYS -79.0 -22.7 176.6 -148.3 53.7 -146.8 -59.0 120 GLU -81.0 -10.0 -178.9 -62.0 -178.3 -3.2 121 ASN -130.8 24.6 -179.3 -70.1 -80.1 122 VAL -47.5 -46.6 179.6 158.7 123 GLN -54.8 -37.1 -178.6 -69.9 -166.6 8.0 124 THR -70.8 -21.3 178.6 48.0 125 PHE -64.5 -17.4 -178.5 -74.6 97.9 126 SER -106.2 -6.0 -178.0 -63.3 127 THR -74.9 173.6 179.5 70.2 128 GLY 128.0 -153.8 -178.0 129 GLN -108.1 -3.5 178.8 -172.7 -168.9 -70.3 130 SER -120.8 -168.4 -178.1 69.6 131 GLU -102.0 142.8 -178.9 -66.3 170.3 -9.7 132 ALA -77.4 113.9 179.4 133 PRO -71.3 -179.7 179.1 -10.3 28.9 134 GLU -90.8 129.4 179.7 -57.6 140.9 -35.9 135 ALA -46.8 -23.8 -179.7 136 THR -69.8 -35.5 -179.7 62.6 137 ALA -77.9 148.6 -179.5 138 ASP -82.9 161.8 -177.0 -45.4 -47.5 139 THR -118.7 -26.0 -178.7 165.6 140 ASN 72.7 -6.2 179.2 -61.6 -51.5 141 LEU -106.9 150.2 -175.7 -61.1 -176.1 142 HIS -138.7 155.9 178.8 -166.3 40.6 143 TYR -113.7 137.2 177.8 -81.9 111.8 144 ILE -145.1 164.7 -173.8 56.3 177.0 145 THR -135.9 151.9 -180.0 -48.3 146 TYR -124.7 130.2 175.6 -67.5 103.9 147 VAL -141.0 156.9 177.3 -67.7 148 GLU -107.4 111.7 179.3 -179.3 177.4 -1.8 149 GLU -128.0 125.8 179.3 -153.4 78.6 -28.0 150 ASN 52.6 43.0 -178.6 -59.6 -63.1 151 GLY 62.6 15.5 177.6 152 GLY -108.2 155.9 177.4 153 ILE -117.9 128.1 -177.9 -76.5 167.8 154 PHE -127.5 151.0 176.7 -54.1 75.6 155 GLU -112.2 127.4 -178.4 177.1 171.5 90.5 156 LEU -116.9 119.9 -179.8 -50.0 163.6 157 ASP -128.3 123.5 -179.8 -166.0 149.2 158 GLY -64.0 -23.8 180.0 159 ARG -90.2 -9.1 179.1 -73.5 -78.7 58.8 -150.7 160 ASN -83.0 97.3 -178.4 -172.2 -60.2 161 LEU -51.5 -31.4 -180.0 -81.5 -100.5 162 SER -70.4 -5.3 179.8 -17.8 163 GLY 92.4 -160.9 179.9 164 PRO -62.4 150.4 179.3 27.5 -38.7 165 LEU -111.9 124.9 -179.2 -61.6 -168.7 166 TYR -83.2 132.9 179.1 -178.6 47.8 167 LEU -106.1 -8.9 -178.9 -60.9 175.1 168 GLY 126.3 -177.1 -177.3 169 LYS -76.4 153.6 -179.9 -54.5 -164.5 -171.6 173.8 170 SER -77.8 169.8 177.6 -26.3 171 ASP -114.6 108.0 179.9 172.4 -3.1 172 PRO -61.9 -7.4 176.5 -37.1 49.4 173 THR -77.8 -6.4 -178.6 59.7 174 ALA -84.2 115.5 177.6 175 THR -64.4 -35.9 178.9 58.6 176 ASP -153.5 -168.5 -177.4 57.6 48.0 177 LEU -67.7 -24.8 -179.2 -137.2 48.4 178 ILE -70.0 -27.4 180.0 -64.7 -161.1 179 GLU -92.4 24.2 178.8 -87.7 153.2 21.8 180 GLN -107.4 110.1 178.5 -59.8 -79.7 -17.4 181 GLU -53.7 -40.1 -179.1 -96.0 -79.8 -56.5 182 LEU -62.0 -27.0 179.0 -66.6 173.5 183 VAL -80.5 -51.1 179.0 174.2 184 ARG -53.1 -43.6 179.7 -63.1 -174.7 150.1 143.1 185 VAL -66.3 -48.4 -179.1 153.8 186 ARG -64.2 -37.2 177.9 173.7 86.3 169.3 -171.8 187 VAL -67.8 -50.1 -178.8 164.5 188 ALA -51.7 -35.3 178.8 189 SER -68.5 -26.4 178.7 79.6 190 TYR -74.0 -46.0 179.5 -73.8 124.9 191 MET -56.9 -36.5 -178.1 -57.6 -178.3 150.9 192 GLU -65.0 -35.0 176.1 -171.5 38.4 -119.4 193 ASN -70.6 -20.8 178.5 -48.8 137.6 194 ALA -87.3 -26.4 179.3 195 ASN -76.0 -27.7 178.5 -90.4 -12.9 196 GLU -78.3 -36.6 -177.5 -66.1 176.7 -16.7 197 GLU -89.8 3.4 -178.2 -68.4 -174.5 -20.4 198 ASP 58.2 18.6 176.5 -81.4 -15.4 199 VAL -86.1 130.4 178.9 160.4 200 LEU -110.7 11.0 -176.5 -72.1 176.0 201 ASN -76.9 84.6 -177.6 -65.9 -48.3 202 PHE -148.8 137.9 177.4 -99.8 84.9 203 ALA -146.2 148.9 177.2 204 MET -136.8 145.4 175.9 -75.9 176.7 79.9 205 LEU -130.8 141.6 175.3 -55.6 155.9 206 GLY -115.5 145.4 177.6 207 LEU -99.0 112.4 179.9 176.5 66.8 208 GLY -149.7 -176.4 179.7 209 PRO -60.1 153.9 -179.7 20.2 -39.2 210 ASN -86.9 119.7 0.0 -136.7 -20.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 97.828 24.680 -2.890 2 VAL 97.510 23.748 0.774 3 VAL 95.494 21.164 2.715 4 PRO 92.153 22.759 3.839 5 ILE 92.293 23.525 7.525 6 GLU 89.934 21.754 9.865 7 SER 87.528 23.868 11.959 8 ASN 89.386 22.799 15.078 9 PRO 90.065 25.299 17.863 10 GLU 93.438 23.644 18.738 11 VAL 94.721 23.934 15.173 12 PHE 93.559 27.569 14.799 13 THR 95.118 28.374 18.167 14 ASN 98.401 26.650 17.198 15 PHE 98.760 28.579 13.930 16 ALA 97.744 31.831 15.660 17 HIS 100.305 31.429 18.445 18 LYS 103.037 30.731 15.904 19 LEU 102.125 33.934 14.068 20 GLY 102.206 36.032 17.221 21 LEU 98.890 35.717 19.056 22 LYS 99.667 36.134 22.774 23 ASN 99.350 33.002 24.875 24 GLU 96.576 34.531 27.012 25 TRP 94.273 34.258 23.964 26 ALA 92.901 31.318 21.916 27 TYR 90.225 30.131 19.515 28 PHE 87.238 28.193 20.857 29 ASP 84.160 26.379 19.602 30 ILE 80.883 28.272 19.142 31 TYR 77.943 25.840 19.081 32 SER 75.099 28.156 19.800 33 LEU 74.367 31.651 18.750 34 THR 71.439 33.084 20.634 35 GLU 71.382 30.844 23.583 36 PRO 71.957 31.951 27.236 37 GLU 73.430 28.996 29.086 38 LEU 75.803 28.013 26.327 39 LEU 77.191 31.604 26.447 40 ALA 78.303 31.319 30.083 41 PHE 80.773 28.630 28.955 42 LEU 82.272 30.730 26.099 43 PRO 85.190 33.043 27.046 44 ARG 84.489 36.804 26.694 45 PRO 85.285 39.218 25.108 46 VAL 85.033 37.443 21.756 47 LYS 87.288 39.508 19.501 48 ALA 86.818 37.785 16.151 49 ILE 84.501 35.123 14.824 50 VAL 85.402 32.725 12.055 51 LEU 82.640 31.009 10.102 52 LEU 82.983 27.915 7.942 53 PHE 80.081 27.322 5.507 54 PRO 79.350 26.412 1.846 55 VAL 90.446 47.541 8.701 56 ILE 93.037 45.153 7.373 57 TRP 92.072 42.919 4.480 58 PHE 94.219 40.408 2.580 59 LYS 93.541 39.092 -0.882 60 GLN 93.687 35.280 -0.946 61 SER 96.388 34.035 -3.336 62 VAL 96.906 30.413 -2.319 63 LYS 94.408 27.570 -2.971 64 ASN 92.702 26.124 0.125 65 ALA 94.442 28.661 2.333 66 CYS 91.194 30.492 3.351 67 GLY 91.493 29.271 6.942 68 LEU 94.962 30.904 7.290 69 TYR 93.657 34.149 5.790 70 ALA 90.801 33.983 8.345 71 ILE 93.394 33.788 11.112 72 LEU 95.311 36.684 9.471 73 HIS 92.027 38.752 9.376 74 SER 91.193 37.888 12.979 75 LEU 94.700 38.749 14.237 76 SER 95.543 41.711 12.022 77 ASN 92.462 43.625 13.171 78 ASN 93.273 42.783 16.791 79 GLN 96.947 43.930 16.889 80 SER 96.778 44.525 20.643 81 LEU 96.610 40.758 21.133 82 LEU 99.897 40.186 19.219 83 GLU 103.325 39.709 20.820 84 PRO 105.449 42.802 20.140 85 GLY 108.265 41.522 17.904 86 SER 106.405 38.363 16.659 87 ASP 106.283 37.613 12.953 88 LEU 102.844 39.092 12.106 89 ASP 103.352 42.156 14.275 90 ASN 106.603 42.917 12.418 91 PHE 104.925 42.406 9.086 92 LEU 102.040 44.713 9.969 93 LYS 104.203 47.547 11.313 94 SER 106.593 47.256 8.366 95 GLN 103.877 48.135 5.836 96 SER 102.691 50.966 8.070 97 ASP 106.222 52.450 8.256 98 THR 106.722 52.231 4.500 99 SER 102.976 52.952 3.893 100 SER 102.753 50.291 1.138 101 SER 99.116 49.158 1.491 102 LYS 97.645 50.857 4.594 103 ASN 94.951 48.159 4.723 104 ARG 94.578 46.246 1.438 105 PHE 97.340 43.653 1.180 106 ASP 97.684 42.322 -2.395 107 ASP 101.369 43.072 -2.928 108 VAL 104.633 41.287 -3.372 109 THR 105.532 41.962 0.265 110 THR 102.340 40.202 1.379 111 ASP 102.299 37.166 -0.942 112 GLN 105.906 36.411 0.184 113 PHE 105.232 36.917 3.887 114 VAL 102.365 34.478 3.531 115 LEU 104.153 31.869 1.426 116 ASN 106.796 32.063 4.110 117 VAL 104.214 31.429 6.812 118 ILE 102.725 28.674 4.696 119 LYS 106.016 26.919 4.159 120 GLU 107.253 27.289 7.746 121 ASN 104.013 25.617 8.966 122 VAL 103.005 22.962 6.380 123 GLN 102.565 20.117 8.920 124 THR 99.866 21.886 10.957 125 PHE 97.620 22.250 7.884 126 SER 97.017 18.495 8.137 127 THR 96.443 18.142 11.912 128 GLY 93.199 17.636 13.794 129 GLN 90.367 15.168 14.324 130 SER 89.621 14.176 10.625 131 GLU 91.523 12.908 7.559 132 ALA 93.604 15.165 5.296 133 PRO 92.230 15.560 1.759 134 GLU 94.642 16.380 -1.037 135 ALA 95.408 20.084 -1.331 136 THR 94.659 19.539 -5.037 137 ALA 90.992 18.711 -4.357 138 ASP 88.184 21.228 -3.798 139 THR 86.169 21.512 -0.640 140 ASN 82.957 23.516 -1.330 141 LEU 83.447 24.977 2.186 142 HIS 84.755 28.442 2.923 143 TYR 86.178 30.525 5.837 144 ILE 85.235 34.190 6.514 145 THR 85.744 36.420 9.527 146 TYR 83.894 39.059 11.487 147 VAL 85.589 41.821 13.427 148 GLU 84.592 45.099 15.125 149 GLU 86.938 47.869 13.969 150 ASN 86.434 51.562 14.774 151 GLY 82.877 50.825 15.799 152 GLY 82.254 49.450 12.313 153 ILE 81.353 45.799 11.729 154 PHE 82.994 43.930 8.872 155 GLU 82.850 40.590 7.148 156 LEU 86.269 39.679 5.677 157 ASP 86.618 37.293 2.810 158 GLY 89.950 36.787 1.032 159 ARG 88.018 35.861 -2.121 160 ASN 85.805 38.930 -2.155 161 LEU 87.714 40.954 -4.735 162 SER 85.841 44.121 -3.714 163 GLY 87.632 43.885 -0.357 164 PRO 86.176 43.980 3.168 165 LEU 82.353 44.311 3.491 166 TYR 80.925 46.857 5.881 167 LEU 77.825 45.604 7.639 168 GLY 77.076 48.811 9.574 169 LYS 77.788 50.373 12.989 170 SER 78.404 48.493 16.233 171 ASP 76.125 48.479 19.243 172 PRO 77.986 49.786 22.325 173 THR 75.739 47.861 24.752 174 ALA 77.807 44.930 23.412 175 THR 80.562 43.564 25.653 176 ASP 81.685 41.736 22.534 177 LEU 81.104 40.435 19.021 178 ILE 78.697 37.693 20.058 179 GLU 76.343 40.424 21.238 180 GLN 76.322 42.191 17.878 181 GLU 72.984 41.828 16.148 182 LEU 74.570 42.730 12.825 183 VAL 76.818 39.640 13.011 184 ARG 74.108 37.236 14.230 185 VAL 71.773 38.431 11.500 186 ARG 74.364 38.184 8.739 187 VAL 75.392 34.693 9.980 188 ALA 71.777 33.638 10.431 189 SER 71.125 34.474 6.803 190 TYR 73.782 32.013 5.630 191 MET 72.294 29.239 7.794 192 GLU 68.804 29.848 6.324 193 ASN 70.095 29.058 2.832 194 ALA 71.479 25.915 4.557 195 ASN 68.184 25.028 6.337 196 GLU 66.426 25.000 2.987 197 GLU 69.186 22.853 1.434 198 ASP 69.525 20.220 4.183 199 VAL 73.245 21.058 4.429 200 LEU 74.547 20.848 8.021 201 ASN 78.078 21.938 7.091 202 PHE 78.638 24.830 9.433 203 ALA 81.198 25.689 12.044 204 MET 82.109 28.770 14.042 205 LEU 85.138 29.706 16.144 206 GLY 85.623 32.605 18.503 207 LEU 88.913 34.295 19.471 208 GLY 88.766 35.042 23.176 209 PRO 90.791 34.571 26.394 210 ASN 92.485 31.289 27.326 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/S S S S H H H 10 H H H H H H H H H H 20 C C C C C S S S S S 30 S S S S S S/H H H H H 40 3 3/S S S/P S/S S S S/S S S 50 S S S S/X X/S S S S S S 60 S/S S S S H H H H H H 70 H H H H H H H H H C 80 S S S S C H H H H H 90 H H H H H H H H H C 100 T T T T C C H H H H 110 H H H H H H H H H H 120 H H/H H H H 3 3 C S S 130 S S S S C S S S S S/S 140 S S S S S S S T T T 150 T/S S S S S S S S C T 160 T T T/S S S S S S/S S S 170 S S C C C T T T T H 180 H H H H H H H H H H 190 H H H H H H H H C S 200 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 S h H H 10 H H H H H H H H H h 20 B t T e E E E E E E 30 S S t g G G G g 40 t S S S E E E 50 E E E E E e 60 t T T h H H H H H 70 H H H H H H h g G G 80 G B t T T h H H H H 90 H H H H H H H h T t 100 S e E E h H H H 110 H H H H H H H H H H 120 h G G G G G g S S S 130 t T T t S 140 E E E E E E E E T 150 e E E E E E t T T t 160 T T t E E E E E e 170 t T T t S g G G G h 180 H H H H H H H H H H 190 H H H H H H h T t 200 E E E E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 49.9 68.8 61.7 2 VAL 108.4 91.3 33.9 3 VAL 90.5 76.2 54.3 4 PRO 105.9 85.1 57.5 5 ILE 143.1 99.7 44.2 6 GLU 101.8 73.5 68.0 7 SER 64.3 76.9 41.6 8 ASN 96.3 79.6 44.5 9 PRO 94.3 75.8 64.0 10 GLU 18.0 13.0 81.9 11 VAL 112.2 94.5 56.8 12 PHE 166.8 100.0 33.1 13 THR 93.7 87.6 58.6 14 ASN 51.3 42.4 66.4 15 PHE 165.6 99.3 35.4 16 ALA 72.6 100.0 36.5 17 HIS 117.6 78.3 69.8 18 LYS 78.9 45.5 75.3 19 LEU 143.2 96.9 34.4 20 GLY 31.3 89.9 59.6 21 LEU 147.8 100.0 35.2 22 LYS 118.8 68.5 72.5 23 ASN 21.8 18.0 83.0 24 GLU 36.2 26.2 69.7 25 TRP 166.6 81.3 41.4 26 ALA 62.0 85.4 60.3 27 TYR 181.0 100.0 33.9 28 PHE 142.4 85.4 46.2 29 ASP 44.9 40.6 61.4 30 ILE 143.0 99.7 35.5 31 TYR 68.8 38.0 65.6 32 SER 53.7 64.3 56.0 33 LEU 138.1 93.4 36.0 34 THR 28.9 27.1 76.5 35 GLU 63.3 45.7 64.2 36 PRO 37.5 30.1 77.5 37 GLU 25.4 18.3 69.8 38 LEU 93.7 63.4 58.6 39 LEU 125.4 84.9 65.7 40 ALA 14.2 19.6 84.3 41 PHE 41.1 24.6 85.0 42 LEU 136.2 92.2 43.8 43 PRO 81.4 65.4 56.8 44 ARG 155.5 74.4 64.7 45 PRO 79.2 63.6 58.0 46 VAL 118.8 100.0 41.4 47 LYS 97.7 56.3 59.5 48 ALA 72.6 100.0 44.5 49 ILE 143.0 99.7 29.3 50 VAL 118.4 99.6 43.3 51 LEU 147.8 100.0 30.8 52 LEU 126.8 85.8 45.5 53 PHE 143.4 86.0 37.2 54 PRO 89.1 71.6 46.7 55 VAL 99.0 83.3 48.6 56 ILE 124.9 87.1 53.5 57 TRP 194.1 94.7 48.2 58 PHE 165.3 99.1 31.7 59 LYS 130.6 75.3 54.7 60 GLN 131.5 88.5 50.1 61 SER 46.7 55.8 70.4 62 VAL 101.3 85.3 52.8 63 LYS 34.9 20.1 82.8 64 ASN 106.2 87.8 56.8 65 ALA 72.6 100.0 41.1 66 CYS 86.6 87.3 59.6 67 GLY 34.8 100.0 34.8 68 LEU 147.7 100.0 23.4 69 TYR 175.2 96.8 44.1 70 ALA 70.8 97.6 55.9 71 ILE 143.5 100.0 33.9 72 LEU 147.7 99.9 26.0 73 HIS 148.5 98.9 49.2 74 SER 83.6 100.0 42.0 75 LEU 147.6 99.9 33.9 76 SER 83.6 100.0 34.3 77 ASN 120.6 99.7 50.5 78 ASN 98.0 81.0 52.9 79 GLN 89.0 59.9 59.1 80 SER 0.0 0.0 80.8 81 LEU 133.2 90.1 42.0 82 LEU 147.6 99.9 49.3 83 GLU 63.9 46.1 67.5 84 PRO 34.7 27.9 87.8 85 GLY 5.8 16.7 84.0 86 SER 63.1 75.5 64.0 87 ASP 34.1 30.9 78.8 88 LEU 147.8 100.0 30.7 89 ASP 98.9 89.5 55.4 90 ASN 40.6 33.6 80.4 91 PHE 152.8 91.6 33.5 92 LEU 146.3 99.0 44.2 93 LYS 53.9 31.1 86.5 94 SER 36.9 44.1 70.3 95 GLN 144.6 97.3 56.3 96 SER 29.1 34.8 73.9 97 ASP 19.3 17.5 76.0 98 THR 26.3 24.6 80.4 99 SER 25.3 30.2 82.3 100 SER 50.5 60.4 78.3 101 SER 68.4 81.9 73.4 102 LYS 21.2 12.2 85.7 103 ASN 55.5 45.9 69.1 104 ARG 44.5 21.3 81.4 105 PHE 161.8 97.0 41.1 106 ASP 57.6 52.2 67.7 107 ASP 76.8 69.5 70.3 108 VAL 0.0 0.0 80.1 109 THR 42.0 39.3 66.5 110 THR 101.4 94.9 48.5 111 ASP 47.4 42.9 72.5 112 GLN 42.2 28.4 80.9 113 PHE 138.3 82.9 36.3 114 VAL 116.0 97.7 35.0 115 LEU 56.2 38.0 69.3 116 ASN 47.6 39.4 79.9 117 VAL 108.0 90.9 40.0 118 ILE 137.7 96.0 26.1 119 LYS 42.7 24.6 75.0 120 GLU 44.2 31.9 88.7 121 ASN 99.0 81.9 55.9 122 VAL 56.2 47.3 58.0 123 GLN 0.0 0.0 85.6 124 THR 90.0 84.2 56.4 125 PHE 166.0 99.5 37.7 126 SER 45.3 54.2 64.0 127 THR 48.0 44.9 68.5 128 GLY 30.3 87.0 71.2 129 GLN 4.2 2.8 90.9 130 SER 20.9 25.0 80.8 131 GLU 0.0 0.0 90.7 132 ALA 48.7 67.1 62.4 133 PRO 57.1 45.9 66.0 134 GLU 17.5 12.6 83.1 135 ALA 57.3 79.0 59.7 136 THR 15.4 14.4 74.7 137 ALA 30.7 42.2 84.7 138 ASP 12.3 11.1 84.9 139 THR 71.8 67.2 66.1 140 ASN 0.0 0.0 84.5 141 LEU 103.1 69.8 57.7 142 HIS 113.1 75.3 53.5 143 TYR 175.2 96.8 36.7 144 ILE 141.3 98.4 48.6 145 THR 106.9 100.0 44.3 146 TYR 181.0 100.0 29.3 147 VAL 118.2 99.5 46.5 148 GLU 87.9 63.4 64.2 149 GLU 103.2 74.5 67.1 150 ASN 13.1 10.8 80.8 151 GLY 9.9 28.5 76.0 152 GLY 29.3 84.1 64.4 153 ILE 143.5 100.0 39.9 154 PHE 140.1 84.0 43.5 155 GLU 132.4 95.6 44.8 156 LEU 147.8 100.0 43.0 157 ASP 87.4 79.1 54.0 158 GLY 34.8 100.0 61.4 159 ARG 100.2 48.0 74.9 160 ASN 77.8 64.4 65.2 161 LEU 55.1 37.3 84.1 162 SER 10.7 12.8 84.0 163 GLY 29.5 84.8 56.0 164 PRO 90.4 72.6 50.1 165 LEU 96.1 65.0 78.4 166 TYR 85.4 47.2 62.3 167 LEU 130.1 88.0 50.1 168 GLY 17.1 49.1 58.2 169 LYS 17.0 9.8 89.9 170 SER 80.1 95.8 55.4 171 ASP 50.6 45.8 69.6 172 PRO 19.1 15.3 87.8 173 THR 5.8 5.5 89.1 174 ALA 71.7 98.8 75.1 175 THR 23.5 22.0 84.4 176 ASP 106.8 96.6 57.6 177 LEU 146.2 98.9 46.6 178 ILE 142.6 99.4 35.5 179 GLU 88.6 63.9 75.4 180 GLN 146.8 98.8 53.6 181 GLU 30.9 22.3 73.6 182 LEU 86.7 58.6 63.8 183 VAL 117.8 99.1 31.0 184 ARG 163.5 78.3 49.5 185 VAL 31.7 26.7 74.5 186 ARG 134.0 64.1 60.9 187 VAL 116.8 98.3 29.8 188 ALA 25.1 34.6 67.3 189 SER 28.2 33.7 72.6 190 TYR 138.3 76.4 61.0 191 MET 88.6 55.6 54.8 192 GLU 50.6 36.5 78.4 193 ASN 35.9 29.7 80.6 194 ALA 64.5 88.8 55.2 195 ASN 32.4 26.8 82.4 196 GLU 38.0 27.4 83.8 197 GLU 34.9 25.2 76.7 198 ASP 1.2 1.1 90.7 199 VAL 80.0 67.3 62.6 200 LEU 3.2 2.1 87.8 201 ASN 39.3 32.5 59.8 202 PHE 145.9 87.5 42.9 203 ALA 46.4 63.9 62.7 204 MET 151.1 94.8 31.9 205 LEU 145.9 98.7 39.4 206 GLY 34.8 100.0 40.5 207 LEU 147.8 100.0 34.0 208 GLY 34.8 100.0 47.0 209 PRO 83.6 67.2 58.8 210 ASN 59.7 49.4 69.6