Protein Data Bank File : 1b12b Title : HYDROLASE 24-NOV-99 1B12 Number of Amino Acid Residues : 211 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PHE ILE TYR GLU PRO PHE GLN ILE PRO SER 10 GLY SER MET MET PRO THR LEU LEU ILE GLY 20 ASP PHE ILE LEU VAL GLU LYS PHE GLY HIS 30 PRO LYS ARG GLY ASP ILE VAL VAL PHE LYS 40 TYR PRO GLU ASP PRO LYS LEU ASP TYR ILE 50 LYS ARG ALA VAL GLY LEU PRO GLY ASP LYS 60 VAL THR TYR ASP PRO VAL SER LYS GLU LEU 70 THR ILE GLN PRO GLY CYS CYS GLU ASN ALA 80 LEU PRO VAL THR TYR SER ASN VAL GLU PRO 90 SER ASP PHE VAL GLN THR PHE SER ARG GLU 100 ALA THR SER GLY PHE PHE GLU VAL PRO LYS 110 ASN GLU THR LYS GLU ASN GLY ILE ARG LEU 120 SER GLU ARG LYS GLU THR LEU GLY ASP VAL 130 THR HIS ARG ILE LEU THR VAL PRO ILE ALA 140 GLN ASP GLN VAL GLY MET TYR TYR GLN GLN 150 PRO GLY GLN GLN LEU ALA THR TRP ILE VAL 160 PRO PRO GLY GLN TYR PHE MET MET GLY ASP 170 ASN ARG ASP ASN SER ALA ASP SER ARG TYR 180 TRP GLY PHE VAL PRO GLU ALA ASN LEU VAL 190 GLY ARG ALA THR ALA ILE TRP MET SER PHE 200 ASP LEU ARG LEU SER ARG ILE GLY GLY ILE 210 HIS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PHE 0.0 128.8 178.4 -60.9 -88.2 2 ILE -142.2 123.4 177.5 -67.8 -174.4 3 TYR -81.8 97.9 -179.8 -71.9 68.2 4 GLU -54.0 126.4 -179.6 -60.8 -51.4 -32.9 5 PRO -82.1 0.6 180.0 35.9 -43.1 6 PHE -119.7 147.1 179.9 35.8 82.7 7 GLN -74.9 153.9 176.2 -67.1 175.4 -60.4 8 ILE -68.0 123.9 -179.5 -70.4 -63.7 9 PRO -83.9 -22.5 -178.5 36.5 -44.7 10 SER -130.7 162.6 -176.7 -53.8 11 GLY -97.1 23.6 -177.9 12 SER -70.6 -9.1 177.4 75.7 13 MET -110.3 15.6 178.8 -84.7 -61.6 -71.8 14 MET -66.4 151.1 -1.7 -69.2 168.7 66.6 15 PRO -88.0 0.8 -178.9 42.1 -40.5 16 THR -60.8 -45.4 176.6 -51.5 17 LEU -127.4 132.9 178.9 -73.2 -179.7 18 LEU -113.2 155.9 176.6 -54.8 -173.2 19 ILE -59.7 128.1 179.6 -68.4 162.5 20 GLY 106.0 -13.7 177.4 21 ASP -73.9 149.1 175.7 -79.4 -17.1 22 PHE -116.6 127.8 -178.3 -71.8 82.4 23 ILE -111.5 159.3 178.8 63.2 173.8 24 LEU -100.8 124.7 -179.3 -173.2 66.5 25 VAL -116.5 130.8 179.1 176.9 26 GLU -106.0 108.7 -178.6 171.4 172.7 -63.0 27 LYS -64.1 151.7 -179.4 -68.8 -173.3 61.2 64.5 28 PHE -81.9 175.7 -13.9 -71.8 -63.6 29 GLY 70.0 -169.4 179.8 30 HIS -132.3 145.3 179.8 -69.8 -62.5 31 PRO -69.3 152.1 178.8 27.4 -41.6 32 LYS -99.4 160.0 178.8 -49.8 176.0 97.9 76.6 33 ARG -60.2 136.6 -179.8 -98.2 -156.7 -127.8 75.1 34 GLY 91.5 -8.6 179.4 35 ASP -64.8 144.8 176.9 -88.6 -0.3 36 ILE -92.1 112.9 -174.7 -61.2 175.1 37 VAL -112.4 137.4 177.0 -179.1 38 VAL -98.0 130.8 -179.4 -179.8 39 PHE -152.6 161.8 178.9 62.3 -82.4 40 LYS -79.4 127.6 179.3 -46.3 -100.0 60.2 175.5 41 TYR -59.7 113.8 -179.7 -179.1 39.0 42 PRO -51.6 -33.9 179.6 20.2 -38.2 43 GLU -75.3 -26.4 -179.9 -75.6 48.3 55.8 44 ASP -147.3 76.3 -179.8 -163.9 -49.0 45 PRO -46.4 -10.1 179.9 -31.7 43.9 46 LYS -78.1 -35.6 -178.6 -109.2 -66.6 -175.4 -179.5 47 LEU -87.6 133.5 178.2 -51.5 171.8 48 ASP -90.6 140.3 178.4 -80.9 -53.3 49 TYR -121.9 157.5 177.9 -96.7 41.1 50 ILE -133.5 123.3 -179.5 -65.2 176.9 51 LYS -147.4 174.2 178.3 -61.9 -68.3 -178.4 178.6 52 ARG -100.1 129.8 -179.5 178.6 176.0 -54.7 -85.5 53 ALA -77.9 94.3 -179.9 54 VAL -89.7 -23.2 179.5 -55.3 55 GLY -121.0 126.4 179.1 56 LEU -102.6 163.1 -179.9 -61.0 179.4 57 PRO -47.3 133.9 178.9 -29.6 42.3 58 GLY 91.1 -17.8 -179.0 59 ASP -69.5 140.3 174.2 -79.8 -5.6 60 LYS -102.8 112.5 -178.0 179.3 173.1 174.0 -179.6 61 VAL -107.4 126.4 177.4 175.0 62 THR -122.7 130.6 177.7 -62.5 63 TYR -112.5 126.8 177.9 -172.3 61.9 64 ASP -95.3 106.8 -179.3 170.1 6.5 65 PRO -64.7 -25.0 -179.4 34.3 -44.0 66 VAL -73.2 -56.9 -179.6 -179.8 67 SER -85.5 -10.2 -179.1 69.9 68 LYS 59.1 46.8 179.3 -63.3 171.9 -174.4 -179.2 69 GLU -124.9 146.4 178.8 -62.3 179.1 12.7 70 LEU -98.2 149.9 176.0 -74.7 156.6 71 THR -128.8 132.0 -177.8 -73.7 72 ILE -133.1 128.3 178.3 -60.8 -168.4 73 GLN -118.2 105.9 -179.7 -81.8 109.4 -166.6 74 PRO -66.3 161.8 178.6 -19.1 37.5 75 GLY 45.3 55.0 178.2 76 CYS -107.8 121.5 -5.2 -78.8 77 CYS 136.5 101.4 -177.0 79.5 78 GLU -116.0 0.6 -178.6 37.8 -159.2 44.9 79 ASN -101.8 157.0 -179.4 -54.6 -25.3 80 ALA -118.5 150.5 177.4 81 LEU -92.0 131.6 180.0 -170.7 -73.6 82 PRO -65.2 121.6 177.6 -17.5 36.8 83 VAL -129.3 118.0 -179.2 171.7 84 THR -129.9 154.5 -176.7 54.9 85 TYR -127.2 141.9 177.4 -67.5 -87.9 86 SER -85.7 173.6 177.9 61.4 87 ASN -63.6 148.9 178.6 -79.0 -51.2 88 VAL -76.5 141.4 -179.8 179.7 89 GLU -149.8 161.6 179.3 63.9 177.0 -53.8 90 PRO -61.3 140.5 178.4 -32.9 40.8 91 SER -96.2 -177.4 179.5 72.1 92 ASP -93.6 11.4 -178.0 -67.4 -49.5 93 PHE -121.7 143.3 178.4 -60.4 -80.5 94 VAL -121.6 134.1 179.4 171.5 95 GLN -105.6 130.2 -179.6 -176.8 167.8 6.0 96 THR -121.5 128.7 -177.7 -58.5 97 PHE -100.5 164.7 178.9 -58.3 79.7 98 SER -172.1 172.7 179.3 67.7 99 ARG 25.6 -171.3 128.5 -58.1 66.2 -104.1 17.4 100 GLU 8.1 112.8 179.9 -50.6 174.7 -3.5 101 ALA -73.3 141.8 -179.5 102 THR -153.4 176.1 -178.8 -168.9 103 SER -163.9 168.4 178.0 60.5 104 GLY -136.2 158.8 179.9 105 PHE -111.5 140.3 179.9 -61.6 -74.3 106 PHE -131.3 133.6 177.8 -58.0 -86.5 107 GLU -83.2 120.3 -178.6 -178.5 149.6 22.2 108 VAL -131.6 125.2 179.7 -172.2 109 PRO -50.1 142.1 -179.4 -34.8 45.2 110 LYS -60.7 -26.6 -178.9 -67.3 171.1 -176.8 174.9 111 ASN -85.2 4.1 178.4 56.9 -108.4 112 GLU -136.9 172.1 -178.3 46.4 -167.3 54.5 113 THR -127.1 163.2 177.4 65.5 114 LYS -112.3 135.6 -177.6 -179.7 171.9 179.2 -69.1 115 GLU -51.1 -52.1 -178.7 -175.6 56.3 40.3 116 ASN -119.6 132.6 178.8 -53.6 -53.9 117 GLY 138.3 -179.1 178.6 118 ILE -127.4 130.8 179.0 177.9 169.2 119 ARG -74.9 123.0 179.4 -172.0 172.3 -72.6 -78.9 120 LEU -73.2 152.2 177.1 -83.5 22.3 121 SER -95.9 163.3 178.7 -63.3 122 GLU -144.9 156.6 176.8 67.3 166.0 53.8 123 ARG -162.1 167.0 178.7 74.3 -165.8 -48.8 -170.8 124 LYS -96.0 140.5 177.6 -71.6 176.7 -173.9 177.7 125 GLU -120.4 125.3 178.6 175.2 -179.3 83.2 126 THR -112.0 113.4 178.9 -62.0 127 LEU -103.0 99.9 -178.1 -61.7 176.5 128 GLY 67.4 -105.6 -178.7 129 ASP -113.1 5.6 -179.4 63.3 -37.4 130 VAL -105.8 117.3 179.3 -173.8 131 THR -107.0 134.9 179.4 -63.2 132 HIS -154.4 172.8 178.8 67.9 94.7 133 ARG -101.1 160.6 174.1 -70.3 -175.6 -64.5 170.3 134 ILE -137.2 154.4 175.3 59.1 168.0 135 LEU -114.8 150.3 177.1 -58.6 -169.7 136 THR -138.6 149.5 179.1 55.9 137 VAL -96.6 114.1 -179.0 174.1 138 PRO -50.0 -35.3 -177.2 -28.5 42.3 139 ILE -93.1 -0.9 -177.5 59.6 171.6 140 ALA -104.2 150.7 177.3 141 GLN -148.7 130.2 178.9 -176.8 175.2 -75.8 142 ASP -52.9 144.4 175.5 -70.9 5.3 143 GLN -102.0 104.3 -176.0 -74.9 -179.2 -50.7 144 VAL -56.7 -24.2 179.0 -59.2 145 GLY -66.4 -13.8 179.6 146 MET -94.8 -6.5 -179.6 -56.2 -64.4 -72.8 147 TYR -72.0 164.7 171.8 -74.9 -8.4 148 TYR -79.5 122.1 -179.0 152.0 65.7 149 GLN -103.2 114.3 -179.1 168.6 161.5 34.8 150 GLN -69.8 127.5 -179.7 -172.2 179.9 40.4 151 PRO -46.1 128.6 179.8 -33.4 43.6 152 GLY 82.9 -7.7 179.3 153 GLN -107.6 153.0 178.6 -64.2 -58.9 -57.5 154 GLN -75.2 165.6 179.8 -132.9 52.4 60.8 155 LEU -61.5 143.5 178.5 -70.3 170.9 156 ALA 74.6 12.6 175.5 157 THR -129.6 132.9 -178.3 -70.2 158 TRP -139.2 136.9 178.1 -58.1 -91.0 159 ILE -102.3 119.3 -178.0 -51.1 -70.9 160 VAL -74.8 118.4 -179.8 -176.0 161 PRO -64.9 155.1 179.6 26.6 -38.3 162 PRO -59.2 146.2 179.9 28.5 -42.2 163 GLY 71.9 8.9 -179.9 164 GLN -133.2 169.4 -176.7 -61.3 -174.1 66.6 165 TYR -136.8 150.3 177.3 -59.4 86.5 166 PHE -102.9 117.1 -177.9 -165.3 83.2 167 MET -104.3 140.3 176.5 -61.2 -65.0 171.6 168 MET -142.3 143.5 179.3 -77.5 178.8 82.3 169 GLY -86.7 146.6 179.8 170 ASP -68.7 -23.6 178.4 -70.1 -7.2 171 ASN -90.5 77.3 -171.8 -164.2 -18.4 172 ARG -51.0 -30.4 177.9 -65.1 -75.9 173.2 76.9 173 ASP -101.2 4.5 179.7 -63.3 -53.1 174 ASN -131.7 49.7 -177.1 -66.5 -62.1 175 SER -145.3 122.6 177.8 176.8 176 ALA -95.6 95.0 -177.1 177 ASP -124.0 -157.5 -178.1 48.8 30.9 178 SER -54.5 -26.8 178.0 -59.8 179 ARG -56.1 -30.3 -176.7 -74.8 173.1 -82.4 -176.1 180 TYR -103.9 -32.8 179.8 -62.3 -78.2 181 TRP -121.3 15.3 177.0 41.3 -106.7 182 GLY 85.7 -162.1 -176.5 183 PHE -86.3 165.2 179.2 -40.2 -85.8 184 VAL -113.7 118.4 180.0 49.0 185 PRO -64.4 149.3 179.0 -24.6 41.2 186 GLU -53.2 -32.7 -179.3 163.6 68.7 39.9 187 ALA -69.1 -21.2 179.7 188 ASN -87.3 -6.7 -178.7 -74.0 53.0 189 LEU -70.3 139.5 -179.8 -59.4 176.4 190 VAL -113.2 -54.7 -179.9 176.0 191 GLY -175.7 -170.4 179.0 192 ARG -118.4 134.5 179.0 69.1 164.4 68.5 177.1 193 ALA -79.9 117.3 -178.2 194 THR -103.4 -19.9 -178.6 66.4 195 ALA -165.5 168.5 177.4 196 ILE -109.7 120.4 -179.4 -67.9 175.7 197 TRP -102.1 -10.7 179.0 63.1 -86.1 198 MET -163.6 155.9 178.7 -177.2 45.3 49.9 199 SER -153.5 121.2 -179.5 -171.3 200 PHE -120.7 132.3 -179.0 -177.1 60.2 201 ASP -110.5 -44.2 29.1 157.4 33.6 202 LEU -91.8 127.1 177.8 -70.8 -173.3 203 ARG -113.6 74.3 -175.2 -54.5 139.9 162.4 159.2 204 LEU -66.7 -22.4 179.9 -59.3 178.3 205 SER -66.9 -17.8 -179.3 68.0 206 ARG -82.1 -12.6 -179.3 -60.3 -173.1 57.4 73.1 207 ILE -69.1 127.1 -178.0 -64.6 177.0 208 GLY 148.0 -178.2 -179.4 209 GLY -68.6 155.4 177.8 210 ILE -130.5 166.8 178.3 55.4 -174.8 211 HIS -158.6 164.9 0.0 42.8 84.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PHE -13.504 37.349 38.496 2 ILE -14.329 38.250 34.918 3 TYR -15.809 36.110 32.183 4 GLU -13.857 37.597 29.264 5 PRO -16.293 38.565 26.461 6 PHE -13.788 38.136 23.651 7 GLN -12.403 34.974 22.120 8 ILE -8.760 34.019 22.314 9 PRO -7.525 35.270 18.909 10 SER -4.280 33.284 18.444 11 GLY -2.920 29.808 19.093 12 SER 0.305 30.458 20.975 13 MET -1.135 28.803 24.120 14 MET -2.386 25.610 22.409 15 PRO -3.473 23.094 23.379 16 THR -4.214 24.736 26.741 17 LEU -6.027 27.681 25.110 18 LEU -7.397 27.465 21.585 19 ILE -8.452 30.250 19.227 20 GLY -12.140 30.684 20.051 21 ASP -11.894 29.896 23.748 22 PHE -13.441 32.403 26.173 23 ILE -11.615 32.541 29.502 24 LEU -12.380 33.387 33.080 25 VAL -9.769 35.802 34.445 26 GLU -9.016 36.425 38.108 27 LYS -7.363 39.855 38.460 28 PHE -4.286 40.266 40.686 29 GLY -1.170 39.320 44.495 30 HIS 1.521 37.561 42.453 31 PRO 1.415 34.769 39.863 32 LYS 2.759 31.350 40.832 33 ARG 5.102 29.435 38.543 34 GLY 3.082 27.721 35.849 35 ASP 0.265 30.257 36.123 36 ILE -1.479 31.168 32.873 37 VAL -1.113 34.951 33.063 38 VAL -2.841 37.785 31.270 39 PHE -0.528 40.785 30.870 40 LYS 0.094 43.892 28.778 41 TYR 2.524 43.223 25.942 42 PRO 5.654 45.211 26.960 43 GLU 6.428 46.150 23.335 44 ASP 2.840 47.371 22.846 45 PRO 1.175 47.913 26.292 46 LYS -2.097 48.369 24.385 47 LEU -2.254 44.683 23.444 48 ASP -3.003 42.018 26.035 49 TYR -0.999 38.787 25.935 50 ILE -1.555 35.451 27.641 51 LYS 1.413 33.200 28.365 52 ARG 2.527 30.821 31.068 53 ALA 4.787 32.258 33.787 54 VAL 7.638 29.795 33.773 55 GLY 10.203 32.116 35.368 56 LEU 9.703 34.079 38.580 57 PRO 12.006 36.845 39.879 58 GLY 15.403 35.376 40.701 59 ASP 14.933 32.279 38.545 60 LYS 17.711 31.172 36.265 61 VAL 15.797 29.868 33.271 62 THR 17.485 27.818 30.575 63 TYR 15.734 26.648 27.406 64 ASP 17.254 23.817 25.401 65 PRO 16.119 24.524 21.790 66 VAL 17.044 21.060 20.651 67 SER 14.960 19.001 23.069 68 LYS 12.579 21.942 23.719 69 GLU 12.841 21.399 27.462 70 LEU 13.283 23.915 30.283 71 THR 15.760 23.733 33.167 72 ILE 15.001 26.107 36.064 73 GLN 17.135 27.118 39.058 74 PRO 15.164 29.168 41.662 75 GLY 16.686 31.926 43.787 76 CYS 19.684 32.765 41.599 77 CYS 21.876 29.265 44.046 78 GLU 22.589 25.553 44.007 79 ASN 19.085 24.134 43.809 80 ALA 16.963 22.976 40.917 81 LEU 13.244 23.088 40.343 82 PRO 12.019 19.603 39.440 83 VAL 11.040 19.849 35.748 84 THR 9.903 16.645 34.005 85 TYR 8.483 15.657 30.621 86 SER 6.264 12.809 29.449 87 ASN 6.914 10.993 26.182 88 VAL 6.294 12.896 22.972 89 GLU 3.164 11.755 21.117 90 PRO 0.940 12.900 18.211 91 SER -1.397 15.765 19.194 92 ASP -4.931 16.375 17.922 93 PHE -3.687 19.324 15.870 94 VAL -2.302 19.830 12.387 95 GLN -0.640 23.085 11.383 96 THR -0.969 24.158 7.739 97 PHE 1.136 26.910 6.234 98 SER 0.737 29.353 3.396 99 ARG 1.709 32.719 1.896 100 GLU 4.438 37.057 4.530 101 ALA 4.386 33.490 5.950 102 THR 1.324 32.378 7.934 103 SER -0.578 29.282 9.042 104 GLY -3.745 27.899 10.549 105 PHE -4.436 25.086 13.023 106 PHE -6.931 22.269 12.474 107 GLU -8.153 19.764 15.009 108 VAL -7.773 16.362 13.373 109 PRO -8.466 12.955 14.948 110 LYS -5.275 11.005 15.577 111 ASN -6.622 8.084 13.512 112 GLU -6.976 10.169 10.360 113 THR -4.933 12.613 8.356 114 LYS -5.287 16.014 6.736 115 GLU -3.875 16.093 3.221 116 ASN -1.647 19.114 3.775 117 GLY 0.031 20.231 6.965 118 ILE 2.131 18.817 9.773 119 ARG 0.754 17.050 12.810 120 LEU 2.129 18.746 15.915 121 SER 3.557 16.658 18.728 122 GLU 2.534 17.057 22.327 123 ARG 3.838 16.040 25.731 124 LYS 3.302 16.966 29.324 125 GLU 5.586 19.423 31.060 126 THR 5.710 19.471 34.844 127 LEU 7.245 22.658 36.257 128 GLY 7.640 21.881 39.913 129 ASP 4.085 20.904 40.816 130 VAL 2.238 22.257 37.783 131 THR 1.648 19.819 34.923 132 HIS 0.331 21.017 31.547 133 ARG 0.771 20.206 27.891 134 ILE 2.870 21.821 25.204 135 LEU 2.796 21.317 21.431 136 THR 5.901 21.259 19.294 137 VAL 6.412 21.381 15.533 138 PRO 8.680 18.385 14.686 139 ILE 10.646 20.125 11.907 140 ALA 11.241 23.422 13.724 141 GLN 13.975 24.521 16.067 142 ASP 14.405 27.966 17.659 143 GLN 17.286 29.960 16.174 144 VAL 19.008 31.143 19.336 145 GLY 20.586 34.009 17.401 146 MET 17.046 35.434 17.265 147 TYR 16.533 35.388 21.030 148 TYR 16.594 38.319 23.394 149 GLN 20.087 37.827 24.761 150 GLN 20.411 39.042 28.352 151 PRO 23.664 41.013 28.839 152 GLY 26.349 38.776 30.299 153 GLN 24.373 35.553 29.824 154 GLN 24.922 33.005 27.104 155 LEU 22.180 32.595 24.541 156 ALA 19.144 30.673 25.868 157 THR 19.781 31.354 29.581 158 TRP 17.977 34.182 31.443 159 ILE 18.108 35.349 35.025 160 VAL 14.713 36.770 35.849 161 PRO 15.125 40.278 37.300 162 PRO 13.322 41.235 40.491 163 GLY 9.781 42.410 39.801 164 GLN 9.660 40.722 36.397 165 TYR 8.647 37.382 34.851 166 PHE 9.741 35.028 32.099 167 MET 6.711 34.073 29.972 168 MET 6.374 31.219 27.480 169 GLY 3.575 29.916 25.285 170 ASP 2.444 26.290 25.427 171 ASN 2.459 26.106 21.605 172 ARG 6.222 26.235 21.943 173 ASP 7.304 26.670 18.331 174 ASN 4.424 29.074 17.571 175 SER 4.910 31.574 20.339 176 ALA 6.562 35.003 20.387 177 ASP 7.309 35.132 24.081 178 SER 10.043 36.169 26.537 179 ARG 12.608 34.132 24.622 180 TYR 12.333 36.827 21.991 181 TRP 11.348 40.065 23.759 182 GLY 12.524 39.710 27.339 183 PHE 10.730 39.934 30.659 184 VAL 7.349 41.215 31.756 185 PRO 7.277 43.781 34.619 186 GLU 5.032 43.266 37.656 187 ALA 3.238 46.438 36.539 188 ASN 2.100 44.865 33.226 189 LEU 0.311 42.010 34.971 190 VAL -3.467 41.847 34.653 191 GLY -4.586 38.511 36.041 192 ARG -4.537 34.719 35.849 193 ALA -6.630 32.669 33.429 194 THR -8.407 30.134 35.610 195 ALA -10.904 28.526 33.271 196 ILE -12.573 28.318 29.876 197 TRP -16.251 29.261 30.165 198 MET -17.185 28.985 26.515 199 SER -15.510 27.918 23.319 200 PHE -16.477 28.634 19.727 201 ASP -14.595 27.293 16.771 202 LEU -18.934 24.917 19.912 203 ARG -16.348 22.977 21.896 204 LEU -18.291 22.441 25.074 205 SER -15.911 19.780 26.325 206 ARG -13.362 22.557 26.823 207 ILE -15.505 24.375 29.394 208 GLY -13.953 23.994 32.828 209 GLY -10.861 24.862 34.819 210 ILE -7.472 25.122 33.161 211 HIS -3.939 25.084 34.526 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 S S T T/P T T/S S S S S 20 S S S S S S S SPX X/S S 30 S S S C S S S S S S 40 T T T T C S S S S S 50 S S C S S S S S S S 60 S S S S/T T T T S S S 70 S S S/T T T TPX X/C S S S 80 S S/S S S S S S/S S S S 90 S S/S S S S S S S S/X X/S 100 S S S/S S S S S S S/T T 110 T T/S S S S/S S S S/S S S 120 S S S S S S/T T T T/S S 130 S S S S S S S S S/S S 140 S S S/T T T T C C C T 150 T T T C C S S S S S 160 S/T T T T/S S S S S S S 170 T T T T/S S S S/T T T T/S 180 S S S C T T T T/S S S 190 S/S S S S S/S S S S T T 200 T/X X/T T T T T S S S S 210 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E e S S 10 t T T T T T t t T e 20 E E E E E E E e 30 t T T e E E E E E 40 e T T t T T e E E E 50 E E E E E t T T e E 60 E E E E T T T T E E 70 E E E S 80 e E E E e E E 90 E E E E E E E E 100 E E E E E E e t T 110 T t S S S E E E 120 E E E E E E E e T E 130 E E E E E E t T T t 140 g G G G g t 150 T T t t T e E E E e 160 t T e E E E E E S 170 B T T t h H H H 180 H h E E e T e E E 190 E E E E E E E E E e 200 g G G G g E E e 210 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PHE 45.1 27.1 78.5 2 ILE 62.4 43.5 70.8 3 TYR 64.0 35.4 60.8 4 GLU 116.6 84.1 42.4 5 PRO 45.3 36.4 67.0 6 PHE 45.9 27.5 73.3 7 GLN 93.3 62.8 59.2 8 ILE 128.5 89.6 46.0 9 PRO 29.9 24.0 77.3 10 SER 20.8 24.9 69.8 11 GLY 34.7 99.6 50.2 12 SER 62.1 74.3 68.8 13 MET 155.2 97.4 49.2 14 MET 155.5 97.6 31.4 15 PRO 123.6 99.3 47.9 16 THR 90.8 85.0 58.1 17 LEU 147.2 99.6 26.2 18 LEU 143.9 97.4 54.2 19 ILE 69.9 48.7 67.2 20 GLY 31.7 91.2 72.0 21 ASP 110.5 100.0 47.3 22 PHE 135.0 80.9 57.0 23 ILE 140.1 97.6 27.8 24 LEU 117.5 79.5 49.9 25 VAL 115.3 97.1 44.1 26 GLU 85.6 61.8 60.7 27 LYS 65.4 37.7 67.7 28 PHE 144.7 86.8 55.3 29 GLY 0.0 0.0 80.5 30 HIS 49.8 33.2 76.6 31 PRO 124.5 100.0 36.6 32 LYS 35.5 20.5 88.0 33 ARG 165.1 79.0 50.6 34 GLY 34.8 100.0 48.5 35 ASP 90.7 82.1 55.0 36 ILE 142.5 99.3 42.6 37 VAL 118.8 100.0 36.4 38 VAL 106.5 89.6 36.7 39 PHE 166.8 100.0 30.3 40 LYS 110.4 63.7 68.0 41 TYR 147.2 81.3 43.3 42 PRO 108.3 87.0 54.4 43 GLU 70.2 50.6 60.6 44 ASP 54.1 48.9 52.7 45 PRO 48.7 39.2 80.5 46 LYS 7.7 4.4 89.3 47 LEU 52.6 35.6 72.9 48 ASP 57.6 52.1 65.2 49 TYR 126.9 70.1 50.9 50 ILE 120.0 83.6 33.4 51 LYS 168.4 97.1 42.7 52 ARG 208.9 100.0 48.7 53 ALA 72.6 100.0 44.1 54 VAL 118.8 100.0 36.4 55 GLY 34.8 100.0 47.0 56 LEU 113.6 76.9 55.7 57 PRO 88.8 71.4 59.5 58 GLY 17.6 50.6 77.6 59 ASP 109.0 98.6 53.3 60 LYS 101.9 58.8 64.2 61 VAL 118.8 100.0 36.6 62 THR 67.9 63.5 64.5 63 TYR 180.9 100.0 43.7 64 ASP 53.7 48.6 64.0 65 PRO 103.1 82.8 53.1 66 VAL 25.8 21.8 82.4 67 SER 44.6 53.3 72.0 68 LYS 153.9 88.8 65.7 69 GLU 85.7 61.8 66.6 70 LEU 147.8 100.0 37.7 71 THR 39.3 36.7 72.6 72 ILE 143.5 100.0 40.3 73 GLN 105.3 70.9 53.7 74 PRO 94.6 76.0 64.7 75 GLY 0.0 0.0 77.5 76 CYS 92.6 93.3 42.6 77 CYS 66.0 66.6 67.4 78 GLU 1.7 1.2 90.5 79 ASN 16.0 13.2 82.3 80 ALA 22.5 30.9 72.2 81 LEU 125.0 84.6 44.7 82 PRO 33.8 27.2 72.0 83 VAL 113.9 95.9 50.4 84 THR 22.9 21.4 74.5 85 TYR 170.6 94.3 58.2 86 SER 41.4 49.6 68.3 87 ASN 0.0 0.0 90.2 88 VAL 61.6 51.8 75.0 89 GLU 60.8 43.9 73.3 90 PRO 45.0 36.2 64.2 91 SER 83.6 99.9 49.5 92 ASP 68.3 61.8 65.7 93 PHE 153.1 91.8 43.2 94 VAL 113.5 95.5 54.7 95 GLN 145.9 98.2 42.2 96 THR 79.5 74.4 55.7 97 PHE 80.3 48.1 68.8 98 SER 44.6 53.3 64.3 99 ARG 36.4 17.4 83.7 100 GLU 0.0 0.0 97.6 101 ALA 7.3 10.0 83.1 102 THR 31.8 29.8 80.9 103 SER 69.2 82.7 58.2 104 GLY 9.8 28.3 66.9 105 PHE 145.6 87.3 50.5 106 PHE 80.3 48.1 68.1 107 GLU 60.5 43.7 64.2 108 VAL 105.4 88.7 53.4 109 PRO 59.9 48.1 79.8 110 LYS 93.2 53.8 82.7 111 ASN 16.3 13.5 80.1 112 GLU 56.0 40.4 70.1 113 THR 8.5 7.9 82.7 114 LYS 120.9 69.7 53.3 115 GLU 8.1 5.8 90.4 116 ASN 25.7 21.2 77.1 117 GLY 27.5 79.0 61.9 118 ILE 107.8 75.1 47.2 119 ARG 168.8 80.8 57.2 120 LEU 147.8 100.0 46.9 121 SER 66.6 79.6 57.9 122 GLU 127.8 92.2 57.4 123 ARG 172.7 82.7 54.5 124 LYS 60.8 35.1 66.3 125 GLU 138.6 100.0 47.7 126 THR 74.7 69.9 72.9 127 LEU 147.8 100.0 36.0 128 GLY 26.6 76.4 55.9 129 ASP 1.7 1.6 78.8 130 VAL 87.3 73.4 74.9 131 THR 58.6 54.8 61.4 132 HIS 141.7 94.4 59.3 133 ARG 126.3 60.4 66.8 134 ILE 143.4 99.9 47.8 135 LEU 147.8 100.0 39.1 136 THR 92.3 86.3 45.4 137 VAL 113.0 95.1 42.5 138 PRO 75.4 60.6 68.7 139 ILE 29.0 20.2 68.4 140 ALA 39.7 54.7 66.6 141 GLN 62.4 42.0 70.9 142 ASP 98.9 89.5 60.0 143 GLN 20.4 13.7 82.5 144 VAL 73.3 61.7 48.8 145 GLY 2.6 7.4 65.7 146 MET 41.2 25.8 79.8 147 TYR 181.0 100.0 39.5 148 TYR 113.7 62.8 60.2 149 GLN 77.9 52.4 71.9 150 GLN 122.1 82.2 46.8 151 PRO 24.9 20.0 82.6 152 GLY 0.0 0.0 84.9 153 GLN 101.6 68.4 65.8 154 GLN 9.4 6.3 89.5 155 LEU 97.4 65.9 61.5 156 ALA 62.9 86.7 49.3 157 THR 89.2 83.4 56.8 158 TRP 204.4 99.7 38.3 159 ILE 98.1 68.4 61.1 160 VAL 118.8 100.0 44.7 161 PRO 94.1 75.6 53.5 162 PRO 15.8 12.7 76.4 163 GLY 6.2 17.8 63.4 164 GLN 97.1 65.3 53.7 165 TYR 174.4 96.4 35.8 166 PHE 166.8 100.0 27.6 167 MET 159.4 100.0 28.9 168 MET 159.4 100.0 38.6 169 GLY 34.8 100.0 59.8 170 ASP 110.5 100.0 54.1 171 ASN 120.9 100.0 48.5 172 ARG 208.9 100.0 50.8 173 ASP 105.2 95.2 57.3 174 ASN 91.6 75.8 65.8 175 SER 82.5 98.6 69.3 176 ALA 21.5 29.5 72.1 177 ASP 110.5 100.0 51.9 178 SER 83.6 100.0 44.1 179 ARG 208.1 99.6 44.5 180 TYR 125.3 69.2 64.5 181 TRP 183.9 89.7 46.9 182 GLY 30.7 88.3 45.0 183 PHE 156.9 94.0 45.8 184 VAL 118.8 100.0 31.7 185 PRO 78.6 63.1 64.9 186 GLU 84.5 60.9 62.7 187 ALA 2.7 3.7 81.6 188 ASN 98.6 81.5 45.8 189 LEU 146.0 98.8 39.5 190 VAL 86.1 72.5 60.0 191 GLY 34.8 100.0 44.9 192 ARG 141.7 67.8 61.6 193 ALA 72.6 100.0 34.8 194 THR 76.1 71.2 55.2 195 ALA 58.1 80.1 53.3 196 ILE 140.4 97.8 52.7 197 TRP 131.7 64.3 50.8 198 MET 103.0 64.6 41.2 199 SER 83.6 100.0 50.6 200 PHE 60.0 36.0 74.6 201 ASP 32.1 29.1 74.4 202 LEU 63.5 42.9 63.2 203 ARG 161.9 77.5 64.9 204 LEU 57.7 39.1 64.3 205 SER 0.0 0.0 82.1 206 ARG 164.9 78.9 62.9 207 ILE 92.1 64.2 59.9 208 GLY 2.9 8.3 79.5 209 GLY 9.5 27.3 69.8 210 ILE 129.8 90.5 48.3 211 HIS 28.5 19.0 81.3