Protein Data Bank File : 1hq6b Title : LYASE 14-DEC-00 1HQ6 Number of Amino Acid Residues : 228 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PHE THR GLY VAL GLN GLY ARG VAL ILE GLY 10 TYR ASP ILE LEU ARG SER PRO GLU VAL ASP 20 LYS ALA LYS PRO LEU PHE THR GLU THR GLN 30 TRP ASP GLY SER GLU LEU PRO ILE TYR ASP 40 ALA LYS PRO LEU GLN ASP ALA LEU VAL GLU 50 TYR PHE GLY THR GLU GLN ASP ARG ARG HIS 60 TYR PRO ALA PRO GLY SER PHE ILE VAL CYS 70 ALA ASN LYS GLY VAL THR ALA GLU ARG PRO 80 LYS ASN ASP ALA ASP MET LYS PRO GLY GLN 90 GLY TYR GLY VAL TRP SER ALA ILE ALA ILE 100 SER PHE ALA LYS ASP PRO THR LYS ASP SER 110 SER MET PHE VAL GLU ASP ALA GLY VAL TRP 120 GLU THR PRO ASN GLU ASP GLU LEU LEU GLU 130 TYR LEU GLU GLY ARG ARG LYS ALA MET ALA 140 LYS SER ILE ALA GLU CYS GLY GLN ASP ALA 150 HIS ALA SER PHE GLU SER SER TRP ILE GLY 160 PHE ALA TYR THR MET MET GLU PRO GLY GLN 170 ILE GLY ASN ALA ILE THR VAL ALA PRO TYR 180 VAL SER LEU PRO ILE ASP SER ILE PRO GLY 190 GLY SER ILE LEU THR PRO ASP LYS ASP MET 200 GLU ILE MET GLU ASN LEU THR MET PRO GLU 210 TRP LEU GLU LYS MET GLY TYR LYS SER LEU 220 SER ALA ASN ASN ALA LEU LYS TYR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PHE 0.0 145.8 171.2 -65.5 -74.7 2 THR -130.4 131.5 -170.6 168.9 3 GLY -134.1 -130.3 -177.8 4 VAL -58.6 -22.9 -176.6 -65.2 5 GLN -101.0 12.5 -167.5 -58.1 144.9 98.4 6 GLY -133.2 163.7 178.2 7 ARG -134.1 156.6 -178.6 -79.8 -171.8 -176.1 98.5 8 VAL -119.2 125.5 -179.1 179.4 9 ILE -63.7 122.9 178.3 -53.6 -177.4 10 GLY 101.1 -9.6 -179.8 11 TYR -125.0 -56.0 -179.8 -178.1 87.1 12 ASP -86.5 -33.0 -179.8 -62.3 111.9 13 ILE -131.4 143.4 178.6 59.5 149.1 14 LEU 60.5 24.6 -176.0 -88.7 51.7 15 ARG -46.5 131.1 -178.6 -179.8 -179.2 -81.1 -132.8 16 SER -87.5 139.3 172.1 61.4 17 PRO -49.4 -33.3 173.4 21.4 -36.5 18 GLU -51.9 -31.2 176.8 -75.0 125.7 -125.2 19 VAL -63.4 -27.1 176.8 176.8 20 ASP -87.0 -30.9 177.1 -52.4 -69.6 21 LYS -71.3 -28.1 -169.8 -66.3 163.2 163.1 50.7 22 ALA -61.7 120.6 174.9 23 LYS -88.9 135.3 172.7 55.8 169.1 -170.3 -178.2 24 PRO -61.8 147.7 176.1 27.9 -40.9 25 LEU -76.1 -38.5 176.9 -63.7 -178.6 26 PHE -174.8 172.3 -177.5 47.7 -78.7 27 THR -126.6 96.9 178.0 64.4 28 GLU -72.1 133.5 -178.6 -113.3 69.9 -71.3 29 THR -63.3 110.5 -179.7 -47.5 30 GLN -91.6 137.2 -180.0 63.3 179.9 26.0 31 TRP -14.4 -45.2 -176.9 66.6 -84.7 32 ASP -79.7 0.6 179.3 66.9 158.0 33 GLY 112.4 -27.8 -180.0 34 SER -61.6 148.2 175.2 -34.1 35 GLU -95.5 125.5 -179.0 -69.3 -60.1 -74.4 36 LEU -95.5 99.3 178.1 171.4 52.7 37 PRO -58.5 144.6 -179.9 27.7 -42.7 38 ILE -114.9 137.7 -176.8 -59.6 -52.1 39 TYR -134.4 158.1 178.1 -61.4 69.9 40 ASP -80.2 124.8 179.9 173.3 16.5 41 ALA -74.2 10.3 -179.0 42 LYS -61.4 -27.4 161.6 -149.8 -94.6 -176.9 -168.2 43 PRO -51.0 -61.1 -178.0 8.0 -32.6 44 LEU -58.6 -42.9 178.1 -88.1 48.7 45 GLN -60.9 -48.5 176.2 -68.3 164.5 -115.2 46 ASP -56.8 -35.5 179.1 -93.1 177.9 47 ALA -63.2 -42.7 -179.9 48 LEU -63.0 -38.7 -178.3 -176.2 59.6 49 VAL -63.8 -40.8 174.4 176.8 50 GLU -55.8 -51.4 -178.5 -71.6 -66.0 21.6 51 TYR -69.5 -46.3 -179.7 -165.9 65.3 52 PHE -80.0 -30.9 -177.7 -70.7 179.5 53 GLY 85.5 -172.8 -176.8 54 THR -117.8 162.1 -177.6 58.2 55 GLU -51.4 -23.3 179.9 -156.6 -72.2 -83.3 56 GLN -105.9 -8.3 176.2 -62.7 -69.2 146.6 57 ASP -144.6 72.4 -175.4 -160.2 3.7 58 ARG -73.0 127.8 176.4 -61.5 -174.9 -168.6 -171.6 59 ARG -112.7 -113.0 -175.9 -69.0 172.7 -176.6 -178.7 60 HIS -93.4 57.3 -176.3 -56.8 -55.9 61 TYR -75.2 152.1 175.4 60.1 -72.2 62 PRO -59.0 134.5 -178.4 21.1 -39.8 63 ALA -48.1 129.3 176.6 64 PRO -49.9 113.6 178.6 15.2 -36.1 65 GLY 99.2 -2.3 -178.4 66 SER -70.4 169.0 178.4 59.8 67 PHE -112.0 110.0 -178.4 -80.9 68.4 68 ILE -112.0 122.1 176.4 -48.3 -56.7 69 VAL -82.7 133.6 -176.1 63.1 70 CYS -131.1 151.3 167.9 -68.9 71 ALA -94.7 112.3 -177.3 72 ASN -148.3 146.2 174.8 59.8 -70.7 73 LYS -139.3 156.5 179.5 -67.2 -173.3 176.0 -171.1 74 GLY -169.7 147.1 -175.3 75 VAL -132.1 141.3 -177.7 65.2 76 THR -122.9 131.5 179.1 -45.7 77 ALA -146.8 152.9 -175.9 78 GLU -112.9 155.2 170.5 173.7 165.3 57.4 79 ARG -122.9 116.0 -173.1 172.7 141.5 99.1 118.3 80 PRO -72.6 169.7 -178.1 38.2 -43.6 81 LYS -76.1 100.0 177.5 -79.7 -169.4 172.7 -69.4 82 ASN 54.5 -1.4 -178.3 -74.1 112.2 83 ASP -50.0 161.7 -175.5 -174.3 34.3 84 ALA -112.3 -65.8 -179.1 85 ASP -84.3 69.7 -171.8 -62.6 101.4 86 MET -64.6 156.6 -175.5 -18.4 131.9 -66.8 87 LYS -49.8 152.5 -173.1 -66.3 143.0 43.7 58.1 88 PRO -56.8 -10.1 179.5 -23.6 41.3 89 GLY -127.1 51.2 179.9 90 GLN -140.6 164.4 -179.0 -69.3 -177.8 -37.0 91 GLY -173.0 -173.6 -176.8 92 TYR -103.0 -19.9 180.0 -70.3 -106.6 93 GLY -146.4 172.6 178.7 94 VAL -144.9 150.4 -177.8 89.9 95 TRP -147.3 156.8 175.2 60.0 -80.8 96 SER -142.5 158.8 -176.9 49.4 97 ALA -149.6 154.2 177.6 98 ILE -144.1 148.5 178.8 -157.1 -178.1 99 ALA -143.4 128.0 176.2 100 ILE -114.2 133.1 -179.3 174.0 56.0 101 SER -121.7 119.7 -176.0 -45.2 102 PHE -80.8 125.3 -177.0 -67.8 -65.8 103 ALA -72.8 146.7 -178.7 104 LYS -63.9 -50.0 -179.8 -148.8 86.3 109.2 174.0 105 ASP -117.4 91.9 -176.7 -172.3 15.2 106 PRO -69.9 4.8 175.9 -9.6 30.0 107 THR -94.5 -15.9 -175.8 68.1 108 LYS -119.0 -40.4 -176.4 -144.5 -170.6 -175.8 -58.1 109 ASP -120.4 160.1 177.8 -66.2 -47.4 110 SER -97.3 162.9 175.1 -179.6 111 SER -94.6 147.9 -169.9 -60.7 112 MET -121.1 152.2 178.5 -176.0 -176.6 73.3 113 PHE -118.1 139.7 172.2 -84.2 -73.0 114 VAL -121.4 135.4 179.1 173.0 115 GLU -138.3 140.7 178.0 -63.6 -178.6 -64.1 116 ASP -152.3 166.1 178.7 -163.8 -171.2 117 ALA -169.5 155.3 -177.4 118 GLY -165.5 176.8 -179.5 119 VAL -104.7 163.8 -179.3 -168.6 120 TRP -128.4 133.0 -176.9 -177.2 -120.8 121 GLU -87.2 -47.1 -176.8 -42.7 -79.8 38.8 122 THR -71.3 160.4 169.3 85.9 123 PRO -84.2 10.4 -171.4 37.6 -43.9 124 ASN -91.9 99.2 179.4 -161.4 -102.9 125 GLU -54.7 -39.8 179.5 -171.7 177.9 135.8 126 ASP -66.0 -26.0 177.7 -47.6 145.2 127 GLU -74.6 -45.8 179.2 -143.5 -169.8 -48.5 128 LEU -52.6 -60.0 179.9 180.0 53.1 129 LEU -47.8 -41.9 178.7 -80.8 154.2 130 GLU -71.7 -38.0 175.6 -101.6 60.7 16.4 131 TYR -59.0 -41.4 -178.7 168.8 60.3 132 LEU -65.1 -42.3 175.3 -105.1 43.8 133 GLU -63.5 -36.2 178.2 174.4 45.7 71.7 134 GLY -63.0 -37.6 -176.5 135 ARG -76.1 -31.9 176.6 -159.6 56.1 177.5 -117.5 136 ARG -60.8 -50.3 179.5 158.1 171.3 -75.9 -178.3 137 LYS -60.9 -36.3 178.4 -164.0 116.4 -169.0 159.0 138 ALA -63.9 -49.6 -179.4 139 MET -60.9 -46.3 174.2 -82.3 152.6 53.5 140 ALA -43.5 -43.9 179.7 141 LYS -74.6 -42.7 -174.0 -77.0 -165.3 -175.9 62.3 142 SER -60.7 -39.9 178.7 45.1 143 ILE -55.2 -65.6 -178.7 -66.0 -178.6 144 ALA -45.5 -38.8 177.7 145 GLU -74.5 -76.2 -177.1 -85.2 71.7 -70.8 146 CYS -42.2 -26.4 174.2 -160.3 147 GLY -56.5 -38.9 175.4 148 GLN -48.0 -46.4 -177.6 164.0 70.0 -84.5 149 ASP -51.9 -39.0 174.5 174.7 76.3 150 ALA -108.6 8.1 178.9 151 HIS 55.2 33.9 175.9 -56.5 -60.5 152 ALA -83.0 133.9 -179.8 153 SER -113.5 128.4 -179.9 -165.5 154 PHE -110.3 178.8 179.0 -58.0 -81.5 155 GLU -128.0 -16.2 174.1 39.8 114.8 -84.5 156 SER -158.4 156.2 169.4 56.9 157 SER -133.4 138.9 -174.2 -66.2 158 TRP -118.9 113.3 -174.3 -63.0 72.4 159 ILE -113.7 137.0 -179.1 -54.4 -175.8 160 GLY -137.0 149.5 -173.8 161 PHE -134.6 158.1 178.6 -73.9 -94.9 162 ALA -153.0 144.7 -174.1 163 TYR -155.2 151.4 173.1 72.6 -88.8 164 THR -142.4 138.6 177.1 -141.1 165 MET -94.2 138.6 175.5 -64.6 -53.7 -52.4 166 MET -90.4 147.8 169.3 -69.4 73.0 127.3 167 GLU -88.0 172.0 -173.6 -109.5 68.2 112.5 168 PRO -68.7 140.3 177.1 -14.3 35.7 169 GLY 73.1 36.1 176.6 170 GLN -138.4 141.3 178.6 -80.2 -167.6 -44.1 171 ILE -103.5 140.8 -179.4 59.8 123.9 172 GLY -114.8 142.4 179.9 173 ASN -126.2 135.9 -179.6 -167.9 -104.4 174 ALA -137.4 130.7 -174.8 175 ILE -129.9 150.1 174.9 59.0 162.8 176 THR -128.5 123.3 -176.2 178.3 177 VAL -146.2 136.9 175.0 53.7 178 ALA -126.4 111.7 -173.2 179 PRO -91.2 153.1 177.1 41.0 -43.2 180 TYR -117.0 109.7 -173.6 -69.2 86.2 181 VAL -125.7 174.4 173.9 -62.5 182 SER -121.9 151.7 -169.3 60.6 183 LEU -98.8 133.6 176.9 -45.4 -174.4 184 PRO -67.8 150.0 -178.0 28.8 -40.1 185 ILE -62.3 -45.6 176.0 -65.7 -56.0 186 ASP -74.3 64.6 -176.4 61.0 -45.5 187 SER -161.3 -21.9 -179.5 -76.1 188 ILE -109.1 110.0 165.0 -54.9 166.9 189 PRO -60.9 120.3 179.4 -36.8 47.1 190 GLY 89.1 3.3 -175.6 191 GLY -85.3 152.8 176.4 192 SER -141.6 155.5 175.5 179.7 193 ILE -65.6 -24.3 177.3 -167.9 73.8 194 LEU -81.5 -7.0 -179.8 -75.2 163.4 195 THR -121.9 47.6 -166.3 39.8 196 PRO -46.5 -56.5 -178.4 -28.6 45.1 197 ASP -63.0 -33.7 -178.5 32.8 109.0 198 LYS -72.5 -37.1 177.6 -155.3 -142.8 171.4 66.4 199 ASP -47.2 -44.8 179.5 -68.7 -24.7 200 MET -65.9 -47.3 178.0 -60.6 -45.5 -68.8 201 GLU -54.9 -35.8 177.6 -145.9 159.8 -108.5 202 ILE -63.4 -47.8 -178.2 -63.0 175.0 203 MET -69.2 -27.4 178.6 -62.1 -60.9 -91.6 204 GLU -74.1 -22.3 -178.4 166.3 175.5 91.1 205 ASN -103.8 -27.6 -179.6 -68.7 -42.1 206 LEU -74.0 143.1 174.2 -62.6 -179.1 207 THR -88.4 168.7 176.8 55.7 208 MET -60.7 -43.1 -172.3 -174.7 59.2 52.9 209 PRO -69.2 -39.9 174.4 -31.1 47.8 210 GLU -55.0 -49.4 -178.0 -72.6 -170.1 -85.4 211 TRP -61.9 -42.0 -177.3 -179.1 71.7 212 LEU -63.6 -40.1 -179.8 -87.0 -18.0 213 GLU -63.5 -57.4 -179.1 -57.3 175.6 -115.4 214 LYS -50.2 -42.6 -178.7 -74.6 -75.7 -165.9 -60.0 215 MET -85.3 -8.4 -175.4 -63.5 -72.2 -51.1 216 GLY 68.2 40.3 178.4 217 TYR -111.8 141.4 -179.3 -70.5 -27.1 218 LYS -81.5 120.6 -179.1 -81.9 53.3 72.2 -79.2 219 SER -56.0 98.3 175.1 176.5 220 LEU -62.1 -17.4 176.5 -62.2 -172.5 221 SER -70.0 -37.8 -175.6 -38.6 222 ALA 44.7 -127.1 173.6 223 ASN -120.8 108.4 -179.8 -65.0 70.4 224 ASN 38.6 46.1 -179.4 -60.0 65.1 225 ALA -74.4 -14.5 -173.0 226 LEU -111.7 131.2 179.7 -95.4 15.0 227 LYS -118.2 147.4 -178.7 50.6 67.1 60.9 -132.5 228 TYR -131.2 160.7 0.0 -58.6 -60.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PHE 55.406 48.294 42.115 2 THR 53.523 48.608 38.797 3 GLY 55.523 50.782 36.423 4 VAL 56.281 51.346 32.817 5 GLN 54.572 48.095 31.676 6 GLY 51.309 48.337 33.524 7 ARG 47.798 49.445 33.826 8 VAL 45.357 49.288 36.799 9 ILE 41.854 47.920 36.463 10 GLY 39.438 50.641 37.240 11 TYR 41.826 53.586 36.718 12 ASP 43.809 53.063 33.518 13 ILE 41.435 50.580 31.972 14 LEU 37.693 50.142 32.444 15 ARG 37.667 53.295 34.586 16 SER 34.493 53.551 36.647 17 PRO 32.707 56.949 36.680 18 GLU 33.103 56.785 40.528 19 VAL 36.851 57.457 39.934 20 ASP 35.619 60.729 38.480 21 LYS 32.949 61.209 41.216 22 ALA 35.508 60.666 43.968 23 LYS 36.281 63.288 46.534 24 PRO 39.644 62.961 48.362 25 LEU 39.479 62.147 52.031 26 PHE 42.351 64.628 52.675 27 THR 45.677 65.541 50.983 28 GLU 49.069 64.838 52.712 29 THR 51.882 67.149 51.584 30 GLN 54.493 65.124 49.724 31 TRP 58.048 66.217 50.035 32 ASP 58.464 68.219 46.764 33 GLY 55.665 70.599 47.771 34 SER 52.804 68.868 45.928 35 GLU 49.701 67.953 47.943 36 LEU 49.048 64.255 47.367 37 PRO 45.226 63.730 47.546 38 ILE 44.302 60.506 49.327 39 TYR 41.137 58.662 48.150 40 ASP 39.226 55.567 49.221 41 ALA 40.194 52.828 46.793 42 LYS 36.719 51.213 46.968 43 PRO 36.163 52.284 43.269 44 LEU 39.262 50.407 42.130 45 GLN 38.411 47.480 44.385 46 ASP 34.860 47.289 42.981 47 ALA 36.339 47.347 39.461 48 LEU 38.415 44.192 40.076 49 VAL 35.363 42.328 41.342 50 GLU 33.598 43.341 38.153 51 TYR 36.336 41.944 35.920 52 PHE 37.086 38.615 37.720 53 GLY 33.556 38.065 39.007 54 THR 32.613 36.178 42.118 55 GLU 32.768 32.495 43.083 56 GLN 29.078 32.112 42.140 57 ASP 29.142 34.329 38.999 58 ARG 32.633 33.714 37.728 59 ARG 33.876 36.008 34.892 60 HIS 37.577 36.529 33.778 61 TYR 39.133 34.820 36.714 62 PRO 42.681 33.503 36.434 63 ALA 42.966 30.108 34.849 64 PRO 42.927 27.051 37.147 65 GLY 46.494 26.114 37.944 66 SER 48.101 29.249 36.559 67 PHE 51.015 31.094 38.132 68 ILE 50.014 34.643 38.983 69 VAL 52.746 36.686 40.572 70 CYS 51.098 38.812 43.241 71 ALA 52.122 41.525 45.621 72 ASN 50.439 39.953 48.674 73 LYS 50.424 39.864 52.417 74 GLY 47.779 38.128 54.557 75 VAL 47.130 37.249 58.202 76 THR 45.281 34.415 59.908 77 ALA 44.287 34.557 63.583 78 GLU 42.101 32.533 65.874 79 ARG 39.750 33.385 68.716 80 PRO 39.640 30.381 71.161 81 LYS 36.358 29.160 72.738 82 ASN 35.780 31.995 75.044 83 ASP 39.266 31.841 76.673 84 ALA 40.681 35.044 78.122 85 ASP 44.449 35.496 78.386 86 MET 44.632 33.813 74.868 87 LYS 47.704 32.325 73.165 88 PRO 50.339 34.724 71.556 89 GLY 48.949 34.425 67.976 90 GLN 45.267 34.949 68.642 91 GLY 42.995 37.944 68.890 92 TYR 39.431 39.079 68.496 93 GLY 39.634 40.652 65.029 94 VAL 41.733 40.841 61.873 95 TRP 42.453 43.466 59.124 96 SER 44.329 44.054 55.813 97 ALA 45.015 47.167 53.708 98 ILE 46.227 48.238 50.318 99 ALA 47.171 51.564 48.773 100 ILE 48.110 52.177 45.133 101 SER 49.800 55.463 44.421 102 PHE 50.003 56.725 40.800 103 ALA 53.319 58.264 39.779 104 LYS 53.382 61.782 38.353 105 ASP 55.679 60.719 35.504 106 PRO 55.227 56.979 34.661 107 THR 57.997 57.167 32.050 108 LYS 60.580 57.865 34.711 109 ASP 59.189 56.662 38.024 110 SER 56.987 53.744 39.034 111 SER 53.699 53.631 40.775 112 MET 53.736 51.944 44.166 113 PHE 51.607 49.623 46.230 114 VAL 51.706 49.591 50.004 115 GLU 50.152 46.579 51.626 116 ASP 49.892 45.741 55.291 117 ALA 47.734 43.543 57.527 118 GLY 47.624 42.643 61.179 119 VAL 45.555 41.121 63.954 120 TRP 43.493 43.071 66.540 121 GLU 43.608 42.290 70.193 122 THR 40.649 44.115 71.884 123 PRO 37.003 42.882 71.138 124 ASN 36.020 46.478 70.481 125 GLU 34.961 46.758 66.857 126 ASP 34.561 50.529 67.312 127 GLU 38.176 50.732 68.529 128 LEU 39.397 48.763 65.498 129 LEU 37.682 50.990 62.957 130 GLU 39.230 54.097 64.446 131 TYR 42.673 52.524 64.581 132 LEU 42.252 51.736 60.868 133 GLU 41.414 55.346 59.976 134 GLY 44.453 56.185 62.113 135 ARG 46.471 53.652 60.143 136 ARG 45.130 55.009 56.821 137 LYS 46.339 58.415 57.804 138 ALA 49.622 56.725 58.815 139 MET 50.194 55.022 55.451 140 ALA 49.310 58.293 53.693 141 LYS 52.296 59.835 55.473 142 SER 54.875 57.068 55.024 143 ILE 54.218 57.197 51.298 144 ALA 54.613 60.981 51.138 145 GLU 57.840 60.677 53.065 146 CYS 59.541 57.549 51.585 147 GLY 58.921 58.871 48.001 148 GLN 61.756 61.441 48.699 149 ASP 64.357 58.667 49.098 150 ALA 63.973 57.680 45.379 151 HIS 62.589 61.165 44.557 152 ALA 59.344 59.736 43.238 153 SER 56.523 62.267 43.051 154 PHE 52.929 60.873 42.918 155 GLU 49.587 62.560 42.163 156 SER 46.970 60.557 44.102 157 SER 46.917 57.568 46.513 158 TRP 43.960 55.263 46.751 159 ILE 43.820 53.349 50.063 160 GLY 41.389 50.515 50.827 161 PHE 40.831 48.395 53.975 162 ALA 38.960 45.194 54.841 163 TYR 38.256 43.582 58.280 164 THR 36.459 40.821 60.176 165 MET 35.750 40.419 63.859 166 MET 35.782 36.783 64.949 167 GLU 33.041 35.335 67.108 168 PRO 34.507 32.922 69.856 169 GLY 35.972 29.738 68.410 170 GLN 36.308 31.105 64.808 171 ILE 39.440 31.947 62.733 172 GLY 39.694 35.023 60.588 173 ASN 41.783 35.389 57.515 174 ALA 42.425 38.759 55.893 175 ILE 44.443 39.183 52.637 176 THR 45.801 42.068 50.572 177 VAL 46.733 41.129 46.997 178 ALA 47.489 42.907 43.732 179 PRO 47.823 40.402 40.817 180 TYR 49.777 40.927 37.620 181 VAL 47.814 39.390 34.779 182 SER 47.233 39.416 31.024 183 LEU 43.730 39.817 29.551 184 PRO 41.599 37.268 27.513 185 ILE 40.217 38.225 24.063 186 ASP 36.545 37.597 25.032 187 SER 36.843 40.538 27.411 188 ILE 37.661 43.109 24.767 189 PRO 34.570 43.928 22.674 190 GLY 35.933 44.212 19.170 191 GLY 39.157 42.621 20.290 192 SER 41.037 40.000 18.372 193 ILE 44.106 37.916 19.071 194 LEU 45.314 39.541 15.865 195 THR 45.012 43.150 17.097 196 PRO 46.940 43.105 20.452 197 ASP 47.894 46.706 20.853 198 LYS 44.511 47.970 19.806 199 ASP 42.972 45.544 22.300 200 MET 44.561 47.387 25.215 201 GLU 43.407 50.724 23.701 202 ILE 39.812 49.432 23.589 203 MET 39.982 48.573 27.316 204 GLU 41.749 51.857 28.006 205 ASN 38.782 53.704 26.451 206 LEU 35.751 51.703 27.633 207 THR 34.303 52.779 30.927 208 MET 33.111 50.099 33.348 209 PRO 29.336 50.646 32.622 210 GLU 30.019 50.579 28.905 211 TRP 31.950 47.318 29.283 212 LEU 29.155 45.724 31.325 213 GLU 26.513 46.605 28.720 214 LYS 28.699 45.457 25.808 215 MET 29.413 42.132 27.513 216 GLY 25.849 41.629 28.801 217 TYR 27.105 41.498 32.423 218 LYS 25.183 42.660 35.488 219 SER 27.058 45.354 37.452 220 LEU 28.104 43.603 40.612 221 SER 29.085 47.008 42.077 222 ALA 25.422 47.972 41.722 223 ASN 24.979 50.664 44.388 224 ASN 27.354 49.513 47.101 225 ALA 26.484 45.814 46.795 226 LEU 29.954 44.828 47.789 227 LYS 31.214 44.934 51.343 228 TYR 34.821 44.244 52.334 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S C C C T T T 10 T/T T T T/S S S S/H H H H 20 H H/S S S S/S S S S S S/T 30 T T T/S S S S S S S S 40 H H H H H H H H H H 50 H H H T T T T/S S S S 60 C C C C S S S S S C 70 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 C C S S S S S S 100 S S S S T T T T/S S S 110 S S S S S S S S/S S S 120 S S C H H H H H H H 130 H H H H H H H H H H 140 H H H H H H H H/T T T 150 T/S S S S S S/S S S S S 160 S S S/S S S S S S S S 170 S S S S S S S S S S 180 S S C T T T T/S S S S/S 190 S S S C H H H H H H 200 H H H H H H H H H H 210 H H H H H H/S S S S C 220 T T T T S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B t T T t t T T 10 T t S S h H H H H 20 H h S E E E E e 30 T T t e E E E E E E 40 h H H H H H H H H H 50 H H E E T T E E e S 60 t T T t E E 70 E E E E E E E E E 80 S S S S t T T B 90 e E E E E E E E E 100 E E E e t T T T t 110 B E E E E E E E E E 120 S S h H H H H H H 130 H H H H H H H H H H 140 H H H H H H h G G G 150 g t e E E E E E E E 160 E E E E E e t T T E 170 E E E E E E E E E E 180 t T T t T T 190 t t T T h H H H H H 200 H H H H H h h H H H 210 H H H H H h t t T 220 T T T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PHE 50.0 30.0 75.9 2 THR 91.1 85.2 44.5 3 GLY 26.1 75.0 77.4 4 VAL 38.0 32.0 81.3 5 GLN 5.3 3.6 84.7 6 GLY 19.0 54.5 81.1 7 ARG 128.1 61.3 60.1 8 VAL 94.7 79.7 48.0 9 ILE 122.8 85.6 35.1 10 GLY 34.8 99.9 54.4 11 TYR 151.3 83.6 54.2 12 ASP 66.7 60.4 55.9 13 ILE 139.0 96.8 36.5 14 LEU 147.8 100.0 29.7 15 ARG 121.2 58.0 69.4 16 SER 75.1 89.8 48.2 17 PRO 79.2 63.6 65.6 18 GLU 72.9 52.6 58.4 19 VAL 116.5 98.1 50.4 20 ASP 42.2 38.2 76.5 21 LYS 48.3 27.8 75.9 22 ALA 54.0 74.4 60.7 23 LYS 7.4 4.3 83.3 24 PRO 82.4 66.1 59.2 25 LEU 95.4 64.6 63.8 26 PHE 128.9 77.3 56.8 27 THR 65.2 61.0 58.0 28 GLU 109.4 78.9 54.2 29 THR 42.1 39.4 81.6 30 GLN 147.7 99.4 52.4 31 TRP 148.8 72.6 66.1 32 ASP 70.2 63.5 65.2 33 GLY 2.6 7.5 80.0 34 SER 56.9 68.0 78.1 35 GLU 60.8 43.8 78.0 36 LEU 147.5 99.8 50.6 37 PRO 99.7 80.1 50.7 38 ILE 143.5 100.0 39.9 39 TYR 146.4 80.9 46.4 40 ASP 61.1 55.3 65.3 41 ALA 69.9 96.2 48.9 42 LYS 133.0 76.7 67.3 43 PRO 107.2 86.1 53.0 44 LEU 138.1 93.4 33.7 45 GLN 110.2 74.2 53.3 46 ASP 102.5 92.7 61.7 47 ALA 71.2 98.1 50.4 48 LEU 95.2 64.4 50.4 49 VAL 88.9 74.9 52.4 50 GLU 138.0 99.6 52.2 51 TYR 178.6 98.7 29.5 52 PHE 133.3 79.9 43.0 53 GLY 34.8 100.0 61.9 54 THR 58.0 54.3 58.5 55 GLU 33.7 24.3 83.8 56 GLN 13.9 9.4 89.0 57 ASP 45.4 41.1 79.2 58 ARG 91.8 44.0 73.6 59 ARG 199.6 95.6 53.7 60 HIS 133.2 88.7 52.4 61 TYR 98.1 54.2 62.4 62 PRO 79.0 63.4 52.9 63 ALA 15.8 21.7 69.8 64 PRO 28.6 22.9 79.0 65 GLY 0.0 0.0 86.6 66 SER 52.3 62.5 58.1 67 PHE 0.0 0.0 89.2 68 ILE 107.8 75.1 55.8 69 VAL 12.3 10.3 79.1 70 CYS 77.1 77.7 53.0 71 ALA 44.0 60.6 66.9 72 ASN 47.1 39.0 71.3 73 LYS 64.1 37.0 79.0 74 GLY 27.0 77.6 57.7 75 VAL 88.8 74.7 60.4 76 THR 50.1 46.9 68.5 77 ALA 68.7 94.7 47.8 78 GLU 65.9 47.5 62.9 79 ARG 168.4 80.6 49.4 80 PRO 102.4 82.3 57.4 81 LYS 21.5 12.4 83.8 82 ASN 22.5 18.6 74.9 83 ASP 41.9 37.9 71.7 84 ALA 12.7 17.5 84.0 85 ASP 0.0 0.0 87.2 86 MET 135.5 85.0 63.0 87 LYS 47.3 27.3 78.8 88 PRO 4.8 3.9 83.7 89 GLY 0.0 0.0 81.1 90 GLN 144.5 97.2 45.0 91 GLY 34.8 100.0 51.6 92 TYR 143.1 79.0 55.4 93 GLY 34.8 100.0 44.5 94 VAL 118.6 99.9 42.1 95 TRP 198.8 97.0 40.2 96 SER 81.6 97.6 48.0 97 ALA 70.2 96.7 42.1 98 ILE 109.8 76.5 56.3 99 ALA 72.6 100.0 42.5 100 ILE 135.4 94.4 32.5 101 SER 83.6 100.0 41.9 102 PHE 153.3 91.9 44.5 103 ALA 72.6 100.0 58.9 104 LYS 95.0 54.8 69.1 105 ASP 48.9 44.3 65.0 106 PRO 56.1 45.1 82.6 107 THR 19.1 17.9 78.7 108 LYS 25.8 14.9 90.1 109 ASP 75.4 68.3 69.4 110 SER 57.5 68.8 56.8 111 SER 73.1 87.4 48.2 112 MET 128.8 80.8 40.8 113 PHE 145.2 87.1 39.4 114 VAL 81.9 68.9 49.5 115 GLU 129.2 93.2 45.6 116 ASP 75.5 68.3 59.7 117 ALA 70.0 96.5 45.0 118 GLY 18.6 53.6 54.6 119 VAL 88.0 74.0 55.7 120 TRP 176.3 86.0 48.8 121 GLU 29.3 21.2 75.2 122 THR 61.6 57.7 59.2 123 PRO 49.5 39.8 59.9 124 ASN 53.6 44.4 73.4 125 GLU 68.6 49.5 60.9 126 ASP 14.6 13.2 79.9 127 GLU 56.3 40.6 66.4 128 LEU 147.8 100.0 30.7 129 LEU 80.8 54.7 67.3 130 GLU 24.4 17.6 81.9 131 TYR 105.8 58.4 59.9 132 LEU 139.7 94.5 32.5 133 GLU 60.1 43.3 65.5 134 GLY 3.0 8.6 73.7 135 ARG 128.0 61.3 59.0 136 ARG 175.1 83.8 45.9 137 LYS 90.6 52.3 70.2 138 ALA 29.9 41.2 70.3 139 MET 148.6 93.2 44.3 140 ALA 72.6 100.0 39.0 141 LYS 83.3 48.1 71.3 142 SER 26.3 31.4 68.5 143 ILE 141.5 98.6 39.1 144 ALA 70.9 97.7 56.7 145 GLU 44.6 32.2 71.4 146 CYS 17.8 17.9 76.5 147 GLY 29.3 84.2 66.9 148 GLN 62.1 41.8 64.8 149 ASP 10.3 9.3 78.4 150 ALA 10.7 14.8 81.2 151 HIS 42.6 28.4 79.8 152 ALA 59.9 82.5 56.5 153 SER 66.3 79.2 63.9 154 PHE 162.5 97.4 46.8 155 GLU 77.7 56.1 69.2 156 SER 76.4 91.4 53.4 157 SER 83.6 100.0 37.5 158 TRP 197.9 96.6 34.1 159 ILE 143.4 100.0 38.6 160 GLY 34.4 99.0 63.3 161 PHE 149.3 89.5 46.2 162 ALA 43.0 59.2 71.1 163 TYR 127.8 70.6 51.8 164 THR 47.0 44.0 66.2 165 MET 135.4 85.0 53.0 166 MET 156.2 98.0 55.7 167 GLU 30.8 22.2 77.8 168 PRO 89.7 72.1 69.4 169 GLY 27.0 77.6 68.3 170 GLN 42.8 28.8 78.2 171 ILE 57.1 39.8 65.4 172 GLY 31.7 91.1 45.4 173 ASN 57.2 47.3 63.9 174 ALA 62.3 85.8 61.9 175 ILE 49.4 34.4 73.2 176 THR 100.2 93.7 48.6 177 VAL 73.9 62.2 54.1 178 ALA 65.3 89.9 38.1 179 PRO 103.1 82.8 35.9 180 TYR 113.1 62.5 60.3 181 VAL 92.6 78.0 45.8 182 SER 0.0 0.0 80.7 183 LEU 135.8 91.9 35.6 184 PRO 70.6 56.7 79.5 185 ILE 92.2 64.3 64.6 186 ASP 9.0 8.2 76.8 187 SER 83.6 100.0 43.8 188 ILE 140.5 97.9 40.0 189 PRO 100.7 80.9 47.0 190 GLY 0.0 0.0 80.0 191 GLY 34.8 100.0 57.9 192 SER 44.9 53.7 62.0 193 ILE 18.7 13.0 73.0 194 LEU 13.7 9.3 80.1 195 THR 46.8 43.7 66.4 196 PRO 44.9 36.1 84.6 197 ASP 0.0 0.0 78.9 198 LYS 59.2 34.2 74.8 199 ASP 105.6 95.6 45.7 200 MET 97.9 61.4 63.3 201 GLU 56.9 41.1 78.1 202 ILE 120.5 84.0 51.3 203 MET 159.4 100.0 31.1 204 GLU 84.2 60.7 74.5 205 ASN 30.3 25.0 77.9 206 LEU 129.8 87.9 46.8 207 THR 55.0 51.5 67.1 208 MET 151.4 95.0 30.8 209 PRO 65.4 52.5 59.2 210 GLU 71.4 51.5 72.5 211 TRP 205.0 100.0 29.6 212 LEU 138.1 93.5 51.7 213 GLU 18.2 13.2 81.6 214 LYS 69.4 40.0 66.4 215 MET 128.0 80.3 56.9 216 GLY 0.0 0.0 85.1 217 TYR 141.0 77.9 51.7 218 LYS 33.8 19.5 85.7 219 SER 47.8 57.1 67.5 220 LEU 111.3 75.3 66.6 221 SER 70.3 84.1 66.3 222 ALA 29.3 40.3 76.4 223 ASN 0.0 0.0 88.1 224 ASN 18.2 15.1 84.6 225 ALA 35.4 48.8 72.6 226 LEU 116.4 78.8 57.5 227 LYS 15.3 8.8 86.9 228 TYR 136.8 75.6 61.8