Protein Data Bank File : 1fs0g Title : HYDROLASE 07-SEP-00 1FS0 Number of Amino Acid Residues : 219 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS ILE THR LYS ALA MET GLU MET VAL ALA 10 ALA SER LYS MET ARG LYS SER GLN ASP ARG 20 MET ALA ALA SER ARG PRO TYR ALA GLU THR 30 MET ARG LYS VAL ILE GLY HIS LEU ALA HIS 40 TYR LYS HIS PRO TYR LEU GLU ASP ARG ASP 50 VAL LYS ARG VAL GLY TYR LEU VAL VAL SER 60 THR ASP ARG GLY LEU CYS GLY GLY LEU ASN 70 ILE ASN LEU PHE LYS LYS LEU LEU ALA GLU 80 MET LYS THR TRP THR ASP LYS GLY VAL GLN 90 CYS ASP LEU ALA MET ILE GLY SER LYS GLY 100 VAL SER PHE PHE ASN SER VAL GLY GLY ASN 110 VAL VAL ALA GLN VAL THR GLY MET GLY ASP 120 ASN PRO SER LEU SER GLU LEU ILE GLY PRO 130 VAL LYS VAL MET LEU GLN ALA TYR ASP GLU 140 GLY ARG LEU ASP LYS LEU TYR ILE VAL SER 150 ASN LYS PHE ILE ASN THR MET SER GLN VAL 160 PRO THR ILE SER GLN LEU LEU PRO LEU PRO 170 LYS HIS LYS SER TRP ASP TYR LEU TYR GLU 180 PRO ASP PRO LYS ALA LEU LEU ASP THR LEU 190 LEU ARG ARG TYR VAL GLU SER GLN VAL TYR 200 GLN GLY VAL VAL GLU ASN LEU ALA SER GLU 210 GLN ALA ALA ARG MET VAL ALA MET LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 -31.1 179.8 -122.1 166.7 -167.6 -70.6 2 ILE -89.8 -27.3 178.6 -145.2 -69.2 3 THR -79.9 -35.3 178.5 76.8 4 LYS -64.7 -37.5 179.2 142.7 64.3 61.5 175.1 5 ALA -68.9 -43.6 179.1 6 MET -56.1 -41.9 -179.5 -147.8 161.2 -120.0 7 GLU -70.8 -38.8 179.4 -56.9 176.2 -47.0 8 MET -61.7 -45.2 179.8 -66.1 -66.5 -71.9 9 VAL -60.3 -45.4 178.6 172.0 10 ALA -65.9 -41.0 -179.2 11 ALA -62.6 -36.5 -179.7 12 SER -63.3 -43.8 178.0 -175.0 13 LYS -67.4 -42.5 -179.4 -66.5 178.6 -165.8 179.0 14 MET -61.6 -40.5 178.9 176.9 75.2 -91.0 15 ARG -61.4 -35.7 179.9 -76.8 -165.5 -71.7 -82.5 16 LYS -65.6 -45.0 179.8 -132.9 -70.2 174.5 51.3 17 SER -66.6 -35.6 179.3 -67.8 18 GLN -68.1 -36.7 177.2 -78.7 162.8 148.5 19 ASP -66.6 -44.0 179.1 -66.2 -25.0 20 ARG -59.2 -48.1 178.8 -78.5 -171.6 -125.2 -77.5 21 MET -54.8 -51.8 -179.0 -69.1 -170.7 -80.2 22 ALA -64.5 -38.2 -177.8 23 ALA -71.7 -18.0 -178.6 24 SER -84.0 -14.1 -177.5 78.4 25 ARG -64.9 -52.9 -179.6 -72.8 -174.0 51.1 -150.1 26 PRO -45.0 -50.5 -178.6 -28.9 41.9 27 TYR -60.4 -46.1 -178.6 -178.8 99.9 28 ALA -68.0 -42.8 -178.5 29 GLU -71.1 -36.5 178.3 -70.7 164.7 7.0 30 THR -67.4 -42.9 -179.3 -69.1 31 MET -59.8 -43.5 -178.4 -170.2 95.9 -78.1 32 ARG -63.4 -36.0 178.9 -169.6 53.4 -168.8 79.5 33 LYS -72.8 -36.6 -179.6 -74.3 -176.3 -58.5 179.9 34 VAL -68.7 -40.6 179.0 175.7 35 ILE -60.4 -42.5 178.8 -77.2 170.0 36 GLY -57.4 -44.4 179.5 37 HIS -58.4 -53.4 -179.1 -173.2 -67.0 38 LEU -66.8 -35.3 -178.6 -63.2 -139.5 39 ALA -74.2 -20.8 178.9 40 HIS -86.0 63.1 -34.3 -173.5 -54.1 41 TYR 19.2 112.7 178.5 177.7 -87.8 42 LYS -98.6 124.3 179.3 -173.9 77.8 169.7 174.5 43 HIS -63.3 135.9 -179.8 -167.0 -64.1 44 PRO -49.4 -34.9 -179.5 -30.3 41.9 45 TYR -70.9 -10.8 -177.0 -65.1 9.6 46 LEU -105.7 6.0 -179.9 -55.7 177.1 47 GLU -137.1 151.3 178.4 64.7 -163.7 -51.1 48 ASP -80.4 154.7 177.2 -70.1 -39.2 49 ARG -150.4 168.4 -179.3 65.9 -168.2 -173.4 -162.6 50 ASP -56.6 129.7 -177.7 175.5 53.6 51 VAL -91.5 104.7 179.4 177.5 52 LYS -102.8 -32.9 178.8 -56.2 161.3 -158.0 -58.2 53 ARG -143.9 145.6 179.8 -42.9 -176.0 70.5 -102.1 54 VAL -122.3 152.8 -179.4 -61.8 55 GLY -124.7 141.2 178.4 56 TYR -125.8 130.5 174.7 -61.3 90.2 57 LEU -100.4 111.7 -176.2 -82.8 141.8 58 VAL -106.0 125.3 179.0 -174.5 59 VAL -103.4 112.3 177.5 -172.4 60 SER -121.0 163.3 178.1 72.1 61 THR -78.7 169.4 176.8 68.7 62 ASP -97.6 -17.7 -176.4 -78.9 -47.7 63 ARG -125.2 154.5 -179.0 -53.4 149.4 -67.2 -174.2 64 GLY -82.4 -156.6 -178.7 65 LEU 50.2 51.9 178.6 -98.9 -162.2 66 CYS -135.9 35.7 180.0 52.1 67 GLY 49.9 -134.5 -179.5 68 GLY -98.0 24.1 -179.5 69 LEU -54.2 -50.9 179.0 -166.6 59.5 70 ASN -73.7 -47.4 -179.4 -67.3 -53.0 71 ILE -49.6 -52.8 -179.3 -70.1 164.0 72 ASN -63.8 -33.7 179.5 -64.4 -25.2 73 LEU -71.1 -47.3 -179.7 -177.0 69.5 74 PHE -56.7 -43.9 179.1 -67.8 168.4 75 LYS -55.6 -50.9 -179.0 -148.2 165.7 174.2 -174.5 76 LYS -60.9 -39.6 179.9 178.9 -167.0 -118.2 -62.1 77 LEU -68.8 -41.8 179.7 164.8 65.9 78 LEU -61.4 -41.9 178.8 -71.7 158.8 79 ALA -56.7 -46.5 -179.3 80 GLU -68.8 -39.1 -179.9 -68.4 -164.6 28.4 81 MET -59.7 -45.8 -178.0 -73.1 176.1 72.5 82 LYS -60.1 -44.3 179.5 -174.2 -177.2 -171.7 -53.5 83 THR -58.6 -30.8 179.4 63.1 84 TRP -76.8 -50.9 -178.2 -81.0 122.0 85 THR -65.0 -28.5 177.4 60.0 86 ASP -62.2 -29.7 -179.1 -82.8 -4.7 87 LYS -94.2 9.9 -179.9 -64.2 158.3 62.8 175.1 88 GLY 82.2 13.9 179.8 89 VAL -98.9 116.9 -179.2 168.4 90 GLN -74.8 148.4 -179.9 -68.5 165.8 -175.4 91 CYS -121.7 129.9 176.5 -62.3 92 ASP -107.5 143.5 -179.5 -76.8 -7.7 93 LEU -123.5 133.7 176.9 -55.2 167.4 94 ALA -112.4 111.2 -175.5 95 MET -93.6 128.5 178.6 -163.0 60.1 50.0 96 ILE -115.5 118.1 179.8 -62.3 161.4 97 GLY 102.4 142.7 -178.5 98 SER -60.5 -48.4 -179.5 -61.6 99 LYS -54.4 -43.4 -179.0 -68.8 -60.2 176.5 168.9 100 GLY -65.4 -39.2 -179.9 101 VAL -65.7 -42.4 -179.3 171.1 102 SER -71.2 -40.3 179.9 66.1 103 PHE -58.9 -50.1 -179.2 -174.5 73.7 104 PHE -72.3 -28.9 176.9 -74.7 84.9 105 ASN -61.6 -37.3 -178.3 -76.9 -14.0 106 SER -70.2 -49.1 -177.5 169.5 107 VAL -90.5 1.1 -178.5 -57.5 108 GLY 94.7 179.9 -178.5 109 GLY 125.8 148.2 -179.3 110 ASN -98.9 91.8 178.8 -175.2 -156.7 111 VAL -90.1 106.3 -178.0 -177.7 112 VAL -88.5 -10.3 179.7 -59.4 113 ALA -173.6 154.2 -178.3 114 GLN -156.0 164.4 173.4 83.6 -165.7 -141.6 115 VAL -148.2 125.6 180.0 58.2 116 THR -130.2 169.6 177.0 65.1 117 GLY 74.7 31.4 177.5 118 MET -89.5 -29.5 177.9 -72.8 -172.6 -67.2 119 GLY 54.3 -129.5 -179.0 120 ASP -76.2 -5.4 -178.5 -60.5 -21.7 121 ASN -125.9 66.3 179.7 -60.9 -66.5 122 PRO -72.3 163.5 -179.5 29.6 -37.5 123 SER -150.7 158.2 178.5 69.0 124 LEU -66.6 -42.1 -176.3 172.4 55.3 125 SER -56.7 -33.9 179.0 60.2 126 GLU -78.6 -10.8 179.2 -71.6 -142.3 -110.0 127 LEU -100.2 -11.2 -179.6 -66.1 166.3 128 ILE -56.9 -51.1 -179.0 -68.1 164.2 129 GLY -57.8 -59.8 179.5 130 PRO -51.9 -45.6 -178.8 -38.7 45.8 131 VAL -66.0 -44.4 179.9 171.3 132 LYS -54.5 -44.2 179.2 166.8 61.8 172.8 -57.3 133 VAL -56.1 -42.1 -179.1 173.2 134 MET -75.6 -38.1 179.7 -54.3 -55.3 -95.2 135 LEU -64.2 -43.1 -179.2 -69.0 179.8 136 GLN -63.7 -40.0 178.7 175.2 -176.4 162.3 137 ALA -63.4 -37.4 178.9 138 TYR -68.9 -43.0 179.8 -164.6 99.9 139 ASP -59.3 -32.0 -177.5 -65.8 -18.7 140 GLU -90.0 4.5 -179.8 -70.5 174.8 6.1 141 GLY 81.3 4.5 -179.9 142 ARG -82.5 -9.3 175.1 -60.1 -171.6 -71.4 94.9 143 LEU -139.6 145.6 -179.3 -66.4 177.1 144 ASP -122.3 -1.2 177.1 -56.0 -58.8 145 LYS -155.0 146.9 178.9 -77.2 -167.5 114.1 69.8 146 LEU -140.4 124.1 -179.1 178.9 52.1 147 TYR -119.8 161.1 174.9 -55.8 88.0 148 ILE -115.9 131.4 179.7 178.8 -179.2 149 VAL -115.7 112.3 -179.3 -171.8 150 SER -161.3 178.0 -179.9 59.7 151 ASN -99.2 125.9 179.0 -68.5 -69.6 152 LYS -82.5 132.8 -179.3 -111.5 -170.3 170.9 -178.0 153 PHE -89.2 130.1 179.4 -176.0 82.4 154 ILE -116.2 -56.1 179.7 -65.2 177.5 155 ASN -163.7 167.6 -177.6 60.5 50.6 156 THR -52.1 -5.0 179.5 64.4 157 MET -128.2 0.0 -178.5 -67.8 -64.3 -72.4 158 SER -137.5 117.5 177.8 162.8 159 GLN -133.2 140.3 -177.9 -63.1 87.6 51.0 160 VAL -118.8 121.1 179.4 -172.0 161 PRO -60.5 127.9 -176.2 -26.4 39.2 162 THR -137.2 140.0 177.2 -58.1 163 ILE -122.6 113.8 -178.9 -66.5 180.0 164 SER -119.9 150.1 179.0 -56.5 165 GLN -85.8 128.6 179.0 -179.5 178.9 -61.0 166 LEU -102.0 -38.7 177.8 -64.2 -177.7 167 LEU -135.6 136.0 -0.4 -64.3 -178.1 168 PRO -73.7 160.7 -177.7 28.6 -39.8 169 LEU -53.4 131.6 179.6 -116.9 -167.1 170 PRO -74.6 -60.5 135.8 -29.1 44.2 171 LYS -96.1 -55.2 -179.8 -172.5 168.4 -64.9 -178.0 172 HIS -138.3 156.4 179.8 -160.2 -52.7 173 LYS -72.6 150.9 179.0 -56.3 -56.0 173.8 67.6 174 SER -74.7 -30.3 -179.2 60.1 175 TRP -96.3 170.2 176.0 53.7 -96.5 176 ASP -137.1 157.4 -179.4 -165.9 -169.3 177 TYR -77.3 155.2 170.8 -60.8 105.5 178 LEU -89.3 123.2 -179.0 162.9 44.3 179 TYR -99.3 121.6 178.7 -60.0 95.7 180 GLU -118.0 114.0 0.3 -64.8 -165.7 32.7 181 PRO -77.0 -44.0 -179.6 38.8 -45.4 182 ASP -157.6 160.6 -179.4 56.9 85.7 183 PRO -62.9 -30.3 -179.2 26.2 -40.9 184 LYS -63.2 -53.8 179.0 -176.8 176.5 -174.0 170.6 185 ALA -57.4 -49.0 -179.8 186 LEU -58.7 -48.4 179.9 -70.1 168.4 187 LEU -59.1 -38.5 179.7 173.8 60.4 188 ASP -61.5 -46.2 179.6 179.8 67.4 189 THR -64.3 -44.8 -179.7 -57.5 190 LEU -60.4 -40.7 -179.5 -55.8 -176.3 191 LEU -63.8 -37.8 179.1 -77.5 163.7 192 ARG -68.8 -45.4 178.2 -70.1 171.1 -159.7 -82.4 193 ARG -61.4 -40.7 179.3 -65.5 -66.0 163.8 -87.9 194 TYR -63.9 -43.6 -178.8 -178.5 64.1 195 VAL -66.1 -43.1 177.7 173.0 196 GLU -56.1 -46.6 179.7 -65.8 167.4 -15.4 197 SER -55.8 -45.4 -178.8 -173.4 198 GLN -65.4 -35.8 178.2 -63.6 179.2 96.0 199 VAL -67.3 -43.3 178.1 176.1 200 TYR -58.4 -44.3 -179.5 173.9 72.6 201 GLN -64.3 -37.0 -179.9 -70.3 -177.2 133.5 202 GLY -62.1 -41.9 178.1 203 VAL -63.8 -49.3 -178.0 174.0 204 VAL -66.5 -33.9 178.6 -56.9 205 GLU -67.8 -39.9 179.3 -120.5 -173.5 -66.0 206 ASN -61.0 -41.9 179.8 -158.5 -100.6 207 LEU -62.1 -41.5 178.1 176.2 59.3 208 ALA -58.7 -42.9 178.8 209 SER -62.5 -46.6 179.4 -67.7 210 GLU -56.1 -53.1 -178.6 179.1 -177.0 178.4 211 GLN -59.8 -39.2 178.0 -67.0 168.6 -28.0 212 ALA -64.0 -48.3 -179.7 213 ALA -61.4 -38.5 -179.6 214 ARG -67.5 -39.5 -179.7 -178.0 162.6 -60.8 119.6 215 MET -63.9 -38.1 177.9 -177.9 54.1 -106.8 216 VAL -64.1 -46.8 179.5 166.8 217 ALA -63.2 -42.4 178.6 218 MET -56.5 -31.2 178.2 -141.7 53.5 -140.2 219 LYS 51.8 -92.1 0.0 -176.5 53.0 -172.4 172.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 2.294 61.502 79.280 2 ILE 1.389 64.042 76.623 3 THR 4.980 64.552 75.461 4 LYS 5.440 60.780 75.437 5 ALA 2.288 60.493 73.287 6 MET 3.601 63.302 71.102 7 GLU 6.802 61.289 70.644 8 MET 5.021 57.998 69.851 9 VAL 3.006 59.709 67.097 10 ALA 6.183 61.272 65.618 11 ALA 8.185 58.051 65.897 12 SER 5.512 56.194 63.962 13 LYS 5.721 58.691 61.056 14 MET 9.551 58.805 61.171 15 ARG 9.863 55.040 60.927 16 LYS 7.693 55.280 57.779 17 SER 9.973 57.907 56.265 18 GLN 13.094 55.908 57.219 19 ASP 11.647 52.801 55.544 20 ARG 10.970 54.826 52.363 21 MET 14.546 56.106 52.378 22 ALA 15.918 52.604 52.842 23 ALA 13.550 50.995 50.347 24 SER 14.580 53.486 47.669 25 ARG 18.310 52.570 47.643 26 PRO 18.500 49.240 45.716 27 TYR 16.911 50.680 42.570 28 ALA 19.169 53.744 42.549 29 GLU 22.361 51.876 43.352 30 THR 21.791 49.079 40.834 31 MET 20.966 51.660 38.193 32 ARG 24.125 53.628 38.958 33 LYS 26.268 50.529 38.524 34 VAL 24.629 49.550 35.248 35 ILE 25.111 53.099 33.982 36 GLY 28.763 52.815 34.993 37 HIS 29.073 49.640 32.935 38 LEU 27.470 51.277 29.865 39 ALA 29.180 54.657 30.182 40 HIS 32.555 52.948 30.230 41 TYR 29.077 58.864 20.904 42 LYS 29.127 60.466 24.333 43 HIS 25.665 61.067 25.861 44 PRO 25.121 64.811 26.682 45 TYR 24.453 63.976 30.337 46 LEU 27.976 62.572 30.687 47 GLU 30.046 65.532 29.585 48 ASP 30.574 69.130 30.606 49 ARG 29.752 71.887 28.165 50 ASP 29.717 75.695 28.265 51 VAL 27.278 76.811 30.969 52 LYS 24.713 79.417 29.795 53 ARG 21.701 78.504 31.951 54 VAL 21.315 76.348 35.080 55 GLY 18.431 74.409 36.577 56 TYR 17.332 73.585 40.129 57 LEU 14.839 70.992 41.420 58 VAL 14.018 72.513 44.783 59 VAL 12.563 70.563 47.657 60 SER 10.673 72.559 50.254 61 THR 8.065 71.199 52.681 62 ASP 4.301 71.522 52.188 63 ARG 3.731 72.343 55.874 64 GLY 4.971 74.798 58.491 65 LEU 6.179 74.355 62.054 66 CYS 9.541 72.937 60.935 67 GLY 11.804 75.639 62.285 68 GLY 14.334 76.851 59.733 69 LEU 14.382 73.723 57.511 70 ASN 13.160 75.623 54.433 71 ILE 14.743 78.971 55.393 72 ASN 18.268 77.624 55.641 73 LEU 17.931 75.764 52.351 74 PHE 16.488 78.785 50.502 75 LYS 19.337 80.882 51.856 76 LYS 21.926 78.438 50.478 77 LEU 20.181 78.297 47.062 78 LEU 19.835 82.092 46.670 79 ALA 23.547 82.540 47.318 80 GLU 24.313 80.125 44.477 81 MET 21.718 81.531 42.078 82 LYS 23.142 85.046 42.457 83 THR 26.689 83.973 41.691 84 TRP 25.253 82.548 38.426 85 THR 23.022 85.441 37.459 86 ASP 25.849 87.856 38.292 87 LYS 27.746 86.106 35.468 88 GLY 24.885 86.280 32.967 89 VAL 23.748 82.662 33.566 90 GLN 19.946 82.292 33.767 91 CYS 18.323 79.999 36.359 92 ASP 15.179 77.907 35.977 93 LEU 13.483 76.425 39.048 94 ALA 11.335 73.287 39.329 95 MET 9.595 73.682 42.693 96 ILE 8.589 70.783 44.919 97 GLY 6.386 71.718 47.868 98 SER 4.085 74.586 48.831 99 LYS 6.438 76.615 51.008 100 GLY 8.926 76.843 48.161 101 VAL 6.258 77.879 45.717 102 SER 4.989 80.635 47.938 103 PHE 8.500 81.864 48.820 104 PHE 9.596 82.203 45.199 105 ASN 6.360 83.603 43.856 106 SER 7.050 86.321 46.416 107 VAL 10.745 87.076 45.804 108 GLY 10.717 86.468 42.081 109 GLY 12.410 83.572 40.358 110 ASN 11.610 81.636 37.221 111 VAL 9.519 78.676 38.392 112 VAL 8.927 76.691 35.223 113 ALA 7.084 73.795 36.857 114 GLN 5.998 72.591 40.269 115 VAL 4.332 69.878 42.327 116 THR 2.928 70.545 45.802 117 GLY 0.819 68.749 48.385 118 MET 2.513 65.356 48.621 119 GLY 3.045 65.659 52.363 120 ASP 3.830 62.381 54.125 121 ASN 3.264 60.410 50.904 122 PRO 5.573 61.582 48.112 123 SER 5.816 59.411 45.006 124 LEU 7.888 58.959 41.903 125 SER 4.818 59.383 39.731 126 GLU 4.198 62.926 40.983 127 LEU 7.828 63.828 40.206 128 ILE 7.887 62.516 36.603 129 GLY 6.394 65.727 35.214 130 PRO 8.542 68.282 37.094 131 VAL 11.661 66.257 36.292 132 LYS 10.667 65.780 32.651 133 VAL 10.451 69.567 32.114 134 MET 14.064 69.945 33.284 135 LEU 15.412 66.911 31.444 136 GLN 13.848 68.148 28.216 137 ALA 15.251 71.627 28.670 138 TYR 18.700 70.006 29.083 139 ASP 18.094 67.812 26.003 140 GLU 17.249 70.975 24.133 141 GLY 20.343 72.900 25.156 142 ARG 18.222 75.150 27.384 143 LEU 19.998 73.989 30.597 144 ASP 23.678 73.071 31.030 145 LYS 23.491 72.017 34.644 146 LEU 20.741 70.517 36.745 147 TYR 20.989 70.413 40.511 148 ILE 18.907 69.013 43.298 149 VAL 18.378 71.263 46.314 150 SER 17.233 69.503 49.485 151 ASN 17.956 68.555 53.071 152 LYS 20.143 65.560 53.841 153 PHE 18.892 63.521 56.799 154 ILE 21.378 62.605 59.570 155 ASN 19.442 62.074 62.815 156 THR 16.375 63.388 64.673 157 MET 18.411 66.496 65.577 158 SER 20.605 67.024 62.470 159 GLN 19.663 67.836 58.825 160 VAL 21.895 69.430 56.215 161 PRO 20.816 71.846 53.421 162 THR 22.365 70.407 50.255 163 ILE 22.843 71.309 46.602 164 SER 24.076 68.442 44.446 165 GLN 24.740 68.204 40.730 166 LEU 22.549 65.696 38.842 167 LEU 23.545 66.678 35.302 168 PRO 25.932 66.248 33.904 169 LEU 26.508 63.007 35.847 170 PRO 29.125 63.172 38.641 171 LYS 37.728 47.782 37.543 172 HIS 35.468 46.359 34.819 173 LYS 33.626 43.118 34.113 174 SER 35.108 40.542 31.744 175 TRP 31.686 40.070 30.096 176 ASP 29.262 42.428 28.351 177 TYR 25.470 42.479 28.034 178 LEU 23.437 41.473 25.053 179 TYR 21.643 44.801 24.487 180 GLU 18.022 44.789 23.291 181 PRO 17.635 46.933 21.123 182 ASP 21.025 48.597 21.536 183 PRO 23.147 50.157 24.303 184 LYS 22.520 53.764 23.207 185 ALA 18.745 53.644 23.632 186 LEU 19.117 51.751 26.939 187 LEU 21.716 54.099 28.388 188 ASP 19.503 57.096 27.633 189 THR 16.576 55.539 29.543 190 LEU 18.736 54.470 32.521 191 LEU 20.136 57.986 32.864 192 ARG 16.602 59.430 32.966 193 ARG 15.432 56.806 35.514 194 TYR 18.510 57.400 37.631 195 VAL 17.983 61.171 37.809 196 GLU 14.292 60.714 38.613 197 SER 15.330 58.268 41.346 198 GLN 17.747 60.768 42.894 199 VAL 15.080 63.451 42.930 200 TYR 12.698 60.992 44.642 201 GLN 15.341 60.151 47.214 202 GLY 15.915 63.869 47.798 203 VAL 12.214 64.350 48.448 204 VAL 11.826 61.427 50.885 205 GLU 14.939 62.484 52.747 206 ASN 13.652 66.048 53.002 207 LEU 10.410 64.643 54.425 208 ALA 12.386 62.631 56.979 209 SER 14.054 65.970 57.810 210 GLU 10.711 67.764 57.968 211 GLN 9.130 65.300 60.419 212 ALA 12.199 65.387 62.638 213 ALA 12.218 69.227 62.579 214 ARG 8.497 69.363 63.350 215 MET 8.742 67.119 66.405 216 VAL 11.477 69.450 67.617 217 ALA 9.263 72.508 66.881 218 MET 6.289 70.753 68.488 219 LYS 8.891 70.587 71.250 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H H H H H H H H H 20 H H H H H/H H H H H H 30 H H H H H H H H H H/X 40 X/C C T T T T/S S S S S/S 50 S S S/S S S S S S S S 60 S S S S S/S S S S/H H H 70 H H H H H H H H H H 80 H H H H H H H H/S S S 90 S S S S S S S/H H H H 100 H H H H H H H H S S 110 S S C S S S S T T T 120 T C H H H H H H/H H H 130 H H H H H H H H H H 140 H S S S S/S S S S S S 150 S/S S S S S/T T T T/S S S 160 S S S S S T T/P T T C/X 170 X/S S S S/S S S S S S S/P 180 C H H H H H H H H H 190 H H H H H H H H H H 200 H H H H H H H H H H 210 H H H H H H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H H H H 10 H H H H H H H 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 g G G G g 50 e E E E E E E E e 60 S S S t T h H H 70 H H H H H H H H H H 80 H H H H H H h T t E 90 E E E E E E h H H H 100 H H H H H H H h e 110 E E E E E t T T 120 t h H H H H H H 130 H H H H H H H H H h 140 T t S e E E E E E 150 E E E E E T T E E E 160 E E E E E E E S 170 S S 180 S h H H H H H H H H 190 H H H H H H H H H H 200 H H H H H H H H H H 210 H H H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 0.0 0.0 91.7 2 ILE 28.1 19.6 69.0 3 THR 26.9 25.1 71.3 4 LYS 57.4 33.1 73.7 5 ALA 26.5 36.6 67.1 6 MET 106.1 66.6 51.5 7 GLU 50.7 36.6 69.8 8 MET 48.9 30.7 77.2 9 VAL 28.9 24.3 74.5 10 ALA 52.0 71.6 55.4 11 ALA 34.5 47.6 75.1 12 SER 29.8 35.7 82.2 13 LYS 78.1 45.0 72.6 14 MET 143.9 90.3 50.3 15 ARG 73.6 35.2 79.1 16 LYS 66.1 38.1 84.2 17 SER 82.8 99.0 56.3 18 GLN 83.9 56.5 52.8 19 ASP 22.7 20.5 75.0 20 ARG 163.8 78.4 60.6 21 MET 128.8 80.8 46.7 22 ALA 17.0 23.4 75.8 23 ALA 10.7 14.8 80.3 24 SER 69.9 83.7 56.1 25 ARG 70.9 33.9 84.2 26 PRO 40.1 32.2 81.3 27 TYR 71.6 39.6 66.9 28 ALA 68.7 94.7 58.9 29 GLU 62.9 45.4 72.0 30 THR 34.4 32.2 71.2 31 MET 137.4 86.2 40.9 32 ARG 126.3 60.5 54.8 33 LYS 28.0 16.2 83.9 34 VAL 82.6 69.6 49.8 35 ILE 143.1 99.7 31.9 36 GLY 13.0 37.5 75.6 37 HIS 130.7 87.0 54.5 38 LEU 140.2 94.8 45.2 39 ALA 54.5 75.0 54.9 40 HIS 38.5 25.6 76.7 41 TYR 69.7 38.5 74.6 42 LYS 79.0 45.6 74.2 43 HIS 137.4 91.4 37.6 44 PRO 81.1 65.2 67.7 45 TYR 180.5 99.7 36.9 46 LEU 135.8 91.8 40.3 47 GLU 65.6 47.4 69.5 48 ASP 22.4 20.3 78.7 49 ARG 137.1 65.6 69.1 50 ASP 25.4 23.0 78.3 51 VAL 93.8 79.0 53.9 52 LYS 46.5 26.8 78.9 53 ARG 156.9 75.1 64.5 54 VAL 118.8 100.0 33.6 55 GLY 34.8 100.0 43.6 56 TYR 181.0 100.0 32.0 57 LEU 147.8 100.0 27.7 58 VAL 118.8 100.0 30.6 59 VAL 115.3 97.1 46.7 60 SER 83.6 100.0 54.7 61 THR 102.5 95.8 62.3 62 ASP 96.4 87.3 57.7 63 ARG 131.7 63.0 71.3 64 GLY 18.0 51.6 68.0 65 LEU 49.0 33.1 69.8 66 CYS 94.8 95.5 58.9 67 GLY 0.0 0.0 81.4 68 GLY 24.0 68.9 69.7 69 LEU 136.0 92.0 56.0 70 ASN 108.4 89.7 42.3 71 ILE 33.6 23.4 73.9 72 ASN 45.8 37.9 63.2 73 LEU 147.8 100.0 56.0 74 PHE 155.5 93.2 34.1 75 LYS 28.4 16.4 81.6 76 LYS 87.9 50.7 70.4 77 LEU 147.8 100.0 24.8 78 LEU 82.2 55.6 54.0 79 ALA 13.0 17.9 77.9 80 GLU 85.4 61.6 64.4 81 MET 137.5 86.2 37.5 82 LYS 46.0 26.5 88.3 83 THR 25.6 23.9 76.2 84 TRP 165.3 80.7 53.1 85 THR 53.3 49.8 69.4 86 ASP 47.2 42.7 77.6 87 LYS 47.8 27.6 76.8 88 GLY 0.0 0.0 81.3 89 VAL 109.0 91.7 50.4 90 GLN 44.6 30.0 76.0 91 CYS 97.8 98.6 44.8 92 ASP 102.9 93.1 56.2 93 LEU 147.8 100.0 29.1 94 ALA 72.6 100.0 43.8 95 MET 159.4 100.0 34.6 96 ILE 140.6 98.0 33.6 97 GLY 32.4 93.2 67.6 98 SER 43.0 51.5 69.2 99 LYS 91.7 52.9 74.9 100 GLY 34.8 100.0 41.6 101 VAL 101.9 85.8 60.4 102 SER 22.0 26.4 77.4 103 PHE 99.0 59.4 48.1 104 PHE 165.7 99.3 30.2 105 ASN 36.6 30.2 72.0 106 SER 19.4 23.3 79.2 107 VAL 65.5 55.1 62.5 108 GLY 1.3 3.6 85.8 109 GLY 22.3 64.0 58.0 110 ASN 47.8 39.5 75.8 111 VAL 106.9 90.0 59.4 112 VAL 84.8 71.4 62.0 113 ALA 51.1 70.3 51.8 114 GLN 79.7 53.7 57.3 115 VAL 101.7 85.6 47.0 116 THR 75.1 70.2 68.8 117 GLY 5.9 17.1 79.5 118 MET 149.9 94.1 53.6 119 GLY 22.5 64.8 76.1 120 ASP 75.8 68.6 70.3 121 ASN 31.4 26.0 82.3 122 PRO 123.3 99.0 39.1 123 SER 47.5 56.9 69.9 124 LEU 83.8 56.7 56.4 125 SER 23.2 27.7 68.0 126 GLU 60.8 43.8 72.8 127 LEU 147.8 100.0 32.3 128 ILE 57.6 40.1 67.4 129 GLY 3.3 9.4 61.5 130 PRO 112.6 90.4 47.3 131 VAL 118.8 100.0 33.6 132 LYS 63.3 36.5 72.8 133 VAL 62.9 52.9 62.3 134 MET 158.5 99.5 37.3 135 LEU 144.6 97.8 42.4 136 GLN 78.9 53.1 72.2 137 ALA 69.4 95.6 60.4 138 TYR 180.8 99.9 50.1 139 ASP 72.6 65.7 67.8 140 GLU 67.7 48.8 77.5 141 GLY 12.7 36.4 83.5 142 ARG 102.4 49.0 74.0 143 LEU 147.7 100.0 48.9 144 ASP 105.8 95.7 56.8 145 LYS 139.2 80.3 50.7 146 LEU 147.8 100.0 32.1 147 TYR 160.1 88.5 44.4 148 ILE 129.7 90.4 48.2 149 VAL 118.8 100.0 33.2 150 SER 73.7 88.2 48.8 151 ASN 120.5 99.7 48.9 152 LYS 48.8 28.2 78.6 153 PHE 150.0 89.9 51.5 154 ILE 68.6 47.8 70.2 155 ASN 50.0 41.4 62.6 156 THR 28.9 27.0 64.8 157 MET 37.7 23.6 81.7 158 SER 50.3 60.2 67.3 159 GLN 130.8 88.0 54.9 160 VAL 52.4 44.1 66.0 161 PRO 94.0 75.5 56.5 162 THR 76.7 71.8 61.9 163 ILE 139.5 97.2 44.8 164 SER 38.2 45.6 61.7 165 GLN 109.4 73.6 57.9 166 LEU 144.3 97.6 41.5 167 LEU 147.8 100.0 30.0 168 PRO 119.6 96.1 66.6 169 LEU 142.0 96.1 41.1 170 PRO 59.9 48.1 68.7 171 LYS 0.0 0.0 93.0 172 HIS 96.9 64.5 62.1 173 LYS 58.9 34.0 74.7 174 SER 0.0 0.0 82.0 175 TRP 87.4 42.6 73.9 176 ASP 43.9 39.7 67.4 177 TYR 105.1 58.1 53.3 178 LEU 17.4 11.8 84.7 179 TYR 153.7 84.9 45.9 180 GLU 20.3 14.6 73.8 181 PRO 42.6 34.2 70.9 182 ASP 54.6 49.4 53.7 183 PRO 61.7 49.5 53.2 184 LYS 52.4 30.2 71.6 185 ALA 28.9 39.8 68.2 186 LEU 90.2 61.0 59.7 187 LEU 128.0 86.6 40.0 188 ASP 71.0 64.2 71.3 189 THR 48.8 45.6 72.5 190 LEU 119.8 81.0 38.3 191 LEU 147.8 100.0 29.8 192 ARG 152.4 73.0 68.0 193 ARG 112.6 53.9 67.4 194 TYR 155.6 86.0 45.1 195 VAL 118.8 100.0 37.5 196 GLU 126.4 91.2 41.0 197 SER 74.8 89.5 46.3 198 GLN 119.6 80.5 52.7 199 VAL 118.8 100.0 27.3 200 TYR 139.9 77.3 45.4 201 GLN 105.3 70.8 59.2 202 GLY 27.5 79.2 63.5 203 VAL 111.0 93.5 31.4 204 VAL 117.6 99.0 40.2 205 GLU 94.6 68.3 56.7 206 ASN 118.0 97.6 53.8 207 LEU 140.5 95.0 66.2 208 ALA 72.6 100.0 42.7 209 SER 83.6 100.0 43.2 210 GLU 133.8 96.5 52.2 211 GLN 137.9 92.8 52.5 212 ALA 67.1 92.5 56.5 213 ALA 59.8 82.3 58.6 214 ARG 165.0 79.0 57.5 215 MET 120.6 75.7 52.8 216 VAL 53.1 44.7 66.4 217 ALA 52.7 72.6 64.6 218 MET 82.4 51.7 54.1 219 LYS 17.4 10.0 90.2