Protein Data Bank File : 1vzv Title : SERINE PROTEASE 10-FEB-97 1VZV Number of Amino Acid Residues : 211 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU ALA LEU TYR VAL ALA GLY TYR LEU ALA 10 LEU TYR SER LYS ASP GLU GLY GLU LEU ASN 20 ILE THR PRO GLU ILE VAL ARG SER ALA LEU 30 PRO PRO THR SER LYS ILE PRO ILE ASN ILE 40 ASP HIS ARG LYS ASP CYS VAL VAL GLY GLU 50 VAL ILE ALA ILE ILE GLU ASP ILE ARG GLY 60 PRO PHE PHE LEU GLY ILE VAL ARG CYS PRO 70 GLN LEU HIS ALA VAL LEU PHE GLU ALA ALA 80 HIS SER ASN PHE PHE GLY ASN ARG ASP SER 90 VAL LEU SER PRO LEU GLU ARG ALA LEU TYR 100 LEU VAL THR ASN TYR LEU PRO SER VAL SER 110 LEU SER SER LYS ARG LEU PHE THR HIS VAL 120 ALA LEU CYS VAL VAL GLY ARG ARG VAL GLY 130 THR VAL VAL ASN TYR ASP CYS THR PRO GLU 140 SER SER ILE GLU PRO PHE ARG VAL LEU SER 150 MET GLU SER LYS ALA ARG LEU LEU SER LEU 160 VAL LYS ASP TYR ALA GLY LEU ASN LYS VAL 170 TRP LYS VAL SER GLU ASP LYS LEU ALA LYS 180 VAL LEU LEU SER THR ALA VAL ASN ASN MET 190 LEU LEU ARG ASP ARG TRP ASP VAL VAL ALA 200 LYS ARG ARG ARG GLU ALA GLY ILE MET GLY 210 HIS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 105.3 -179.3 -68.6 177.6 -48.6 2 ALA -107.1 173.0 178.7 3 LEU -125.6 143.5 177.9 -83.0 53.2 4 TYR -115.2 136.5 179.5 -68.7 80.7 5 VAL -121.0 139.4 178.6 -169.3 6 ALA -144.6 142.2 -179.6 7 GLY 178.2 179.6 179.4 8 TYR -92.4 131.8 179.0 -64.8 -85.9 9 LEU -67.7 -32.5 -178.5 -95.4 19.4 10 ALA -169.3 147.3 178.4 11 LEU -99.4 125.9 -178.7 -74.8 -167.0 12 TYR -49.1 115.4 -179.1 -68.8 -28.2 13 SER 85.6 -64.2 -178.4 0.0 14 LYS -36.9 -44.4 179.9 0.0 0.0 0.0 0.0 15 ASP -55.5 -20.1 178.2 61.7 -6.6 16 GLU 89.8 178.2 179.9 0.0 0.0 0.0 17 GLY -46.1 164.7 -177.8 18 GLU 53.7 -75.6 178.0 -78.0 105.4 -64.8 19 LEU -47.3 -30.1 -178.4 -69.9 -59.8 20 ASN -43.3 126.6 178.8 -120.3 -60.8 21 ILE -111.6 143.2 -177.6 -69.7 -46.1 22 THR -141.9 162.5 -179.6 75.5 23 PRO -48.2 -46.3 178.1 -33.7 45.2 24 GLU -53.2 -28.1 -178.3 -178.1 139.6 37.4 25 ILE -86.9 -48.1 -179.0 -43.4 179.9 26 VAL -57.2 -68.5 -178.7 -153.7 27 ARG -48.2 -41.1 177.9 0.0 0.0 0.0 0.0 28 SER -65.1 -53.3 -178.1 50.6 29 ALA -55.4 -29.3 -179.4 30 LEU -115.6 153.4 -0.2 -15.0 174.8 31 PRO -70.4 133.3 -180.0 -9.2 30.2 32 PRO -59.3 135.9 -178.6 -28.3 42.5 33 THR -67.5 -54.1 -178.6 82.5 34 SER -87.7 122.7 178.9 0.0 35 LYS -50.5 102.1 -177.9 0.0 0.0 0.0 0.0 36 ILE -64.4 128.3 -179.8 -57.7 -177.1 37 PRO -98.0 158.4 -179.6 40.8 -42.2 38 ILE -115.4 113.8 178.0 -85.3 -174.4 39 ASN -123.5 174.8 -178.5 68.1 30.1 40 ILE -106.3 133.0 177.8 -60.7 171.3 41 ASP 67.3 14.7 -177.5 -174.6 49.9 42 HIS 71.4 13.0 178.9 -68.9 -80.8 43 ARG -71.7 104.4 178.0 -76.0 -66.8 -87.8 -88.4 44 LYS -55.4 -31.6 180.0 -54.7 -177.4 174.3 -57.6 45 ASP -86.5 3.2 -179.0 57.3 -20.4 46 CYS -134.3 68.0 179.9 -168.2 47 VAL -97.8 138.1 -177.1 173.7 48 VAL -133.0 13.8 -179.3 -68.1 49 GLY 172.6 -168.6 179.5 50 GLU -155.9 135.6 177.8 78.0 161.9 -48.3 51 VAL -57.5 117.2 179.8 154.6 52 ILE -88.2 -10.1 179.7 78.7 -168.0 53 ALA -178.4 146.2 179.6 54 ILE -138.9 127.1 178.0 -42.8 -176.0 55 ILE -118.1 179.8 -179.7 59.5 155.3 56 GLU -114.2 113.2 179.8 178.2 -166.8 -40.8 57 ASP -97.1 156.8 178.8 170.2 41.0 58 ILE -49.8 -34.7 -179.3 -127.0 -63.6 59 ARG -89.8 -28.4 -179.7 -72.9 -168.8 64.4 152.6 60 GLY 163.4 -176.6 179.6 61 PRO -70.3 132.2 178.5 -23.7 40.2 62 PHE -119.5 129.8 -177.3 -171.5 84.3 63 PHE -125.3 165.8 178.6 90.4 -68.1 64 LEU -137.0 141.5 -179.3 -178.9 53.1 65 GLY -147.9 167.0 178.4 66 ILE -117.7 132.8 178.7 -167.5 163.7 67 VAL -121.2 95.4 179.9 173.6 68 ARG -123.1 88.0 179.7 -178.5 -174.6 -75.0 -107.5 69 CYS -135.9 108.2 -179.6 168.0 70 PRO -59.1 -34.3 -178.9 29.5 -41.7 71 GLN -67.3 -36.2 -179.9 -68.5 69.2 31.5 72 LEU -53.3 -33.7 179.0 -169.9 -102.5 73 HIS -84.7 -35.9 -178.6 -57.0 -164.4 74 ALA -62.7 -47.5 -178.2 75 VAL -65.9 -35.1 179.3 -15.4 76 LEU -70.8 -52.3 178.8 -125.4 30.0 77 PHE -51.3 -41.2 178.8 -93.5 -15.8 78 GLU -64.0 -48.5 -178.7 -172.5 175.9 42.3 79 ALA -57.5 -38.6 -179.9 80 ALA -61.6 140.5 -179.2 81 HIS -68.9 162.5 177.7 -82.0 162.7 82 SER -51.0 -16.0 179.6 -99.5 83 ASN -123.6 21.7 174.1 -69.7 77.8 84 PHE -73.8 124.3 -178.7 -164.4 -82.6 85 PHE 87.8 118.4 179.1 -61.8 -63.2 86 GLY -79.7 -157.7 178.1 87 ASN -87.3 -12.5 178.3 -69.7 -61.6 88 ARG -68.4 -13.8 178.7 45.2 166.3 -81.7 -129.9 89 ASP -97.9 -37.7 177.7 -63.0 -51.2 90 SER -47.3 -56.2 -178.6 -71.8 91 VAL -78.8 49.1 176.3 -129.3 92 LEU 177.5 -30.5 -177.5 -132.4 61.7 93 SER -109.4 141.2 -179.5 -61.9 94 PRO -116.3 -52.8 -179.9 42.8 -39.6 95 LEU -135.9 -11.2 177.6 139.2 100.7 96 GLU -72.6 -13.8 177.2 -51.9 175.7 -44.3 97 ARG -80.4 -26.0 178.3 -68.5 -151.2 -96.8 -118.4 98 ALA -73.5 -52.2 -179.8 99 LEU -53.3 -37.9 179.5 -164.9 59.8 100 TYR -66.1 -39.5 179.2 176.8 -85.9 101 LEU -69.5 -50.4 -178.8 -94.7 -39.0 102 VAL -65.5 -32.0 179.7 61.8 103 THR -71.4 -42.5 -178.8 -64.5 104 ASN -78.3 -28.3 179.0 -77.0 -94.0 105 TYR -78.6 -47.4 -179.1 -158.3 -86.3 106 LEU -115.5 66.1 -179.3 -62.7 176.3 107 PRO -70.0 -20.3 -179.6 29.7 -40.7 108 SER -115.1 168.8 -178.3 -57.1 109 VAL -127.3 136.2 -179.1 140.0 110 SER -119.8 117.9 -179.7 -141.3 111 LEU -87.0 95.3 178.6 172.5 73.2 112 SER -74.7 87.8 -179.4 -9.6 113 SER -68.4 146.8 178.1 -171.5 114 LYS -97.4 -25.0 -178.8 -156.1 -159.0 56.9 51.4 115 ARG 161.8 -42.6 178.8 0.0 0.0 0.0 0.0 116 LEU 178.2 134.5 -56.0 0.0 0.0 117 PHE -97.1 -59.1 179.0 -86.3 -44.2 118 THR 135.4 -83.2 178.3 -73.7 119 HIS -158.0 155.4 180.0 73.6 110.4 120 VAL -102.9 123.5 -179.5 165.9 121 ALA -102.5 144.7 177.1 122 LEU -99.3 141.9 -176.8 -68.1 -178.5 123 CYS -165.2 -179.9 177.4 47.1 124 VAL -65.1 -72.9 178.0 170.9 125 VAL -132.7 145.7 -178.8 -39.9 126 GLY -98.0 168.5 179.0 127 ARG -63.0 -30.9 -178.4 -21.2 -97.0 -50.4 -53.6 128 ARG -85.5 158.6 -174.7 -72.0 167.5 -171.0 167.9 129 VAL -76.4 -18.7 179.1 -49.1 130 GLY -125.6 20.0 -175.8 131 THR -70.4 19.2 176.7 57.0 132 VAL -81.8 146.5 -178.9 136.5 133 VAL -124.4 163.9 178.4 -70.5 134 ASN -118.6 140.6 179.8 -167.8 56.6 135 TYR -123.9 145.4 177.0 -65.1 77.3 136 ASP -163.0 -174.7 -179.0 -144.2 -31.9 137 CYS -107.7 29.0 177.9 9.6 138 THR -164.3 136.3 -179.9 61.6 139 PRO -49.8 -44.1 -178.1 27.5 -44.9 140 GLU -68.6 -10.6 179.0 77.7 -90.8 11.7 141 SER -96.2 -25.9 179.7 -64.0 142 SER -68.3 -39.3 -179.2 -44.0 143 ILE -92.1 -10.9 -178.9 63.0 174.3 144 GLU -55.1 -38.2 -180.0 -173.5 -152.2 61.8 145 PRO -78.2 -6.7 178.7 32.6 -44.7 146 PHE -78.4 96.1 -176.7 -65.7 -86.1 147 ARG -60.1 -21.1 179.5 -55.4 -161.2 -156.9 -176.5 148 VAL -92.7 -33.0 -179.4 -66.5 149 LEU -55.6 118.8 -179.5 -170.8 66.0 150 SER -56.5 147.6 178.2 61.1 151 MET -64.0 -30.6 179.1 -173.1 68.6 -141.6 152 GLU -62.0 -36.9 178.2 -162.3 -171.1 61.7 153 SER -77.8 -49.5 179.9 -85.9 154 LYS -54.2 -43.7 -179.4 -68.0 -163.5 -179.8 167.7 155 ALA -56.7 -52.0 -178.2 156 ARG -54.8 -44.1 179.8 179.7 63.4 -153.0 -36.9 157 LEU -64.1 -50.7 -179.0 -50.8 168.2 158 LEU -51.3 -33.4 179.7 -107.4 35.5 159 SER -76.0 -49.3 179.5 174.6 160 LEU -51.2 -38.7 180.0 -67.3 160.6 161 VAL -62.3 -42.0 -179.5 -179.2 162 LYS -56.9 -37.3 178.9 -178.6 49.7 -173.1 178.2 163 ASP -61.8 -63.0 -177.5 -65.0 -4.9 164 TYR -26.9 99.9 177.5 -178.1 79.8 165 ALA -102.1 142.7 -176.5 166 GLY 120.3 9.3 178.9 167 LEU -74.0 23.4 179.2 68.1 140.2 168 ASN -113.7 -40.7 179.2 128.8 -75.3 169 LYS -29.3 114.5 177.2 -134.8 172.3 -172.6 152.3 170 VAL -105.7 114.9 179.7 -41.3 171 TRP -72.9 118.9 179.8 -69.1 -95.5 172 LYS -107.6 123.0 176.2 -75.6 175.2 161.6 -70.0 173 VAL -120.3 179.8 -176.7 175.1 174 SER -119.3 113.1 179.3 -22.5 175 GLU -19.1 -50.6 -179.3 -136.2 137.9 -15.8 176 ASP -58.7 -40.8 178.9 -81.5 -26.3 177 LYS -89.9 -23.7 179.5 85.1 118.5 57.5 62.7 178 LEU -71.4 -40.2 -179.9 -159.9 49.6 179 ALA -69.0 -17.1 178.9 180 LYS -90.2 -39.4 178.5 -75.0 173.9 -177.3 -79.8 181 VAL -68.7 -39.3 -179.1 -172.8 182 LEU -72.9 -25.4 176.3 -65.1 179.8 183 LEU -77.2 -34.3 -178.4 165.0 71.2 184 SER -65.7 -26.2 179.3 179.8 185 THR -78.7 -22.2 178.2 68.0 186 ALA -76.7 -56.6 179.7 187 VAL -50.4 -52.2 179.7 160.3 188 ASN -77.0 32.0 -178.4 -73.7 -68.3 189 ASN -161.3 2.6 -179.1 -87.0 -81.8 190 MET -61.2 -31.7 -177.2 55.1 -173.6 -169.2 191 LEU -81.7 -18.7 179.2 -73.6 17.5 192 LEU -58.2 129.7 -179.5 145.9 66.2 193 ARG -104.7 157.1 -176.8 -89.4 140.8 -122.8 -123.8 194 ASP 50.8 44.8 179.2 -63.4 -27.9 195 ARG -51.5 -58.9 -178.9 177.3 -173.6 -35.0 -102.1 196 TRP -71.4 -16.8 178.5 -65.4 109.5 197 ASP -82.3 -35.6 177.4 -66.8 -39.6 198 VAL -64.5 -55.0 178.4 168.0 199 VAL -61.3 -23.3 178.2 178.4 200 ALA -66.4 -52.8 -178.5 201 LYS -73.4 -29.9 178.3 71.2 -156.4 75.1 -46.8 202 ARG -65.9 -34.1 179.1 -58.7 -77.0 -165.1 65.8 203 ARG -63.2 -51.0 178.7 -146.0 -168.7 55.8 91.0 204 ARG -61.4 -35.1 179.8 -107.6 -76.6 -122.6 -70.9 205 GLU -69.1 -37.3 -179.2 -94.3 -54.4 -2.6 206 ALA -71.1 -13.6 -178.8 207 GLY 97.1 2.9 178.2 208 ILE -78.5 83.5 -179.8 -58.1 -173.6 209 MET -95.3 -30.9 179.9 -142.5 -80.5 87.9 210 GLY -4.7 92.9 179.7 211 HIS 153.0 -75.7 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 65.564 20.285 57.113 2 ALA 64.697 17.975 54.179 3 LEU 61.585 16.519 52.675 4 TYR 61.202 12.941 51.658 5 VAL 58.886 12.157 48.807 6 ALA 57.670 8.620 48.081 7 GLY 55.240 7.254 45.489 8 TYR 54.950 4.945 42.480 9 LEU 56.784 5.927 39.344 10 ALA 54.120 3.967 37.420 11 LEU 51.403 1.361 37.903 12 TYR 51.955 -1.816 35.880 13 SER 49.653 -1.616 32.887 14 LYS 47.243 1.054 34.177 15 ASP 49.292 4.112 32.993 16 GLU 48.431 2.985 29.384 17 GLY 50.301 2.640 26.098 18 GLU 53.771 4.087 25.351 19 LEU 53.999 5.497 28.892 20 ASN 53.476 1.883 29.955 21 ILE 56.187 0.494 32.242 22 THR 56.638 -3.256 32.731 23 PRO 58.763 -5.794 34.722 24 GLU 61.245 -6.634 31.857 25 ILE 61.931 -2.910 32.093 26 VAL 61.930 -2.391 35.831 27 ARG 64.162 -5.309 36.818 28 SER 66.551 -4.526 34.001 29 ALA 66.525 -0.821 34.977 30 LEU 67.358 -1.284 38.690 31 PRO 69.482 -0.910 40.587 32 PRO 69.891 2.217 38.351 33 THR 73.534 2.908 37.450 34 SER 73.315 6.690 37.557 35 LYS 72.093 8.305 40.764 36 ILE 68.681 9.534 39.567 37 PRO 67.803 13.197 40.219 38 ILE 64.603 15.035 41.070 39 ASN 63.940 18.302 39.306 40 ILE 60.845 20.456 38.816 41 ASP 59.018 20.705 35.437 42 HIS 61.673 18.368 33.923 43 ARG 64.033 21.369 34.117 44 LYS 67.571 20.028 33.907 45 ASP 68.618 23.436 35.261 46 CYS 66.214 23.006 38.127 47 VAL 67.127 19.908 40.182 48 VAL 66.219 20.055 43.870 49 GLY 66.963 16.622 45.298 50 GLU 67.686 13.036 44.271 51 VAL 65.886 9.659 44.329 52 ILE 67.647 7.750 47.123 53 ALA 66.037 4.388 46.207 54 ILE 63.537 2.613 43.905 55 ILE 62.182 -0.899 44.440 56 GLU 59.882 -3.089 42.500 57 ASP 56.445 -3.571 44.039 58 ILE 53.792 -6.155 43.131 59 ARG 51.919 -3.072 41.808 60 GLY 54.798 -1.095 40.298 61 PRO 58.057 0.809 40.836 62 PHE 57.923 2.548 44.263 63 PHE 60.467 5.252 45.080 64 LEU 61.739 7.413 47.851 65 GLY 63.681 10.579 47.301 66 ILE 65.150 13.518 49.087 67 VAL 64.291 17.156 48.319 68 ARG 66.745 19.263 50.277 69 CYS 66.873 22.682 48.537 70 PRO 66.819 25.737 50.769 71 GLN 65.643 27.985 47.953 72 LEU 62.604 25.827 47.124 73 HIS 61.049 26.759 50.496 74 ALA 62.104 30.389 50.465 75 VAL 60.472 31.395 47.121 76 LEU 57.184 29.623 47.921 77 PHE 57.016 31.105 51.422 78 GLU 57.476 34.481 49.803 79 ALA 54.686 33.705 47.253 80 ALA 52.082 32.741 49.874 81 HIS 49.969 35.703 51.021 82 SER 50.343 37.154 54.527 83 ASN 47.474 34.879 55.525 84 PHE 48.094 31.549 53.968 85 PHE 47.939 29.658 57.307 86 GLY 45.871 31.140 60.103 87 ASN 47.086 31.705 63.641 88 ARG 45.920 28.169 64.328 89 ASP 49.089 27.326 62.427 90 SER 51.224 29.946 64.165 91 VAL 50.674 27.923 67.222 92 LEU 51.849 24.668 65.595 93 SER 53.717 24.611 62.242 94 PRO 57.528 25.310 61.556 95 LEU 58.967 23.714 58.307 96 GLU 55.730 21.694 58.086 97 ARG 54.579 24.904 56.500 98 ALA 57.105 24.339 53.690 99 LEU 55.831 20.839 53.399 100 TYR 52.212 22.071 53.275 101 LEU 52.988 24.442 50.376 102 VAL 55.088 21.988 48.330 103 THR 52.593 19.154 48.665 104 ASN 49.699 21.197 47.326 105 TYR 51.618 23.039 44.561 106 LEU 53.574 20.023 43.220 107 PRO 51.456 16.919 43.949 108 SER 52.647 14.547 41.241 109 VAL 55.880 12.925 39.984 110 SER 56.871 12.264 36.371 111 LEU 59.395 9.548 35.501 112 SER 61.107 10.697 32.356 113 SER 62.147 7.150 31.515 114 LYS 65.000 7.032 29.061 115 ARG 63.969 3.404 28.620 116 LEU 65.609 3.058 31.953 117 PHE 65.776 6.051 34.080 118 THR 66.975 9.675 33.669 119 HIS 65.038 11.906 36.075 120 VAL 61.871 12.220 38.222 121 ALA 59.858 15.448 37.716 122 LEU 57.604 17.110 40.281 123 CYS 54.419 18.608 38.783 124 VAL 50.644 19.138 39.206 125 VAL 49.504 15.879 37.633 126 GLY 51.419 13.379 35.596 127 ARG 50.733 11.463 32.422 128 ARG 50.619 8.200 34.492 129 VAL 47.837 6.753 36.644 130 GLY 49.101 6.364 40.240 131 THR 51.633 9.217 40.098 132 VAL 50.334 11.182 43.072 133 VAL 52.989 11.544 45.778 134 ASN 53.382 11.978 49.508 135 TYR 55.943 14.294 51.140 136 ASP 56.976 14.369 54.841 137 CYS 59.997 14.951 57.027 138 THR 61.305 11.433 57.621 139 PRO 61.620 8.545 55.160 140 GLU 59.354 6.265 57.196 141 SER 56.633 8.923 57.115 142 SER 56.625 9.580 53.392 143 ILE 55.856 5.931 52.915 144 GLU 53.777 5.470 56.017 145 PRO 50.366 6.298 54.276 146 PHE 50.454 3.855 51.324 147 ARG 47.919 1.316 52.690 148 VAL 48.726 -1.387 50.131 149 LEU 52.543 -1.221 50.220 150 SER 53.734 -4.288 52.135 151 MET 55.555 -3.858 55.434 152 GLU 58.196 -6.085 53.763 153 SER 58.565 -3.369 51.019 154 LYS 58.311 -0.408 53.351 155 ALA 61.082 -2.098 55.317 156 ARG 63.356 -2.571 52.339 157 LEU 63.294 1.102 51.321 158 LEU 63.950 2.264 54.861 159 SER 67.125 0.187 54.938 160 LEU 68.426 1.291 51.566 161 VAL 67.956 4.797 52.937 162 LYS 70.139 4.011 55.920 163 ASP 72.997 3.195 53.525 164 TYR 72.453 6.415 51.552 165 ALA 75.141 8.844 52.605 166 GLY 74.790 12.311 51.205 167 LEU 71.589 12.963 53.126 168 ASN 73.286 16.366 53.858 169 LYS 73.773 17.542 50.259 170 VAL 71.811 20.795 49.911 171 TRP 70.594 21.474 46.355 172 LYS 70.910 25.136 45.542 173 VAL 68.890 26.660 42.679 174 SER 68.339 30.408 42.420 175 GLU 65.146 32.147 43.593 176 ASP 65.015 34.194 40.343 177 LYS 64.968 31.070 38.118 178 LEU 63.142 28.983 40.691 179 ALA 60.282 31.502 40.617 180 LYS 60.223 31.056 36.836 181 VAL 60.195 27.281 36.824 182 LEU 57.458 27.369 39.490 183 LEU 55.550 30.001 37.555 184 SER 55.937 27.774 34.486 185 THR 54.127 24.863 36.064 186 ALA 51.120 27.164 36.741 187 VAL 50.893 28.752 33.295 188 ASN 51.233 25.331 31.648 189 ASN 48.391 23.884 33.720 190 MET 45.887 26.650 33.996 191 LEU 43.442 24.994 31.595 192 LEU 43.271 21.585 33.321 193 ARG 39.862 20.849 34.867 194 ASP 38.893 18.842 37.959 195 ARG 42.510 19.319 39.022 196 TRP 41.868 18.219 42.599 197 ASP 39.507 15.482 41.445 198 VAL 42.196 14.052 39.213 199 VAL 44.621 14.229 42.134 200 ALA 41.827 12.821 44.270 201 LYS 41.667 9.584 42.290 202 ARG 45.412 9.211 41.496 203 ARG 45.803 9.369 45.298 204 ARG 43.277 6.559 45.853 205 GLU 44.987 4.508 43.165 206 ALA 48.395 4.799 44.845 207 GLY 46.983 3.425 48.061 208 ILE 47.280 6.779 49.819 209 MET 44.012 6.157 51.597 210 GLY 45.361 7.613 54.854 211 HIS 42.335 8.836 56.938 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S C C 10 T T T T C T T T T/S S 20 S S/H H H H H H H H H/P 30 C C C S S S S S S/T T 40 T T T T T T/S S S S/S S 50 S S S S S S S/T T T T/S 60 S S S S S S S S S/H H 70 H H 3 3/H H H H H H H 80 C C C C C H H H H H 90 H H C H H H H 3 3/H H 100 H H H H H H H/S S S S 110 S S T T T T/S S S S/S S 120 S S S S/S S S S/S S S S 130 S S S S S S S H H H 140 H H H H C C C C C H 150 H H H H H H H H H H 160 H H H H C C C S S S 170 S S S S/H H H H H H H 180 H H H H H H H H H H 190 S S S S/H H H H H H H 200 H H H H H H H C S S 210 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E E e 10 t T T T T t T T T t 20 h H H H H H H H h 30 S S S e E E E E 40 e T t T T e E E E E 50 E E E E E E e S S e 60 E E E E E E E e h H 70 H H H H H H H H H h 80 t T T t S h H H H H 90 h T t S h H H H H H 100 H H H H H h E E E 110 E E S E E 120 E E E S S S t T T 130 t B E E E S h H H 140 H H h T T t S S S h 150 H H H H H H H H H H 160 H H H h t T T t 170 h H H H H H H 180 H H H H H H H h T T 190 T t S h H H H H H H 200 H H H H H H h t 210 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 29.9 21.6 75.5 2 ALA 71.6 98.6 54.4 3 LEU 147.3 99.6 37.8 4 TYR 162.3 89.7 43.9 5 VAL 118.8 100.0 30.2 6 ALA 72.6 100.0 37.3 7 GLY 34.8 100.0 39.0 8 TYR 181.0 100.0 44.2 9 LEU 147.8 100.0 25.0 10 ALA 72.6 100.0 46.8 11 LEU 140.5 95.1 49.9 12 TYR 149.5 82.6 54.5 13 SER 53.9 64.5 85.4 14 LYS 130.5 75.3 65.5 15 ASP 110.5 100.0 53.8 16 GLU 81.8 59.0 89.8 17 GLY 5.5 15.9 78.6 18 GLU 0.0 0.0 82.5 19 LEU 110.3 74.6 70.3 20 ASN 86.1 71.3 67.0 21 ILE 136.1 94.8 43.7 22 THR 53.9 50.4 51.2 23 PRO 56.1 45.0 65.6 24 GLU 0.0 0.0 87.3 25 ILE 93.1 64.9 66.3 26 VAL 118.8 100.0 37.7 27 ARG 157.8 75.5 82.1 28 SER 22.9 27.4 79.5 29 ALA 67.0 92.3 50.2 30 LEU 134.0 90.7 42.4 31 PRO 7.9 6.4 78.2 32 PRO 102.6 82.4 54.5 33 THR 0.0 0.0 85.9 34 SER 12.8 15.3 89.9 35 LYS 112.5 64.9 88.6 36 ILE 139.7 97.3 43.5 37 PRO 83.8 67.3 58.6 38 ILE 143.5 100.0 34.7 39 ASN 118.0 97.6 48.2 40 ILE 143.5 100.0 29.6 41 ASP 75.3 68.2 55.9 42 HIS 84.0 55.9 72.1 43 ARG 124.5 59.6 70.5 44 LYS 21.7 12.5 86.9 45 ASP 53.1 48.1 70.4 46 CYS 99.2 100.0 36.0 47 VAL 84.4 71.1 64.5 48 VAL 118.8 100.0 24.0 49 GLY 34.8 100.0 45.4 50 GLU 121.4 87.6 51.7 51 VAL 115.1 96.9 34.7 52 ILE 141.3 98.4 32.6 53 ALA 60.0 82.7 46.9 54 ILE 142.1 99.0 26.9 55 ILE 130.5 90.9 50.4 56 GLU 76.3 55.0 61.6 57 ASP 98.6 89.3 53.5 58 ILE 0.7 0.5 84.0 59 ARG 139.3 66.7 57.8 60 GLY 34.8 100.0 49.4 61 PRO 124.5 100.0 37.0 62 PHE 166.8 100.0 27.7 63 PHE 166.8 100.0 28.3 64 LEU 147.8 100.0 32.1 65 GLY 34.8 100.0 44.9 66 ILE 143.3 99.8 44.9 67 VAL 118.8 100.0 30.5 68 ARG 162.9 78.0 57.5 69 CYS 99.2 100.0 43.4 70 PRO 69.8 56.0 69.0 71 GLN 116.0 78.1 57.1 72 LEU 147.4 99.7 22.6 73 HIS 125.3 83.4 48.4 74 ALA 32.7 45.1 73.5 75 VAL 113.1 95.2 44.0 76 LEU 135.9 92.0 37.5 77 PHE 95.9 57.5 60.2 78 GLU 24.8 17.9 84.5 79 ALA 16.8 23.1 78.5 80 ALA 57.3 78.9 57.1 81 HIS 0.8 0.6 90.7 82 SER 0.0 0.0 89.4 83 ASN 20.2 16.7 80.7 84 PHE 90.3 54.1 56.8 85 PHE 137.6 82.5 48.5 86 GLY 10.5 30.3 78.0 87 ASN 8.6 7.1 85.5 88 ARG 15.2 7.3 88.7 89 ASP 88.4 80.0 60.8 90 SER 38.0 45.5 77.1 91 VAL 6.7 5.6 81.6 92 LEU 11.6 7.8 91.2 93 SER 62.8 75.1 59.3 94 PRO 58.1 46.7 75.0 95 LEU 124.9 84.5 49.6 96 GLU 64.8 46.8 63.8 97 ARG 145.8 69.8 54.0 98 ALA 69.3 95.5 41.7 99 LEU 127.7 86.4 51.3 100 TYR 76.8 42.5 64.7 101 LEU 130.0 88.0 38.3 102 VAL 117.8 99.2 31.5 103 THR 66.4 62.1 66.4 104 ASN 60.3 49.9 61.0 105 TYR 109.2 60.3 60.9 106 LEU 147.7 99.9 39.1 107 PRO 117.3 94.2 52.8 108 SER 83.6 100.0 53.8 109 VAL 118.8 100.0 32.6 110 SER 71.0 84.9 51.2 111 LEU 147.8 100.0 37.3 112 SER 55.0 65.8 68.4 113 SER 72.5 86.7 57.5 114 LYS 47.1 27.2 83.2 115 ARG 145.1 69.5 79.8 116 LEU 131.1 88.7 56.2 117 PHE 166.7 100.0 30.4 118 THR 61.5 57.6 61.9 119 HIS 137.4 91.5 54.8 120 VAL 118.8 100.0 30.2 121 ALA 72.5 99.9 60.8 122 LEU 147.8 100.0 29.9 123 CYS 79.1 79.7 54.4 124 VAL 104.8 88.2 51.2 125 VAL 100.4 84.5 50.3 126 GLY 32.4 93.2 63.3 127 ARG 60.0 28.7 74.9 128 ARG 189.9 90.9 45.1 129 VAL 77.3 65.0 60.2 130 GLY 34.8 100.0 50.5 131 THR 105.6 98.7 68.2 132 VAL 115.1 96.9 45.1 133 VAL 118.8 100.0 44.1 134 ASN 91.9 76.0 51.2 135 TYR 181.0 100.0 37.9 136 ASP 69.5 62.9 61.2 137 CYS 68.7 69.3 54.9 138 THR 55.4 51.9 65.9 139 PRO 97.3 78.2 42.6 140 GLU 55.6 40.1 59.6 141 SER 55.9 66.9 74.3 142 SER 83.6 100.0 52.8 143 ILE 141.5 98.6 28.5 144 GLU 28.3 20.4 78.3 145 PRO 98.2 78.9 61.5 146 PHE 166.8 100.0 41.9 147 ARG 106.4 50.9 71.2 148 VAL 64.2 54.1 72.2 149 LEU 147.0 99.5 40.7 150 SER 35.4 42.4 78.7 151 MET 21.2 13.3 77.0 152 GLU 0.0 0.0 84.5 153 SER 68.3 81.7 56.1 154 LYS 141.8 81.8 51.7 155 ALA 30.9 42.6 66.9 156 ARG 86.1 41.2 63.2 157 LEU 147.8 100.0 32.9 158 LEU 103.5 70.0 50.7 159 SER 20.8 24.9 78.6 160 LEU 108.7 73.5 69.2 161 VAL 101.8 85.6 38.3 162 LYS 7.4 4.3 89.1 163 ASP 15.6 14.2 81.4 164 TYR 150.4 83.1 52.9 165 ALA 7.3 10.0 80.5 166 GLY 14.2 40.8 67.7 167 LEU 53.3 36.0 75.5 168 ASN 9.1 7.5 79.6 169 LYS 63.7 36.7 77.9 170 VAL 66.4 55.9 59.7 171 TRP 169.5 82.7 52.4 172 LYS 59.3 34.2 76.2 173 VAL 107.8 90.7 49.3 174 SER 20.2 24.2 67.6 175 GLU 70.0 50.5 61.6 176 ASP 0.0 0.0 81.9 177 LYS 111.0 64.0 63.2 178 LEU 147.8 100.0 30.4 179 ALA 30.2 41.6 67.1 180 LYS 35.2 20.3 81.8 181 VAL 118.8 100.0 46.6 182 LEU 140.7 95.2 32.9 183 LEU 41.5 28.1 73.2 184 SER 58.4 69.8 75.4 185 THR 103.7 97.0 52.2 186 ALA 31.8 43.8 76.5 187 VAL 43.2 36.3 64.0 188 ASN 39.0 32.2 79.8 189 ASN 87.5 72.4 59.9 190 MET 55.3 34.7 73.1 191 LEU 32.1 21.7 78.4 192 LEU 105.4 71.3 59.3 193 ARG 28.1 13.5 86.4 194 ASP 22.8 20.6 77.5 195 ARG 135.5 64.9 58.2 196 TRP 82.2 40.1 69.0 197 ASP 38.3 34.7 69.9 198 VAL 86.6 72.9 52.3 199 VAL 106.8 89.9 37.8 200 ALA 29.5 40.6 78.7 201 LYS 55.1 31.8 70.7 202 ARG 175.2 83.9 56.7 203 ARG 133.7 64.0 58.3 204 ARG 65.8 31.5 77.9 205 GLU 55.8 40.3 77.7 206 ALA 72.6 100.0 52.5 207 GLY 29.0 83.4 61.1 208 ILE 131.9 91.9 47.9 209 MET 101.7 63.8 74.1 210 GLY 17.0 48.7 70.0 211 HIS 83.4 55.6 90.7