Protein Data Bank File : 1c5ea Title : VIRUS/VIRAL PROTEIN 18-NOV-99 1C5E Number of Amino Acid Residues : 95 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER ASP PRO ALA HIS THR ALA THR ALA PRO 10 GLY GLY LEU SER ALA LYS ALA PRO ALA MET 20 THR PRO LEU MET LEU ASP THR SER SER ARG 30 LYS LEU VAL ALA TRP ASP GLY THR THR ASP 40 GLY ALA ALA VAL GLY ILE LEU ALA VAL ALA 50 ALA ASP GLN THR SER THR THR LEU THR PHE 60 TYR LYS SER GLY THR PHE ARG TYR GLU ASP 70 VAL LEU TRP PRO GLU ALA ALA SER ASP GLU 80 THR LYS LYS ARG THR ALA PHE ALA GLY THR 90 ALA ILE SER ILE VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 -77.2 169.2 -163.6 2 ASP -115.2 96.5 -175.7 164.9 40.8 3 PRO -52.4 141.4 174.1 -30.7 39.7 4 ALA -97.8 104.5 -179.1 5 HIS -89.0 141.3 176.9 -63.3 -51.7 6 THR -99.5 171.2 -172.0 55.8 7 ALA -158.7 161.1 172.7 8 THR -129.1 150.6 172.9 53.5 9 ALA -159.9 162.6 178.3 10 PRO -59.7 136.9 -179.8 -30.4 41.9 11 GLY -108.3 149.6 179.3 12 GLY -134.9 32.7 -179.7 13 LEU -61.7 155.3 173.7 -58.3 174.7 14 SER -112.8 -1.3 -176.9 66.9 15 ALA -158.4 166.7 173.7 16 LYS -54.2 140.1 173.8 -60.6 -165.4 166.1 175.0 17 ALA -135.9 121.7 173.7 18 PRO -75.2 163.1 166.6 -17.2 37.4 19 ALA -51.3 146.2 -180.0 20 MET 86.2 9.9 173.7 -60.4 -54.8 -74.3 21 THR -81.1 123.4 174.5 -59.2 22 PRO -64.0 144.0 -175.6 -25.5 40.3 23 LEU -121.4 150.3 173.6 -53.5 171.0 24 MET -134.9 170.3 170.3 71.4 -175.6 -176.0 25 LEU -87.6 139.4 167.2 -65.2 -175.3 26 ASP -67.2 127.9 -173.4 -176.7 -88.2 27 THR -72.9 -14.3 177.3 56.9 28 SER -89.2 -55.6 -172.7 -66.6 29 SER -90.6 -26.4 -172.5 61.6 30 ARG 63.0 23.3 156.6 -55.7 -161.8 66.6 84.2 31 LYS -64.7 154.9 174.1 -64.8 -174.4 178.8 174.3 32 LEU -79.6 129.2 -179.3 -146.1 41.1 33 VAL -136.6 173.9 178.2 -56.7 34 ALA -66.2 140.0 169.1 35 TRP -63.3 133.9 179.7 -177.1 41.9 36 ASP -72.1 -16.1 -175.7 55.2 18.9 37 GLY 79.3 -2.6 -175.5 38 THR -124.9 -20.2 177.1 56.9 39 THR -87.4 112.4 -174.4 -59.5 40 ASP -64.0 132.4 173.9 -73.3 -16.8 41 GLY 75.4 6.5 -178.1 42 ALA -85.4 -13.6 -177.6 43 ALA -72.2 129.3 -173.9 44 VAL -124.1 -8.9 -177.1 -66.0 45 GLY -170.8 173.1 177.8 46 ILE -127.4 121.3 -176.7 -64.8 169.5 47 LEU -57.8 136.7 -175.6 -168.4 64.7 48 ALA -106.1 -25.8 179.2 49 VAL -129.8 127.0 -178.4 179.8 50 ALA -55.0 147.0 -170.3 51 ALA -150.0 171.7 175.2 52 ASP -151.3 -169.3 -174.9 71.6 16.5 53 GLN -67.0 -14.0 177.6 65.7 -75.3 -11.0 54 THR -90.5 -10.7 -172.8 74.3 55 SER -75.7 121.9 178.6 -59.0 56 THR -82.6 -28.4 177.0 50.9 57 THR -123.8 132.7 170.5 -61.9 58 LEU -101.2 142.4 174.8 -54.0 -171.0 59 THR -108.7 122.7 -166.8 -56.8 60 PHE -140.6 155.1 167.3 66.4 -78.9 61 TYR -78.2 131.7 173.9 -58.1 -69.2 62 LYS -113.0 0.1 176.5 63.2 169.5 172.3 161.7 63 SER -154.8 170.7 178.8 77.2 64 GLY 116.2 174.1 176.0 65 THR -116.3 127.7 -174.5 -62.1 66 PHE -122.3 142.9 176.3 -61.4 86.6 67 ARG -71.0 136.7 174.9 -63.6 -172.1 20.5 -129.7 68 TYR -48.9 -40.2 -178.1 177.2 70.1 69 GLU -73.8 -17.8 -175.6 60.3 -110.4 57.7 70 ASP -94.8 -23.0 179.3 -63.0 -20.8 71 VAL -73.7 134.3 179.9 176.6 72 LEU -89.5 74.0 -176.7 -63.7 175.9 73 TRP -60.0 146.7 170.7 -55.0 102.5 74 PRO -68.0 149.9 179.6 26.8 -33.6 75 GLU -58.4 -34.9 -176.8 -155.9 169.9 -41.3 76 ALA -67.4 -19.4 173.1 77 ALA -78.9 82.2 -169.0 78 SER -92.5 -6.5 -176.1 61.2 79 ASP -108.1 119.5 -177.2 -174.8 80.8 80 GLU -59.6 -45.1 179.3 178.2 168.8 -8.6 81 THR -60.7 -44.5 -176.7 -72.5 82 LYS -65.5 -33.6 172.4 -63.9 -176.5 -173.3 -164.3 83 LYS -65.3 -46.7 -177.7 -74.5 177.5 -83.2 -173.8 84 ARG -61.0 -26.9 175.2 -72.8 179.6 178.8 -80.9 85 THR -108.9 19.0 -178.3 64.2 86 ALA -63.1 -22.6 -176.6 87 PHE -109.6 7.1 -177.5 -64.7 -81.4 88 ALA -60.7 135.0 -175.5 89 GLY 94.3 -16.2 170.7 90 THR -91.0 -177.4 172.7 77.3 91 ALA -84.9 -6.7 173.9 92 ILE -82.6 137.3 166.6 -59.9 166.3 93 SER -137.7 170.1 -176.4 66.1 94 ILE -119.2 138.8 174.9 -55.6 -60.6 95 VAL -122.6 -34.8 0.0 64.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER 8.363 55.118 -14.652 2 ASP 8.984 51.505 -13.871 3 PRO 5.620 49.918 -14.688 4 ALA 4.324 47.466 -12.149 5 HIS 3.108 44.493 -14.166 6 THR 0.708 41.996 -12.767 7 ALA 0.561 38.247 -13.069 8 THR -1.583 35.343 -11.928 9 ALA -0.654 31.935 -10.551 10 PRO -2.154 29.116 -8.449 11 GLY -2.447 30.055 -4.830 12 GLY -1.864 28.081 -1.682 13 LEU -2.413 30.539 1.160 14 SER -3.486 29.313 4.597 15 ALA -4.835 32.648 5.859 16 LYS -5.995 36.063 4.640 17 ALA -3.361 38.166 2.861 18 PRO -3.923 41.792 1.968 19 ALA -2.552 43.407 -1.122 20 MET 1.167 44.287 -0.722 21 THR 2.017 40.946 0.943 22 PRO 5.305 39.387 -0.323 23 LEU 4.929 35.951 -1.883 24 MET 7.179 32.903 -2.353 25 LEU 6.756 29.473 -3.904 26 ASP 5.879 26.534 -1.690 27 THR 8.820 24.178 -2.247 28 SER 6.574 21.054 -2.412 29 SER 3.614 22.175 -4.487 30 ARG 5.135 25.295 -6.082 31 LYS 1.898 27.173 -5.499 32 LEU 2.286 30.810 -4.548 33 VAL 2.198 31.329 -0.755 34 ALA 3.178 34.076 1.664 35 TRP 6.913 34.696 1.937 36 ASP 8.003 33.398 5.360 37 GLY 10.448 36.299 5.777 38 THR 13.266 33.887 6.642 39 THR 14.086 31.921 3.494 40 ASP 16.691 34.055 1.741 41 GLY 15.988 34.819 -1.922 42 ALA 12.586 33.098 -1.968 43 ALA 10.403 36.172 -2.559 44 VAL 9.036 36.153 -6.120 45 GLY 6.139 38.612 -6.111 46 ILE 3.938 41.054 -4.159 47 LEU 0.221 40.311 -3.869 48 ALA -1.848 42.792 -5.839 49 VAL -5.402 41.689 -4.916 50 ALA -6.293 40.584 -1.435 51 ALA -6.711 36.833 -1.133 52 ASP -7.153 34.033 1.392 53 GLN -7.011 30.264 1.874 54 THR -10.000 29.887 -0.508 55 SER -8.356 31.708 -3.408 56 THR -7.436 29.423 -6.237 57 THR -5.565 32.107 -8.203 58 LEU -3.462 34.890 -6.771 59 THR -3.013 38.137 -8.669 60 PHE 0.443 39.632 -7.933 61 TYR 2.932 42.214 -9.037 62 LYS 5.928 40.723 -10.884 63 SER 7.634 44.056 -11.588 64 GLY 7.811 47.631 -10.354 65 THR 9.380 49.673 -7.621 66 PHE 7.671 49.616 -4.209 67 ARG 8.250 51.684 -1.106 68 TYR 9.781 49.873 1.831 69 GLU 7.033 51.380 4.016 70 ASP 4.214 50.187 1.740 71 VAL 5.105 46.523 1.515 72 LEU 3.377 44.420 4.219 73 TRP 6.451 42.496 5.254 74 PRO 6.051 39.450 7.486 75 GLU 7.043 40.050 11.095 76 ALA 9.717 37.380 10.873 77 ALA 11.592 39.505 8.285 78 SER 13.282 41.562 10.991 79 ASP 16.295 42.845 9.030 80 GLU 15.766 45.966 6.914 81 THR 18.589 45.250 4.455 82 LYS 17.377 41.696 3.759 83 LYS 13.891 43.071 3.063 84 ARG 15.287 45.781 0.794 85 THR 17.075 43.181 -1.349 86 ALA 14.419 40.447 -1.013 87 PHE 13.524 40.911 -4.700 88 ALA 17.028 41.411 -6.159 89 GLY 17.290 39.521 -9.394 90 THR 13.582 39.763 -10.060 91 ALA 11.966 42.692 -11.888 92 ILE 10.737 44.100 -8.529 93 SER 12.815 46.479 -6.399 94 ILE 12.310 48.389 -3.119 95 VAL 12.928 52.107 -2.505 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 S S/S S S S S S S 20 S S S S S S/T T T T C 30 S S S S C C C S S S 40 S S S S S/S S S S S/S S 50 S S S C C S S S S S 60 S S S S S C T T T T 70 C S S S S C C C H H 80 H H H H H H T T T T 90 S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E E 10 e S S B t T T 20 e E E E E e T T T t 30 e E E E e S t T 40 T e E E E E E e S 50 B t T T t e E E E E 60 E e E E E E E e T T 70 t t T T t h H 80 H H H H h T T T T t 90 E E E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 0.0 0.0 92.3 2 ASP 53.9 48.7 77.7 3 PRO 42.2 33.9 85.6 4 ALA 49.1 67.7 59.8 5 HIS 51.3 34.2 69.5 6 THR 52.4 49.0 60.8 7 ALA 49.4 68.0 53.5 8 THR 41.5 38.8 65.8 9 ALA 45.1 62.1 48.7 10 PRO 38.3 30.8 67.7 11 GLY 34.8 100.0 58.9 12 GLY 21.3 61.3 61.8 13 LEU 142.8 96.6 48.8 14 SER 4.7 5.6 78.2 15 ALA 15.5 21.3 88.8 16 LYS 20.8 12.0 85.3 17 ALA 67.0 92.3 43.5 18 PRO 49.2 39.5 68.7 19 ALA 40.5 55.8 64.8 20 MET 119.7 75.1 47.6 21 THR 90.2 84.4 44.5 22 PRO 124.4 99.9 34.5 23 LEU 147.8 100.0 34.7 24 MET 126.9 79.6 54.4 25 LEU 99.7 67.5 62.3 26 ASP 64.1 58.0 63.8 27 THR 10.5 9.8 89.0 28 SER 3.5 4.2 89.7 29 SER 40.8 48.8 61.4 30 ARG 70.7 33.8 75.6 31 LYS 77.5 44.7 69.8 32 LEU 145.9 98.7 31.4 33 VAL 98.7 83.1 54.1 34 ALA 34.9 48.1 59.3 35 TRP 195.7 95.5 43.1 36 ASP 63.5 57.4 69.5 37 GLY 34.8 100.0 41.5 38 THR 36.3 34.0 76.5 39 THR 41.4 38.7 77.1 40 ASP 22.0 19.9 81.4 41 GLY 1.6 4.7 86.1 42 ALA 50.5 69.5 59.3 43 ALA 72.5 99.9 44.3 44 VAL 71.8 60.4 55.4 45 GLY 34.8 100.0 43.1 46 ILE 143.5 100.0 27.9 47 LEU 147.8 100.0 42.8 48 ALA 68.9 94.9 44.8 49 VAL 30.1 25.3 76.3 50 ALA 23.3 32.1 69.0 51 ALA 62.5 86.1 54.0 52 ASP 80.5 72.8 60.9 53 GLN 70.4 47.4 69.5 54 THR 21.0 19.6 85.9 55 SER 59.7 71.4 72.1 56 THR 2.3 2.2 91.3 57 THR 48.5 45.3 73.8 58 LEU 147.0 99.5 38.4 59 THR 68.7 64.2 48.9 60 PHE 146.2 87.7 44.8 61 TYR 130.7 72.2 50.4 62 LYS 71.3 41.1 65.5 63 SER 74.3 88.9 52.7 64 GLY 34.7 99.8 59.9 65 THR 66.2 62.0 66.3 66 PHE 148.0 88.7 39.1 67 ARG 84.7 40.5 79.1 68 TYR 139.6 77.1 60.7 69 GLU 55.3 39.9 79.0 70 ASP 59.5 53.8 68.0 71 VAL 118.8 100.0 35.0 72 LEU 61.6 41.7 73.5 73 TRP 188.9 92.2 36.8 74 PRO 92.0 73.9 60.1 75 GLU 0.0 0.0 93.2 76 ALA 27.9 38.4 70.8 77 ALA 67.6 93.1 50.9 78 SER 10.9 13.0 86.5 79 ASP 49.6 44.9 67.0 80 GLU 59.5 42.9 71.9 81 THR 17.1 16.0 74.7 82 LYS 48.9 28.2 83.1 83 LYS 145.9 84.1 49.8 84 ARG 130.0 62.2 61.8 85 THR 35.6 33.3 72.3 86 ALA 66.7 91.9 50.6 87 PHE 165.8 99.4 39.0 88 ALA 17.8 24.5 78.7 89 GLY 0.0 0.0 83.8 90 THR 69.1 64.6 68.6 91 ALA 21.6 29.8 75.5 92 ILE 143.4 99.9 48.6 93 SER 28.1 33.6 71.0 94 ILE 143.4 99.9 42.6 95 VAL 34.0 28.6 71.2