Protein Data Bank File : 1a6s Title : CORE PROTEIN 02-MAR-98 1A6S Number of Amino Acid Residues : 87 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY GLU ALA VAL ILE LYS VAL ILE SER SER 10 ALA CYS LYS THR TYR CYS GLY LYS THR SER 20 PRO SER LYS LYS GLU ILE GLY ALA MET LEU 30 SER LEU LEU GLN LYS GLU GLY LEU LEU MET 40 SER PRO SER ASP LEU TYR SER PRO GLY SER 50 TRP ASP PRO ILE THR ALA ALA LEU SER GLN 60 ARG ALA MET ILE LEU GLY LYS SER GLY GLU 70 LEU LYS THR TRP GLY LEU VAL LEU GLY ALA 80 LEU LYS ALA ALA ARG GLU GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 80.3 180.0 2 GLU -64.3 -9.1 -180.0 -111.8 150.9 -27.1 3 ALA -84.9 -40.9 -180.0 4 VAL -40.6 -34.9 -180.0 107.5 5 ILE -93.4 -55.4 179.9 -16.7 49.5 6 LYS -52.4 -42.1 -180.0 -133.3 69.1 126.5 -160.7 7 VAL -60.3 -64.5 -180.0 98.3 8 ILE -44.4 -47.4 180.0 -152.9 53.2 9 SER -72.6 -65.6 180.0 127.7 10 SER -59.2 -53.1 180.0 -130.0 11 ALA -44.1 -54.8 -180.0 12 CYS -40.3 -58.6 180.0 -177.0 13 LYS -93.7 -57.1 -180.0 -122.7 -128.6 51.0 -108.1 14 THR -49.8 -30.9 180.0 -38.5 15 TYR -69.7 -76.7 -180.0 -147.8 -25.9 16 CYS -111.4 47.7 180.0 163.8 17 GLY -164.8 -18.2 -180.0 18 LYS -27.7 96.9 -180.0 34.0 172.3 -153.2 121.8 19 THR 165.7 -64.0 180.0 -99.2 20 SER -62.3 170.4 180.0 -116.1 21 PRO -75.0 -43.7 -180.0 18.7 -14.0 22 SER 159.2 59.8 -180.0 158.6 23 LYS -65.6 -39.8 -180.0 63.1 -141.6 -104.6 163.2 24 LYS -143.1 12.1 180.0 41.4 98.4 -117.3 115.1 25 GLU -48.0 -89.8 -180.0 176.2 -172.3 -51.0 26 ILE -54.5 -33.4 180.0 -53.6 -167.1 27 GLY -48.8 -82.0 180.0 28 ALA -50.5 -46.5 180.0 29 MET -40.0 -47.4 180.0 147.6 -91.7 -153.8 30 LEU -95.0 -60.5 -180.0 -110.9 160.6 31 SER -55.8 -42.3 180.0 -84.5 32 LEU -63.2 -62.8 180.0 -138.7 -45.1 33 LEU -68.4 -47.7 -180.0 -70.2 -87.1 34 GLN -68.9 3.0 -180.0 -156.6 -174.3 77.5 35 LYS -136.3 21.9 180.0 -152.6 169.0 -87.0 140.1 36 GLU -137.0 8.6 -180.0 -96.7 41.1 69.0 37 GLY 96.8 27.1 180.0 38 LEU -121.5 50.2 -180.0 -71.5 -28.9 39 LEU -91.1 17.1 -180.0 -126.7 -178.4 40 MET -91.6 10.2 -180.0 -130.8 72.4 106.3 41 SER 94.1 177.8 180.0 96.8 42 PRO -75.0 18.4 -180.0 18.7 -14.1 43 SER -68.9 -23.2 -180.0 -92.5 44 ASP -39.2 -40.5 -180.0 161.4 -52.2 45 LEU -61.6 -33.4 -180.0 161.9 156.0 46 TYR -56.1 -4.5 180.0 -72.4 -17.3 47 SER -127.7 137.2 180.0 167.4 48 PRO -75.0 128.9 179.9 18.7 -14.0 49 GLY 65.6 46.0 -180.0 50 SER -96.6 15.2 -180.0 -105.8 51 TRP -95.9 -3.5 -180.0 -82.4 79.1 52 ASP -79.2 -23.6 180.0 -136.2 48.7 53 PRO -75.0 -34.5 -180.0 18.6 -14.0 54 ILE -77.2 -18.2 180.0 -133.1 -114.6 55 THR -72.6 -53.5 180.0 -99.6 56 ALA -72.6 -12.8 180.0 57 ALA -66.9 -71.8 180.0 58 LEU -52.4 -36.6 -180.0 70.4 -64.6 59 SER -60.8 -37.0 -180.0 -145.7 60 GLN -70.0 -21.2 180.0 -119.1 -55.6 -57.2 61 ARG -164.4 66.2 -180.0 46.9 -133.6 -159.5 178.7 62 ALA -67.3 -9.0 180.0 63 MET -97.2 12.9 180.0 73.5 115.2 131.3 64 ILE -102.7 -11.9 180.0 -83.3 177.6 65 LEU -112.5 151.9 -180.0 -8.9 -175.4 66 GLY 179.7 73.1 -180.0 67 LYS -112.8 -7.4 -179.9 -155.6 68.4 -123.3 -138.7 68 SER -155.9 24.3 -180.0 -138.7 69 GLY 138.8 -59.3 180.0 70 GLU -178.0 -65.3 180.0 -154.8 138.1 84.6 71 LEU -124.7 1.5 180.0 -135.9 91.7 72 LYS -51.8 -46.1 -180.0 -107.4 -68.2 -157.7 -160.4 73 THR -58.7 -46.0 180.0 -37.5 74 TRP -59.3 -50.3 180.0 156.0 95.3 75 GLY -37.9 -49.4 -180.0 76 LEU -65.1 -41.1 180.0 -65.1 -18.1 77 VAL -69.5 -56.8 180.0 94.0 78 LEU -71.9 -59.4 -180.0 -147.2 -59.8 79 GLY -36.2 -31.3 180.0 80 ALA -69.3 -47.5 180.0 81 LEU -51.6 -43.5 -179.9 148.7 73.5 82 LYS -69.1 -24.3 180.0 -94.7 102.0 -108.5 -32.4 83 ALA -70.1 -36.4 180.0 84 ALA -63.9 -45.0 180.0 85 ARG -63.4 -34.3 -180.0 -133.1 155.4 173.1 -173.9 86 GLU -77.6 -23.6 180.0 96.5 100.5 -86.8 87 GLU 69.0 -93.3 0.0 -108.0 -107.8 16.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 11.035 -7.289 10.437 2 GLU 9.266 -4.491 12.272 3 ALA 9.301 -2.790 8.891 4 VAL 7.288 -5.474 7.139 5 ILE 4.433 -3.930 9.086 6 LYS 5.640 -0.369 9.523 7 VAL 6.440 -0.376 5.824 8 ILE 3.088 -1.703 4.670 9 SER 1.509 0.815 7.014 10 SER 4.000 3.653 6.763 11 ALA 4.955 2.762 3.211 12 CYS 1.313 3.026 2.217 13 LYS 1.328 6.611 3.431 14 THR 4.947 7.118 4.416 15 TYR 5.714 5.824 0.943 16 CYS 3.573 7.933 -1.358 17 GLY 2.015 9.985 1.415 18 LYS 4.792 10.627 3.905 19 THR 3.257 13.764 5.364 20 SER -0.332 13.254 6.453 21 PRO -1.216 11.652 9.795 22 SER -2.848 8.595 8.274 23 LYS -5.754 9.409 5.990 24 LYS -5.313 6.075 4.252 25 GLU -2.015 4.983 5.755 26 ILE -2.945 1.893 7.733 27 GLY -6.110 1.884 5.657 28 ALA -4.745 1.042 2.229 29 MET -1.830 -0.658 3.942 30 LEU -4.274 -3.278 5.163 31 SER -7.377 -2.657 3.087 32 LEU -5.155 -2.060 0.082 33 LEU -2.934 -5.083 0.580 34 GLN -5.580 -6.949 2.541 35 LYS -7.776 -6.128 -0.431 36 GLU -5.284 -6.774 -3.206 37 GLY -4.321 -10.344 -2.398 38 LEU -2.000 -9.503 0.471 39 LEU -3.898 -11.174 3.287 40 MET -0.707 -13.009 4.167 41 SER 0.156 -10.292 6.657 42 PRO 2.647 -7.417 6.451 43 SER 5.172 -10.070 5.498 44 ASP 4.941 -8.760 1.955 45 LEU 7.800 -6.521 3.025 46 TYR 9.699 -9.678 3.893 47 SER 10.077 -9.869 0.131 48 PRO 11.890 -7.462 -2.200 49 GLY 9.620 -5.817 -4.742 50 SER 6.488 -7.325 -3.244 51 TRP 4.546 -4.208 -4.160 52 ASP 4.169 -5.555 -7.677 53 PRO 1.588 -8.039 -6.377 54 ILE -0.596 -5.283 -4.977 55 THR -0.272 -3.536 -8.319 56 ALA -1.830 -6.276 -10.414 57 ALA -4.193 -6.761 -7.498 58 LEU -6.204 -3.560 -7.689 59 SER -5.742 -3.822 -11.437 60 GLN -7.475 -7.185 -11.321 61 ARG -10.329 -5.461 -9.530 62 ALA -9.815 -1.727 -9.191 63 MET -13.562 -1.680 -8.660 64 ILE -13.210 -3.643 -5.443 65 LEU -11.636 -0.737 -3.599 66 GLY -13.191 2.587 -2.675 67 LYS -11.961 4.292 0.472 68 SER -11.129 7.566 -1.235 69 GLY -12.815 7.242 -4.608 70 GLU -11.871 3.843 -5.978 71 LEU -8.155 3.292 -6.439 72 LYS -7.042 6.666 -5.135 73 THR -6.074 4.968 -1.893 74 TRP -4.102 2.344 -3.778 75 GLY -2.406 5.054 -5.805 76 LEU -0.802 6.253 -2.593 77 VAL -0.008 2.676 -1.644 78 LEU 1.089 1.576 -5.096 79 GLY 2.066 4.983 -6.421 80 ALA 4.595 4.812 -3.611 81 LEU 6.079 1.564 -4.868 82 LYS 6.637 3.296 -8.187 83 ALA 8.130 6.157 -6.209 84 ALA 10.792 3.836 -4.848 85 ARG 11.741 2.766 -8.353 86 GLU 11.867 6.416 -9.347 87 GLU 13.946 7.171 -6.275 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C H H H H H H H H/T T 10 T T/T T T T C C C C C 20 C C C H H H H H H H 30 H/H H H H H H H C C C 40 C C T T T T/S S S S/H H 50 H 3 3 3/H H H H H H H 60 H/T T T T C T T T T C 70 H H H H H H H H/H H H 80 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 T T t 20 S S h H H H H H H 30 H h G G G g T t T T 40 g G G G G G g T T T 50 h H H H H H H H H H 60 h T T t S S S S 70 h H H H H H H H H H 80 H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 10.4 29.8 76.7 2 GLU 0.0 0.0 85.5 3 ALA 24.6 33.9 58.0 4 VAL 116.9 98.4 35.2 5 ILE 81.4 56.7 56.4 6 LYS 33.4 19.3 79.8 7 VAL 74.3 62.6 50.6 8 ILE 139.3 97.1 32.5 9 SER 72.2 86.4 43.8 10 SER 54.5 65.2 59.1 11 ALA 66.4 91.4 35.9 12 CYS 99.2 100.0 50.5 13 LYS 166.0 95.7 56.2 14 THR 53.4 50.0 65.3 15 TYR 141.5 78.2 49.9 16 CYS 62.1 62.6 61.5 17 GLY 16.9 48.5 57.5 18 LYS 39.9 23.0 81.8 19 THR 6.1 5.7 86.5 20 SER 60.0 71.7 52.1 21 PRO 17.0 13.7 84.0 22 SER 53.7 64.3 64.0 23 LYS 47.6 27.5 71.3 24 LYS 164.7 95.0 38.3 25 GLU 112.5 81.2 61.1 26 ILE 54.3 37.9 66.8 27 GLY 8.4 24.2 67.9 28 ALA 72.5 99.8 39.3 29 MET 145.5 91.3 32.5 30 LEU 71.2 48.2 69.1 31 SER 47.4 56.7 62.4 32 LEU 144.2 97.6 30.1 33 LEU 144.1 97.5 36.4 34 GLN 83.0 55.9 53.6 35 LYS 82.1 47.3 70.3 36 GLU 138.6 100.0 38.6 37 GLY 4.6 13.3 81.2 38 LEU 128.5 87.0 51.0 39 LEU 39.7 26.8 82.6 40 MET 2.0 1.2 87.7 41 SER 33.3 39.9 70.6 42 PRO 91.1 73.2 43.7 43 SER 50.9 60.9 57.5 44 ASP 96.6 87.4 48.3 45 LEU 114.2 77.3 52.0 46 TYR 83.6 46.2 69.0 47 SER 39.1 46.8 74.2 48 PRO 9.5 7.6 90.5 49 GLY 3.8 11.0 77.4 50 SER 68.0 81.3 61.6 51 TRP 188.3 91.9 36.2 52 ASP 35.4 32.0 75.0 53 PRO 75.3 60.5 65.3 54 ILE 143.5 100.0 29.7 55 THR 69.5 65.0 54.5 56 ALA 14.9 20.5 73.8 57 ALA 64.3 88.5 58.1 58 LEU 140.8 95.3 34.4 59 SER 28.4 34.0 67.8 60 GLN 22.3 15.0 84.6 61 ARG 105.8 50.7 66.5 62 ALA 40.1 55.2 57.2 63 MET 18.1 11.4 81.5 64 ILE 76.0 53.0 59.7 65 LEU 139.5 94.4 49.1 66 GLY 20.2 58.1 77.8 67 LYS 33.4 19.2 81.3 68 SER 33.4 40.0 73.1 69 GLY 0.2 0.6 74.7 70 GLU 42.8 30.9 78.5 71 LEU 118.8 80.4 42.7 72 LYS 34.3 19.8 79.7 73 THR 104.0 97.3 36.5 74 TRP 155.1 75.6 39.2 75 GLY 18.9 54.2 56.8 76 LEU 107.3 72.6 55.0 77 VAL 118.8 100.0 29.5 78 LEU 147.3 99.6 33.5 79 GLY 13.8 39.7 56.0 80 ALA 72.6 100.0 49.0 81 LEU 130.2 88.1 51.1 82 LYS 97.6 56.3 65.4 83 ALA 38.6 53.2 63.2 84 ALA 29.4 40.5 73.4 85 ARG 33.0 15.8 89.5 86 GLU 29.2 21.1 80.7 87 GLU 4.4 3.1 86.6