Protein Data Bank File : 1pfia Title : COMPLEX(VIRAL COAT PROTEIN/DNA) 06-APR-94 1PFI Number of Amino Acid Residues : 46 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY VAL ILE ASP THR SER ALA VAL GLU SER 10 ALA ILE THR ASP GLY GLN GLY ASP MET LYS 20 ALA ILE GLY GLY TYR ILE VAL GLY ALA LEU 30 VAL ILE LEU ALA VAL ALA GLY LEU ILE TYR 40 SER MET LEU ARG LYS ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 27.5 -179.9 2 VAL -114.8 -39.8 180.0 172.0 3 ILE -65.1 -91.0 -180.0 -64.2 -58.9 4 ASP -65.0 -20.6 179.9 -172.5 38.6 5 THR -64.9 -40.0 180.0 -86.9 6 SER -65.2 -39.8 179.9 69.4 7 ALA -65.1 -39.8 179.9 8 VAL -65.0 -40.1 -179.9 12.7 9 GLU -65.0 -40.2 -179.8 -177.9 -177.4 -2.3 10 SER -64.9 -39.9 -180.0 69.3 11 ALA -65.0 -40.0 -179.9 12 ILE -65.1 -40.1 -180.0 100.1 128.8 13 THR -64.8 -40.2 -180.0 -61.4 14 ASP -65.0 -40.1 -179.9 -88.5 38.8 15 GLY -75.0 -40.0 180.0 16 GLN -75.0 -5.0 180.0 -178.0 -177.3 177.8 17 GLY -69.9 -20.1 -180.0 18 ASP -65.1 -39.9 180.0 3.4 -79.9 19 MET -65.1 -40.0 179.9 113.4 137.5 13.1 20 LYS -64.9 -40.1 180.0 -36.7 -140.4 173.1 172.9 21 ALA -65.0 -40.0 -180.0 22 ILE -65.0 -40.0 -180.0 117.3 -2.9 23 GLY -60.1 -20.0 180.0 24 GLY -60.0 -20.0 180.0 25 TYR -65.1 -40.0 180.0 -169.2 7.7 26 ILE -64.9 -40.0 180.0 104.0 110.7 27 VAL -65.1 -39.9 -179.8 156.7 28 GLY -75.0 -5.0 179.9 29 ALA -65.0 -40.1 180.0 30 LEU -64.8 -40.1 -179.9 -57.8 -175.4 31 VAL -65.1 -39.9 179.9 -145.9 32 ILE -64.9 -40.1 -180.0 -52.2 166.6 33 LEU -65.1 -39.9 -180.0 112.7 83.5 34 ALA -65.1 -40.1 180.0 35 VAL -64.9 -40.0 180.0 -48.3 36 ALA -65.0 -39.9 -179.9 37 GLY -65.2 -39.9 -179.9 38 LEU -65.1 -39.9 -179.9 -68.6 -104.8 39 ILE -65.0 -40.0 -179.9 -56.3 0.0 40 TYR -65.0 -40.1 -180.0 105.5 55.9 41 SER -65.0 -40.1 -180.0 69.5 42 MET -65.0 -40.0 -179.9 85.2 145.7 -165.2 43 LEU -65.0 -40.0 -180.0 -178.8 -83.6 44 ARG -65.0 -39.9 -180.0 142.0 -177.1 -177.0 -134.2 45 LYS -65.1 -40.1 -180.0 -101.8 -53.8 177.2 172.8 46 ALA -65.1 0.6 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 17.758 -21.270 58.012 2 VAL 20.467 -18.726 56.827 3 ILE 23.710 -20.884 56.604 4 ASP 22.874 -24.192 54.712 5 THR 19.388 -22.558 54.078 6 SER 21.043 -19.859 51.802 7 ALA 22.987 -22.641 49.877 8 VAL 19.689 -24.693 49.480 9 GLU 17.830 -21.496 48.230 10 SER 20.738 -20.757 45.735 11 ALA 20.645 -24.459 44.500 12 ILE 16.767 -24.249 44.097 13 THR 17.065 -20.905 42.048 14 ASP 19.823 -22.520 39.808 15 GLY 17.618 -25.712 39.363 16 GLN 14.318 -23.644 39.102 17 GLY 16.267 -21.486 36.499 18 ASP 15.388 -24.266 33.903 19 MET 11.609 -23.325 34.151 20 LYS 12.420 -19.517 33.600 21 ALA 14.665 -20.432 30.540 22 ILE 11.863 -22.767 29.157 23 GLY 9.223 -19.943 29.681 24 GLY 11.536 -17.920 27.278 25 TYR 9.811 -20.058 24.507 26 ILE 6.425 -18.235 25.183 27 VAL 8.237 -14.779 25.038 28 GLY 10.003 -15.827 21.721 29 ALA 6.433 -16.861 20.534 30 LEU 5.621 -13.142 19.675 31 VAL 8.999 -12.827 17.750 32 ILE 8.248 -16.150 15.843 33 LEU 4.659 -14.872 14.999 34 ALA 6.139 -11.464 13.795 35 VAL 8.789 -13.360 11.644 36 ALA 5.987 -15.635 10.163 37 GLY 3.805 -12.489 9.403 38 LEU 6.873 -10.740 7.741 39 ILE 7.600 -13.961 5.655 40 TYR 3.843 -14.151 4.610 41 SER 3.899 -10.370 3.644 42 MET 7.184 -10.916 1.611 43 LEU 5.600 -14.018 -0.150 44 ARG 2.380 -11.952 -0.934 45 LYS 4.570 -9.029 -2.311 46 ALA 6.620 -11.556 -4.468 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C H H H H H H H H 10 H H H H H H H/H H H H 20 H H H H 3 3 3 H H H 30 H H H H H H H H H H 40 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 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 H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 5.8 16.8 83.4 2 VAL 0.0 0.0 83.5 3 ILE 0.0 0.0 84.9 4 ASP 3.9 3.6 74.4 5 THR 54.7 51.2 65.0 6 SER 28.9 34.6 80.8 7 ALA 21.6 29.8 86.5 8 VAL 42.3 35.6 69.1 9 GLU 29.8 21.5 73.3 10 SER 21.1 25.2 78.6 11 ALA 15.1 20.8 80.0 12 ILE 53.4 37.2 73.0 13 THR 36.0 33.6 77.3 14 ASP 8.3 7.6 82.8 15 GLY 2.0 5.8 83.7 16 GLN 67.5 45.4 63.0 17 GLY 16.6 47.8 71.5 18 ASP 21.3 19.3 74.3 19 MET 39.8 25.0 73.3 20 LYS 52.3 30.2 75.7 21 ALA 9.7 13.3 83.5 22 ILE 39.2 27.3 72.3 23 GLY 16.7 48.0 62.7 24 GLY 10.1 28.9 74.7 25 TYR 19.5 10.8 82.8 26 ILE 17.4 12.1 72.1 27 VAL 13.7 11.5 76.4 28 GLY 14.8 42.5 63.2 29 ALA 32.4 44.6 68.0 30 LEU 22.9 15.5 77.8 31 VAL 25.0 21.1 71.2 32 ILE 49.5 34.5 66.1 33 LEU 34.3 23.2 72.4 34 ALA 23.6 32.5 68.2 35 VAL 46.7 39.3 57.0 36 ALA 20.7 28.5 70.4 37 GLY 14.7 42.3 60.8 38 LEU 32.9 22.3 75.3 39 ILE 47.9 33.4 62.8 40 TYR 57.3 31.6 69.6 41 SER 44.8 53.5 65.8 42 MET 38.4 24.1 73.6 43 LEU 27.7 18.8 74.4 44 ARG 52.1 24.9 76.2 45 LYS 22.6 13.1 87.1 46 ALA 16.0 22.1 81.9