Protein Data Bank File : 1fjgn Title : RIBOSOME 08-AUG-00 1FJG Number of Amino Acid Residues : 60 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA ARG LYS ALA LEU ILE GLU LYS ALA LYS 10 ARG THR PRO LYS PHE LYS VAL ARG ALA TYR 20 THR ARG CYS VAL ARG CYS GLY ARG ALA ARG 30 SER VAL TYR ARG PHE PHE GLY LEU CYS ARG 40 ILE CYS LEU ARG GLU LEU ALA HIS LYS GLY 50 GLN LEU PRO GLY VAL ARG LYS ALA SER TRP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 118.0 179.4 2 ARG -85.4 129.8 179.7 -74.6 149.6 40.8 -161.1 3 LYS -51.9 -45.5 179.8 -158.4 172.1 -173.2 -179.5 4 ALA -52.6 -43.7 -179.4 5 LEU -68.2 -14.2 178.4 -89.4 -168.7 6 ILE -86.2 54.6 178.7 -58.2 -174.0 7 GLU -92.2 -21.6 179.7 87.5 -142.0 -62.4 8 LYS -46.1 -35.9 179.7 -173.2 -74.1 163.0 176.1 9 ALA -54.9 -13.3 178.6 10 LYS -76.9 92.8 179.3 -68.1 179.4 -174.9 177.2 11 ARG -59.6 14.6 -179.0 53.2 130.8 -171.7 176.1 12 THR -114.0 69.6 179.6 -52.4 13 PRO -101.6 129.7 -179.9 40.0 -43.1 14 LYS -34.2 -43.1 179.7 -77.0 177.6 171.9 -68.9 15 PHE -142.9 143.8 -177.9 -30.6 78.4 16 LYS -64.6 -14.4 179.0 77.3 135.8 46.0 -177.8 17 VAL -69.9 -19.7 -179.8 -80.9 18 ARG -84.1 -15.4 -179.3 -58.3 -159.5 -177.6 -179.7 19 ALA -72.8 114.2 178.7 20 TYR -105.5 -145.4 -177.4 55.9 -81.6 21 THR -117.4 -75.7 -178.1 40.9 22 ARG 78.0 142.2 179.6 -66.9 -80.9 -178.8 -152.7 23 CYS -75.3 140.9 178.7 -178.4 24 VAL -63.3 -42.4 -177.9 177.9 25 ARG -83.2 -64.4 -178.9 172.2 167.3 170.4 168.6 26 CYS -88.1 -15.1 179.2 74.5 27 GLY 84.2 12.5 -179.9 28 ARG -63.6 -168.5 179.6 -156.8 144.6 -178.2 -69.0 29 ALA -162.1 -31.8 -177.3 30 ARG -54.1 -34.3 177.6 -136.1 78.1 -157.8 -140.1 31 SER -156.5 69.3 -179.2 70.3 32 VAL -86.8 140.0 179.4 -71.4 33 TYR -99.5 112.4 -179.6 -76.5 52.7 34 ARG -42.3 -55.6 -178.7 -71.7 176.2 174.4 173.2 35 PHE -52.0 -22.8 -179.1 -175.4 -88.3 36 PHE -116.7 -29.7 -178.3 -68.7 112.0 37 GLY 81.3 3.3 -179.8 38 LEU -104.4 156.5 178.2 -60.8 178.2 39 CYS -85.1 170.9 -178.8 70.4 40 ARG -59.7 -32.7 179.5 66.7 106.6 -179.6 -56.7 41 ILE -75.1 -55.0 -179.8 -65.4 168.6 42 CYS -56.3 -36.6 179.0 -66.0 43 LEU -63.5 -42.8 179.9 154.5 45.1 44 ARG -67.7 -40.3 179.1 -164.0 164.0 88.8 95.6 45 GLU -59.3 -67.3 178.5 -51.6 -174.4 -49.1 46 LEU -52.1 -45.6 179.4 -74.0 163.9 47 ALA -48.4 -56.0 -178.7 48 HIS -56.4 -37.9 -179.6 -73.7 -52.5 49 LYS -67.5 -20.9 -179.3 -79.2 174.1 -179.5 163.9 50 GLY 89.5 15.9 179.9 51 GLN -87.6 -1.6 177.3 -75.6 -172.5 26.9 52 LEU -107.7 97.9 -179.5 -58.9 -176.1 53 PRO -52.1 130.9 179.3 28.8 -42.9 54 GLY 78.6 -26.8 179.7 55 VAL -68.6 150.3 -176.2 -171.8 56 ARG -164.6 -176.2 -179.7 179.3 174.0 170.5 166.7 57 LYS -88.6 118.3 -179.5 -69.6 -110.0 -66.5 170.6 58 ALA -79.8 127.8 179.6 59 SER -139.2 139.3 -179.6 169.3 60 TRP 177.8 142.0 0.0 79.0 103.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 217.219 118.472 28.336 2 ARG 217.452 116.249 31.366 3 LYS 216.914 118.000 34.685 4 ALA 219.662 115.680 35.865 5 LEU 222.063 116.949 33.177 6 ILE 221.695 120.527 34.339 7 GLU 224.363 119.669 36.892 8 LYS 226.530 122.132 34.997 9 ALA 224.992 124.692 37.334 10 LYS 227.336 123.025 39.839 11 ARG 230.115 125.617 39.860 12 THR 231.963 122.662 41.387 13 PRO 233.587 120.784 38.468 14 LYS 236.699 118.665 39.127 15 PHE 238.492 120.688 36.436 16 LYS 237.379 123.824 34.613 17 VAL 237.727 122.184 31.203 18 ARG 234.569 120.225 32.003 19 ALA 232.516 123.368 32.636 20 TYR 230.257 124.072 29.656 21 THR 227.310 126.404 29.048 22 ARG 223.577 125.541 28.603 23 CYS 220.771 128.003 27.836 24 VAL 219.494 130.072 30.745 25 ARG 215.963 129.638 29.371 26 CYS 215.416 126.310 27.539 27 GLY 218.406 124.544 29.052 28 ARG 219.859 123.811 25.636 29 ALA 223.587 123.586 24.986 30 ARG 224.095 123.083 21.281 31 SER 224.293 126.752 20.355 32 VAL 224.193 129.232 23.226 33 TYR 225.256 132.897 22.826 34 ARG 227.572 134.171 25.592 35 PHE 226.372 137.766 25.388 36 PHE 222.859 136.557 26.183 37 GLY 223.195 133.229 27.929 38 LEU 220.391 132.179 25.603 39 CYS 220.377 129.554 22.839 40 ARG 219.801 130.407 19.154 41 ILE 216.145 129.442 19.470 42 CYS 215.391 131.187 22.771 43 LEU 217.205 134.272 21.470 44 ARG 214.936 134.600 18.410 45 GLU 211.808 134.090 20.526 46 LEU 212.702 136.675 23.191 47 ALA 214.205 138.858 20.493 48 HIS 210.865 138.965 18.671 49 LYS 208.906 139.747 21.837 50 GLY 211.025 142.836 22.331 51 GLN 212.273 141.445 25.598 52 LEU 215.888 141.771 24.489 53 PRO 216.596 145.502 25.039 54 GLY 218.274 147.246 22.144 55 VAL 218.226 144.018 20.129 56 ARG 216.367 144.268 16.847 57 LYS 216.010 143.059 13.261 58 ALA 219.149 143.724 11.218 59 SER 218.539 144.928 7.664 60 TRP 220.961 146.269 5.066 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C T T T T C C C C C 10 S S S S T T T T/S S S 20 S S S/T T T T S S S S/S 30 S S S/T T T T C C H H 40 H H H H H H H H H H 50 S S S S/S S S S/S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T T T T T T t 10 S S g G G G g 20 S S S t T 30 T B t T T T t h H 40 H H H H H H H H H h 50 t t T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 44.9 61.8 81.8 2 ARG 61.6 29.5 72.2 3 LYS 0.0 0.0 88.2 4 ALA 7.6 10.5 83.5 5 LEU 92.0 62.3 80.7 6 ILE 81.8 57.0 64.0 7 GLU 59.6 43.0 69.6 8 LYS 105.2 60.7 61.7 9 ALA 14.9 20.5 75.2 10 LYS 39.0 22.5 79.4 11 ARG 0.0 0.0 91.7 12 THR 10.9 10.2 76.2 13 PRO 86.0 69.1 67.4 14 LYS 31.6 18.2 79.9 15 PHE 63.5 38.1 73.6 16 LYS 10.1 5.8 82.1 17 VAL 12.2 10.3 74.2 18 ARG 67.5 32.3 69.7 19 ALA 42.9 59.1 60.4 20 TYR 104.6 57.8 68.9 21 THR 43.2 40.4 59.8 22 ARG 174.6 83.6 42.6 23 CYS 99.2 100.0 42.0 24 VAL 21.8 18.4 75.2 25 ARG 131.8 63.1 58.0 26 CYS 58.9 59.4 49.7 27 GLY 29.5 84.7 55.9 28 ARG 147.1 70.4 53.8 29 ALA 50.4 69.4 59.5 30 ARG 18.0 8.6 89.6 31 SER 46.6 55.7 72.5 32 VAL 105.5 88.8 57.7 33 TYR 71.3 39.4 69.5 34 ARG 0.0 0.0 89.4 35 PHE 12.1 7.3 76.6 36 PHE 128.7 77.1 39.3 37 GLY 13.4 38.6 66.5 38 LEU 134.1 90.7 36.9 39 CYS 99.2 100.0 35.3 40 ARG 90.2 43.2 71.0 41 ILE 67.8 47.2 68.7 42 CYS 97.3 98.1 39.4 43 LEU 120.3 81.4 36.6 44 ARG 42.9 20.5 77.4 45 GLU 67.2 48.5 68.4 46 LEU 123.9 83.8 48.2 47 ALA 55.8 76.9 50.7 48 HIS 73.0 48.6 69.7 49 LYS 72.3 41.7 80.9 50 GLY 3.5 10.1 87.7 51 GLN 53.6 36.1 68.1 52 LEU 134.6 91.1 33.7 53 PRO 16.4 13.2 85.9 54 GLY 0.0 0.0 85.8 55 VAL 80.9 68.1 54.1 56 ARG 13.5 6.5 87.1 57 LYS 19.4 11.2 82.0 58 ALA 13.0 17.9 75.0 59 SER 6.1 7.4 81.5 60 TRP 13.3 6.5 89.7