Protein Data Bank File : 1fjgl Title : RIBOSOME 08-AUG-00 1FJG Number of Amino Acid Residues : 125 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PRO THR ILE ASN GLN LEU VAL ARG LYS GLY 10 ARG GLU LYS VAL ARG LYS LYS SER LYS VAL 20 PRO ALA LEU LYS GLY ALA PRO PHE ARG ARG 30 GLY VAL CYS THR VAL VAL ARG THR VAL THR 40 PRO LYS LYS PRO ASN SER ALA LEU ARG LYS 50 VAL ALA LYS VAL ARG LEU THR SER GLY TYR 60 GLU VAL THR ALA TYR ILE PRO GLY GLU GLY 70 HIS ASN LEU GLN GLU HIS SER VAL VAL LEU 80 ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO 90 GLY VAL ARG TYR HIS ILE VAL ARG GLY VAL 100 TYR ASP ALA ALA GLY VAL LYS ASP ARG LYS 110 LYS SER ARG SER LYS TYR GLY THR LYS LYS 120 PRO LYS GLU ALA ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PRO 0.0 153.1 178.4 -4.1 22.1 2 THR -74.9 162.6 -179.5 68.9 3 ILE -63.5 -29.2 -179.5 -88.4 -58.9 4 ASN -68.7 -38.7 179.4 -165.5 59.6 5 GLN -65.7 -40.8 179.5 -62.2 178.7 -55.5 6 LEU -60.3 -30.9 -179.9 -82.8 174.8 7 VAL -77.0 -35.2 -179.9 169.4 8 ARG -77.1 -47.5 -176.7 -55.6 -159.5 -70.3 108.0 9 LYS -106.2 -25.8 178.8 -55.0 -178.4 174.6 178.2 10 GLY 61.0 177.2 -180.0 11 ARG -92.2 156.9 180.0 -62.1 -65.8 -174.2 173.9 12 GLU -104.8 121.8 -179.1 -175.4 174.9 71.0 13 LYS -65.9 136.2 179.0 -58.7 -91.0 -159.7 60.2 14 VAL -70.1 138.2 179.8 172.1 15 ARG -104.9 132.2 180.0 -44.8 173.0 -166.3 175.6 16 LYS -89.6 133.6 -179.3 -69.3 -168.0 174.9 -173.0 17 LYS -109.6 121.1 -179.2 172.5 55.1 -176.5 176.4 18 SER -63.3 145.9 179.6 173.1 19 LYS -112.5 18.2 -177.8 -64.6 175.3 -178.2 178.2 20 VAL -152.5 71.5 179.4 167.3 21 PRO -69.8 86.1 178.0 -31.8 41.9 22 ALA -110.7 40.8 -178.9 23 LEU 29.7 -139.1 179.4 -142.5 75.4 24 LYS -1.5 33.6 -177.6 -79.0 -171.6 178.1 179.5 25 GLY 30.5 44.8 -177.6 26 ALA -82.7 158.3 179.5 27 PRO -76.3 -41.2 179.6 -20.6 37.6 28 PHE -143.7 168.5 -179.2 -47.0 -74.6 29 ARG -153.8 136.8 179.6 -149.6 61.5 160.2 164.7 30 ARG -98.3 154.8 -179.7 65.2 151.5 -171.8 172.8 31 GLY -160.6 -172.1 179.5 32 VAL -122.5 140.6 179.4 -167.1 33 CYS -64.0 148.0 -179.7 -65.7 34 THR -119.6 -50.2 178.1 -85.9 35 VAL -131.6 141.2 178.2 -172.2 36 VAL -123.8 79.6 -177.2 176.0 37 ARG -81.0 -169.1 178.2 -156.2 177.7 -40.5 156.4 38 THR -136.5 138.4 -177.7 -176.5 39 VAL -133.1 144.5 179.0 160.5 40 THR -93.0 145.8 -180.0 75.3 41 PRO -68.6 -174.7 179.9 -19.3 38.1 42 LYS -118.6 -164.7 178.7 74.9 156.8 174.9 -172.4 43 LYS 28.1 -91.4 -179.1 -92.5 48.5 -90.3 -175.3 44 PRO -113.1 9.8 -179.5 47.4 -37.3 45 ASN -108.0 153.4 179.9 -83.1 176.6 46 SER -140.4 128.4 180.0 176.4 47 ALA 177.9 176.7 179.7 48 LEU -116.6 73.7 -178.9 -59.8 -172.7 49 ARG -53.0 137.5 179.2 -81.0 62.4 -157.0 -76.8 50 LYS -92.2 114.5 -178.9 -73.8 63.4 173.4 177.6 51 VAL -114.1 174.9 178.3 -161.9 52 ALA -158.3 135.5 178.4 53 LYS -85.4 126.8 -177.6 -101.8 -175.5 -176.8 -178.4 54 VAL -122.9 131.1 177.1 -157.9 55 ARG -95.7 111.5 -178.1 174.2 126.6 57.8 -148.0 56 LEU -83.1 159.5 177.8 -70.9 -45.0 57 THR -69.2 -20.4 179.8 57.5 58 SER -76.7 1.6 179.8 63.6 59 GLY 83.7 6.3 178.9 60 TYR -105.2 141.8 179.3 -75.0 65.2 61 GLU -110.5 102.5 -178.0 -59.9 58.1 48.9 62 VAL -125.3 165.8 -179.9 -46.7 63 THR -93.7 133.7 -178.9 -135.7 64 ALA -133.2 146.2 179.8 65 TYR -80.8 148.4 178.8 -170.3 74.8 66 ILE -117.4 91.6 -179.7 -50.4 169.4 67 PRO -65.4 158.0 -179.7 38.2 -45.0 68 GLY 113.0 170.5 179.9 69 GLU -80.5 -20.8 178.8 -69.0 84.7 67.0 70 GLY -165.9 158.0 179.7 71 HIS -137.8 -175.7 -178.5 68.6 -81.1 72 ASN -134.1 42.0 -178.7 63.3 -61.2 73 LEU -100.2 122.7 179.5 -62.7 174.0 74 GLN -103.4 -168.0 -178.1 -57.4 170.8 -56.7 75 GLU -63.1 -36.2 -179.5 -172.3 170.5 75.7 76 HIS -118.9 41.7 -177.3 -53.9 74.0 77 SER -54.5 -47.7 -178.9 -79.3 78 VAL 75.6 113.5 -178.1 166.7 79 VAL -158.2 174.4 -179.9 58.7 80 LEU -100.0 131.0 179.7 -163.3 61.9 81 ILE -102.1 142.1 -178.9 -74.0 -176.8 82 ARG -125.0 -4.0 180.0 75.6 173.3 176.8 54.2 83 GLY 76.8 131.0 -179.0 84 GLY 156.0 113.5 -179.1 85 ARG -60.9 177.0 176.8 84.4 -177.6 -64.0 -162.9 86 VAL -140.6 75.2 -179.5 171.8 87 LYS -13.2 -52.2 -179.0 177.8 73.8 172.8 -173.3 88 ASP -69.0 -21.3 -179.8 -92.2 6.7 89 LEU -119.9 96.4 179.7 -44.9 177.0 90 PRO -59.5 144.9 179.5 -30.0 43.5 91 GLY 98.2 -27.2 178.9 92 VAL -88.3 105.7 -179.1 -167.5 93 ARG -115.4 5.5 178.9 -67.0 -161.0 -79.4 175.5 94 TYR -142.0 152.4 177.9 -40.5 74.9 95 HIS -107.8 152.6 176.9 -81.0 59.4 96 ILE -88.7 146.0 -179.4 -68.6 179.4 97 VAL -94.0 115.7 -179.7 168.6 98 ARG -79.1 136.4 179.8 -51.1 -141.2 43.5 175.7 99 GLY 103.7 1.5 178.9 100 VAL -126.7 135.7 -179.6 171.0 101 TYR 60.9 -144.0 -177.8 -61.0 145.6 102 ASP -76.4 8.0 178.8 -57.6 174.9 103 ALA -94.5 101.1 -179.7 104 ALA -64.1 152.8 179.1 105 GLY -80.1 155.3 180.0 106 VAL -51.3 135.9 -179.8 174.9 107 LYS -87.8 137.3 179.3 -60.1 177.2 -177.2 176.6 108 ASP 79.9 -10.4 179.9 -72.4 169.6 109 ARG -51.5 123.8 -179.6 -116.7 -68.5 167.2 169.6 110 LYS -116.6 -14.0 -179.1 -61.5 -169.4 73.1 -176.2 111 LYS -100.5 -111.5 -179.4 -59.8 -132.3 -177.5 -177.8 112 SER -64.1 69.6 -176.9 -43.4 113 ARG -81.1 -24.2 179.7 -40.9 -178.7 -31.9 -99.3 114 SER -48.4 -44.1 177.1 173.9 115 LYS -89.5 150.3 -177.8 -39.1 174.3 169.9 -174.8 116 TYR 79.8 8.2 179.3 -55.3 131.7 117 GLY 22.2 53.4 178.2 118 THR -107.3 123.6 -179.1 84.0 119 LYS -55.0 159.3 179.2 -44.5 -91.1 -171.9 -170.3 120 LYS -66.8 134.1 179.9 163.1 108.6 85.2 164.9 121 PRO -61.8 147.8 -179.3 -25.3 42.3 122 LYS -86.4 55.1 177.9 -67.3 -176.0 178.6 -179.8 123 GLU -73.6 -32.8 179.6 -58.5 -178.5 -58.1 124 ALA -57.9 -13.9 179.4 125 ALA -78.3 -111.9 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PRO 150.324 103.194 -25.418 2 THR 147.108 104.394 -27.021 3 ILE 143.921 103.235 -25.296 4 ASN 143.317 100.957 -28.240 5 GLN 146.670 99.280 -27.744 6 LEU 145.920 98.856 -24.055 7 VAL 142.793 97.047 -25.089 8 ARG 144.624 94.831 -27.523 9 LYS 147.712 94.124 -25.434 10 GLY 146.953 95.332 -21.918 11 ARG 149.459 95.740 -19.101 12 GLU 151.726 92.960 -17.772 13 LYS 151.473 92.097 -14.069 14 VAL 154.772 92.146 -12.195 15 ARG 156.048 88.728 -11.001 16 LYS 157.815 88.363 -7.641 17 LYS 160.998 86.274 -7.502 18 SER 162.004 84.579 -4.235 19 LYS 165.408 85.221 -2.743 20 VAL 165.238 82.192 -0.488 21 PRO 164.482 78.829 -2.059 22 ALA 163.827 77.048 1.260 23 LEU 161.306 75.294 -0.993 24 LYS 157.899 74.777 0.667 25 GLY 157.820 78.561 1.020 26 ALA 158.878 77.612 4.519 27 PRO 159.906 79.883 7.396 28 PHE 162.839 77.597 8.245 29 ARG 164.253 74.332 6.990 30 ARG 166.536 71.795 8.657 31 GLY 169.537 70.081 7.139 32 VAL 172.948 68.669 8.009 33 CYS 176.318 70.339 7.919 34 THR 178.578 68.968 5.217 35 VAL 181.502 71.300 5.429 36 VAL 181.974 73.827 8.190 37 ARG 184.351 76.263 6.534 38 THR 185.660 79.772 7.162 39 VAL 185.140 82.408 4.470 40 THR 186.697 85.789 3.719 41 PRO 184.520 88.872 3.031 42 LYS 184.538 90.927 -0.169 43 LYS 185.039 94.416 -1.501 44 PRO 186.257 96.378 1.530 45 ASN 185.928 93.922 4.369 46 SER 188.321 91.487 5.952 47 ALA 187.548 88.823 8.522 48 LEU 187.072 85.066 8.636 49 ARG 183.298 84.623 8.431 50 LYS 182.029 81.241 9.647 51 VAL 179.952 79.478 7.003 52 ALA 178.547 75.940 6.632 53 LYS 177.403 73.726 3.752 54 VAL 173.984 72.393 4.599 55 ARG 172.102 69.579 2.912 56 LEU 168.444 70.524 3.419 57 THR 165.418 68.292 3.889 58 SER 164.142 70.337 0.963 59 GLY 166.726 68.565 -1.152 60 TYR 168.967 71.629 -1.469 61 GLU 172.610 71.730 -0.429 62 VAL 173.263 75.348 0.447 63 THR 175.741 77.569 2.241 64 ALA 174.600 79.250 5.485 65 TYR 176.115 81.797 7.861 66 ILE 176.806 80.960 11.537 67 PRO 176.204 84.135 13.611 68 GLY 177.698 84.633 17.082 69 GLU 181.182 84.863 18.608 70 GLY 181.769 81.107 18.421 71 HIS 180.116 77.800 17.578 72 ASN 180.006 74.029 17.938 73 LEU 179.273 72.860 14.434 74 GLN 181.077 69.746 13.190 75 GLU 180.687 67.823 9.953 76 HIS 177.333 66.225 10.714 77 SER 175.877 68.845 12.991 78 VAL 172.238 69.047 11.786 79 VAL 170.557 72.388 12.111 80 LEU 167.788 74.853 11.194 81 ILE 168.212 77.401 8.392 82 ARG 166.271 80.670 8.389 83 GLY 167.258 82.741 5.413 84 GLY 169.046 86.079 5.414 85 ARG 171.770 87.078 2.968 86 VAL 175.177 88.123 4.279 87 LYS 176.080 91.181 2.215 88 ASP 179.813 90.529 2.599 89 LEU 179.770 86.940 1.344 90 PRO 178.087 86.548 -2.034 91 GLY 176.385 83.168 -2.186 92 VAL 175.503 83.121 1.481 93 ARG 171.715 83.655 1.590 94 TYR 170.559 82.013 4.816 95 HIS 171.571 82.138 8.470 96 ILE 171.766 79.150 10.762 97 VAL 169.541 79.422 13.831 98 ARG 171.415 79.236 17.111 99 GLY 169.620 77.499 19.918 100 VAL 168.042 74.878 17.685 101 TYR 169.239 71.320 17.091 102 ASP 172.983 70.748 17.362 103 ALA 173.657 74.475 17.071 104 ALA 174.403 75.650 20.601 105 GLY 173.339 79.152 21.502 106 VAL 176.071 81.754 21.915 107 LYS 177.886 81.333 25.222 108 ASP 178.032 84.329 27.576 109 ARG 175.635 86.323 25.383 110 LYS 173.956 88.869 27.630 111 LYS 172.152 91.247 25.273 112 SER 170.142 90.558 22.127 113 ARG 169.829 86.904 23.222 114 SER 166.425 86.218 21.671 115 LYS 168.617 85.955 18.607 116 TYR 171.646 83.740 19.396 117 GLY 169.229 81.623 21.404 118 THR 170.895 81.928 24.806 119 LYS 168.595 81.423 27.806 120 LYS 168.230 84.181 30.379 121 PRO 171.095 84.187 32.928 122 LYS 170.060 83.094 36.403 123 GLU 170.800 86.419 38.067 124 ALA 167.239 86.157 39.344 125 ALA 168.715 83.353 41.441 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 S 10 S S S S S S S S S S 20 C T T T T C S S S S 30 S S S S/S S S S S/S S S 40 S S/T T T T/S S S S/S S S 50 S S S S S T T T T/S S 60 S S S/S S S S S S S C 70 S S S S S S S S S S 80 S S/S S S S S/T T T T C 90 S S S S/S S S S S S T 100 T T T/S S S S C S S S 110 S T T T T S S S S/S S 120 S S S S/S S 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 S 20 t T T T t S E E 30 E E E E E e E E 40 t T T t E E 50 E E E E E E e T t e 60 E E E E E e S S 70 t T T t E E 80 E t T T t T 90 T t E E e t T T t 100 T T t S S 110 S S t T T T T t 120 g G G G g Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PRO 63.3 50.8 78.7 2 THR 26.4 24.7 75.9 3 ILE 19.0 13.2 73.9 4 ASN 26.3 21.7 74.4 5 GLN 79.7 53.6 67.2 6 LEU 107.3 72.6 59.7 7 VAL 23.2 19.5 78.1 8 ARG 90.8 43.5 75.7 9 LYS 42.7 24.6 88.3 10 GLY 13.3 38.2 72.0 11 ARG 61.3 29.3 70.4 12 GLU 18.8 13.6 90.9 13 LYS 0.0 0.0 92.0 14 VAL 3.4 2.8 86.9 15 ARG 23.4 11.2 90.2 16 LYS 0.0 0.0 89.7 17 LYS 22.8 13.1 86.7 18 SER 27.9 33.4 72.5 19 LYS 16.3 9.4 87.6 20 VAL 72.9 61.4 60.5 21 PRO 86.5 69.5 75.3 22 ALA 64.3 88.6 54.1 23 LEU 65.9 44.6 71.9 24 LYS 33.6 19.4 82.2 25 GLY 0.0 0.0 85.9 26 ALA 64.3 88.5 61.8 27 PRO 28.0 22.5 72.9 28 PHE 82.1 49.2 57.1 29 ARG 172.2 82.5 49.3 30 ARG 80.7 38.6 66.2 31 GLY 31.7 91.1 49.1 32 VAL 65.9 55.4 61.6 33 CYS 99.2 100.0 42.1 34 THR 64.5 60.4 62.4 35 VAL 62.7 52.8 66.9 36 VAL 104.6 88.0 56.1 37 ARG 101.7 48.7 62.5 38 THR 44.3 41.5 58.6 39 VAL 84.2 70.9 52.9 40 THR 26.3 24.6 68.9 41 PRO 123.7 99.4 55.3 42 LYS 107.0 61.7 61.9 43 LYS 39.2 22.6 70.9 44 PRO 35.8 28.7 77.0 45 ASN 62.5 51.7 73.6 46 SER 4.1 4.9 76.3 47 ALA 32.6 44.9 73.1 48 LEU 46.6 31.5 76.6 49 ARG 152.9 73.2 49.4 50 LYS 81.3 46.9 71.2 51 VAL 115.3 97.1 40.9 52 ALA 71.8 98.8 42.3 53 LYS 82.1 47.3 71.1 54 VAL 118.8 100.0 44.7 55 ARG 71.2 34.1 78.7 56 LEU 142.9 96.7 47.0 57 THR 57.7 53.9 71.2 58 SER 81.5 97.5 50.5 59 GLY 1.1 3.2 82.9 60 TYR 93.0 51.4 64.9 61 GLU 65.7 47.4 68.9 62 VAL 92.2 77.6 50.4 63 THR 79.0 73.9 52.1 64 ALA 72.6 100.0 41.6 65 TYR 137.2 75.8 45.6 66 ILE 142.2 99.1 35.6 67 PRO 103.0 82.8 51.2 68 GLY 32.9 94.4 60.1 69 GLU 34.0 24.5 79.3 70 GLY 2.5 7.1 81.7 71 HIS 120.5 80.2 48.7 72 ASN 60.9 50.4 66.2 73 LEU 147.2 99.6 34.2 74 GLN 4.1 2.7 88.7 75 GLU 43.8 31.6 75.3 76 HIS 34.0 22.6 77.5 77 SER 76.8 91.9 49.7 78 VAL 75.0 63.1 58.1 79 VAL 118.8 100.0 39.2 80 LEU 118.3 80.0 40.8 81 ILE 140.7 98.0 33.5 82 ARG 119.5 57.2 61.0 83 GLY 33.4 96.0 49.4 84 GLY 10.3 29.5 76.8 85 ARG 69.5 33.3 77.6 86 VAL 98.7 83.1 52.0 87 LYS 47.0 27.1 86.2 88 ASP 92.1 83.3 53.2 89 LEU 145.3 98.3 33.7 90 PRO 42.1 33.8 77.8 91 GLY 0.0 0.0 73.6 92 VAL 113.7 95.7 44.5 93 ARG 103.0 49.3 67.1 94 TYR 169.4 93.6 47.2 95 HIS 121.5 80.9 56.8 96 ILE 143.4 100.0 30.1 97 VAL 90.2 75.9 50.1 98 ARG 203.7 97.5 46.7 99 GLY 22.8 65.6 71.1 100 VAL 73.4 61.8 57.3 101 TYR 97.1 53.7 59.6 102 ASP 37.2 33.7 71.8 103 ALA 70.7 97.4 55.9 104 ALA 36.1 49.7 75.5 105 GLY 32.2 92.6 65.4 106 VAL 117.1 98.6 56.0 107 LYS 17.8 10.2 85.5 108 ASP 0.0 0.0 88.3 109 ARG 157.9 75.6 58.6 110 LYS 55.0 31.7 75.4 111 LYS 12.8 7.4 86.9 112 SER 25.8 30.9 67.8 113 ARG 158.1 75.7 64.1 114 SER 0.0 0.0 80.6 115 LYS 25.7 14.8 78.6 116 TYR 134.2 74.1 54.4 117 GLY 17.9 51.5 72.4 118 THR 92.2 86.3 59.4 119 LYS 0.0 0.0 93.5 120 LYS 42.9 24.7 85.2 121 PRO 82.2 66.0 62.8 122 LYS 12.2 7.0 85.9 123 GLU 27.3 19.7 80.9 124 ALA 0.0 0.0 83.1 125 ALA 20.1 27.7 70.1