Protein Data Bank File : 1jj2p Title : RIBOSOME 03-JUL-01 1JJ2 Number of Amino Acid Residues : 95 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PRO SER SER ASN GLY PRO LEU GLU GLY THR 10 ARG GLY LYS LEU LYS ASN LYS PRO ARG ASP 20 ARG GLY THR SER PRO PRO GLN ARG ALA VAL 30 GLU GLU PHE ASP ASP GLY GLU LYS VAL HIS 40 LEU LYS ILE ASP PRO SER VAL PRO ASN GLY 50 ARG PHE HIS PRO ARG PHE ASP GLY GLN THR 60 GLY THR VAL GLU GLY LYS GLN GLY ASP ALA 70 TYR LYS VAL ASP ILE VAL ASP GLY GLY LYS 80 GLU LYS THR ILE ILE VAL THR ALA ALA HIS 90 LEU ARG ARG GLN GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PRO 0.0 144.9 179.4 -18.6 36.3 2 SER -84.3 -13.5 179.4 59.3 3 SER -145.4 169.9 -177.2 52.5 4 ASN -131.2 28.5 178.4 -156.9 54.3 5 GLY -71.6 169.2 -179.9 6 PRO -61.4 -33.3 -178.5 -25.3 40.9 7 LEU -89.7 10.2 178.8 -50.8 -167.2 8 GLU -61.9 129.3 179.1 171.0 -83.2 -53.9 9 GLY 63.3 29.3 -179.7 10 THR -107.3 9.4 -178.3 64.7 11 ARG -46.1 -49.4 -179.9 -170.1 -129.4 -105.6 -66.6 12 GLY -74.2 -59.8 -178.2 13 LYS -55.6 -21.1 -179.8 54.6 168.1 59.6 169.1 14 LEU -111.3 21.9 179.4 -61.8 -173.3 15 LYS -121.2 138.4 179.3 174.8 -178.7 63.4 163.6 16 ASN -87.4 151.2 175.1 -95.8 153.1 17 LYS -71.5 141.7 -179.5 -114.6 63.4 179.4 -175.6 18 PRO -38.1 -32.9 -179.0 -36.8 45.5 19 ARG -83.9 -20.7 179.5 -85.3 -178.6 56.3 169.2 20 ASP -92.4 6.1 179.9 -48.1 -69.4 21 ARG -65.0 152.4 178.9 -169.5 -118.9 -56.5 174.8 22 GLY 96.7 160.0 179.8 23 THR -40.0 130.4 180.0 -55.0 24 SER -81.2 159.8 179.8 -62.0 25 PRO -66.4 135.4 -179.3 -21.0 38.5 26 PRO -66.7 -23.7 -178.3 -7.1 28.7 27 GLN -46.7 -51.9 -177.7 -170.0 82.9 -26.8 28 ARG -77.0 -10.0 179.3 61.0 -153.9 -168.8 -160.7 29 ALA -86.5 -11.6 -178.5 30 VAL -113.4 -1.7 178.8 -172.1 31 GLU -51.2 146.3 179.7 -175.9 66.6 -73.6 32 GLU -115.8 134.6 179.6 -66.4 -82.6 -51.4 33 PHE -118.6 151.4 179.6 -57.3 92.8 34 ASP -102.2 152.3 178.7 -59.1 -51.6 35 ASP -57.4 130.6 179.8 -57.1 -10.9 36 GLY 105.7 -22.3 179.8 37 GLU -68.2 145.7 178.6 -71.5 -164.1 64.7 38 LYS -91.6 127.7 179.7 -69.7 -73.0 -172.1 174.0 39 VAL -128.2 139.8 178.1 -63.3 40 HIS -86.8 136.4 178.6 -63.1 121.2 41 LEU -96.4 131.1 178.2 -79.8 65.7 42 LYS -162.1 113.7 179.8 176.4 62.5 -160.0 80.5 43 ILE -64.2 138.3 178.1 -67.9 175.4 44 ASP -97.2 111.0 -179.8 -179.6 -25.5 45 PRO -44.4 -35.5 -177.4 -34.4 44.7 46 SER -78.7 -18.1 -179.5 -53.8 47 VAL -102.5 108.9 -179.6 -175.5 48 PRO -59.7 -53.3 -177.1 -25.3 40.7 49 ASN -80.9 172.1 179.3 -46.4 -58.8 50 GLY 62.5 17.1 -179.3 51 ARG -77.9 174.3 178.9 -63.6 -174.4 172.0 -162.7 52 PHE -135.4 169.2 -179.3 50.8 80.2 53 HIS -60.6 123.7 -179.9 -167.9 -67.9 54 PRO -42.7 -24.7 -179.7 -37.4 45.2 55 ARG -63.2 -26.1 -178.1 -90.9 175.2 -168.6 152.3 56 PHE -87.3 1.7 177.8 -53.0 -48.1 57 ASP -59.3 128.7 179.5 -120.9 23.3 58 GLY 102.5 -15.6 179.1 59 GLN -68.9 162.1 177.0 -79.8 -70.5 -44.2 60 THR -134.5 108.9 -178.9 -63.0 61 GLY -112.3 -171.7 -179.6 62 THR -116.9 120.3 178.1 -60.6 63 VAL -62.9 131.3 179.8 167.8 64 GLU -142.0 71.6 -179.7 -66.1 -74.2 44.4 65 GLY 89.6 178.3 178.8 66 LYS -143.1 169.2 -179.0 48.0 164.0 52.4 -165.6 67 GLN -135.1 105.5 -176.8 -169.2 162.4 -60.8 68 GLY 71.1 -138.2 179.1 69 ASP -87.9 -15.8 179.9 -63.3 -38.3 70 ALA -74.1 159.3 178.8 71 TYR -104.0 157.6 177.6 -76.0 92.2 72 LYS -111.8 108.8 -179.1 -77.3 -164.1 -72.4 -179.9 73 VAL -108.8 133.2 179.6 179.1 74 ASP -97.0 128.3 178.5 -63.1 -33.5 75 ILE -132.1 174.2 178.0 61.0 161.5 76 VAL -126.5 107.4 179.4 174.8 77 ASP -85.7 110.4 -178.6 -171.6 -6.7 78 GLY 59.5 -109.4 179.3 79 GLY -110.9 -2.1 -177.6 80 LYS -97.1 138.0 -179.8 -173.7 178.9 -169.3 -173.1 81 GLU -80.6 127.6 178.1 -123.9 162.7 -70.5 82 LYS -136.7 156.4 180.0 -61.2 -177.9 177.5 178.7 83 THR -116.5 128.1 -178.6 -65.7 84 ILE -115.7 129.9 179.1 -59.5 178.6 85 ILE -90.6 116.3 -179.2 -57.5 -57.6 86 VAL -151.9 144.5 -180.0 51.7 87 THR -86.8 164.0 -179.4 58.7 88 ALA -57.9 -34.2 -179.0 89 ALA -53.4 -21.3 -178.8 90 HIS -115.8 14.6 179.7 -49.4 -74.7 91 LEU -120.1 153.4 178.9 -62.7 -179.0 92 ARG -141.8 138.5 178.1 -51.7 -74.0 -73.7 177.2 93 ARG -67.4 134.4 178.9 -82.0 -156.8 -177.3 65.7 94 GLN -73.3 147.5 -179.9 173.7 175.3 49.0 95 GLU 65.6 122.6 0.0 -121.1 70.3 52.4 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PRO 62.892 75.476 93.488 2 SER 66.616 76.123 93.504 3 SER 66.964 73.878 90.440 4 ASN 64.632 72.588 87.757 5 GLY 65.615 69.016 86.978 6 PRO 63.008 66.210 86.773 7 LEU 63.861 64.909 90.256 8 GLU 63.532 68.273 91.966 9 GLY 61.454 67.803 95.111 10 THR 61.018 64.077 94.574 11 ARG 62.778 62.937 97.769 12 GLY 59.610 61.448 99.239 13 LYS 57.664 60.155 96.237 14 LEU 60.657 58.275 94.825 15 LYS 61.764 56.728 98.091 16 ASN 60.640 53.406 99.549 17 LYS 59.620 52.868 103.158 18 PRO 62.536 50.831 104.635 19 ARG 60.523 47.579 104.472 20 ASP 59.472 47.862 100.840 21 ARG 63.158 48.266 100.053 22 GLY 64.784 45.832 97.638 23 THR 63.958 44.244 94.298 24 SER 60.203 44.338 93.696 25 PRO 58.091 41.225 92.865 26 PRO 58.061 40.451 89.071 27 GLN 54.348 39.694 88.951 28 ARG 53.322 43.331 88.490 29 ALA 56.121 44.105 86.044 30 VAL 54.645 41.573 83.624 31 GLU 50.973 42.444 84.110 32 GLU 49.122 42.977 80.807 33 PHE 46.597 45.771 80.198 34 ASP 44.049 46.269 77.438 35 ASP 43.381 49.467 75.499 36 GLY 40.708 51.366 77.382 37 GLU 41.626 50.124 80.854 38 LYS 42.090 52.722 83.584 39 VAL 45.484 52.575 85.271 40 HIS 46.930 54.482 88.231 41 LEU 50.421 55.856 87.684 42 LYS 52.938 55.435 90.486 43 ILE 56.677 55.031 90.125 44 ASP 58.087 52.067 91.992 45 PRO 61.244 53.335 93.738 46 SER 62.949 49.956 93.246 47 VAL 62.414 49.756 89.481 48 PRO 64.794 52.028 87.482 49 ASN 63.258 51.622 84.024 50 GLY 59.948 52.287 82.324 51 ARG 59.426 55.405 84.434 52 PHE 57.661 58.669 83.640 53 HIS 58.166 62.245 84.812 54 PRO 57.581 62.380 88.600 55 ARG 55.008 65.153 88.197 56 PHE 52.560 62.565 86.925 57 ASP 52.752 60.324 90.005 58 GLY 49.172 59.903 91.165 59 GLN 47.554 60.360 87.761 60 THR 45.033 57.813 86.490 61 GLY 45.068 57.431 82.736 62 THR 43.686 55.290 79.959 63 VAL 45.850 52.658 78.300 64 GLU 45.729 53.283 74.570 65 GLY 48.122 50.927 72.865 66 LYS 51.751 50.239 73.617 67 GLN 55.287 50.870 72.368 68 GLY 57.661 47.958 72.710 69 ASP 56.867 46.444 76.103 70 ALA 56.000 49.833 77.550 71 TYR 52.443 51.094 77.523 72 LYS 51.111 54.335 76.093 73 VAL 48.798 55.884 78.664 74 ASP 46.720 58.973 77.990 75 ILE 46.282 61.516 80.779 76 VAL 45.152 65.095 81.213 77 ASP 47.671 67.403 82.900 78 GLY 45.601 70.286 84.185 79 GLY 43.718 71.037 81.002 80 LYS 46.227 69.547 78.576 81 GLU 46.141 66.138 76.930 82 LYS 49.339 64.125 77.252 83 THR 50.602 60.678 76.380 84 ILE 52.847 58.825 78.768 85 ILE 55.176 55.956 77.897 86 VAL 55.262 53.677 80.919 87 THR 55.871 50.045 81.852 88 ALA 53.665 47.766 83.950 89 ALA 56.046 47.953 86.900 90 HIS 54.700 51.459 87.562 91 LEU 51.040 50.832 86.727 92 ARG 48.065 49.431 88.702 93 ARG 44.534 48.553 87.529 94 GLN 41.938 50.994 88.828 95 GLU 39.233 49.519 91.075 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S C C C H 10 H H H H H C T T T T 20 C S S S S H H H H H 30 H/S S S S S S S S S S 40 S S S T T T T C C S 50 S S S/T T T T C S S S 60 S S S S C T T T T/S S 70 S S S S S S/T T T T/S S 80 S S S S S S S/T T T T/S 90 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 10 T T T T t t T T t 20 S S g G G G G g 30 t T T e E E E 40 E e t T T t S S 50 g G G G g T e E 60 E E E E E E E T T E 70 E E E E E E E T T E 80 E E E E E E g G G e 90 E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PRO 36.8 29.6 91.4 2 SER 0.0 0.0 87.8 3 SER 16.0 19.2 81.1 4 ASN 21.6 17.9 83.9 5 GLY 5.8 16.6 67.9 6 PRO 44.4 35.6 66.0 7 LEU 44.6 30.2 68.5 8 GLU 74.8 53.9 71.7 9 GLY 4.0 11.4 83.4 10 THR 97.0 90.8 51.0 11 ARG 14.7 7.0 89.5 12 GLY 5.7 16.5 70.3 13 LYS 97.5 56.2 65.8 14 LEU 134.5 91.0 49.3 15 LYS 59.5 34.3 79.3 16 ASN 93.5 77.3 61.4 17 LYS 18.0 10.4 84.1 18 PRO 17.2 13.8 77.3 19 ARG 0.0 0.0 91.4 20 ASP 31.9 28.8 76.9 21 ARG 32.9 15.7 85.2 22 GLY 4.2 11.9 76.4 23 THR 0.4 0.3 87.1 24 SER 74.6 89.2 64.6 25 PRO 51.6 41.4 71.7 26 PRO 23.2 18.6 75.3 27 GLN 0.0 0.0 84.5 28 ARG 122.4 58.6 72.9 29 ALA 42.0 57.9 57.5 30 VAL 17.1 14.4 83.3 31 GLU 69.8 50.3 70.5 32 GLU 29.9 21.6 86.1 33 PHE 165.7 99.3 40.0 34 ASP 11.5 10.4 81.9 35 ASP 38.0 34.4 72.9 36 GLY 10.3 29.7 75.1 37 GLU 98.7 71.2 62.5 38 LYS 73.2 42.2 77.7 39 VAL 118.8 100.0 35.5 40 HIS 85.7 57.1 67.4 41 LEU 147.8 100.0 35.4 42 LYS 91.6 52.8 69.9 43 ILE 142.8 99.5 45.0 44 ASP 95.2 86.2 64.8 45 PRO 109.0 87.5 75.3 46 SER 67.7 81.0 79.3 47 VAL 85.8 72.2 60.2 48 PRO 36.2 29.1 82.4 49 ASN 6.2 5.1 79.1 50 GLY 22.0 63.1 63.4 51 ARG 153.0 73.2 58.1 52 PHE 156.3 93.7 43.1 53 HIS 93.5 62.2 51.7 54 PRO 115.9 93.1 39.5 55 ARG 55.6 26.6 83.5 56 PHE 141.0 84.5 43.6 57 ASP 104.5 94.6 48.9 58 GLY 0.0 0.0 84.3 59 GLN 92.6 62.3 62.5 60 THR 78.3 73.2 63.7 61 GLY 32.7 94.0 53.6 62 THR 80.0 74.8 65.5 63 VAL 118.3 99.6 43.6 64 GLU 70.2 50.7 68.2 65 GLY 14.9 42.9 68.0 66 LYS 107.0 61.7 68.7 67 GLN 46.3 31.2 69.8 68 GLY 0.0 0.0 86.7 69 ASP 0.0 0.0 88.9 70 ALA 59.7 82.2 54.7 71 TYR 176.9 97.7 48.7 72 LYS 102.6 59.2 65.9 73 VAL 118.8 100.0 39.0 74 ASP 64.4 58.3 63.9 75 ILE 138.8 96.7 37.9 76 VAL 47.2 39.7 73.0 77 ASP 66.6 60.2 61.2 78 GLY 0.0 0.0 87.8 79 GLY 0.0 0.0 77.5 80 LYS 36.6 21.1 79.9 81 GLU 11.9 8.6 78.3 82 LYS 106.7 61.6 61.9 83 THR 53.7 50.2 65.1 84 ILE 133.6 93.1 32.6 85 ILE 77.3 53.9 62.3 86 VAL 118.7 99.9 37.2 87 THR 73.5 68.8 57.0 88 ALA 69.2 95.3 55.0 89 ALA 67.2 92.6 48.6 90 HIS 149.3 99.4 53.8 91 LEU 147.8 100.0 32.8 92 ARG 73.9 35.4 73.5 93 ARG 119.8 57.3 76.3 94 GLN 92.8 62.4 63.2 95 GLU 4.2 3.0 84.9