Protein Data Bank File : 1rip Title : RIBOSOMAL PROTEIN 17-AUG-93 1RIP Number of Amino Acid Residues : 81 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLN ARG LYS VAL TYR VAL GLY ARG VAL VAL 10 SER ASP LYS MET ASP LYS THR ILE THR VAL 20 LEU VAL GLU THR TYR LYS LYS HIS PRO LEU 30 TYR GLY LYS ARG VAL LYS TYR SER LYS LYS 40 TYR LYS ALA HIS ASP GLU HIS ASN GLU ALA 50 LYS VAL GLY ASP ILE VAL LYS ILE MET GLU 60 THR ARG PRO LEU SER ALA THR LYS ARG PHE 70 ARG LEU VAL GLU ILE VAL GLU LYS ALA VAL 80 ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLN 0.0 140.0 179.9 -76.1 -107.5 -48.7 2 ARG -61.0 -77.8 179.7 -112.3 167.9 -149.2 164.6 3 LYS -135.4 -154.6 179.5 -52.6 154.1 -130.8 -125.5 4 VAL 101.8 -152.0 -179.7 -45.8 5 TYR 156.0 -153.4 -177.6 58.5 84.6 6 VAL 154.7 159.5 175.8 32.3 7 GLY 129.3 -124.9 -174.1 8 ARG -29.0 138.1 171.9 -112.9 -113.7 -68.6 166.4 9 VAL 74.1 -101.9 -173.4 -126.5 10 VAL 98.9 -17.3 176.4 -160.8 11 SER -141.6 -164.8 178.0 118.6 12 ASP 139.2 -36.7 -177.3 111.8 88.8 13 LYS 93.8 144.8 -178.1 -148.5 -119.5 -172.2 -35.5 14 MET 156.5 46.7 179.9 172.5 101.5 -58.8 15 ASP 35.6 27.6 180.0 -71.4 -0.3 16 LYS -123.0 -60.9 176.7 -77.6 -73.1 171.3 -147.4 17 THR 97.3 100.1 178.9 78.8 18 ILE 88.9 156.3 179.9 -145.0 150.0 19 THR 145.6 -94.3 -174.7 -72.5 20 VAL 158.3 -139.1 -176.1 52.5 21 LEU 147.5 166.6 -170.3 -140.0 138.7 22 VAL 174.7 54.5 176.1 158.9 23 GLU 71.7 -113.8 -177.7 -87.6 87.7 -65.4 24 THR 150.9 110.7 178.7 161.8 25 TYR 108.9 165.7 179.1 173.9 -86.0 26 LYS -47.3 -87.5 178.5 -97.8 100.9 106.1 113.7 27 LYS 143.8 -34.9 -179.6 175.1 -121.8 164.9 87.8 28 HIS 37.0 -155.6 -178.2 74.0 23.2 29 PRO -76.4 -56.0 -178.9 7.0 2.3 30 LEU 150.8 -24.6 -179.9 -99.3 159.7 31 TYR -2.5 -84.1 -179.8 171.0 61.3 32 GLY 174.3 37.2 179.4 33 LYS -98.4 40.4 -178.3 -136.7 -172.2 -148.1 128.6 34 ARG 65.4 -91.0 178.5 -99.9 -168.1 -82.8 165.2 35 VAL 99.9 -92.7 -175.9 164.9 36 LYS 115.2 -50.4 171.5 -67.7 172.5 -161.3 161.1 37 TYR 99.5 34.9 173.8 -54.0 -64.7 38 SER 114.4 -79.7 -177.9 71.2 39 LYS -173.4 -153.0 -174.5 -103.7 -146.0 -171.7 102.7 40 LYS 168.1 144.9 -173.4 47.7 -166.4 -169.2 176.2 41 TYR -155.7 129.0 -177.9 -19.2 84.8 42 LYS -19.1 -157.2 179.6 72.7 -151.4 156.3 156.2 43 ALA 136.9 -154.4 -179.9 44 HIS 171.9 -151.5 178.8 80.8 -40.3 45 ASP -108.6 96.5 -178.8 25.1 69.5 46 GLU -85.2 57.4 -180.0 69.1 130.5 -81.3 47 HIS 89.0 145.2 -178.8 -147.0 101.6 48 ASN 69.1 8.5 -178.7 -118.8 14.4 49 GLU 69.0 6.5 179.7 -150.5 120.2 39.3 50 ALA 37.7 -99.0 -178.8 51 LYS 87.9 78.6 -178.2 -153.4 117.2 -127.9 -96.4 52 VAL 64.9 72.7 -179.4 -175.6 53 GLY -28.3 -45.1 -179.4 54 ASP 135.3 -109.7 179.6 176.4 3.5 55 ILE -137.2 92.7 -178.5 -64.1 -69.5 56 VAL -94.7 -107.3 -176.9 50.3 57 LYS 158.7 174.2 -177.9 162.3 173.5 -156.1 173.5 58 ILE 151.2 -118.9 -179.5 44.6 99.4 59 MET 162.1 -105.1 -177.2 171.7 155.1 101.2 60 GLU 81.9 52.7 179.0 101.5 95.1 8.5 61 THR -47.9 160.5 179.9 91.1 62 ARG -66.9 145.8 179.6 -80.5 162.7 124.9 165.4 63 PRO -62.7 136.5 -180.0 1.1 -0.6 64 LEU -125.5 4.4 -180.0 50.2 135.8 65 SER 168.0 -69.9 -179.9 22.0 66 ALA -143.2 56.9 180.0 67 THR -148.6 104.6 -179.6 61.1 68 LYS -119.2 -9.0 179.5 -147.9 172.6 -164.0 -129.5 69 ARG -65.9 172.0 -179.8 -27.6 -45.1 -145.1 165.5 70 PHE -125.6 -179.7 -179.5 74.5 -12.6 71 ARG -116.8 177.0 -179.4 -126.5 84.9 -96.2 165.0 72 LEU 164.7 -132.1 -174.0 67.0 135.7 73 VAL 144.6 -15.3 177.1 -83.1 74 GLU 91.6 179.2 -178.8 -141.6 -134.3 -30.4 75 ILE 150.8 -177.2 -178.5 -91.1 -78.1 76 VAL 146.1 -41.4 179.5 49.6 77 GLU -173.7 153.6 -180.0 -134.8 -96.5 -4.2 78 LYS -79.4 155.6 -179.9 -52.0 -137.3 156.9 47.4 79 ALA 72.2 89.2 -179.9 80 VAL 154.0 64.4 -179.9 -90.0 81 ARG 88.6 -104.3 0.0 -162.6 94.0 -111.9 164.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLN 4.913 13.461 6.497 2 ARG 5.373 14.383 2.814 3 LYS 4.008 11.247 1.112 4 VAL 4.262 7.402 1.399 5 TYR 1.815 5.131 3.237 6 VAL 1.859 1.496 4.289 7 GLY -0.197 -1.407 5.467 8 ARG -2.541 -3.791 3.826 9 VAL -1.321 -6.868 2.311 10 VAL 2.513 -7.095 1.807 11 SER 1.361 -9.732 -0.665 12 ASP -1.896 -9.543 -2.850 13 LYS -0.846 -10.462 -6.439 14 MET -0.285 -7.927 -9.225 15 ASP 2.404 -9.219 -11.599 16 LYS 4.716 -7.423 -9.166 17 THR 5.150 -9.635 -6.094 18 ILE 5.185 -8.232 -2.523 19 THR 4.139 -4.660 -1.469 20 VAL 0.944 -3.920 0.551 21 LEU -2.278 -2.064 -0.242 22 VAL -4.313 0.060 2.059 23 GLU -7.804 1.058 0.707 24 THR -7.779 4.271 -1.545 25 TYR -8.794 8.013 -0.924 26 LYS -8.967 10.383 2.108 27 LYS -11.697 8.543 4.117 28 HIS -13.610 11.362 5.880 29 PRO -16.354 9.904 8.205 30 LEU -18.225 7.576 5.786 31 TYR -21.469 9.561 5.189 32 GLY -21.893 8.513 1.555 33 LYS -19.463 10.461 -0.635 34 ARG -18.132 7.241 -2.143 35 VAL -14.625 7.705 -0.718 36 LYS -12.525 4.646 -1.636 37 TYR -10.582 4.930 1.758 38 SER -6.787 5.838 1.434 39 LYS -4.636 3.797 -1.128 40 LYS -3.278 0.361 -2.304 41 TYR -0.070 -1.166 -3.819 42 LYS 0.743 -4.388 -5.794 43 ALA 2.306 -7.624 -4.299 44 HIS 1.712 -11.465 -4.626 45 ASP 2.346 -14.727 -2.752 46 GLU 5.883 -14.556 -1.337 47 HIS 5.858 -18.209 -0.149 48 ASN 3.199 -19.909 1.927 49 GLU 0.836 -18.482 -0.693 50 ALA 0.992 -15.349 1.503 51 LYS -2.683 -14.251 1.132 52 VAL -2.844 -10.608 2.271 53 GLY 0.725 -10.298 3.632 54 ASP -0.866 -8.344 6.575 55 ILE 0.292 -4.716 7.210 56 VAL 3.738 -3.793 5.751 57 LYS 4.622 -0.316 4.399 58 ILE 6.530 1.598 1.565 59 MET 5.165 4.284 -0.786 60 GLU 5.698 4.373 -4.583 61 THR 4.174 7.817 -5.233 62 ARG 2.440 8.221 -8.621 63 PRO 4.758 8.821 -11.590 64 LEU 5.049 12.532 -12.476 65 SER 7.649 12.343 -15.239 66 ALA 10.570 9.963 -14.587 67 THR 10.076 8.374 -11.139 68 LYS 8.480 4.922 -10.703 69 ARG 10.535 3.539 -7.786 70 PHE 8.863 3.588 -4.350 71 ARG 9.691 4.496 -0.766 72 LEU 9.440 2.464 2.452 73 VAL 11.528 0.734 5.165 74 GLU 9.177 -2.322 5.362 75 ILE 6.766 -3.616 7.973 76 VAL 3.976 -6.357 7.817 77 GLU 3.991 -8.114 11.217 78 LYS 5.869 -8.210 14.547 79 ALA 8.458 -10.955 15.168 80 VAL 10.516 -11.412 11.939 81 ARG 13.647 -9.197 11.787 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S/S S S S S 10 S S S/T T T T S S S S 20 S S S/S S S S/S S S S C 30 C C C C C C C C C S 40 S S S S S T T T T/S S 50 S S C S S S S S S S 60 C C T T T T/S S S S/S S 70 S S S/S S S S S S S S 80 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S B e E E S 10 S S S S 20 B S S 30 S S S S B 40 t T T t 50 S S E E e B 60 S S S 70 B S S S 80 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLN 12.1 8.1 88.3 2 ARG 8.7 4.2 85.2 3 LYS 52.1 30.0 67.5 4 VAL 80.7 67.9 54.6 5 TYR 156.0 86.2 34.5 6 VAL 73.7 62.1 44.6 7 GLY 31.8 91.5 38.4 8 ARG 114.1 54.6 54.0 9 VAL 117.9 99.2 46.5 10 VAL 108.5 91.3 48.0 11 SER 82.6 98.8 49.5 12 ASP 81.9 74.1 55.9 13 LYS 44.1 25.4 82.9 14 MET 53.8 33.7 72.9 15 ASP 0.0 0.0 86.0 16 LYS 79.4 45.8 73.8 17 THR 46.2 43.2 68.8 18 ILE 55.1 38.4 69.9 19 THR 103.6 96.9 32.5 20 VAL 118.8 100.0 34.3 21 LEU 116.5 78.8 54.9 22 VAL 94.9 79.9 53.6 23 GLU 60.0 43.3 70.3 24 THR 76.4 71.5 52.7 25 TYR 112.7 62.3 53.4 26 LYS 17.4 10.0 81.1 27 LYS 64.2 37.0 66.7 28 HIS 104.5 69.6 53.7 29 PRO 31.4 25.2 68.3 30 LEU 47.2 31.9 75.6 31 TYR 12.7 7.0 81.2 32 GLY 6.6 19.0 75.4 33 LYS 27.7 16.0 81.8 34 ARG 18.5 8.9 85.6 35 VAL 118.7 99.9 41.7 36 LYS 61.1 35.2 67.0 37 TYR 113.8 62.9 54.8 38 SER 48.3 57.8 63.0 39 LYS 85.5 49.3 60.8 40 LYS 61.8 35.6 64.2 41 TYR 172.5 95.3 34.4 42 LYS 117.8 67.9 49.9 43 ALA 72.6 100.0 57.2 44 HIS 114.2 76.0 52.7 45 ASP 50.0 45.3 62.9 46 GLU 55.7 40.2 66.1 47 HIS 0.0 0.0 89.4 48 ASN 0.1 0.1 81.1 49 GLU 21.4 15.4 77.1 50 ALA 60.9 83.9 59.6 51 LYS 20.2 11.6 83.2 52 VAL 49.9 42.0 68.1 53 GLY 24.4 70.0 50.0 54 ASP 62.8 56.8 55.9 55 ILE 58.9 41.1 67.8 56 VAL 113.4 95.4 40.9 57 LYS 111.7 64.4 49.9 58 ILE 137.4 95.8 29.3 59 MET 144.5 90.7 34.5 60 GLU 87.7 63.2 57.8 61 THR 73.0 68.3 52.6 62 ARG 16.2 7.8 84.8 63 PRO 60.9 48.9 70.2 64 LEU 38.6 26.1 88.4 65 SER 20.7 24.7 73.4 66 ALA 0.6 0.8 82.2 67 THR 42.5 39.7 76.1 68 LYS 41.9 24.2 79.9 69 ARG 22.0 10.6 89.9 70 PHE 114.4 68.6 54.5 71 ARG 75.4 36.1 64.6 72 LEU 93.8 63.5 51.8 73 VAL 32.4 27.3 71.0 74 GLU 50.2 36.2 61.9 75 ILE 51.3 35.8 62.2 76 VAL 89.8 75.6 53.0 77 GLU 45.1 32.6 75.3 78 LYS 0.0 0.0 87.7 79 ALA 0.0 0.0 83.5 80 VAL 31.3 26.3 79.8 81 ARG 4.7 2.3 95.7