Protein Data Bank File : 1c52 Title : ELECTRON TRANSPORT PROTEIN 23-JUN-97 1C52 Number of Amino Acid Residues : 131 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLN ALA ASP GLY ALA LYS ILE TYR ALA GLN 10 CYS ALA GLY CYS HIS GLN GLN ASN GLY GLN 20 GLY ILE PRO GLY ALA PHE PRO PRO LEU ALA 30 GLY HIS VAL ALA GLU ILE LEU ALA LYS GLU 40 GLY GLY ARG GLU TYR LEU ILE LEU VAL LEU 50 LEU TYR GLY LEU GLN GLY GLN ILE GLU VAL 60 LYS GLY MET LYS TYR ASN GLY VAL MET SER 70 SER PHE ALA GLN LEU LYS ASP GLU GLU ILE 80 ALA ALA VAL LEU ASN HIS ILE ALA THR ALA 90 TRP GLY ASP ALA LYS LYS VAL LYS GLY PHE 100 LYS PRO PHE THR ALA GLU GLU VAL LYS LYS 110 LEU ARG ALA LYS LYS LEU THR PRO GLN GLN 120 VAL LEU ALA GLU ARG LYS LYS LEU GLY LEU 130 LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLN 0.0 -130.6 179.6 -159.7 56.8 -126.2 2 ALA 61.6 99.5 177.9 3 ASP -118.0 105.5 -179.0 176.8 -11.9 4 GLY -57.3 -34.2 -178.9 5 ALA -67.8 -34.3 179.4 6 LYS -72.9 -42.8 -179.6 -166.6 64.8 178.8 -177.9 7 ILE -63.6 -33.3 179.9 -64.0 155.2 8 TYR -61.1 -17.8 177.9 -172.9 74.9 9 ALA -57.8 -29.7 179.4 10 GLN -72.4 -14.4 -178.9 -61.7 -179.5 42.6 11 CYS -106.5 -22.4 -173.9 -33.4 12 ALA -60.4 -31.6 179.3 13 GLY -61.1 -28.3 179.3 14 CYS -98.9 -59.2 -177.9 -63.4 15 HIS -81.7 -11.1 176.8 -62.2 -72.2 16 GLN 76.0 151.7 179.9 -50.3 -51.0 132.9 17 GLN -62.0 -31.7 177.4 -84.2 -63.4 -19.2 18 ASN -86.2 5.9 179.1 63.4 13.3 19 GLY 64.9 14.3 -178.4 20 GLN -90.2 -3.8 178.7 -68.9 166.4 28.5 21 GLY 59.2 -158.7 178.1 22 ILE -139.6 106.9 179.6 -62.5 178.6 23 PRO -49.8 135.9 -179.4 -33.9 41.9 24 GLY 86.7 -5.8 -178.4 25 ALA -135.3 -65.1 -177.0 26 PHE -126.8 124.5 -178.9 -49.7 -60.2 27 PRO -67.7 152.9 179.0 32.5 -40.4 28 PRO -72.7 151.1 176.1 33.5 -45.1 29 LEU -109.3 -36.1 179.9 -62.3 179.4 30 ALA -61.9 128.6 -179.9 31 GLY 86.0 -45.7 -178.4 32 HIS -68.3 -39.3 179.4 -179.1 49.6 33 VAL -56.7 -39.1 178.2 170.1 34 ALA -61.8 -38.1 -179.8 35 GLU -64.4 -40.6 -179.7 -30.6 -116.7 43.6 36 ILE -70.3 -42.6 -179.0 -68.4 167.0 37 LEU -63.8 -25.8 178.7 -74.8 172.9 38 ALA -70.2 -14.5 179.6 39 LYS -92.9 145.4 177.4 -54.6 -59.6 -170.6 174.6 40 GLU -68.5 132.4 -178.7 -147.1 72.4 -81.0 41 GLY 91.9 -8.9 180.0 42 GLY -57.5 -47.0 -179.9 43 ARG -65.4 -37.2 178.5 65.2 -171.5 -62.1 102.8 44 GLU -65.3 -43.5 -179.7 -71.6 74.0 24.1 45 TYR -55.0 -47.5 -179.8 169.2 69.2 46 LEU -59.6 -38.7 177.6 -68.5 168.8 47 ILE -65.9 -43.0 178.9 -67.1 168.7 48 LEU -59.6 -40.5 178.2 -64.7 177.2 49 VAL -58.5 -45.0 -179.6 172.5 50 LEU -67.6 -36.4 -179.7 -86.5 -76.5 51 LEU -80.5 -33.1 -172.1 -70.5 174.0 52 TYR -123.6 -5.9 -179.6 -54.7 -64.0 53 GLY 83.4 -176.6 -178.8 54 LEU -156.1 143.4 176.7 175.8 65.6 55 GLN -151.0 150.2 179.2 -66.5 176.8 25.7 56 GLY 122.3 167.6 -179.0 57 GLN -77.2 130.8 177.8 -165.7 172.3 -148.0 58 ILE -138.0 161.6 175.3 60.4 174.9 59 GLU -121.3 138.3 179.9 -167.1 168.0 -86.6 60 VAL -141.4 125.3 -179.0 172.4 61 LYS 50.6 45.5 178.1 -65.6 -177.9 178.4 -172.6 62 GLY 63.2 19.7 179.2 63 MET -122.8 143.2 -178.3 -60.7 -172.2 -174.7 64 LYS -92.8 142.6 178.3 -71.8 -71.1 -166.9 -168.3 65 TYR -135.4 138.7 177.4 -62.2 85.4 66 ASN -140.8 71.6 -177.9 -169.6 4.6 67 GLY -125.6 -160.7 -179.2 68 VAL -136.3 139.1 174.6 -49.2 69 MET -124.2 131.6 179.1 -179.8 172.8 145.3 70 SER -75.4 163.8 177.2 69.2 71 SER -79.4 156.2 176.5 117.6 72 PHE -123.9 34.5 -178.5 -80.7 77.9 73 ALA -64.0 -16.2 178.5 74 GLN -69.0 -19.3 178.7 72.2 -81.3 -0.6 75 LEU -73.1 154.3 177.1 -65.4 176.2 76 LYS -71.5 157.9 177.3 -63.3 -171.7 -89.1 -75.7 77 ASP -53.5 -43.4 179.4 -67.5 -19.8 78 GLU -62.6 -35.9 179.8 -68.8 -164.8 -45.7 79 GLU -70.4 -40.0 178.2 -68.3 175.9 -33.8 80 ILE -67.7 -45.1 177.9 -69.8 172.2 81 ALA -60.4 -40.8 179.9 82 ALA -63.8 -46.9 -178.5 83 VAL -69.4 -32.7 177.1 76.6 84 LEU -68.3 -38.7 177.2 -74.7 173.2 85 ASN -66.3 -33.5 177.3 -79.3 142.3 86 HIS -63.0 -50.8 -179.4 176.3 79.2 87 ILE -67.9 -21.5 177.8 66.6 171.2 88 ALA -80.7 -16.1 -176.9 89 THR -123.5 -27.3 -177.4 58.6 90 ALA -52.2 -34.3 -179.2 91 TRP -117.5 20.4 177.5 -46.5 -68.8 92 GLY 80.4 16.6 -179.0 93 ASP -65.9 -38.0 -177.0 -72.6 62.6 94 ALA -56.4 -42.1 179.3 95 LYS -61.8 -26.0 -179.7 -174.9 -170.8 -135.6 -55.4 96 LYS -87.9 1.0 -179.9 -59.6 -167.1 -87.4 -140.7 97 VAL -108.7 113.1 179.3 178.7 98 LYS -61.7 122.6 178.2 -177.4 169.2 102.1 -68.5 99 GLY 71.8 29.7 179.2 100 PHE -48.5 129.4 178.2 174.4 77.6 101 LYS -118.2 122.8 179.9 -64.1 -57.2 -59.0 -166.3 102 PRO -59.6 146.0 177.0 -29.2 44.1 103 PHE -68.0 145.7 178.6 -66.1 88.5 104 THR -123.2 158.7 178.3 71.0 105 ALA -61.6 -37.8 -179.0 106 GLU -64.3 -35.4 179.4 -69.1 178.0 75.3 107 GLU -63.9 -41.6 -179.2 -76.0 -174.3 -82.7 108 VAL -65.9 -48.1 -179.8 177.7 109 LYS -52.8 -45.7 -179.8 178.9 169.1 -170.8 160.7 110 LYS -59.3 -38.9 -177.5 174.3 73.7 177.5 -177.9 111 LEU -78.8 -4.9 176.7 -72.4 168.5 112 ARG -69.1 -18.5 178.1 -64.9 -139.0 -176.6 -126.2 113 ALA -73.5 -19.2 -178.6 114 LYS -58.1 -44.4 179.2 -67.5 -80.6 165.6 -78.6 115 LYS 50.7 57.3 -178.3 -65.0 -178.5 176.7 -176.6 116 LEU -95.3 160.6 175.2 -52.0 178.3 117 THR -95.4 163.9 179.2 57.4 118 PRO -59.3 -29.5 179.3 -30.3 39.1 119 GLN -70.6 -38.0 177.2 -68.5 63.9 -139.4 120 GLN -66.2 -34.3 177.2 -78.0 172.5 130.9 121 VAL -65.4 -42.1 176.3 176.3 122 LEU -59.9 -42.0 178.1 178.9 67.1 123 ALA -58.5 -37.8 177.8 124 GLU -65.4 -39.0 179.8 -73.5 -47.3 -61.8 125 ARG -61.9 -44.3 -179.1 -168.9 -177.8 -169.0 -81.3 126 LYS -60.0 -27.0 178.4 -68.8 171.0 176.6 175.1 127 LYS -76.7 -12.9 -179.4 -61.1 174.8 -170.6 178.9 128 LEU -75.1 -26.3 -179.3 -61.4 174.3 129 GLY 71.6 49.6 179.9 130 LEU -76.1 -79.9 -179.5 -67.4 171.8 131 LYS -150.3 26.8 0.0 -70.9 175.8 -179.5 177.4 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLN 37.904 28.269 30.491 2 ALA 34.361 29.736 30.464 3 ASP 31.862 27.978 28.188 4 GLY 28.749 30.136 27.986 5 ALA 26.619 27.235 26.801 6 LYS 27.557 25.207 29.868 7 ILE 26.943 28.115 32.231 8 TYR 23.555 28.584 30.573 9 ALA 22.489 25.225 32.055 10 GLN 21.910 27.192 35.270 11 CYS 19.381 29.406 33.437 12 ALA 17.682 26.818 31.236 13 GLY 15.141 25.458 33.726 14 CYS 13.555 28.902 33.621 15 HIS 14.425 30.560 30.290 16 GLN 14.666 27.203 28.416 17 GLN 17.299 25.779 26.095 18 ASN 15.521 27.401 23.124 19 GLY 15.433 30.732 24.995 20 GLN 11.657 30.990 24.688 21 GLY 10.941 31.009 28.421 22 ILE 7.480 30.202 29.720 23 PRO 4.800 32.907 29.231 24 GLY 3.335 33.918 32.578 25 ALA 6.441 32.693 34.362 26 PHE 9.894 33.262 32.830 27 PRO 10.477 35.701 30.015 28 PRO 11.965 34.685 26.669 29 LEU 15.539 35.668 25.915 30 ALA 15.572 34.573 22.237 31 GLY 14.655 37.596 20.105 32 HIS 14.257 39.748 23.175 33 VAL 17.983 40.186 23.933 34 ALA 18.419 41.969 20.540 35 GLU 15.655 44.377 21.485 36 ILE 17.412 45.257 24.730 37 LEU 20.826 45.582 23.120 38 ALA 19.428 48.038 20.569 39 LYS 18.830 50.507 23.438 40 GLU 21.583 52.734 24.722 41 GLY 22.440 51.303 28.143 42 GLY 21.074 47.901 27.072 43 ARG 24.352 45.956 27.461 44 GLU 25.003 47.482 30.902 45 TYR 21.466 46.590 31.932 46 LEU 21.938 42.926 31.023 47 ILE 25.121 42.833 33.110 48 LEU 23.252 44.458 36.038 49 VAL 20.548 41.760 35.872 50 LEU 23.217 39.081 36.166 51 LEU 25.080 40.809 39.004 52 TYR 22.132 42.034 41.018 53 GLY 18.981 40.212 39.979 54 LEU 15.643 41.707 38.957 55 GLN 12.158 41.987 40.463 56 GLY 9.027 43.837 39.490 57 GLN 6.481 43.976 36.719 58 ILE 7.867 43.939 33.189 59 GLU 6.434 43.299 29.759 60 VAL 8.273 41.188 27.196 61 LYS 6.896 40.447 23.713 62 GLY 3.636 41.972 24.833 63 MET 3.314 39.596 27.745 64 LYS 3.447 40.540 31.396 65 TYR 5.766 39.043 34.032 66 ASN 5.896 39.954 37.691 67 GLY 8.493 37.634 39.075 68 VAL 11.914 37.509 40.611 69 MET 15.309 36.609 39.333 70 SER 18.220 36.041 41.672 71 SER 21.623 37.573 41.179 72 PHE 24.391 35.382 39.726 73 ALA 27.204 37.496 41.148 74 GLN 28.853 34.327 42.478 75 LEU 29.885 33.579 38.874 76 LYS 33.267 34.826 37.704 77 ASP 33.418 37.900 35.478 78 GLU 34.478 35.646 32.561 79 GLU 31.507 33.356 33.230 80 ILE 28.985 36.210 33.229 81 ALA 30.452 37.621 30.006 82 ALA 30.338 34.109 28.551 83 VAL 26.725 33.386 29.435 84 LEU 25.600 36.826 28.260 85 ASN 27.404 36.225 24.962 86 HIS 25.603 32.867 24.869 87 ILE 22.113 34.361 25.215 88 ALA 23.119 37.030 22.673 89 THR 24.118 34.415 20.050 90 ALA 22.462 31.039 20.728 91 TRP 19.224 32.071 18.976 92 GLY 20.689 34.584 16.535 93 ASP 20.195 37.847 18.390 94 ALA 23.700 39.216 17.737 95 LYS 23.229 39.259 13.967 96 LYS 20.159 41.403 14.652 97 VAL 22.091 44.038 16.654 98 LYS 23.781 46.671 14.481 99 GLY 27.368 46.828 15.668 100 PHE 26.992 44.063 18.264 101 LYS 29.904 44.095 20.742 102 PRO 30.561 40.969 22.761 103 PHE 30.342 41.294 26.548 104 THR 33.729 41.249 28.230 105 ALA 34.920 40.236 31.681 106 GLU 36.248 43.778 32.264 107 GLU 32.841 45.306 31.618 108 VAL 31.336 43.009 34.231 109 LYS 34.149 43.742 36.685 110 LYS 33.514 47.494 36.370 111 LEU 29.829 47.155 37.194 112 ARG 30.507 45.254 40.436 113 ALA 31.042 48.651 42.104 114 LYS 27.325 49.445 41.556 115 LYS 25.950 47.312 44.405 116 LEU 22.313 47.531 43.336 117 THR 19.130 45.886 44.580 118 PRO 16.795 44.077 42.116 119 GLN 14.489 47.127 42.383 120 GLN 17.294 49.460 41.286 121 VAL 17.899 47.133 38.322 122 LEU 14.192 47.466 37.403 123 ALA 14.614 51.285 37.611 124 GLU 17.514 50.925 35.162 125 ARG 15.294 48.859 32.834 126 LYS 12.626 51.555 32.819 127 LYS 15.195 54.074 31.535 128 LEU 15.836 52.001 28.402 129 GLY 12.432 52.807 26.935 130 LEU 11.602 49.240 25.862 131 LYS 7.837 48.636 26.043 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/T T 10 T T/T T T T T T T T C 20 C T T T T/S S S S S S 30 H H H H H H H H 3 C 40 H H H H H H H H H H 50 H H/S S S S S S C T T 60 T T/S S S S S S S/S S S 70 S S C C C H H H H H 80 H H H H H H H H H H 90 C H H H H H H C S S 100 S S S S/H H H H H H H 110 H H C C C C H H H H 120 H H H H H H H H S S 130 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 10 H H H H H h T T t 20 B T T T B t T 30 h H H H H H H h t T 40 h H H H H H H H H H 50 H H h E E E E E E E 60 T T E E E E E E E 70 t T T t h H H H H 80 H H H H H H H H H h 90 T t g G G G g T T t 100 h H H H H H H 110 H h T t h H H H 120 H H H H H H h T t 130 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLN 0.0 0.0 92.5 2 ALA 59.3 81.6 51.7 3 ASP 33.8 30.6 71.7 4 GLY 31.8 91.5 55.2 5 ALA 27.5 37.8 75.8 6 LYS 20.6 11.9 83.5 7 ILE 128.7 89.7 48.2 8 TYR 180.9 99.9 42.0 9 ALA 29.1 40.1 76.7 10 GLN 66.2 44.6 63.6 11 CYS 77.0 77.6 46.9 12 ALA 61.8 85.1 65.4 13 GLY 0.0 0.0 81.0 14 CYS 46.1 46.5 62.8 15 HIS 127.9 85.1 42.2 16 GLN 94.3 63.5 72.6 17 GLN 44.8 30.1 70.2 18 ASN 48.2 39.9 72.1 19 GLY 34.8 100.0 58.5 20 GLN 47.4 31.9 77.7 21 GLY 34.8 100.0 60.7 22 ILE 63.9 44.5 68.3 23 PRO 56.7 45.6 69.5 24 GLY 3.6 10.5 75.9 25 ALA 40.2 55.4 55.2 26 PHE 93.9 56.3 54.3 27 PRO 97.6 78.4 40.1 28 PRO 115.1 92.5 53.7 29 LEU 123.3 83.4 41.3 30 ALA 61.1 84.2 58.9 31 GLY 21.9 62.8 75.3 32 HIS 134.3 89.4 44.8 33 VAL 118.5 99.8 32.0 34 ALA 65.2 89.8 51.1 35 GLU 67.2 48.5 68.4 36 ILE 136.6 95.2 36.6 37 LEU 144.5 97.8 36.9 38 ALA 22.8 31.4 75.4 39 LYS 105.8 61.0 72.4 40 GLU 0.0 0.0 92.2 41 GLY 12.0 34.4 73.4 42 GLY 34.8 100.0 54.0 43 ARG 161.2 77.2 59.5 44 GLU 70.2 50.7 58.3 45 TYR 174.7 96.5 31.7 46 LEU 137.7 93.2 30.2 47 ILE 143.1 99.7 36.3 48 LEU 138.6 93.8 31.3 49 VAL 105.5 88.8 39.5 50 LEU 132.5 89.6 34.5 51 LEU 146.5 99.1 42.6 52 TYR 157.6 87.1 50.0 53 GLY 34.6 99.4 59.0 54 LEU 126.3 85.5 42.0 55 GLN 84.1 56.6 65.3 56 GLY 17.6 50.7 67.8 57 GLN 58.9 39.6 72.8 58 ILE 128.3 89.4 46.2 59 GLU 96.3 69.5 55.0 60 VAL 118.0 99.3 43.5 61 LYS 101.3 58.4 66.7 62 GLY 8.3 23.9 72.3 63 MET 61.3 38.5 74.0 64 LYS 70.3 40.6 74.6 65 TYR 172.8 95.5 51.0 66 ASN 37.3 30.8 77.1 67 GLY 8.7 25.0 80.2 68 VAL 31.4 26.4 78.6 69 MET 112.9 70.8 59.0 70 SER 13.7 16.4 75.0 71 SER 54.2 64.9 71.2 72 PHE 134.7 80.7 60.6 73 ALA 43.6 60.1 78.1 74 GLN 43.3 29.1 77.1 75 LEU 133.8 90.5 52.4 76 LYS 42.9 24.8 83.7 77 ASP 84.3 76.3 54.5 78 GLU 43.9 31.7 63.0 79 GLU 106.9 77.1 44.8 80 ILE 143.5 100.0 38.0 81 ALA 65.5 90.2 57.1 82 ALA 56.9 78.4 61.4 83 VAL 115.7 97.4 33.4 84 LEU 147.3 99.7 28.9 85 ASN 87.9 72.7 53.1 86 HIS 118.1 78.6 49.3 87 ILE 133.1 92.8 28.2 88 ALA 72.6 100.0 38.3 89 THR 50.7 47.4 68.6 90 ALA 52.6 72.5 65.0 91 TRP 169.7 82.8 59.6 92 GLY 5.7 16.2 79.4 93 ASP 110.5 100.0 52.7 94 ALA 57.7 79.5 44.2 95 LYS 0.7 0.4 89.6 96 LYS 69.2 39.9 74.1 97 VAL 107.0 90.1 53.3 98 LYS 0.0 0.0 91.2 99 GLY 0.0 0.0 82.9 100 PHE 144.4 86.6 47.0 101 LYS 36.3 20.9 81.2 102 PRO 54.9 44.1 69.8 103 PHE 166.5 99.8 41.9 104 THR 42.9 40.2 73.1 105 ALA 46.8 64.4 54.5 106 GLU 2.6 1.9 82.5 107 GLU 93.5 67.4 66.2 108 VAL 118.8 100.0 39.6 109 LYS 36.0 20.8 81.7 110 LYS 18.5 10.7 85.2 111 LEU 130.0 88.0 42.6 112 ARG 140.9 67.4 66.6 113 ALA 10.7 14.8 84.4 114 LYS 81.9 47.2 59.9 115 LYS 21.5 12.4 84.3 116 LEU 124.7 84.4 45.1 117 THR 42.2 39.5 70.1 118 PRO 96.0 77.1 68.5 119 GLN 55.1 37.1 71.7 120 GLN 68.1 45.8 65.7 121 VAL 118.8 100.0 40.2 122 LEU 127.9 86.6 54.7 123 ALA 29.8 41.0 68.6 124 GLU 89.1 64.3 56.7 125 ARG 190.2 91.1 41.5 126 LYS 47.2 27.2 76.1 127 LYS 49.5 28.5 86.1 128 LEU 139.7 94.5 48.4 129 GLY 0.0 0.0 83.7 130 LEU 138.1 93.5 48.4 131 LYS 75.1 43.3 76.1