Protein Data Bank File : 1dj7a Title : ELECTRON TRANSPORT 02-DEC-99 1DJ7 Number of Amino Acid Residues : 109 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASN ASN LYS THR LEU ALA ALA MET LYS ASN 10 PHE ALA GLU GLN TYR ALA LYS ARG THR ASP 20 THR TYR PHE CYS SER ASP LEU SER VAL THR 30 ALA VAL VAL ILE GLU GLY LEU ALA ARG HIS 40 LYS GLU GLU LEU GLY SER PRO LEU CYS PRO 50 CYS ARG HIS TYR GLU ASP LYS GLU ALA GLU 60 VAL LYS ASN THR PHE TRP ASN CYS PRO CYS 70 VAL PRO MET ARG GLU ARG LYS GLU CYS HIS 80 CYS MET LEU PHE LEU THR PRO ASP ASN ASP 90 PHE ALA GLY ASP ALA GLN ASP ILE PRO MET 100 GLU THR LEU GLU GLU VAL LYS ALA SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASN 0.0 91.2 178.4 -142.8 -79.9 2 ASN -53.8 -26.9 171.3 -70.9 -47.0 3 LYS -68.1 -44.2 176.3 0.0 0.0 0.0 0.0 4 THR -63.6 -40.0 176.9 -53.7 5 LEU -60.8 -39.9 178.3 -178.0 64.4 6 ALA -72.3 -39.0 177.5 7 ALA -63.0 -43.0 179.6 8 MET -62.9 -41.0 177.4 -160.9 65.0 57.0 9 LYS -59.4 -44.4 179.1 174.6 -145.6 -175.2 -89.9 10 ASN -65.1 -40.5 177.5 -174.1 -121.5 11 PHE -58.6 -51.3 -177.0 150.7 77.8 12 ALA -57.5 -43.4 -178.5 13 GLU -68.5 -40.2 179.6 -56.9 -179.6 -35.5 14 GLN -72.1 -36.9 -179.3 78.6 -153.9 4.8 15 TYR -69.4 -38.7 177.5 -165.5 73.7 16 ALA -61.6 -42.6 178.7 17 LYS -68.0 -42.4 -179.0 -66.6 166.7 -173.8 -169.9 18 ARG -66.8 -26.9 -178.2 0.0 0.0 0.0 0.0 19 THR -103.4 5.7 -177.0 56.4 20 ASP 55.6 44.8 178.7 -61.4 -30.3 21 THR -120.8 159.5 -172.0 52.7 22 TYR -124.9 157.3 179.0 -70.2 -88.9 23 PHE -80.8 159.0 175.9 -69.1 -26.4 24 CYS -52.1 149.4 177.8 178.9 25 SER -65.4 -24.9 173.2 47.9 26 ASP -98.7 100.5 -178.9 177.4 2.8 27 LEU -63.6 -15.8 175.6 -66.3 172.3 28 SER -71.6 -26.8 174.5 77.1 29 VAL -63.5 -49.3 176.2 170.7 30 THR -56.1 -48.9 -178.5 -50.5 31 ALA -61.9 -38.8 178.8 32 VAL -64.5 -40.5 179.6 167.1 33 VAL -69.6 -39.3 178.7 178.6 34 ILE -63.8 -41.5 178.1 -67.2 166.4 35 GLU -65.1 -36.1 179.7 0.0 0.0 0.0 36 GLY -68.1 -34.9 178.7 37 LEU -64.2 -46.0 178.4 -78.5 170.0 38 ALA -62.8 -45.1 179.1 39 ARG -57.8 -50.9 176.9 -155.5 163.5 -161.6 -168.2 40 HIS -59.3 -43.3 178.2 -89.4 -15.5 41 LYS -60.5 -39.4 178.2 -179.1 162.9 -179.3 54.0 42 GLU -68.5 -46.4 -178.5 -62.2 152.2 11.2 43 GLU -70.7 -42.8 -174.8 -62.3 171.3 -23.3 44 LEU -106.9 -16.9 -178.9 -90.4 19.2 45 GLY 97.8 -13.3 179.3 46 SER -141.4 153.8 -177.4 -54.6 47 PRO -79.5 63.8 177.7 31.1 -32.5 48 LEU -56.9 133.6 179.9 -175.2 61.6 49 CYS -51.2 133.2 -177.7 -174.6 50 PRO -91.1 -8.7 -178.0 29.8 -27.5 51 CYS -101.0 23.2 176.7 65.5 52 ARG -126.2 162.9 172.5 -49.6 -169.3 77.6 72.9 53 HIS -108.8 151.8 -176.4 -61.3 147.1 54 TYR -135.1 152.4 176.8 -55.9 -79.5 55 GLU -85.8 -30.8 -177.0 0.0 0.0 0.0 56 ASP -148.6 89.7 -176.5 -168.4 -32.8 57 LYS -59.9 -36.8 178.7 -67.0 -171.7 -81.8 -179.8 58 GLU -63.9 -41.0 178.7 0.0 0.0 0.0 59 ALA -67.4 -37.1 178.6 60 GLU -60.9 -44.4 178.9 -65.2 -76.8 -9.0 61 VAL -66.1 -34.2 177.3 169.0 62 LYS -70.8 -42.5 178.3 0.0 0.0 0.0 0.0 63 ASN -63.7 -42.8 175.1 166.1 -88.7 64 THR 87.3 -7.4 -176.9 72.9 65 PHE -51.4 -44.2 -176.1 -172.3 -82.9 66 TRP -98.0 11.2 175.9 -73.8 122.9 67 ASN -77.1 128.8 -176.0 -70.0 -21.5 68 CYS -60.3 150.3 -50.6 -159.1 69 PRO -36.3 118.8 -174.4 36.7 -31.9 70 CYS -73.0 174.3 177.7 56.0 71 VAL -55.4 -53.6 179.5 166.9 72 PRO -55.6 -38.0 -179.9 -29.1 43.6 73 MET -74.9 -45.8 -178.0 176.3 65.5 -166.1 74 ARG -61.9 -43.2 -177.5 -72.0 -173.0 -77.6 104.5 75 GLU -87.6 -44.7 -173.1 -63.8 -169.9 0.5 76 ARG -113.9 4.1 -175.8 -53.3 -170.1 -178.8 -168.8 77 LYS 57.3 35.9 -179.9 -89.8 -170.4 -175.1 169.9 78 GLU -108.0 119.0 -179.3 -77.9 167.8 17.4 79 CYS -119.5 99.5 -179.1 177.1 80 HIS -60.9 -24.9 -179.9 178.3 65.8 81 CYS -77.5 -14.6 -179.8 -60.3 82 MET 69.8 33.9 174.0 -57.3 -175.8 176.2 83 LEU -85.8 -49.6 178.2 170.7 58.8 84 PHE -111.5 105.2 -175.7 -52.4 -71.3 85 LEU -110.2 142.2 178.4 -54.8 151.1 86 THR -73.7 155.9 -176.5 46.9 87 PRO -57.7 -27.6 178.1 -15.1 24.2 88 ASP -76.7 -21.2 -176.6 56.7 -75.5 89 ASN -60.7 136.3 178.4 -167.9 -62.0 90 ASP -56.9 -31.8 -176.8 -68.7 -29.8 91 PHE -94.0 4.9 179.2 -48.9 -69.7 92 ALA -80.8 132.1 176.4 93 GLY -96.1 -143.0 -179.4 94 ASP -127.6 6.7 -179.3 -123.2 -22.0 95 ALA -89.7 143.0 172.4 96 GLN -122.7 15.0 177.4 -64.8 175.4 -51.8 97 ASP -141.3 150.2 179.7 0.0 0.0 98 ILE -132.6 124.8 179.1 178.7 162.7 99 PRO -55.2 132.1 179.5 -17.8 26.9 100 MET -56.8 -31.2 176.5 -169.0 57.4 -160.8 101 GLU -54.7 -41.5 178.0 -155.9 -145.1 42.4 102 THR -63.7 -42.3 176.5 -49.2 103 LEU -68.7 -34.6 179.1 -39.9 -177.3 104 GLU -63.8 -32.1 175.4 -62.4 -70.5 -0.8 105 GLU -64.9 -36.4 178.0 -65.3 174.3 -22.7 106 VAL -74.0 -25.4 175.3 0.0 107 LYS -76.0 -32.3 177.5 -81.3 -64.3 171.3 -155.0 108 ALA -60.3 -36.6 174.0 109 SER -109.3 -81.2 0.0 46.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASN 19.333 6.562 50.232 2 ASN 15.785 7.288 51.328 3 LYS 16.937 10.815 52.173 4 THR 17.977 10.925 48.494 5 LEU 14.546 9.571 47.409 6 ALA 12.887 12.462 49.288 7 ALA 15.409 14.985 47.959 8 MET 14.686 13.815 44.405 9 LYS 10.896 14.140 44.885 10 ASN 11.343 17.690 46.162 11 PHE 13.605 18.491 43.214 12 ALA 11.035 17.227 40.716 13 GLU 8.228 19.246 42.296 14 GLN 10.312 22.436 42.463 15 TYR 11.615 22.023 38.909 16 ALA 8.116 21.456 37.483 17 LYS 6.898 24.646 39.139 18 ARG 9.907 26.727 38.000 19 THR 9.560 25.602 34.377 20 ASP 5.747 25.719 34.165 21 THR 5.701 21.986 33.466 22 TYR 3.365 19.345 34.859 23 PHE 3.476 15.729 35.962 24 CYS 2.043 12.870 33.918 25 SER -1.697 12.360 34.536 26 ASP -0.660 8.916 35.812 27 LEU 1.477 9.746 38.856 28 SER 2.927 6.205 39.044 29 VAL 4.795 7.077 35.834 30 THR 6.192 10.086 37.637 31 ALA 7.018 8.005 40.719 32 VAL 8.916 5.374 38.730 33 VAL 11.066 8.057 37.123 34 ILE 11.689 9.774 40.470 35 GLU 12.758 6.464 42.017 36 GLY 15.108 5.738 39.077 37 LEU 16.716 9.158 39.394 38 ALA 17.386 8.519 43.083 39 ARG 18.729 5.022 42.389 40 HIS 21.079 6.412 39.780 41 LYS 22.084 9.230 42.134 42 GLU 22.914 6.654 44.815 43 GLU 24.792 4.316 42.455 44 LEU 26.585 6.882 40.293 45 GLY 26.703 10.109 42.347 46 SER 24.496 12.075 39.927 47 PRO 20.877 11.767 38.766 48 LEU 21.555 10.211 35.390 49 CYS 18.255 9.967 33.468 50 PRO 16.593 6.621 34.209 51 CYS 14.480 6.127 31.084 52 ARG 17.431 5.486 28.741 53 HIS 20.013 2.724 28.254 54 TYR 23.741 3.503 28.239 55 GLU 26.992 1.891 27.102 56 ASP 28.975 3.549 29.886 57 LYS 27.021 5.176 32.729 58 GLU 30.103 6.485 34.536 59 ALA 31.213 8.311 31.383 60 GLU 27.678 9.697 30.945 61 VAL 27.678 11.180 34.456 62 LYS 31.100 12.736 33.799 63 ASN 29.998 14.228 30.460 64 THR 26.820 15.499 32.186 65 PHE 24.435 15.735 29.167 66 TRP 21.888 13.324 30.680 67 ASN 22.169 14.290 34.351 68 CYS 18.738 15.519 35.444 69 PRO 17.533 18.162 34.341 70 CYS 19.262 17.134 31.117 71 VAL 20.386 19.274 28.182 72 PRO 17.166 18.691 26.187 73 MET 15.008 19.627 29.181 74 ARG 17.071 22.677 30.196 75 GLU 17.284 24.070 26.695 76 ARG 14.157 22.836 24.905 77 LYS 11.872 21.712 27.718 78 GLU 11.850 18.202 26.227 79 CYS 11.639 15.364 28.749 80 HIS 11.707 11.901 27.161 81 CYS 10.844 10.242 30.495 82 MET 7.562 12.142 30.729 83 LEU 8.511 13.454 34.140 84 PHE 8.239 17.138 33.140 85 LEU 5.499 17.731 30.548 86 THR 4.458 20.974 28.886 87 PRO 0.809 21.896 29.436 88 ASP -0.199 21.126 25.838 89 ASN 1.068 17.545 26.081 90 ASP -1.602 14.834 25.957 91 PHE -0.126 13.031 28.984 92 ALA 0.126 16.112 31.186 93 GLY -2.149 16.135 34.187 94 ASP -2.435 19.127 36.428 95 ALA -0.232 18.198 39.324 96 GLN 3.111 19.808 40.074 97 ASP 3.231 17.772 43.279 98 ILE 3.248 14.060 44.012 99 PRO 2.105 12.526 47.294 100 MET 5.080 10.860 49.056 101 GLU 2.848 7.809 49.559 102 THR 2.900 7.210 45.798 103 LEU 6.711 7.008 45.686 104 GLU 6.627 4.695 48.733 105 GLU 4.402 2.286 46.761 106 VAL 7.071 2.059 44.040 107 LYS 9.674 1.300 46.708 108 ALA 7.307 -1.412 47.966 109 SER 7.725 -3.098 44.562 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H H H H H H H H H/S 20 S S S S C H H H H H 30 H H H H H H H H H H 40 H H H H C S S S S C 50 S S S S S H H H H H 60 H H H H C C C C C H 70 H H H H H H C C T T 80 T T S S S S S C C C 90 S S S S C S S S S/H H 100 H H H H H H H H H 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 H 10 H H H H H H H H h T 20 t B B S h H H H H 30 H H H H H H H H H H 40 H H H H h S B S 50 S S S h H H H H 60 H H H h T T B S S h 70 H H H H H H h t T 80 T t S S B t T T t T 90 T B S S h H 100 H H H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASN 33.9 28.1 78.9 2 ASN 11.5 9.5 78.2 3 LYS 107.1 61.8 84.8 4 THR 86.8 81.2 46.8 5 LEU 145.5 98.4 44.9 6 ALA 31.5 43.4 67.2 7 ALA 16.0 22.1 76.0 8 MET 150.0 94.1 37.0 9 LYS 135.3 78.0 53.8 10 ASN 36.8 30.5 82.2 11 PHE 130.3 78.1 47.3 12 ALA 72.6 100.0 33.4 13 GLU 117.3 84.6 63.4 14 GLN 51.3 34.5 72.6 15 TYR 143.2 79.1 38.4 16 ALA 72.6 100.0 54.5 17 LYS 63.5 36.6 78.2 18 ARG 151.7 72.6 77.8 19 THR 85.0 79.5 54.1 20 ASP 18.3 16.6 87.7 21 THR 106.9 100.0 44.4 22 TYR 128.7 71.1 65.8 23 PHE 166.8 100.0 44.1 24 CYS 90.6 91.3 54.0 25 SER 28.9 34.6 73.1 26 ASP 37.1 33.5 74.6 27 LEU 105.3 71.2 57.5 28 SER 27.0 32.3 73.3 29 VAL 67.8 57.1 64.7 30 THR 106.9 100.0 34.3 31 ALA 71.6 98.6 43.2 32 VAL 26.6 22.4 72.7 33 VAL 106.7 89.8 40.8 34 ILE 143.5 100.0 31.7 35 GLU 125.0 90.2 58.9 36 GLY 19.5 56.0 60.2 37 LEU 146.7 99.3 32.3 38 ALA 72.6 100.0 50.4 39 ARG 51.5 24.7 86.6 40 HIS 127.7 85.0 58.6 41 LYS 95.3 54.9 63.8 42 GLU 96.3 69.5 64.7 43 GLU 62.4 45.0 72.4 44 LEU 118.1 79.9 56.4 45 GLY 2.4 7.0 84.2 46 SER 59.6 71.3 55.0 47 PRO 99.3 79.7 49.3 48 LEU 147.8 100.0 42.7 49 CYS 87.4 88.1 40.1 50 PRO 112.7 90.6 49.8 51 CYS 68.0 68.6 49.7 52 ARG 131.7 63.0 54.6 53 HIS 0.0 0.0 86.8 54 TYR 170.2 94.0 51.7 55 GLU 61.5 44.4 83.8 56 ASP 34.5 31.3 71.4 57 LYS 90.5 52.2 61.2 58 GLU 74.7 53.9 77.6 59 ALA 23.0 31.6 76.1 60 GLU 93.0 67.1 54.2 61 VAL 100.4 84.5 64.9 62 LYS 112.0 64.6 81.2 63 ASN 31.6 26.1 79.3 64 THR 37.6 35.2 87.1 65 PHE 91.5 54.8 60.5 66 TRP 160.9 78.5 51.4 67 ASN 101.5 84.0 54.1 68 CYS 85.1 85.8 37.5 69 PRO 100.4 80.6 42.1 70 CYS 85.9 86.6 52.3 71 VAL 83.4 70.2 56.5 72 PRO 96.8 77.7 45.6 73 MET 156.8 98.4 44.2 74 ARG 109.5 52.4 72.4 75 GLU 42.7 30.8 74.7 76 ARG 46.9 22.4 84.5 77 LYS 91.0 52.5 61.2 78 GLU 46.3 33.4 72.3 79 CYS 87.9 88.6 55.9 80 HIS 34.7 23.1 83.7 81 CYS 92.0 92.7 34.5 82 MET 79.2 49.7 58.7 83 LEU 145.7 98.6 25.3 84 PHE 165.2 99.1 29.2 85 LEU 141.5 95.7 56.2 86 THR 71.9 67.3 61.2 87 PRO 61.0 49.0 66.8 88 ASP 11.4 10.4 80.7 89 ASN 74.0 61.2 62.9 90 ASP 7.6 6.9 80.4 91 PHE 67.9 40.7 68.0 92 ALA 70.9 97.7 61.8 93 GLY 20.8 59.7 66.3 94 ASP 8.9 8.0 78.8 95 ALA 40.3 55.4 69.0 96 GLN 111.5 75.1 52.3 97 ASP 90.8 82.2 60.6 98 ILE 143.5 100.0 31.2 99 PRO 50.2 40.3 72.5 100 MET 101.7 63.8 56.1 101 GLU 21.7 15.6 79.5 102 THR 83.2 77.8 52.4 103 LEU 147.8 100.0 34.1 104 GLU 57.0 41.1 62.5 105 GLU 43.3 31.2 76.5 106 VAL 101.3 85.2 63.6 107 LYS 110.8 63.9 67.9 108 ALA 12.3 17.0 81.2 109 SER 6.1 7.4 78.6