Protein Data Bank File : 1ayfb Title : ELECTRON TRANSPORT 03-NOV-97 1AYF Number of Amino Acid Residues : 104 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP LYS ILE THR VAL HIS PHE ILE ASN ARG 10 ASP GLY GLU THR LEU THR THR LYS GLY LYS 20 ILE GLY ASP SER LEU LEU ASP VAL VAL VAL 30 GLN ASN ASN LEU ASP ILE ASP GLY PHE GLY 40 ALA CYS GLU GLY THR LEU ALA CYS SER THR 50 CYS HIS LEU ILE PHE GLU GLN HIS ILE PHE 60 GLU LYS LEU GLU ALA ILE THR ASP GLU GLU 70 ASN ASP MET LEU ASP LEU ALA TYR GLY LEU 80 THR ASP ARG SER ARG LEU GLY CYS GLN ILE 90 CYS LEU THR LYS ALA MET ASP ASN MET THR 100 VAL ARG VAL PRO Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 127.2 -172.9 0.0 0.0 2 LYS -122.7 -18.7 176.8 119.6 -171.5 -53.5 104.9 3 ILE -116.3 144.2 -177.1 71.0 134.1 4 THR -87.9 135.2 172.2 -55.7 5 VAL -128.3 131.4 175.3 177.2 6 HIS -101.4 119.8 179.9 -53.6 -78.2 7 PHE -106.1 115.7 173.0 -67.0 84.0 8 ILE -82.9 110.7 -174.7 -55.7 -172.6 9 ASN -75.8 171.9 -179.4 -159.8 4.9 10 ARG -62.4 -19.8 179.6 -99.5 175.4 -149.8 111.2 11 ASP -92.3 3.9 176.3 57.6 5.2 12 GLY 83.7 1.8 178.2 13 GLU -89.5 146.9 -177.8 -54.8 -55.6 -21.4 14 THR -95.2 126.2 175.7 -63.1 15 LEU -108.9 118.9 -176.9 -47.7 177.4 16 THR -111.5 132.8 177.1 -56.3 17 THR -150.8 -175.7 -179.8 -173.6 18 LYS -130.0 154.0 176.3 -48.5 -178.0 145.9 -178.5 19 GLY -141.5 174.1 174.8 20 LYS -104.5 146.5 172.8 44.1 -106.1 150.5 -98.3 21 ILE -46.3 130.5 177.5 -59.0 147.7 22 GLY 106.9 -19.8 177.5 23 ASP -78.5 148.2 170.8 -73.9 -20.7 24 SER -77.3 163.3 175.4 79.1 25 LEU -67.4 -26.8 174.2 -57.7 -170.6 26 LEU -62.7 -47.1 174.1 176.5 48.6 27 ASP -51.5 -50.4 -178.3 -70.2 -29.4 28 VAL -56.8 -44.1 179.2 179.4 29 VAL -65.4 -57.2 -170.3 170.6 30 VAL -73.5 -33.7 -177.1 -58.1 31 GLN -71.9 -18.8 177.7 -75.8 173.6 7.1 32 ASN -106.0 7.7 -177.9 -67.8 -76.0 33 ASN 49.8 43.5 175.8 -77.4 -14.7 34 LEU -64.9 144.9 -174.2 -66.5 -158.6 35 ASP -87.9 63.2 178.0 -176.0 23.1 36 ILE -109.6 100.7 -174.3 -57.1 159.7 37 ASP -46.3 119.0 174.4 -170.1 38.7 38 GLY 69.4 7.7 -175.5 39 PHE -71.4 123.4 177.6 -166.5 -77.4 40 GLY 92.0 18.2 -172.9 41 ALA -55.4 -41.0 178.4 42 CYS -80.5 3.9 174.9 92.3 43 GLU 63.4 37.3 174.3 -55.8 -163.8 -18.3 44 GLY 76.5 24.3 -178.8 45 THR -99.3 12.1 175.8 58.2 46 LEU 61.3 40.4 -179.0 -120.9 175.1 47 ALA -124.5 13.2 176.9 48 CYS -151.2 -172.8 171.8 76.4 49 SER -136.3 28.3 -179.6 57.1 50 THR -73.1 -13.7 176.9 64.5 51 CYS -95.8 12.2 177.5 64.1 52 HIS -52.1 129.5 173.2 -178.0 -179.6 53 LEU -133.3 149.0 -179.8 -66.5 162.5 54 ILE -109.3 122.9 -173.7 -65.7 160.7 55 PHE -100.9 157.2 173.0 -69.4 75.1 56 GLU -74.9 148.6 -172.8 -85.1 -179.2 -18.4 57 GLN -51.9 -47.5 -178.8 -172.2 49.4 -140.0 58 HIS -60.5 -30.5 175.7 69.6 -78.8 59 ILE -81.9 -45.4 -176.7 -61.8 -57.8 60 PHE -51.4 -45.4 -178.7 -178.9 79.0 61 GLU -70.1 -10.3 174.2 63.6 -159.6 9.8 62 LYS -100.8 -2.7 -177.5 -99.9 81.0 -161.6 157.4 63 LEU -70.3 159.0 177.0 -59.6 -179.1 64 GLU -61.2 147.9 -177.9 -57.4 -57.3 -38.2 65 ALA -56.9 131.7 -176.6 66 ILE -74.1 132.2 178.5 -173.9 168.2 67 THR -79.5 161.9 176.3 68.3 68 ASP -61.4 -41.5 177.2 -73.6 -8.9 69 GLU -52.8 -56.7 179.5 -152.9 -176.2 -13.4 70 GLU -56.9 -46.3 178.0 179.3 177.3 -17.3 71 ASN -58.7 -44.5 -178.7 -155.9 64.9 72 ASP -60.6 -40.7 -178.9 -71.1 -18.6 73 MET -76.1 -38.8 -179.9 179.6 72.2 56.4 74 LEU -63.9 -28.9 176.9 -167.6 56.7 75 ASP -54.1 -37.5 -175.6 -88.4 -14.7 76 LEU -95.0 12.2 -177.2 -59.3 -48.1 77 ALA -80.3 147.7 172.7 78 TYR -67.1 133.2 173.0 175.6 78.3 79 GLY 68.4 32.9 178.0 80 LEU -60.7 133.0 176.0 178.8 57.3 81 THR -126.2 179.9 175.7 68.5 82 ASP -71.0 -21.2 -178.2 -86.7 -11.4 83 ARG -109.3 32.9 -175.0 -71.4 175.1 -69.4 108.0 84 SER -101.3 144.3 171.8 -73.6 85 ARG -142.8 160.3 171.3 -62.9 -66.5 -62.1 -94.1 86 LEU -83.5 114.4 -176.4 -63.1 179.5 87 GLY -51.9 -31.1 -178.2 88 CYS -74.1 -10.4 179.2 67.2 89 GLN -99.0 -1.2 -174.2 -64.9 -52.1 -69.9 90 ILE -108.2 109.5 179.8 -57.3 -51.4 91 CYS -90.0 134.2 -177.1 -72.7 92 LEU -64.1 135.5 174.0 -131.6 40.4 93 THR -128.2 165.4 177.7 66.1 94 LYS -57.2 -33.2 176.8 -170.5 177.1 -144.4 -126.6 95 ALA -60.7 -23.4 -177.3 96 MET -78.7 -3.7 177.9 -66.4 170.6 -165.9 97 ASP -51.9 125.6 -177.5 -153.9 -4.6 98 ASN 65.5 14.2 176.6 -77.6 -58.0 99 MET -65.3 158.4 178.7 91.3 176.0 161.5 100 THR -121.5 125.6 179.6 -60.0 101 VAL -122.6 150.1 -172.4 -73.1 102 ARG -123.0 137.9 178.3 -179.2 163.4 63.7 79.7 103 VAL -98.1 118.1 178.2 -173.3 104 PRO -80.0 -20.7 0.0 34.4 -40.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP -20.948 -26.876 26.811 2 LYS -19.928 -25.699 30.281 3 ILE -19.330 -21.938 30.385 4 THR -21.808 -19.125 29.815 5 VAL -21.198 -16.210 27.443 6 HIS -23.513 -13.204 27.114 7 PHE -23.420 -11.514 23.700 8 ILE -24.838 -8.001 23.465 9 ASN -26.117 -7.935 19.883 10 ARG -26.220 -4.881 17.593 11 ASP -29.865 -4.291 18.491 12 GLY -28.872 -3.970 22.157 13 GLU -30.440 -7.306 23.107 14 THR -28.543 -9.897 25.121 15 LEU -28.105 -13.376 23.661 16 THR -26.935 -15.903 26.248 17 THR -25.578 -19.344 25.361 18 LYS -22.867 -21.787 26.452 19 GLY -19.655 -23.230 25.010 20 LYS -16.809 -25.526 26.055 21 ILE -13.286 -24.455 26.981 22 GLY -11.162 -24.590 23.822 23 ASP -13.876 -23.432 21.422 24 SER -13.506 -20.091 19.624 25 LEU -16.159 -17.429 20.217 26 LEU -17.005 -17.873 16.530 27 ASP -17.835 -21.523 17.288 28 VAL -20.046 -20.456 20.204 29 VAL -21.970 -18.053 17.974 30 VAL -22.438 -20.189 14.863 31 GLN -22.961 -23.580 16.510 32 ASN -25.858 -22.182 18.531 33 ASN -27.353 -20.233 15.629 34 LEU -27.178 -16.931 17.536 35 ASP -28.893 -14.201 15.513 36 ILE -25.839 -12.019 14.943 37 ASP -26.029 -10.758 11.365 38 GLY -23.059 -11.808 9.247 39 PHE -20.897 -12.898 12.197 40 GLY -18.152 -15.329 11.189 41 ALA -18.457 -14.870 7.401 42 CYS -14.828 -15.768 6.541 43 GLU -15.160 -18.858 8.726 44 GLY -12.326 -18.095 11.129 45 THR -9.624 -17.637 8.502 46 LEU -8.597 -14.153 9.626 47 ALA -9.768 -12.536 6.394 48 CYS -12.599 -10.339 7.683 49 SER -13.714 -8.518 10.825 50 THR -17.318 -9.693 10.960 51 CYS -16.474 -11.570 14.171 52 HIS -15.357 -8.345 15.900 53 LEU -16.301 -8.284 19.584 54 ILE -15.818 -5.652 22.295 55 PHE -14.726 -6.976 25.688 56 GLU -14.986 -5.626 29.231 57 GLN -11.613 -4.351 30.489 58 HIS -10.988 -7.074 33.088 59 ILE -11.434 -9.826 30.478 60 PHE -9.690 -7.985 27.634 61 GLU -6.492 -7.586 29.628 62 LYS -6.332 -11.336 30.276 63 LEU -6.718 -12.362 26.629 64 GLU -3.928 -14.021 24.648 65 ALA -1.445 -11.645 23.009 66 ILE -2.747 -10.274 19.708 67 THR -0.876 -11.273 16.559 68 ASP 0.117 -8.782 13.868 69 GLU -2.197 -10.604 11.448 70 GLU -5.196 -10.076 13.726 71 ASN -4.159 -6.487 14.410 72 ASP -3.766 -5.668 10.690 73 MET -7.303 -6.887 9.949 74 LEU -8.823 -5.425 13.131 75 ASP -7.436 -2.019 12.144 76 LEU -9.956 -1.722 9.305 77 ALA -12.940 -2.868 11.346 78 TYR -16.073 -0.821 11.855 79 GLY -16.362 0.551 15.398 80 LEU -12.847 -0.470 16.384 81 THR -12.100 0.206 20.057 82 ASP -9.216 -0.270 22.479 83 ARG -11.022 -3.345 23.812 84 SER -11.694 -5.020 20.463 85 ARG -10.663 -8.473 19.259 86 LEU -11.579 -10.782 16.369 87 GLY -13.870 -13.357 18.018 88 CYS -12.663 -16.284 15.885 89 GLN -9.198 -15.825 17.387 90 ILE -10.414 -15.975 20.995 91 CYS -10.516 -19.402 22.602 92 LEU -12.799 -19.989 25.528 93 THR -11.162 -20.486 28.925 94 LYS -12.662 -21.048 32.373 95 ALA -12.127 -17.387 33.285 96 MET -14.685 -16.316 30.663 97 ASP -17.690 -17.764 32.512 98 ASN -20.529 -15.249 32.521 99 MET -18.453 -12.676 30.614 100 THR -20.237 -10.144 28.419 101 VAL -19.062 -9.295 24.893 102 ARG -20.635 -6.710 22.591 103 VAL -21.117 -6.689 18.825 104 PRO -20.604 -3.288 17.219 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/T T 10 T T/S S S S S S S S S 20 S C C H H H H H H H 30 H H H C S S S S C T 40 T T T C C C S S S S 50 S S S S S S/H H H H H 60 H H H S S S S/H H H H 70 H H H H H 3 3 C S S 80 S S/S S S S S/T T T T/S S 90 S S S/T T T T C S S S 100 S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E E e T 10 T t e E E E E E E t 20 T T t h H H H H H H 30 H h T t t T T T T 40 T T T T t S S t T 50 e E E E E h H H H H 60 h T t h H H H 70 H H H H h T t T T t 80 t T e E E E e G G g 90 B g G G G g T E E 100 E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 102.5 92.7 68.5 2 LYS 46.0 26.5 72.8 3 ILE 139.6 97.3 48.9 4 THR 88.7 83.0 53.0 5 VAL 118.8 100.0 35.3 6 HIS 107.8 71.8 56.7 7 PHE 166.8 100.0 31.4 8 ILE 93.6 65.2 57.9 9 ASN 109.2 90.3 54.1 10 ARG 120.3 57.6 76.0 11 ASP 37.7 34.2 73.9 12 GLY 5.7 16.5 75.9 13 GLU 34.2 24.7 83.5 14 THR 58.2 54.4 67.4 15 LEU 106.7 72.2 56.3 16 THR 62.0 58.0 61.1 17 THR 87.5 81.8 50.8 18 LYS 61.7 35.6 80.4 19 GLY 34.1 98.1 52.7 20 LYS 74.2 42.8 80.4 21 ILE 71.7 49.9 56.0 22 GLY 5.2 15.1 74.2 23 ASP 88.3 79.9 62.2 24 SER 69.7 83.3 63.8 25 LEU 147.8 100.0 28.3 26 LEU 133.9 90.6 45.6 27 ASP 67.8 61.4 69.5 28 VAL 116.3 97.9 43.2 29 VAL 115.9 97.5 37.1 30 VAL 57.0 48.0 66.1 31 GLN 60.2 40.5 79.5 32 ASN 72.5 59.9 70.5 33 ASN 2.6 2.2 91.2 34 LEU 129.5 87.6 44.7 35 ASP 1.7 1.5 82.3 36 ILE 143.5 100.0 37.8 37 ASP 0.0 0.0 89.5 38 GLY 0.0 0.0 81.0 39 PHE 166.6 99.9 40.3 40 GLY 33.4 96.0 50.1 41 ALA 21.3 29.3 75.6 42 CYS 74.8 75.4 61.4 43 GLU 15.3 11.0 84.7 44 GLY 27.1 77.7 51.7 45 THR 28.6 26.7 75.4 46 LEU 132.6 89.7 57.3 47 ALA 28.4 39.1 66.4 48 CYS 75.4 76.0 55.4 49 SER 65.8 78.7 50.3 50 THR 59.9 56.1 65.5 51 CYS 96.6 97.4 38.2 52 HIS 143.5 95.5 49.2 53 LEU 147.8 100.0 29.1 54 ILE 139.3 97.1 60.6 55 PHE 166.6 99.9 33.6 56 GLU 59.1 42.6 74.2 57 GLN 60.6 40.8 67.5 58 HIS 47.7 31.8 71.4 59 ILE 126.1 87.9 44.5 60 PHE 121.0 72.5 59.5 61 GLU 62.5 45.1 74.8 62 LYS 37.5 21.6 85.8 63 LEU 143.5 97.1 41.7 64 GLU 8.3 6.0 88.5 65 ALA 0.0 0.0 89.9 66 ILE 96.3 67.1 70.5 67 THR 27.8 26.0 78.0 68 ASP 0.0 0.0 85.6 69 GLU 38.0 27.4 75.2 70 GLU 135.7 97.9 43.6 71 ASN 56.1 46.4 68.9 72 ASP 24.9 22.5 82.1 73 MET 101.1 63.4 66.7 74 LEU 140.3 94.9 44.1 75 ASP 53.6 48.5 69.9 76 LEU 30.6 20.7 85.1 77 ALA 71.7 98.8 62.2 78 TYR 11.3 6.3 87.4 79 GLY 8.6 24.8 62.5 80 LEU 96.9 65.6 69.1 81 THR 66.6 62.3 69.1 82 ASP 0.0 0.0 86.7 83 ARG 131.5 63.0 60.7 84 SER 83.5 99.9 49.8 85 ARG 194.9 93.3 42.6 86 LEU 147.5 99.8 34.6 87 GLY 34.8 100.0 43.0 88 CYS 95.9 96.7 45.0 89 GLN 103.5 69.7 60.4 90 ILE 139.2 97.0 44.5 91 CYS 36.3 36.6 76.6 92 LEU 147.8 100.0 38.6 93 THR 51.9 48.5 61.0 94 LYS 18.4 10.6 77.8 95 ALA 11.8 16.3 80.0 96 MET 147.3 92.4 38.9 97 ASP 59.2 53.6 74.7 98 ASN 40.5 33.5 79.2 99 MET 151.6 95.1 33.7 100 THR 74.0 69.2 57.5 101 VAL 118.1 99.4 31.5 102 ARG 105.7 50.6 61.4 103 VAL 118.5 99.7 46.2 104 PRO 111.3 89.4 60.2