Protein Data Bank File : 1cxya Title : ELECTRON TRANSPORT 31-AUG-99 1CXY Number of Amino Acid Residues : 81 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR LEU PRO VAL PHE THR LEU GLU GLN VAL 10 ALA GLU HIS HIS SER PRO ASP ASP CYS TRP 20 MET ALA ILE HIS GLY LYS VAL TYR ASP LEU 30 THR PRO TYR VAL PRO ASN HIS PRO GLY PRO 40 ALA GLY MET MET LEU VAL TRP CYS GLY GLN 50 GLU SER THR GLU ALA TRP GLU THR LYS SER 60 TYR GLY GLU PRO HIS SER SER LEU ALA ALA 70 ARG LEU LEU GLN ARG TYR LEU ILE GLY THR 80 LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 151.4 -178.4 -173.4 2 LEU -64.2 132.0 169.9 -75.8 153.3 3 PRO -55.9 150.8 177.6 -27.3 38.5 4 VAL -113.8 132.8 -178.7 178.5 5 PHE -120.9 164.9 170.7 -60.4 96.4 6 THR -107.1 168.9 173.9 60.1 7 LEU -63.6 -29.7 179.1 -77.3 176.7 8 GLU -64.8 -38.0 177.3 -71.4 71.0 33.6 9 GLN -69.1 -44.3 176.4 -71.5 168.2 -119.4 10 VAL -57.2 -36.8 -178.6 178.2 11 ALA -66.8 -15.3 176.2 12 GLU -75.9 -14.2 -178.5 -69.0 -65.1 -54.9 13 HIS -113.7 76.1 -173.0 -55.7 -96.4 14 HIS -121.3 26.0 -178.7 65.6 85.9 15 SER -128.8 167.6 179.0 -49.7 16 PRO -58.4 -33.2 178.7 -24.6 35.5 17 ASP -91.9 8.0 178.2 68.7 171.0 18 ASP -165.8 77.7 -167.3 -172.5 -177.6 19 CYS -116.9 104.1 175.2 -179.0 20 TRP -109.1 151.7 173.4 -71.0 14.0 21 MET -136.5 160.1 172.4 -63.9 -177.5 -170.4 22 ALA -114.0 127.5 -179.7 23 ILE -138.8 126.8 -179.1 -66.8 163.1 24 HIS 52.3 41.3 178.6 -68.3 -44.0 25 GLY 72.2 9.1 -179.9 26 LYS -117.8 152.7 -179.2 -67.3 167.4 -76.9 -69.4 27 VAL -112.0 133.8 -174.8 176.6 28 TYR -127.5 140.7 175.6 -58.9 85.6 29 ASP -104.1 95.5 -171.4 175.1 -5.3 30 LEU -95.1 10.5 -179.7 -71.8 158.5 31 THR -50.4 -49.6 178.2 -48.4 32 PRO -65.9 -28.6 -177.1 24.2 -38.3 33 TYR -79.5 -24.8 -177.4 -176.3 -100.8 34 VAL -36.3 -59.7 -177.0 162.6 35 PRO -69.3 -12.9 -178.0 26.0 -38.4 36 ASN -95.9 -6.6 -177.1 -66.2 -37.4 37 HIS -63.4 127.8 178.1 -174.0 -123.0 38 PRO -71.7 171.3 177.9 -14.8 34.0 39 GLY 89.5 -171.7 -179.2 40 PRO -55.5 133.6 -178.2 -26.7 39.8 41 ALA -50.2 133.3 174.6 42 GLY 70.3 17.6 178.7 43 MET -69.1 -31.3 -179.3 -72.9 -86.1 -59.1 44 MET -79.1 -28.0 -177.6 -164.5 -174.1 159.2 45 LEU -59.0 -31.1 177.8 -51.8 178.2 46 VAL -64.5 -20.2 -178.5 -9.8 47 TRP -98.4 -1.1 177.2 -59.9 98.1 48 CYS -59.8 134.9 179.1 -66.8 49 GLY 83.6 3.9 -173.6 50 GLN -118.1 164.2 161.0 -58.8 -73.9 -40.9 51 GLU -73.2 117.8 -168.2 -155.7 -62.7 -45.1 52 SER -128.3 24.8 -177.5 -53.6 53 THR -56.5 -46.3 -178.7 -62.5 54 GLU -61.1 -45.2 177.0 177.7 168.9 -103.2 55 ALA -61.1 -40.9 176.5 56 TRP -60.8 -45.0 -175.5 168.3 -104.5 57 GLU -70.5 -29.4 -174.6 -70.3 -73.5 -45.8 58 THR -117.8 -10.8 -172.8 65.7 59 LYS 60.4 17.7 -177.8 -68.2 173.2 174.9 162.5 60 SER 66.6 9.8 175.1 -71.3 61 TYR -138.5 -11.0 177.2 75.4 107.9 62 GLY 115.7 37.0 171.4 63 GLU -138.1 135.2 178.1 0.0 0.0 0.0 64 PRO -76.3 163.4 166.8 32.6 -38.6 65 HIS -76.2 146.2 -178.5 -79.7 89.8 66 SER -69.9 173.1 174.9 70.6 67 SER -65.0 -39.4 174.9 -72.7 68 LEU -56.2 -50.6 178.6 173.5 162.8 69 ALA -59.7 -36.5 179.6 70 ALA -68.1 -33.6 173.9 71 ARG -68.8 -38.8 178.7 -67.2 -176.2 -50.6 -100.4 72 LEU -67.4 -40.8 178.7 -65.3 179.1 73 LEU -59.4 -45.0 -176.9 169.1 61.4 74 GLN -59.7 -30.9 176.5 -158.7 -172.5 85.4 75 ARG -57.5 -30.8 -175.9 175.6 0.0 0.0 0.0 76 TYR -91.6 11.1 178.6 -63.0 103.6 77 LEU -59.1 135.1 172.0 179.8 67.9 78 ILE -126.8 -11.7 179.7 58.4 167.4 79 GLY 174.1 -170.6 177.9 80 THR -113.9 164.5 -179.5 60.4 81 LEU -96.6 -45.9 0.0 -163.1 62.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR 48.139 10.608 26.644 2 LEU 44.567 11.465 25.728 3 PRO 41.937 10.630 28.302 4 VAL 39.379 8.080 27.184 5 PHE 35.658 8.708 27.702 6 THR 32.467 6.779 27.018 7 LEU 29.330 8.132 25.330 8 GLU 27.616 7.873 28.734 9 GLN 30.122 10.296 30.248 10 VAL 29.750 12.682 27.307 11 ALA 25.963 12.580 27.846 12 GLU 26.342 14.094 31.361 13 HIS 27.521 17.317 29.704 14 HIS 24.396 18.086 27.756 15 SER 23.501 21.737 28.415 16 PRO 24.561 25.173 27.145 17 ASP 26.550 25.796 30.324 18 ASP 28.232 22.345 30.259 19 CYS 28.457 21.122 26.676 20 TRP 30.642 18.231 25.509 21 MET 30.318 16.468 22.161 22 ALA 31.785 13.404 20.481 23 ILE 32.737 13.940 16.782 24 HIS 34.784 11.446 14.721 25 GLY 35.621 9.352 17.800 26 LYS 37.068 12.378 19.682 27 VAL 35.614 14.195 22.682 28 TYR 35.450 17.980 22.912 29 ASP 34.512 20.363 25.751 30 LEU 32.748 23.080 23.803 31 THR 31.284 25.047 26.717 32 PRO 33.454 28.166 26.156 33 TYR 32.758 28.063 22.404 34 VAL 28.947 27.996 22.724 35 PRO 28.247 31.748 22.587 36 ASN 30.683 32.235 19.697 37 HIS 29.167 29.794 17.211 38 PRO 28.176 31.595 13.984 39 GLY 24.832 31.056 12.235 40 PRO 21.270 30.738 13.509 41 ALA 21.021 31.028 17.277 42 GLY 21.272 27.757 19.175 43 MET 21.984 25.153 16.443 44 MET 24.902 23.631 18.270 45 LEU 22.958 23.358 21.529 46 VAL 20.812 20.420 20.367 47 TRP 24.027 18.358 20.131 48 CYS 25.480 19.042 23.589 49 GLY 26.121 15.685 25.252 50 GLN 25.840 13.701 22.009 51 GLU 27.661 11.877 19.261 52 SER 27.318 14.623 16.659 53 THR 29.388 13.611 13.627 54 GLU 26.579 13.926 11.062 55 ALA 25.584 17.389 12.274 56 TRP 29.264 18.416 12.188 57 GLU 29.718 17.092 8.671 58 THR 26.578 18.611 7.168 59 LYS 25.517 21.508 9.448 60 SER 22.161 19.643 9.242 61 TYR 21.335 21.083 5.776 62 GLY 24.214 20.026 3.479 63 GLU 27.283 22.206 3.903 64 PRO 30.502 21.121 5.619 65 HIS 32.359 23.102 8.222 66 SER 35.327 24.929 6.798 67 SER 38.973 24.114 7.403 68 LEU 39.041 27.182 9.657 69 ALA 36.141 25.710 11.656 70 ALA 37.943 22.321 11.897 71 ARG 41.005 24.053 13.384 72 LEU 38.758 25.821 15.871 73 LEU 37.033 22.528 16.821 74 GLN 40.373 20.825 17.502 75 ARG 41.341 23.424 20.134 76 TYR 38.463 22.153 22.353 77 LEU 39.672 18.522 22.208 78 ILE 39.829 16.800 25.621 79 GLY 40.093 13.068 24.754 80 THR 38.969 10.119 22.656 81 LEU 35.827 7.995 22.721 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S/H H H H H 10 H H 3 3 T T T T/S S S 20 S S/T T T T/S S S S S S/T 30 T T T/T T T T/S S S S C 40 C T T T T C C C C C 50 C H H H H H H H H/T T 60 T T/S S S S S/H H H H H 70 H H H H H 3 3 C S S 80 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B h H H H H 10 h T e E E T T E E E 20 E E E T e E E E E e 30 T T g G G G g S t 40 T T T g G G G g T t 50 B h H H H H H H h T 60 T T t h H H H H 70 H H H H H h E E E E 80 e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 0.0 0.0 95.7 2 LEU 78.3 53.0 60.6 3 PRO 51.4 41.3 69.8 4 VAL 33.4 28.1 82.2 5 PHE 142.4 85.4 46.3 6 THR 40.4 37.8 73.2 7 LEU 78.8 53.3 58.1 8 GLU 16.3 11.7 77.7 9 GLN 67.3 45.3 66.2 10 VAL 118.8 100.0 40.0 11 ALA 37.9 52.2 76.7 12 GLU 26.7 19.3 81.3 13 HIS 110.8 73.8 61.2 14 HIS 49.3 32.8 82.8 15 SER 48.8 58.4 64.8 16 PRO 55.3 44.4 55.7 17 ASP 9.7 8.8 73.1 18 ASP 55.6 50.3 74.5 19 CYS 99.2 100.0 44.2 20 TRP 170.2 83.0 51.1 21 MET 152.7 95.8 38.2 22 ALA 72.6 100.0 39.1 23 ILE 139.3 97.1 37.4 24 HIS 74.0 49.2 69.1 25 GLY 10.1 29.1 68.8 26 LYS 99.1 57.2 63.4 27 VAL 118.8 100.0 31.0 28 TYR 175.4 96.9 37.7 29 ASP 71.3 64.6 56.4 30 LEU 143.4 97.1 29.5 31 THR 72.7 68.0 66.5 32 PRO 47.7 38.3 70.6 33 TYR 151.1 83.5 40.3 34 VAL 100.7 84.8 41.7 35 PRO 41.8 33.6 80.9 36 ASN 34.8 28.8 77.2 37 HIS 113.4 75.5 62.7 38 PRO 32.3 26.0 86.2 39 GLY 8.1 23.3 65.3 40 PRO 24.2 19.4 73.1 41 ALA 0.0 0.0 90.5 42 GLY 19.3 55.5 65.4 43 MET 84.0 52.7 68.3 44 MET 132.7 83.2 38.9 45 LEU 94.4 63.9 50.4 46 VAL 33.9 28.5 75.4 47 TRP 127.8 62.3 60.9 48 CYS 99.0 99.8 50.5 49 GLY 34.8 100.0 60.4 50 GLN 60.7 40.8 75.9 51 GLU 78.4 56.6 64.1 52 SER 80.4 96.1 46.9 53 THR 75.4 70.5 62.3 54 GLU 5.6 4.0 80.7 55 ALA 63.3 87.2 61.6 56 TRP 165.0 80.5 47.4 57 GLU 67.5 48.7 67.7 58 THR 60.9 56.9 64.9 59 LYS 105.5 60.9 70.4 60 SER 39.9 47.7 67.2 61 TYR 38.6 21.3 77.9 62 GLY 7.9 22.6 69.0 63 GLU 114.4 82.5 58.3 64 PRO 32.2 25.9 81.5 65 HIS 126.4 84.2 52.8 66 SER 26.3 31.4 72.9 67 SER 10.5 12.6 83.3 68 LEU 46.6 31.5 74.5 69 ALA 54.5 75.1 51.2 70 ALA 31.7 43.6 64.8 71 ARG 55.7 26.7 74.6 72 LEU 64.8 43.9 64.8 73 LEU 130.4 88.2 37.5 74 GLN 31.3 21.1 76.2 75 ARG 128.8 61.7 78.9 76 TYR 132.3 73.1 50.5 77 LEU 114.1 77.2 50.8 78 ILE 95.4 66.4 53.0 79 GLY 34.8 100.0 40.5 80 THR 64.8 60.7 54.0 81 LEU 120.9 81.8 43.0