Protein Data Bank File : 1jer Title : ELECTRON TRANSPORT 21-AUG-96 1JER Number of Amino Acid Residues : 110 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET GLN SER THR VAL HIS ILE VAL GLY ASP 10 ASN THR GLY TRP SER VAL PRO SER SER PRO 20 ASN PHE TYR SER GLN TRP ALA ALA GLY LYS 30 THR PHE ARG VAL GLY ASP SER LEU GLN PHE 40 ASN PHE PRO ALA ASN ALA HIS ASN VAL HIS 50 GLU MET GLU THR LYS GLN SER PHE ASP ALA 60 CYS ASN PHE VAL ASN SER ASP ASN ASP VAL 70 GLU ARG THR SER PRO VAL ILE GLU ARG LEU 80 ASP GLU LEU GLY MET HIS TYR PHE VAL CYS 90 THR VAL GLY THR HIS CYS SER ASN GLY GLN 100 LYS LEU SER ILE ASN VAL VAL ALA ALA ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 112.2 175.4 0.0 0.0 0.0 2 GLN -73.7 148.0 171.2 -59.4 -60.8 109.3 3 SER -73.2 166.0 -176.1 -68.6 4 THR -103.1 145.6 170.0 -66.5 5 VAL -106.1 111.3 -174.8 178.0 6 HIS -88.7 140.8 178.8 -58.0 -88.7 7 ILE -97.9 109.7 -173.9 -60.3 -56.4 8 VAL -58.4 123.6 -178.3 173.1 9 GLY 75.2 10.4 -178.3 10 ASP 48.9 -128.0 -173.9 -61.0 -31.6 11 ASN -67.3 -19.3 -178.0 -73.1 157.1 12 THR -75.0 -30.8 179.2 -61.8 13 GLY 76.5 -164.0 -173.8 14 TRP -104.2 108.1 179.7 -172.7 -132.6 15 SER -154.8 -179.7 176.2 61.3 16 VAL -80.1 122.7 -170.7 177.9 17 PRO -82.9 161.6 177.4 34.6 -37.3 18 SER -74.4 -35.6 175.3 -14.9 19 SER -112.1 135.7 -178.5 -82.0 20 PRO -62.9 -16.5 -178.0 23.9 -34.6 21 ASN -94.2 4.4 -174.4 59.2 140.7 22 PHE -50.6 -53.3 -172.1 -178.0 80.7 23 TYR -78.0 -23.1 178.0 -76.3 -66.5 24 SER -78.1 -26.4 172.5 64.7 25 GLN -71.2 -34.4 -178.5 -74.7 -176.8 -34.5 26 TRP -64.7 -45.6 -177.9 171.5 80.9 27 ALA -65.1 -35.7 -178.0 28 ALA -70.1 -12.8 176.5 29 GLY -89.3 0.5 -174.9 30 LYS -122.1 166.5 170.5 -53.9 -73.2 -173.4 160.8 31 THR -121.1 127.0 -175.2 -71.8 32 PHE -108.8 127.9 -178.4 -63.2 -77.2 33 ARG -119.4 150.8 179.3 -64.2 -178.6 -178.6 -81.0 34 VAL -52.2 135.4 -175.7 168.6 35 GLY 103.4 -26.8 -179.3 36 ASP -76.6 170.5 176.8 -79.5 -1.5 37 SER -131.2 163.8 179.7 -71.1 38 LEU -120.0 127.0 178.1 -78.8 -170.5 39 GLN -106.5 122.8 178.8 175.5 161.5 -25.6 40 PHE -108.1 119.6 -178.8 -73.3 86.4 41 ASN -111.0 128.2 179.1 -70.8 -35.2 42 PHE -157.9 164.3 177.5 48.0 -86.2 43 PRO -68.0 130.4 -178.0 9.1 -8.3 44 ALA -46.9 149.8 175.8 45 ASN 67.8 -10.4 -179.2 -80.4 27.9 46 ALA -91.2 -28.0 -178.6 47 HIS -142.0 -174.4 172.5 -66.7 -69.5 48 ASN -152.4 -179.5 179.4 56.2 -147.3 49 VAL -135.1 123.3 179.9 -178.4 50 HIS -133.0 133.2 178.2 173.1 66.9 51 GLU -89.0 136.5 179.5 -179.8 178.6 4.4 52 MET -104.0 155.5 -179.0 -36.0 -113.1 73.9 53 GLU -77.5 -48.2 -170.4 -2.6 47.6 80.3 54 THR -121.0 154.5 178.3 -49.2 55 LYS -64.2 -34.1 -175.6 -179.0 -166.1 162.5 49.0 56 GLN -64.0 -49.0 178.5 -76.6 61.5 68.7 57 SER -62.4 -44.6 179.2 -75.0 58 PHE -59.1 -47.0 -177.1 172.9 72.4 59 ASP -61.6 -38.4 -174.9 -74.0 -13.6 60 ALA -89.3 -1.1 -171.2 61 CYS 51.6 45.8 -178.0 -60.8 62 ASN -101.2 113.7 -169.2 -178.1 132.0 63 PHE -105.9 22.9 -176.7 -55.3 -39.0 64 VAL -56.2 -31.6 177.9 92.6 65 ASN -96.7 16.5 -173.9 -58.8 134.3 66 SER -86.4 156.7 -172.3 -35.0 67 ASP -95.6 103.3 172.8 -136.7 -76.6 68 ASN 7.7 -12.0 -176.7 23.0 -131.3 69 ASP 101.2 -125.9 173.0 -130.5 -69.0 70 VAL 103.8 -63.0 -175.8 131.8 71 GLU -103.5 121.2 179.3 38.0 173.4 -51.5 72 ARG -123.5 27.4 179.9 -66.9 -143.8 -167.7 154.7 73 THR -87.1 150.9 -177.9 49.7 74 SER -128.2 148.7 1.4 166.9 75 PRO -82.7 153.8 175.2 32.1 -40.6 76 VAL -106.7 124.0 -176.7 166.4 77 ILE -119.1 119.5 -175.4 -70.0 139.1 78 GLU -109.2 134.0 179.2 -69.3 -80.9 -22.1 79 ARG -85.5 140.4 178.5 -157.2 169.3 -137.1 -94.8 80 LEU -100.3 99.9 -171.9 -59.5 177.9 81 ASP -95.1 -23.5 -173.1 -76.6 -35.7 82 GLU -129.1 153.5 178.5 -8.6 -108.5 19.0 83 LEU -72.6 161.4 170.7 -69.1 -178.1 84 GLY 96.4 -169.8 -171.7 85 MET -74.7 138.6 175.5 -74.1 -49.0 -67.2 86 HIS -130.8 144.4 -173.8 -71.6 76.1 87 TYR -129.1 127.9 179.7 -65.1 -66.2 88 PHE -129.6 145.6 178.9 -63.8 -86.0 89 VAL -142.5 169.6 168.6 -63.0 90 CYS -104.3 128.9 -173.7 175.5 91 THR -96.9 8.4 179.0 64.6 92 VAL -77.3 131.2 171.8 166.0 93 GLY 44.5 -126.7 -179.9 94 THR -102.7 15.7 -173.6 54.7 95 HIS -58.0 -42.8 -178.7 -63.8 -172.3 96 CYS -64.4 -45.0 179.8 175.6 97 SER -62.3 -22.4 -179.1 -62.6 98 ASN -92.0 11.7 173.3 -78.8 127.0 99 GLY 103.3 1.8 179.8 100 GLN -89.0 77.3 -179.4 -169.8 175.0 17.2 101 LYS -157.0 152.0 -171.5 57.5 -161.9 -49.2 -167.4 102 LEU -144.1 130.7 175.8 166.6 80.2 103 SER -123.3 131.9 -177.1 63.8 104 ILE -135.0 155.7 -179.3 60.2 154.8 105 ASN -110.5 120.6 -178.2 178.0 -130.6 106 VAL -98.1 127.7 178.7 -176.3 107 VAL -112.8 170.8 -177.4 -60.1 108 ALA -66.1 168.7 177.9 109 ALA -94.9 -34.4 179.6 110 ASN -67.7 135.3 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 45.488 24.587 65.688 2 GLN 45.180 25.109 61.937 3 SER 41.731 25.548 60.355 4 THR 40.648 23.000 57.752 5 VAL 40.559 23.467 53.975 6 HIS 37.692 21.212 52.901 7 ILE 37.780 19.872 49.324 8 VAL 34.242 20.213 47.994 9 GLY 33.110 16.765 46.851 10 ASP 36.417 15.240 47.985 11 ASN 38.040 13.418 45.002 12 THR 35.051 14.221 42.773 13 GLY 35.556 17.936 42.915 14 TRP 32.978 20.463 41.740 15 SER 30.956 19.257 38.718 16 VAL 27.403 18.373 37.773 17 PRO 26.714 15.247 39.798 18 SER 25.031 12.004 38.691 19 SER 22.716 12.182 41.714 20 PRO 21.167 15.506 42.688 21 ASN 21.756 14.870 46.378 22 PHE 25.506 14.449 45.967 23 TYR 26.770 17.681 47.528 24 SER 24.249 17.745 50.340 25 GLN 25.348 14.275 51.404 26 TRP 28.961 15.432 51.195 27 ALA 28.267 18.501 53.361 28 ALA 26.329 16.473 55.984 29 GLY 29.420 14.363 56.680 30 LYS 31.583 17.352 57.719 31 THR 31.609 20.088 60.404 32 PHE 32.505 23.570 59.072 33 ARG 33.944 26.197 61.465 34 VAL 34.630 29.919 61.009 35 GLY 38.187 30.166 59.677 36 ASP 37.963 27.026 57.528 37 SER 37.976 27.354 53.743 38 LEU 36.202 25.490 50.919 39 GLN 38.267 24.538 47.855 40 PHE 36.310 23.974 44.589 41 ASN 38.379 22.122 41.933 42 PHE 37.033 21.881 38.372 43 PRO 38.330 22.079 34.781 44 ALA 38.972 25.713 33.924 45 ASN 36.261 27.432 31.961 46 ALA 33.676 24.664 32.497 47 HIS 32.040 25.855 35.747 48 ASN 32.239 28.694 38.251 49 VAL 31.497 29.335 41.923 50 HIS 29.089 32.003 43.136 51 GLU 27.827 32.593 46.656 52 MET 24.103 33.441 46.953 53 GLU 22.505 35.638 49.627 54 THR 19.203 33.873 50.328 55 LYS 17.848 30.342 50.405 56 GLN 14.989 31.300 48.069 57 SER 17.349 32.343 45.271 58 PHE 19.600 29.294 45.856 59 ASP 16.579 27.010 45.819 60 ALA 15.250 28.463 42.601 61 CYS 18.708 28.819 40.949 62 ASN 17.691 32.446 40.339 63 PHE 20.797 34.476 39.564 64 VAL 19.255 37.873 39.012 65 ASN 21.471 39.375 41.680 66 SER 24.467 37.341 40.480 67 ASP 27.626 38.601 38.990 68 ASN 27.783 38.442 35.316 69 ASP 30.332 35.653 35.749 70 VAL 33.817 36.586 34.500 71 GLU 36.250 34.245 36.376 72 ARG 36.235 30.500 35.652 73 THR 39.721 29.706 36.925 74 SER 40.167 26.798 39.349 75 PRO 40.774 26.173 42.092 76 VAL 38.471 28.681 43.788 77 ILE 39.048 28.735 47.580 78 GLU 36.412 30.519 49.672 79 ARG 36.989 31.482 53.301 80 LEU 34.173 30.814 55.772 81 ASP 34.150 34.101 57.652 82 GLU 30.643 34.234 59.161 83 LEU 28.401 31.920 61.162 84 GLY 25.271 30.358 59.722 85 MET 24.081 29.056 56.371 86 HIS 26.100 29.701 53.207 87 TYR 24.909 28.846 49.695 88 PHE 27.174 28.366 46.649 89 VAL 26.183 27.454 43.105 90 CYS 27.565 27.152 39.606 91 THR 25.774 29.681 37.362 92 VAL 26.673 28.034 34.043 93 GLY 23.708 26.884 32.034 94 THR 21.486 24.394 33.827 95 HIS 24.181 23.139 36.230 96 CYS 22.524 24.550 39.355 97 SER 19.154 23.056 38.451 98 ASN 20.961 19.731 37.895 99 GLY 22.371 19.683 41.419 100 GLN 25.612 21.639 41.237 101 LYS 24.861 23.710 44.346 102 LEU 26.015 23.380 47.975 103 SER 24.576 24.724 51.233 104 ILE 26.581 24.489 54.416 105 ASN 26.173 25.536 58.035 106 VAL 29.195 27.274 59.564 107 VAL 29.653 27.141 63.353 108 ALA 32.106 28.884 65.649 109 ALA 35.640 27.639 66.176 110 ASN 35.931 28.020 69.949 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S/T T T T 10 C C S S S S C C C C 20 H H H H H H H H H 3/S 30 S S S S S S S S S S 40 S S S/T T T T/S S S S S 50 S S S S/H H H H H H H 60 H/S S S S S S S S/S S S 70 S/S S S S/P S S S S S S 80 S/S S S S/S S S S S S C 90 C C C H H H H H H S 100 S S S S S S 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 g G 10 G G g S S S t T 20 h H H H H H H H h t 30 E E e T e E E E E 40 t T T T t E 50 E E S h H H H H H H 60 h t t T T t 70 S E E E E e 80 S S E E E E E E e 90 t T T g G G G g e 100 E E E E E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 115.6 72.5 95.7 2 GLN 0.0 0.0 92.6 3 SER 43.5 52.1 80.0 4 THR 39.1 36.5 76.2 5 VAL 54.1 45.5 68.0 6 HIS 137.3 91.4 46.4 7 ILE 87.7 61.1 76.8 8 VAL 118.8 100.0 28.3 9 GLY 34.8 100.0 42.9 10 ASP 47.2 42.7 72.4 11 ASN 0.0 0.0 88.0 12 THR 45.2 42.3 74.9 13 GLY 29.2 83.9 76.5 14 TRP 205.0 100.0 39.1 15 SER 48.6 58.2 73.0 16 VAL 79.2 66.7 58.6 17 PRO 116.0 93.2 57.2 18 SER 0.0 0.0 89.9 19 SER 31.4 37.5 71.8 20 PRO 31.9 25.7 81.6 21 ASN 61.9 51.2 72.9 22 PHE 106.5 63.8 60.1 23 TYR 179.4 99.1 46.0 24 SER 24.2 28.9 76.3 25 GLN 32.1 21.6 84.6 26 TRP 184.5 90.0 45.9 27 ALA 65.2 89.8 50.1 28 ALA 9.8 13.5 84.8 29 GLY 0.3 0.7 81.9 30 LYS 112.7 65.0 69.6 31 THR 36.9 34.5 72.6 32 PHE 162.1 97.2 38.4 33 ARG 100.9 48.3 71.5 34 VAL 75.3 63.4 59.8 35 GLY 25.9 74.3 75.6 36 ASP 103.6 93.7 58.3 37 SER 69.8 83.6 47.6 38 LEU 147.8 100.0 23.7 39 GLN 111.5 75.1 48.0 40 PHE 166.8 100.0 24.8 41 ASN 71.4 59.1 58.6 42 PHE 161.0 96.5 48.2 43 PRO 36.1 29.0 70.9 44 ALA 23.2 32.0 76.7 45 ASN 16.1 13.3 76.1 46 ALA 36.2 49.9 69.3 47 HIS 134.8 89.8 41.9 48 ASN 120.4 99.6 51.5 49 VAL 118.3 99.6 34.8 50 HIS 110.8 73.8 62.6 51 GLU 72.5 52.3 63.8 52 MET 158.5 99.5 50.1 53 GLU 61.5 44.4 72.7 54 THR 56.4 52.8 71.7 55 LYS 74.4 42.9 75.2 56 GLN 20.0 13.5 74.6 57 SER 65.2 78.0 63.7 58 PHE 152.7 91.5 46.5 59 ASP 62.9 57.0 68.7 60 ALA 21.8 30.1 76.2 61 CYS 90.0 90.7 56.9 62 ASN 56.1 46.4 64.9 63 PHE 127.2 76.3 55.9 64 VAL 12.7 10.7 92.2 65 ASN 35.3 29.2 80.0 66 SER 77.4 92.6 50.2 67 ASP 29.1 26.3 81.1 68 ASN 25.4 21.0 77.1 69 ASP 80.2 72.6 78.8 70 VAL 19.7 16.6 79.2 71 GLU 34.4 24.8 75.3 72 ARG 132.7 63.5 70.7 73 THR 13.3 12.4 78.2 74 SER 74.9 89.6 58.9 75 PRO 67.7 54.3 72.8 76 VAL 92.6 78.0 60.7 77 ILE 76.3 53.2 64.4 78 GLU 85.4 61.6 56.2 79 ARG 75.8 36.3 82.5 80 LEU 146.5 99.1 38.3 81 ASP 45.0 40.7 70.2 82 GLU 29.0 20.9 81.5 83 LEU 55.7 37.7 67.0 84 GLY 10.0 28.7 79.0 85 MET 85.8 53.8 72.4 86 HIS 132.5 88.2 51.8 87 TYR 158.0 87.3 42.8 88 PHE 164.3 98.5 32.7 89 VAL 118.8 100.0 31.0 90 CYS 99.2 100.0 57.2 91 THR 96.6 90.4 46.8 92 VAL 93.2 78.4 71.3 93 GLY 0.0 0.0 73.1 94 THR 17.4 16.3 82.9 95 HIS 111.9 74.5 57.8 96 CYS 97.7 98.5 46.5 97 SER 26.0 31.1 69.4 98 ASN 45.0 37.2 73.1 99 GLY 30.7 88.1 58.8 100 GLN 148.6 100.0 38.2 101 LYS 131.4 75.8 53.5 102 LEU 146.2 98.9 27.8 103 SER 59.9 71.7 46.1 104 ILE 140.5 97.9 26.7 105 ASN 53.0 43.9 59.9 106 VAL 118.8 100.0 46.1 107 VAL 61.0 51.3 70.1 108 ALA 27.3 37.6 67.9 109 ALA 32.8 45.2 73.0 110 ASN 75.4 62.4 86.8