Protein Data Bank File : 1abv Title : ATP SYNTHESIS 29-JAN-97 1ABV Number of Amino Acid Residues : 105 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER GLU PHE ILE THR VAL ALA ARG PRO TYR 10 ALA LYS ALA ALA PHE ASP PHE ALA VAL GLU 20 HIS GLN SER VAL GLU ARG TRP GLN ASP MET 30 LEU ALA PHE ALA ALA GLU VAL THR LYS ASN 40 GLU GLN MET ALA GLU LEU LEU SER GLY ALA 50 LEU ALA PRO GLU THR LEU ALA GLU SER PHE 60 ILE ALA VAL CYS GLY GLU GLN LEU ASP GLU 70 ASN GLY GLN ASN LEU ILE ARG VAL MET ALA 80 GLU ASN GLY ARG LEU ASN ALA LEU PRO ASP 90 VAL LEU GLU GLN PHE ILE HIS LEU ARG ALA 100 VAL SER GLU ALA THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 71.6 -177.9 -39.5 2 GLU -100.2 169.5 -179.8 -63.4 59.6 55.7 3 PHE -139.5 41.2 -179.6 -116.6 -83.3 4 ILE -47.2 -38.1 179.4 51.6 109.9 5 THR -53.4 -39.9 179.1 -45.3 6 VAL -76.1 -37.9 179.9 160.9 7 ALA -71.2 -31.6 -179.4 8 ARG -42.2 -58.9 179.9 -93.4 -174.1 125.7 135.1 9 PRO -73.1 -40.6 179.4 22.0 -23.0 10 TYR -57.2 -49.6 179.1 -86.9 68.5 11 ALA -72.1 -40.5 179.9 12 LYS -58.9 -61.7 -179.2 -158.9 -58.4 -137.7 -130.9 13 ALA -53.9 -45.7 179.8 14 ALA -65.6 -37.3 179.4 15 PHE -65.4 -43.7 179.4 -175.7 73.6 16 ASP -48.7 -69.3 179.9 -71.7 -39.1 17 PHE -56.8 -36.6 178.6 117.2 88.0 18 ALA -56.4 -37.5 178.6 19 VAL -74.8 -51.1 179.3 172.4 20 GLU -56.0 -45.9 179.9 -70.0 167.9 -60.3 21 HIS -79.1 4.8 -179.8 -83.9 -148.5 22 GLN 55.3 25.0 179.9 -111.6 -179.5 -95.0 23 SER -90.9 -17.7 -179.5 -172.7 24 VAL -34.2 -52.7 -179.7 172.9 25 GLU -58.1 -50.8 179.4 -75.7 -85.6 42.4 26 ARG -74.3 -39.6 179.6 -153.3 78.3 138.7 117.8 27 TRP -58.4 -30.3 179.2 -170.6 44.9 28 GLN -48.1 -46.5 178.9 -160.4 114.3 41.5 29 ASP -66.4 -47.2 179.3 157.1 68.3 30 MET -47.6 -47.5 179.3 -75.0 -168.9 -141.6 31 LEU -67.2 -48.2 179.8 -68.1 121.3 32 ALA -59.5 -59.3 179.2 33 PHE -53.0 -42.6 179.1 -155.6 79.1 34 ALA -60.6 -47.3 179.5 35 ALA -73.0 -33.3 179.8 36 GLU -59.7 -50.7 -179.4 -124.8 65.8 70.9 37 VAL -68.6 -41.7 -179.7 60.2 38 THR -58.9 -30.5 -179.9 24.4 39 LYS -72.1 -15.2 179.7 -73.3 177.0 -70.1 145.3 40 ASN -69.3 131.1 179.6 175.3 -1.1 41 GLU -48.8 -54.3 179.7 -72.0 146.3 -79.2 42 GLN -54.9 -33.8 178.2 -77.4 168.3 -55.7 43 MET -66.4 -44.4 178.0 -163.5 59.1 -106.6 44 ALA -60.8 -40.0 178.4 45 GLU -57.7 -48.4 178.6 -63.7 -171.3 88.4 46 LEU -68.9 -35.2 179.5 -63.5 156.6 47 LEU -66.3 -47.0 179.7 -73.6 158.3 48 SER -85.9 57.6 -179.8 -79.9 49 GLY -74.0 177.3 -179.8 50 ALA -70.5 74.4 179.5 51 LEU 56.6 27.3 180.0 -65.5 158.5 52 ALA -108.9 99.7 179.6 53 PRO -70.8 -45.6 179.2 21.4 -24.0 54 GLU -61.7 -35.8 179.3 55.2 -99.9 83.7 55 THR -59.6 -56.1 -179.7 -66.1 56 LEU -67.3 -37.0 179.5 50.7 106.6 57 ALA -67.8 -61.4 -179.8 58 GLU -57.4 -48.1 179.1 -53.3 -44.0 85.8 59 SER -57.0 -36.4 179.0 -168.5 60 PHE -66.5 -48.7 179.0 -170.7 88.0 61 ILE -56.1 -39.5 179.3 -99.4 92.5 62 ALA -72.9 -46.4 180.0 63 VAL -69.6 -32.4 179.8 76.9 64 CYS -73.2 -32.8 179.7 -162.7 65 GLY 108.7 149.1 -179.9 66 GLU -62.7 -13.8 179.7 -76.3 115.4 -62.3 67 GLN -70.7 63.8 -179.3 55.8 158.8 80.2 68 LEU -134.9 134.6 178.8 -78.5 163.4 69 ASP -62.8 154.1 179.2 -146.1 -66.9 70 GLU -55.0 -38.7 177.6 46.9 132.8 -65.3 71 ASN -70.0 -36.8 179.5 -90.7 -102.2 72 GLY -62.7 -51.4 179.2 73 GLN -59.7 -47.7 178.8 -71.5 -129.2 -23.4 74 ASN -61.0 -43.1 179.1 -84.6 -48.6 75 LEU -52.4 -49.0 179.0 -175.3 132.1 76 ILE -57.8 -47.4 179.0 -57.6 -56.3 77 ARG -60.5 -54.6 178.7 -143.5 -143.1 -100.5 -78.2 78 VAL -52.5 -39.4 178.2 -175.2 79 MET -66.7 -43.7 179.2 -66.9 -107.6 -79.5 80 ALA -66.7 -51.0 179.6 81 GLU -51.0 -42.2 179.8 -102.7 99.2 65.8 82 ASN -85.6 2.6 -179.9 -71.0 -92.7 83 GLY 67.0 33.3 -179.8 84 ARG -124.0 17.3 179.9 -54.6 -75.7 154.9 -99.2 85 LEU -53.4 -32.8 180.0 -130.3 -178.2 86 ASN -65.0 -18.4 179.7 -80.1 88.8 87 ALA -81.0 37.0 179.4 88 LEU -68.8 -38.0 179.5 -146.8 5.6 89 PRO -71.4 -40.0 178.0 21.4 -22.7 90 ASP -51.6 -46.3 178.6 -55.7 71.5 91 VAL -67.3 -43.4 179.1 170.9 92 LEU -56.9 -54.4 179.6 176.4 76.8 93 GLU -55.7 -51.4 178.9 -57.1 -122.6 -88.5 94 GLN -57.3 -42.4 179.2 -113.0 76.1 -136.2 95 PHE -61.9 -48.2 179.4 160.2 65.8 96 ILE -53.1 -47.5 179.0 -95.4 68.5 97 HIS -65.8 -48.9 179.0 -151.1 144.2 98 LEU -54.5 -46.3 179.0 -106.0 76.1 99 ARG -59.3 -53.3 179.4 -145.5 -133.5 128.6 146.8 100 ALA -57.2 -33.7 179.8 101 VAL -65.5 -60.7 -179.8 175.1 102 SER -51.3 -37.6 179.6 -91.8 103 GLU -60.1 -32.2 179.1 -110.6 116.1 -87.2 104 ALA -95.2 -42.1 180.0 105 THR -161.6 -63.4 0.0 -60.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER -4.552 15.675 -3.697 2 GLU -1.672 13.373 -2.691 3 PHE -0.483 12.321 0.812 4 ILE 3.206 11.302 0.307 5 THR 3.939 12.542 3.894 6 VAL 1.708 9.677 5.159 7 ALA 3.124 7.174 2.601 8 ARG 6.767 8.140 3.467 9 PRO 6.719 6.053 6.704 10 TYR 4.152 3.487 5.402 11 ALA 6.405 2.650 2.404 12 LYS 9.620 3.130 4.473 13 ALA 8.632 0.758 7.343 14 ALA 7.234 -1.796 4.838 15 PHE 10.406 -1.462 2.666 16 ASP 12.723 -2.121 5.687 17 PHE 11.203 -5.526 6.547 18 ALA 10.639 -6.116 2.773 19 VAL 14.472 -6.004 2.425 20 GLU 15.168 -8.064 5.611 21 HIS 12.529 -10.657 4.548 22 GLN 14.001 -10.591 0.963 23 SER 10.396 -9.896 -0.219 24 VAL 11.295 -6.552 -1.965 25 GLU 11.351 -8.342 -5.388 26 ARG 7.949 -10.038 -4.767 27 TRP 6.607 -7.105 -2.655 28 GLN 7.176 -4.879 -5.757 29 ASP 4.024 -6.449 -7.306 30 MET 2.105 -6.203 -3.977 31 LEU 2.632 -2.390 -4.045 32 ALA 1.880 -2.132 -7.804 33 PHE -1.221 -4.403 -7.665 34 ALA -2.311 -2.523 -4.485 35 ALA -1.938 0.887 -6.241 36 GLU -3.313 -0.537 -9.556 37 VAL -6.692 -1.523 -7.982 38 THR -6.944 1.656 -5.780 39 LYS -6.746 3.793 -8.975 40 ASN -9.965 2.077 -10.254 41 GLU -13.010 4.400 -9.857 42 GLN -15.098 1.567 -8.294 43 MET -12.187 0.989 -5.853 44 ALA -12.333 4.694 -4.861 45 GLU -16.139 4.274 -4.466 46 LEU -15.540 1.382 -2.003 47 LEU -12.596 3.320 -0.444 48 SER -14.707 6.479 0.136 49 GLY -17.450 4.525 1.998 50 ALA -19.886 6.137 4.489 51 LEU -17.180 6.741 7.178 52 ALA -16.538 2.937 7.237 53 PRO -12.767 2.205 7.442 54 GLU -13.121 -1.589 7.980 55 THR -15.421 -1.718 4.889 56 LEU -12.811 -0.174 2.520 57 ALA -9.893 -1.971 4.308 58 GLU -11.422 -5.501 4.467 59 SER -13.044 -5.034 1.004 60 PHE -9.570 -4.009 -0.279 61 ILE -7.870 -7.147 1.162 62 ALA -10.632 -9.200 -0.559 63 VAL -10.563 -7.215 -3.871 64 CYS -6.709 -7.135 -3.831 65 GLY -6.499 -10.952 -3.319 66 GLU -5.084 -13.184 -0.521 67 GLN -1.614 -12.848 -2.196 68 LEU -0.605 -10.195 0.402 69 ASP 2.225 -10.235 3.000 70 GLU 1.082 -10.056 6.681 71 ASN 2.585 -6.520 6.701 72 GLY 0.859 -5.807 3.325 73 GLN -2.630 -6.792 4.607 74 ASN -2.014 -4.838 7.861 75 LEU -0.657 -1.876 5.806 76 ILE -4.013 -1.648 3.931 77 ARG -5.872 -1.775 7.290 78 VAL -3.517 0.799 8.924 79 MET -4.116 2.954 5.795 80 ALA -7.908 2.412 6.125 81 GLU -7.946 2.935 9.946 82 ASN -6.187 6.320 9.411 83 GLY -8.488 7.087 6.394 84 ARG -5.453 7.103 4.027 85 LEU -6.086 3.847 2.027 86 ASN -6.287 6.034 -1.143 87 ALA -2.560 6.945 -0.603 88 LEU -1.551 3.533 -2.101 89 PRO 0.450 5.173 -4.971 90 ASP 2.239 7.588 -2.569 91 VAL 3.657 4.468 -0.821 92 LEU 4.314 2.803 -4.227 93 GLU 6.291 5.840 -5.542 94 GLN 8.261 6.098 -2.250 95 PHE 8.894 2.303 -2.422 96 ILE 10.150 2.534 -6.060 97 HIS 12.647 5.236 -4.946 98 LEU 13.526 3.339 -1.710 99 ARG 14.111 0.176 -3.812 100 ALA 16.297 2.080 -6.341 101 VAL 18.187 3.591 -3.348 102 SER 19.104 0.258 -1.631 103 GLU 20.223 -1.107 -5.054 104 ALA 22.825 1.736 -5.119 105 THR 23.318 2.210 -1.323 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 H H 10 H H H H H H H H H H 20 H H H H H H H H 3/H H 30 H H H H H H H H H H/H 40 H H H H H H H H H C 50 C H H H H H H H H H 60 H H H H H C C C H H 70 H H H H H H H H H H 80 H H H C C C H H H H 90 H H H H H H H H H H 100 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 10 H H H H H H H H H H 20 h T h H H H H H H H 30 H H H H H H H H h h 40 H H H H H H H h t S 50 S h H H H H H H H H 60 H H H H h S h H 70 H H H H H H H H H H 80 H h T g G G h H H H 90 H H H H H H H H H H 100 H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 0.0 0.0 95.3 2 GLU 32.7 23.6 86.0 3 PHE 74.0 44.3 68.7 4 ILE 66.3 46.2 72.4 5 THR 14.2 13.3 66.8 6 VAL 84.9 71.5 41.8 7 ALA 72.6 100.0 46.5 8 ARG 64.7 31.0 72.2 9 PRO 54.1 43.5 67.8 10 TYR 145.5 80.4 42.4 11 ALA 72.6 100.0 44.5 12 LYS 68.9 39.7 72.6 13 ALA 14.4 19.8 81.4 14 ALA 67.0 92.3 45.0 15 PHE 155.7 93.4 40.4 16 ASP 60.1 54.4 69.4 17 PHE 142.4 85.4 59.4 18 ALA 72.6 100.0 34.0 19 VAL 58.9 49.6 61.0 20 GLU 26.9 19.4 75.2 21 HIS 48.3 32.1 71.6 22 GLN 1.2 0.8 91.8 23 SER 68.4 81.8 55.9 24 VAL 101.4 85.4 42.5 25 GLU 26.1 18.9 87.3 26 ARG 23.6 11.3 86.5 27 TRP 197.5 96.3 30.8 28 GLN 98.3 66.2 56.0 29 ASP 49.8 45.0 71.6 30 MET 136.9 85.9 60.0 31 LEU 142.4 96.3 33.9 32 ALA 39.5 54.5 68.2 33 PHE 79.2 47.5 74.1 34 ALA 67.8 93.5 38.8 35 ALA 72.3 99.6 47.7 36 GLU 57.7 41.6 71.6 37 VAL 96.1 80.9 42.3 38 THR 104.7 97.9 38.1 39 LYS 69.3 40.0 76.0 40 ASN 51.0 42.2 74.8 41 GLU 0.0 0.0 86.9 42 GLN 29.4 19.8 82.7 43 MET 157.4 98.7 36.9 44 ALA 36.3 50.0 73.7 45 GLU 33.5 24.2 73.1 46 LEU 69.9 47.3 66.2 47 LEU 147.6 99.8 44.8 48 SER 14.1 16.8 88.6 49 GLY 20.6 59.3 78.8 50 ALA 0.0 0.0 82.6 51 LEU 0.0 0.0 91.2 52 ALA 46.3 63.8 68.5 53 PRO 75.8 60.9 70.5 54 GLU 39.0 28.1 67.7 55 THR 41.5 38.8 63.2 56 LEU 132.7 89.8 50.3 57 ALA 72.6 100.0 48.0 58 GLU 67.3 48.6 67.8 59 SER 52.3 62.6 54.2 60 PHE 166.8 100.0 26.4 61 ILE 111.0 77.4 56.9 62 ALA 11.9 16.4 79.9 63 VAL 65.7 55.3 56.1 64 CYS 98.1 98.9 36.8 65 GLY 14.1 40.4 81.0 66 GLU 0.0 0.0 89.6 67 GLN 47.3 31.8 78.2 68 LEU 143.9 97.3 46.1 69 ASP 79.8 72.2 51.6 70 GLU 30.8 22.2 85.5 71 ASN 69.8 57.7 58.2 72 GLY 28.8 82.8 57.2 73 GLN 97.7 65.7 55.4 74 ASN 41.6 34.4 72.0 75 LEU 126.4 85.5 36.6 76 ILE 141.2 98.4 29.8 77 ARG 105.3 50.4 76.7 78 VAL 54.6 46.0 69.2 79 MET 159.4 100.0 35.9 80 ALA 72.6 100.0 49.3 81 GLU 71.3 51.4 60.7 82 ASN 48.9 40.5 71.1 83 GLY 6.8 19.6 79.2 84 ARG 128.1 61.3 52.4 85 LEU 146.3 99.0 32.9 86 ASN 54.2 44.9 65.7 87 ALA 67.8 93.3 50.7 88 LEU 146.3 99.0 32.9 89 PRO 80.5 64.6 58.5 90 ASP 102.6 92.9 40.5 91 VAL 118.7 99.9 33.2 92 LEU 113.1 76.5 45.1 93 GLU 27.0 19.5 73.6 94 GLN 115.5 77.7 47.5 95 PHE 166.8 100.0 32.8 96 ILE 63.3 44.1 61.8 97 HIS 26.6 17.7 72.3 98 LEU 108.5 73.4 44.1 99 ARG 162.0 77.6 63.5 100 ALA 22.6 31.2 72.3 101 VAL 46.5 39.1 73.6 102 SER 47.6 57.0 66.9 103 GLU 56.8 41.0 77.6 104 ALA 10.1 13.8 86.7 105 THR 0.0 0.0 89.5