Protein Data Bank File : 1am9b Title : COMPLEX (TRANSCRIPTION REGULATION/DNA) 25-JUN-97 1AM9 Number of Amino Acid Residues : 75 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER ARG GLY GLU LYS ARG THR ALA HIS ASN 10 ALA ILE GLU LYS ARG TYR ARG SER SER ILE 20 ASN ASP LYS ILE ILE GLU LEU LYS ASP LEU 30 VAL VAL GLY THR GLU ALA LYS LEU ASN LYS 40 SER ALA VAL LEU ARG LYS ALA ILE ASP TYR 50 ILE ARG PHE LEU GLN HIS SER ASN GLN LYS 60 LEU LYS GLN GLU ASN LEU SER LEU ARG THR 70 ALA VAL HIS LYS SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 -24.6 175.6 -92.7 2 ARG -65.5 -50.9 178.9 0.0 0.0 0.0 0.0 3 GLY -60.9 -48.2 -179.8 4 GLU -60.9 -36.7 179.3 -64.3 150.1 66.7 5 LYS -66.2 -40.9 178.9 0.0 0.0 0.0 0.0 6 ARG -59.2 -53.0 -179.2 -89.2 -85.2 67.5 -130.7 7 THR -54.0 -46.1 -179.8 -54.7 8 ALA -62.7 -49.2 -179.1 9 HIS -64.3 -31.5 178.9 -156.8 -99.9 10 ASN -57.5 -40.4 177.9 -84.4 -15.4 11 ALA -64.6 -34.9 179.7 12 ILE -67.6 -43.7 -179.9 -75.5 155.1 13 GLU -64.9 -32.6 177.8 -64.8 169.3 7.7 14 LYS -68.1 -42.8 178.1 -170.1 169.6 -179.8 -176.5 15 ARG -57.6 -44.1 179.8 -169.4 -176.8 -57.0 141.2 16 TYR -63.1 -50.6 178.8 162.6 72.3 17 ARG -55.6 -42.5 178.7 -68.0 -159.4 -62.9 -87.8 18 SER -64.7 -31.0 -179.8 -66.1 19 SER -64.3 -25.9 179.0 76.4 20 ILE -92.6 -51.2 -180.0 -66.8 169.6 21 ASN -57.3 -40.4 -179.1 -68.3 -17.7 22 ASP -67.7 -25.1 -179.6 -69.3 -16.0 23 LYS -77.8 -38.4 179.1 -51.1 -76.6 -161.4 -65.9 24 ILE -61.5 -39.1 178.7 -64.4 -175.7 25 ILE -63.3 -40.0 178.0 -73.6 161.2 26 GLU -67.3 -43.1 179.4 -77.0 -171.9 71.8 27 LEU -61.1 -41.5 -178.9 -88.3 176.3 28 LYS -62.3 -42.7 178.9 -176.9 -111.9 155.7 -168.7 29 ASP -63.4 -31.2 -179.7 -78.6 1.1 30 LEU -74.5 -37.4 -176.7 -105.6 -174.4 31 VAL -100.3 -16.7 179.4 -54.8 32 VAL -142.6 -1.3 179.6 -56.8 33 GLY 83.2 -179.8 -176.6 34 THR -78.1 -38.0 -178.0 -83.9 35 GLU -72.4 -29.9 -179.1 -62.7 -156.6 -74.3 36 ALA -64.6 162.7 177.0 37 LYS -126.3 126.2 -178.6 -70.4 -73.2 -176.3 -176.8 38 LEU -152.7 138.7 -178.1 -176.0 62.4 39 ASN -75.9 157.9 -178.4 57.3 -58.8 40 LYS -44.5 -52.2 -177.2 -65.8 178.2 -172.6 172.8 41 SER -65.9 -26.3 -178.8 45.1 42 ALA -77.1 -34.6 178.3 43 VAL -62.4 -44.5 -179.5 173.0 44 LEU -70.3 -43.0 178.2 -58.9 171.9 45 ARG -57.3 -44.2 179.5 178.7 72.5 -89.5 139.3 46 LYS -66.4 -50.1 179.6 -86.3 170.7 174.8 -72.4 47 ALA -52.0 -51.8 179.6 48 ILE -56.3 -52.8 -177.8 -59.7 175.3 49 ASP -63.3 -34.9 -179.5 -63.5 -16.9 50 TYR -67.0 -41.2 179.5 -168.5 29.1 51 ILE -64.5 -46.9 179.5 -73.2 174.2 52 ARG -61.5 -38.1 178.7 -62.0 -164.0 170.8 131.6 53 PHE -63.3 -52.9 -179.9 165.9 66.5 54 LEU -65.3 -31.4 -179.9 -69.5 173.4 55 GLN -63.8 -51.0 178.3 -95.1 170.7 -4.7 56 HIS -63.0 -39.9 -179.8 -74.6 121.0 57 SER -62.9 -39.7 -179.0 -54.4 58 ASN -74.1 -35.4 179.5 -64.9 -9.1 59 GLN -61.8 -63.3 -179.2 -57.1 157.5 -154.0 60 LYS -44.6 -45.8 179.9 -173.0 47.5 155.0 -70.6 61 LEU -64.0 -36.6 179.6 -90.7 171.0 62 LYS -72.4 -35.9 179.4 -77.2 177.1 -172.6 151.8 63 GLN -72.2 -37.0 178.4 179.4 46.2 -115.4 64 GLU -68.4 -39.5 178.2 -179.7 176.4 -47.7 65 ASN -67.3 -30.5 179.1 -75.3 -178.2 66 LEU -62.0 -63.1 -179.5 179.7 52.0 67 SER -50.7 -37.2 180.0 -52.0 68 LEU -69.2 -40.2 179.0 -76.8 157.1 69 ARG -72.2 -41.2 177.5 -90.8 -171.8 -65.2 -102.5 70 THR -57.1 -59.0 177.9 0.0 71 ALA -43.8 -54.7 179.7 72 VAL -56.2 -43.6 180.0 171.6 73 HIS -67.6 -46.9 -179.7 0.0 0.0 74 LYS -78.6 40.0 178.6 0.0 0.0 0.0 0.0 75 SER -166.3 37.1 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER 52.185 36.247 108.880 2 ARG 55.464 36.142 110.820 3 GLY 52.938 36.800 113.540 4 GLU 50.181 34.606 112.045 5 LYS 52.752 31.872 111.726 6 ARG 53.670 32.488 115.383 7 THR 50.072 32.282 116.570 8 ALA 49.554 29.104 114.683 9 HIS 52.737 27.558 116.030 10 ASN 51.823 28.782 119.506 11 ALA 48.800 26.465 119.235 12 ILE 51.150 23.703 118.222 13 GLU 53.397 24.417 121.205 14 LYS 50.468 24.322 123.628 15 ARG 49.466 20.927 122.273 16 TYR 53.089 19.894 122.850 17 ARG 53.332 21.296 126.377 18 SER 50.120 19.460 127.105 19 SER 51.623 16.236 125.782 20 ILE 54.142 16.414 128.638 21 ASN 51.950 18.038 131.264 22 ASP 49.046 15.600 130.937 23 LYS 51.480 12.782 131.539 24 ILE 52.897 14.413 134.652 25 ILE 49.318 14.718 135.900 26 GLU 48.861 10.970 135.283 27 LEU 52.114 10.179 136.991 28 LYS 50.944 12.444 139.834 29 ASP 47.578 10.704 140.183 30 LEU 49.558 7.485 140.389 31 VAL 51.924 8.578 143.107 32 VAL 49.914 10.909 145.331 33 GLY 46.503 10.633 143.914 34 THR 43.972 13.070 142.635 35 GLU 43.077 15.253 145.620 36 ALA 46.662 16.225 146.256 37 LYS 48.405 19.247 144.837 38 LEU 52.038 18.615 144.057 39 ASN 54.433 20.429 141.729 40 LYS 55.910 18.860 138.621 41 SER 59.354 18.016 139.908 42 ALA 58.026 16.315 143.031 43 VAL 55.744 14.227 140.886 44 LEU 58.747 13.138 138.837 45 ARG 61.003 12.679 141.921 46 LYS 58.339 10.422 143.428 47 ALA 57.740 8.550 140.185 48 ILE 61.475 7.893 139.904 49 ASP 61.748 6.823 143.510 50 TYR 58.600 4.737 143.245 51 ILE 59.859 2.865 140.227 52 ARG 63.179 2.222 141.941 53 PHE 61.296 1.079 144.998 54 LEU 59.082 -1.385 143.097 55 GLN 62.054 -2.474 141.097 56 HIS 63.898 -3.502 144.215 57 SER 60.758 -4.986 145.785 58 ASN 60.080 -7.104 142.783 59 GLN 63.736 -8.217 142.492 60 LYS 63.830 -9.267 146.109 61 LEU 60.500 -11.031 145.654 62 LYS 61.766 -12.804 142.530 63 GLN 64.981 -13.962 144.167 64 GLU 62.976 -15.156 147.142 65 ASN 60.511 -16.919 144.848 66 LEU 63.575 -18.342 143.188 67 SER 64.900 -19.726 146.461 68 LEU 61.417 -20.979 147.302 69 ARG 61.095 -22.796 144.021 70 THR 64.631 -24.182 144.227 71 ALA 63.842 -25.435 147.766 72 VAL 60.607 -27.000 146.489 73 HIS 62.444 -28.567 143.549 74 LYS 65.352 -29.630 145.758 75 SER 62.708 -31.457 147.828 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 20 H H H H H H H H H H 30 H H C C S S S S S/H H 40 H H H H H H H H H H 50 H H H H H H H H H H 60 H H H H H H H H H H 70 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 H 20 H H H H H H H H H H 30 H h t S S h H 40 H H H H H H H H H H 50 H H H H H H H H H H 60 H H H H H H H H H H 70 H H H h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 17.8 21.3 87.3 2 ARG 126.4 60.5 84.4 3 GLY 0.1 0.3 70.5 4 GLU 26.0 18.8 86.3 5 LYS 115.3 66.5 78.3 6 ARG 92.4 44.2 80.4 7 THR 16.4 15.3 80.3 8 ALA 16.4 22.6 74.8 9 HIS 65.8 43.8 69.0 10 ASN 55.2 45.7 78.2 11 ALA 21.3 29.4 79.4 12 ILE 66.7 46.4 71.7 13 GLU 89.4 64.5 72.1 14 LYS 38.0 21.9 87.3 15 ARG 54.4 26.1 75.2 16 TYR 51.3 28.3 70.7 17 ARG 90.7 43.4 71.1 18 SER 44.0 52.6 72.8 19 SER 36.8 44.0 70.7 20 ILE 61.6 43.0 71.6 21 ASN 75.5 62.5 60.3 22 ASP 32.6 29.5 69.6 23 LYS 60.1 34.6 74.3 24 ILE 125.7 87.6 37.3 25 ILE 46.0 32.1 75.5 26 GLU 32.4 23.4 76.3 27 LEU 92.6 62.7 49.3 28 LYS 150.2 86.6 54.0 29 ASP 62.7 56.8 71.3 30 LEU 37.0 25.0 76.3 31 VAL 108.3 91.1 44.1 32 VAL 94.5 79.5 48.0 33 GLY 12.2 35.1 79.3 34 THR 23.6 22.1 80.0 35 GLU 0.0 0.0 88.5 36 ALA 38.2 52.6 68.2 37 LYS 1.0 0.6 88.7 38 LEU 110.9 75.0 49.2 39 ASN 31.1 25.7 78.1 40 LYS 64.4 37.1 71.1 41 SER 16.8 20.1 79.8 42 ALA 47.8 65.8 61.8 43 VAL 117.4 98.8 38.2 44 LEU 78.9 53.4 53.6 45 ARG 90.7 43.4 76.7 46 LYS 86.7 50.0 60.8 47 ALA 65.7 90.6 41.4 48 ILE 81.5 56.8 71.9 49 ASP 48.7 44.1 72.6 50 TYR 89.8 49.6 57.1 51 ILE 50.0 34.9 71.7 52 ARG 78.9 37.8 76.2 53 PHE 48.2 28.9 74.1 54 LEU 78.7 53.2 67.5 55 GLN 45.2 30.4 72.9 56 HIS 40.2 26.8 80.7 57 SER 49.7 59.5 56.7 58 ASN 51.4 42.5 64.6 59 GLN 50.7 34.1 71.9 60 LYS 28.8 16.6 83.4 61 LEU 49.1 33.2 81.3 62 LYS 31.9 18.4 80.8 63 GLN 49.5 33.3 71.7 64 GLU 56.2 40.6 65.0 65 ASN 65.7 54.3 65.3 66 LEU 56.3 38.1 81.5 67 SER 29.1 34.8 72.3 68 LEU 51.7 35.0 76.4 69 ARG 57.0 27.3 77.8 70 THR 54.3 50.8 68.6 71 ALA 17.4 24.0 74.3 72 VAL 13.0 11.0 77.8 73 HIS 87.6 58.3 82.0 74 LYS 108.4 62.5 79.2 75 SER 20.9 25.0 78.5