Protein Data Bank File : 1etc Title : TRANSCRIPTION REGULATION 22-MAR-95 1ETC Number of Amino Acid Residues : 106 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ILE GLN LEU TRP GLN PHE LEU LEU GLU LEU 10 LEU THR ASP LYS SER CYS GLN SER PHE ILE 20 SER TRP THR GLY ASP GLY TRP GLU PHE LYS 30 LEU SER ASP PRO ASP GLU VAL ALA ARG ARG 40 TRP GLY LYS ARG LYS ASN LYS PRO LYS MET 50 ASN TYR GLU LYS LEU SER ARG GLY LEU ARG 60 TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS 70 THR ALA GLY LYS ARG TYR VAL TYR ARG PHE 80 VAL CYS ASP LEU GLN SER LEU LEU GLY TYR 90 THR PRO GLU GLU LEU HIS ALA MET LEU ASP 100 VAL LYS PRO ASP ALA ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ILE 0.0 102.1 -179.7 -103.9 136.5 2 GLN -129.8 107.5 179.7 -45.6 129.6 119.2 3 LEU -147.2 -21.2 179.9 11.3 59.3 4 TRP -42.2 -52.5 179.6 -9.5 112.2 5 GLN -78.4 -70.6 -179.9 -31.0 -44.7 -21.5 6 PHE -19.8 -57.3 179.7 162.2 89.8 7 LEU -67.6 -56.5 -179.9 173.9 62.8 8 LEU -63.2 -62.6 179.7 -179.0 40.5 9 GLU -41.8 -49.5 178.8 -170.6 -166.1 -60.9 10 LEU -44.0 -53.6 179.0 -158.9 45.5 11 LEU -70.3 -73.4 179.6 -50.2 141.1 12 THR 7.8 74.2 -179.9 -57.3 13 ASP 158.1 103.6 179.9 -103.6 23.7 14 LYS -75.4 1.3 179.8 167.6 -97.3 -79.5 99.8 15 SER -89.1 24.6 179.9 178.7 16 CYS -121.9 4.5 179.9 -74.8 17 GLN -42.6 163.1 -179.7 -64.8 171.5 137.4 18 SER 83.4 -45.7 179.8 -153.5 19 PHE -82.9 -78.7 -179.5 -27.9 -46.3 20 ILE -152.3 140.7 179.5 82.9 84.8 21 SER 159.8 168.5 180.0 31.9 22 TRP -38.0 160.1 179.6 -35.4 121.5 23 THR -101.5 -63.3 -180.0 -81.9 24 GLY 179.7 -37.3 -179.8 25 ASP -79.7 92.2 -179.5 -133.8 44.5 26 GLY 76.4 -73.1 178.6 27 TRP 172.0 75.6 178.2 42.5 -165.0 28 GLU -97.7 105.8 -176.7 122.2 176.3 41.9 29 PHE -99.6 128.5 -179.6 111.0 80.0 30 LYS -118.4 158.5 179.7 23.2 -179.5 -157.4 -163.0 31 LEU -118.1 108.2 -179.7 -48.5 97.0 32 SER -130.6 -48.3 -179.9 -121.9 33 ASP -117.3 48.0 -180.0 -90.7 51.5 34 PRO -69.6 95.8 179.2 24.1 -31.4 35 ASP -71.3 -80.6 179.8 176.2 0.7 36 GLU -75.9 -23.8 179.5 -42.5 -120.5 43.1 37 VAL -71.4 -36.8 179.0 -86.2 38 ALA -80.0 -21.6 179.5 39 ARG -67.8 -51.7 179.6 -160.4 135.1 -132.3 -112.3 40 ARG -64.4 -48.4 179.9 -87.4 -133.9 -154.7 72.4 41 TRP -62.0 -34.9 179.5 -87.7 21.7 42 GLY -100.3 11.9 -179.9 43 LYS -84.1 24.2 -179.8 -126.0 -142.1 -173.0 177.6 44 ARG -55.2 -13.2 -180.0 -40.5 108.9 50.0 -108.8 45 LYS -38.2 -52.4 179.8 -55.8 -172.0 -102.2 -117.1 46 ASN -89.3 -19.5 179.9 -45.7 -42.2 47 LYS -79.9 165.4 -180.0 -37.0 -51.6 -51.1 -147.7 48 PRO -72.2 -63.5 180.0 23.9 -27.7 49 LYS -157.9 37.4 179.9 56.8 -171.7 -47.9 90.2 50 MET -81.9 81.9 -179.9 173.4 51.6 45.7 51 ASN -104.7 -152.3 -180.0 -48.4 14.9 52 TYR -78.9 -11.4 -179.7 -179.7 36.0 53 GLU -68.6 -74.6 -179.4 -130.3 122.2 -84.3 54 LYS -44.0 -76.6 -179.2 -130.8 157.3 -164.5 -33.6 55 LEU -39.5 -51.8 -179.5 127.7 64.7 56 SER -46.8 -50.2 -180.0 164.1 57 ARG -54.1 -43.3 180.0 -42.7 -156.4 122.6 -132.4 58 GLY -55.9 -71.5 -179.9 59 LEU -67.8 -6.1 -179.3 10.8 134.9 60 ARG -72.9 -41.9 -179.1 162.7 -175.9 -83.6 -142.2 61 TYR -99.8 -17.6 -179.0 155.4 -87.5 62 TYR -19.5 80.3 -179.7 -117.5 26.8 63 TYR -159.7 159.0 -179.8 -135.5 -78.7 64 ASP 78.5 -72.5 179.7 -150.6 -49.4 65 LYS -119.3 7.8 -180.0 -63.3 137.7 -133.2 -56.9 66 ASN -98.9 -104.4 180.0 -89.1 126.9 67 ILE 171.8 -65.4 -177.6 160.8 -81.7 68 ILE -64.3 160.8 179.2 -143.5 -153.0 69 HIS -129.6 162.4 -179.5 62.1 -62.9 70 LYS -99.4 133.0 -180.0 177.4 -110.4 -85.7 -94.2 71 THR -119.7 152.3 -179.9 3.7 72 ALA 56.7 159.6 180.0 73 GLY -129.6 44.7 -179.9 74 LYS -106.8 -64.4 -179.7 -101.3 -110.4 -110.3 -80.8 75 ARG -142.4 -145.8 -179.7 -54.1 101.8 102.7 51.5 76 TYR -60.9 127.4 179.5 -76.9 40.3 77 VAL -165.1 80.1 179.7 170.3 78 TYR -107.4 142.2 -179.5 -27.0 -29.2 79 ARG -141.5 108.7 -179.3 -54.0 165.6 -24.7 124.6 80 PHE -40.3 167.9 -179.6 -87.5 50.9 81 VAL -132.4 -45.5 -179.3 89.8 82 CYS -57.3 -144.3 -179.3 -147.3 83 ASP -108.3 53.9 179.6 -86.0 73.2 84 LEU -80.3 34.4 -179.9 171.0 125.6 85 GLN -86.7 -21.7 -179.8 -38.7 176.8 -1.0 86 SER -122.6 22.6 -179.7 -134.6 87 LEU -87.9 -42.8 -179.9 -75.4 58.7 88 LEU -34.6 -40.8 -179.8 -77.3 179.6 89 GLY -81.4 60.0 -179.9 90 TYR -70.4 94.8 179.6 -81.8 -39.6 91 THR -114.1 -69.3 179.7 13.3 92 PRO -73.7 -24.8 -179.8 24.3 -27.6 93 GLU -64.7 151.0 179.8 -134.6 134.5 -24.2 94 GLU -100.1 83.1 -179.8 -39.3 -119.1 -24.7 95 LEU -72.4 -29.1 180.0 -82.5 -70.7 96 HIS -52.0 -69.6 179.9 -44.8 -57.4 97 ALA -63.0 -55.0 179.9 98 MET -41.8 -27.1 -180.0 -163.3 83.0 -159.9 99 LEU -78.6 -56.2 -179.6 -157.6 -144.8 100 ASP -67.3 -4.6 -179.8 -120.3 51.0 101 VAL -100.0 -178.5 179.7 -161.9 102 LYS -153.9 56.4 -179.3 56.6 -79.3 -146.4 -79.6 103 PRO -76.2 -43.7 -179.8 24.3 -24.7 104 ASP -40.3 -28.4 -180.0 -105.1 37.3 105 ALA -90.3 -50.9 -179.9 106 ASP -67.5 0.0 0.0 76.7 -12.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ILE -7.501 10.984 12.523 2 GLN -5.750 11.227 9.132 3 LEU -6.802 8.844 6.333 4 TRP -8.617 10.994 3.741 5 GLN -5.326 11.214 1.819 6 PHE -3.423 8.086 2.949 7 LEU -6.259 6.091 1.342 8 LEU -6.832 8.485 -1.588 9 GLU -3.194 9.581 -2.046 10 LEU -2.348 5.868 -2.036 11 LEU -4.581 5.513 -5.110 12 THR -4.200 8.984 -6.707 13 ASP -2.820 7.418 -9.908 14 LYS -4.682 5.446 -12.597 15 SER -1.282 3.963 -13.530 16 CYS -1.694 1.333 -10.786 17 GLN -4.584 -0.633 -12.322 18 SER -4.246 -4.420 -11.903 19 PHE -2.891 -3.929 -8.362 20 ILE -5.423 -1.819 -6.444 21 SER -7.631 1.169 -7.326 22 TRP -11.149 2.280 -8.331 23 THR -13.051 -0.250 -10.478 24 GLY -15.282 1.739 -12.874 25 ASP -18.630 2.605 -11.235 26 GLY -17.815 6.043 -9.771 27 TRP -14.683 4.756 -8.013 28 GLU -14.698 1.408 -6.191 29 PHE -11.024 0.744 -5.355 30 LYS -9.951 -2.751 -4.278 31 LEU -6.559 -4.102 -3.135 32 SER -5.582 -7.499 -4.605 33 ASP -2.268 -7.228 -6.505 34 PRO -0.832 -4.237 -4.664 35 ASP 2.836 -4.435 -5.589 36 GLU 4.317 -1.152 -4.299 37 VAL 0.987 -0.302 -2.643 38 ALA 1.176 -3.470 -0.518 39 ARG 4.883 -2.812 0.073 40 ARG 4.275 0.512 1.861 41 TRP 1.154 -0.805 3.638 42 GLY 3.115 -3.951 4.562 43 LYS 6.330 -1.939 5.006 44 ARG 5.720 -1.939 8.780 45 LYS 9.311 -3.265 8.935 46 ASN 10.416 0.267 9.895 47 LYS 6.958 1.196 11.232 48 PRO 5.786 0.308 14.733 49 LYS 2.642 -1.718 13.937 50 MET 0.889 -0.058 10.975 51 ASN -0.475 -3.228 9.333 52 TYR -3.859 -3.969 7.719 53 GLU -5.480 -3.795 11.175 54 LYS -5.257 -0.075 12.034 55 LEU -5.748 1.305 8.495 56 SER -8.502 -1.288 7.916 57 ARG -10.420 0.170 10.882 58 GLY -10.105 3.633 9.297 59 LEU -11.555 2.783 5.862 60 ARG -13.522 0.060 7.681 61 TYR -16.063 2.454 9.226 62 TYR -15.618 5.372 6.760 63 TYR -19.319 6.257 7.201 64 ASP -21.565 8.974 8.681 65 LYS -18.843 11.655 8.640 66 ASN -16.265 9.749 6.557 67 ILE -17.112 8.769 2.956 68 ILE -15.909 5.390 1.574 69 HIS -17.916 2.226 2.309 70 LYS -16.912 -1.448 2.639 71 THR -18.139 -3.916 -0.006 72 ALA -17.979 -7.734 -0.019 73 GLY -16.559 -9.515 3.049 74 LYS -13.650 -11.509 1.583 75 ARG -10.507 -9.334 1.514 76 TYR -9.455 -5.750 0.675 77 VAL -12.418 -3.951 -0.967 78 TYR -12.910 -0.205 -0.313 79 ARG -15.014 2.001 -2.619 80 PHE -15.376 5.783 -2.087 81 VAL -18.971 7.092 -1.782 82 CYS -18.951 10.915 -1.956 83 ASP -17.991 12.625 -5.244 84 LEU -14.338 11.504 -5.487 85 GLN -14.770 11.235 -9.286 86 SER -12.817 14.451 -9.979 87 LEU -10.469 14.385 -6.970 88 LEU -7.638 12.303 -8.497 89 GLY -6.735 15.556 -10.269 90 TYR -5.757 17.279 -7.000 91 THR -4.390 20.567 -8.387 92 PRO -6.097 23.588 -6.826 93 GLU -7.144 21.474 -3.816 94 GLU -4.826 21.671 -0.782 95 LEU -3.973 18.003 -0.127 96 HIS -0.888 19.023 1.886 97 ALA -2.803 20.499 4.843 98 MET -5.979 18.475 4.187 99 LEU -3.636 15.528 4.841 100 ASP -2.080 16.683 8.134 101 VAL -5.621 17.745 9.119 102 LYS -8.632 15.611 10.119 103 PRO -11.762 17.570 9.251 104 ASP -13.621 14.679 7.585 105 ALA -14.132 13.561 11.205 106 ASP -14.772 16.907 12.942 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 10 H H C C C T T T T/S S 20 S S C T T T T/S S S S 30 S S/S S S S/H H H H H H 40 H H H T T T T C S S 50 S S/H H H H H H H H C 60 C C T T T T/S S S S S 70 S S C C S S S S S S 80 S S C T T T T C C T 90 T T T C H H H H H H 100 H T T T T/S S 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 g G G G g T e E 20 E S S S e E E E 30 E e S h H H H H H 40 H h t T T T t S S 50 h H H H H H H H H H 60 H h S S S E E 70 e S S S e E E e 80 S t T T t S S 90 S S S h H H H H H H 100 h t T T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ILE 47.2 32.9 63.0 2 GLN 64.6 43.4 72.6 3 LEU 124.8 84.4 43.4 4 TRP 190.6 93.0 58.1 5 GLN 143.3 96.4 39.2 6 PHE 104.5 62.6 47.5 7 LEU 147.7 99.9 22.7 8 LEU 143.8 97.3 42.7 9 GLU 48.2 34.8 69.3 10 LEU 128.7 87.1 46.1 11 LEU 146.3 99.0 37.1 12 THR 72.9 68.2 55.6 13 ASP 32.6 29.5 74.0 14 LYS 38.8 22.4 81.5 15 SER 6.4 7.6 79.9 16 CYS 70.7 71.3 63.5 17 GLN 41.3 27.8 78.4 18 SER 10.3 12.4 74.0 19 PHE 100.4 60.2 61.7 20 ILE 140.2 97.7 34.0 21 SER 75.2 89.9 48.5 22 TRP 176.7 86.2 33.7 23 THR 63.9 59.8 72.7 24 GLY 0.0 0.0 75.3 25 ASP 0.0 0.0 89.5 26 GLY 17.5 50.3 65.1 27 TRP 181.3 88.5 52.0 28 GLU 103.9 75.0 52.7 29 PHE 166.8 100.0 24.5 30 LYS 74.7 43.1 71.4 31 LEU 146.2 98.9 27.1 32 SER 21.5 25.7 79.3 33 ASP 21.4 19.4 73.3 34 PRO 105.7 84.9 43.5 35 ASP 23.2 21.0 70.6 36 GLU 23.9 17.2 81.3 37 VAL 106.4 89.6 42.0 38 ALA 37.0 51.0 61.8 39 ARG 69.7 33.4 79.9 40 ARG 57.7 27.6 73.5 41 TRP 185.1 90.3 35.3 42 GLY 12.3 35.2 74.8 43 LYS 88.3 50.9 68.9 44 ARG 123.8 59.3 70.1 45 LYS 64.7 37.3 83.8 46 ASN 29.3 24.2 74.7 47 LYS 76.7 44.2 68.1 48 PRO 29.2 23.5 70.4 49 LYS 37.3 21.5 78.1 50 MET 93.8 58.8 56.5 51 ASN 64.4 53.3 72.2 52 TYR 106.1 58.6 60.2 53 GLU 7.5 5.4 83.6 54 LYS 59.3 34.2 67.6 55 LEU 131.9 89.3 31.9 56 SER 67.2 80.4 52.9 57 ARG 63.2 30.2 78.2 58 GLY 17.8 51.3 62.7 59 LEU 145.5 98.4 28.4 60 ARG 84.3 40.4 80.2 61 TYR 66.7 36.8 77.0 62 TYR 179.9 99.4 40.4 63 TYR 50.3 27.8 71.3 64 ASP 39.0 35.3 72.0 65 LYS 49.0 28.3 89.0 66 ASN 106.0 87.6 43.8 67 ILE 122.0 85.0 42.2 68 ILE 143.5 100.0 34.2 69 HIS 117.9 78.5 59.0 70 LYS 78.8 45.4 79.5 71 THR 71.9 67.3 64.8 72 ALA 20.7 28.5 69.7 73 GLY 7.6 21.8 80.6 74 LYS 28.7 16.6 83.7 75 ARG 48.5 23.2 77.0 76 TYR 133.0 73.5 43.5 77 VAL 95.9 80.7 54.0 78 TYR 172.7 95.4 32.6 79 ARG 158.1 75.7 55.3 80 PHE 157.8 94.6 25.4 81 VAL 57.6 48.5 54.4 82 CYS 21.3 21.5 68.5 83 ASP 14.6 13.3 78.3 84 LEU 146.9 99.4 29.3 85 GLN 54.0 36.3 77.1 86 SER 0.7 0.9 82.5 87 LEU 104.3 70.6 63.9 88 LEU 100.2 67.8 62.5 89 GLY 0.0 0.0 82.3 90 TYR 158.4 87.5 48.3 91 THR 14.5 13.5 79.2 92 PRO 23.5 18.8 87.4 93 GLU 52.4 37.8 61.2 94 GLU 21.6 15.6 79.8 95 LEU 116.9 79.1 50.6 96 HIS 0.0 0.0 84.3 97 ALA 18.6 25.7 67.7 98 MET 89.2 56.0 62.6 99 LEU 90.6 61.3 72.3 100 ASP 11.5 10.4 80.0 101 VAL 60.2 50.7 56.8 102 LYS 67.9 39.2 66.7 103 PRO 90.5 72.7 57.0 104 ASP 71.0 64.3 52.7 105 ALA 47.1 64.9 57.2 106 ASP 13.8 12.5 68.6