Protein Data Bank File : 1bqv Title : TRANSCRIPTION FACTOR 19-AUG-98 1BQV Number of Amino Acid Residues : 110 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET GLU CYS ALA ASP VAL PRO LEU LEU THR 10 PRO SER SER LYS GLU MET MET SER GLN ALA 20 LEU LYS ALA THR PHE SER GLY PHE THR LYS 30 GLU GLN GLN ARG LEU GLY ILE PRO LYS ASP 40 PRO ARG GLN TRP THR GLU THR HIS VAL ARG 50 ASP TRP VAL MET TRP ALA VAL ASN GLU PHE 60 SER LEU LYS GLY VAL ASP PHE GLN LYS PHE 70 CYS MET SER GLY ALA ALA LEU CYS ALA LEU 80 GLY LYS GLU CYS PHE LEU GLU LEU ALA PRO 90 ASP PHE VAL GLY ASP ILE LEU TRP GLU HIS 100 LEU GLU ILE LEU GLN LYS GLU ASP VAL LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 -59.2 179.9 -142.2 -157.6 146.0 2 GLU -86.9 177.4 179.9 -109.7 169.0 86.7 3 CYS -59.0 122.9 -179.9 -135.2 4 ALA -94.3 53.4 -179.9 5 ASP -147.6 118.5 -179.8 -67.8 -81.6 6 VAL 63.7 87.7 -179.8 -173.7 7 PRO -74.0 104.5 179.8 27.3 -31.4 8 LEU 61.7 -164.7 -179.8 -33.4 143.5 9 LEU -58.7 141.1 179.8 177.6 73.1 10 THR -87.6 158.0 179.9 58.3 11 PRO -53.6 136.2 -179.9 -25.2 34.3 12 SER -62.2 -34.8 180.0 63.9 13 SER -76.4 -92.5 179.7 -63.0 14 LYS -172.3 36.3 179.7 -147.5 -159.2 102.4 -73.4 15 GLU -78.1 76.1 -179.8 -90.6 -90.4 86.3 16 MET -76.5 155.2 -179.8 -95.5 -64.9 -155.5 17 MET -64.6 125.0 -179.8 60.6 -159.0 -92.9 18 SER -164.5 73.9 179.8 48.0 19 GLN -77.7 -85.8 179.1 -72.8 -93.7 2.4 20 ALA -76.3 18.6 -180.0 21 LEU -74.0 104.5 179.1 -114.1 -63.2 22 LYS -67.7 -2.9 -179.7 74.8 162.7 -78.1 111.3 23 ALA 89.4 44.4 179.5 24 THR -90.8 76.2 179.8 52.0 25 PHE -54.3 -56.2 178.7 -60.6 -80.2 26 SER -100.4 -20.1 -179.9 55.8 27 GLY -58.3 -41.8 179.9 28 PHE -63.0 -45.4 179.5 92.9 86.1 29 THR -60.2 -40.9 -179.1 -46.1 30 LYS -56.1 -32.8 179.7 97.8 -168.7 -122.6 80.3 31 GLU -55.7 -34.9 -180.0 -94.3 71.1 -86.4 32 GLN -92.1 -31.7 -179.5 -53.0 157.0 -39.5 33 GLN -78.5 -57.7 -179.2 159.5 66.5 19.5 34 ARG -60.6 -65.3 -178.8 161.7 60.3 114.9 79.9 35 LEU -69.6 -49.0 179.8 -60.5 138.7 36 GLY 116.3 31.2 179.6 37 ILE -70.8 137.3 -179.3 -68.7 -59.4 38 PRO -57.1 -66.5 -179.6 -25.3 37.9 39 LYS -167.7 -52.5 179.6 40.3 -169.3 -77.0 138.1 40 ASP -134.6 113.9 -179.3 -113.7 67.7 41 PRO -74.1 19.3 178.5 25.6 -28.7 42 ARG -87.4 -34.1 -180.0 58.2 143.3 112.3 173.7 43 GLN -163.3 79.3 179.1 -111.1 140.8 60.7 44 TRP -68.5 -167.9 179.7 -70.8 -30.3 45 THR -132.5 151.4 180.0 19.4 46 GLU -44.0 -30.3 179.6 -79.9 172.1 88.3 47 THR -58.9 -75.6 179.9 -65.7 48 HIS -75.2 -16.7 177.5 41.0 -120.5 49 VAL -66.1 -41.3 178.2 153.7 50 ARG -69.0 -45.5 177.8 97.4 171.9 53.8 85.9 51 ASP -56.9 -41.7 177.7 118.5 77.4 52 TRP -58.9 -43.0 178.4 166.7 61.0 53 VAL -56.2 -42.9 179.5 179.7 54 MET -54.4 -40.2 179.8 119.9 78.6 126.5 55 TRP -46.9 -34.1 -179.9 106.9 -57.3 56 ALA -69.1 -48.8 179.9 57 VAL -62.5 -34.3 180.0 -172.1 58 ASN -81.7 -38.2 -179.4 -173.5 -96.1 59 GLU -59.4 -49.8 -179.2 -90.2 -77.4 -86.6 60 PHE -111.0 22.6 180.0 -92.0 43.4 61 SER 41.7 52.5 -179.2 58.7 62 LEU -81.5 173.9 179.8 -44.7 169.1 63 LYS -152.0 151.5 -179.4 28.6 63.3 162.2 -83.3 64 GLY 77.3 38.4 179.9 65 VAL -116.5 138.3 -179.7 -173.6 66 ASP -110.7 142.2 179.5 -146.8 -86.1 67 PHE -73.4 -32.3 179.2 -69.3 85.1 68 GLN -74.2 -10.4 179.7 -63.0 -100.8 100.5 69 LYS -82.0 13.8 179.6 -111.4 54.3 -131.9 121.8 70 PHE -110.6 31.8 179.8 -93.9 58.6 71 CYS 57.9 -157.6 179.6 -47.0 72 MET -75.6 -160.0 179.6 -144.3 132.8 91.5 73 SER -64.0 -172.9 -179.8 -58.9 74 GLY -45.5 -36.3 -179.9 75 ALA -57.1 -59.8 179.8 76 ALA -69.7 -52.2 180.0 77 LEU -49.4 -42.2 179.2 120.5 79.5 78 CYS -72.4 -37.3 -179.9 -167.6 79 ALA -79.2 -88.6 -179.6 80 LEU -70.9 -27.0 179.7 97.9 -55.6 81 GLY -62.6 -33.7 179.6 82 LYS -71.1 -49.7 179.2 -126.1 -174.3 -168.7 -153.8 83 GLU -62.5 -41.2 179.9 -155.9 -170.0 82.0 84 CYS -94.1 12.4 179.7 -149.9 85 PHE -67.0 -46.4 179.4 -123.5 -34.8 86 LEU -55.5 -35.6 -179.9 36.3 133.2 87 GLU -74.1 -45.6 -179.9 -73.5 120.7 -80.9 88 LEU -76.4 -68.8 179.5 -65.1 157.3 89 ALA -85.9 127.9 -179.4 90 PRO -92.5 -157.5 179.4 32.5 -23.2 91 ASP -67.9 -4.2 -179.7 60.7 -84.7 92 PHE -97.5 -63.7 -179.7 -63.9 -67.6 93 VAL -73.1 -61.3 -179.4 179.6 94 GLY -55.4 -38.3 -179.4 95 ASP -48.4 -39.1 -179.5 179.9 78.4 96 ILE -78.6 -66.3 -179.2 -23.1 -158.3 97 LEU -54.2 -61.3 -179.2 24.0 132.3 98 TRP -47.8 -41.1 179.0 -166.7 88.2 99 GLU -57.8 -50.0 178.7 173.4 -116.2 77.9 100 HIS -63.9 -38.2 179.1 121.5 -114.4 101 LEU -54.6 -43.2 179.2 -92.5 -99.9 102 GLU -63.3 -42.0 179.4 -58.3 -42.5 -81.8 103 ILE -63.3 -50.7 179.6 -57.3 158.0 104 LEU -74.3 -78.0 179.2 -103.4 177.5 105 GLN 48.3 80.1 179.7 -113.1 -166.2 62.8 106 LYS -60.2 119.2 -179.8 -136.0 -84.7 116.1 77.9 107 GLU -71.9 148.1 179.9 -83.3 156.6 87.6 108 ASP -140.2 46.7 179.7 -136.3 81.6 109 VAL -125.6 92.3 -179.8 -171.1 110 LYS 68.3 172.8 0.0 -148.2 105.9 111.2 -163.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET -36.609 -6.276 -28.292 2 GLU -33.369 -8.129 -27.475 3 CYS -30.040 -6.695 -26.255 4 ALA -28.820 -4.097 -28.773 5 ASP -25.119 -4.626 -27.988 6 VAL -22.649 -6.852 -29.872 7 PRO -24.662 -8.722 -32.567 8 LEU -23.698 -12.409 -32.270 9 LEU -20.031 -13.528 -32.211 10 THR -17.471 -10.736 -32.696 11 PRO -14.712 -10.694 -35.393 12 SER -11.760 -12.994 -34.637 13 SER -9.322 -10.226 -35.644 14 LYS -10.436 -6.807 -34.300 15 GLU -13.156 -5.372 -36.587 16 MET -14.879 -3.264 -33.910 17 MET -17.989 -1.179 -34.658 18 SER -17.022 2.266 -35.997 19 GLN -19.319 3.722 -38.681 20 ALA -19.562 7.518 -38.194 21 LEU -16.489 7.316 -35.892 22 LYS -14.260 10.231 -36.949 23 ALA -11.483 8.525 -34.873 24 THR -11.969 10.384 -31.574 25 PHE -9.824 8.169 -29.314 26 SER -9.777 10.764 -26.525 27 GLY -12.255 13.153 -28.171 28 PHE -15.249 10.980 -27.241 29 THR -14.128 10.772 -23.587 30 LYS -13.656 14.565 -23.404 31 GLU -17.413 15.030 -24.045 32 GLN -18.037 13.526 -20.583 33 GLN -14.863 14.835 -18.889 34 ARG -14.739 18.434 -20.193 35 LEU -18.475 19.244 -20.289 36 GLY -19.565 16.691 -17.682 37 ILE -21.814 14.238 -19.558 38 PRO -22.956 11.189 -17.485 39 LYS -22.513 8.388 -20.049 40 ASP -25.380 8.270 -22.554 41 PRO -27.440 11.412 -23.402 42 ARG -30.354 9.173 -24.485 43 GLN -31.783 8.763 -20.960 44 TRP -29.831 10.261 -18.029 45 THR -30.985 10.169 -14.376 46 GLU -32.197 12.836 -11.915 47 THR -28.783 12.435 -10.224 48 HIS -26.429 13.674 -12.973 49 VAL -29.386 15.292 -14.803 50 ARG -29.657 17.802 -11.937 51 ASP -25.860 18.230 -11.790 52 TRP -26.045 18.814 -15.553 53 VAL -28.708 21.491 -14.888 54 MET -26.256 23.246 -12.540 55 TRP -23.817 23.558 -15.478 56 ALA -26.210 26.180 -16.938 57 VAL -26.314 28.356 -13.805 58 ASN -22.501 28.164 -13.536 59 GLU -21.808 28.565 -17.281 60 PHE -23.675 31.887 -17.590 61 SER -23.686 32.780 -13.843 62 LEU -27.500 32.587 -13.845 63 LYS -29.895 32.897 -10.891 64 GLY -33.430 31.816 -9.993 65 VAL -33.167 28.356 -11.575 66 ASP -34.639 25.126 -10.179 67 PHE -33.302 21.590 -10.667 68 GLN -36.844 20.152 -10.507 69 LYS -37.781 22.451 -13.438 70 PHE -36.079 19.992 -15.844 71 CYS -38.988 17.498 -15.922 72 MET -38.294 13.840 -15.007 73 SER -35.042 11.935 -15.711 74 GLY -33.393 11.785 -19.150 75 ALA -36.447 9.892 -20.453 76 ALA -38.984 12.670 -19.790 77 LEU -36.492 15.565 -20.002 78 CYS -35.424 14.317 -23.461 79 ALA -39.045 13.696 -24.520 80 LEU -41.449 16.318 -23.067 81 GLY -38.545 18.273 -21.555 82 LYS -37.263 19.178 -25.032 83 GLU -40.645 20.353 -26.361 84 CYS -41.355 22.211 -23.097 85 PHE -37.698 23.337 -22.748 86 LEU -38.359 26.734 -24.365 87 GLU -41.122 27.304 -21.782 88 LEU -39.071 26.207 -18.743 89 ALA -35.495 27.148 -19.698 90 PRO -35.126 30.546 -21.472 91 ASP -32.297 32.152 -23.497 92 PHE -30.189 31.926 -20.304 93 VAL -30.491 28.355 -18.982 94 GLY -31.701 26.510 -22.096 95 ASP -29.248 28.400 -24.338 96 ILE -26.356 26.434 -22.774 97 LEU -27.802 22.924 -22.224 98 TRP -30.076 22.834 -25.300 99 GLU -27.092 23.921 -27.432 100 HIS -25.042 20.948 -26.198 101 LEU -28.145 18.730 -26.578 102 GLU -28.182 19.488 -30.317 103 ILE -24.473 18.610 -30.579 104 LEU -24.834 15.315 -28.662 105 GLN -28.451 14.182 -29.264 106 LYS -28.227 10.435 -28.561 107 GLU -29.772 8.600 -31.532 108 ASP -32.422 5.927 -30.914 109 VAL -33.202 4.487 -34.368 110 LYS -32.067 0.847 -34.745 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C C S S S S/S S S 10 S/T T T T C S S S S S 20 C S S S S H H H H H 30 H 3/T T T T/S S S S C T 40 T T T C H H H H H H 50 H H H H H 3 3/T T T T 60 S S S S C T T T T C 70 C C H H H H H H H H/H 80 H H H H H/T T T T/S S S 90 S H H H H 3 3/H H H H 100 H H H H H/S S S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S 10 S S S S 20 t T h H H H H 30 H H H h T t S t 40 T T t h H H H H H 50 H H H H H H H H H h 60 T t S g G G G G 70 g S h H H H H H H H 80 H H H h H H H H h t 90 T 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 MET 0.0 0.0 96.4 2 GLU 0.0 0.0 89.6 3 CYS 7.7 7.8 86.3 4 ALA 1.9 2.7 88.9 5 ASP 21.9 19.8 76.1 6 VAL 46.0 38.7 61.6 7 PRO 18.6 15.0 78.0 8 LEU 0.0 0.0 88.9 9 LEU 0.0 0.0 90.3 10 THR 46.9 43.9 59.1 11 PRO 65.3 52.5 71.3 12 SER 0.0 0.0 90.8 13 SER 5.8 6.9 82.6 14 LYS 16.7 9.6 82.5 15 GLU 11.6 8.3 78.6 16 MET 29.7 18.6 79.4 17 MET 10.2 6.4 84.0 18 SER 38.0 45.5 73.0 19 GLN 0.0 0.0 91.5 20 ALA 0.0 0.0 82.8 21 LEU 65.0 44.0 77.9 22 LYS 23.0 13.2 82.9 23 ALA 20.6 28.4 68.1 24 THR 74.2 69.4 51.4 25 PHE 3.4 2.0 84.3 26 SER 1.3 1.5 83.2 27 GLY 20.2 58.2 55.8 28 PHE 54.6 32.7 86.4 29 THR 44.2 41.4 68.0 30 LYS 68.0 39.2 72.1 31 GLU 84.8 61.2 51.7 32 GLN 96.6 65.0 65.0 33 GLN 16.8 11.3 80.3 34 ARG 49.1 23.5 78.5 35 LEU 93.4 63.2 53.5 36 GLY 11.4 32.7 80.6 37 ILE 139.0 96.9 37.8 38 PRO 114.0 91.6 46.6 39 LYS 33.7 19.5 79.1 40 ASP 64.8 58.7 62.7 41 PRO 115.0 92.3 44.1 42 ARG 91.6 43.8 76.3 43 GLN 60.2 40.5 70.4 44 TRP 197.0 96.1 37.7 45 THR 35.6 33.3 69.9 46 GLU 52.9 38.1 76.6 47 THR 20.7 19.4 82.8 48 HIS 106.7 71.0 52.3 49 VAL 114.1 96.0 38.1 50 ARG 93.1 44.6 64.1 51 ASP 40.0 36.2 64.5 52 TRP 195.9 95.6 32.9 53 VAL 118.0 99.4 33.7 54 MET 63.6 39.9 64.3 55 TRP 169.2 82.5 46.9 56 ALA 72.6 100.0 42.0 57 VAL 78.8 66.4 56.8 58 ASN 26.2 21.6 73.9 59 GLU 65.4 47.2 59.9 60 PHE 69.7 41.8 73.7 61 SER 4.7 5.7 87.5 62 LEU 133.8 90.5 41.8 63 LYS 6.8 3.9 86.0 64 GLY 0.0 0.0 79.8 65 VAL 102.6 86.3 46.9 66 ASP 41.4 37.5 62.4 67 PHE 89.1 53.4 57.3 68 GLN 18.6 12.5 89.4 69 LYS 59.7 34.4 70.4 70 PHE 161.0 96.5 32.9 71 CYS 77.6 78.3 49.8 72 MET 29.5 18.5 78.7 73 SER 60.3 72.1 55.4 74 GLY 32.8 94.1 44.6 75 ALA 28.6 39.5 71.9 76 ALA 53.4 73.5 51.2 77 LEU 143.4 97.1 34.1 78 CYS 60.3 60.8 68.6 79 ALA 13.2 18.2 82.0 80 LEU 65.9 44.6 54.4 81 GLY 33.2 95.4 45.9 82 LYS 125.1 72.1 64.2 83 GLU 0.0 0.0 86.5 84 CYS 59.7 60.2 61.4 85 PHE 160.6 96.3 34.1 86 LEU 30.1 20.3 84.4 87 GLU 48.8 35.2 67.4 88 LEU 105.7 71.5 55.2 89 ALA 69.2 95.3 38.7 90 PRO 65.6 52.7 70.1 91 ASP 20.0 18.1 65.9 92 PHE 57.8 34.6 65.8 93 VAL 112.3 94.5 23.5 94 GLY 30.2 86.7 49.5 95 ASP 42.3 38.3 68.5 96 ILE 134.0 93.4 51.0 97 LEU 147.8 100.0 32.7 98 TRP 92.5 45.1 60.1 99 GLU 48.6 35.0 66.5 100 HIS 145.3 96.7 30.6 101 LEU 139.3 94.3 40.7 102 GLU 93.3 67.3 61.4 103 ILE 32.1 22.4 77.9 104 LEU 110.9 75.0 45.9 105 GLN 69.5 46.8 80.7 106 LYS 104.7 60.4 70.6 107 GLU 3.2 2.3 85.6 108 ASP 29.4 26.6 78.1 109 VAL 2.6 2.2 86.5 110 LYS 0.0 0.0 92.4