Protein Data Bank File : 1du6 Title : GENE REGULATION 14-JAN-00 1DU6 Number of Amino Acid Residues : 64 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER SER GLY HIS ILE GLU GLY ARG HIS MET 10 ASN LYS GLN ALA THR GLU ILE LEU ASN GLU 20 TYR PHE TYR SER HIS LEU SER ASN PRO TYR 30 PRO SER GLU GLU ALA LYS GLU GLU LEU ALA 40 LYS LYS CYS GLY ILE THR VAL SER GLN VAL 50 SER ASN TRP PHE GLY ASN LYS ARG ILE ARG 60 TYR LYS LYS ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 -55.9 -180.0 -128.5 2 SER -128.5 158.1 -180.0 -94.0 3 GLY 124.5 -85.7 179.9 4 HIS 59.6 166.7 -180.0 -53.2 -129.4 5 ILE 59.9 67.9 180.0 -51.0 138.8 6 GLU -156.2 108.4 -180.0 -85.4 -125.7 155.8 7 GLY 172.1 90.9 -180.0 8 ARG -158.8 117.3 -179.9 -45.5 -178.2 88.7 -88.8 9 HIS 61.2 153.8 -180.0 -63.1 138.5 10 MET 77.9 48.3 -179.7 -38.0 -114.9 82.1 11 ASN 52.9 -168.4 -180.0 -120.3 57.6 12 LYS -67.4 -100.9 -179.9 -70.5 -62.6 125.2 87.1 13 GLN -84.6 17.4 179.9 -82.6 -71.6 -96.8 14 ALA -55.9 -54.8 179.4 15 THR -56.6 -24.9 178.9 -75.8 16 GLU -78.7 -33.4 178.1 -89.8 -52.4 -92.9 17 ILE -70.6 -50.5 178.6 -78.8 -1.8 18 LEU -61.4 -51.3 179.4 -55.8 176.6 19 ASN -58.9 -64.6 179.1 -177.2 104.2 20 GLU -52.7 -27.3 179.7 -66.7 176.7 3.7 21 TYR -76.5 -60.3 -179.2 172.5 -129.0 22 PHE -61.9 -49.8 -179.7 156.4 -92.1 23 TYR -48.2 -76.0 178.7 -97.8 -107.7 24 SER -38.2 -36.9 -177.4 -169.1 25 HIS -106.2 28.8 -179.8 -74.3 -60.3 26 LEU -69.8 -20.8 179.6 79.7 154.1 27 SER -64.0 -25.5 180.0 -138.5 28 ASN -169.5 64.8 -179.7 -149.4 5.0 29 PRO -78.7 -89.8 180.0 27.2 -26.4 30 TYR 42.9 52.9 179.9 -88.0 43.6 31 PRO -50.2 105.6 -179.9 -26.7 33.2 32 SER -51.3 171.2 -179.9 -36.6 33 GLU -51.7 -31.7 179.9 -82.2 -175.7 49.4 34 GLU -71.2 -54.5 -179.8 -146.3 165.1 -36.0 35 ALA -58.8 -46.0 179.7 36 LYS -58.5 -56.5 179.1 160.9 -103.9 -76.8 161.1 37 GLU -56.5 -40.6 179.6 -101.4 160.6 74.1 38 GLU -56.0 -62.1 179.4 -86.2 -106.1 53.5 39 LEU -54.6 -43.1 180.0 -53.7 173.4 40 ALA -57.4 -57.2 -180.0 41 LYS -75.8 -7.7 179.8 -52.0 -43.3 -55.0 -154.2 42 LYS -76.6 -33.2 178.8 141.1 -79.7 130.7 68.2 43 CYS -93.1 -16.1 -178.7 -137.0 44 GLY 81.6 27.0 -179.4 45 ILE -94.1 -112.9 179.8 43.2 158.3 46 THR -163.7 133.6 -177.6 52.9 47 VAL -48.6 -37.2 179.5 137.2 48 SER -56.7 -29.6 176.3 -117.6 49 GLN -63.6 -39.5 176.7 -60.4 -85.6 82.6 50 VAL -83.3 -59.0 178.4 -171.7 51 SER -37.5 -48.4 -179.1 -136.1 52 ASN -76.5 -46.5 -178.8 98.2 102.6 53 TRP -46.6 -54.1 -178.8 -168.4 98.3 54 PHE -75.0 -24.3 179.0 -55.9 -107.4 55 GLY -60.2 -31.4 179.2 56 ASN -96.3 -24.5 179.1 -139.1 -124.6 57 LYS -75.5 -25.9 177.4 -131.7 80.1 -174.0 176.5 58 ARG -74.8 -0.5 179.0 -136.8 159.9 79.5 -91.5 59 ILE -75.9 -8.3 -178.3 -149.5 83.5 60 ARG 75.8 76.7 -179.7 -106.4 57.2 -160.9 -80.2 61 TYR -62.6 8.2 179.8 64.7 -13.8 62 LYS -86.9 -143.0 179.8 -44.1 -167.0 58.4 132.1 63 LYS -79.1 57.2 180.0 -77.2 59.0 166.6 -112.1 64 ASN 60.7 -91.3 0.0 -156.5 -56.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER 9.670 -16.537 -5.804 2 SER 10.645 -15.627 -9.366 3 GLY 11.260 -12.390 -11.240 4 HIS 13.705 -10.123 -9.425 5 ILE 15.010 -6.865 -10.891 6 GLU 11.950 -4.676 -10.334 7 GLY 11.924 -1.270 -8.671 8 ARG 11.662 2.092 -10.422 9 HIS 9.224 4.943 -9.800 10 MET 5.853 4.463 -8.087 11 ASN 7.186 4.186 -4.532 12 LYS 8.669 0.903 -3.323 13 GLN 6.227 -2.010 -3.733 14 ALA 3.470 0.433 -4.735 15 THR 3.455 -0.735 -8.355 16 GLU 3.277 -4.224 -6.876 17 ILE 0.314 -3.149 -4.810 18 LEU -1.347 -1.461 -7.757 19 ASN -0.373 -4.278 -10.093 20 GLU -1.216 -7.109 -7.717 21 TYR -4.351 -5.090 -6.980 22 PHE -5.573 -4.339 -10.503 23 TYR -4.319 -7.624 -11.965 24 SER -6.007 -9.995 -9.492 25 HIS -8.971 -7.725 -9.923 26 LEU -8.672 -7.265 -13.686 27 SER -12.052 -8.966 -14.080 28 ASN -13.607 -5.787 -12.675 29 PRO -11.047 -3.218 -11.418 30 TYR -11.919 0.369 -12.415 31 PRO -10.796 1.664 -8.971 32 SER -13.265 4.483 -8.305 33 GLU -11.997 7.902 -7.215 34 GLU -12.077 6.521 -3.670 35 ALA -10.098 3.337 -4.321 36 LYS -7.591 5.178 -6.504 37 GLU -7.040 7.957 -3.971 38 GLU -6.935 5.301 -1.252 39 LEU -4.138 3.261 -2.825 40 ALA -2.443 6.502 -3.780 41 LYS -2.539 7.957 -0.267 42 LYS -2.017 4.449 1.121 43 CYS 1.578 4.418 -0.117 44 GLY 2.019 8.125 0.500 45 ILE 2.699 8.803 -3.166 46 THR 0.407 10.791 -5.437 47 VAL -2.728 9.835 -7.197 48 SER -1.208 10.629 -10.542 49 GLN 1.062 7.702 -9.718 50 VAL -2.188 5.812 -9.343 51 SER -4.282 8.010 -11.650 52 ASN -1.811 7.270 -14.459 53 TRP -1.001 3.637 -13.581 54 PHE -4.587 2.510 -14.038 55 GLY -5.057 4.959 -16.886 56 ASN -2.793 2.734 -18.968 57 LYS -3.884 -0.488 -17.280 58 ARG -7.441 0.251 -18.345 59 ILE -5.959 -0.075 -21.837 60 ARG -6.490 -3.797 -21.430 61 TYR -3.015 -5.197 -20.865 62 LYS -4.398 -8.461 -22.243 63 LYS -4.696 -9.495 -25.895 64 ASN -5.459 -5.924 -26.970 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S/S S S S S C 10 C C H H H H H H H H 20 H H H H H H S S S S 30 C H H H H H H H H H 40 H H H H C H H H H H 50 H H H H H H H H H C 60 S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S t 10 T T h H H H H H H H 20 H H H H h T T t 30 h H H H H H H H H 40 H H H h t h H H H H 50 H H H H H H H h T T 60 t S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 0.0 0.0 94.2 2 SER 5.2 6.2 82.5 3 GLY 0.0 0.0 75.6 4 HIS 25.5 17.0 81.0 5 ILE 0.0 0.0 87.0 6 GLU 31.5 22.7 87.0 7 GLY 6.7 19.2 79.8 8 ARG 33.8 16.2 89.7 9 HIS 13.7 9.1 86.1 10 MET 132.1 82.8 60.6 11 ASN 67.5 55.8 59.6 12 LYS 2.3 1.3 87.7 13 GLN 48.4 32.6 70.6 14 ALA 71.5 98.5 35.7 15 THR 62.7 58.7 65.1 16 GLU 95.9 69.2 69.6 17 ILE 89.4 62.3 57.1 18 LEU 146.2 98.9 29.6 19 ASN 88.9 73.5 52.8 20 GLU 49.4 35.7 76.1 21 TYR 118.3 65.3 46.9 22 PHE 157.7 94.6 30.0 23 TYR 94.3 52.1 66.1 24 SER 18.5 22.2 79.2 25 HIS 52.3 34.8 72.2 26 LEU 102.9 69.6 55.0 27 SER 0.8 0.9 77.6 28 ASN 6.0 4.9 81.7 29 PRO 112.0 89.9 45.2 30 TYR 59.0 32.6 69.4 31 PRO 116.9 93.9 40.1 32 SER 8.7 10.4 84.0 33 GLU 15.4 11.1 85.2 34 GLU 5.4 3.9 81.3 35 ALA 45.4 62.5 60.4 36 LYS 135.8 78.3 50.6 37 GLU 58.7 42.3 67.7 38 GLU 30.2 21.8 74.3 39 LEU 120.0 81.2 34.3 40 ALA 72.6 100.0 43.1 41 LYS 59.4 34.3 75.9 42 LYS 88.7 51.2 60.7 43 CYS 84.7 85.4 56.6 44 GLY 6.9 19.8 77.0 45 ILE 132.2 92.1 51.0 46 THR 30.8 28.8 68.9 47 VAL 86.1 72.5 52.7 48 SER 12.3 14.7 73.4 49 GLN 97.9 65.9 60.8 50 VAL 118.8 100.0 30.4 51 SER 44.9 53.7 61.1 52 ASN 43.3 35.8 68.8 53 TRP 187.1 91.3 42.5 54 PHE 151.3 90.7 32.4 55 GLY 17.4 49.9 80.4 56 ASN 17.8 14.7 80.4 57 LYS 129.6 74.8 50.7 58 ARG 100.3 48.0 68.3 59 ILE 37.5 26.1 82.1 60 ARG 73.0 34.9 79.5 61 TYR 140.9 77.9 40.9 62 LYS 69.3 39.9 63.5 63 LYS 0.0 0.0 82.6 64 ASN 0.0 0.0 93.6