Protein Data Bank File : 1dl6 Title : GENE REGULATION 08-DEC-99 1DL6 Number of Amino Acid Residues : 58 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA SER THR SER ARG LEU ASP ALA LEU PRO 10 ARG VAL THR CYS PRO ASN HIS PRO ASP ALA 20 ILE LEU VAL GLU ASP TYR ARG ALA GLY ASP 30 MET ILE CYS PRO GLU CYS GLY LEU VAL VAL 40 GLY ASP ARG VAL ILE ASP VAL GLY SER GLU 50 TRP ARG THR PHE SER ASN ASP LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 104.3 180.0 2 SER -67.8 -30.6 -180.0 -57.1 3 THR -59.3 -31.3 179.9 55.9 4 SER -91.8 112.8 179.9 -154.5 5 ARG -72.0 -60.9 -180.0 -105.2 -164.1 150.0 79.3 6 LEU -150.4 125.0 180.0 -130.4 174.9 7 ASP -110.9 -30.0 -180.0 52.2 70.8 8 ALA -63.9 80.8 -180.0 9 LEU -77.4 -61.0 -179.9 -96.5 136.5 10 PRO -73.7 130.9 179.9 27.7 -33.0 11 ARG -93.1 118.5 -179.8 -64.3 -161.1 108.8 161.7 12 VAL -72.9 101.6 179.6 -74.7 13 THR 61.7 177.9 180.0 -26.8 14 CYS -84.1 132.3 -179.8 171.5 15 PRO -55.8 -37.3 -179.6 -23.0 32.6 16 ASN -102.1 11.4 179.8 -76.7 -4.3 17 HIS -153.1 89.2 179.9 -69.3 127.4 18 PRO -70.0 -46.3 179.9 25.5 -32.9 19 ASP -64.2 -38.3 180.0 -72.3 158.9 20 ALA -93.5 122.9 -179.9 21 ILE -104.6 134.8 179.7 -49.2 129.7 22 LEU -59.2 112.7 -180.0 -96.4 97.8 23 VAL -75.8 157.7 -180.0 -166.3 24 GLU -123.2 145.3 180.0 -165.6 -178.5 -20.1 25 ASP -81.2 -164.3 -179.9 -123.1 -98.5 26 TYR -93.5 -29.2 179.8 -42.8 80.8 27 ARG 172.0 122.0 -180.0 -128.4 62.0 -158.9 -70.9 28 ALA 75.5 27.7 179.9 29 GLY -118.5 -16.1 180.0 30 ASP 67.5 -173.0 179.9 -42.7 -23.9 31 MET -117.3 118.3 -179.3 -89.0 -158.6 -76.8 32 ILE -111.2 155.9 179.7 59.1 105.9 33 CYS -100.4 136.5 -179.5 -176.1 34 PRO -75.7 1.8 -180.0 28.9 -33.4 35 GLU -115.1 -77.8 179.7 -68.2 -70.9 -59.2 36 CYS -68.4 -13.3 -179.8 54.7 37 GLY 60.8 54.1 -180.0 38 LEU -97.7 178.7 -179.9 83.3 97.8 39 VAL -146.3 92.6 179.9 -173.2 40 VAL -98.5 130.8 -180.0 63.6 41 GLY 94.2 65.5 -180.0 42 ASP -88.2 -31.5 -180.0 -56.9 114.4 43 ARG -74.1 169.8 180.0 50.5 131.3 81.4 74.1 44 VAL -140.4 102.9 180.0 -172.0 45 ILE -59.6 93.4 -180.0 -178.3 134.2 46 ASP -101.6 91.4 180.0 -93.6 102.3 47 VAL -113.9 82.1 180.0 -171.8 48 GLY -84.6 93.0 -180.0 49 SER -162.5 33.2 180.0 -147.6 50 GLU -126.1 11.3 180.0 -96.9 -78.6 112.9 51 TRP 67.0 -66.3 -180.0 -56.6 -80.2 52 ARG 68.3 86.7 -180.0 -134.7 -58.5 -164.1 174.5 53 THR -157.7 166.6 179.9 -43.2 54 PHE -90.1 59.7 180.0 42.8 89.2 55 SER 62.6 148.5 180.0 -41.0 56 ASN -73.5 156.4 180.0 -122.7 46.6 57 ASP -87.5 -32.3 180.0 -159.5 98.7 58 LYS -92.4 -26.3 0.0 -102.0 112.7 -65.2 109.4 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA -7.388 7.379 -20.783 2 SER -3.851 8.224 -21.899 3 THR -3.686 10.970 -19.271 4 SER -3.776 8.246 -16.617 5 ARG -0.482 6.352 -16.443 6 LEU -1.333 3.830 -13.724 7 ASP -4.249 3.725 -11.282 8 ALA -4.134 0.079 -10.199 9 LEU -2.232 0.729 -6.970 10 PRO -3.470 -2.159 -4.757 11 ARG -2.718 -5.652 -6.063 12 VAL -5.624 -8.074 -5.708 13 THR -4.064 -11.207 -4.212 14 CYS -0.847 -12.794 -5.476 15 PRO -0.516 -13.175 -9.293 16 ASN 0.958 -16.649 -8.833 17 HIS -1.179 -17.459 -5.780 18 PRO -4.969 -16.852 -5.941 19 ASP -5.818 -18.888 -2.842 20 ALA -2.988 -17.231 -0.918 21 ILE -3.344 -13.485 -0.384 22 LEU -0.383 -11.227 0.384 23 VAL -0.751 -10.358 4.071 24 GLU 0.066 -6.892 5.406 25 ASP 1.796 -5.821 8.619 26 TYR 0.833 -2.998 10.985 27 ARG 3.469 -0.530 9.775 28 ALA 6.885 -0.860 8.153 29 GLY 6.324 -4.543 7.445 30 ASP 5.178 -4.470 3.818 31 MET 2.968 -7.149 2.266 32 ILE 4.251 -10.714 2.016 33 CYS 2.763 -13.817 0.387 34 PRO 2.187 -17.040 2.411 35 GLU 3.169 -19.080 -0.657 36 CYS 5.937 -17.611 -2.836 37 GLY 7.043 -15.689 0.241 38 LEU 7.344 -12.337 -1.503 39 VAL 7.457 -8.798 -0.117 40 VAL 5.602 -6.054 -1.989 41 GLY 5.653 -2.509 -0.644 42 ASP 9.023 -1.878 0.988 43 ARG 8.877 1.909 0.662 44 VAL 6.793 4.176 2.894 45 ILE 4.989 7.193 1.443 46 ASP 5.842 9.729 4.147 47 VAL 4.141 12.987 3.168 48 GLY 3.884 15.105 6.301 49 SER 2.101 18.253 5.154 50 GLU -1.546 17.891 6.178 51 TRP -1.276 19.009 9.819 52 ARG -3.499 16.145 10.985 53 THR -5.602 17.426 13.884 54 PHE -9.149 17.571 15.251 55 SER -9.827 21.093 13.985 56 ASN -8.304 24.191 15.581 57 ASP -9.568 25.529 18.910 58 LYS -9.239 29.199 17.967 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 T T T T S S S S S S 10 S S S T T T T/T T T T 20 S S S S S/T T T T/S S S 30 S C T T T T S S S S 40 S S S S S S S S C C 50 S S S S S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T t S S 10 S B T T B S S S 20 E E e S S S e 30 E E e T T T t e E E 40 S S 50 S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 14.4 19.8 87.9 2 SER 0.0 0.0 88.9 3 THR 0.0 0.0 81.3 4 SER 38.1 45.5 78.4 5 ARG 0.0 0.0 92.6 6 LEU 30.5 20.6 82.4 7 ASP 12.9 11.7 77.6 8 ALA 15.0 20.6 75.1 9 LEU 8.4 5.7 83.4 10 PRO 25.7 20.7 75.9 11 ARG 59.6 28.5 77.2 12 VAL 0.0 0.0 91.5 13 THR 76.6 71.7 63.1 14 CYS 97.4 98.2 39.6 15 PRO 50.7 40.7 75.9 16 ASN 9.7 8.0 76.5 17 HIS 108.7 72.4 47.4 18 PRO 29.2 23.5 80.2 19 ASP 0.0 0.0 83.1 20 ALA 61.0 84.0 46.3 21 ILE 39.9 27.8 82.3 22 LEU 135.9 91.9 37.6 23 VAL 30.9 26.0 76.5 24 GLU 43.2 31.2 72.2 25 ASP 47.5 42.9 68.8 26 TYR 0.0 0.0 88.6 27 ARG 18.1 8.7 86.6 28 ALA 16.7 23.0 77.4 29 GLY 20.5 58.9 75.7 30 ASP 83.4 75.5 65.4 31 MET 102.4 64.3 61.5 32 ILE 68.2 47.5 61.3 33 CYS 99.2 100.0 38.3 34 PRO 72.6 58.4 61.1 35 GLU 60.3 43.5 65.6 36 CYS 56.5 56.9 53.0 37 GLY 8.3 23.9 79.9 38 LEU 94.4 63.9 49.6 39 VAL 64.0 53.9 68.7 40 VAL 70.8 59.6 50.7 41 GLY 5.3 15.1 68.3 42 ASP 33.6 30.4 82.3 43 ARG 11.5 5.5 86.8 44 VAL 54.5 45.9 79.1 45 ILE 6.9 4.8 77.5 46 ASP 17.1 15.4 78.2 47 VAL 30.6 25.7 73.0 48 GLY 0.0 0.0 83.3 49 SER 11.5 13.8 80.4 50 GLU 16.7 12.1 78.5 51 TRP 9.6 4.7 92.7 52 ARG 5.4 2.6 89.9 53 THR 45.8 42.9 70.2 54 PHE 0.0 0.0 85.3 55 SER 0.2 0.3 86.3 56 ASN 22.4 18.5 85.5 57 ASP 6.5 5.9 85.0 58 LYS 28.5 16.4 91.0