Protein Data Bank File : 1bh9a Title : TRANSCRIPTION REGULATION COMPLEX 16-JUN-98 1BH9 Number of Amino Acid Residues : 45 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU PHE SER LYS GLU LEU ARG CYS MET MET 10 TYR GLY PHE GLY ASP ASP GLN ASN PRO TYR 20 THR GLU SER VAL ASP ILE LEU GLU ASP LEU 30 VAL ILE GLU PHE ILE THR GLU MET THR HIS 40 LYS ALA MET SER ILE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 -48.7 177.3 -138.1 67.9 2 PHE -161.5 66.8 -177.8 26.8 59.5 3 SER -85.3 -36.0 -179.6 163.2 4 LYS -75.5 -50.1 -179.0 -168.5 160.7 -166.1 165.6 5 GLU -56.2 -34.6 179.8 -61.1 88.3 -41.3 6 LEU -70.1 -33.0 -179.7 -151.6 51.2 7 ARG -70.4 -42.2 178.0 -58.7 -177.1 66.0 -77.6 8 CYS -67.4 -35.8 -178.9 -86.5 9 MET -64.7 -44.4 178.5 -168.8 166.5 -74.1 10 MET -67.7 -36.3 179.4 -61.3 174.6 60.2 11 TYR -69.4 -45.6 179.1 172.5 51.8 12 GLY -59.9 -21.6 180.0 13 PHE -96.2 -1.0 178.1 -80.8 -53.7 14 GLY 120.9 0.4 179.4 15 ASP -85.6 168.0 179.9 -171.6 29.4 16 ASP -51.7 147.1 179.8 174.4 77.0 17 GLN -50.7 -27.0 179.2 -175.4 -153.4 -58.7 18 ASN -135.2 88.3 179.8 -163.0 -61.8 19 PRO -62.2 170.7 179.5 30.5 -47.5 20 TYR -86.7 139.2 -178.9 -72.0 -58.3 21 THR -59.5 -41.9 -179.6 -61.2 22 GLU -61.3 -27.9 179.8 -44.0 77.3 69.8 23 SER -79.4 -38.1 179.3 -68.5 24 VAL -62.1 -37.5 -178.8 -179.4 25 ASP -77.2 -39.3 177.4 -55.0 -38.2 26 ILE -57.8 -43.3 179.8 -77.1 -178.1 27 LEU -59.9 -43.5 -179.4 -135.9 -165.0 28 GLU -56.7 -52.6 179.8 -168.4 172.6 -36.9 29 ASP -54.4 -40.3 179.1 -69.8 59.0 30 LEU -67.3 -39.3 178.4 -64.2 163.4 31 VAL -64.3 -47.1 178.9 174.8 32 ILE -58.7 -48.0 179.2 -64.3 172.7 33 GLU -56.6 -41.0 -179.1 -178.3 -178.3 61.2 34 PHE -62.5 -50.5 -179.8 178.9 67.2 35 ILE -61.0 -44.5 179.3 -60.9 -179.0 36 THR -55.2 -41.4 179.4 -65.3 37 GLU -66.2 -50.0 -179.8 177.0 77.3 1.9 38 MET -56.7 -54.6 178.9 -61.3 -61.5 -67.4 39 THR -45.2 -62.6 -180.0 -63.2 40 HIS -53.6 -36.7 -179.7 -73.1 -52.8 41 LYS -77.3 -31.2 179.2 -128.6 87.1 170.0 -169.1 42 ALA -72.3 -34.1 179.3 43 MET -57.5 -33.2 -179.1 -81.2 165.8 160.2 44 SER -79.6 -53.3 179.6 -55.1 45 ILE -70.4 100.4 0.0 177.2 178.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 33.817 -1.355 31.863 2 PHE 32.945 -2.215 28.232 3 SER 35.868 -3.444 26.143 4 LYS 34.378 -6.321 24.314 5 GLU 31.181 -4.561 23.288 6 LEU 33.354 -1.700 22.221 7 ARG 35.544 -4.033 20.123 8 CYS 32.588 -5.556 18.214 9 MET 31.212 -2.017 17.927 10 MET 34.384 -0.663 16.364 11 TYR 34.411 -3.688 14.009 12 GLY 30.772 -3.191 13.157 13 PHE 31.660 0.376 12.203 14 GLY 34.534 -0.413 9.883 15 ASP 37.677 -1.042 11.897 16 ASP 39.841 -4.165 11.564 17 GLN 38.164 -7.384 12.698 18 ASN 40.593 -7.293 15.598 19 PRO 41.367 -3.703 16.704 20 TYR 44.337 -2.593 18.816 21 THR 43.945 -2.568 22.610 22 GLU 45.447 0.878 23.073 23 SER 42.714 2.165 20.708 24 VAL 39.869 0.346 22.450 25 ASP 40.775 2.033 25.728 26 ILE 41.198 5.528 24.362 27 LEU 37.706 5.013 22.960 28 GLU 36.441 3.879 26.356 29 ASP 37.708 7.014 28.031 30 LEU 36.030 9.110 25.313 31 VAL 32.727 7.272 25.734 32 ILE 32.916 7.821 29.486 33 GLU 33.810 11.503 29.010 34 PHE 30.846 11.623 26.600 35 ILE 28.187 10.117 28.839 36 THR 29.322 12.357 31.728 37 GLU 28.875 15.425 29.532 38 MET 25.388 14.452 28.330 39 THR 24.348 13.628 31.869 40 HIS 25.516 16.974 33.244 41 LYS 23.891 18.797 30.327 42 ALA 20.656 16.820 30.637 43 MET 20.563 17.605 34.400 44 SER 20.284 21.275 33.459 45 ILE 17.745 21.145 30.625 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C H H H H H H H H H 10 H H H H C C S S S S/H 20 H H H H H H H H H H 30 H H H H H H H H H H 40 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 10 H H h T t S S h 20 H H H H H H H H H H 30 H H H H H H H H H H 40 H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 43.7 29.6 72.3 2 PHE 113.5 68.0 54.1 3 SER 38.7 46.3 68.3 4 LYS 19.8 11.4 83.9 5 GLU 34.1 24.6 69.3 6 LEU 138.8 93.9 39.1 7 ARG 145.6 69.7 62.8 8 CYS 17.0 17.1 74.3 9 MET 61.2 38.4 64.1 10 MET 133.3 83.6 43.9 11 TYR 72.5 40.1 75.9 12 GLY 0.6 1.8 78.8 13 PHE 25.2 15.1 81.8 14 GLY 1.1 3.2 86.1 15 ASP 57.1 51.7 60.7 16 ASP 25.1 22.7 77.6 17 GLN 29.3 19.7 75.7 18 ASN 33.7 27.9 86.0 19 PRO 120.7 96.9 62.1 20 TYR 16.5 9.1 90.6 21 THR 22.2 20.7 82.0 22 GLU 20.6 14.9 75.7 23 SER 38.5 46.0 63.0 24 VAL 117.2 98.7 46.8 25 ASP 49.2 44.5 70.0 26 ILE 29.6 20.6 74.2 27 LEU 96.3 65.1 46.5 28 GLU 113.3 81.8 51.2 29 ASP 21.8 19.7 72.9 30 LEU 55.0 37.2 70.6 31 VAL 78.2 65.8 42.7 32 ILE 71.0 49.5 62.8 33 GLU 18.8 13.6 78.5 34 PHE 48.9 29.3 66.5 35 ILE 51.0 35.5 67.2 36 THR 42.9 40.1 70.8 37 GLU 51.8 37.3 71.2 38 MET 54.2 34.0 66.5 39 THR 48.8 45.6 58.1 40 HIS 49.9 33.2 64.9 41 LYS 36.7 21.1 85.2 42 ALA 21.4 29.4 72.0 43 MET 44.2 27.7 78.8 44 SER 14.8 17.7 84.4 45 ILE 8.6 6.0 86.9