Protein Data Bank File : 1bor Title : TRANSCRIPTION REGULATION 27-SEP-95 1BOR Number of Amino Acid Residues : 56 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU GLU GLU PHE GLN PHE LEU ARG CYS GLN 10 GLN CYS GLN ALA GLU ALA LYS CYS PRO LYS 20 LEU LEU PRO CYS LEU HIS THR LEU CYS SER 30 GLY CYS LEU GLU ALA SER GLY MET GLN CYS 40 PRO ILE CYS GLN ALA PRO TRP PRO LEU GLY 50 ALA ASP THR PRO ALA LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 -39.0 179.9 -157.5 102.3 -8.7 2 GLU -124.5 152.1 -180.0 -61.6 -98.3 13.2 3 GLU 59.7 -94.9 180.0 -69.1 83.0 28.4 4 PHE -42.5 115.4 -179.9 166.9 44.2 5 GLN -157.2 16.0 179.4 -163.9 -161.3 26.3 6 PHE -151.1 170.4 -179.9 -137.6 49.6 7 LEU -160.9 23.3 -179.4 45.4 144.5 8 ARG -127.3 -75.5 179.9 -50.3 -158.8 -133.8 -115.1 9 CYS -178.2 165.2 178.8 139.5 10 GLN -62.8 -64.8 -179.6 -179.1 -138.6 49.7 11 GLN -108.7 -56.4 179.4 -117.1 -80.4 -99.8 12 CYS -78.3 77.0 -179.7 8.3 13 GLN -83.5 103.0 179.4 53.5 -132.0 34.1 14 ALA -126.3 -63.9 179.4 15 GLU -150.0 86.2 179.8 -153.9 -172.5 -64.6 16 ALA 21.3 99.5 180.0 17 LYS -98.2 -6.1 -179.9 -130.7 136.3 -162.3 -112.2 18 CYS -115.6 111.1 178.9 161.4 19 PRO -82.8 -2.6 -179.1 23.0 -18.9 20 LYS -47.5 154.1 -179.4 -172.9 -176.0 143.7 160.3 21 LEU -38.7 160.4 -178.0 36.9 78.4 22 LEU -111.6 7.4 179.7 -117.2 -168.1 23 PRO -76.7 -30.2 -179.8 22.6 -22.3 24 CYS -113.9 63.2 179.6 72.0 25 LEU 27.2 57.2 179.8 -158.9 160.6 26 HIS -121.0 59.5 176.7 -116.1 103.4 27 THR -127.8 34.0 -178.2 -55.4 28 LEU -81.3 -109.7 -178.1 -69.7 -44.5 29 CYS -152.7 103.9 -179.9 128.1 30 SER -51.8 89.5 179.8 -160.5 31 GLY 161.7 -28.1 -179.6 32 CYS -139.7 3.6 -178.9 87.5 33 LEU -119.9 142.5 179.3 -170.1 -82.5 34 GLU -169.2 65.0 -178.8 47.3 139.6 26.8 35 ALA 47.5 25.5 -179.5 36 SER -89.0 -21.6 -179.8 -96.5 37 GLY -176.1 37.8 178.6 38 MET -125.5 -33.6 179.1 47.0 83.5 132.7 39 GLN 132.2 65.7 179.3 -81.1 -98.4 -128.8 40 CYS -163.4 154.4 -177.9 -95.6 41 PRO -85.4 93.3 179.9 23.3 -17.0 42 ILE 30.9 38.3 -179.3 175.1 33.2 43 CYS -38.3 -78.5 179.1 -98.3 44 GLN 24.1 71.9 178.9 -144.2 -113.5 72.3 45 ALA -171.1 -64.4 179.7 46 PRO -81.0 25.7 -179.1 23.3 -20.9 47 TRP -55.7 -43.6 -178.7 -126.8 -83.1 48 PRO -74.2 -25.2 179.4 21.7 -21.3 49 LEU -97.8 117.4 -179.8 -123.8 173.0 50 GLY -124.1 160.2 179.8 51 ALA -100.2 -100.0 179.5 52 ASP -104.6 85.6 -179.5 38.6 37.0 53 THR -130.1 -179.9 -179.7 100.6 54 PRO -81.7 -47.3 -179.9 22.6 -18.2 55 ALA 74.2 -178.4 -179.8 56 LEU -147.1 -11.2 0.0 34.3 139.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 4.408 -0.192 14.358 2 GLU 2.861 2.875 12.687 3 GLU 1.613 3.396 9.116 4 PHE 3.270 0.311 7.570 5 GLN 0.824 -2.434 8.589 6 PHE 0.001 -4.501 5.479 7 LEU 1.547 -6.423 2.578 8 ARG -1.418 -7.803 0.603 9 CYS -4.101 -5.324 -0.501 10 GLN -6.924 -3.068 0.705 11 GLN -9.819 -5.417 -0.194 12 CYS -8.472 -8.086 -2.609 13 GLN -5.663 -9.299 -0.283 14 ALA -3.894 -12.098 -2.193 15 GLU -0.215 -11.272 -2.830 16 ALA 0.818 -7.606 -2.263 17 LYS -0.571 -5.896 -5.407 18 CYS 0.797 -2.451 -4.487 19 PRO 4.578 -2.015 -4.754 20 LYS 4.153 1.605 -3.592 21 LEU 6.577 2.695 -0.841 22 LEU 6.055 0.960 2.535 23 PRO 6.423 3.838 5.109 24 CYS 2.752 4.828 4.751 25 LEU 1.051 1.384 4.679 26 HIS 1.048 1.533 0.880 27 THR 1.626 -2.066 -0.111 28 LEU -2.065 -2.682 -0.682 29 CYS -3.214 -3.141 -4.288 30 SER -2.903 -0.544 -7.052 31 GLY -6.521 -0.808 -8.238 32 CYS -8.812 -0.724 -5.178 33 LEU -6.784 1.088 -2.482 34 GLU -6.239 4.822 -2.007 35 ALA -6.078 5.774 1.674 36 SER -9.768 4.877 1.467 37 GLY -9.618 2.237 4.224 38 MET -6.095 0.931 4.949 39 GLN -4.431 3.828 6.903 40 CYS -3.317 6.717 4.684 41 PRO -4.254 10.306 3.747 42 ILE -5.875 10.066 0.270 43 CYS -2.385 8.889 -0.746 44 GLN -3.332 7.799 -4.301 45 ALA -0.338 9.501 -5.980 46 PRO 3.166 8.168 -5.141 47 TRP 1.939 4.606 -5.895 48 PRO 4.619 4.057 -8.575 49 LEU 7.382 5.521 -6.368 50 GLY 8.206 3.279 -3.373 51 ALA 11.062 3.316 -0.815 52 ASP 11.960 0.049 0.973 53 THR 9.101 -2.322 0.081 54 PRO 8.551 -5.795 -1.393 55 ALA 6.882 -4.749 -4.668 56 LEU 5.465 -7.303 -7.133 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 T T T T C C C C T T 10 T T/S S S S C C C C C 20 C T T T T C C C T T 30 T T T T T T C S S S 40 S C C C C T T T T/S S 50 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 B S 20 t T T t S B T 30 T t S S S S S S 40 S S S S S S 50 S S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 0.0 0.0 92.1 2 GLU 26.1 18.8 85.6 3 GLU 58.9 42.5 73.6 4 PHE 83.4 50.0 67.8 5 GLN 31.1 20.9 76.8 6 PHE 110.2 66.1 59.0 7 LEU 60.4 40.9 64.0 8 ARG 91.8 44.0 65.3 9 CYS 99.0 99.8 40.2 10 GLN 117.4 79.0 43.2 11 GLN 22.9 15.4 79.8 12 CYS 28.4 28.7 58.1 13 GLN 67.0 45.1 70.5 14 ALA 13.8 18.9 76.3 15 GLU 0.0 0.0 85.7 16 ALA 60.8 83.8 63.1 17 LYS 60.7 35.0 70.2 18 CYS 99.2 100.0 42.4 19 PRO 82.4 66.2 60.3 20 LYS 173.2 99.9 36.3 21 LEU 116.9 79.1 43.3 22 LEU 128.5 86.9 48.5 23 PRO 58.2 46.8 62.2 24 CYS 72.5 73.1 42.6 25 LEU 144.6 97.9 44.1 26 HIS 150.2 100.0 31.5 27 THR 106.9 100.0 41.0 28 LEU 146.6 99.2 31.2 29 CYS 92.8 93.5 38.5 30 SER 38.6 46.2 64.4 31 GLY 0.0 0.0 76.5 32 CYS 62.7 63.2 60.2 33 LEU 147.8 100.0 40.8 34 GLU 81.0 58.4 61.5 35 ALA 72.6 100.0 53.5 36 SER 45.3 54.1 81.5 37 GLY 2.3 6.6 78.2 38 MET 148.4 93.1 41.2 39 GLN 36.8 24.8 78.6 40 CYS 93.9 94.7 38.4 41 PRO 27.1 21.8 65.8 42 ILE 32.6 22.7 79.0 43 CYS 84.8 85.5 49.4 44 GLN 53.7 36.1 67.3 45 ALA 16.3 22.5 77.5 46 PRO 75.1 60.3 55.2 47 TRP 183.1 89.3 45.6 48 PRO 31.2 25.1 77.7 49 LEU 14.1 9.5 83.5 50 GLY 30.5 87.7 57.0 51 ALA 24.7 34.1 64.7 52 ASP 6.7 6.0 76.1 53 THR 101.1 94.6 55.6 54 PRO 70.0 56.2 60.8 55 ALA 35.0 48.2 67.6 56 LEU 85.9 58.1 67.8