Protein Data Bank File : 1pou Title : DNA-BINDING PROTEIN 14-JUN-93 1POU Number of Amino Acid Residues : 71 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP LEU GLU GLU LEU GLU GLN PHE ALA LYS 10 THR PHE LYS GLN ARG ARG ILE LYS LEU GLY 20 PHE THR GLN GLY ASP VAL GLY LEU ALA MET 30 GLY LYS LEU TYR GLY ASN ASP PHE SER GLN 40 THR THR ILE SER ARG PHE GLU ALA LEU ASN 50 LEU SER PHE LYS ASN MET CYS LYS LEU LYS 60 PRO LEU LEU GLU LYS TRP LEU ASN ASP ALA 70 GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 156.6 175.6 177.9 81.2 2 LEU -40.1 -48.3 -178.8 -78.6 70.1 3 GLU -54.0 -36.5 174.3 -65.4 -62.1 -58.9 4 GLU -79.9 -49.1 -175.7 -61.9 87.0 73.5 5 LEU -51.8 -48.8 -177.2 -66.1 168.0 6 GLU -55.9 -62.7 -178.2 57.2 -160.2 71.7 7 GLN -59.1 -43.6 177.0 64.9 -175.6 -79.5 8 PHE -56.0 -52.4 -178.9 173.6 86.6 9 ALA -58.8 -52.3 176.4 10 LYS -51.7 -48.9 -179.9 -179.2 -79.9 -56.3 -176.5 11 THR -62.3 -45.8 176.0 -57.2 12 PHE -54.9 -46.0 174.1 -174.1 85.9 13 LYS -57.9 -46.1 179.1 -175.5 172.9 178.1 175.6 14 GLN -59.2 -46.8 177.4 -52.4 -35.8 -76.1 15 ARG -58.9 -46.4 176.8 -73.0 -73.1 -62.5 99.4 16 ARG -55.2 -47.1 175.4 -173.4 175.4 66.6 94.9 17 ILE -59.5 -47.0 178.8 -69.4 166.2 18 LYS -57.8 -42.0 173.8 -178.0 55.5 57.7 174.9 19 LEU -67.5 -15.7 -173.6 -63.5 173.7 20 GLY 69.2 33.0 -174.9 21 PHE -91.9 79.5 -173.0 -87.5 28.1 22 THR -105.7 -178.0 -175.5 175.7 23 GLN 59.5 -71.9 169.1 -49.8 -53.0 -81.1 24 GLY -169.1 39.2 -177.9 25 ASP -59.5 -49.8 170.4 -165.6 -33.2 26 VAL -50.8 -50.4 178.7 161.4 27 GLY -51.8 -44.7 178.5 28 LEU -64.4 -52.1 -179.3 -175.0 60.9 29 ALA -56.3 -57.4 169.8 30 MET -50.3 -42.5 170.7 -142.7 179.2 -51.5 31 GLY -44.5 -54.3 178.3 32 LYS -67.2 -49.1 -169.5 -64.7 169.0 177.9 -65.5 33 LEU -71.7 -53.4 -169.6 -62.3 159.9 34 TYR -116.4 -58.2 -171.4 -47.5 -34.5 35 GLY 168.4 152.4 -169.8 36 ASN -76.6 60.9 172.5 54.1 -100.4 37 ASP -110.4 174.3 176.2 -171.4 12.8 38 PHE 66.7 39.9 171.2 -58.9 82.7 39 SER -74.9 57.7 -173.9 44.9 40 GLN 72.5 -53.0 177.1 -148.1 65.6 -143.1 41 THR -41.7 -70.8 -171.3 45.9 42 THR -63.0 -32.8 171.4 -22.1 43 ILE -60.5 -53.6 177.6 -73.3 -66.3 44 SER -53.9 -48.4 175.7 -51.4 45 ARG -56.7 -42.8 178.9 -69.6 -173.5 63.3 162.6 46 PHE -57.9 -55.5 176.5 -172.3 45.3 47 GLU -57.1 -38.0 175.6 -76.0 82.3 74.3 48 ALA -76.3 -1.4 -173.3 49 LEU 51.3 30.6 -174.6 -56.5 98.8 50 ASN -83.9 35.2 179.4 -170.3 51.2 51 LEU -139.9 19.7 169.3 -71.1 167.3 52 SER 28.6 60.8 171.7 -48.1 53 PHE 68.9 -58.6 -170.8 -166.0 72.0 54 LYS -41.3 -56.0 177.4 58.1 -166.3 -178.8 -179.0 55 ASN -76.7 -49.7 -173.4 -179.2 -103.8 56 MET -45.1 -44.8 179.9 -60.9 -176.7 67.0 57 CYS -59.8 -35.7 174.9 179.7 58 LYS -79.4 -36.0 -178.1 -46.7 -169.4 -175.0 72.5 59 LEU -65.3 -45.3 178.5 117.9 61.0 60 LYS -44.7 -62.3 -178.0 170.4 163.5 59.1 -179.1 61 PRO -60.3 -34.5 178.7 22.2 -32.7 62 LEU -62.1 -48.3 178.5 -111.5 68.7 63 LEU -64.2 -38.8 178.2 -60.5 -157.2 64 GLU -59.1 -51.6 175.6 -167.0 172.3 85.6 65 LYS -60.9 -39.1 173.7 178.2 52.8 57.0 177.7 66 TRP -57.0 -44.8 180.0 -170.7 94.2 67 LEU -60.0 -47.3 175.5 -139.3 -179.4 68 ASN -56.0 -46.7 -177.6 178.3 -174.5 69 ASP -67.4 -51.2 -174.3 162.2 82.7 70 ALA 41.1 48.8 169.7 71 GLU -54.2 -65.0 0.0 -179.3 -176.0 76.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP 3.261 6.263 -1.466 2 LEU 5.248 7.249 1.661 3 GLU 4.937 3.639 2.916 4 GLU 7.001 2.439 -0.088 5 LEU 9.263 5.517 -0.258 6 GLU 10.476 5.222 3.378 7 GLN 11.488 1.551 3.295 8 PHE 12.774 1.910 -0.298 9 ALA 14.938 4.928 0.668 10 LYS 16.201 3.213 3.842 11 THR 17.023 0.096 1.769 12 PHE 18.772 2.209 -0.904 13 LYS 20.873 3.701 1.923 14 GLN 21.726 0.186 3.217 15 ARG 22.780 -0.876 -0.301 16 ARG 24.776 2.370 -0.663 17 ILE 26.518 1.602 2.663 18 LYS 27.165 -1.998 1.482 19 LEU 28.776 -0.583 -1.706 20 GLY 30.785 1.771 0.579 21 PHE 29.387 4.669 -1.491 22 THR 30.145 7.425 1.006 23 GLN 31.066 11.151 0.838 24 GLY 29.096 11.470 -2.407 25 ASP 30.002 8.421 -4.551 26 VAL 26.315 7.969 -5.509 27 GLY 26.245 11.759 -6.082 28 LEU 29.218 11.494 -8.500 29 ALA 27.799 8.478 -10.328 30 MET 24.353 10.135 -10.616 31 GLY 26.388 13.233 -11.565 32 LYS 27.654 11.375 -14.640 33 LEU 24.445 9.424 -15.394 34 TYR 21.615 11.916 -14.704 35 GLY 22.832 15.126 -12.984 36 ASN 24.902 16.293 -9.959 37 ASP 22.261 15.829 -7.228 38 PHE 22.355 13.480 -4.157 39 SER 25.641 14.822 -2.760 40 GLN 24.791 12.949 0.516 41 THR 22.285 15.786 1.229 42 THR 19.424 14.730 -1.066 43 ILE 19.894 11.044 -0.083 44 SER 19.621 12.024 3.605 45 ARG 16.534 14.120 2.745 46 PHE 15.073 11.133 0.836 47 GLU 15.445 8.807 3.834 48 ALA 14.042 11.646 6.017 49 LEU 11.183 12.023 3.437 50 ASN 11.997 15.784 3.509 51 LEU 10.774 16.127 -0.119 52 SER 7.016 15.547 0.553 53 PHE 6.138 12.961 -2.164 54 LYS 6.119 15.345 -5.190 55 ASN 9.823 14.943 -6.046 56 MET 10.267 11.651 -4.203 57 CYS 7.914 9.757 -6.533 58 LYS 10.125 10.768 -9.501 59 LEU 13.307 10.314 -7.417 60 LYS 12.527 6.675 -6.422 61 PRO 12.715 5.141 -9.965 62 LEU 15.881 7.158 -10.782 63 LEU 17.508 5.644 -7.675 64 GLU 16.064 2.190 -8.494 65 LYS 17.593 2.354 -11.991 66 TRP 20.751 3.760 -10.355 67 LEU 20.773 0.654 -8.094 68 ASN 20.393 -1.580 -11.178 69 ASP 23.228 0.330 -12.940 70 ALA 25.597 0.678 -9.919 71 GLU 28.236 2.663 -11.835 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H H H H H H H H H 20 C C C H H H H H H H 30 H H H H S S S S C H 40 H H H H H H H H H C 50 C C H H H H H H H H/H 60 H H H H H H H H H H/S 70 S 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 H 10 H H H H H H H H H h 20 t t T h H H H H H H 30 H H H h t S S h 40 H H H H H H H h T T 50 T T T T h H H H H H 60 H H H H H H H H H h 70 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 42.2 38.2 63.4 2 LEU 58.8 39.8 65.4 3 GLU 31.4 22.7 86.4 4 GLU 58.8 42.4 74.8 5 LEU 147.6 99.8 35.9 6 GLU 72.8 52.5 65.0 7 GLN 38.9 26.2 70.5 8 PHE 132.1 79.2 44.5 9 ALA 72.6 100.0 50.1 10 LYS 63.2 36.5 70.1 11 THR 46.0 43.0 66.5 12 PHE 164.7 98.7 30.3 13 LYS 98.0 56.5 68.3 14 GLN 69.5 46.8 60.7 15 ARG 123.8 59.3 52.3 16 ARG 195.2 93.4 42.4 17 ILE 48.9 34.1 74.9 18 LYS 25.8 14.9 87.7 19 LEU 104.1 70.4 56.2 20 GLY 3.5 10.0 77.7 21 PHE 130.0 77.9 58.4 22 THR 34.6 32.4 81.9 23 GLN 9.6 6.5 86.8 24 GLY 22.6 65.0 73.9 25 ASP 61.4 55.6 59.6 26 VAL 116.7 98.2 28.2 27 GLY 32.1 92.2 61.3 28 LEU 33.3 22.5 77.9 29 ALA 68.5 94.3 60.6 30 MET 157.5 98.8 32.7 31 GLY 28.8 82.7 65.2 32 LYS 54.2 31.2 77.3 33 LEU 108.4 73.3 62.8 34 TYR 129.3 71.5 47.7 35 GLY 4.7 13.6 79.9 36 ASN 1.3 1.1 85.6 37 ASP 45.4 41.1 66.4 38 PHE 158.2 94.8 38.5 39 SER 24.6 29.5 76.2 40 GLN 91.6 61.6 76.7 41 THR 24.2 22.6 82.6 42 THR 86.1 80.5 54.9 43 ILE 142.5 99.3 42.8 44 SER 33.0 39.4 75.2 45 ARG 101.0 48.3 66.9 46 PHE 166.8 100.0 33.5 47 GLU 120.1 86.7 48.6 48 ALA 20.5 28.2 72.8 49 LEU 108.9 73.7 57.6 50 ASN 40.5 33.5 72.7 51 LEU 119.2 80.6 54.1 52 SER 9.5 11.4 75.4 53 PHE 85.0 50.9 56.7 54 LYS 24.6 14.2 80.0 55 ASN 55.3 45.7 55.1 56 MET 158.8 99.6 39.6 57 CYS 45.9 46.2 59.8 58 LYS 34.2 19.7 80.0 59 LEU 141.6 95.8 33.8 60 LYS 130.3 75.2 45.8 61 PRO 60.5 48.6 69.4 62 LEU 67.9 46.0 61.1 63 LEU 147.8 100.0 23.4 64 GLU 42.1 30.3 65.8 65 LYS 53.4 30.8 81.8 66 TRP 203.3 99.2 31.4 67 LEU 108.1 73.1 53.6 68 ASN 30.5 25.2 82.8 69 ASP 64.7 58.6 59.1 70 ALA 50.3 69.3 65.3 71 GLU 68.7 49.5 57.5