Protein Data Bank File : 1aa3 Title : DOUBLE-STRANDED DNA BINDING DOMAIN 22-JAN-97 1AA3 Number of Amino Acid Residues : 63 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ILE ASN PHE TYR GLY GLU LEU VAL ASP LEU 10 GLY VAL LYS GLU LYS LEU ILE GLU LYS ALA 20 GLY ALA TRP TYR SER TYR LYS GLY GLU LYS 30 ILE GLY GLN GLY LYS ALA ASN ALA THR ALA 40 TRP LEU LYS ASP ASN PRO GLU THR ALA LYS 50 GLU ILE GLU LYS LYS VAL ARG GLU LEU LEU 60 LEU SER ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ILE 0.0 -90.8 -179.8 26.5 153.1 2 ASN 43.9 -100.1 179.6 -65.1 -77.8 3 PHE 161.0 -97.3 179.9 36.7 20.3 4 TYR 82.2 -2.2 179.0 -71.1 13.8 5 GLY -120.1 -40.5 177.5 6 GLU -95.9 -24.2 177.9 120.0 176.5 -51.9 7 LEU -65.0 -56.8 178.1 158.3 72.8 8 VAL -61.3 -30.6 179.2 -177.7 9 ASP -75.7 -18.2 180.0 -159.7 -60.8 10 LEU -91.8 -41.6 -179.8 -139.8 -48.2 11 GLY -72.5 -60.7 179.0 12 VAL -46.7 -28.8 178.0 -165.9 13 LYS -90.1 -30.0 178.3 174.4 105.7 -120.0 157.8 14 GLU -97.0 -76.7 177.8 -84.5 -52.9 -19.5 15 LYS 167.5 39.2 177.4 39.7 106.2 114.2 -58.9 16 LEU -98.1 -40.4 179.5 -70.5 88.0 17 ILE -100.0 117.2 176.7 -38.3 -58.1 18 GLU -89.4 126.8 -178.0 -31.4 -154.3 -3.4 19 LYS -143.3 151.0 -179.7 70.5 126.9 -150.4 -160.8 20 ALA -96.5 29.0 -179.8 21 GLY 116.1 -62.2 179.9 22 ALA -113.1 -49.9 179.9 23 TRP -71.6 126.5 -179.9 -107.2 103.1 24 TYR -97.7 170.5 -179.5 -80.6 39.1 25 SER -151.1 159.7 178.6 -133.3 26 TYR -128.6 164.3 180.0 -144.8 52.0 27 LYS -61.3 52.4 179.8 45.0 77.2 159.6 -119.3 28 GLY 161.8 -40.1 -178.7 29 GLU -151.5 136.8 176.8 176.0 144.4 -79.3 30 LYS -46.5 141.2 -179.9 -156.5 85.1 113.6 -100.6 31 ILE -89.4 -35.1 -179.5 -14.9 -159.4 32 GLY 135.6 177.7 179.2 33 GLN -46.8 172.4 -178.7 -146.4 -173.1 -49.0 34 GLY -77.5 -31.7 -178.0 35 LYS -121.2 -23.4 179.5 24.3 -159.4 113.2 174.3 36 ALA -85.6 -27.0 -179.2 37 ASN -161.4 32.9 179.7 -72.4 -91.4 38 ALA -62.4 -64.7 -179.8 39 THR -91.0 12.5 178.5 164.7 40 ALA -69.9 -42.0 175.6 41 TRP -71.3 -20.5 177.6 158.2 111.4 42 LEU -89.5 -11.0 178.9 -168.6 26.2 43 LYS -73.1 -43.7 179.7 -160.7 174.5 -146.2 -93.1 44 ASP -101.4 22.3 -179.9 -123.3 87.2 45 ASN -106.3 61.0 179.0 -133.2 78.6 46 PRO -68.3 -16.3 179.2 21.4 -26.0 47 GLU -70.7 -47.4 -179.6 55.4 -154.3 21.7 48 THR -105.4 -25.0 179.5 -120.5 49 ALA -36.6 -22.9 178.8 50 LYS -91.3 -37.3 179.0 -25.3 97.9 111.6 -147.4 51 GLU -59.0 -23.8 178.8 -116.7 85.0 -35.8 52 ILE -66.3 -71.0 178.3 -6.8 -66.4 53 GLU -44.7 -35.3 -178.7 -142.5 -126.7 36.8 54 LYS -77.3 -48.4 179.1 -147.5 73.1 85.2 169.3 55 LYS -50.8 -32.4 179.4 -108.9 -58.3 134.4 107.8 56 VAL -90.5 -43.3 -179.9 152.8 57 ARG -64.5 -40.9 179.8 -163.4 106.0 141.4 -176.1 58 GLU -84.8 -11.8 179.5 -88.4 -130.9 -88.3 59 LEU -51.6 -33.8 -180.0 -162.5 79.7 60 LEU -135.4 6.0 -180.0 -132.7 118.3 61 LEU -42.7 -68.5 179.9 167.2 142.6 62 SER -86.7 44.3 -180.0 -137.5 63 ASN -63.2 151.6 0.0 70.6 97.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ILE -3.055 13.408 2.727 2 ASN -3.511 9.845 1.417 3 PHE -0.939 8.211 3.747 4 TYR 1.786 5.771 2.496 5 GLY 2.869 5.278 6.123 6 GLU -0.297 3.842 7.638 7 LEU -1.320 2.615 4.195 8 VAL 1.749 0.416 3.934 9 ASP 1.049 -0.201 7.617 10 LEU -2.514 -1.188 6.686 11 GLY -1.692 -3.422 3.692 12 VAL 1.407 -5.166 5.066 13 LYS -0.991 -5.699 7.979 14 GLU -3.913 -6.324 5.612 15 LYS -2.413 -7.458 2.327 16 LEU -1.533 -4.641 -0.095 17 ILE 2.241 -4.724 0.388 18 GLU 3.838 -8.153 0.052 19 LYS 7.134 -8.140 1.936 20 ALA 9.690 -10.678 3.195 21 GLY 10.206 -8.788 6.475 22 ALA 12.154 -5.710 5.328 23 TRP 11.844 -5.602 1.522 24 TYR 8.267 -4.656 0.589 25 SER 6.474 -5.476 -2.628 26 TYR 3.322 -4.460 -4.440 27 LYS 0.643 -6.091 -6.580 28 GLY 2.720 -5.393 -9.712 29 GLU 6.104 -3.983 -8.698 30 LYS 8.253 -4.136 -5.608 31 ILE 7.498 -1.009 -3.663 32 GLY 10.896 -0.832 -1.932 33 GLN 12.192 -1.648 1.557 34 GLY 9.440 -1.449 4.213 35 LYS 10.776 1.735 5.720 36 ALA 13.496 2.725 3.264 37 ASN 11.178 2.515 0.233 38 ALA 7.872 0.842 1.133 39 THR 5.651 3.645 -0.135 40 ALA 8.432 5.280 -2.182 41 TRP 7.285 3.197 -5.136 42 LEU 3.880 4.091 -3.765 43 LYS 5.089 7.712 -3.708 44 ASP 5.200 7.911 -7.516 45 ASN 2.339 5.401 -7.907 46 PRO -0.616 7.748 -8.506 47 GLU -1.914 5.026 -10.808 48 THR -2.435 2.479 -8.000 49 ALA -1.784 4.864 -5.057 50 LYS -5.566 5.088 -4.813 51 GLU -6.080 1.342 -5.115 52 ILE -3.997 1.127 -1.930 53 GLU -6.355 3.192 0.265 54 LYS -9.140 1.363 -1.606 55 LYS -7.694 -2.140 -1.335 56 VAL -7.803 -1.321 2.366 57 ARG -10.927 0.881 2.361 58 GLU -12.840 -1.725 0.321 59 LEU -11.116 -4.529 2.235 60 LEU -14.053 -4.214 4.627 61 LEU -16.134 -1.489 2.928 62 SER -19.084 -3.826 2.266 63 ASN -18.210 -5.900 5.354 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C H H H H H H H H 10 H H H C C S S S S/T T 20 T T/S S S S S/T T T T C 30 C C T T T T C C H H 40 H H H H H C C H H H 50 H H H H H H H H H 3 60 S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S h H H H H 10 H h T t S S B S 20 S e E E B S S S 30 E E e S S t T h H 40 H H H h t T T h H H 50 H H H H H H H H H H 60 h T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ILE 0.0 0.0 96.5 2 ASN 41.8 34.6 65.7 3 PHE 141.3 84.7 50.6 4 TYR 145.9 80.6 46.6 5 GLY 0.0 0.0 80.4 6 GLU 30.6 22.1 67.4 7 LEU 147.6 99.8 26.0 8 VAL 110.8 93.3 38.6 9 ASP 23.3 21.1 76.5 10 LEU 89.2 60.3 54.7 11 GLY 34.8 100.0 53.2 12 VAL 97.0 81.7 53.4 13 LYS 27.8 16.0 86.2 14 GLU 90.0 65.0 46.3 15 LYS 56.9 32.8 71.5 16 LEU 144.0 97.5 41.7 17 ILE 143.5 100.0 32.3 18 GLU 28.8 20.8 78.7 19 LYS 116.9 67.4 63.8 20 ALA 1.4 2.0 82.6 21 GLY 9.5 27.4 70.8 22 ALA 25.7 35.4 68.8 23 TRP 70.2 34.2 66.7 24 TYR 158.8 87.7 44.4 25 SER 58.6 70.1 53.1 26 TYR 180.5 99.7 28.3 27 LYS 81.2 46.8 66.6 28 GLY 0.0 0.0 75.9 29 GLU 33.7 24.3 78.9 30 LYS 82.2 47.4 66.6 31 ILE 143.5 100.0 35.0 32 GLY 29.5 84.8 48.7 33 GLN 87.4 58.8 54.2 34 GLY 34.8 100.0 44.8 35 LYS 24.6 14.2 88.5 36 ALA 35.0 48.2 76.7 37 ASN 54.4 45.0 64.9 38 ALA 70.2 96.7 46.5 39 THR 74.5 69.7 47.1 40 ALA 40.5 55.8 67.1 41 TRP 168.3 82.1 52.1 42 LEU 147.8 100.0 29.4 43 LYS 30.1 17.4 80.4 44 ASP 0.0 0.0 83.5 45 ASN 114.5 94.7 45.8 46 PRO 35.9 28.9 78.0 47 GLU 26.6 19.2 78.9 48 THR 97.7 91.4 45.9 49 ALA 66.4 91.5 47.7 50 LYS 56.7 32.7 81.4 51 GLU 64.3 46.4 69.2 52 ILE 143.5 100.0 30.5 53 GLU 86.2 62.2 58.9 54 LYS 65.7 37.9 72.9 55 LYS 67.7 39.0 65.0 56 VAL 95.2 80.2 42.0 57 ARG 57.0 27.3 79.7 58 GLU 58.4 42.2 60.0 59 LEU 114.2 77.3 55.4 60 LEU 35.4 24.0 79.5 61 LEU 58.1 39.3 74.7 62 SER 7.7 9.2 77.8 63 ASN 40.0 33.1 73.5