Protein Data Bank File : 1hrya Title : COMPLEX (DNA-BINDING PROTEIN/DNA) 09-MAY-95 1HRY Number of Amino Acid Residues : 73 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP ARG VAL LYS ARG PRO MET ASN ALA PHE 10 ILE VAL TRP SER ARG ASP GLN ARG ARG LYS 20 MET ALA LEU GLU ASN PRO ARG MET ARG ASN 30 SER GLU ILE SER LYS GLN LEU GLY TYR GLN 40 TRP LYS MET LEU THR GLU ALA GLU LYS TRP 50 PRO PHE PHE GLN GLU ALA GLN LYS LEU GLN 60 ALA MET HIS ARG GLU LYS TYR PRO ASN TYR 70 LYS TYR ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 -101.3 -179.2 -67.0 -63.6 2 ARG -76.9 133.6 177.0 -59.4 135.8 167.0 167.5 3 VAL -88.5 156.3 -179.4 -176.0 4 LYS -72.6 151.8 -179.7 16.4 165.1 -88.7 167.0 5 ARG -142.5 124.0 -180.0 48.9 -80.8 133.0 173.5 6 PRO -66.8 -173.1 178.9 10.2 -11.6 7 MET -64.9 147.3 179.7 -55.6 -65.7 -178.7 8 ASN -86.5 143.7 -179.8 -44.9 119.6 9 ALA -44.0 -22.4 179.6 10 PHE -78.6 -53.6 179.7 169.4 77.0 11 ILE -63.1 -25.1 177.9 -79.7 167.3 12 VAL -52.1 -50.5 178.3 172.7 13 TRP -52.5 -55.5 179.8 -80.4 -50.1 14 SER -39.5 -57.9 179.3 -159.6 15 ARG -41.1 -77.0 -177.7 -53.6 -71.4 -46.5 180.0 16 ASP -77.5 -50.3 -177.8 -54.1 -64.1 17 GLN -51.0 -51.8 -178.8 -178.8 61.4 -96.5 18 ARG -58.5 -39.6 180.0 -174.1 171.0 158.2 -59.3 19 ARG -52.2 -34.8 179.1 166.7 65.8 108.6 174.6 20 LYS -64.3 -47.0 179.9 -177.3 -150.4 75.4 159.2 21 MET -63.0 -30.0 -179.2 -163.1 72.7 170.4 22 ALA -72.3 -29.2 -179.0 23 LEU -66.1 -63.8 -177.8 -66.1 172.3 24 GLU -81.0 -20.3 -178.8 -70.4 178.9 31.3 25 ASN -136.7 58.6 178.8 -66.6 78.6 26 PRO -67.1 -3.3 -178.5 9.9 -11.0 27 ARG -124.0 68.2 177.9 -60.1 165.8 -176.4 -66.5 28 MET -81.1 125.8 178.6 -60.8 -53.6 -69.6 29 ARG -64.6 -74.7 -177.7 -87.4 40.3 -172.1 -116.7 30 ASN -85.8 -168.3 179.0 -68.7 1.2 31 SER -91.6 61.2 -179.3 -88.3 32 GLU -80.4 -43.7 179.0 -59.7 -159.4 -57.0 33 ILE -48.8 -15.6 -179.8 157.7 -82.2 34 SER -80.9 -60.7 -180.0 -62.4 35 LYS -65.4 -25.9 -179.3 -66.9 64.5 152.7 32.8 36 GLN -66.5 -46.5 179.5 -72.2 -77.8 21.3 37 LEU -58.7 -34.8 178.9 -74.6 160.2 38 GLY -53.9 -40.7 179.2 39 TYR -62.1 -40.0 -179.9 165.1 89.0 40 GLN -63.1 -34.9 -179.7 -80.5 -87.1 95.9 41 TRP -62.3 -42.9 178.6 -57.5 169.4 42 LYS -68.0 -10.0 178.3 -68.2 120.6 -163.4 -91.0 43 MET -146.1 70.6 -178.3 -61.2 85.0 163.9 44 LEU -61.9 132.1 179.3 -70.0 156.3 45 THR -82.4 117.8 -179.6 59.8 46 GLU -59.0 -27.3 -179.7 -54.0 -179.9 10.7 47 ALA -59.4 -24.9 -178.5 48 GLU -102.2 -24.6 -178.0 -80.2 61.1 87.4 49 LYS -69.3 -78.7 -177.4 -61.0 176.5 82.2 -126.2 50 TRP -37.3 -55.2 -179.1 177.7 56.6 51 PRO -42.2 -76.6 -175.3 -6.9 -3.4 52 PHE -79.2 -15.0 179.1 72.0 80.2 53 PHE -63.4 -39.3 -179.5 -90.4 70.0 54 GLN -53.6 -47.0 179.9 -80.3 140.5 126.4 55 GLU -67.5 -53.3 -178.9 166.9 163.2 -57.5 56 ALA -49.0 -22.5 -179.4 57 GLN -65.0 -57.5 -178.3 -74.5 -85.6 -97.1 58 LYS -66.9 -38.0 178.7 55.8 165.5 166.2 -173.6 59 LEU -46.0 -55.2 -179.8 -84.8 -77.3 60 GLN -61.3 -50.7 -177.7 -111.3 -172.5 -81.6 61 ALA -50.1 -46.9 -178.1 62 MET -64.2 -67.5 -178.5 -58.8 -165.8 -125.6 63 HIS -55.0 -34.9 -180.0 -48.1 148.5 64 ARG -61.2 -46.2 -177.4 -83.8 -83.1 153.4 173.1 65 GLU -66.8 -13.7 178.8 -62.3 -90.0 37.8 66 LYS -87.0 -20.7 -176.8 -76.5 173.9 159.2 26.7 67 TYR -131.7 54.9 -179.1 -62.4 -79.1 68 PRO -50.3 -70.1 -177.0 -3.1 -2.2 69 ASN -84.7 -10.0 179.5 -47.6 88.7 70 TYR -70.9 121.3 -178.8 -162.1 -83.7 71 LYS -122.6 169.5 179.1 -54.1 -150.0 -143.0 77.3 72 TYR -59.9 165.7 -177.3 -78.8 -86.6 73 ARG -141.0 59.3 0.0 -155.1 145.3 -172.0 -64.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP 17.460 -8.995 -4.871 2 ARG 14.121 -8.840 -6.703 3 VAL 12.026 -11.976 -6.542 4 LYS 10.081 -12.994 -9.654 5 ARG 6.373 -11.999 -9.725 6 PRO 3.681 -13.327 -12.140 7 MET 1.111 -10.972 -13.659 8 ASN -0.933 -9.087 -11.034 9 ALA -4.694 -9.788 -10.913 10 PHE -4.870 -6.198 -12.196 11 ILE -2.674 -6.597 -15.301 12 VAL -4.576 -9.884 -15.895 13 TRP -7.574 -7.753 -16.934 14 SER -5.229 -5.725 -19.137 15 ARG -4.272 -8.905 -21.023 16 ASP -7.830 -10.004 -22.056 17 GLN -10.001 -6.991 -21.013 18 ARG -7.830 -4.608 -22.977 19 ARG -7.957 -6.852 -26.034 20 LYS -11.655 -5.912 -26.070 21 MET -10.819 -2.181 -26.052 22 ALA -8.301 -2.825 -28.859 23 LEU -10.990 -4.363 -31.137 24 GLU -13.495 -1.492 -31.288 25 ASN -10.948 1.160 -30.196 26 PRO -7.454 0.131 -31.416 27 ARG -6.678 3.907 -31.672 28 MET -6.938 5.522 -28.229 29 ARG -5.474 9.035 -28.362 30 ASN -4.796 9.648 -24.686 31 SER -4.534 7.210 -21.786 32 GLU -8.326 6.854 -21.424 33 ILE -8.353 3.042 -21.256 34 SER -6.588 3.791 -17.948 35 LYS -9.178 5.966 -16.144 36 GLN -11.891 3.879 -17.830 37 LEU -10.843 0.649 -16.114 38 GLY -11.010 2.609 -12.853 39 TYR -14.760 2.941 -13.523 40 GLN -15.001 -0.861 -13.954 41 TRP -13.332 -1.278 -10.545 42 LYS -16.104 0.660 -8.777 43 MET -18.372 -1.840 -10.626 44 LEU -16.430 -5.086 -11.185 45 THR -18.153 -7.328 -13.767 46 GLU -18.684 -10.811 -12.238 47 ALA -18.460 -12.244 -15.774 48 GLU -14.715 -11.452 -15.612 49 LYS -14.050 -12.103 -11.884 50 TRP -14.946 -15.751 -11.180 51 PRO -13.297 -17.061 -14.435 52 PHE -9.613 -15.989 -13.959 53 PHE -9.671 -15.396 -10.145 54 GLN -9.667 -19.167 -9.459 55 GLU -6.340 -19.509 -11.305 56 ALA -4.794 -16.270 -9.943 57 GLN -5.326 -17.822 -6.487 58 LYS -2.775 -20.646 -6.848 59 LEU -0.260 -18.540 -8.915 60 GLN 0.231 -16.361 -5.836 61 ALA 0.050 -19.305 -3.382 62 MET 2.981 -21.178 -4.998 63 HIS 5.535 -18.382 -5.445 64 ARG 4.375 -16.918 -2.121 65 GLU 5.200 -20.102 -0.237 66 LYS 8.720 -19.970 -1.754 67 TYR 9.438 -16.478 -0.304 68 PRO 7.626 -16.286 3.079 69 ASN 9.881 -13.800 4.952 70 TYR 11.599 -12.389 1.838 71 LYS 10.087 -8.888 1.362 72 TYR 10.610 -5.953 -0.983 73 ARG 13.586 -3.716 -0.139 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S H H H 10 H H H H H 3/H H H H H 20 H H H C C S S S S S 30 C H H H H H H H H H 40 H H H H T T T T/T T T 50 T H H H H H H 3 3/H H 60 H H H H H H H H S S 70 S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H 10 H H H H H H H H H H 20 H H H H h S S S 30 h H H H H H H H H H 40 H H h t h H H H H H 50 H H H H H H H H H H 60 H H H H H H h S S 70 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 0.0 0.0 89.4 2 ARG 17.2 8.3 88.2 3 VAL 86.0 72.3 51.8 4 LYS 58.7 33.8 73.3 5 ARG 82.2 39.3 75.5 6 PRO 80.4 64.6 60.9 7 MET 56.1 35.2 69.6 8 ASN 39.1 32.3 71.5 9 ALA 39.2 54.0 53.3 10 PHE 66.4 39.8 61.6 11 ILE 70.9 49.4 60.0 12 VAL 89.8 75.6 47.2 13 TRP 176.9 86.3 36.6 14 SER 57.5 68.8 47.3 15 ARG 65.7 31.4 74.6 16 ASP 10.3 9.3 77.9 17 GLN 124.5 83.8 49.1 18 ARG 87.3 41.8 69.4 19 ARG 50.0 23.9 76.0 20 LYS 51.6 29.7 76.8 21 MET 115.4 72.4 53.6 22 ALA 44.0 60.6 68.8 23 LEU 45.2 30.6 73.5 24 GLU 9.8 7.0 85.4 25 ASN 57.6 47.7 58.9 26 PRO 58.8 47.2 74.6 27 ARG 19.9 9.5 87.5 28 MET 129.2 81.0 63.0 29 ARG 16.4 7.9 90.4 30 ASN 13.7 11.3 78.4 31 SER 19.7 23.6 71.8 32 GLU 50.9 36.7 65.5 33 ILE 97.8 68.2 42.4 34 SER 38.3 45.8 59.8 35 LYS 27.4 15.8 81.8 36 GLN 50.4 33.9 67.9 37 LEU 130.3 88.1 41.1 38 GLY 15.1 43.5 63.9 39 TYR 57.4 31.7 71.0 40 GLN 105.9 71.3 58.6 41 TRP 152.4 74.3 42.9 42 LYS 34.3 19.8 75.2 43 MET 58.7 36.8 74.8 44 LEU 94.3 63.8 53.9 45 THR 61.1 57.1 79.4 46 GLU 10.4 7.5 83.9 47 ALA 9.0 12.4 81.2 48 GLU 82.1 59.2 65.8 49 LYS 101.1 58.3 52.8 50 TRP 24.4 11.9 79.3 51 PRO 67.3 54.1 70.8 52 PHE 125.3 75.1 46.2 53 PHE 94.7 56.8 51.9 54 GLN 65.9 44.3 67.4 55 GLU 37.7 27.2 68.7 56 ALA 52.5 72.3 50.7 57 GLN 27.1 18.2 84.4 58 LYS 60.1 34.7 65.4 59 LEU 91.5 61.9 52.1 60 GLN 41.6 28.0 79.7 61 ALA 22.5 30.9 65.6 62 MET 63.1 39.6 67.6 63 HIS 110.8 73.8 48.1 64 ARG 56.9 27.2 78.8 65 GLU 20.7 14.9 79.5 66 LYS 56.2 32.4 72.1 67 TYR 107.9 59.6 52.5 68 PRO 47.0 37.7 85.8 69 ASN 2.8 2.3 79.1 70 TYR 92.4 51.0 66.6 71 LYS 23.9 13.8 86.6 72 TYR 13.4 7.4 83.2 73 ARG 3.7 1.8 89.3