Protein Data Bank File : 1r63 Title : GENE REGULATING PROTEIN 08-NOV-96 1R63 Number of Amino Acid Residues : 63 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER ILE SER SER ARG VAL LYS SER LYS ARG 10 ILE GLN LEU GLY LEU ASN GLN ALA GLU LEU 20 ALA GLN LYS VAL GLY THR THR GLN GLN SER 30 ILE GLU GLN LEU GLU ASN GLY LYS THR LYS 40 ARG PRO ARG PHE LEU PRO GLU LEU ALA SER 50 ALA LEU GLY VAL SER VAL ASP TRP LEU LEU 60 ASN GLY THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 144.3 -173.4 21.9 2 ILE -59.9 -54.4 -174.5 -144.0 -68.6 3 SER -61.5 -49.5 174.5 33.2 4 SER -43.6 -59.0 -179.9 171.7 5 ARG -54.4 -55.7 -166.7 -69.5 -170.6 -105.4 88.8 6 VAL -63.4 -33.9 169.5 168.9 7 LYS -72.1 -62.5 -166.1 -164.5 163.2 -171.3 57.8 8 SER -58.7 -36.4 178.4 -47.6 9 LYS -66.8 -38.4 178.1 -134.4 64.4 160.4 65.0 10 ARG -59.9 -47.0 177.5 -144.1 -165.6 -38.8 -64.7 11 ILE -56.6 -47.0 178.4 -59.7 -82.7 12 GLN -53.8 -51.7 179.0 -153.9 -63.9 120.8 13 LEU -64.7 -28.9 -178.9 -89.7 71.6 14 GLY 86.1 15.5 173.4 15 LEU -90.4 140.1 163.8 -61.5 173.5 16 ASN -74.7 174.4 163.8 -49.1 -72.8 17 GLN -49.7 -32.2 -177.1 -66.3 161.6 -94.1 18 ALA -69.0 -58.5 -177.9 19 GLU -63.0 -39.9 176.0 -55.4 109.6 -56.1 20 LEU -54.4 -54.3 177.6 -171.4 -90.7 21 ALA -49.2 -48.8 -177.4 22 GLN -61.6 -45.9 178.7 -168.7 60.8 49.4 23 LYS -59.3 -45.5 178.3 -69.7 -171.1 -175.9 -57.5 24 VAL -65.5 -20.3 -173.3 175.7 25 GLY 67.7 25.7 165.4 26 THR -100.3 -152.4 175.3 -171.4 27 THR -129.8 157.4 -175.0 38.7 28 GLN -56.8 -36.8 -179.0 -170.2 171.6 11.2 29 GLN -59.4 -54.4 170.5 178.5 129.4 -136.3 30 SER -49.2 -51.6 178.5 -77.0 31 ILE -56.7 -36.2 -180.0 -59.1 -53.9 32 GLU -61.4 -57.2 178.3 -159.6 -83.1 -12.9 33 GLN -59.2 -38.5 -178.9 58.5 178.0 109.0 34 LEU -65.3 -44.2 177.0 -137.8 -155.6 35 GLU -57.5 -44.3 175.5 -163.4 177.0 -87.4 36 ASN -68.9 -12.2 170.7 -75.0 -100.3 37 GLY 92.9 25.4 -175.4 38 LYS -74.1 -31.0 -178.4 -137.2 -175.5 -167.8 -51.3 39 THR -95.2 145.6 -177.8 -4.6 40 LYS -125.9 -48.6 -179.7 -165.7 91.1 70.3 -145.3 41 ARG -120.4 57.7 -179.1 -131.1 75.2 -83.6 -75.7 42 PRO -67.3 146.7 176.4 27.1 -33.7 43 ARG -60.3 -34.9 -177.2 -42.1 103.9 79.2 86.5 44 PHE -91.5 28.4 174.8 65.8 -77.6 45 LEU -54.5 -58.2 -177.0 -159.1 -61.2 46 PRO -63.0 -29.6 179.1 27.2 -36.0 47 GLU -66.2 -49.9 173.2 -52.0 -84.3 38.2 48 LEU -54.7 -47.7 -179.2 177.2 66.4 49 ALA -54.8 -46.8 179.4 50 SER -66.9 -52.5 -175.0 -54.0 51 ALA -59.3 -46.0 171.8 52 LEU -64.4 -43.1 -173.0 -79.0 -179.1 53 GLY 83.7 58.8 179.2 54 VAL -142.8 159.0 -179.9 -63.7 55 SER -70.3 155.3 165.9 50.6 56 VAL -53.6 -48.7 -179.1 173.8 57 ASP -58.4 -44.9 175.4 -78.2 74.7 58 TRP -59.0 -48.3 -179.7 -178.3 93.1 59 LEU -66.2 -31.5 173.1 -89.4 167.2 60 LEU -67.0 -71.9 179.2 175.1 50.6 61 ASN -100.5 -77.9 -164.8 145.7 48.3 62 GLY 145.5 100.1 -167.3 63 THR -138.5 -43.7 0.0 -130.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER -1.705 -12.874 1.107 2 ILE 0.004 -9.752 -0.298 3 SER -3.114 -8.271 -1.869 4 SER -5.274 -9.182 1.145 5 ARG -3.033 -7.138 3.422 6 VAL -2.642 -4.174 1.127 7 LYS -6.397 -3.774 0.668 8 SER -7.564 -4.722 4.161 9 LYS -5.092 -2.536 6.052 10 ARG -6.147 0.401 3.892 11 ILE -9.769 -0.387 4.738 12 GLN -8.735 -0.648 8.410 13 LEU -7.146 2.822 8.254 14 GLY -10.229 4.103 6.360 15 LEU -8.128 5.557 3.530 16 ASN -9.108 4.652 -0.013 17 GLN -6.428 3.685 -2.457 18 ALA -6.516 7.417 -3.407 19 GLU -5.564 9.025 -0.070 20 LEU -3.197 6.137 0.632 21 ALA -1.435 6.780 -2.701 22 GLN -1.175 10.490 -1.881 23 LYS 0.292 9.871 1.611 24 VAL 2.774 7.430 0.033 25 GLY 3.467 10.057 -2.665 26 THR 2.741 7.470 -5.369 27 THR -0.457 7.387 -7.491 28 GLN -3.716 5.452 -7.140 29 GLN -2.894 3.438 -10.279 30 SER 0.291 1.982 -8.749 31 ILE -1.744 1.295 -5.586 32 GLU -4.421 -0.441 -7.774 33 GLN -1.966 -2.878 -9.358 34 LEU -0.275 -3.298 -5.963 35 GLU -3.618 -4.050 -4.256 36 ASN -4.215 -6.684 -6.956 37 GLY -0.738 -7.956 -5.933 38 LYS 1.183 -7.187 -9.144 39 THR 4.199 -5.741 -7.289 40 LYS 6.492 -7.859 -5.012 41 ARG 9.693 -5.783 -4.618 42 PRO 8.318 -2.235 -5.227 43 ARG 10.732 0.685 -4.788 44 PHE 8.108 2.287 -2.492 45 LEU 7.876 -0.719 -0.121 46 PRO 8.942 1.259 3.017 47 GLU 6.710 4.186 1.967 48 LEU 3.691 1.869 1.789 49 ALA 4.924 0.283 5.041 50 SER 5.017 3.678 6.802 51 ALA 1.720 5.006 5.399 52 LEU -0.095 1.790 6.351 53 GLY 1.986 1.545 9.555 54 VAL 3.119 -2.086 9.115 55 SER 6.527 -3.780 8.901 56 VAL 8.373 -4.348 5.638 57 ASP 8.395 -8.000 6.785 58 TRP 4.598 -8.041 7.278 59 LEU 4.124 -6.571 3.784 60 LEU 6.626 -9.054 2.347 61 ASN 5.276 -12.129 4.158 62 GLY 3.144 -11.321 7.227 63 THR 4.808 -10.984 10.649 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 C H H H H H 20 H H H H H C H H H H 30 H H H H H H H S S S 40 S C C H H H H H H H 50 H H H C H H H H H H 60 H/S S 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 t h H H H H 20 H H H H h t h H H H 30 H H H H H H h t S 40 S t T h H H H H H H 50 H H h t h H H H H H 60 h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 16.1 19.2 89.5 2 ILE 114.9 80.1 62.6 3 SER 48.4 57.9 66.3 4 SER 29.5 35.2 80.3 5 ARG 187.8 89.9 51.8 6 VAL 118.8 100.0 44.0 7 LYS 79.9 46.1 75.1 8 SER 25.4 30.4 71.8 9 LYS 114.6 66.1 54.4 10 ARG 205.3 98.3 38.9 11 ILE 35.7 24.9 75.6 12 GLN 38.6 26.0 76.5 13 LEU 108.6 73.5 65.7 14 GLY 4.6 13.1 82.8 15 LEU 119.8 81.1 49.8 16 ASN 27.6 22.8 78.8 17 GLN 116.8 78.6 59.0 18 ALA 36.9 50.8 70.3 19 GLU 67.8 48.9 65.1 20 LEU 147.8 100.0 31.9 21 ALA 69.8 96.1 52.1 22 GLN 16.3 11.0 84.9 23 LYS 64.4 37.2 67.5 24 VAL 115.9 97.5 39.7 25 GLY 6.8 19.6 86.8 26 THR 84.4 78.9 49.1 27 THR 16.3 15.2 78.6 28 GLN 60.4 40.6 64.6 29 GLN 7.1 4.8 85.4 30 SER 51.5 61.6 70.7 31 ILE 143.5 100.0 39.5 32 GLU 50.7 36.6 78.6 33 GLN 77.5 52.1 66.1 34 LEU 146.7 99.3 37.7 35 GLU 127.4 91.9 62.9 36 ASN 39.0 32.2 78.1 37 GLY 32.3 92.7 65.5 38 LYS 33.1 19.1 84.3 39 THR 70.8 66.2 56.7 40 LYS 38.5 22.2 75.3 41 ARG 81.6 39.0 62.9 42 PRO 119.9 96.3 39.2 43 ARG 0.0 0.0 89.6 44 PHE 131.5 78.8 39.6 45 LEU 137.9 93.3 43.0 46 PRO 50.8 40.8 64.4 47 GLU 48.3 34.9 68.8 48 LEU 147.5 99.8 26.6 49 ALA 67.0 92.3 51.7 50 SER 13.7 16.4 83.9 51 ALA 58.0 79.9 55.9 52 LEU 147.8 100.0 35.0 53 GLY 5.2 15.1 78.3 54 VAL 105.3 88.7 46.0 55 SER 39.7 47.5 67.1 56 VAL 55.1 46.3 61.7 57 ASP 27.8 25.2 65.6 58 TRP 157.3 76.7 47.4 59 LEU 147.8 100.0 35.5 60 LEU 70.0 47.3 73.9 61 ASN 23.9 19.8 83.5 62 GLY 21.4 61.5 67.1 63 THR 43.1 40.3 74.4