Protein Data Bank File : 1nkd Title : TRANSCRIPTION REGULATION 23-SEP-97 1NKD Number of Amino Acid Residues : 59 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET THR LYS GLN GLU LYS THR ALA LEU ASN 10 MET ALA ARG PHE ILE ARG SER GLN THR LEU 20 THR LEU LEU GLU LYS LEU ASN GLU LEU ALA 30 ASP ALA ALA ASP GLU GLN ALA ASP ILE CYS 40 GLU SER LEU HIS ASP HIS ALA ASP GLU LEU 50 TYR ARG SER CYS LEU ALA ARG PHE GLY Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 155.6 171.7 90.1 -171.5 53.0 2 THR -73.4 164.9 171.6 72.8 3 LYS -64.3 -37.7 176.1 -55.3 -33.6 -147.3 -68.8 4 GLN -65.5 -38.2 174.6 -70.5 166.4 91.2 5 GLU -63.6 -39.9 178.1 -73.1 165.0 -8.3 6 LYS -63.4 -42.1 177.1 -162.6 157.8 -18.2 -77.8 7 THR -56.9 -46.7 -179.1 -62.5 8 ALA -63.6 -43.3 179.4 9 LEU -62.7 -45.3 178.2 -179.4 62.9 10 ASN -60.5 -41.4 177.9 -67.3 -20.7 11 MET -66.0 -39.7 177.6 -159.6 166.7 -12.2 12 ALA -62.5 -40.3 175.7 13 ARG -60.1 -46.0 -179.7 -171.7 -178.6 -60.7 109.3 14 PHE -60.4 -47.1 -179.9 177.8 67.1 15 ILE -62.9 -40.7 177.0 -69.4 166.1 16 ARG -58.8 -43.8 179.2 -179.0 177.4 82.9 167.4 17 SER -68.0 -40.4 179.2 178.6 18 GLN -64.6 -41.3 178.7 -68.5 -76.1 -73.1 19 THR -64.7 -32.8 174.0 64.7 20 LEU -67.1 -43.7 176.5 -174.5 59.5 21 THR -58.8 -45.7 178.6 -61.2 22 LEU -63.6 -40.8 177.4 179.8 56.0 23 LEU -57.6 -45.2 177.8 -179.8 53.3 24 GLU -58.5 -46.8 -178.5 -67.4 170.3 -6.5 25 LYS -62.5 -42.9 179.6 -70.0 -177.8 175.9 -53.1 26 LEU -67.2 -40.0 176.8 -66.3 168.2 27 ASN -61.3 -39.7 179.3 -76.1 -15.4 28 GLU -64.4 -27.4 175.2 -79.6 149.7 48.7 29 LEU -75.6 -7.4 169.0 -68.9 169.2 30 ALA 58.0 -135.3 -173.9 31 ASP -58.0 -29.5 -177.3 67.4 -67.7 32 ALA -66.3 -13.6 -179.7 33 ALA -139.7 26.8 -171.7 34 ASP -58.2 -52.3 -178.8 57.5 1.7 35 GLU -63.7 -36.8 -179.0 -176.1 179.8 -4.4 36 GLN -67.1 -40.3 175.4 -65.6 67.6 42.0 37 ALA -61.8 -41.8 179.1 38 ASP -64.1 -42.3 175.9 -71.0 -27.1 39 ILE -62.0 -44.2 -176.6 -64.1 165.1 40 CYS -66.7 -31.1 176.4 -163.5 41 GLU -60.1 -46.3 176.5 -158.8 94.2 28.7 42 SER -63.1 -43.9 -179.8 -179.1 43 LEU -58.0 -46.4 178.9 -175.7 67.8 44 HIS -62.3 -43.1 176.2 174.3 65.7 45 ASP -60.3 -38.4 179.2 -71.8 -9.4 46 HIS -69.6 -34.9 174.9 -150.6 -33.6 47 ALA -67.5 -37.8 175.4 48 ASP -63.5 -42.9 178.2 -177.0 61.5 49 GLU -61.1 -43.4 179.1 -178.0 -171.9 23.8 50 LEU -60.9 -48.4 180.0 177.6 60.3 51 TYR -57.6 -47.8 178.8 174.9 66.5 52 ARG -59.9 -41.3 178.6 -66.9 -172.1 -164.8 -165.6 53 SER -63.3 -44.1 173.8 -175.3 54 CYS -61.0 -46.1 -179.2 -68.4 55 LEU -58.2 -41.7 177.8 -176.4 59.8 56 ALA -71.9 -31.4 175.9 57 ARG -80.9 -39.5 -175.2 -165.0 171.0 -168.9 -175.2 58 PHE -87.4 -26.0 -164.1 -53.9 -27.8 59 GLY -98.0 27.7 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 2.572 3.459 2.456 2 THR 4.994 1.843 0.043 3 LYS 7.264 -0.965 1.222 4 GLN 10.254 1.275 0.776 5 GLU 8.574 3.904 2.912 6 LYS 7.841 1.283 5.584 7 THR 11.473 0.249 5.720 8 ALA 12.476 3.848 6.263 9 LEU 9.810 4.460 8.881 10 ASN 10.830 1.303 10.809 11 MET 14.453 2.384 10.707 12 ALA 13.582 5.862 11.972 13 ARG 11.688 4.243 14.903 14 PHE 14.682 2.042 15.656 15 ILE 17.113 4.985 15.599 16 ARG 14.884 6.955 17.944 17 SER 14.910 4.064 20.415 18 GLN 18.670 3.512 20.110 19 THR 19.388 7.170 20.713 20 LEU 17.301 7.058 23.901 21 THR 19.210 4.008 25.113 22 LEU 22.505 5.757 24.427 23 LEU 21.255 8.884 26.175 24 GLU 20.479 6.808 29.272 25 LYS 23.933 5.255 29.199 26 LEU 25.672 8.631 28.820 27 ASN 23.540 10.131 31.608 28 GLU 24.515 7.273 33.878 29 LEU 28.198 8.091 33.379 30 ALA 27.573 11.484 35.002 31 ASP 30.453 13.922 34.908 32 ALA 32.607 11.483 32.867 33 ALA 30.298 11.890 29.871 34 ASP 28.569 15.191 30.584 35 GLU 29.169 17.013 27.269 36 GLN 28.415 13.791 25.387 37 ALA 25.113 13.380 27.199 38 ASP 24.192 16.954 26.319 39 ILE 24.947 16.307 22.629 40 CYS 22.991 13.020 22.805 41 GLU 19.946 14.747 24.344 42 SER 19.780 16.943 21.268 43 LEU 20.448 13.918 19.020 44 HIS 17.510 12.058 20.524 45 ASP 15.199 15.052 20.071 46 HIS 16.308 15.231 16.460 47 ALA 15.659 11.507 15.954 48 ASP 12.191 11.963 17.446 49 GLU 11.525 14.851 15.062 50 LEU 12.608 12.658 12.085 51 TYR 10.396 9.789 13.193 52 ARG 7.386 12.060 13.651 53 SER 7.987 13.602 10.260 54 CYS 8.154 10.249 8.534 55 LEU 5.061 9.031 10.298 56 ALA 3.090 12.076 9.209 57 ARG 4.238 11.924 5.689 58 PHE 4.113 8.265 4.965 59 GLY 1.309 7.334 7.201 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C H H H H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 C C H H H H H H H H 40 H H H H H H H H H H 50 H H H H H H H H H 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 10 H H H H H H H H H H 20 H H H H H H H H h G 30 G G h H H H H H H H 40 H H H H H H H H H H 50 H H H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 127.7 80.1 61.3 2 THR 35.4 33.1 77.0 3 LYS 14.8 8.6 85.2 4 GLN 0.0 0.0 86.6 5 GLU 83.8 60.5 53.5 6 LYS 94.4 54.4 66.5 7 THR 28.0 26.1 74.1 8 ALA 34.4 47.3 61.9 9 LEU 139.9 94.6 43.8 10 ASN 54.1 44.8 72.4 11 MET 59.9 37.6 64.9 12 ALA 67.5 92.9 46.5 13 ARG 107.4 51.4 70.6 14 PHE 47.1 28.3 74.0 15 ILE 64.4 44.8 55.8 16 ARG 135.6 64.9 63.0 17 SER 23.6 28.3 77.0 18 GLN 60.8 40.9 67.3 19 THR 94.1 88.0 46.8 20 LEU 70.6 47.8 69.0 21 THR 50.0 46.8 73.5 22 LEU 66.2 44.8 57.3 23 LEU 140.4 95.0 54.5 24 GLU 51.6 37.2 72.4 25 LYS 53.8 31.1 72.7 26 LEU 119.6 80.9 42.0 27 ASN 53.1 43.9 69.0 28 GLU 27.7 20.0 80.1 29 LEU 51.7 35.0 70.6 30 ALA 13.1 18.1 89.6 31 ASP 6.5 5.9 78.3 32 ALA 15.3 21.1 79.0 33 ALA 67.1 92.5 56.0 34 ASP 27.6 25.0 77.9 35 GLU 31.5 22.7 79.1 36 GLN 62.8 42.3 64.6 37 ALA 63.8 87.9 61.9 38 ASP 17.1 15.4 78.0 39 ILE 34.9 24.3 76.7 40 CYS 94.7 95.4 42.4 41 GLU 58.7 42.3 73.0 42 SER 16.7 19.9 81.7 43 LEU 63.3 42.8 60.7 44 HIS 120.7 80.3 55.3 45 ASP 31.1 28.2 74.3 46 HIS 32.6 21.7 81.6 47 ALA 63.9 88.1 57.4 48 ASP 86.6 78.3 67.3 49 GLU 21.1 15.2 82.1 50 LEU 52.3 35.4 66.4 51 TYR 160.9 88.9 53.6 52 ARG 54.4 26.0 82.3 53 SER 22.5 26.9 74.5 54 CYS 81.3 81.9 43.4 55 LEU 69.8 47.3 66.0 56 ALA 9.7 13.4 83.0 57 ARG 25.0 12.0 84.5 58 PHE 127.2 76.3 49.9 59 GLY 15.2 43.8 56.2