Protein Data Bank File : 1ocp Title : DNA-BINDING PROTEIN 21-FEB-95 1OCP Number of Amino Acid Residues : 67 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET GLU THR LEU VAL GLN ALA ARG LYS ARG 10 LYS ARG THR SER ILE GLU ASN ARG VAL ARG 20 TRP SER LEU GLU THR MET PHE LEU LYS CYS 30 PRO LYS PRO SER LEU GLN GLN ILE THR HIS 40 ILE ALA ASN GLN LEU GLY LEU GLU LYS ASP 50 VAL VAL ARG VAL TRP PHE CYS ASN ARG ARG 60 GLN LYS GLY LYS ARG SER SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 -49.9 -179.9 -101.7 -84.9 160.4 2 GLU -99.3 50.6 179.8 -153.7 161.4 37.7 3 THR -126.2 150.9 -179.8 -179.4 4 LEU -136.0 52.1 179.9 53.9 145.2 5 VAL -149.4 26.7 180.0 -171.7 6 GLN -146.2 52.3 180.0 -75.0 169.6 -117.3 7 ALA -73.8 179.4 -179.8 8 ARG -97.5 -49.9 -179.9 -55.7 -169.2 -176.0 77.4 9 LYS -112.7 -52.3 179.8 -90.4 -76.1 154.7 -174.3 10 ARG -156.8 -70.1 180.0 -139.7 89.3 137.6 64.4 11 LYS -160.4 162.1 179.6 58.3 -168.1 104.6 69.6 12 ARG -138.1 16.3 179.0 52.3 -97.1 164.8 93.9 13 THR -79.3 -28.7 179.3 -42.2 14 SER -154.0 31.6 179.5 41.7 15 ILE -151.0 71.5 178.4 -68.8 -63.2 16 GLU -67.2 155.2 -180.0 -75.3 -92.7 47.7 17 ASN -60.2 -24.1 179.1 -153.8 33.6 18 ARG -80.4 -31.0 179.9 -126.9 72.6 147.9 -87.6 19 VAL -63.9 -45.8 -179.4 97.5 20 ARG -59.6 -46.7 179.6 -76.6 -166.7 146.5 162.2 21 TRP -79.1 -6.3 172.8 -56.5 137.2 22 SER -75.8 -38.6 175.9 -160.0 23 LEU -56.4 -46.2 -178.4 -61.9 152.9 24 GLU -50.5 -53.6 -179.3 -134.0 -173.5 64.0 25 THR -62.2 -28.5 179.7 175.8 26 MET -76.1 -25.4 179.9 -60.0 -63.6 -79.5 27 PHE -91.3 -16.6 -179.2 -76.9 -64.0 28 LEU -91.8 23.1 179.0 -60.5 166.5 29 LYS -99.0 -41.3 178.9 64.3 -166.0 -165.4 -137.6 30 CYS -141.2 145.9 179.6 -83.0 31 PRO -84.5 7.9 -178.0 23.8 -19.1 32 LYS -122.6 64.1 178.6 53.0 174.2 -81.5 -146.9 33 PRO -75.4 125.7 -179.0 21.9 -21.3 34 SER -80.7 153.2 177.3 -88.3 35 LEU -61.8 -22.0 177.7 77.6 168.0 36 GLN -69.7 -40.9 177.3 -109.6 -94.1 -81.7 37 GLN -66.1 -25.4 178.2 -168.2 108.5 47.3 38 ILE -71.0 -30.6 177.9 -75.5 -58.7 39 THR -66.9 -45.3 177.8 -25.0 40 HIS -67.6 -21.1 178.6 -146.3 74.5 41 ILE -70.7 -43.3 179.8 -108.1 107.7 42 ALA -61.9 -52.3 177.5 43 ASN -63.5 -19.3 179.9 -56.7 -38.0 44 GLN -74.5 -31.1 179.1 -100.0 -61.4 -67.3 45 LEU -133.4 24.5 178.2 78.1 164.4 46 GLY 41.4 32.5 179.1 47 LEU -100.3 179.1 178.2 93.8 -174.5 48 GLU -91.4 144.3 -179.7 -154.4 144.6 56.7 49 LYS -55.1 -22.3 -179.4 -64.1 151.7 70.7 176.2 50 ASP -71.7 -39.4 -180.0 -153.5 67.3 51 VAL -80.3 -23.0 179.9 62.6 52 VAL -79.3 -27.1 179.6 94.4 53 ARG -78.4 -46.9 179.2 -157.5 -89.9 -107.5 139.4 54 VAL -66.4 -31.4 179.3 -175.5 55 TRP -72.7 -35.1 178.6 171.3 95.4 56 PHE -83.6 -10.2 178.3 -156.9 51.1 57 CYS -66.9 -43.7 178.2 -146.2 58 ASN -70.8 -40.8 178.7 59.0 71.3 59 ARG -61.5 -20.8 -179.4 -134.3 -70.2 102.2 -176.8 60 ARG -83.8 -36.9 -179.4 -91.3 173.8 81.3 -111.5 61 GLN -115.8 58.5 178.9 53.5 148.8 -132.5 62 LYS -81.6 -31.7 179.8 -60.8 -72.3 -78.7 138.1 63 GLY 172.5 41.4 179.9 64 LYS -90.8 -28.5 179.8 -62.5 -159.0 81.5 84.7 65 ARG -134.9 75.7 -179.8 52.4 -159.1 -75.5 -111.2 66 SER -94.0 133.4 180.0 71.1 67 SER -132.3 -51.8 0.0 -171.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 46.358 -2.594 23.681 2 GLU 49.080 -5.249 24.116 3 THR 48.266 -7.117 20.872 4 LEU 50.182 -7.319 17.560 5 VAL 47.839 -9.127 15.125 6 GLN 45.173 -6.538 14.182 7 ALA 46.898 -3.762 12.195 8 ARG 45.063 -1.611 9.627 9 LYS 47.292 -1.907 6.537 10 ARG 50.414 -3.840 7.606 11 LYS 52.467 -2.473 10.533 12 ARG 53.482 0.807 12.226 13 THR 56.434 -0.260 14.438 14 SER 58.902 0.765 11.702 15 ILE 56.701 1.689 8.716 16 GLU 54.801 4.948 9.257 17 ASN 52.464 5.905 6.397 18 ARG 54.906 8.771 5.737 19 VAL 57.907 6.388 5.597 20 ARG 56.347 4.376 2.746 21 TRP 55.637 7.506 0.701 22 SER 59.089 8.769 1.732 23 LEU 60.388 5.763 -0.280 24 GLU 58.232 7.051 -3.157 25 THR 60.007 10.448 -3.385 26 MET 63.330 8.545 -3.243 27 PHE 62.293 6.321 -6.215 28 LEU 60.891 9.234 -8.297 29 LYS 64.353 10.846 -8.677 30 CYS 65.779 8.388 -11.196 31 PRO 64.152 5.469 -13.071 32 LYS 67.286 3.353 -12.444 33 PRO 67.286 2.384 -8.721 34 SER 69.991 -0.241 -8.100 35 LEU 69.286 -3.268 -5.903 36 GLN 72.169 -1.790 -3.835 37 GLN 70.040 1.333 -3.408 38 ILE 67.252 -1.094 -2.366 39 THR 69.555 -2.227 0.470 40 HIS 69.899 1.420 1.570 41 ILE 66.106 1.633 1.159 42 ALA 65.666 -1.075 3.833 43 ASN 68.066 0.647 6.232 44 GLN 66.177 3.817 5.164 45 LEU 62.863 2.572 6.707 46 GLY 64.003 -0.465 8.809 47 LEU 61.574 -2.731 6.831 48 GLU 62.096 -6.196 5.296 49 LYS 63.139 -6.399 1.609 50 ASP 59.905 -8.398 1.081 51 VAL 57.596 -5.484 2.026 52 VAL 59.829 -3.016 0.140 53 ARG 59.599 -5.099 -3.075 54 VAL 55.795 -5.531 -2.983 55 TRP 55.530 -1.838 -2.045 56 PHE 57.691 -0.840 -5.049 57 CYS 55.709 -3.264 -7.270 58 ASN 52.765 -0.851 -7.144 59 ARG 55.158 2.151 -7.399 60 ARG 56.407 0.473 -10.618 61 GLN 52.958 0.062 -12.223 62 LYS 51.099 3.170 -10.980 63 GLY 50.127 4.197 -14.531 64 LYS 53.030 3.645 -16.966 65 ARG 51.178 1.115 -19.160 66 SER 47.402 1.687 -18.916 67 SER 45.190 -0.029 -21.522 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S C T T T T 10 C T T T T H H H H H 20 H H H H H H H H 3 C 30 S S S S/H H H H H H H 40 H H H H H H C H H H 50 H H H H H H H H H H 60 H H C S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S 10 S S h H H H H 20 H H H H H H H h S 30 S h H H H H H H 40 H H H H H h h H H 50 H H H H H H H H H H 60 h S S S S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 0.0 0.0 94.4 2 GLU 0.0 0.0 89.6 3 THR 49.2 46.1 75.6 4 LEU 3.1 2.1 85.8 5 VAL 7.8 6.6 83.9 6 GLN 22.1 14.9 85.7 7 ALA 55.4 76.3 74.1 8 ARG 27.6 13.2 86.8 9 LYS 9.3 5.4 88.8 10 ARG 84.0 40.2 74.2 11 LYS 107.8 62.2 61.5 12 ARG 85.1 40.8 82.0 13 THR 0.0 0.0 85.8 14 SER 33.2 39.7 73.2 15 ILE 141.7 98.8 49.1 16 GLU 28.7 20.7 79.2 17 ASN 17.0 14.1 80.7 18 ARG 5.9 2.8 87.6 19 VAL 84.3 71.0 51.5 20 ARG 170.0 81.4 42.6 21 TRP 108.1 52.7 74.1 22 SER 30.2 36.1 69.6 23 LEU 142.9 96.7 28.6 24 GLU 99.3 71.7 44.9 25 THR 32.4 30.3 70.1 26 MET 81.3 51.0 70.0 27 PHE 164.7 98.8 27.4 28 LEU 79.5 53.8 76.9 29 LYS 89.4 51.6 69.1 30 CYS 41.4 41.8 59.6 31 PRO 12.3 9.9 75.5 32 LYS 18.9 10.9 76.5 33 PRO 94.5 75.9 56.1 34 SER 25.4 30.4 72.8 35 LEU 7.4 5.0 77.0 36 GLN 20.2 13.6 76.8 37 GLN 79.6 53.6 62.1 38 ILE 105.2 73.3 43.7 39 THR 47.2 44.2 76.8 40 HIS 41.1 27.3 80.2 41 ILE 136.9 95.4 25.8 42 ALA 59.8 82.4 59.6 43 ASN 29.8 24.6 76.6 44 GLN 67.5 45.5 65.8 45 LEU 140.9 95.3 35.6 46 GLY 1.9 5.5 78.0 47 LEU 143.0 96.7 41.9 48 GLU 13.3 9.6 78.4 49 LYS 41.0 23.7 69.3 50 ASP 17.7 16.0 78.5 51 VAL 111.9 94.2 61.2 52 VAL 117.9 99.2 30.0 53 ARG 52.3 25.0 76.4 54 VAL 35.9 30.2 79.5 55 TRP 198.6 96.9 39.7 56 PHE 138.7 83.1 39.3 57 CYS 51.2 51.6 72.7 58 ASN 65.1 53.8 60.3 59 ARG 164.3 78.7 42.0 60 ARG 61.2 29.3 74.6 61 GLN 42.9 28.9 77.6 62 LYS 84.0 48.5 82.5 63 GLY 7.2 20.6 74.6 64 LYS 35.2 20.3 87.6 65 ARG 16.4 7.8 86.0 66 SER 7.6 9.1 84.0 67 SER 0.0 0.0 92.4