Protein Data Bank File : 1pfsa Title : DNA-BINDING PROTEIN 03-AUG-96 1PFS Number of Amino Acid Residues : 78 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ASN ILE GLN ILE THR PHE THR ASP SER 10 VAL ARG GLN GLY THR SER ALA LYS GLY ASN 20 PRO TYR THR PHE GLN GLU GLY PHE LEU HIS 30 LEU GLU ASP LYS PRO HIS PRO LEU GLN CYS 40 GLN PHE PHE VAL GLU SER VAL ILE PRO ALA 50 GLY SER TYR GLN VAL PRO TYR ARG ILE ASN 60 VAL ASN ASN GLY ARG PRO GLU LEU ALA PHE 70 ASP PHE LYS ALA MET LYS ARG ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 123.7 179.7 -54.0 -164.4 -76.4 2 ASN -144.4 165.5 179.8 77.2 115.1 3 ILE -150.8 145.6 -179.8 -172.5 174.3 4 GLN -77.6 126.0 179.9 -169.4 168.0 -111.2 5 ILE -130.1 116.9 179.3 -63.9 178.6 6 THR -92.2 104.5 -178.9 -54.1 7 PHE -80.3 160.9 179.3 -73.4 -60.0 8 THR -129.8 -179.3 -179.7 64.6 9 ASP -97.4 23.7 179.5 87.8 -82.8 10 SER -100.9 101.2 -179.7 -113.5 11 VAL -120.5 119.8 179.5 -157.3 12 ARG -89.3 114.0 -180.0 -161.6 114.9 -31.3 146.5 13 GLN -113.2 145.9 179.9 -50.4 155.7 -39.5 14 GLY 172.1 -178.4 179.9 15 THR -107.1 145.6 179.9 7.0 16 SER -87.2 172.0 179.9 25.1 17 ALA -57.9 -24.8 -179.9 18 LYS -87.3 8.0 179.8 -56.1 -63.6 -133.0 74.9 19 GLY 76.6 2.6 -179.9 20 ASN -82.5 143.9 180.0 -69.1 66.2 21 PRO -83.3 140.6 179.8 25.0 -19.4 22 TYR -136.3 148.1 179.9 65.4 79.1 23 THR -127.8 99.0 179.4 -50.8 24 PHE -98.9 126.6 180.0 -81.0 -63.9 25 GLN -114.1 143.9 -179.9 -179.6 165.6 -2.9 26 GLU -81.8 155.2 179.6 179.3 164.4 -76.3 27 GLY -173.7 145.8 179.8 28 PHE -96.7 137.7 -178.8 -84.5 -80.9 29 LEU -104.3 142.8 179.9 -131.8 94.4 30 HIS -117.2 118.0 -179.5 -68.5 -99.7 31 LEU -113.5 138.9 -179.6 -104.8 69.9 32 GLU -62.1 -24.5 -178.9 -64.9 122.8 83.0 33 ASP -98.3 11.1 179.7 67.5 -53.3 34 LYS -131.4 131.5 -179.6 -54.2 -96.4 -170.7 -119.6 35 PRO -73.5 -35.0 179.8 24.7 -27.3 36 HIS -112.1 151.8 180.0 -62.9 -70.5 37 PRO -78.3 151.5 -179.2 25.3 -23.9 38 LEU -107.1 139.0 178.9 -57.0 161.1 39 GLN -78.1 120.1 -178.9 170.0 -170.0 3.1 40 CYS -134.7 157.7 179.5 -34.2 41 GLN -115.1 146.4 -178.3 -71.9 178.7 132.6 42 PHE -124.3 145.6 178.8 -58.2 78.8 43 PHE -90.9 75.8 -178.4 -171.4 -87.9 44 VAL -82.6 161.6 178.4 -56.0 45 GLU -96.5 -36.3 179.3 -30.2 177.1 -51.4 46 SER -126.4 146.7 -179.5 -21.8 47 VAL -66.9 127.8 179.6 178.7 48 ILE -98.3 134.1 179.7 -61.0 169.9 49 PRO -66.6 131.5 -179.5 23.9 -31.7 50 ALA -49.5 128.4 -179.9 51 GLY 162.6 158.5 -179.9 52 SER -81.5 129.9 -179.6 27.8 53 TYR -129.1 155.0 176.5 -75.9 81.3 54 GLN -107.2 87.8 -175.8 -64.7 -162.6 -138.0 55 VAL -84.1 127.2 176.5 -169.9 56 PRO -80.1 112.0 -178.6 24.0 -21.2 57 TYR -110.9 165.3 179.0 69.3 87.3 58 ARG -142.3 163.0 -179.9 -27.3 170.7 162.1 175.9 59 ILE -100.9 102.3 179.9 -61.0 164.4 60 ASN -95.7 156.0 179.8 -127.5 -133.5 61 VAL -116.2 112.7 179.9 171.4 62 ASN -113.0 133.7 179.7 -163.6 50.0 63 ASN 49.1 24.4 178.1 106.0 114.8 64 GLY 88.1 17.1 179.4 65 ARG -123.8 130.3 -179.6 -97.4 169.1 47.4 150.4 66 PRO -72.0 120.9 179.8 24.6 -28.7 67 GLU -134.5 163.6 -179.2 -54.2 -155.5 -13.0 68 LEU -88.6 138.5 178.3 -66.0 174.5 69 ALA -122.4 107.4 -178.4 70 PHE -88.8 128.3 -180.0 -60.8 -85.1 71 ASP -94.2 89.0 -179.6 178.9 -51.1 72 PHE -69.8 -9.9 -179.7 -66.5 -50.5 73 LYS -80.0 -20.8 -178.2 -74.7 48.0 156.9 67.5 74 ALA -120.1 14.0 179.7 75 MET -72.8 143.1 -179.0 61.2 161.9 166.1 76 LYS -110.0 128.3 179.2 -94.9 174.0 169.9 68.8 77 ARG -62.7 129.0 -179.5 -120.7 -147.8 132.1 -163.1 78 ALA -95.6 -46.8 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 4.324 19.646 0.505 2 ASN 5.338 18.632 4.024 3 ILE 3.790 17.207 7.198 4 GLN 4.672 17.083 10.894 5 ILE 5.731 13.615 12.047 6 THR 6.605 12.870 15.675 7 PHE 8.979 9.901 15.655 8 THR 9.569 7.580 18.582 9 ASP 12.208 5.112 19.739 10 SER 10.003 2.158 18.771 11 VAL 11.587 0.364 15.832 12 ARG 10.345 -3.032 14.677 13 GLN 13.158 -5.053 13.108 14 GLY 12.884 -8.515 11.551 15 THR 12.912 -10.688 8.431 16 SER 10.087 -10.995 5.907 17 ALA 8.581 -14.202 4.533 18 LYS 11.000 -13.746 1.616 19 GLY 13.933 -13.825 4.056 20 ASN 14.504 -10.112 3.372 21 PRO 15.390 -7.762 6.277 22 TYR 13.106 -4.856 7.166 23 THR 13.316 -1.929 9.571 24 PHE 9.991 -0.451 10.610 25 GLN 10.094 2.587 12.880 26 GLU 7.202 4.063 14.851 27 GLY 6.052 7.642 14.458 28 PHE 3.005 9.838 15.049 29 LEU 1.338 11.654 12.148 30 HIS -0.277 15.092 12.321 31 LEU -3.145 15.902 9.957 32 GLU -4.785 19.311 9.499 33 ASP -8.134 17.521 9.394 34 LYS -7.461 15.564 12.598 35 PRO -7.401 16.948 16.190 36 HIS -5.259 14.097 17.511 37 PRO -2.130 12.512 15.959 38 LEU -2.174 8.980 14.531 39 GLN 0.328 6.239 15.360 40 CYS 2.018 5.091 12.150 41 GLN 5.029 2.979 11.183 42 PHE 7.626 3.788 8.535 43 PHE 9.949 1.617 6.444 44 VAL 13.134 3.546 7.183 45 GLU 16.667 2.624 6.130 46 SER 18.325 4.236 9.140 47 VAL 16.979 4.755 12.664 48 ILE 15.631 8.283 13.156 49 PRO 15.974 9.981 16.593 50 ALA 12.663 10.486 18.398 51 GLY 11.364 14.012 17.782 52 SER 8.870 16.047 15.742 53 TYR 9.927 16.749 12.158 54 GLN 8.492 18.611 9.176 55 VAL 9.064 16.051 6.451 56 PRO 8.759 17.063 2.750 57 TYR 6.745 14.339 1.028 58 ARG 5.659 13.641 -2.537 59 ILE 3.157 11.333 -4.235 60 ASN 5.011 8.547 -6.050 61 VAL 3.427 5.867 -8.207 62 ASN 4.643 2.304 -7.678 63 ASN 3.401 -0.678 -9.692 64 GLY 0.581 1.651 -10.827 65 ARG -0.517 2.631 -7.312 66 PRO -0.235 6.181 -5.845 67 GLU 1.867 6.183 -2.656 68 LEU 3.616 8.700 -0.407 69 ALA 7.373 9.244 -0.602 70 PHE 8.864 10.966 2.439 71 ASP 12.131 12.836 1.955 72 PHE 13.960 12.298 5.253 73 LYS 16.955 14.069 3.698 74 ALA 15.137 17.419 3.731 75 MET 13.017 17.039 6.867 76 LYS 13.198 19.891 9.345 77 ARG 13.187 19.278 13.101 78 ALA 10.082 20.859 14.617 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S S/S S 10 S S S S S S/T T T T/S S 20 S S S S S S S S/S S S 30 S/T T T T S S S S S S 40 S S S C S S S S S S 50 S S S S/S S S S S S S 60 S/T T T T/S S S S S/S S S 70 S/T T T T/S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E E E E E E 10 E E E E E e T T t e 20 E E E E E E E E E e 30 t T T t S S E E E 40 E E E e S S S 50 E E E E E E E E E E 60 E E T T E E E E E E 70 e T T t E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 58.4 36.6 76.7 2 ASN 61.5 50.9 67.9 3 ILE 118.6 82.7 50.5 4 GLN 83.4 56.1 56.7 5 ILE 143.5 100.0 29.4 6 THR 65.3 61.1 63.9 7 PHE 166.8 100.0 35.0 8 THR 77.1 72.1 57.7 9 ASP 0.0 0.0 81.2 10 SER 34.1 40.8 77.9 11 VAL 107.1 90.2 53.4 12 ARG 63.8 30.5 82.4 13 GLN 49.3 33.1 71.7 14 GLY 10.2 29.4 72.6 15 THR 37.5 35.1 70.9 16 SER 46.0 55.0 62.7 17 ALA 0.0 0.0 81.1 18 LYS 18.0 10.4 86.2 19 GLY 3.6 10.3 77.3 20 ASN 32.7 27.0 73.1 21 PRO 30.1 24.2 78.7 22 TYR 127.8 70.6 58.1 23 THR 73.9 69.1 57.4 24 PHE 97.9 58.7 55.9 25 GLN 148.5 100.0 46.1 26 GLU 114.5 82.6 57.9 27 GLY 34.8 100.0 45.5 28 PHE 101.4 60.8 61.3 29 LEU 119.5 80.8 34.7 30 HIS 97.0 64.6 64.3 31 LEU 99.2 67.1 57.4 32 GLU 0.0 0.0 88.0 33 ASP 32.7 29.6 70.8 34 LYS 90.6 52.3 67.2 35 PRO 25.1 20.2 78.5 36 HIS 16.2 10.8 75.6 37 PRO 80.6 64.8 62.4 38 LEU 64.9 43.9 61.9 39 GLN 59.5 40.1 68.4 40 CYS 64.4 64.9 56.7 41 GLN 81.4 54.8 66.5 42 PHE 149.2 89.5 37.5 43 PHE 62.6 37.5 68.9 44 VAL 116.0 97.7 43.6 45 GLU 15.3 11.0 86.6 46 SER 9.0 10.7 82.5 47 VAL 50.1 42.2 68.4 48 ILE 131.5 91.7 36.2 49 PRO 33.1 26.6 82.4 50 ALA 39.0 53.7 71.1 51 GLY 22.0 63.2 71.1 52 SER 55.3 66.2 64.8 53 TYR 160.6 88.7 44.8 54 GLN 68.1 45.8 70.1 55 VAL 118.8 100.0 33.2 56 PRO 90.5 72.7 60.0 57 TYR 135.0 74.6 46.8 58 ARG 58.5 28.0 77.6 59 ILE 62.7 43.7 59.5 60 ASN 30.7 25.4 73.1 61 VAL 46.2 38.9 73.6 62 ASN 22.0 18.2 81.6 63 ASN 27.1 22.5 80.3 64 GLY 4.0 11.6 71.5 65 ARG 54.3 26.0 83.9 66 PRO 44.2 35.5 65.2 67 GLU 60.8 43.9 79.0 68 LEU 71.2 48.2 55.5 69 ALA 36.4 50.2 65.5 70 PHE 139.2 83.5 35.8 71 ASP 79.3 71.8 61.6 72 PHE 128.4 77.0 36.0 73 LYS 29.2 16.8 87.6 74 ALA 25.0 34.4 74.3 75 MET 136.2 85.4 42.2 76 LYS 20.4 11.7 86.6 77 ARG 64.1 30.7 79.0 78 ALA 59.5 81.9 73.7