Protein Data Bank File : 1enw Title : TRANSCRIPTION 21-MAR-00 1ENW Number of Amino Acid Residues : 114 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY SER HIS MET PRO ARG ASN SER LYS ASN 10 ASP GLY VAL ASP THR ALA ILE TYR HIS HIS 20 LYS LEU ARG ASP GLN VAL LEU LYS ALA LEU 30 TYR ASP VAL LEU ALA LYS GLU SER GLU HIS 40 PRO PRO GLN SER ILE LEU HIS THR ALA LYS 50 ALA ILE GLU SER GLU MET ASN LYS VAL ASN 60 ASN CYS ASP THR ASN GLU ALA ALA TYR LYS 70 ALA ARG TYR ARG ILE ILE TYR SER ASN VAL 80 ILE SER LYS ASN ASN PRO ASP LEU LYS HIS 90 LYS ILE ALA ASN GLY ASP ILE THR PRO GLU 100 PHE LEU ALA THR CYS ASP ALA LYS ASP LEU 110 ALA PRO ALA PRO Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 61.1 -180.0 2 SER -179.5 7.8 180.0 -97.5 3 HIS -133.4 80.3 180.0 -50.5 -114.5 4 MET -98.3 -30.1 -180.0 -51.4 -62.2 -164.3 5 PRO -68.9 -170.7 -180.0 1.1 5.1 6 ARG -89.9 -149.0 -180.0 -63.5 173.3 67.8 151.8 7 ASN -142.3 -18.7 180.0 -98.2 -121.4 8 SER -78.8 31.1 180.0 -149.9 9 LYS -92.4 -19.9 -180.0 -121.6 79.1 -173.2 77.0 10 ASN -71.6 -48.3 -179.9 -27.5 125.7 11 ASP -63.2 -53.8 -180.0 -146.6 -115.4 12 GLY 52.2 60.2 -179.8 13 VAL -96.7 139.3 179.7 58.6 14 ASP -87.9 139.8 -179.6 -176.5 -96.2 15 THR -144.8 89.9 179.9 72.4 16 ALA -136.5 88.5 -179.9 17 ILE -156.3 -92.2 180.0 20.0 -177.5 18 TYR -87.1 -6.4 179.9 -52.6 94.6 19 HIS -39.9 -6.2 -179.8 152.9 -67.8 20 HIS -31.1 -72.9 -179.8 -60.6 -41.5 21 LYS -96.9 -72.9 -179.9 -55.6 160.1 178.2 -162.6 22 LEU -135.8 0.8 179.9 77.0 -175.3 23 ARG -59.5 -16.2 179.7 -109.2 140.4 -85.1 135.5 24 ASP -69.0 -41.2 -180.0 43.9 116.3 25 GLN -65.1 -32.5 179.9 -47.4 -80.5 124.9 26 VAL -73.5 -56.3 179.8 -171.5 27 LEU -63.2 -14.2 -180.0 -89.4 134.3 28 LYS -84.6 -52.4 180.0 -91.3 173.1 149.1 -73.8 29 ALA -66.2 -29.8 -179.9 30 LEU -75.1 -38.4 -179.9 -66.3 165.2 31 TYR -79.2 -54.1 -179.7 178.1 97.8 32 ASP -62.1 -27.2 -179.8 -161.4 -70.1 33 VAL -82.5 -44.0 179.9 -179.6 34 LEU -82.0 -18.1 180.0 -47.6 171.1 35 ALA -79.3 -70.4 -179.9 36 LYS -43.8 -37.1 -179.9 -174.2 151.3 179.0 -7.4 37 GLU -44.9 -70.3 -179.9 -168.5 169.0 -129.4 38 SER -150.5 134.3 -179.9 -46.4 39 GLU -95.9 -10.0 -179.8 -50.2 176.7 -87.1 40 HIS -94.3 -39.1 -180.0 -132.7 -117.2 41 PRO -103.8 27.8 180.0 22.1 -7.7 42 PRO -60.2 133.9 180.0 -0.9 1.1 43 GLN -71.0 -8.5 -179.9 36.2 165.5 95.6 44 SER 116.7 57.1 180.0 67.0 45 ILE -39.7 -53.6 -179.9 -39.5 -39.2 46 LEU -54.3 -54.6 -179.9 -132.3 -61.1 47 HIS -73.4 -10.4 -179.9 -151.8 -113.5 48 THR -90.1 -61.2 -179.9 -70.2 49 ALA -62.4 -22.0 -180.0 50 LYS -78.1 -29.5 -179.7 -83.6 -169.4 66.7 -106.2 51 ALA -94.6 -11.8 -179.9 52 ILE -95.5 -49.6 -180.0 -92.5 71.0 53 GLU -49.5 -8.3 -179.8 66.3 82.7 66.9 54 SER -90.5 -14.5 -179.9 78.2 55 GLU -95.7 -66.1 -180.0 -169.1 178.7 -67.5 56 MET -53.8 -15.9 -179.7 16.0 170.7 -70.0 57 ASN -98.0 -7.4 -179.9 89.6 -51.1 58 LYS -32.4 -72.3 179.4 -158.1 -173.0 175.8 -73.1 59 VAL -161.4 77.7 179.8 62.7 60 ASN -161.4 -10.4 -179.2 -69.6 101.4 61 ASN -52.8 -80.2 -179.5 49.3 -33.9 62 CYS -103.4 -50.0 -179.4 117.5 63 ASP -85.5 52.0 179.8 -163.3 21.1 64 THR -152.9 -75.4 179.9 24.3 65 ASN -148.4 65.0 -180.0 -47.6 114.4 66 GLU -42.7 -24.4 180.0 78.5 -168.2 76.9 67 ALA -73.0 -46.3 180.0 68 ALA -76.1 -46.1 179.9 69 TYR -45.5 -51.3 -179.9 -178.6 57.9 70 LYS -59.5 -63.3 -180.0 166.1 148.5 74.1 -138.0 71 ALA -49.3 -62.8 180.0 72 ARG -41.8 -71.0 -179.8 175.6 -139.9 -154.1 159.6 73 TYR -50.7 -71.4 -179.8 164.4 74.3 74 ARG -43.7 -62.9 -179.7 -166.7 156.3 -171.9 67.4 75 ILE -61.1 -71.3 -179.8 -59.8 -170.8 76 ILE -57.3 -9.5 179.9 -123.6 164.0 77 TYR -37.8 -28.3 180.0 170.1 42.3 78 SER -65.7 -48.2 179.9 -178.0 79 ASN -72.7 -18.2 179.8 -75.4 96.4 80 VAL -70.6 -42.2 179.9 178.5 81 ILE -69.2 -11.9 -179.9 -51.4 145.7 82 SER -95.3 -63.8 -179.9 -53.6 83 LYS -129.9 -87.6 -179.9 -156.6 104.4 170.2 96.3 84 ASN -159.2 -159.2 -179.9 47.9 -118.3 85 ASN -99.5 119.0 179.9 -68.0 127.3 86 PRO -69.8 27.2 -180.0 7.4 -5.6 87 ASP 60.4 65.2 179.9 -102.9 -124.4 88 LEU -33.1 -32.9 -179.8 -154.5 83.1 89 LYS -96.0 -36.3 -179.8 -57.2 -80.8 -63.2 105.1 90 HIS -83.6 -9.3 -180.0 115.1 -37.6 91 LYS -42.6 -55.5 179.9 178.0 142.1 164.3 53.2 92 ILE -57.5 -29.4 -179.9 -62.0 -171.9 93 ALA -62.3 -46.4 180.0 94 ASN -155.4 57.1 -180.0 -75.9 -99.4 95 GLY -95.3 -10.4 -179.9 96 ASP -61.5 -29.4 -179.9 57.0 161.9 97 ILE -108.2 -172.1 -179.9 -57.6 -76.1 98 THR -100.7 7.2 -178.7 64.9 99 PRO 18.7 34.4 179.4 -34.6 15.4 100 GLU -99.5 -25.8 179.9 -112.3 -91.3 19.1 101 PHE -87.1 -69.5 -179.9 -30.8 131.2 102 LEU -53.4 -8.3 180.0 -49.0 161.0 103 ALA -38.8 -40.5 -180.0 104 THR -150.3 -16.5 180.0 -42.6 105 CYS -50.9 -36.1 -180.0 151.7 106 ASP -93.3 -53.4 -180.0 -161.0 36.7 107 ALA -59.9 -10.1 179.9 108 LYS -73.2 -23.7 179.8 159.2 64.5 -171.1 -67.8 109 ASP -58.8 -38.9 179.7 -168.6 166.6 110 LEU -149.4 83.4 179.8 42.4 131.5 111 ALA -80.6 -49.4 -179.9 112 PRO -63.0 -151.5 -179.9 -1.8 4.0 113 ALA -168.8 86.9 180.0 114 PRO -66.1 164.3 0.0 -0.7 4.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 0.595 25.576 -5.928 2 SER 1.014 22.673 -3.508 3 HIS 0.117 19.484 -5.383 4 MET 2.946 18.344 -7.650 5 PRO 3.108 14.638 -6.716 6 ARG 0.607 12.022 -7.858 7 ASN -2.433 10.660 -6.025 8 SER -2.153 6.882 -6.217 9 LYS 0.055 7.023 -3.139 10 ASN -2.757 6.308 -0.698 11 ASP -3.633 2.887 -2.073 12 GLY -0.039 1.725 -2.511 13 VAL -1.097 -1.573 -4.016 14 ASP 1.365 -4.197 -5.066 15 THR 0.725 -5.666 -8.454 16 ALA 2.958 -8.425 -9.754 17 ILE 1.058 -11.321 -11.304 18 TYR -0.873 -11.237 -14.560 19 HIS 0.395 -7.678 -15.082 20 HIS 2.129 -9.179 -18.158 21 LYS 0.371 -7.033 -20.855 22 LEU -2.485 -4.918 -19.453 23 ARG -3.923 -7.258 -16.923 24 ASP -2.098 -4.989 -14.539 25 GLN -4.452 -2.209 -15.413 26 VAL -7.283 -4.546 -14.820 27 LEU -6.138 -5.922 -11.507 28 LYS -5.292 -2.308 -10.696 29 ALA -8.603 -0.654 -11.374 30 LEU -10.341 -3.618 -9.798 31 TYR -8.226 -3.553 -6.710 32 ASP -7.712 0.171 -6.169 33 VAL -11.374 0.897 -6.775 34 LEU -12.858 -1.768 -4.554 35 ALA -10.053 -1.441 -2.027 36 LYS -9.866 2.254 -1.187 37 GLU -13.643 2.177 -1.039 38 SER -13.901 0.202 2.178 39 GLU -11.549 -2.166 3.966 40 HIS -14.137 -3.594 6.398 41 PRO -16.943 -4.552 3.998 42 PRO -14.876 -5.671 0.907 43 GLN -16.784 -8.201 -1.189 44 SER -13.355 -9.941 -1.667 45 ILE -11.338 -7.711 -3.924 46 LEU -8.694 -10.352 -4.227 47 HIS -11.209 -13.065 -5.041 48 THR -13.203 -10.610 -7.115 49 ALA -10.711 -9.070 -9.476 50 LYS -9.064 -12.495 -9.783 51 ALA -12.202 -14.226 -11.062 52 ILE -13.385 -11.361 -13.292 53 GLU -10.236 -10.288 -15.120 54 SER -10.436 -13.744 -16.756 55 GLU -13.661 -13.087 -18.720 56 MET -13.590 -9.599 -20.180 57 ASN -10.012 -10.484 -21.110 58 LYS -10.774 -13.791 -22.955 59 VAL -10.007 -12.245 -26.300 60 ASN -11.042 -8.652 -26.721 61 ASN -8.433 -6.894 -24.677 62 CYS -5.761 -5.560 -27.051 63 ASP -5.880 -7.364 -30.417 64 THR -9.543 -6.754 -30.896 65 ASN -10.984 -3.448 -29.904 66 GLU -8.622 -1.718 -27.508 67 ALA -11.190 0.966 -27.865 68 ALA -14.015 -1.198 -26.656 69 TYR -11.978 -3.226 -24.167 70 LYS -11.225 -0.007 -22.306 71 ALA -14.705 1.474 -22.431 72 ARG -16.435 -1.819 -21.721 73 TYR -14.295 -2.753 -18.770 74 ARG -13.704 0.729 -17.357 75 ILE -17.258 2.035 -17.887 76 ILE -19.338 -1.076 -17.379 77 TYR -16.884 -1.953 -14.571 78 SER -19.890 -1.231 -12.383 79 ASN -21.924 -4.048 -13.851 80 VAL -18.796 -6.171 -13.826 81 ILE -18.584 -6.120 -10.069 82 SER -22.208 -7.162 -10.172 83 LYS -22.562 -9.896 -12.819 84 ASN -20.676 -9.886 -16.147 85 ASN -20.352 -8.356 -19.628 86 PRO -23.552 -8.254 -21.731 87 ASP -21.239 -8.658 -24.683 88 LEU -20.712 -4.954 -25.370 89 LYS -20.442 -5.957 -29.055 90 HIS -22.982 -8.795 -29.351 91 LYS -25.577 -6.853 -27.369 92 ILE -27.199 -5.679 -30.579 93 ALA -27.055 -9.277 -31.726 94 ASN -29.382 -10.464 -28.963 95 GLY -29.802 -7.850 -26.228 96 ASP -33.581 -7.728 -26.586 97 ILE -33.808 -10.760 -24.293 98 THR -32.070 -11.951 -21.100 99 PRO -29.859 -14.892 -22.500 100 GLU -30.114 -16.144 -18.961 101 PHE -32.350 -18.946 -20.093 102 LEU -30.986 -20.063 -23.426 103 ALA -27.638 -19.868 -21.623 104 THR -27.676 -23.655 -21.749 105 CYS -31.334 -24.623 -21.999 106 ASP -30.896 -24.875 -25.767 107 ALA -27.241 -25.716 -26.217 108 LYS -27.938 -28.466 -23.726 109 ASP -29.686 -30.392 -26.450 110 LEU -26.299 -30.791 -27.936 111 ALA -23.520 -29.289 -25.875 112 PRO -20.669 -31.609 -26.905 113 ALA -19.719 -32.182 -30.539 114 PRO -19.506 -35.679 -32.045 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C S S S S S/T T T 10 T S S S S S S C C C 20 C H H H H H H H H H 30 H H H H H H H H/T T T 40 T C C H H H H H H H 50 H H H H/T T T T/T T T T/T 60 T T T C H H H H H H 70 H H H H H H/H H H H H 80 H H H C C C T T T T/T 90 T T T C C S S S S/T T 100 T T C H H H H H H 3 110 S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S t T T T 10 T t S t T T 20 T h H H H H H H H H 30 H H H H H H H h S S 40 S S h H H H H H H 50 H H h T T T T t S t 60 T T T T h H H H H H 70 H H H H H H H H H H 80 h T t t T T h 90 H H H H h S S S 100 h H H H H h T T T T 110 t S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 80.7 2 SER 17.9 21.4 79.1 3 HIS 18.8 12.5 79.4 4 MET 20.9 13.1 79.5 5 PRO 30.2 24.3 75.4 6 ARG 28.2 13.5 80.9 7 ASN 5.0 4.1 85.4 8 SER 29.9 35.8 82.4 9 LYS 32.6 18.8 82.4 10 ASN 35.9 29.7 75.1 11 ASP 98.0 88.7 54.8 12 GLY 1.0 2.9 84.1 13 VAL 104.0 87.5 60.8 14 ASP 4.7 4.3 79.8 15 THR 91.7 85.8 49.2 16 ALA 12.9 17.8 78.3 17 ILE 67.1 46.7 59.2 18 TYR 93.7 51.8 53.5 19 HIS 61.9 41.2 74.4 20 HIS 40.5 27.0 81.4 21 LYS 45.6 26.3 80.8 22 LEU 115.1 77.9 53.3 23 ARG 171.9 82.3 51.8 24 ASP 98.4 89.1 52.9 25 GLN 42.5 28.6 71.7 26 VAL 117.1 98.6 38.8 27 LEU 134.6 91.1 39.1 28 LYS 92.5 53.3 69.1 29 ALA 51.9 71.5 62.9 30 LEU 147.0 99.4 36.1 31 TYR 115.8 64.0 52.5 32 ASP 74.5 67.4 59.9 33 VAL 50.4 42.5 66.4 34 LEU 138.9 94.0 42.9 35 ALA 57.2 78.8 60.2 36 LYS 55.5 32.0 84.7 37 GLU 31.6 22.8 82.6 38 SER 48.3 57.8 61.6 39 GLU 6.1 4.4 82.5 40 HIS 0.0 0.0 81.4 41 PRO 47.5 38.2 70.6 42 PRO 88.1 70.8 65.3 43 GLN 74.1 49.9 63.9 44 SER 37.5 44.8 71.2 45 ILE 129.2 90.0 43.5 46 LEU 38.5 26.1 67.3 47 HIS 22.3 14.9 79.1 48 THR 94.8 88.7 53.8 49 ALA 70.4 96.9 44.3 50 LYS 98.0 56.5 58.4 51 ALA 23.7 32.6 77.5 52 ILE 108.4 75.5 47.5 53 GLU 126.2 91.1 38.0 54 SER 33.8 40.4 81.7 55 GLU 54.7 39.5 77.9 56 MET 158.6 99.5 42.4 57 ASN 96.4 79.7 66.4 58 LYS 27.6 15.9 85.1 59 VAL 34.2 28.8 79.2 60 ASN 70.4 58.3 71.0 61 ASN 98.6 81.6 48.0 62 CYS 30.4 30.6 68.5 63 ASP 0.0 0.0 82.6 64 THR 77.2 72.2 74.8 65 ASN 64.7 53.5 65.6 66 GLU 18.2 13.2 82.0 67 ALA 5.9 8.2 72.4 68 ALA 53.3 73.4 49.6 69 TYR 167.0 92.2 39.2 70 LYS 41.1 23.7 73.6 71 ALA 39.5 54.3 54.7 72 ARG 183.4 87.8 45.6 73 TYR 165.6 91.5 34.3 74 ARG 59.0 28.2 66.5 75 ILE 23.4 16.3 72.9 76 ILE 117.4 81.8 47.3 77 TYR 161.6 89.3 38.4 78 SER 13.0 15.5 77.7 79 ASN 36.9 30.5 71.6 80 VAL 116.3 97.9 43.0 81 ILE 113.7 79.3 53.5 82 SER 26.4 31.6 79.9 83 LYS 37.5 21.6 90.4 84 ASN 57.9 47.9 72.0 85 ASN 118.7 98.2 46.4 86 PRO 62.7 50.4 64.2 87 ASP 45.2 40.9 71.5 88 LEU 95.9 64.9 49.6 89 LYS 57.4 33.1 80.7 90 HIS 82.1 54.6 66.7 91 LYS 69.3 39.9 70.6 92 ILE 0.0 0.0 87.3 93 ALA 28.0 38.5 69.8 94 ASN 37.1 30.7 78.2 95 GLY 24.2 69.6 75.4 96 ASP 19.1 17.3 73.9 97 ILE 62.5 43.6 67.0 98 THR 36.1 33.8 55.5 99 PRO 83.8 67.3 64.6 100 GLU 44.8 32.3 68.9 101 PHE 54.0 32.3 64.7 102 LEU 55.8 37.7 59.7 103 ALA 26.4 36.3 84.7 104 THR 29.2 27.3 71.3 105 CYS 22.0 22.2 70.7 106 ASP 21.3 19.2 75.5 107 ALA 20.4 28.2 74.6 108 LYS 36.3 20.9 76.8 109 ASP 19.3 17.5 77.6 110 LEU 25.7 17.4 83.2 111 ALA 30.6 42.2 66.3 112 PRO 23.5 18.9 71.8 113 ALA 9.0 12.4 73.5 114 PRO 8.5 6.8 85.2