Protein Data Bank File : 1qcrf Title : OXIDOREDUCTASE 17-MAY-97 1QCR Number of Amino Acid Residues : 103 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA SER SER ARG TRP LEU GLU GLY ILE ARG 10 LYS TRP TYR TYR ASN ALA ALA GLY PHE ASN 20 LYS LEU GLY LEU MET ARG ASP ASP THR ILE 30 HIS GLU ASN ASP ASP VAL LYS GLU ALA ILE 40 ARG ARG LEU PRO GLU ASN LEU TYR ASP ASP 50 ARG VAL PHE ARG ILE LYS ARG ALA LEU ASP 60 LEU SER MET ARG GLN GLN ILE LEU PRO LYS 70 GLU GLN TRP THR LYS TYR GLU GLU ASP LYS 80 SER TYR LEU GLU PRO TYR LEU LYS GLU VAL 90 ILE ARG GLU ARG LYS GLU ARG GLU GLU TRP 100 ALA LYS LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 0.0 0.0 2 SER 0.0 0.0 0.0 0.0 3 SER 0.0 0.0 0.0 0.0 4 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 5 TRP 0.0 0.0 0.0 0.0 0.0 6 LEU 0.0 0.0 0.0 0.0 0.0 7 GLU 0.0 0.0 0.0 0.0 0.0 0.0 8 GLY 0.0 0.0 0.0 9 ILE 0.0 0.0 0.0 0.0 0.0 10 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 11 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 12 TRP 0.0 0.0 0.0 0.0 0.0 13 TYR 0.0 0.0 0.0 0.0 0.0 14 TYR 0.0 0.0 0.0 0.0 0.0 15 ASN 0.0 0.0 0.0 0.0 0.0 16 ALA 0.0 0.0 0.0 17 ALA 0.0 0.0 0.0 18 GLY 0.0 0.0 0.0 19 PHE 0.0 0.0 0.0 0.0 0.0 20 ASN 0.0 0.0 0.0 0.0 0.0 21 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 22 LEU 0.0 0.0 0.0 0.0 0.0 23 GLY 0.0 0.0 0.0 24 LEU 0.0 0.0 0.0 0.0 0.0 25 MET 0.0 0.0 0.0 0.0 0.0 0.0 26 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 27 ASP 0.0 0.0 0.0 0.0 0.0 28 ASP 0.0 0.0 0.0 0.0 0.0 29 THR 0.0 0.0 0.0 0.0 30 ILE 0.0 0.0 0.0 0.0 0.0 31 HIS 0.0 0.0 0.0 0.0 0.0 32 GLU 0.0 0.0 0.0 0.0 0.0 0.0 33 ASN 0.0 0.0 0.0 0.0 0.0 34 ASP 0.0 0.0 0.0 0.0 0.0 35 ASP 0.0 0.0 0.0 0.0 0.0 36 VAL 0.0 0.0 0.0 0.0 37 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 38 GLU 0.0 0.0 0.0 0.0 0.0 0.0 39 ALA 0.0 0.0 0.0 40 ILE 0.0 0.0 0.0 0.0 0.0 41 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 42 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 43 LEU 0.0 0.0 0.0 0.0 0.0 44 PRO 0.0 0.0 0.0 0.0 0.0 45 GLU 0.0 0.0 0.0 0.0 0.0 0.0 46 ASN 0.0 0.0 0.0 0.0 0.0 47 LEU 0.0 0.0 0.0 0.0 0.0 48 TYR 0.0 0.0 0.0 0.0 0.0 49 ASP 0.0 0.0 0.0 0.0 0.0 50 ASP 0.0 0.0 0.0 0.0 0.0 51 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 52 VAL 0.0 0.0 0.0 0.0 53 PHE 0.0 0.0 0.0 0.0 0.0 54 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 55 ILE 0.0 0.0 0.0 0.0 0.0 56 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 57 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 58 ALA 0.0 0.0 0.0 59 LEU 0.0 0.0 0.0 0.0 0.0 60 ASP 0.0 0.0 0.0 0.0 0.0 61 LEU 0.0 0.0 0.0 0.0 0.0 62 SER 0.0 0.0 0.0 0.0 63 MET 0.0 0.0 0.0 0.0 0.0 0.0 64 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 65 GLN 0.0 0.0 0.0 0.0 0.0 0.0 66 GLN 0.0 0.0 0.0 0.0 0.0 0.0 67 ILE 0.0 0.0 0.0 0.0 0.0 68 LEU 0.0 0.0 0.0 0.0 0.0 69 PRO 0.0 0.0 0.0 0.0 0.0 70 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 71 GLU 0.0 0.0 0.0 0.0 0.0 0.0 72 GLN 0.0 0.0 0.0 0.0 0.0 0.0 73 TRP 0.0 0.0 0.0 0.0 0.0 74 THR 0.0 0.0 0.0 0.0 75 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 76 TYR 0.0 0.0 0.0 0.0 0.0 77 GLU 0.0 0.0 0.0 0.0 0.0 0.0 78 GLU 0.0 0.0 0.0 0.0 0.0 0.0 79 ASP 0.0 0.0 0.0 0.0 0.0 80 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 81 SER 0.0 0.0 0.0 0.0 82 TYR 0.0 0.0 0.0 0.0 0.0 83 LEU 0.0 0.0 0.0 0.0 0.0 84 GLU 0.0 0.0 0.0 0.0 0.0 0.0 85 PRO 0.0 0.0 0.0 0.0 0.0 86 TYR 0.0 0.0 0.0 0.0 0.0 87 LEU 0.0 0.0 0.0 0.0 0.0 88 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 89 GLU 0.0 0.0 0.0 0.0 0.0 0.0 90 VAL 0.0 0.0 0.0 0.0 91 ILE 0.0 0.0 0.0 0.0 0.0 92 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 93 GLU 0.0 0.0 0.0 0.0 0.0 0.0 94 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 95 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 96 GLU 0.0 0.0 0.0 0.0 0.0 0.0 97 ARG 0.0 0.0 0.0 0.0 0.0 0.0 0.0 98 GLU 0.0 0.0 0.0 0.0 0.0 0.0 99 GLU 0.0 0.0 0.0 0.0 0.0 0.0 100 TRP 0.0 0.0 0.0 0.0 0.0 101 ALA 0.0 0.0 0.0 102 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 103 LYS 0.0 0.0 0.0 0.0 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 51.197 21.183 122.282 2 SER 49.640 22.529 125.517 3 SER 52.580 24.892 125.997 4 ARG 49.588 26.917 124.985 5 TRP 49.376 27.024 128.756 6 LEU 52.905 28.434 128.902 7 GLU 51.562 31.172 126.608 8 GLY 49.021 31.183 129.390 9 ILE 51.291 32.539 132.060 10 ARG 52.510 35.126 129.579 11 LYS 49.348 36.637 128.074 12 TRP 48.214 36.791 131.688 13 TYR 51.348 38.566 132.854 14 TYR 50.998 40.921 129.862 15 ASN 47.521 42.102 130.844 16 ALA 49.084 42.035 134.300 17 ALA 52.175 43.984 133.316 18 GLY 49.950 46.976 132.531 19 PHE 51.112 48.452 129.141 20 ASN 47.911 47.731 127.291 21 LYS 45.527 50.030 129.138 22 LEU 48.076 52.726 128.235 23 GLY 47.802 52.204 124.471 24 LEU 51.398 51.063 124.731 25 MET 53.345 48.262 123.134 26 ARG 56.110 46.140 124.536 27 ASP 59.175 47.874 123.149 28 ASP 58.009 51.379 124.046 29 THR 58.997 50.288 127.527 30 ILE 62.649 49.292 127.485 31 HIS 65.530 50.782 129.567 32 GLU 67.034 53.144 127.060 33 ASN 70.612 52.274 127.835 34 ASP 72.805 53.238 124.858 35 ASP 72.504 49.898 123.097 36 VAL 68.802 50.720 123.075 37 LYS 69.430 54.274 122.155 38 GLU 70.819 53.540 118.708 39 ALA 67.926 51.181 118.093 40 ILE 65.446 53.915 118.504 41 ARG 68.090 55.610 116.412 42 ARG 68.181 53.196 113.539 43 LEU 64.408 53.128 113.472 44 PRO 62.823 53.873 110.056 45 GLU 60.801 57.029 109.787 46 ASN 57.252 55.729 110.353 47 LEU 58.233 53.478 113.312 48 TYR 59.874 56.329 115.272 49 ASP 57.020 58.537 114.222 50 ASP 54.691 56.005 115.814 51 ARG 56.643 54.943 118.939 52 VAL 56.846 58.623 119.711 53 PHE 53.195 59.058 119.466 54 ARG 52.243 56.196 121.663 55 ILE 54.845 56.729 124.342 56 LYS 53.552 60.238 124.214 57 ARG 50.023 59.060 124.981 58 ALA 51.126 56.787 127.784 59 LEU 52.314 59.920 129.465 60 ASP 49.209 61.911 128.695 61 LEU 47.337 59.198 130.419 62 SER 49.712 58.766 133.396 63 MET 49.332 62.483 133.804 64 ARG 45.615 62.279 134.284 65 GLN 45.685 58.865 135.908 66 GLN 43.404 57.173 133.395 67 ILE 43.697 54.355 130.884 68 LEU 42.237 54.239 127.456 69 PRO 38.971 52.259 127.258 70 LYS 39.306 48.575 126.594 71 GLU 39.118 47.649 122.894 72 GLN 41.914 50.143 122.589 73 TRP 44.442 48.319 124.736 74 THR 47.420 46.839 122.903 75 LYS 46.251 43.301 122.430 76 TYR 48.806 40.685 123.467 77 GLU 50.772 39.022 120.691 78 GLU 49.358 41.423 118.098 79 ASP 52.085 43.371 119.840 80 LYS 54.833 43.889 117.310 81 SER 58.464 43.857 118.452 82 TYR 59.617 46.426 115.858 83 LEU 62.564 47.309 118.103 84 GLU 63.834 43.754 118.543 85 PRO 65.719 43.349 115.289 86 TYR 67.820 46.512 115.479 87 LEU 68.370 46.144 119.152 88 LYS 69.729 42.694 118.408 89 GLU 71.920 43.896 115.639 90 VAL 73.086 46.896 117.783 91 ILE 74.191 44.447 120.335 92 ARG 75.859 42.206 117.866 93 GLU 78.106 44.903 116.427 94 ARG 78.979 45.946 119.950 95 LYS 79.864 42.437 121.117 96 GLU 81.957 42.121 118.007 97 ARG 83.837 45.113 119.156 98 GLU 84.246 43.935 122.757 99 GLU 85.651 40.883 121.032 100 TRP 88.643 42.631 119.413 101 ALA 89.282 44.615 122.553 102 LYS 90.501 41.230 123.774 103 LYS 93.150 39.842 121.453 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 10 20 30 40 50 60 70 80 90 100 Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 10 20 30 40 50 60 70 80 90 100 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 0.0 2 SER 0.0 0.0 0.0 3 SER 0.0 0.0 0.0 4 ARG 0.0 0.0 0.0 5 TRP 0.0 0.0 0.0 6 LEU 0.0 0.0 0.0 7 GLU 0.0 0.0 0.0 8 GLY 0.0 0.0 0.0 9 ILE 0.0 0.0 0.0 10 ARG 0.0 0.0 0.0 11 LYS 0.0 0.0 0.0 12 TRP 0.0 0.0 0.0 13 TYR 0.0 0.0 0.0 14 TYR 0.0 0.0 0.0 15 ASN 0.0 0.0 0.0 16 ALA 0.0 0.0 0.0 17 ALA 0.0 0.0 0.0 18 GLY 0.0 0.0 0.0 19 PHE 0.0 0.0 0.0 20 ASN 0.0 0.0 0.0 21 LYS 0.0 0.0 0.0 22 LEU 0.0 0.0 0.0 23 GLY 0.0 0.0 0.0 24 LEU 0.0 0.0 0.0 25 MET 0.0 0.0 0.0 26 ARG 0.0 0.0 0.0 27 ASP 0.0 0.0 0.0 28 ASP 0.0 0.0 0.0 29 THR 0.0 0.0 0.0 30 ILE 0.0 0.0 0.0 31 HIS 0.0 0.0 0.0 32 GLU 0.0 0.0 0.0 33 ASN 0.0 0.0 0.0 34 ASP 0.0 0.0 0.0 35 ASP 0.0 0.0 0.0 36 VAL 0.0 0.0 0.0 37 LYS 0.0 0.0 0.0 38 GLU 0.0 0.0 0.0 39 ALA 0.0 0.0 0.0 40 ILE 0.0 0.0 0.0 41 ARG 0.0 0.0 0.0 42 ARG 0.0 0.0 0.0 43 LEU 0.0 0.0 0.0 44 PRO 0.0 0.0 0.0 45 GLU 0.0 0.0 0.0 46 ASN 0.0 0.0 0.0 47 LEU 0.0 0.0 0.0 48 TYR 0.0 0.0 0.0 49 ASP 0.0 0.0 0.0 50 ASP 0.0 0.0 0.0 51 ARG 0.0 0.0 0.0 52 VAL 0.0 0.0 0.0 53 PHE 0.0 0.0 0.0 54 ARG 0.0 0.0 0.0 55 ILE 0.0 0.0 0.0 56 LYS 0.0 0.0 0.0 57 ARG 0.0 0.0 0.0 58 ALA 0.0 0.0 0.0 59 LEU 0.0 0.0 0.0 60 ASP 0.0 0.0 0.0 61 LEU 0.0 0.0 0.0 62 SER 0.0 0.0 0.0 63 MET 0.0 0.0 0.0 64 ARG 0.0 0.0 0.0 65 GLN 0.0 0.0 0.0 66 GLN 0.0 0.0 0.0 67 ILE 0.0 0.0 0.0 68 LEU 0.0 0.0 0.0 69 PRO 0.0 0.0 0.0 70 LYS 0.0 0.0 0.0 71 GLU 0.0 0.0 0.0 72 GLN 0.0 0.0 0.0 73 TRP 0.0 0.0 0.0 74 THR 0.0 0.0 0.0 75 LYS 0.0 0.0 0.0 76 TYR 0.0 0.0 0.0 77 GLU 0.0 0.0 0.0 78 GLU 0.0 0.0 0.0 79 ASP 0.0 0.0 0.0 80 LYS 0.0 0.0 0.0 81 SER 0.0 0.0 0.0 82 TYR 0.0 0.0 0.0 83 LEU 0.0 0.0 0.0 84 GLU 0.0 0.0 0.0 85 PRO 0.0 0.0 0.0 86 TYR 0.0 0.0 0.0 87 LEU 0.0 0.0 0.0 88 LYS 0.0 0.0 0.0 89 GLU 0.0 0.0 0.0 90 VAL 0.0 0.0 0.0 91 ILE 0.0 0.0 0.0 92 ARG 0.0 0.0 0.0 93 GLU 0.0 0.0 0.0 94 ARG 0.0 0.0 0.0 95 LYS 0.0 0.0 0.0 96 GLU 0.0 0.0 0.0 97 ARG 0.0 0.0 0.0 98 GLU 0.0 0.0 0.0 99 GLU 0.0 0.0 0.0 100 TRP 0.0 0.0 0.0 101 ALA 0.0 0.0 0.0 102 LYS 0.0 0.0 0.0 103 LYS 0.0 0.0 0.0