Protein Data Bank File : 2occh Title : OXIDOREDUCTASE 26-MAY-98 2OCC Number of Amino Acid Residues : 79 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS ILE LYS ASN TYR GLN THR ALA PRO PHE 10 ASP SER ARG PHE PRO ASN GLN ASN GLN THR 20 ARG ASN CYS TRP GLN ASN TYR LEU ASP PHE 30 HIS ARG CYS GLU LYS ALA MET THR ALA LYS 40 GLY GLY ASP VAL SER VAL CYS GLU TRP TYR 50 ARG ARG VAL TYR LYS SER LEU CYS PRO ILE 60 SER TRP VAL SER THR TRP ASP ASP ARG ARG 70 ALA GLU GLY THR PHE PRO GLY LYS ILE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 168.5 -178.7 -112.3 67.9 -78.4 172.8 2 ILE -104.5 122.7 178.5 69.3 175.7 3 LYS -99.9 20.1 177.5 -60.3 161.2 -174.3 171.9 4 ASN -129.6 140.1 -178.7 74.5 -82.9 5 TYR -161.7 -162.6 178.3 66.7 6.9 6 GLN -98.9 -58.8 178.9 -74.9 -111.7 -124.9 7 THR -168.1 163.0 178.7 -166.7 8 ALA -50.0 119.7 -179.9 9 PRO -75.1 172.9 179.5 32.4 -42.9 10 PHE -63.8 129.1 -179.4 171.6 81.4 11 ASP -114.5 110.0 -178.5 -167.1 -18.3 12 SER -56.2 -14.7 178.8 86.0 13 ARG -76.4 -19.8 -178.9 -46.4 -159.3 -61.5 -71.9 14 PHE -135.1 72.6 -179.1 -45.1 -81.0 15 PRO -84.4 -1.4 -177.3 36.9 -37.9 16 ASN -107.4 178.8 -179.7 -53.3 -60.0 17 GLN -59.5 -28.8 -179.6 -63.5 -161.0 -6.7 18 ASN -83.9 106.6 -178.4 -175.8 -10.7 19 GLN -101.7 9.3 -180.0 -66.8 -69.8 -47.5 20 THR -49.7 -48.0 -179.7 -49.7 21 ARG -71.5 -23.2 179.8 -71.3 -136.4 -49.0 -78.1 22 ASN -64.1 -48.6 177.7 -155.8 -14.3 23 CYS -60.7 -53.0 -178.8 153.7 24 TRP -56.6 -51.7 -179.6 171.7 -105.9 25 GLN -57.4 -54.7 -179.4 -162.1 56.8 -120.0 26 ASN -59.1 -31.0 177.1 -71.1 -60.7 27 TYR -69.3 -35.1 180.0 174.5 -90.7 28 LEU -74.4 -52.9 -179.9 -84.8 -179.3 29 ASP -46.7 -40.1 179.3 -81.0 -5.7 30 PHE -62.5 -63.5 -179.3 167.9 72.9 31 HIS -57.3 -23.8 176.9 -66.6 82.5 32 ARG -75.8 -42.9 179.0 -71.4 176.7 -179.8 172.9 33 CYS -69.8 -38.3 179.9 -176.7 34 GLU -59.4 -44.7 178.6 -173.5 -172.2 60.1 35 LYS -57.6 -66.0 179.9 -71.7 -75.5 -76.8 -63.7 36 ALA -44.8 -58.0 179.8 37 MET -60.2 -36.0 -179.4 -62.2 -50.4 125.8 38 THR -85.6 -9.6 -179.4 -144.8 39 ALA -100.3 -52.0 179.3 40 LYS -80.5 29.4 179.8 -57.3 -178.5 178.3 -177.5 41 GLY 51.1 41.3 -179.3 42 GLY -104.4 -165.4 -179.0 43 ASP -90.6 113.2 179.8 -154.0 9.6 44 VAL -76.2 -18.5 179.7 -174.5 45 SER -66.5 -12.0 178.5 -45.1 46 VAL -72.0 -29.3 179.5 -68.4 47 CYS -77.1 -4.4 -177.2 -51.9 48 GLU -57.9 -46.2 179.2 -169.9 60.4 8.6 49 TRP -45.8 -55.7 179.8 174.4 -108.7 50 TYR -56.5 -37.2 -179.3 -58.8 -58.2 51 ARG -70.6 -35.1 179.2 -152.2 -159.1 68.0 -128.6 52 ARG -65.0 -53.8 179.4 -73.5 -48.3 -68.4 -71.1 53 VAL -55.8 -53.6 -179.1 170.6 54 TYR -65.1 -28.0 179.7 96.3 59.0 55 LYS -70.1 -39.3 178.2 -100.1 -72.2 166.2 -172.5 56 SER -63.6 -51.1 -176.3 -84.6 57 LEU -81.8 -36.0 -175.9 -49.8 171.4 58 CYS -77.5 134.5 179.4 -56.8 59 PRO -66.0 146.6 178.8 -32.7 44.5 60 ILE -52.4 -43.9 179.3 -74.1 164.2 61 SER -59.6 -34.8 -179.3 -50.1 62 TRP -72.6 -48.6 179.3 -64.6 15.4 63 VAL -58.9 -47.9 177.3 -177.5 64 SER -56.4 -51.5 -179.9 -65.1 65 THR -64.8 -40.4 178.2 51.8 66 TRP -63.5 -40.4 177.7 -67.5 -16.8 67 ASP -64.0 -47.4 178.1 -78.0 -18.4 68 ASP -57.2 -35.0 -179.7 -86.5 23.6 69 ARG -76.9 -38.0 177.7 -73.2 174.0 -174.5 165.4 70 ARG -62.2 -35.3 178.6 -78.4 -173.8 -44.3 107.9 71 ALA -71.7 -40.1 179.1 72 GLU -73.3 -18.0 179.4 177.2 178.9 40.7 73 GLY 90.8 2.8 -178.8 74 THR -104.9 18.2 179.0 58.8 75 PHE -73.8 114.6 -179.1 -178.5 68.7 76 PRO -63.9 -20.6 -179.3 37.2 -47.4 77 GLY -79.9 159.8 179.6 78 LYS -92.6 111.9 179.3 -104.8 77.3 71.9 168.4 79 ILE -114.5 112.0 0.0 -64.4 178.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 85.960 306.693 143.315 2 ILE 82.293 307.773 143.664 3 LYS 81.028 311.360 144.121 4 ASN 77.556 309.725 143.966 5 TYR 76.223 307.729 146.948 6 GLN 73.376 306.854 149.294 7 THR 74.019 309.015 152.393 8 ALA 76.868 310.062 154.705 9 PRO 78.326 306.786 155.991 10 PHE 79.289 305.909 159.549 11 ASP 82.304 307.914 160.606 12 SER 84.374 306.396 163.436 13 ARG 85.583 309.865 164.362 14 PHE 82.026 310.633 165.470 15 PRO 80.633 307.373 166.881 16 ASN 78.115 308.730 169.365 17 GLN 74.627 310.234 169.352 18 ASN 75.988 313.745 169.212 19 GLN 76.689 314.385 165.511 20 THR 77.177 318.118 165.783 21 ARG 80.857 318.030 164.947 22 ASN 80.329 315.629 162.004 23 CYS 78.285 318.239 160.225 24 TRP 80.675 320.986 161.274 25 GLN 83.883 319.241 160.344 26 ASN 82.656 318.187 156.907 27 TYR 81.369 321.671 156.330 28 LEU 84.774 323.147 157.082 29 ASP 86.769 320.550 155.245 30 PHE 84.786 321.337 152.132 31 HIS 85.329 325.094 152.098 32 ARG 88.962 324.548 152.980 33 CYS 89.341 322.108 150.076 34 GLU 87.285 324.359 147.833 35 LYS 89.722 327.226 148.467 36 ALA 92.969 325.293 147.763 37 MET 91.622 323.600 144.618 38 THR 90.009 326.803 143.339 39 ALA 93.103 328.850 144.221 40 LYS 96.110 326.744 143.157 41 GLY 94.355 326.229 139.796 42 GLY 93.378 322.728 140.813 43 ASP 90.478 320.310 140.746 44 VAL 87.496 321.354 142.921 45 SER 85.749 317.987 142.371 46 VAL 88.033 316.377 144.931 47 CYS 86.073 318.433 147.450 48 GLU 82.753 316.923 146.315 49 TRP 82.666 314.199 148.926 50 TYR 82.644 316.632 151.844 51 ARG 79.821 318.701 150.355 52 ARG 77.665 315.659 149.918 53 VAL 78.284 314.582 153.521 54 TYR 77.814 317.967 155.080 55 LYS 74.723 318.493 152.926 56 SER 73.226 315.226 154.152 57 LEU 73.930 315.892 157.847 58 CYS 73.708 319.634 158.322 59 PRO 70.402 321.268 159.043 60 ILE 69.494 323.773 156.337 61 SER 69.451 326.668 158.863 62 TRP 73.006 325.997 159.963 63 VAL 74.375 325.773 156.419 64 SER 72.487 328.973 155.479 65 THR 73.752 331.010 158.469 66 TRP 77.314 329.714 158.100 67 ASP 77.251 330.651 154.360 68 ASP 75.813 334.116 155.145 69 ARG 78.621 334.524 157.652 70 ARG 81.453 333.372 155.388 71 ALA 80.222 336.051 152.941 72 GLU 79.902 338.638 155.748 73 GLY 83.445 337.900 157.017 74 THR 82.179 336.749 160.424 75 PHE 82.458 332.954 160.045 76 PRO 84.177 331.895 163.316 77 GLY 85.786 328.783 161.919 78 LYS 89.182 328.882 160.291 79 ILE 88.898 328.406 156.545 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S S S S 10 T T T T C C C C H H 20 H H H H H H H H H H 30 H H H H H H H H H H 40 H/S S S S C C H H H H 50 H H H H H H H H H H 60 H H H H H H H H H H 70 H H H C C S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S 10 t T T t S S h H 20 H H H H H H H H H H 30 H H H H H H H H H h 40 T t g G G G h H H H 50 H H H H H H H h h H 60 H H H H H H H H H H 70 H H h t S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 0.0 0.0 93.3 2 ILE 39.2 27.3 80.4 3 LYS 78.0 45.0 69.7 4 ASN 25.4 21.0 72.1 5 TYR 161.2 89.0 56.1 6 GLN 0.0 0.0 83.9 7 THR 30.3 28.3 73.5 8 ALA 70.4 96.9 39.9 9 PRO 55.1 44.2 68.1 10 PHE 40.0 24.0 77.6 11 ASP 84.8 76.8 71.3 12 SER 15.7 18.8 68.6 13 ARG 85.6 41.0 76.6 14 PHE 151.2 90.7 64.6 15 PRO 71.5 57.5 73.8 16 ASN 16.9 14.0 81.0 17 GLN 0.0 0.0 89.4 18 ASN 21.6 17.9 83.2 19 GLN 85.3 57.4 76.5 20 THR 40.9 38.3 69.8 21 ARG 52.5 25.2 75.0 22 ASN 113.4 93.8 52.6 23 CYS 95.3 96.1 37.0 24 TRP 143.0 69.7 45.6 25 GLN 98.6 66.3 70.5 26 ASN 115.0 95.2 53.9 27 TYR 181.0 100.0 36.8 28 LEU 141.4 95.7 53.6 29 ASP 78.0 70.6 61.1 30 PHE 151.9 91.1 49.5 31 HIS 142.7 95.0 56.1 32 ARG 120.4 57.6 70.3 33 CYS 74.8 75.4 47.5 34 GLU 83.1 60.0 51.0 35 LYS 61.4 35.4 76.1 36 ALA 38.7 53.4 58.2 37 MET 103.8 65.1 56.8 38 THR 43.5 40.7 64.4 39 ALA 26.5 36.5 70.9 40 LYS 12.9 7.4 84.0 41 GLY 0.0 0.0 85.1 42 GLY 15.3 44.0 70.1 43 ASP 30.6 27.7 73.6 44 VAL 65.3 54.9 63.5 45 SER 38.4 46.0 77.9 46 VAL 53.3 44.9 63.1 47 CYS 99.0 99.8 40.0 48 GLU 103.7 74.8 61.2 49 TRP 114.9 56.1 52.5 50 TYR 110.8 61.2 64.6 51 ARG 123.1 58.9 61.5 52 ARG 130.7 62.6 67.0 53 VAL 111.4 93.8 47.1 54 TYR 171.8 94.9 34.7 55 LYS 78.4 45.2 70.3 56 SER 55.7 66.6 71.2 57 LEU 104.9 71.0 63.1 58 CYS 99.2 100.0 36.3 59 PRO 65.5 52.6 65.2 60 ILE 6.8 4.7 88.6 61 SER 11.7 14.0 70.7 62 TRP 108.8 53.1 56.6 63 VAL 110.5 93.0 53.8 64 SER 29.4 35.1 70.5 65 THR 46.1 43.2 74.7 66 TRP 172.9 84.4 41.0 67 ASP 66.3 60.0 74.1 68 ASP 15.0 13.5 78.6 69 ARG 102.9 49.3 70.7 70 ARG 144.8 69.3 60.4 71 ALA 8.9 12.2 84.2 72 GLU 40.1 28.9 79.0 73 GLY 1.3 3.7 83.3 74 THR 38.6 36.1 74.5 75 PHE 159.4 95.6 32.1 76 PRO 46.0 36.9 70.3 77 GLY 27.9 80.2 43.3 78 LYS 4.9 2.8 90.6 79 ILE 127.8 89.1 49.1