Protein Data Bank File : 2occf Title : OXIDOREDUCTASE 26-MAY-98 2OCC Number of Amino Acid Residues : 98 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA SER GLY GLY GLY VAL PRO THR ASP GLU 10 GLU GLN ALA THR GLY LEU GLU ARG GLU VAL 20 MET LEU ALA ALA ARG LYS GLY GLN ASP PRO 30 TYR ASN ILE LEU ALA PRO LYS ALA THR SER 40 GLY THR LYS GLU ASP PRO ASN LEU VAL PRO 50 SER ILE THR ASN LYS ARG ILE VAL GLY CYS 60 ILE CYS GLU GLU ASP ASN SER THR VAL ILE 70 TRP PHE TRP LEU HIS LYS GLY GLU ALA GLN 80 ARG CYS PRO SER CYS GLY THR HIS TYR LYS 90 LEU VAL PRO HIS GLN LEU ALA HIS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 107.0 -178.5 2 SER -76.4 135.1 179.6 -178.9 3 GLY -124.4 6.4 -179.6 4 GLY 62.0 -158.2 179.3 5 GLY 115.9 -14.6 179.5 6 VAL -100.6 131.2 -180.0 -25.9 7 PRO -57.3 159.1 176.2 -27.4 40.7 8 THR -109.8 165.6 179.6 58.6 9 ASP -63.1 -45.4 179.8 -77.5 -28.2 10 GLU -49.9 -34.6 179.7 167.8 83.0 71.7 11 GLU -96.2 -20.0 -177.1 48.6 -172.9 -86.1 12 GLN -122.5 -18.8 -179.9 -159.9 161.5 -74.1 13 ALA -59.1 142.0 -178.7 14 THR -133.9 -174.0 179.4 -174.0 15 GLY 41.0 -146.0 -178.6 16 LEU -56.3 -32.4 180.0 -165.3 54.6 17 GLU -61.3 -44.2 178.9 -179.0 -167.4 -14.8 18 ARG -67.1 -44.1 178.7 -171.7 168.2 -175.5 80.8 19 GLU -56.4 -50.9 179.7 -89.8 -159.0 66.1 20 VAL -66.0 -26.3 -179.6 -27.2 21 MET -69.5 -51.8 179.6 178.4 -175.6 68.3 22 LEU -63.0 -51.3 179.2 -68.7 168.4 23 ALA -55.3 -34.2 -178.6 24 ALA -65.2 -38.6 -179.3 25 ARG -76.1 -14.8 177.9 69.6 169.9 60.7 133.9 26 LYS -93.4 4.3 -179.9 -76.3 178.0 -77.8 176.3 27 GLY 81.3 4.4 -179.3 28 GLN -96.6 171.3 -178.7 -62.0 167.0 31.2 29 ASP -146.3 62.3 -179.5 -166.9 32.2 30 PRO -61.8 -13.1 -177.4 30.0 -42.3 31 TYR -113.3 24.8 176.5 -62.6 -80.0 32 ASN 41.6 50.8 179.3 -58.5 -80.1 33 ILE -88.8 -23.0 -179.2 -80.0 -178.8 34 LEU -110.4 154.4 179.3 -88.1 34.0 35 ALA -85.2 129.4 -180.0 36 PRO -70.3 137.5 178.7 27.7 -41.0 37 LYS -84.2 133.9 -178.8 -107.4 116.5 -68.6 177.6 38 ALA -75.1 149.0 176.4 39 THR -99.1 -165.7 -179.2 65.4 40 SER -71.4 -18.3 178.7 55.8 41 GLY 72.3 16.4 179.3 42 THR -81.4 172.7 -179.9 65.3 43 LYS -57.9 -31.5 -178.5 -167.1 -179.7 -65.5 176.3 44 GLU -90.3 -24.3 178.0 32.2 -89.5 -34.0 45 ASP -124.9 61.5 -179.6 -169.9 16.6 46 PRO -66.4 160.8 176.6 34.3 -45.8 47 ASN -75.9 128.4 -178.3 -75.4 -75.1 48 LEU -92.6 109.9 -177.6 -61.1 167.5 49 VAL -96.1 105.7 179.6 176.8 50 PRO -67.5 150.8 177.1 -23.5 37.6 51 SER -156.6 149.1 -178.1 166.9 52 ILE -98.1 6.7 179.6 -152.8 176.8 53 THR -142.2 -156.4 -177.5 -28.9 54 ASN -104.0 5.1 179.1 37.9 100.7 55 LYS -158.8 146.9 179.6 52.5 170.3 162.3 54.3 56 ARG -149.0 142.0 179.4 -168.8 -175.0 178.6 -174.6 57 ILE -73.8 132.1 176.6 -70.9 156.4 58 VAL -109.6 138.5 176.3 162.8 59 GLY -116.2 121.4 -178.3 60 CYS -111.5 120.6 178.1 179.9 61 ILE -92.2 88.5 -176.0 -60.3 169.2 62 CYS -44.4 -49.6 178.5 -56.5 63 GLU -128.8 139.8 -177.6 -68.3 158.6 -84.1 64 GLU -23.5 -59.4 -178.2 -152.8 -173.3 -43.7 65 ASP -102.4 35.9 178.8 -77.9 -27.1 66 ASN -78.5 140.9 -179.8 -94.4 16.3 67 SER -92.8 -16.3 179.1 42.7 68 THR -111.6 125.6 178.1 -8.8 69 VAL -89.2 140.7 177.9 177.8 70 ILE -95.5 121.6 -176.1 -62.8 -64.9 71 TRP -107.8 143.9 178.0 -56.0 100.1 72 PHE -170.3 153.2 177.7 60.2 -87.6 73 TRP -80.0 134.2 177.5 -78.1 105.4 74 LEU -105.6 121.5 178.5 -142.3 -151.8 75 HIS -101.3 161.2 176.7 -64.7 -94.1 76 LYS -63.3 129.7 -179.4 -175.1 -176.9 -72.5 179.8 77 GLY 143.3 -143.5 -179.9 78 GLU -71.8 156.6 177.9 -76.0 -80.7 -71.6 79 ALA -57.6 130.4 177.8 80 GLN -105.8 159.7 -178.8 -62.1 164.0 -127.7 81 ARG -114.8 149.9 178.3 -48.3 176.6 73.9 174.9 82 CYS -65.4 128.5 179.8 161.8 83 PRO -52.9 -24.2 -178.2 -29.1 39.9 84 SER -98.6 -44.5 -177.8 161.8 85 CYS -116.9 0.7 179.1 62.0 86 GLY 72.5 -1.6 177.8 87 THR -55.3 141.2 -177.6 -73.4 88 HIS -93.0 141.4 179.9 -69.8 86.5 89 TYR -138.2 141.4 179.4 -66.4 88.6 90 LYS -137.6 130.8 -179.1 -179.0 173.7 171.1 63.7 91 LEU -72.2 146.4 -179.0 -153.1 78.1 92 VAL -142.2 153.1 179.7 163.5 93 PRO -79.4 156.3 -178.3 29.7 -42.3 94 HIS -86.5 179.8 178.1 -156.4 56.6 95 GLN -52.9 -38.2 178.3 52.1 94.2 -120.6 96 LEU -93.7 111.2 -179.0 -147.4 -54.4 97 ALA -63.7 82.2 179.3 98 HIS 45.0 152.2 0.0 -59.4 159.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 110.937 341.760 219.320 2 SER 107.916 341.208 221.720 3 GLY 106.198 344.002 223.625 4 GLY 103.015 342.301 224.874 5 GLY 99.711 344.165 225.094 6 VAL 97.085 341.511 224.533 7 PRO 94.916 340.486 227.501 8 THR 94.937 336.916 228.798 9 ASP 91.832 334.929 229.655 10 GLU 92.768 334.989 233.335 11 GLU 92.571 338.774 233.250 12 GLN 89.714 339.423 230.830 13 ALA 87.400 336.418 230.612 14 THR 84.030 337.101 232.150 15 GLY 80.635 335.535 232.891 16 LEU 80.113 331.817 232.420 17 GLU 83.318 331.511 230.423 18 ARG 85.263 332.658 233.506 19 GLU 83.207 330.458 235.762 20 VAL 83.924 327.269 233.855 21 MET 87.565 328.390 233.647 22 LEU 88.074 328.921 237.388 23 ALA 86.024 325.891 238.337 24 ALA 88.131 323.879 235.863 25 ARG 91.469 324.589 237.524 26 LYS 90.031 323.586 240.902 27 GLY 89.103 320.169 239.454 28 GLN 85.304 320.714 239.463 29 ASP 82.597 320.627 236.727 30 PRO 79.493 322.611 237.697 31 TYR 78.479 322.874 234.040 32 ASN 78.502 319.285 232.954 33 ILE 81.189 319.705 230.326 34 LEU 82.818 316.404 231.308 35 ALA 81.472 312.884 231.377 36 PRO 80.989 311.480 234.879 37 LYS 82.978 308.374 235.754 38 ALA 80.939 305.410 236.992 39 THR 81.341 303.749 240.398 40 SER 80.509 300.054 240.880 41 GLY 76.805 300.830 240.929 42 THR 75.924 298.454 243.784 43 LYS 73.352 299.253 246.492 44 GLU 76.311 300.369 248.667 45 ASP 78.398 302.244 246.072 46 PRO 75.692 303.940 244.016 47 ASN 76.507 306.355 241.207 48 LEU 76.194 309.739 242.758 49 VAL 74.124 311.969 240.546 50 PRO 74.470 315.674 241.394 51 SER 71.426 317.926 240.924 52 ILE 70.439 321.504 241.468 53 THR 66.846 320.348 242.112 54 ASN 65.178 317.200 243.403 55 LYS 65.225 315.074 240.227 56 ARG 67.441 314.674 237.199 57 ILE 67.143 312.468 234.130 58 VAL 69.641 309.644 234.086 59 GLY 70.705 307.955 230.878 60 CYS 72.239 304.621 231.464 61 ILE 74.322 303.001 228.775 62 CYS 73.965 299.552 230.279 63 GLU 76.788 297.909 228.309 64 GLU 79.783 299.539 226.565 65 ASP 78.685 299.230 222.925 66 ASN 74.910 299.614 223.373 67 SER 73.108 301.802 220.826 68 THR 70.149 302.598 223.091 69 VAL 70.513 304.638 226.228 70 ILE 67.979 303.805 228.971 71 TRP 66.429 307.003 230.278 72 PHE 64.652 307.729 233.561 73 TRP 64.131 310.332 236.231 74 LEU 66.218 309.891 239.434 75 HIS 64.429 311.448 242.378 76 LYS 65.678 312.759 245.720 77 GLY 65.577 309.855 248.132 78 GLU 66.760 306.266 248.130 79 ALA 69.035 304.886 245.464 80 GLN 67.038 303.954 242.375 81 ARG 68.070 301.336 239.825 82 CYS 68.269 301.346 236.029 83 PRO 65.102 299.523 234.693 84 SER 67.337 297.443 232.427 85 CYS 70.546 296.552 234.330 86 GLY 69.833 297.323 237.954 87 THR 72.807 299.678 238.260 88 HIS 72.230 302.039 241.239 89 TYR 72.027 305.810 241.133 90 LYS 71.474 308.204 244.018 91 LEU 70.774 311.888 243.816 92 VAL 73.109 314.324 245.524 93 PRO 73.017 318.142 245.603 94 HIS 74.993 320.465 243.264 95 GLN 77.372 323.393 244.051 96 LEU 74.357 325.751 244.411 97 ALA 72.260 324.562 247.393 98 HIS 68.798 324.206 245.668 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/T T T 10 T S S S S/H H H H H H 20 H H H H H H H C T T 30 T T S S S S S S S S 40 C T T T T S S S S S 50 S S C S S S S S S S 60 S C C S S S S/S S S S 70 S S S S S S C S S S 80 S S/T T T T S S S S S 90 S S S S S/S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H 10 H H h h H H H H H H 20 H H H H H h T t t T 30 T t S 40 S S S S E E E E 50 E S S e E E E E E E 60 t T T t S S E 70 E E E E E e S S E 80 E e T T T t e E E E 90 E E E e S S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 96.7 2 SER 6.3 7.5 87.5 3 GLY 0.0 0.0 87.9 4 GLY 0.0 0.0 86.4 5 GLY 0.0 0.0 80.3 6 VAL 6.9 5.8 81.7 7 PRO 71.4 57.3 73.0 8 THR 35.1 32.9 77.3 9 ASP 28.7 26.0 75.1 10 GLU 60.2 43.4 77.8 11 GLU 40.4 29.2 74.5 12 GLN 39.8 26.7 76.9 13 ALA 65.1 89.6 58.6 14 THR 6.5 6.1 82.7 15 GLY 0.0 0.0 80.6 16 LEU 56.4 38.1 68.1 17 GLU 35.1 25.3 77.7 18 ARG 135.9 65.0 64.4 19 GLU 55.3 39.9 71.3 20 VAL 76.9 64.7 46.7 21 MET 120.3 75.5 59.7 22 LEU 93.7 63.4 68.1 23 ALA 61.9 85.3 54.7 24 ALA 25.1 34.5 84.0 25 ARG 97.4 46.6 70.4 26 LYS 55.5 32.0 77.7 27 GLY 0.0 0.0 84.1 28 GLN 48.9 32.9 71.9 29 ASP 78.8 71.3 56.1 30 PRO 111.5 89.6 48.0 31 TYR 115.4 63.8 58.7 32 ASN 55.7 46.1 85.1 33 ILE 58.2 40.6 66.7 34 LEU 47.5 32.2 79.6 35 ALA 4.8 6.6 75.3 36 PRO 14.7 11.8 84.4 37 LYS 16.4 9.5 90.4 38 ALA 16.0 22.0 88.1 39 THR 62.9 58.8 81.8 40 SER 30.5 36.5 75.7 41 GLY 34.1 97.9 74.4 42 THR 51.5 48.2 72.1 43 LYS 29.7 17.1 82.3 44 GLU 13.9 10.0 78.8 45 ASP 47.0 42.6 74.9 46 PRO 108.6 87.2 55.2 47 ASN 105.3 87.1 47.4 48 LEU 62.0 41.9 64.1 49 VAL 102.5 86.2 40.3 50 PRO 71.6 57.5 72.9 51 SER 76.7 91.7 58.0 52 ILE 57.6 40.2 72.0 53 THR 46.7 43.7 77.5 54 ASN 51.9 42.9 55.7 55 LYS 92.8 53.5 60.9 56 ARG 126.3 60.5 63.2 57 ILE 72.1 50.2 58.6 58 VAL 108.2 91.0 41.4 59 GLY 32.3 92.7 44.5 60 CYS 92.7 93.5 44.6 61 ILE 61.1 42.6 73.4 62 CYS 93.6 94.3 53.2 63 GLU 17.9 12.9 87.5 64 GLU 0.0 0.0 88.7 65 ASP 2.1 1.9 87.4 66 ASN 74.2 61.4 74.2 67 SER 0.0 0.0 89.8 68 THR 10.9 10.2 84.6 69 VAL 84.6 71.2 54.3 70 ILE 90.7 63.2 55.9 71 TRP 66.4 32.4 69.4 72 PHE 135.8 81.4 46.5 73 TRP 96.7 47.1 65.8 74 LEU 147.8 100.0 46.1 75 HIS 61.8 41.1 70.5 76 LYS 73.7 42.5 70.1 77 GLY 2.5 7.2 81.7 78 GLU 0.0 0.0 91.4 79 ALA 62.3 85.9 51.8 80 GLN 92.5 62.2 66.6 81 ARG 80.5 38.5 72.9 82 CYS 99.2 100.0 32.0 83 PRO 53.3 42.8 64.2 84 SER 43.3 51.8 55.5 85 CYS 68.1 68.6 59.8 86 GLY 25.0 71.9 71.6 87 THR 69.6 65.1 65.1 88 HIS 137.8 91.8 46.6 89 TYR 156.6 86.5 37.1 90 LYS 99.1 57.1 61.6 91 LEU 144.4 97.7 50.3 92 VAL 72.5 61.0 52.2 93 PRO 51.3 41.2 72.8 94 HIS 121.9 81.1 60.4 95 GLN 71.8 48.3 62.6 96 LEU 46.4 31.4 78.6 97 ALA 2.5 3.5 78.7 98 HIS 94.1 62.7 69.8