Protein Data Bank File : 1ezvi Title : OXIDOREDUCTASE/ELECTRON TRANSPORT 12-MAY-00 1EZV Number of Amino Acid Residues : 55 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER SER LEU TYR LYS THR PHE PHE LYS ARG 10 ASN ALA VAL PHE VAL GLY THR ILE PHE ALA 20 GLY ALA PHE VAL PHE GLN THR VAL PHE ASP 30 THR ALA ILE THR SER TRP TYR GLU ASN HIS 40 ASN LYS GLY LYS LEU TRP LYS ASP VAL LYS 50 ALA ARG ILE ALA ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 144.1 179.9 -165.7 2 SER -101.2 -1.9 172.6 -76.3 3 LEU -69.6 -31.1 177.0 177.4 71.0 4 TYR -70.9 -44.4 -175.4 -167.2 -93.4 5 LYS -72.3 -1.4 174.5 -95.9 170.7 88.8 163.3 6 THR -90.3 -42.0 -178.1 60.8 7 PHE -84.2 -52.2 -168.1 -64.9 -77.6 8 PHE -112.7 -15.1 168.0 -51.3 -70.4 9 LYS 51.9 71.1 176.1 -54.3 173.6 -172.9 176.8 10 ARG 61.8 -5.5 172.9 93.4 115.8 102.7 -98.0 11 ASN -95.6 153.0 174.2 -101.5 175.3 12 ALA -68.2 157.2 174.8 13 VAL -73.5 134.3 -172.5 -170.7 14 PHE -91.2 151.2 -174.9 -54.4 114.6 15 VAL -47.8 -43.0 -178.9 -111.2 16 GLY -59.2 -43.3 175.7 17 THR -68.0 -36.3 177.7 -48.8 18 ILE -65.0 -49.8 179.9 -66.0 -65.5 19 PHE -60.7 -43.6 -179.8 -77.7 -3.6 20 ALA -64.7 -44.1 176.0 21 GLY -62.0 -31.2 -178.5 22 ALA -69.6 -40.1 176.1 23 PHE -62.3 -39.3 178.4 -77.6 -132.0 24 VAL -67.0 -48.7 179.5 -175.3 25 PHE -53.8 -49.5 -175.6 179.0 86.0 26 GLN -50.4 -45.7 -177.1 -166.0 153.2 -91.7 27 THR -75.3 -46.6 -179.0 -49.7 28 VAL -60.8 -49.9 -177.7 174.2 29 PHE -60.9 -41.9 179.9 -172.5 64.0 30 ASP -62.6 -42.1 -179.3 -169.9 50.8 31 THR -69.2 -43.0 176.9 -58.5 32 ALA -57.2 -40.4 -177.0 33 ILE -77.1 -46.7 176.7 -65.2 -58.8 34 THR -57.5 -39.7 179.7 -61.5 35 SER -63.1 -53.7 177.4 -77.0 36 TRP -56.2 -44.2 -174.4 -175.3 88.6 37 TYR -65.4 -49.7 -179.7 -169.6 72.1 38 GLU -65.7 -34.2 176.3 -71.9 -165.2 147.3 39 ASN -68.2 -50.4 176.8 -179.5 67.8 40 HIS -53.8 -30.0 -178.9 -179.4 88.3 41 ASN -105.3 24.5 177.8 -81.5 -84.1 42 LYS -57.0 132.1 -176.3 -152.6 -168.1 -73.6 -63.1 43 GLY 105.5 -37.3 -171.5 44 LYS -93.1 -24.6 -177.1 -73.2 146.1 71.4 -175.8 45 LEU -64.5 159.0 170.1 -91.5 11.0 46 TRP -64.2 -36.0 172.6 174.4 -118.8 47 LYS -47.5 -46.5 -173.0 -72.3 -159.2 -47.3 -178.4 48 ASP -79.4 -31.4 -179.7 -51.6 145.7 49 VAL -74.8 -34.0 -178.7 176.6 50 LYS -68.0 -23.9 177.8 -158.1 -162.8 177.3 -178.6 51 ALA -72.0 -8.9 -177.9 52 ARG -118.0 14.7 177.8 -49.0 -148.8 -98.3 -135.6 53 ILE -132.2 146.2 176.7 -44.5 -71.5 54 ALA -161.0 111.9 179.1 55 ALA -168.2 -149.6 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER -36.277 64.386 31.410 2 SER -35.093 64.696 35.010 3 LEU -33.841 61.099 35.197 4 TYR -30.786 62.329 33.285 5 LYS -30.155 65.311 35.589 6 THR -29.875 63.019 38.634 7 PHE -27.034 60.846 37.324 8 PHE -25.133 63.053 34.878 9 LYS -26.590 66.478 35.709 10 ARG -26.727 68.435 32.424 11 ASN -23.269 67.109 31.479 12 ALA -22.631 64.520 28.770 13 VAL -21.733 60.946 29.723 14 PHE -17.950 60.512 29.882 15 VAL -15.899 57.851 28.047 16 GLY -14.932 56.027 31.244 17 THR -18.584 55.544 32.186 18 ILE -19.366 54.591 28.567 19 PHE -16.584 51.984 28.445 20 ALA -17.635 50.613 31.844 21 GLY -21.288 50.426 30.837 22 ALA -20.275 48.575 27.656 23 PHE -18.536 45.747 29.553 24 VAL -21.684 45.347 31.673 25 PHE -23.949 45.436 28.614 26 GLN -21.949 42.772 26.792 27 THR -22.541 40.142 29.481 28 VAL -26.146 41.022 30.359 29 PHE -27.234 41.244 26.717 30 ASP -25.599 37.930 25.781 31 THR -27.361 36.034 28.581 32 ALA -30.727 37.629 27.772 33 ILE -30.405 36.597 24.098 34 THR -29.066 33.080 24.687 35 SER -31.927 32.524 27.148 36 TRP -34.641 33.673 24.759 37 TYR -33.017 31.729 21.905 38 GLU -32.647 28.395 23.721 39 ASN -36.183 28.729 25.117 40 HIS -37.697 29.560 21.713 41 ASN -36.038 26.375 20.420 42 LYS -37.072 24.088 23.298 43 GLY -37.392 20.498 22.122 44 LYS -34.960 20.836 19.222 45 LEU -31.704 21.417 21.126 46 TRP -29.109 18.776 21.972 47 LYS -29.750 19.688 25.646 48 ASP -33.309 18.437 25.207 49 VAL -32.439 15.361 23.149 50 LYS -29.831 14.150 25.660 51 ALA -32.560 14.043 28.325 52 ARG -34.198 11.243 26.312 53 ILE -31.084 9.092 25.800 54 ALA -29.032 7.037 28.294 55 ALA -26.232 4.531 27.578 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C H H H H H H H/T T T 10 T C C H H H H H 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 H C C H H H H H H 50 H 3 3/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T h H H H H h T T 10 t h H H H H 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 T T T h H H H H H 50 h T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 12.5 15.0 85.4 2 SER 8.2 9.8 80.8 3 LEU 22.1 14.9 81.6 4 TYR 95.3 52.7 63.3 5 LYS 53.8 31.0 76.4 6 THR 34.4 32.2 71.9 7 PHE 53.6 32.1 72.2 8 PHE 101.6 60.9 55.3 9 LYS 39.2 22.6 83.0 10 ARG 28.9 13.9 82.2 11 ASN 41.8 34.6 75.9 12 ALA 6.5 9.0 85.3 13 VAL 89.0 74.9 45.9 14 PHE 39.0 23.4 82.4 15 VAL 16.7 14.0 68.1 16 GLY 0.0 0.0 72.2 17 THR 41.9 39.2 63.9 18 ILE 55.1 38.4 66.6 19 PHE 40.6 24.3 69.7 20 ALA 15.9 21.9 76.3 21 GLY 5.8 16.5 74.3 22 ALA 24.5 33.8 70.9 23 PHE 18.5 11.1 81.1 24 VAL 24.2 20.4 74.8 25 PHE 48.2 28.9 66.0 26 GLN 12.8 8.6 83.0 27 THR 13.0 12.1 82.7 28 VAL 24.3 20.4 71.8 29 PHE 66.4 39.8 58.8 30 ASP 20.8 18.8 81.5 31 THR 22.2 20.8 83.0 32 ALA 22.3 30.7 69.8 33 ILE 53.9 37.6 64.3 34 THR 43.6 40.8 74.0 35 SER 24.8 29.7 75.2 36 TRP 52.0 25.4 74.5 37 TYR 49.2 27.2 72.8 38 GLU 83.1 60.0 59.2 39 ASN 39.2 32.4 77.2 40 HIS 50.8 33.8 76.9 41 ASN 97.8 80.9 51.6 42 LYS 47.4 27.3 88.9 43 GLY 8.3 23.8 69.6 44 LYS 39.3 22.7 85.8 45 LEU 104.9 70.9 61.7 46 TRP 43.3 21.1 71.4 47 LYS 58.0 33.5 75.4 48 ASP 78.6 71.1 57.4 49 VAL 63.6 53.5 65.8 50 LYS 43.6 25.1 77.1 51 ALA 13.6 18.7 81.2 52 ARG 43.1 20.6 84.1 53 ILE 45.4 31.7 71.5 54 ALA 1.9 2.7 81.8 55 ALA 1.9 2.6 86.7