Protein Data Bank File : 1h8ei Title : ATP PHOSPHORYLASE 01-FEB-01 1H8E Number of Amino Acid Residues : 36 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 VAL ALA TYR TRP ARG GLN ALA GLY LEU SER 10 TYR ILE ARG TYR SER GLN ILE CYS ALA LYS 20 ALA VAL ARG ASP ALA THR SER GLY SER THR 30 ILE LYS ILE VAL LYS VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 VAL 0.0 141.2 179.9 -164.5 2 ALA -83.9 171.8 -178.8 3 TYR -64.8 -46.3 -175.3 57.3 88.8 4 TRP -64.6 -34.3 171.7 46.8 -86.8 5 ARG -72.3 172.4 -174.6 -156.1 174.2 -69.9 -62.0 6 GLN 72.8 -29.7 177.8 -164.8 80.6 45.1 7 ALA -106.6 9.4 176.4 8 GLY 91.5 -24.4 -177.4 9 LEU -64.2 153.2 175.9 -72.9 65.0 10 SER -108.3 -178.4 177.6 77.0 11 TYR -77.2 -36.1 -178.3 -172.4 78.0 12 ILE -59.6 -41.7 178.6 -67.3 -59.3 13 ARG -59.5 -42.5 175.1 179.1 57.7 -169.4 140.3 14 TYR -62.0 -52.1 -177.5 171.5 95.2 15 SER -58.2 -37.0 -176.8 -175.0 16 GLN -53.2 -52.3 176.2 -152.0 175.0 -66.8 17 ILE -63.5 -52.6 179.0 -50.5 -114.9 18 CYS -59.7 -42.5 -179.4 -45.4 19 ALA -53.3 -48.1 -177.3 20 LYS -63.8 -42.1 179.5 -174.1 -150.1 -145.3 -164.2 21 ALA -58.7 -47.5 178.6 22 VAL -54.9 -41.6 -179.7 -176.0 23 ARG -55.3 -54.7 -179.8 -87.8 -175.0 -139.1 113.8 24 ASP -57.0 -30.3 176.7 -65.8 -28.1 25 ALA -67.4 -18.9 -36.1 26 THR 71.3 179.4 175.6 -31.4 27 SER 49.8 39.7 174.9 70.0 28 GLY -91.7 -165.9 176.1 29 SER -174.4 68.1 178.5 -163.3 30 THR -71.8 -42.7 178.7 -45.3 31 ILE -33.8 141.6 178.3 -99.9 -77.9 32 LYS -135.1 142.1 -176.4 156.9 77.6 149.0 -148.8 33 ILE -82.3 139.8 174.5 -40.9 -81.5 34 VAL -128.3 79.6 -175.5 -172.4 35 LYS -85.1 118.9 177.6 51.7 -165.7 104.1 155.4 36 VAL -150.1 71.7 0.0 -156.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 VAL 18.331 75.495 72.223 2 ALA 19.794 77.228 69.169 3 TYR 19.668 75.844 65.637 4 TRP 23.366 74.987 65.441 5 ARG 23.197 72.952 68.629 6 GLN 20.999 69.879 67.933 7 ALA 23.178 70.140 64.820 8 GLY 26.363 69.395 66.757 9 LEU 27.953 72.856 66.703 10 SER 29.277 74.438 69.897 11 TYR 29.501 78.131 70.802 12 ILE 33.259 78.619 70.202 13 ARG 32.545 77.356 66.724 14 TYR 29.715 79.857 66.413 15 SER 31.858 82.781 67.573 16 GLN 34.517 81.534 65.126 17 ILE 32.224 82.013 62.167 18 CYS 30.764 85.374 63.247 19 ALA 34.282 86.661 64.077 20 LYS 35.458 85.750 60.624 21 ALA 32.434 87.303 58.934 22 VAL 33.110 90.665 60.568 23 ARG 36.666 90.292 59.251 24 ASP 35.631 89.674 55.666 25 ALA 33.481 92.805 55.924 26 THR 45.579 87.298 64.039 27 SER 43.118 84.501 63.262 28 GLY 45.783 81.990 62.282 29 SER 45.707 78.319 63.204 30 THR 49.242 77.019 63.219 31 ILE 48.358 74.613 66.016 32 LYS 48.390 70.943 65.008 33 ILE 46.695 67.949 66.660 34 VAL 48.630 64.922 67.917 35 LYS 46.054 62.249 68.749 36 VAL 47.290 58.883 70.070 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C T T T T/T T T T C H 10 H H H H H H H H H H 20 H H H H H/X X/C S S S S/S 30 S S 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 T t h 10 H H H H H H H H H H 20 H H H H h 30 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 VAL 35.4 29.8 81.8 2 ALA 36.8 50.6 65.0 3 TYR 6.5 3.6 79.1 4 TRP 176.3 86.0 36.9 5 ARG 98.8 47.3 66.1 6 GLN 12.6 8.4 84.3 7 ALA 27.1 37.4 74.1 8 GLY 0.0 0.0 79.6 9 LEU 78.8 53.3 61.2 10 SER 35.9 43.0 70.5 11 TYR 60.1 33.2 65.7 12 ILE 9.3 6.5 83.7 13 ARG 109.7 52.5 66.6 14 TYR 102.2 56.5 57.4 15 SER 36.1 43.2 64.3 16 GLN 54.2 36.5 72.7 17 ILE 62.2 43.3 73.4 18 CYS 45.7 46.0 63.6 19 ALA 35.0 48.2 75.9 20 LYS 50.3 29.0 83.6 21 ALA 20.6 28.4 75.6 22 VAL 9.1 7.6 80.3 23 ARG 100.4 48.1 68.9 24 ASP 24.4 22.1 75.0 25 ALA 9.9 13.6 81.1 26 THR 0.0 0.0 96.1 27 SER 47.5 56.8 75.8 28 GLY 0.0 0.0 84.9 29 SER 12.7 15.2 81.5 30 THR 0.0 0.0 91.2 31 ILE 10.9 7.6 83.7 32 LYS 21.9 12.7 82.7 33 ILE 39.5 27.5 66.5 34 VAL 20.0 16.8 77.6 35 LYS 20.0 11.5 79.1 36 VAL 5.7 4.8 79.9