Protein Data Bank File : 1aie Title : P53 TETRAMERIZATION 17-APR-97 1AIE Number of Amino Acid Residues : 31 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU TYR PHE THR LEU GLN ILE ARG GLY ARG 10 GLU ARG PHE GLU MET PHE ARG GLU LEU ASN 20 GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA 30 GLY Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 126.3 -179.8 -160.3 165.1 16.3 2 TYR -103.6 145.1 179.7 -47.1 69.3 3 PHE -129.4 160.5 -179.5 -56.6 85.5 4 THR -123.8 133.3 -179.9 179.8 5 LEU -118.6 128.1 178.3 -171.1 58.5 6 GLN -90.6 123.7 -177.5 -174.5 169.8 60.4 7 ILE -117.5 139.5 179.5 -60.0 157.5 8 ARG -99.8 122.6 179.5 -159.9 -175.7 -177.4 -160.2 9 GLY 101.4 124.8 179.6 10 ARG -55.1 -44.9 -178.4 173.5 107.7 -88.1 -130.6 11 GLU -66.1 -39.5 179.6 -52.4 -71.3 61.5 12 ARG -67.3 -40.3 -179.8 -179.5 169.7 -63.1 156.4 13 PHE -62.9 -44.0 178.8 169.6 63.6 14 GLU -58.6 -43.2 179.9 -77.3 171.9 20.8 15 MET -62.2 -49.5 -179.8 171.2 -168.4 82.5 16 PHE -66.4 -34.4 178.5 -78.6 -58.9 17 ARG -65.0 -42.6 178.8 171.5 65.4 -173.8 -175.2 18 GLU -65.3 -43.3 179.4 -160.1 -168.8 7.3 19 LEU -62.9 -39.7 -179.1 -72.8 176.4 20 ASN -69.8 -39.0 179.1 -172.0 -120.7 21 GLU -67.6 -36.4 179.0 -78.0 178.5 2.4 22 ALA -63.2 -44.8 179.6 23 LEU -65.0 -37.4 179.3 -68.0 172.7 24 GLU -69.0 -37.8 178.2 -68.7 -172.3 -8.3 25 LEU -65.7 -40.9 179.7 167.3 71.4 26 LYS -60.5 -44.8 179.6 -170.3 177.7 179.4 76.0 27 ASP -66.1 -41.0 -179.0 -70.2 -15.0 28 ALA -57.0 -24.5 179.5 29 GLN -103.5 -41.5 178.4 -45.1 -162.4 125.2 30 ALA 85.9 88.4 179.0 31 GLY 155.8 139.3 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 15.471 16.220 -11.447 2 TYR 15.604 17.298 -7.797 3 PHE 15.212 20.876 -6.587 4 THR 15.769 22.434 -3.209 5 LEU 13.469 24.883 -1.495 6 GLN 14.491 27.016 1.457 7 ILE 11.664 27.406 3.997 8 ARG 11.436 29.743 6.985 9 GLY 10.018 28.329 10.237 10 ARG 9.976 24.830 11.744 11 GLU 6.176 24.541 11.620 12 ARG 6.038 25.620 7.987 13 PHE 8.856 23.205 7.144 14 GLU 7.003 20.355 8.896 15 MET 3.882 21.105 6.874 16 PHE 5.670 21.106 3.508 17 ARG 7.643 17.982 4.467 18 GLU 4.401 16.097 5.237 19 LEU 2.802 17.267 1.986 20 ASN 5.883 16.254 -0.030 21 GLU 6.083 12.815 1.613 22 ALA 2.352 12.341 0.930 23 LEU 2.825 13.062 -2.799 24 GLU 5.793 10.668 -3.000 25 LEU 3.836 7.885 -1.306 26 LYS 0.979 8.458 -3.800 27 ASP 3.394 8.162 -6.757 28 ALA 5.157 5.057 -5.466 29 GLN 1.814 3.272 -5.769 30 ALA 0.367 5.541 -8.491 31 GLY -3.125 6.960 -8.039 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/H H 10 H H H H H H H H H H 20 H H H H H H H H H H/S 30 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H 10 H H H H H H H H H H 20 H H H H H H H H H h 30 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 16.5 11.9 76.3 2 TYR 0.0 0.0 88.6 3 PHE 33.8 20.2 84.1 4 THR 0.0 0.0 87.2 5 LEU 29.5 19.9 79.8 6 GLN 0.0 0.0 88.2 7 ILE 123.2 85.9 46.2 8 ARG 1.3 0.6 91.9 9 GLY 2.6 7.4 79.2 10 ARG 49.3 23.6 76.4 11 GLU 13.7 9.9 84.1 12 ARG 74.1 35.5 69.1 13 PHE 82.6 49.5 64.5 14 GLU 60.7 43.8 74.5 15 MET 64.7 40.6 64.0 16 PHE 90.8 54.4 51.7 17 ARG 74.8 35.8 72.4 18 GLU 14.9 10.7 84.9 19 LEU 47.3 32.0 67.4 20 ASN 48.1 39.8 74.8 21 GLU 65.5 47.2 77.1 22 ALA 23.4 32.2 72.2 23 LEU 37.8 25.6 77.8 24 GLU 36.6 26.4 83.9 25 LEU 33.6 22.8 81.1 26 LYS 65.4 37.7 82.2 27 ASP 19.7 17.9 78.1 28 ALA 15.0 20.7 76.8 29 GLN 32.2 21.7 78.0 30 ALA 18.1 24.9 83.6 31 GLY 0.0 0.0 82.3