Protein Data Bank File : 2a93b Title : LEUCINE ZIPPERS 09-JUN-98 2A93 Number of Amino Acid Residues : 32 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 CYS GLY GLY MET ARG ARG LYS ASN ASP THR 10 HIS GLN GLN ASP ILE ASP ASP LEU LYS ARG 20 GLN ASN ALA LEU LEU GLU GLN GLN VAL ARG 30 ALA LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 CYS 0.0 112.0 -179.9 -55.8 2 GLY -156.8 32.3 -180.0 3 GLY -164.8 32.8 -179.9 4 MET -77.7 -60.9 -179.9 -59.7 164.3 57.5 5 ARG -62.1 -36.8 -179.9 -170.9 -171.6 150.6 -78.1 6 ARG -59.4 -50.0 180.0 -170.4 173.9 -162.4 173.5 7 LYS -72.3 -44.3 -179.9 -87.0 154.3 -172.9 147.4 8 ASN -61.2 -39.8 -180.0 -86.3 -82.8 9 ASP -61.7 -39.3 179.8 -172.1 64.0 10 THR -63.1 -37.1 179.9 -35.5 11 HIS -79.0 -41.5 -179.9 -60.0 -62.4 12 GLN -61.6 -43.4 180.0 -150.0 147.2 69.2 13 GLN -62.1 -53.8 179.9 -165.4 88.8 -57.3 14 ASP -60.5 -41.0 179.7 -149.9 84.8 15 ILE -62.8 -74.5 -178.3 -80.4 -61.7 16 ASP -45.6 -29.8 179.8 -94.1 -42.9 17 ASP -73.9 -38.4 179.9 -172.0 84.9 18 LEU -66.3 -41.3 -180.0 -75.6 162.8 19 LYS -62.9 -41.5 180.0 -84.1 -99.6 99.4 -151.6 20 ARG -61.7 -35.0 -180.0 -81.8 -146.9 -148.2 -70.7 21 GLN -77.7 -50.4 -179.9 -87.4 -81.5 124.5 22 ASN -61.5 -37.9 180.0 -59.1 22.5 23 ALA -61.6 -52.4 179.9 24 LEU -70.0 -30.8 -180.0 -73.3 165.0 25 LEU -60.9 -63.9 -179.9 -88.3 158.6 26 GLU -56.6 -31.6 179.9 57.9 -157.2 79.7 27 GLN -60.2 -32.6 179.9 -153.7 76.9 -28.0 28 GLN -86.5 -33.7 180.0 -76.3 -88.3 87.9 29 VAL -62.4 -34.4 -180.0 -173.0 30 ARG -61.2 -33.8 -180.0 -149.1 94.0 -151.6 -163.5 31 ALA -70.6 -47.3 179.9 32 LEU -88.1 5.7 0.0 -89.0 163.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 CYS -2.263 24.864 1.752 2 GLY -5.060 23.853 -0.613 3 GLY -4.331 20.259 -1.602 4 MET -3.624 18.352 1.606 5 ARG -6.694 16.125 1.812 6 ARG -6.732 15.855 -1.981 7 LYS -3.202 14.457 -2.112 8 ASN -3.519 12.561 1.167 9 ASP -6.786 11.016 -0.015 10 THR -5.047 9.740 -3.142 11 HIS -2.424 8.078 -0.955 12 GLN -4.887 6.944 1.701 13 GLN -7.111 5.341 -0.931 14 ASP -4.248 3.532 -2.663 15 ILE -2.785 2.631 0.725 16 ASP -5.868 1.394 2.579 17 ASP -6.793 -0.393 -0.655 18 LEU -3.447 -2.185 -0.830 19 LYS -3.761 -3.349 2.773 20 ARG -7.240 -4.714 2.096 21 GLN -5.816 -6.713 -0.803 22 ASN -2.606 -7.829 0.896 23 ALA -4.575 -8.684 4.032 24 LEU -7.031 -10.928 2.196 25 LEU -4.235 -12.153 -0.071 26 GLU -1.967 -13.561 2.638 27 GLN -5.108 -14.806 4.386 28 GLN -5.647 -17.152 1.444 29 VAL -1.963 -17.976 1.009 30 ARG -1.924 -19.335 4.559 31 ALA -4.515 -21.907 3.507 32 LEU -2.593 -23.039 0.432 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C H H H H H H 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 H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H 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 T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 CYS 12.4 12.5 80.8 2 GLY 0.0 0.0 81.7 3 GLY 25.0 71.9 68.0 4 MET 39.4 24.7 79.9 5 ARG 26.8 12.8 83.7 6 ARG 18.5 8.9 84.6 7 LYS 35.3 20.3 83.7 8 ASN 35.9 29.7 67.6 9 ASP 54.1 48.9 77.3 10 THR 21.8 20.4 80.7 11 HIS 34.8 23.1 72.8 12 GLN 36.2 24.4 79.9 13 GLN 24.2 16.3 85.4 14 ASP 25.8 23.3 70.4 15 ILE 45.1 31.4 66.3 16 ASP 38.4 34.8 68.6 17 ASP 30.6 27.7 70.6 18 LEU 60.4 40.9 79.6 19 LYS 47.8 27.6 78.7 20 ARG 35.3 16.9 82.3 21 GLN 48.5 32.6 74.2 22 ASN 54.3 44.9 61.2 23 ALA 30.1 41.5 74.7 24 LEU 27.3 18.5 79.9 25 LEU 52.8 35.7 76.2 26 GLU 47.4 34.2 71.3 27 GLN 30.3 20.4 77.2 28 GLN 19.1 12.8 84.4 29 VAL 22.4 18.9 75.5 30 ARG 7.6 3.6 92.1 31 ALA 16.0 22.1 83.4 32 LEU 0.0 0.0 83.2