Protein Data Bank File : 1zfd Title : ZINC FINGER DNA BINDING DOMAIN 04-APR-96 1ZFD Number of Amino Acid Residues : 32 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP ARG PRO TYR SER CYS ASP HIS PRO GLY 10 CYS ASP LYS ALA PHE VAL ARG ASN HIS ASP 20 LEU ILE ARG HIS LYS LYS SER HIS GLN GLU 30 LYS ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 40.6 180.0 54.2 -78.0 2 ARG 49.5 65.6 180.0 -76.7 163.7 -72.3 -161.2 3 PRO -58.7 -10.0 180.0 -4.3 5.2 4 TYR -128.9 79.3 180.0 -64.9 -82.1 5 SER -110.4 76.3 180.0 179.6 6 CYS -45.1 148.6 -179.9 163.9 7 ASP -131.3 49.4 179.9 -175.4 18.6 8 HIS -85.6 141.8 -180.0 165.8 94.1 9 PRO -56.2 124.8 -180.0 0.2 -4.0 10 GLY 89.4 13.8 -180.0 11 CYS -91.4 162.6 180.0 -177.6 12 ASP -170.0 40.3 180.0 61.8 -22.9 13 LYS -140.7 104.1 180.0 -47.3 -159.3 -71.6 -176.0 14 ALA -76.3 168.6 -180.0 15 PHE -149.3 160.9 179.9 -65.8 -77.2 16 VAL -120.4 -31.0 180.0 179.7 17 ARG -88.8 178.7 -179.9 -68.2 168.4 -176.4 66.3 18 ASN -94.1 -62.0 -180.0 -177.9 37.6 19 HIS -43.5 -40.3 179.9 110.4 -76.4 20 ASP -51.0 -50.5 -180.0 -67.6 52.2 21 LEU -60.2 -31.1 179.9 -142.0 -62.0 22 ILE -72.7 -44.4 179.9 -50.1 -173.7 23 ARG -76.2 -22.1 -180.0 -54.5 -65.2 -157.7 -179.5 24 HIS -86.1 -39.4 -179.9 162.4 96.5 25 LYS -63.9 -42.9 180.0 175.8 163.1 65.5 47.9 26 LYS -63.1 -10.5 180.0 -70.5 -164.6 -53.8 -162.9 27 SER -77.1 -36.4 180.0 -167.0 28 HIS -59.6 -5.1 -179.9 -78.4 -61.1 29 GLN -91.1 -70.4 -179.9 -169.1 -173.7 -50.4 30 GLU 55.3 156.8 180.0 -80.9 168.9 31.2 31 LYS -86.8 -164.3 -180.0 -66.3 166.2 56.2 39.8 32 ALA 53.5 -171.4 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP -9.157 -13.362 -9.216 2 ARG -8.820 -10.344 -6.946 3 PRO -12.443 -9.180 -7.332 4 TYR -11.210 -5.947 -5.678 5 SER -8.207 -4.573 -7.564 6 CYS -8.384 -0.807 -7.076 7 ASP -6.702 1.121 -9.932 8 HIS -6.009 4.576 -8.498 9 PRO -2.887 6.465 -9.781 10 GLY -0.010 5.788 -7.349 11 CYS -1.712 2.689 -5.922 12 ASP -0.049 -0.620 -5.148 13 LYS -2.245 -2.728 -2.833 14 ALA -4.469 -5.503 -4.185 15 PHE -7.414 -6.951 -2.277 16 VAL -9.691 -10.005 -2.139 17 ARG -12.426 -8.849 0.235 18 ASN -14.906 -5.990 -0.276 19 HIS -14.748 -3.796 2.827 20 ASP -10.986 -3.676 2.301 21 LEU -11.472 -1.853 -0.995 22 ILE -13.839 0.495 0.812 23 ARG -11.418 1.269 3.615 24 HIS -8.566 1.313 1.106 25 LYS -10.233 3.500 -1.528 26 LYS -11.093 6.208 0.987 27 SER -7.358 6.302 1.669 28 HIS -6.485 7.739 -1.733 29 GLN -8.271 10.830 -0.395 30 GLU -6.636 11.840 2.899 31 LYS -6.821 15.430 4.158 32 ALA -4.353 18.254 3.586 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S S S S 10 S S S S S S C H H H 20 H H H H H H H 3 3 3/S 30 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S B t T T 10 t B S S h H H 20 H H H H H h G G g t 30 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 0.0 0.0 86.7 2 ARG 58.8 28.1 72.9 3 PRO 61.7 49.6 73.3 4 TYR 117.3 64.8 62.7 5 SER 32.8 39.3 74.6 6 CYS 82.9 83.6 49.4 7 ASP 0.0 0.0 86.9 8 HIS 86.2 57.4 58.0 9 PRO 16.0 12.9 83.5 10 GLY 0.0 0.0 85.4 11 CYS 89.4 90.1 63.9 12 ASP 10.2 9.2 76.9 13 LYS 62.6 36.1 77.2 14 ALA 31.6 43.5 66.1 15 PHE 131.2 78.7 55.9 16 VAL 33.0 27.7 70.8 17 ARG 49.6 23.8 80.8 18 ASN 48.5 40.1 63.0 19 HIS 48.6 32.4 67.6 20 ASP 79.2 71.6 52.0 21 LEU 123.9 83.9 42.8 22 ILE 65.6 45.7 72.0 23 ARG 66.3 31.7 78.2 24 HIS 138.6 92.3 39.4 25 LYS 62.0 35.8 65.6 26 LYS 73.1 42.2 78.7 27 SER 39.2 46.9 80.0 28 HIS 114.8 76.4 57.6 29 GLN 19.5 13.1 85.3 30 GLU 22.4 16.2 87.9 31 LYS 5.8 3.4 89.3 32 ALA 0.0 0.0 87.0