Protein Data Bank File : 1dqc Title : ANTIMICROBIAL PROTEIN 04-JAN-00 1DQC Number of Amino Acid Residues : 73 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 TYR LEU ALA PHE ARG CYS GLY ARG TYR SER 10 PRO CYS LEU ASP ASP GLY PRO ASN VAL ASN 20 LEU TYR SER CYS CYS SER PHE TYR ASN CYS 30 HIS LYS CYS LEU ALA ARG LEU GLU ASN CYS 40 PRO LYS GLY LEU HIS TYR ASN ALA TYR LEU 50 LYS VAL CYS ASP TRP PRO SER LYS ALA GLY 60 CYS THR SER VAL ASN LYS GLU CYS HIS LEU 70 TRP LYS THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 TYR 0.0 -19.4 -180.0 179.4 63.5 2 LEU 44.0 83.9 -179.8 -149.9 -52.1 3 ALA -90.3 13.9 -180.0 4 PHE -126.5 -79.8 -179.8 21.9 -72.4 5 ARG 57.6 15.4 179.9 178.4 46.4 48.9 -159.1 6 CYS -98.6 -9.9 179.6 -115.7 7 GLY 85.8 -146.8 179.8 8 ARG -59.9 -12.5 -179.8 -179.9 130.3 161.2 -73.2 9 TYR -86.9 7.5 179.8 -44.5 142.4 10 SER -156.0 48.1 179.7 56.1 11 PRO -76.4 3.8 -179.5 25.1 -27.5 12 CYS -113.9 -174.3 179.2 -40.4 13 LEU -117.9 -13.5 179.8 -99.9 173.4 14 ASP -134.8 -137.0 179.9 61.7 -6.4 15 ASP -136.5 135.6 180.0 57.9 -99.9 16 GLY 145.2 174.0 180.0 17 PRO -72.5 134.9 179.8 24.6 -29.7 18 ASN -138.3 166.2 179.9 -112.3 -65.5 19 VAL -76.0 133.0 179.9 62.6 20 ASN -80.2 147.8 -179.9 59.3 87.1 21 LEU -109.8 4.4 -179.8 -84.3 -58.4 22 TYR -130.0 -73.4 -179.9 -64.1 -112.8 23 SER -56.1 164.2 -180.0 -138.8 24 CYS -124.9 -17.2 179.2 174.6 25 CYS -106.5 -37.6 179.0 -73.5 26 SER -103.3 116.0 -179.3 -125.4 27 PHE -79.8 -166.4 -178.3 91.6 143.5 28 TYR -109.3 120.8 177.4 -90.9 -150.8 29 ASN -103.8 108.3 -177.7 -148.4 91.8 30 CYS -78.9 126.1 179.8 -43.5 31 HIS -145.4 97.8 -179.2 146.1 -149.0 32 LYS 49.7 -138.8 178.8 -156.9 -140.9 -70.8 147.7 33 CYS -84.2 47.0 -179.5 -149.8 34 LEU -154.5 127.8 179.5 -120.3 175.2 35 ALA -117.7 91.2 -179.8 36 ARG -79.1 122.1 -179.7 -146.6 167.7 173.6 -61.7 37 LEU -79.1 163.1 -179.7 -59.8 114.4 38 GLU -136.6 104.5 -179.8 -71.8 -68.5 -35.5 39 ASN -77.7 133.8 179.7 172.6 11.7 40 CYS -74.1 166.9 -179.7 -62.7 41 PRO -73.3 148.8 180.0 24.8 -28.8 42 LYS 59.0 47.1 180.0 -133.6 133.8 106.2 75.1 43 GLY 43.6 52.8 -179.9 44 LEU -95.7 163.0 179.6 -85.0 164.6 45 HIS -100.3 148.1 -179.8 179.9 -152.8 46 TYR -83.4 129.7 179.4 -126.9 -84.5 47 ASN -80.0 90.6 -179.6 -129.0 -36.6 48 ALA -53.9 -21.3 -179.8 49 TYR -78.8 -12.1 -179.9 176.8 -115.9 50 LEU -138.3 10.2 -179.8 -48.6 101.5 51 LYS 53.6 26.6 -179.7 -172.0 -142.8 -48.4 -120.5 52 VAL -122.6 -158.1 -179.9 -52.6 53 CYS -123.5 167.5 -180.0 -80.4 54 ASP 177.2 151.6 -180.0 -138.9 -137.7 55 TRP -42.9 160.5 -180.0 -77.5 112.8 56 PRO -72.8 -10.2 179.9 24.6 -29.2 57 SER -90.1 -11.2 -179.9 35.8 58 LYS -116.7 -37.5 180.0 -45.0 170.3 145.0 119.3 59 ALA -71.3 -3.0 179.9 60 GLY 50.1 87.7 -179.9 61 CYS -88.9 101.4 179.8 -125.1 62 THR -110.8 15.8 -180.0 51.2 63 SER -69.5 138.8 180.0 -37.4 64 VAL -45.4 -33.8 -180.0 162.6 65 ASN -96.2 95.3 -180.0 -142.8 20.7 66 LYS -80.2 -36.6 -180.0 -52.1 -78.2 169.3 117.0 67 GLU -80.4 77.5 -179.9 52.3 157.2 -37.1 68 CYS -62.6 -25.2 179.9 72.5 69 HIS -67.3 59.9 -180.0 57.1 -89.6 70 LEU -119.5 -12.9 -180.0 -89.1 171.0 71 TRP -155.0 -161.7 -179.9 44.2 43.0 72 LYS -117.6 87.2 179.9 -49.1 122.2 -64.3 -174.0 73 THR 37.9 21.7 0.0 -170.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 TYR -22.615 5.136 4.017 2 LEU -18.903 6.026 4.249 3 ALA -17.675 3.035 6.288 4 PHE -14.193 4.589 6.630 5 ARG -13.871 8.386 6.984 6 CYS -10.452 7.609 8.506 7 GLY -8.468 8.868 5.480 8 ARG -5.320 6.986 4.387 9 TYR -5.829 4.987 7.607 10 SER -8.939 3.305 6.137 11 PRO -8.490 2.908 2.380 12 CYS -10.000 -0.595 2.701 13 LEU -13.435 -2.001 3.594 14 ASP -12.331 -4.773 5.983 15 ASP -9.067 -5.743 7.737 16 GLY -5.864 -7.260 6.301 17 PRO -2.908 -6.536 4.018 18 ASN -3.839 -4.767 0.754 19 VAL -2.064 -3.215 -2.254 20 ASN -1.152 0.458 -1.722 21 LEU -2.220 2.988 -4.380 22 TYR 0.177 5.775 -3.329 23 SER 3.328 4.776 -1.412 24 CYS 5.776 2.413 -3.178 25 CYS 7.836 1.003 -0.286 26 SER 5.180 0.810 2.452 27 PHE 2.007 -1.011 1.355 28 TYR -1.410 -0.683 3.040 29 ASN -2.293 -2.783 6.105 30 CYS -6.056 -2.492 6.725 31 HIS -7.009 -2.597 10.425 32 LYS -10.450 -1.280 11.466 33 CYS -10.398 2.525 11.082 34 LEU -6.596 2.401 10.746 35 ALA -4.315 1.544 7.810 36 ARG -0.748 0.991 9.041 37 LEU 1.648 0.914 6.077 38 GLU 4.615 -1.500 6.000 39 ASN 7.863 -0.490 4.257 40 CYS 9.945 -3.435 2.984 41 PRO 13.622 -3.841 3.893 42 LYS 16.221 -2.081 1.710 43 GLY 13.609 0.326 0.294 44 LEU 11.788 -2.656 -1.255 45 HIS 8.240 -2.632 -2.685 46 TYR 5.433 -4.805 -1.266 47 ASN 4.135 -7.465 -3.680 48 ALA 0.371 -6.869 -3.357 49 TYR 0.003 -10.086 -5.388 50 LEU 1.645 -12.072 -2.558 51 LYS 1.293 -9.795 0.496 52 VAL 5.118 -9.896 0.605 53 CYS 8.005 -7.621 -0.462 54 ASP 10.273 -7.394 -3.530 55 TRP 12.417 -4.909 -5.496 56 PRO 10.498 -2.100 -7.200 57 SER 11.313 -3.733 -10.560 58 LYS 9.353 -6.906 -9.711 59 ALA 6.646 -5.763 -7.259 60 GLY 5.429 -3.426 -10.033 61 CYS 5.036 -0.128 -8.140 62 THR 2.085 1.693 -9.747 63 SER 1.129 3.698 -6.636 64 VAL 0.594 7.417 -7.301 65 ASN 3.520 7.950 -4.891 66 LYS 6.575 6.365 -6.562 67 GLU 9.137 8.197 -4.396 68 CYS 8.443 6.313 -1.142 69 HIS 11.658 7.840 0.256 70 LEU 9.633 10.785 1.613 71 TRP 9.342 9.813 5.299 72 LYS 10.248 7.081 7.820 73 THR 7.820 4.138 7.464 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C C C T T T T C 10 S S S S/S S S S/S S S S 20 S C T T T T/S S S S S 30 S/T T T T/S S S S S S S/T 40 T T T/S S S S S/T T T T 50 S S S S S/H H H H H H 60 C C C C C C C C C C 70 S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S g G G G g 10 S S S S E E E 20 S S S e E E E E E 30 E T T E E E E E E e 40 T T t E E e T T T 50 t e E E t T T T T T 60 t S S t T T 70 t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 TYR 0.0 0.0 88.0 2 LEU 92.0 62.3 65.0 3 ALA 40.1 55.2 51.6 4 PHE 92.0 55.2 64.7 5 ARG 47.1 22.5 77.4 6 CYS 74.2 74.8 59.3 7 GLY 0.0 0.0 85.4 8 ARG 141.4 67.7 46.8 9 TYR 68.4 37.8 70.9 10 SER 77.1 92.3 53.0 11 PRO 89.3 71.7 51.8 12 CYS 85.7 86.3 54.6 13 LEU 27.0 18.3 73.9 14 ASP 27.4 24.8 80.6 15 ASP 22.1 20.0 77.1 16 GLY 15.2 43.6 65.4 17 PRO 89.4 71.8 53.3 18 ASN 60.1 49.7 65.8 19 VAL 53.4 44.9 64.2 20 ASN 120.8 99.9 48.0 21 LEU 56.5 38.2 65.9 22 TYR 72.0 39.8 65.5 23 SER 83.6 100.0 52.9 24 CYS 90.9 91.6 46.1 25 CYS 89.5 90.2 49.8 26 SER 81.6 97.6 56.5 27 PHE 163.3 97.9 45.6 28 TYR 174.7 96.5 35.6 29 ASN 74.7 61.8 53.2 30 CYS 97.3 98.1 52.8 31 HIS 72.9 48.5 66.0 32 LYS 28.6 16.5 80.1 33 CYS 50.4 50.9 59.4 34 LEU 66.5 45.0 70.7 35 ALA 72.6 99.9 52.1 36 ARG 54.7 26.2 84.9 37 LEU 123.7 83.7 61.5 38 GLU 80.6 58.1 69.3 39 ASN 79.3 65.6 67.2 40 CYS 97.8 98.6 47.4 41 PRO 32.1 25.8 67.2 42 LYS 31.2 18.0 74.2 43 GLY 11.3 32.5 75.8 44 LEU 124.5 84.2 44.0 45 HIS 144.7 96.3 56.9 46 TYR 144.9 80.1 48.3 47 ASN 99.5 82.3 54.3 48 ALA 54.7 75.4 57.5 49 TYR 10.6 5.8 83.1 50 LEU 70.1 47.5 65.3 51 LYS 54.7 31.5 67.3 52 VAL 51.6 43.4 67.7 53 CYS 77.5 78.1 44.1 54 ASP 65.4 59.2 59.2 55 TRP 97.8 47.7 68.4 56 PRO 69.1 55.5 61.4 57 SER 16.5 19.7 71.0 58 LYS 61.0 35.2 82.2 59 ALA 72.6 100.0 63.4 60 GLY 0.0 0.0 79.3 61 CYS 91.7 92.5 52.9 62 THR 13.6 12.7 83.3 63 SER 82.1 98.2 67.5 64 VAL 16.4 13.8 74.3 65 ASN 88.7 73.4 50.1 66 LYS 66.1 38.1 76.8 67 GLU 64.6 46.6 69.1 68 CYS 83.7 84.4 56.3 69 HIS 26.5 17.7 76.4 70 LEU 81.8 55.3 75.9 71 TRP 118.2 57.7 75.7 72 LYS 9.3 5.4 81.2 73 THR 38.1 35.6 74.4