Protein Data Bank File : 1bk8 Title : PLANT DEFENSIN 15-JUL-98 1BK8 Number of Amino Acid Residues : 50 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU CYS ASN GLU ARG PRO SER GLN THR TRP 10 SER GLY ASN CYS GLY ASN THR ALA HIS CYS 20 ASP LYS GLN CYS GLN ASP TRP GLU LYS ALA 30 SER HIS GLY ALA CYS HIS LYS ARG GLU ASN 40 HIS TRP LYS CYS PHE CYS TYR PHE ASN CYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 114.8 -169.7 -147.4 -177.1 2 CYS -78.0 79.9 -174.6 -36.7 3 ASN -73.3 109.0 -178.5 -48.0 -17.2 4 GLU -73.8 90.0 -177.2 -175.6 -123.1 41.9 5 ARG -98.1 139.9 -175.2 -168.8 -168.0 -65.1 164.6 6 PRO -67.7 172.0 -179.1 24.4 -33.0 7 SER -55.0 105.5 170.0 43.8 8 GLN -84.9 -61.5 -177.1 -71.6 -171.4 -121.8 9 THR -74.8 -53.5 -176.8 38.1 10 TRP -64.7 150.4 -175.2 -158.3 -80.6 11 SER -90.9 -132.0 -177.5 66.0 12 GLY -61.8 -95.4 -170.2 13 ASN -92.7 152.6 -172.7 -157.5 77.8 14 CYS -127.1 151.2 179.0 -168.7 15 GLY -156.7 -51.2 175.5 16 ASN -73.8 75.5 -177.9 -166.7 -27.6 17 THR -62.9 -28.7 171.9 -162.9 18 ALA -59.8 -46.1 174.8 19 HIS -63.0 -52.1 178.6 -166.6 -167.8 20 CYS -44.0 -46.4 -174.6 167.4 21 ASP -62.9 -31.2 174.2 176.2 -81.0 22 LYS -85.2 -36.6 -174.2 -49.7 -144.2 97.1 -50.2 23 GLN -79.0 47.5 -170.6 167.3 148.0 -3.6 24 CYS -166.3 -48.5 177.9 -83.8 25 GLN -74.5 -49.0 -172.7 -179.8 -179.5 94.1 26 ASP -85.3 -50.2 -170.1 -74.5 -77.3 27 TRP -73.9 -66.3 167.0 -74.1 35.7 28 GLU -73.9 -142.1 -172.9 -123.0 -66.8 -7.4 29 LYS -160.5 51.7 174.2 -63.6 -63.3 164.4 -83.2 30 ALA -87.2 170.6 167.7 31 SER -67.0 -49.3 174.7 -52.2 32 HIS -161.3 -164.3 173.3 87.0 121.4 33 GLY -145.9 171.0 176.8 34 ALA -165.2 142.0 179.6 35 CYS -73.9 140.6 168.2 -71.7 36 HIS -145.3 149.4 173.1 -38.5 -46.1 37 LYS -83.0 132.1 172.6 -166.7 -162.3 -97.8 -154.2 38 ARG -141.9 128.4 -179.8 -59.5 -70.4 179.3 -104.7 39 GLU 48.6 41.2 -178.5 -62.8 74.5 85.2 40 ASN 62.3 20.4 174.9 -155.8 46.3 41 HIS -118.8 119.8 174.2 -63.0 -69.0 42 TRP -75.3 104.3 177.3 -76.7 81.0 43 LYS -95.8 140.0 159.9 -32.1 -59.4 -66.8 76.4 44 CYS -69.6 106.9 170.7 170.4 45 PHE -88.3 142.2 172.2 -85.4 71.6 46 CYS -97.6 156.0 -173.6 -61.5 47 TYR -134.2 104.1 -175.9 -79.5 79.7 48 PHE -93.7 178.9 164.4 -75.0 76.6 49 ASN 32.2 45.9 -163.8 46.2 -115.7 50 CYS -82.1 104.8 0.0 171.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU -10.061 -5.183 10.552 2 CYS -6.933 -3.762 8.843 3 ASN -6.950 -5.865 5.646 4 GLU -3.431 -5.662 4.210 5 ARG -4.294 -5.527 0.472 6 PRO -1.481 -5.344 -2.160 7 SER -0.492 -2.386 -4.373 8 GLN -3.536 -1.332 -6.445 9 THR -2.442 2.244 -7.250 10 TRP 1.250 1.816 -6.561 11 SER 3.413 0.057 -9.180 12 GLY 6.462 -2.218 -8.724 13 ASN 8.795 -1.200 -5.925 14 CYS 8.079 1.030 -2.862 15 GLY 10.294 3.189 -0.619 16 ASN 8.413 6.402 0.147 17 THR 6.105 4.670 2.631 18 ALA 4.803 8.120 3.657 19 HIS 3.576 8.519 0.070 20 CYS 2.337 4.880 0.011 21 ASP 0.308 5.585 3.131 22 LYS -1.514 8.400 1.290 23 GLN -1.534 6.631 -2.132 24 CYS -4.120 4.198 -0.662 25 GLN -6.090 6.561 1.588 26 ASP -6.558 9.421 -0.918 27 TRP -6.392 7.702 -4.307 28 GLU -8.121 4.442 -3.396 29 LYS -10.149 4.607 -0.124 30 ALA -8.179 2.612 2.436 31 SER -7.582 3.528 6.080 32 HIS -3.884 3.922 5.159 33 GLY -0.924 2.200 3.429 34 ALA 2.653 0.996 4.147 35 CYS 5.601 -0.399 2.066 36 HIS 6.579 -4.115 2.536 37 LYS 8.933 -6.558 0.803 38 ARG 7.263 -9.576 -0.820 39 GLU 9.152 -11.860 -3.279 40 ASN 11.967 -9.250 -3.179 41 HIS 9.575 -6.498 -4.363 42 TRP 8.698 -3.693 -1.937 43 LYS 4.944 -3.192 -2.525 44 CYS 2.926 -0.357 -1.100 45 PHE 0.220 -2.363 0.652 46 CYS -3.044 -0.581 1.426 47 TYR -4.959 -1.263 4.639 48 PHE -8.729 -0.831 4.427 49 ASN -11.626 -0.945 6.929 50 CYS -9.127 -0.925 9.802 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/S S S S/T T T T 10 C S S S S S/H H H H H 20 H H H H H H H S S S 30 S C S S S S S/T T T T/S 40 S S S S/S S S S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E S S S 10 S h H H H H 20 H H H H H h S S 30 S E E E E E E E T T 40 E E E E E E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 8.2 5.5 92.7 2 CYS 55.4 55.9 55.4 3 ASN 52.0 43.0 72.4 4 GLU 90.3 65.1 64.7 5 ARG 116.3 55.7 60.5 6 PRO 48.0 38.5 62.8 7 SER 77.9 93.2 60.5 8 GLN 86.3 58.1 66.6 9 THR 82.9 77.6 50.6 10 TRP 175.5 85.6 61.7 11 SER 2.3 2.8 84.9 12 GLY 0.0 0.0 78.9 13 ASN 46.7 38.7 75.7 14 CYS 98.1 98.9 43.0 15 GLY 0.0 0.0 73.1 16 ASN 33.4 27.6 71.5 17 THR 42.2 39.5 67.9 18 ALA 3.2 4.4 80.3 19 HIS 72.9 48.5 67.8 20 CYS 99.2 100.0 41.5 21 ASP 69.7 63.1 69.1 22 LYS 76.2 43.9 83.6 23 GLN 134.2 90.3 42.9 24 CYS 99.2 100.0 49.4 25 GLN 86.6 58.3 77.8 26 ASP 39.8 36.0 73.3 27 TRP 79.6 38.9 73.7 28 GLU 92.6 66.8 57.4 29 LYS 42.8 24.7 86.7 30 ALA 72.6 100.0 49.3 31 SER 48.0 57.5 65.6 32 HIS 90.2 60.1 60.3 33 GLY 34.8 100.0 44.6 34 ALA 47.4 65.3 61.8 35 CYS 92.6 93.4 46.7 36 HIS 119.9 79.8 57.1 37 LYS 82.7 47.7 70.7 38 ARG 108.1 51.7 71.3 39 GLU 3.2 2.3 78.8 40 ASN 26.8 22.2 77.6 41 HIS 48.8 32.5 74.1 42 TRP 100.5 49.0 66.0 43 LYS 134.4 77.5 58.4 44 CYS 99.1 99.9 34.4 45 PHE 151.4 90.8 51.4 46 CYS 99.1 99.9 45.4 47 TYR 143.5 79.3 51.5 48 PHE 152.0 91.1 66.1 49 ASN 42.3 35.0 81.2 50 CYS 66.5 67.0 59.9