Protein Data Bank File : 1wdca Title : MUSCLE PROTEIN 19-JAN-96 1WDC Number of Amino Acid Residues : 64 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ARG ASP GLU ARG LEU SER LYS ILE ILE SER 10 MET PHE GLN ALA HIS ILE ARG GLY TYR LEU 20 ILE ARG LYS ALA TYR LYS LYS LEU GLN ASP 30 GLN ARG ILE GLY LEU SER VAL ILE GLN ARG 40 ASN ILE ARG LYS TRP LEU VAL LEU ARG ASN 50 TRP GLN TRP TRP LYS LEU TYR SER LYS VAL 60 LYS PRO LEU LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ARG 0.0 47.6 -170.7 -111.7 101.0 64.9 -163.8 2 ASP -102.6 -61.8 -175.2 160.3 39.1 3 GLU -48.6 -34.0 -179.1 -124.8 170.9 -80.2 4 ARG -78.1 -38.0 177.1 -170.9 -161.3 168.7 -149.0 5 LEU -66.1 -32.9 -178.3 162.5 80.9 6 SER -76.0 -40.5 174.3 44.3 7 LYS -63.1 -36.6 -176.8 178.0 -154.1 35.3 74.2 8 ILE -72.2 -34.6 175.6 -65.9 163.7 9 ILE -66.8 -45.2 172.0 -64.4 -47.8 10 SER -54.4 -43.0 172.8 -61.4 11 MET -68.8 -29.8 169.7 -61.6 -171.5 -59.7 12 PHE -70.9 -42.0 173.2 -169.6 67.9 13 GLN -60.0 -32.1 174.1 -82.7 157.7 -19.8 14 ALA -66.4 -45.0 167.0 15 HIS -52.6 -39.4 -176.2 -109.5 101.5 16 ILE -72.7 -43.9 174.2 -62.0 -178.6 17 ARG -60.8 -34.8 172.7 -57.9 -164.3 -140.6 -89.5 18 GLY -60.2 -54.2 -175.6 19 TYR -53.5 -44.2 -174.9 -177.7 -68.6 20 LEU -68.6 -45.8 167.1 -68.6 -163.5 21 ILE -57.4 -51.2 -176.9 -61.2 -42.9 22 ARG -67.8 -26.5 173.0 -65.1 -165.2 -80.2 -84.4 23 LYS -65.1 -44.2 -169.6 175.0 67.3 -145.1 174.3 24 ALA -76.2 -16.2 -173.5 25 TYR -60.1 -55.9 -170.7 -171.6 60.6 26 LYS -63.3 -25.2 178.8 -78.4 79.0 -171.3 179.3 27 LYS -77.8 -37.9 170.6 -152.9 -154.1 -159.4 159.5 28 LEU -55.6 -48.0 -176.3 -78.2 -162.1 29 GLN -63.4 -42.4 -177.2 -68.4 -179.6 -55.7 30 ASP -65.1 -37.9 -170.1 -71.9 -31.1 31 GLN -79.9 -29.2 170.2 -87.0 175.2 -19.7 32 ARG -54.6 -42.8 176.1 -174.3 -131.2 -85.3 120.5 33 ILE -62.9 -48.1 175.6 -74.7 168.9 34 GLY -58.2 -43.4 -174.1 35 LEU -75.1 -29.0 173.4 178.7 57.5 36 SER -67.4 -51.1 173.6 -71.0 37 VAL -50.4 -40.9 -176.5 173.6 38 ILE -74.0 -47.1 179.9 -71.2 159.6 39 GLN -64.1 -38.0 -176.4 -92.3 172.1 -7.4 40 ARG -82.4 -28.3 177.7 77.9 160.8 172.0 -91.8 41 ASN -82.0 -33.6 169.7 -83.5 -85.8 42 ILE -60.6 -41.1 177.8 -67.8 179.2 43 ARG -67.0 -38.5 165.9 -77.5 176.3 159.6 127.5 44 LYS -55.0 -38.7 179.0 -70.8 -115.4 131.6 129.3 45 TRP -67.6 -48.4 176.8 177.1 68.1 46 LEU -57.2 -41.2 177.1 -61.2 170.3 47 VAL -64.0 -44.9 -179.6 149.0 48 LEU -62.9 -31.7 -172.5 -169.7 58.1 49 ARG -73.3 -15.5 179.1 -94.6 -148.5 116.2 67.3 50 ASN -114.5 8.5 174.1 -110.9 67.1 51 TRP -83.3 122.8 -176.7 -175.9 51.7 52 GLN -53.6 -42.0 173.9 -77.6 -67.9 -5.7 53 TRP -57.5 -43.4 174.4 -73.6 109.7 54 TRP -62.4 -52.9 173.7 -163.5 -106.2 55 LYS -49.7 -41.6 179.1 -64.3 -164.2 -134.2 -174.1 56 LEU -71.2 -56.3 177.3 167.7 62.6 57 TYR -49.3 -38.2 -176.4 -179.2 77.1 58 SER -67.3 -28.2 175.5 -63.7 59 LYS -81.9 -24.4 179.2 -56.6 159.5 146.9 -61.5 60 VAL -93.5 -10.4 176.7 -175.4 61 LYS -57.9 -43.9 175.2 -105.4 -74.3 -96.8 -58.2 62 PRO -63.7 -45.2 -172.0 -29.5 41.1 63 LEU -64.9 -17.7 -172.3 -45.5 -148.1 64 LEU -67.3 -12.7 0.0 -40.1 166.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ARG -31.385 8.882 91.101 2 ASP -27.627 8.302 90.918 3 GLU -26.679 6.826 87.584 4 ARG -28.594 9.748 86.200 5 LEU -26.897 12.251 88.437 6 SER -23.618 10.734 87.253 7 LYS -24.579 10.784 83.603 8 ILE -25.658 14.434 84.057 9 ILE -22.336 15.413 85.674 10 SER -20.370 13.756 82.819 11 MET -22.359 15.835 80.251 12 PHE -21.635 19.020 82.275 13 GLN -17.983 18.020 82.403 14 ALA -18.375 17.589 78.611 15 HIS -19.560 21.162 78.233 16 ILE -16.474 22.233 80.164 17 ARG -13.952 20.317 78.001 18 GLY -15.709 21.981 75.109 19 TYR -15.362 25.493 76.537 20 LEU -11.637 24.931 77.199 21 ILE -10.806 23.588 73.713 22 ARG -12.764 26.342 71.949 23 LYS -11.035 28.881 74.148 24 ALA -7.685 27.315 73.137 25 TYR -8.556 27.272 69.469 26 LYS -7.824 30.851 68.638 27 LYS -4.398 30.652 70.238 28 LEU -3.451 27.560 68.242 29 GLN -4.393 29.374 65.020 30 ASP -2.403 32.499 65.861 31 GLN 0.528 30.336 66.841 32 ARG 0.387 28.292 63.718 33 ILE 1.126 31.583 61.952 34 GLY 3.969 32.338 64.297 35 LEU 5.650 28.904 64.010 36 SER 5.338 28.974 60.207 37 VAL 6.966 32.391 60.061 38 ILE 9.840 31.095 62.258 39 GLN 10.246 27.787 60.371 40 ARG 10.265 29.306 56.874 41 ASN 12.569 32.194 57.704 42 ILE 15.202 30.108 59.540 43 ARG 15.273 27.986 56.380 44 LYS 15.781 30.972 54.058 45 TRP 18.730 31.711 56.313 46 LEU 20.096 28.231 56.012 47 VAL 19.772 28.472 52.208 48 LEU 21.443 31.852 52.185 49 ARG 24.269 30.508 54.359 50 ASN 25.316 27.997 51.685 51 TRP 24.908 30.255 48.694 52 GLN 28.409 30.878 47.289 53 TRP 27.733 34.581 46.547 54 TRP 26.716 35.061 50.219 55 LYS 29.758 33.115 51.372 56 LEU 31.873 35.400 49.205 57 TYR 30.189 38.646 50.257 58 SER 30.476 37.542 53.890 59 LYS 34.310 37.295 53.764 60 VAL 34.751 40.685 52.017 61 LYS 32.258 42.239 54.482 62 PRO 35.059 42.800 57.089 63 LEU 37.799 44.227 54.839 64 LEU 35.683 47.180 53.752 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C H 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 H 30 H H H H H H H H H H 40 H H H H H H H H H H 50 H/H H H H H H H H H H 60 H/S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h 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 H H H H H H H H 40 H H H H H H H H H h 50 h H H H H H H H H H 60 h T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ARG 7.2 3.5 91.8 2 ASP 12.8 11.6 77.4 3 GLU 0.0 0.0 92.5 4 ARG 60.5 29.0 69.5 5 LEU 45.2 30.6 70.5 6 SER 33.8 40.5 70.9 7 LYS 68.6 39.6 66.2 8 ILE 78.6 54.7 67.0 9 ILE 64.3 44.8 67.2 10 SER 26.7 32.0 80.2 11 MET 61.2 38.4 70.9 12 PHE 44.4 26.6 71.9 13 GLN 68.7 46.2 68.5 14 ALA 27.6 38.0 75.4 15 HIS 22.8 15.2 82.6 16 ILE 64.8 45.2 58.3 17 ARG 44.1 21.1 78.7 18 GLY 21.3 61.1 74.3 19 TYR 35.5 19.6 76.6 20 LEU 48.9 33.1 67.6 21 ILE 25.7 17.9 77.5 22 ARG 63.2 30.3 74.6 23 LYS 27.9 16.1 81.6 24 ALA 27.7 38.1 68.3 25 TYR 76.3 42.1 72.3 26 LYS 44.9 25.9 80.7 27 LYS 34.1 19.7 86.0 28 LEU 32.7 22.1 80.9 29 GLN 83.3 56.1 68.0 30 ASP 23.0 20.8 72.0 31 GLN 52.7 35.4 70.0 32 ARG 57.5 27.5 79.1 33 ILE 33.9 23.6 77.2 34 GLY 5.9 17.0 66.4 35 LEU 50.8 34.4 75.6 36 SER 39.2 46.9 76.4 37 VAL 58.8 49.5 73.3 38 ILE 46.0 32.1 63.3 39 GLN 57.8 38.9 71.4 40 ARG 71.3 34.1 73.2 41 ASN 50.9 42.1 69.5 42 ILE 53.8 37.5 60.6 43 ARG 59.2 28.3 75.1 44 LYS 23.9 13.8 85.3 45 TRP 79.0 38.5 66.6 46 LEU 61.5 41.6 61.1 47 VAL 10.8 9.1 81.0 48 LEU 80.9 54.8 54.0 49 ARG 82.4 39.5 73.1 50 ASN 24.1 19.9 84.6 51 TRP 78.4 38.2 65.0 52 GLN 25.7 17.3 78.8 53 TRP 40.9 20.0 71.1 54 TRP 125.2 61.1 57.5 55 LYS 99.3 57.3 77.3 56 LEU 53.1 35.9 64.0 57 TYR 72.8 40.2 64.3 58 SER 48.4 57.8 60.3 59 LYS 30.8 17.7 79.8 60 VAL 52.6 44.3 56.8 61 LYS 78.4 45.2 63.2 62 PRO 48.5 39.0 74.4 63 LEU 27.3 18.5 79.4 64 LEU 57.7 39.1 73.2