Protein Data Bank File : 1bkra Title : ACTIN-BINDING 10-JUL-98 1BKR Number of Amino Acid Residues : 108 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS SER ALA LYS ASP ALA LEU LEU LEU TRP 10 CYS GLN MET LYS THR ALA GLY TYR PRO ASN 20 VAL ASN ILE HIS ASN PHE THR THR SER TRP 30 ARG ASP GLY MET ALA PHE ASN ALA LEU ILE 40 HIS LYS HIS ARG PRO ASP LEU ILE ASP PHE 50 ASP LYS LEU LYS LYS SER ASN ALA HIS TYR 60 ASN LEU GLN ASN ALA PHE ASN LEU ALA GLU 70 GLN HIS LEU GLY LEU THR LYS LEU LEU ASP 80 PRO GLU ASP ILE SER VAL ASP HIS PRO ASP 90 GLU LYS SER ILE ILE THR TYR VAL VAL THR 100 TYR TYR HIS TYR PHE SER LYS MET Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 -40.4 -178.8 179.8 -144.9 126.7 -126.8 2 SER -66.1 -40.2 179.5 -175.6 3 ALA -63.1 -42.6 179.1 4 LYS -66.9 -44.4 177.0 -108.2 -172.2 55.9 153.3 5 ASP -61.4 -41.3 179.4 -76.4 -6.8 6 ALA -62.4 -41.6 -179.2 7 LEU -66.6 -40.6 178.2 -174.0 68.2 8 LEU -59.6 -47.8 179.8 -177.2 68.6 9 LEU -62.1 -41.2 178.2 -176.5 67.4 10 TRP -55.8 -47.9 -180.0 178.7 88.5 11 CYS -60.9 -44.1 -180.0 -69.7 12 GLN -62.1 -41.8 -175.2 -66.0 168.7 -26.7 13 MET -72.4 -36.5 -179.9 -61.0 -168.5 -60.4 14 LYS -68.9 -30.2 -171.5 -72.2 -51.2 172.0 -165.2 15 THR -105.7 15.7 178.8 60.5 16 ALA -57.1 136.9 179.9 17 GLY 77.5 -3.7 177.0 18 TYR -73.7 128.5 176.7 -81.4 70.3 19 PRO -65.9 143.7 173.6 -10.2 22.7 20 ASN 60.6 31.8 168.4 -68.0 -61.0 21 VAL -123.4 126.0 -179.8 173.2 22 ASN -143.1 97.6 -172.6 -120.9 -108.1 23 ILE -101.4 112.9 -178.3 -54.1 171.0 24 HIS -128.3 -5.6 -175.9 -68.2 108.6 25 ASN -162.8 -177.1 177.5 58.6 54.0 26 PHE -113.4 32.5 175.4 -79.1 -63.9 27 THR -135.1 -91.8 -173.9 59.5 28 THR -62.6 -24.5 176.8 56.0 29 SER -67.0 -10.3 -173.2 -61.8 30 TRP -113.8 -11.5 -166.9 -59.7 84.7 31 ARG -69.2 -20.2 -178.8 73.1 144.0 -90.3 -56.1 32 ASP -94.7 1.3 177.1 67.2 22.8 33 GLY 79.4 -9.8 -176.4 34 MET -65.5 -42.6 -178.9 -65.6 -69.2 -78.6 35 ALA -62.4 -40.7 178.9 36 PHE -62.0 -43.1 178.8 -69.7 -64.6 37 ASN -62.6 -39.1 179.9 -80.0 -85.0 38 ALA -65.3 -40.2 179.1 39 LEU -62.4 -42.5 177.4 -76.4 177.8 40 ILE -64.3 -45.8 -176.6 -62.7 168.3 41 HIS -60.1 -39.8 -178.0 -178.8 91.2 42 LYS -55.5 -37.4 -175.7 179.6 64.6 152.6 -179.7 43 HIS -94.1 -32.9 -174.5 -60.3 94.2 44 ARG -136.1 70.4 -178.2 -71.7 -68.4 -55.8 -89.5 45 PRO -65.0 -19.0 176.0 21.2 -32.5 46 ASP -64.5 -19.5 -173.8 55.3 -41.6 47 LEU -91.9 -17.0 -172.8 -69.0 179.8 48 ILE -138.1 130.3 170.6 -73.0 144.4 49 ASP -92.9 84.2 -170.4 -170.7 -13.5 50 PHE -57.4 -35.9 -176.7 -170.3 84.1 51 ASP -58.7 -20.9 -175.7 -16.3 -12.7 52 LYS -84.4 -17.6 -174.2 -59.4 -74.6 -167.0 -78.3 53 LEU -80.7 147.1 176.1 -58.0 178.0 54 LYS -131.3 142.1 -177.1 -59.9 -134.8 -154.8 -54.3 55 LYS -56.2 -32.5 -176.4 -71.8 -174.1 -44.0 -152.5 56 SER -63.4 -21.9 -173.9 60.7 57 ASN -99.5 65.9 -172.3 -51.0 -54.1 58 ALA -58.1 -49.7 -175.5 59 HIS -59.9 -48.2 -179.4 -168.4 101.6 60 TYR -57.1 -48.8 -174.3 179.6 84.4 61 ASN -63.5 -46.0 179.2 -63.9 -19.0 62 LEU -59.8 -52.5 179.5 -69.2 161.2 63 GLN -59.2 -38.1 -178.9 -176.5 178.8 19.6 64 ASN -60.7 -52.0 -179.2 -169.3 62.2 65 ALA -63.9 -44.1 -175.4 66 PHE -64.4 -44.4 -177.9 -61.7 -13.9 67 ASN -69.5 -42.6 -179.7 -77.0 -9.5 68 LEU -65.0 -40.9 -179.6 -72.3 172.4 69 ALA -64.0 -37.9 178.3 70 GLU -66.0 -51.1 -169.8 -167.1 152.5 76.4 71 GLN -72.3 -40.7 -174.8 -71.3 -75.8 -42.6 72 HIS -99.8 -28.7 -179.3 -66.1 95.1 73 LEU -106.9 -6.9 -179.0 -46.2 176.9 74 GLY 74.3 16.4 -176.8 75 LEU -91.5 118.6 -172.5 -65.7 176.3 76 THR -66.7 148.9 -176.4 132.8 77 LYS -81.0 80.8 -179.5 -74.3 -158.2 -60.3 -162.9 78 LEU -70.2 -26.9 -175.1 -63.2 178.7 79 LEU -108.8 146.5 173.1 -48.1 178.8 80 ASP -100.0 128.3 179.8 -175.6 -29.2 81 PRO -51.1 -37.0 -178.7 -34.0 43.7 82 GLU -64.8 -31.7 175.2 -50.2 -173.7 31.0 83 ASP -74.7 -27.1 -173.4 -65.6 -52.5 84 ILE -91.5 -26.3 -175.9 -54.5 -57.0 85 SER -83.7 2.1 171.7 63.3 86 VAL -64.5 166.8 179.3 -59.8 87 ASP -59.9 -40.1 -176.0 -68.7 -6.9 88 HIS -133.1 81.1 -177.8 -65.0 -70.1 89 PRO -71.0 171.5 -173.2 30.4 -37.1 90 ASP -85.8 122.9 -177.8 177.5 65.0 91 GLU -56.9 -49.2 -173.1 -176.8 -172.8 81.6 92 LYS -60.5 -43.9 -179.6 -179.1 176.9 161.6 111.3 93 SER -60.3 -44.0 179.8 -53.4 94 ILE -65.3 -43.9 178.9 -71.0 167.3 95 ILE -61.0 -43.4 -177.8 -70.7 174.6 96 THR -57.9 -41.5 -179.1 -62.6 97 TYR -71.7 -44.8 178.7 -175.1 67.8 98 VAL -60.0 -35.8 177.4 172.0 99 VAL -59.5 -33.6 178.3 164.0 100 THR -66.0 -35.1 176.3 -99.0 101 TYR -67.5 -47.4 -179.3 -76.8 25.2 102 TYR -57.9 -47.1 180.0 165.6 67.2 103 HIS -64.4 -41.2 -179.3 -70.6 -24.5 104 TYR -65.7 -51.7 -174.3 178.0 88.3 105 PHE -74.0 -26.6 173.6 -67.9 -55.6 106 SER -84.7 -1.0 177.0 -64.7 107 LYS -132.3 143.6 -162.6 -47.7 -166.1 -170.3 162.4 108 MET 69.9 0.5 0.0 154.6 -152.7 14.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 9.296 31.931 19.151 2 SER 9.528 34.697 16.535 3 ALA 11.514 32.340 14.277 4 LYS 8.992 29.521 14.734 5 ASP 6.041 31.858 14.140 6 ALA 7.781 33.240 11.025 7 LEU 8.374 29.710 9.667 8 LEU 4.739 28.784 10.325 9 LEU 3.528 31.905 8.495 10 TRP 5.922 31.246 5.610 11 CYS 4.367 27.767 5.226 12 GLN 0.837 29.185 5.389 13 MET 1.540 31.898 2.798 14 LYS 3.303 29.511 0.342 15 THR 0.461 26.989 0.514 16 ALA -2.467 29.472 0.376 17 GLY -5.353 28.112 -1.659 18 TYR -4.116 24.525 -1.782 19 PRO -7.046 22.223 -1.154 20 ASN -6.856 19.902 1.875 21 VAL -3.835 21.693 3.379 22 ASN -4.451 23.391 6.769 23 ILE -1.236 24.435 8.522 24 HIS -1.715 25.502 12.144 25 ASN 1.190 23.843 13.899 26 PHE 4.375 21.799 13.241 27 THR 2.914 18.426 14.208 28 THR -0.609 17.246 13.238 29 SER -0.826 19.707 10.312 30 TRP 1.985 17.677 8.649 31 ARG 1.151 14.021 9.479 32 ASP -0.848 13.314 6.256 33 GLY 1.923 14.533 3.898 34 MET -0.233 17.034 2.019 35 ALA 1.548 20.142 3.297 36 PHE 5.002 18.863 2.338 37 ASN 3.762 18.137 -1.199 38 ALA 2.125 21.598 -1.443 39 LEU 5.374 23.355 -0.477 40 ILE 7.268 21.488 -3.210 41 HIS 4.514 22.064 -5.773 42 LYS 4.402 25.810 -5.190 43 HIS 8.075 25.995 -6.281 44 ARG 8.355 22.981 -8.603 45 PRO 4.852 22.206 -9.953 46 ASP 6.567 19.954 -12.567 47 LEU 7.334 17.469 -9.797 48 ILE 3.746 16.867 -8.404 49 ASP 0.174 16.313 -9.758 50 PHE -1.177 17.770 -6.590 51 ASP -4.781 17.178 -7.630 52 LYS -4.244 13.413 -7.396 53 LEU -3.270 13.390 -3.711 54 LYS -5.712 12.612 -0.897 55 LYS -5.281 13.174 2.846 56 SER -6.130 9.564 3.688 57 ASN -2.906 8.242 2.099 58 ALA -0.393 9.550 4.624 59 HIS 2.392 7.077 3.910 60 TYR 2.163 7.567 0.118 61 ASN 2.072 11.353 0.426 62 LEU 4.964 11.544 2.899 63 GLN 7.163 9.175 0.887 64 ASN 6.317 11.042 -2.305 65 ALA 7.459 14.423 -0.947 66 PHE 10.501 13.025 0.893 67 ASN 11.738 11.050 -2.109 68 LEU 11.151 13.820 -4.657 69 ALA 12.863 16.400 -2.474 70 GLU 15.881 14.073 -2.031 71 GLN 16.168 13.024 -5.667 72 HIS 15.386 16.322 -7.397 73 LEU 16.226 19.003 -4.803 74 GLY 19.136 17.346 -2.918 75 LEU 17.303 17.677 0.414 76 THR 18.214 14.800 2.695 77 LYS 15.412 12.588 3.931 78 LEU 15.608 13.457 7.612 79 LEU 12.141 12.030 8.331 80 ASP 10.698 8.511 7.960 81 PRO 7.048 8.376 6.877 82 GLU 6.257 5.833 9.589 83 ASP 7.378 8.264 12.300 84 ILE 5.467 11.203 10.870 85 SER 2.123 9.503 10.140 86 VAL 1.461 8.816 13.851 87 ASP -1.305 10.736 15.611 88 HIS 1.195 13.121 17.347 89 PRO 4.512 13.360 15.560 90 ASP 7.481 15.229 17.002 91 GLU 7.563 19.006 16.486 92 LYS 11.352 19.489 16.612 93 SER 12.022 16.823 13.941 94 ILE 9.394 18.312 11.598 95 ILE 10.699 21.890 12.103 96 THR 14.281 20.811 11.368 97 TYR 13.147 19.305 8.059 98 VAL 10.818 22.191 7.117 99 VAL 13.708 24.639 7.756 100 THR 15.672 22.771 5.034 101 TYR 12.763 23.489 2.609 102 TYR 12.617 27.130 3.677 103 HIS 16.382 27.657 3.137 104 TYR 16.338 25.844 -0.214 105 PHE 13.270 27.584 -1.724 106 SER 14.227 30.990 -0.263 107 LYS 17.761 30.957 -1.637 108 MET 18.241 30.468 -5.394 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H H H H H S S S S/S 20 S S S S T T T T/T T T 30 T C H H H H H H H H 40 H H H H/T T T T C T T 50 T T/S S S S C H H H H 60 H H H H H H H H H H 70 H H H S S S S C C H 80 H H H H H 3 S S S S/H 90 H H H H H H H H H H 100 H H H H H H H/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 H 10 H H H H h T T t T T 20 t S S S g G G G 30 g T h H H H H H H H 40 H H H h G G G g g G 50 G G g t T T h H H H 60 H H H H H H H H H H 70 H H H h h 80 H H H H h S S S h 90 H H H H H H H H H H 100 H H H H H h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 25.8 14.9 87.8 2 SER 6.8 8.2 83.8 3 ALA 0.0 0.0 83.3 4 LYS 89.7 51.7 67.0 5 ASP 45.0 40.7 65.7 6 ALA 16.9 23.3 77.5 7 LEU 135.0 91.4 35.5 8 LEU 110.8 75.0 59.6 9 LEU 57.0 38.6 68.3 10 TRP 178.0 86.8 41.2 11 CYS 99.2 100.0 29.7 12 GLN 94.4 63.6 57.9 13 MET 55.4 34.7 67.1 14 LYS 103.5 59.7 58.0 15 THR 103.4 96.7 43.3 16 ALA 14.4 19.8 87.3 17 GLY 0.0 0.0 83.8 18 TYR 156.9 86.7 47.1 19 PRO 35.8 28.7 77.7 20 ASN 47.7 39.5 66.4 21 VAL 114.7 96.5 48.5 22 ASN 23.0 19.0 77.8 23 ILE 142.8 99.5 44.8 24 HIS 48.7 32.4 82.0 25 ASN 67.6 55.9 73.1 26 PHE 163.0 97.7 33.4 27 THR 76.0 71.1 56.4 28 THR 60.7 56.8 73.0 29 SER 72.5 86.7 70.9 30 TRP 205.0 100.0 32.5 31 ARG 135.9 65.0 66.4 32 ASP 90.9 82.3 59.8 33 GLY 34.8 100.0 58.5 34 MET 155.4 97.5 54.6 35 ALA 72.1 99.3 40.7 36 PHE 166.8 100.0 28.5 37 ASN 120.9 100.0 40.1 38 ALA 72.6 100.0 35.3 39 LEU 147.8 100.0 29.4 40 ILE 143.5 100.0 36.5 41 HIS 109.4 72.8 57.8 42 LYS 86.4 49.9 74.0 43 HIS 114.5 76.2 49.3 44 ARG 128.0 61.3 59.8 45 PRO 56.1 45.1 81.0 46 ASP 34.9 31.5 75.6 47 LEU 133.8 90.5 50.8 48 ILE 138.6 96.6 51.0 49 ASP 48.1 43.5 73.8 50 PHE 154.1 92.4 41.3 51 ASP 10.0 9.1 85.2 52 LYS 41.9 24.2 85.4 53 LEU 137.2 92.8 50.4 54 LYS 45.6 26.3 87.8 55 LYS 76.1 43.9 75.2 56 SER 11.1 13.3 82.7 57 ASN 48.6 40.2 77.4 58 ALA 63.9 88.1 65.3 59 HIS 64.9 43.2 67.1 60 TYR 52.0 28.7 73.8 61 ASN 120.5 99.7 49.5 62 LEU 147.8 100.0 40.2 63 GLN 65.1 43.8 72.3 64 ASN 85.8 70.9 55.7 65 ALA 72.6 100.0 55.7 66 PHE 165.9 99.5 36.5 67 ASN 74.5 61.7 67.1 68 LEU 113.1 76.5 59.9 69 ALA 72.6 100.0 50.2 70 GLU 86.3 62.3 65.0 71 GLN 32.5 21.9 80.2 72 HIS 75.9 50.6 61.6 73 LEU 146.7 99.3 39.8 74 GLY 1.4 4.0 81.8 75 LEU 126.0 85.3 43.2 76 THR 23.4 21.9 77.5 77 LYS 99.5 57.4 77.0 78 LEU 81.6 55.2 66.2 79 LEU 139.2 94.2 35.7 80 ASP 46.0 41.6 65.4 81 PRO 104.9 84.3 48.9 82 GLU 26.3 19.0 85.1 83 ASP 25.0 22.7 74.0 84 ILE 139.7 97.3 35.6 85 SER 62.0 74.2 65.6 86 VAL 48.1 40.5 80.6 87 ASP 8.7 7.8 79.7 88 HIS 23.5 15.6 72.0 89 PRO 122.5 98.4 49.4 90 ASP 33.1 30.0 78.5 91 GLU 76.5 55.2 65.1 92 LYS 11.8 6.8 87.8 93 SER 39.0 46.7 63.5 94 ILE 143.5 100.0 33.2 95 ILE 115.7 80.6 41.1 96 THR 41.6 38.9 63.1 97 TYR 180.9 100.0 38.9 98 VAL 118.8 100.0 26.3 99 VAL 71.7 60.4 54.6 100 THR 73.5 68.7 49.4 101 TYR 181.0 100.0 28.8 102 TYR 103.2 57.0 56.0 103 HIS 71.9 47.9 60.6 104 TYR 128.8 71.2 50.6 105 PHE 159.1 95.4 37.3 106 SER 52.3 62.5 65.7 107 LYS 43.4 25.0 82.0 108 MET 37.1 23.3 76.5