Protein Data Bank File : 1svq Title : ACTIN-BINDING 12-OCT-94 1SVQ Number of Amino Acid Residues : 94 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU TYR LYS PRO ARG LEU LEU HIS ILE SER 10 GLY ASP LYS ASN ALA LYS VAL ALA GLU VAL 20 PRO LEU ALA THR SER SER LEU ASN SER GLY 30 ASP CYS PHE LEU LEU ASP ALA GLY LEU THR 40 ILE TYR GLN PHE ASN GLY SER LYS SER SER 50 PRO GLN GLU LYS ASN LYS ALA ALA GLU VAL 60 ALA ARG ALA ILE ASP ALA GLU ARG LYS GLY 70 LEU PRO LYS VAL GLU VAL PHE CYS GLU THR 80 ASP SER ASP ILE PRO ALA GLU PHE TRP LYS 90 LEU LEU GLY GLY Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 174.5 -180.0 61.8 157.7 12.7 2 TYR -49.6 170.9 179.9 -48.6 -66.1 3 LYS -111.9 92.5 -179.9 -137.3 -162.4 -108.1 -140.9 4 PRO -77.9 159.6 179.7 22.0 -20.3 5 ARG -140.8 134.3 -179.4 -44.7 -100.3 -107.0 178.4 6 LEU -113.7 111.6 179.4 -79.4 -69.3 7 LEU -107.9 145.2 -176.6 -161.2 -65.3 8 HIS -124.3 135.3 179.3 -178.6 132.2 9 ILE -125.3 96.8 178.4 -37.5 -18.6 10 SER -174.9 171.7 177.8 90.3 11 GLY 165.2 45.5 179.3 12 ASP 37.4 -127.6 179.2 -60.6 36.6 13 LYS -79.9 -21.0 178.0 -109.9 95.6 161.2 124.2 14 ASN -101.6 72.8 -177.6 -124.7 52.3 15 ALA -54.6 145.7 178.3 16 LYS -160.6 140.1 -177.8 36.7 -138.7 -126.5 -94.4 17 VAL -135.9 154.3 -179.7 45.9 18 ALA 178.0 166.2 -179.9 19 GLU -56.8 163.8 -179.5 -148.0 -97.7 3.8 20 VAL -165.7 151.2 179.9 -7.9 21 PRO -76.1 -176.9 179.8 22.6 -22.9 22 LEU -60.5 149.8 177.3 105.4 68.5 23 ALA -175.5 85.6 178.1 24 THR -76.2 -45.7 179.1 -4.6 25 SER -78.1 -50.7 -179.6 28.6 26 SER -68.5 2.9 -179.9 -166.9 27 LEU -51.0 -169.1 180.0 -145.8 109.8 28 ASN -142.1 72.7 178.8 48.6 -80.8 29 SER -57.4 140.4 179.7 172.7 30 GLY 110.6 -28.3 177.7 31 ASP -114.2 -179.1 -177.7 -24.1 83.1 32 CYS -91.2 129.2 -178.3 -81.3 33 PHE -122.0 160.1 -179.6 -150.7 86.6 34 LEU -140.9 118.6 174.7 149.6 72.6 35 LEU -108.3 138.9 179.7 82.6 53.9 36 ASP -109.8 129.8 -178.6 -162.8 -62.5 37 ALA -134.4 103.7 180.0 38 GLY 47.0 -109.5 -179.4 39 LEU -94.7 -23.8 -178.7 -110.8 56.4 40 THR -87.7 165.9 179.9 -37.1 41 ILE -158.0 125.9 -179.6 -76.6 89.9 42 TYR -111.9 101.6 174.8 -59.3 -19.5 43 GLN -71.3 89.9 -180.0 -140.8 -178.3 -57.0 44 PHE -78.5 79.5 180.0 163.9 41.1 45 ASN -66.3 145.9 -178.7 -88.1 22.6 46 GLY -115.0 121.9 -177.9 47 SER -63.5 -13.3 179.8 -110.3 48 LYS -67.6 -9.9 177.8 -71.5 -139.7 104.2 -166.8 49 SER -155.9 120.6 -175.6 36.9 50 SER -110.7 -50.1 -174.7 16.9 51 PRO -69.2 -50.5 -178.9 21.4 -22.5 52 GLN -56.7 -68.8 -179.4 -70.8 5.5 86.1 53 GLU -64.1 -25.9 179.7 60.5 -97.2 -66.1 54 LYS -66.1 -36.5 179.9 166.7 124.9 -72.2 -145.4 55 ASN -75.2 -58.2 179.9 -120.4 -111.4 56 LYS -58.4 -35.1 179.8 -121.2 75.5 102.3 87.6 57 ALA -73.8 -64.0 179.4 58 ALA -42.7 -32.4 177.9 59 GLU -65.6 -52.7 179.8 -159.8 163.6 87.3 60 VAL -60.2 -52.1 -179.2 -177.5 61 ALA -60.3 -31.8 179.8 62 ARG -67.1 -47.6 179.7 -159.9 140.0 -167.4 58.0 63 ALA -60.2 -45.0 179.9 64 ILE -66.5 -27.7 179.8 -44.8 149.1 65 ASP -68.3 -41.6 -179.9 -171.7 -30.4 66 ALA -77.2 -26.2 -179.3 67 GLU -75.3 -45.3 -178.9 -159.6 89.7 7.0 68 ARG -89.2 -4.9 179.5 -49.7 -114.5 120.6 165.5 69 LYS 61.0 29.1 179.1 -33.7 -49.1 -149.2 -80.9 70 GLY 68.8 -1.2 -179.8 71 LEU -48.6 -47.8 -179.1 -145.9 146.9 72 PRO -76.4 160.1 -179.7 21.9 -20.7 73 LYS -96.4 140.1 -179.2 -145.1 176.1 67.3 -169.7 74 VAL -118.8 158.9 179.1 -164.5 75 GLU -141.5 103.1 -176.9 117.9 169.5 -42.7 76 VAL -108.2 137.8 176.0 -177.0 77 PHE -165.0 124.9 179.3 29.5 68.6 78 CYS -99.4 74.0 -175.9 -132.4 79 GLU -107.9 165.7 179.5 154.2 77.2 -26.5 80 THR -124.5 -62.3 179.7 29.7 81 ASP -65.2 151.4 -178.6 19.7 -85.7 82 SER 57.5 10.7 -178.9 171.3 83 ASP -58.1 -8.7 -178.3 49.6 -21.4 84 ILE -118.0 76.7 176.9 -45.4 107.9 85 PRO -79.4 115.2 -178.5 22.0 -18.1 86 ALA -36.7 -25.7 -178.2 87 GLU -69.3 -52.2 -179.8 128.2 72.2 -29.8 88 PHE -72.2 -40.3 -179.3 144.1 45.9 89 TRP -71.7 -26.1 176.6 -62.6 79.6 90 LYS -75.3 -38.7 179.9 168.1 77.8 142.5 104.0 91 LEU -60.0 -61.9 -178.4 -137.2 134.5 92 LEU -88.8 -25.9 -179.2 106.3 66.2 93 GLY -95.2 -38.8 -179.5 94 GLY -88.6 -147.4 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU -11.341 9.816 -4.231 2 TYR -8.988 7.101 -5.537 3 LYS -9.640 3.551 -4.262 4 PRO -6.843 2.634 -1.834 5 ARG -6.436 -0.893 -0.407 6 LEU -4.643 -1.958 2.788 7 LEU -3.233 -5.550 2.780 8 HIS -1.350 -6.882 5.760 9 ILE 1.328 -9.612 5.845 10 SER 2.332 -10.687 9.361 11 GLY 1.713 -12.856 12.432 12 ASP 4.772 -13.223 14.783 13 LYS 5.432 -17.015 14.774 14 ASN 1.838 -17.633 13.599 15 ALA 2.100 -15.704 10.327 16 LYS -1.185 -14.597 8.769 17 VAL -2.000 -12.196 6.006 18 ALA -5.233 -10.735 4.623 19 GLU -7.065 -7.660 3.273 20 VAL -7.482 -4.607 5.502 21 PRO -9.055 -1.109 5.487 22 LEU -7.087 2.155 5.597 23 ALA -4.768 2.383 8.633 24 THR -1.755 4.666 8.856 25 SER -1.621 4.545 12.695 26 SER -3.032 0.998 13.203 27 LEU -0.486 -0.153 10.543 28 ASN 2.109 -2.772 11.531 29 SER 5.681 -1.589 11.108 30 GLY 7.980 -4.586 11.432 31 ASP 6.062 -7.100 9.284 32 CYS 5.513 -6.999 5.553 33 PHE 2.538 -4.750 4.439 34 LEU 1.088 -3.870 1.015 35 LEU -0.970 -0.822 0.062 36 ASP -2.600 -0.698 -3.348 37 ALA -3.263 2.704 -4.925 38 GLY -4.847 2.857 -8.396 39 LEU -1.878 1.786 -10.564 40 THR 0.914 2.154 -8.005 41 ILE 1.373 -0.274 -5.046 42 TYR 3.753 -0.090 -2.060 43 GLN 4.559 -3.365 -0.391 44 PHE 5.767 -1.633 2.804 45 ASN 7.474 -4.700 3.944 46 GLY 8.662 -4.348 7.679 47 SER 12.161 -5.608 8.722 48 LYS 11.080 -6.530 12.307 49 SER 9.848 -9.722 10.611 50 SER 11.057 -11.029 7.274 51 PRO 10.360 -14.766 6.715 52 GLN 6.711 -15.101 7.820 53 GLU 5.327 -12.084 5.946 54 LYS 7.978 -12.428 3.171 55 ASN 6.473 -15.811 2.279 56 LYS 2.795 -14.944 2.826 57 ALA 3.437 -11.555 1.205 58 ALA 5.475 -12.671 -1.826 59 GLU 2.516 -15.039 -2.198 60 VAL 0.011 -12.142 -2.166 61 ALA 2.133 -9.849 -4.415 62 ARG 2.618 -12.755 -6.851 63 ALA -1.142 -13.278 -7.238 64 ILE -1.686 -9.513 -7.671 65 ASP 1.216 -9.578 -10.099 66 ALA -0.541 -12.130 -12.332 67 GLU -3.915 -10.351 -11.941 68 ARG -2.716 -6.868 -13.008 69 LYS -0.147 -8.298 -15.422 70 GLY 2.457 -5.952 -13.878 71 LEU 0.593 -3.028 -15.545 72 PRO 0.642 -1.138 -12.214 73 LYS 3.930 -0.082 -10.519 74 VAL 5.026 -1.733 -7.242 75 GLU 7.494 -0.740 -4.503 76 VAL 8.540 -3.536 -2.055 77 PHE 10.780 -3.207 1.088 78 CYS 10.739 -4.977 4.474 79 GLU 12.290 -2.082 6.371 80 THR 11.855 -0.653 9.895 81 ASP 13.847 2.570 10.335 82 SER 12.693 5.409 8.067 83 ASP 9.660 3.064 7.702 84 ILE 7.548 6.235 7.508 85 PRO 8.357 8.110 4.281 86 ALA 5.907 11.030 4.063 87 GLU 5.104 9.820 0.530 88 PHE 3.525 6.464 1.527 89 TRP 2.188 7.835 4.817 90 LYS 0.789 10.827 2.973 91 LEU -0.836 8.434 0.464 92 LEU -2.720 6.199 2.954 93 GLY -2.367 8.474 6.005 94 GLY -2.592 11.930 4.372 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S S S S 10 S/T T T T/S S S S S/S S S 20 S S T T T T/S S S S S/S 30 S S S S S S S/T T T T/S 40 S S S C C T T T T H 50 H H H H H H H H H H 60 H H H H H H H H H C 70 S S S S S S S S S S 80 C C C C H H H H H H 90 H H/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E E E E 10 t T T t E E E E E 20 S S S t T T 30 t E E E E E E e e E 40 E E E t T T t h 50 H H H H H H H H H H 60 H H H H H H H H h T 70 t S E E E E e t 80 T T t h H H H H H 90 H H h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 8.3 6.0 85.8 2 TYR 0.0 0.0 85.8 3 LYS 18.8 10.9 84.7 4 PRO 84.6 67.9 59.4 5 ARG 77.6 37.1 77.0 6 LEU 146.2 98.9 38.0 7 LEU 125.9 85.2 37.5 8 HIS 104.6 69.6 56.8 9 ILE 143.0 99.7 34.9 10 SER 72.5 86.7 64.3 11 GLY 31.3 90.0 70.5 12 ASP 0.0 0.0 86.2 13 LYS 0.0 0.0 89.0 14 ASN 0.3 0.2 88.4 15 ALA 68.6 94.5 55.0 16 LYS 41.2 23.8 80.2 17 VAL 99.0 83.3 43.3 18 ALA 10.0 13.7 76.4 19 GLU 44.9 32.4 67.8 20 VAL 96.6 81.3 47.7 21 PRO 16.0 12.8 80.7 22 LEU 48.2 32.6 70.6 23 ALA 56.1 77.3 52.3 24 THR 83.8 78.4 47.0 25 SER 0.0 0.0 90.0 26 SER 6.0 7.2 78.7 27 LEU 142.9 96.7 36.5 28 ASN 98.5 81.5 56.9 29 SER 51.9 62.1 64.2 30 GLY 33.6 96.4 56.5 31 ASP 89.8 81.3 68.2 32 CYS 99.2 100.0 48.6 33 PHE 163.7 98.2 41.9 34 LEU 140.0 94.7 34.9 35 LEU 145.9 98.7 35.8 36 ASP 96.9 87.7 47.1 37 ALA 61.2 84.3 49.1 38 GLY 0.0 0.0 79.1 39 LEU 39.4 26.7 74.3 40 THR 69.4 64.9 56.9 41 ILE 138.4 96.4 41.7 42 TYR 159.5 88.1 45.5 43 GLN 142.9 96.2 38.1 44 PHE 164.0 98.3 41.6 45 ASN 120.8 99.9 44.3 46 GLY 34.8 100.0 54.8 47 SER 44.6 53.3 71.2 48 LYS 28.0 16.2 79.7 49 SER 59.8 71.5 69.6 50 SER 29.0 34.7 61.3 51 PRO 39.5 31.8 80.3 52 GLN 83.6 56.2 66.4 53 GLU 138.4 99.8 40.7 54 LYS 74.2 42.8 66.8 55 ASN 14.5 12.0 81.7 56 LYS 105.7 61.0 59.3 57 ALA 71.9 99.0 47.3 58 ALA 24.6 33.9 74.0 59 GLU 20.1 14.5 78.5 60 VAL 84.6 71.2 43.4 61 ALA 51.1 70.3 60.6 62 ARG 32.3 15.5 86.8 63 ALA 11.1 15.3 78.1 64 ILE 99.6 69.4 51.3 65 ASP 40.7 36.9 77.8 66 ALA 7.7 10.6 82.4 67 GLU 22.9 16.5 83.1 68 ARG 96.9 46.4 68.9 69 LYS 41.3 23.8 84.3 70 GLY 9.2 26.5 74.3 71 LEU 30.7 20.8 73.2 72 PRO 119.0 95.6 39.8 73 LYS 23.2 13.4 82.6 74 VAL 67.6 56.9 60.6 75 GLU 88.2 63.6 45.8 76 VAL 76.2 64.1 68.4 77 PHE 100.3 60.2 59.3 78 CYS 89.0 89.7 52.7 79 GLU 85.4 61.6 63.6 80 THR 78.1 73.0 55.8 81 ASP 9.6 8.7 86.9 82 SER 4.8 5.7 85.4 83 ASP 95.2 86.2 44.9 84 ILE 62.8 43.8 64.1 85 PRO 71.2 57.2 68.6 86 ALA 0.0 0.0 82.2 87 GLU 55.5 40.0 66.2 88 PHE 165.5 99.2 24.5 89 TRP 170.4 83.1 42.0 90 LYS 37.5 21.6 82.4 91 LEU 95.3 64.5 56.3 92 LEU 143.8 97.3 35.3 93 GLY 29.6 85.1 64.0 94 GLY 13.3 38.3 64.0