Protein Data Bank File : 1ksr Title : ACTIN BINDING PROTEIN 07-FEB-97 1KSR Number of Amino Acid Residues : 100 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA ASP PRO GLU LYS SER TYR ALA GLU GLY 10 PRO GLY LEU ASP GLY GLY GLU CYS PHE GLN 20 PRO SER LYS PHE LYS ILE HIS ALA VAL ASP 30 PRO ASP GLY VAL HIS ARG THR ASP GLY GLY 40 ASP GLY PHE VAL VAL THR ILE GLU GLY PRO 50 ALA PRO VAL ASP PRO VAL MET VAL ASP ASN 60 GLY ASP GLY THR TYR ASP VAL GLU PHE GLU 70 PRO LYS GLU ALA GLY ASP TYR VAL ILE ASN 80 LEU THR LEU ASP GLY ASP ASN VAL ASN GLY 90 PHE PRO LYS THR VAL THR VAL LYS PRO ALA Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 -150.6 -179.3 2 ASP -115.9 47.2 177.2 175.0 16.8 3 PRO -77.4 1.3 -178.3 22.8 -23.3 4 GLU -135.1 11.9 -179.5 -127.1 -61.6 -55.3 5 LYS -147.6 35.9 -179.7 -149.9 68.1 153.3 -55.9 6 SER -115.4 119.8 -179.1 -54.1 7 TYR -142.2 143.5 178.7 41.9 -73.4 8 ALA -124.6 128.8 -179.7 9 GLU -147.0 142.7 -179.9 50.5 153.8 -46.6 10 GLY -162.7 174.5 176.9 11 PRO -79.6 7.9 -179.6 22.6 -20.6 12 GLY -117.4 157.7 179.7 13 LEU 90.1 -8.7 178.0 104.3 120.7 14 ASP -67.3 -18.6 179.8 -40.4 -32.4 15 GLY 74.9 -129.2 -179.7 16 GLY 66.2 -58.7 -178.3 17 GLU -128.6 142.9 179.3 -72.4 150.6 84.9 18 CYS -88.8 -20.9 -179.1 -92.2 19 PHE -89.0 13.9 176.9 -77.5 -49.1 20 GLN -99.6 143.5 -179.4 -151.9 160.5 -84.5 21 PRO -69.8 129.9 -178.3 21.2 -23.9 22 SER -104.6 111.5 -179.7 -134.3 23 LYS -150.1 135.6 179.3 -38.9 -166.1 171.1 120.8 24 PHE -141.0 159.4 179.8 1.3 -65.7 25 LYS -114.1 139.2 -178.8 -55.2 -114.9 -97.2 42.6 26 ILE -105.3 142.1 -179.5 -51.5 124.1 27 HIS -130.6 114.9 -179.9 -45.4 60.0 28 ALA -103.4 148.2 178.7 29 VAL -136.5 123.8 -180.0 156.8 30 ASP -104.0 -176.4 -179.6 94.7 -44.1 31 PRO -77.6 21.6 179.5 22.1 -20.1 32 ASP -118.4 11.4 -178.5 -90.8 49.1 33 GLY 71.7 34.2 -177.8 34 VAL -150.0 -175.2 179.5 -147.2 35 HIS -98.2 54.2 -179.8 -53.0 -132.1 36 ARG 65.0 70.3 -179.7 -95.2 -163.1 92.1 -35.1 37 THR 43.0 85.0 -179.3 76.6 38 ASP -42.7 153.2 -179.9 -116.8 14.3 39 GLY 87.3 -39.0 -180.0 40 GLY -120.2 46.4 179.8 41 ASP -89.6 122.3 179.2 -46.3 0.8 42 GLY -69.0 60.4 -178.8 43 PHE -99.2 112.2 177.9 -125.8 -35.1 44 VAL -119.6 113.5 -180.0 20.1 45 VAL -118.4 150.2 -179.7 -160.2 46 THR -160.2 129.4 178.0 16.9 47 ILE -120.3 156.2 177.3 -84.6 -136.9 48 GLU -169.2 156.0 -179.7 19.9 154.5 -30.8 49 GLY -163.9 -168.2 179.9 50 PRO -76.6 72.8 -179.7 22.2 -21.4 51 ALA -156.4 178.3 179.9 52 PRO -79.3 -56.9 179.6 22.5 -20.0 53 VAL -89.6 74.4 -178.5 -175.7 54 ASP -90.1 -49.9 -179.7 -72.7 -40.1 55 PRO -80.4 103.3 -179.2 22.9 -20.2 56 VAL -140.5 97.3 178.8 -169.3 57 MET -140.1 136.6 -178.9 71.6 -80.0 142.6 58 VAL -135.3 155.4 179.3 -122.8 59 ASP -120.2 127.9 -179.2 177.7 -40.9 60 ASN -88.3 -22.7 178.7 -127.0 25.8 61 GLY 89.6 23.1 179.5 62 ASP -122.3 26.0 -179.6 60.8 4.4 63 GLY 82.3 -10.4 179.7 64 THR -125.0 127.3 -179.4 59.2 65 TYR -117.6 157.3 -177.9 -51.9 -34.0 66 ASP -123.6 151.2 179.4 68.7 -18.2 67 VAL -137.2 143.8 -178.1 -41.8 68 GLU -151.5 128.6 175.8 -38.9 78.6 -2.9 69 PHE -131.2 156.4 -178.5 68.3 -62.5 70 GLU -150.0 101.8 179.8 175.4 142.5 46.1 71 PRO -80.3 171.9 -179.9 22.6 -20.0 72 LYS -133.0 22.6 179.9 26.0 144.8 107.3 116.9 73 GLU -152.3 -141.4 178.5 66.7 129.8 -22.6 74 ALA -99.8 126.0 -176.9 75 GLY -162.4 161.2 178.5 76 ASP -113.8 156.5 -177.4 55.8 48.7 77 TYR -114.7 140.8 176.4 -48.1 -28.5 78 VAL -119.6 127.8 -176.6 39.8 79 ILE -105.3 158.4 178.7 -4.6 -61.3 80 ASN -149.2 113.7 -179.4 -40.0 96.9 81 LEU -137.2 118.5 -176.4 171.9 -88.2 82 THR -133.3 137.9 178.6 39.8 83 LEU -140.0 74.9 179.7 -166.9 -76.8 84 ASP 141.3 -21.5 -178.5 -84.3 -29.0 85 GLY 130.3 2.3 179.4 86 ASP -127.7 175.1 -179.6 -105.3 57.6 87 ASN -112.0 158.7 -179.8 48.3 40.9 88 VAL -67.0 169.6 -178.3 158.5 89 ASN -83.3 24.6 179.4 78.7 95.6 90 GLY -148.9 13.4 -178.3 91 PHE -107.1 -41.5 179.0 -98.0 86.0 92 PRO -73.1 13.8 178.7 21.3 -20.6 93 LYS -95.1 170.6 -179.1 -168.4 -100.1 -111.8 -147.8 94 THR -124.9 126.8 178.3 -48.2 95 VAL -99.4 155.7 -176.5 159.0 96 THR -121.6 140.6 176.6 -65.8 97 VAL -122.3 145.8 -178.5 154.7 98 LYS -94.5 -173.3 -177.8 -25.1 -61.0 -120.0 169.9 99 PRO -69.1 91.1 -179.8 20.6 -21.8 100 ALA -48.8 -65.6 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA -17.829 -10.248 -1.149 2 ASP -14.183 -9.857 -0.112 3 PRO -14.520 -8.006 3.223 4 GLU -12.307 -10.791 4.633 5 LYS -9.807 -11.497 1.831 6 SER -8.684 -8.068 0.667 7 TYR -5.051 -7.097 1.273 8 ALA -2.628 -4.564 -0.274 9 GLU 1.147 -4.862 0.096 10 GLY 4.134 -3.377 -1.721 11 PRO 7.686 -2.059 -1.444 12 GLY 6.027 1.380 -1.161 13 LEU 4.239 2.976 1.842 14 ASP 6.951 1.744 4.196 15 GLY 7.774 5.447 4.504 16 GLY 11.238 6.118 5.937 17 GLU 12.261 8.081 2.835 18 CYS 10.359 10.493 0.569 19 PHE 12.805 10.079 -2.349 20 GLN 11.919 6.408 -2.557 21 PRO 9.324 5.384 -5.120 22 SER 6.089 4.474 -3.355 23 LYS 4.184 1.686 -5.097 24 PHE 2.171 -1.314 -3.857 25 LYS -0.150 -3.880 -5.441 26 ILE -3.578 -4.696 -4.015 27 HIS -5.101 -8.181 -4.199 28 ALA -8.800 -8.785 -3.480 29 VAL -10.421 -12.242 -3.126 30 ASP -14.171 -12.857 -3.132 31 PRO -16.167 -16.032 -2.499 32 ASP -15.805 -17.042 -6.183 33 GLY -12.102 -17.957 -6.128 34 VAL -11.497 -14.576 -7.720 35 HIS -11.019 -10.911 -6.773 36 ARG -14.758 -10.144 -6.647 37 THR -15.640 -10.642 -10.327 38 ASP -12.522 -9.017 -11.862 39 GLY -13.339 -5.805 -13.758 40 GLY -16.143 -4.994 -11.280 41 ASP -14.242 -5.127 -7.962 42 GLY -15.424 -2.445 -5.509 43 PHE -11.751 -1.671 -4.857 44 VAL -11.124 1.936 -3.845 45 VAL -7.557 2.732 -2.796 46 THR -6.085 6.138 -2.032 47 ILE -2.782 7.385 -0.633 48 GLU -1.753 10.907 0.219 49 GLY 0.781 13.021 2.130 50 PRO 2.461 16.442 2.098 51 ALA 3.310 16.441 -1.637 52 PRO 2.050 17.324 -5.128 53 VAL 1.313 13.824 -6.486 54 ASP -0.404 12.452 -3.351 55 PRO -3.558 10.775 -4.769 56 VAL -2.295 8.024 -7.099 57 MET -4.296 4.828 -7.571 58 VAL -4.957 2.699 -10.678 59 ASP -6.772 -0.598 -11.392 60 ASN -5.403 -3.108 -13.941 61 GLY -8.526 -5.324 -13.992 62 ASP -6.760 -8.588 -13.032 63 GLY -7.942 -8.813 -9.401 64 THR -4.792 -6.887 -8.443 65 TYR -4.626 -3.059 -8.468 66 ASP -1.624 -0.765 -7.952 67 VAL -1.205 2.614 -6.274 68 GLU 1.898 4.902 -6.253 69 PHE 2.871 8.266 -4.736 70 GLU 6.342 9.893 -4.501 71 PRO 7.126 12.873 -2.213 72 LYS 10.372 14.945 -2.315 73 GLU 10.855 16.160 1.300 74 ALA 9.870 15.108 4.858 75 GLY 6.346 13.698 5.033 76 ASP 4.096 11.005 6.489 77 TYR 1.763 8.800 4.474 78 VAL -1.852 8.007 5.108 79 ILE -3.284 5.036 3.252 80 ASN -6.782 4.151 2.170 81 LEU -7.620 0.765 0.629 82 THR -11.215 -0.450 0.540 83 LEU -12.923 -3.490 -1.024 84 ASP -16.638 -3.656 0.001 85 GLY -16.999 -0.343 1.844 86 ASP -14.358 -0.798 4.582 87 ASN -10.562 -0.430 4.619 88 VAL -7.880 -3.096 5.112 89 ASN -6.254 -3.382 8.589 90 GLY -3.111 -1.579 7.352 91 PHE -4.406 1.310 5.200 92 PRO -6.119 3.754 7.557 93 LYS -2.717 3.810 9.251 94 THR -0.067 6.441 8.667 95 VAL 3.532 5.732 7.727 96 THR 6.229 8.384 8.283 97 VAL 9.137 9.651 6.146 98 LYS 11.815 12.109 7.360 99 PRO 13.388 15.056 5.492 100 ALA 14.672 13.214 2.430 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C T T T T/S S S S S S 10 C C C C C S S S S S 20 S S S S S S S S S S/T 30 T T T T T T T/T T T T 40 C S S S S S S S C C 50 C C C S S S S S S S 60 S/T T T T/S S S S S/S S S 70 S S S/S S S S S S S S 80 S S/T T T T/S S S S/T T T 90 T 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 t T T e E E E E 10 S S S B S S S 20 E E E E E E E e B 30 T T T B S S t T T t 40 e E E E E E E S 50 S S S e E E E e 60 S S e E E E E E E 70 S S S E E E E E E 80 E E E e S S B t T T 90 t S e E E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 51.4 70.8 65.4 2 ASP 109.6 99.2 44.5 3 PRO 57.3 46.1 71.1 4 GLU 0.0 0.0 85.2 5 LYS 57.8 33.3 70.8 6 SER 77.2 92.3 50.7 7 TYR 86.3 47.7 62.4 8 ALA 72.6 100.0 35.9 9 GLU 27.8 20.0 74.6 10 GLY 27.9 80.2 55.1 11 PRO 22.1 17.7 81.8 12 GLY 32.4 93.2 65.8 13 LEU 119.6 80.9 46.6 14 ASP 43.5 39.4 75.6 15 GLY 34.5 99.2 52.1 16 GLY 2.0 5.7 72.0 17 GLU 42.7 30.8 74.9 18 CYS 99.2 100.0 45.0 19 PHE 71.3 42.7 70.0 20 GLN 75.6 50.9 77.7 21 PRO 63.0 50.6 71.2 22 SER 79.2 94.7 46.4 23 LYS 68.6 39.6 63.5 24 PHE 166.3 99.7 36.1 25 LYS 64.1 37.0 73.0 26 ILE 143.5 100.0 31.8 27 HIS 113.3 75.4 56.0 28 ALA 72.6 100.0 42.6 29 VAL 86.4 72.8 65.2 30 ASP 106.4 96.3 46.7 31 PRO 48.2 38.7 81.3 32 ASP 33.0 29.9 75.8 33 GLY 0.0 0.0 78.4 34 VAL 63.1 53.1 70.6 35 HIS 110.5 73.6 54.7 36 ARG 158.6 75.9 58.2 37 THR 29.7 27.8 82.1 38 ASP 77.2 69.9 68.3 39 GLY 2.3 6.5 77.8 40 GLY 0.0 0.0 85.8 41 ASP 110.5 100.0 57.6 42 GLY 0.0 0.0 74.4 43 PHE 166.6 99.9 37.0 44 VAL 35.0 29.5 78.0 45 VAL 115.0 96.8 31.9 46 THR 63.3 59.2 53.4 47 ILE 143.5 100.0 33.0 48 GLU 60.4 43.6 66.6 49 GLY 26.7 76.7 56.3 50 PRO 68.7 55.2 72.1 51 ALA 63.7 87.8 58.9 52 PRO 58.4 46.9 65.9 53 VAL 33.1 27.9 68.4 54 ASP 95.6 86.5 49.8 55 PRO 50.3 40.4 68.1 56 VAL 87.4 73.6 59.9 57 MET 81.2 50.9 65.5 58 VAL 34.7 29.2 85.6 59 ASP 62.0 56.1 61.1 60 ASN 21.0 17.4 87.3 61 GLY 20.0 57.5 74.7 62 ASP 48.8 44.2 80.2 63 GLY 34.8 100.0 60.0 64 THR 80.5 75.3 61.3 65 TYR 177.4 98.0 57.4 66 ASP 66.0 59.7 59.5 67 VAL 118.5 99.8 37.8 68 GLU 112.1 80.9 46.7 69 PHE 164.4 98.6 37.9 70 GLU 67.4 48.6 69.9 71 PRO 123.0 98.8 43.2 72 LYS 50.6 29.2 62.4 73 GLU 56.1 40.5 68.5 74 ALA 46.4 63.9 57.1 75 GLY 28.0 80.4 48.6 76 ASP 49.7 45.0 58.5 77 TYR 177.7 98.2 39.7 78 VAL 73.3 61.7 69.9 79 ILE 143.2 99.8 37.8 80 ASN 75.6 62.6 58.6 81 LEU 147.8 100.0 26.9 82 THR 83.8 78.4 52.2 83 LEU 147.6 99.9 44.2 84 ASP 84.8 76.7 55.1 85 GLY 0.0 0.0 79.2 86 ASP 5.9 5.3 81.8 87 ASN 65.5 54.2 59.7 88 VAL 98.8 83.1 55.4 89 ASN 0.0 0.0 81.6 90 GLY 8.3 23.7 61.1 91 PHE 163.9 98.3 37.1 92 PRO 75.9 61.0 74.6 93 LYS 51.7 29.8 75.8 94 THR 56.2 52.6 64.9 95 VAL 102.7 86.4 56.3 96 THR 46.7 43.7 68.0 97 VAL 118.8 100.0 51.1 98 LYS 44.5 25.6 69.4 99 PRO 33.0 26.5 66.0 100 ALA 58.7 80.9 50.1