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HEADER CYTOSKELETON 19-MAY-93 1SHG
TITLE CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-SPECTRIN SH3 DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
EXPDTA X-RAY DIFFRACTION
REMARK 2 RESOLUTION. 1.80 ANGSTORMS
DBREF 1SHG A 2 62 UNP P07751 SPTA2_CHICK 965 1025
SEQRES 1 A 55 GLU LEU VAL LEU ALA LEU TYR ASP TYR GLN GLU LYS SER
SEQRES 2 A 55 PRO ARG GLU VAL THR MET LYS LYS GLY ASP ILE LEU THR
SEQRES 3 A 55 LEU LEU ASN SER THR ASN LYS ASP TRP TRP LYS VAL GLU
SEQRES 4 A 55 VAL ASN ASP ARG GLN GLY PHE VAL PRO ALA ALA TYR VAL
SEQRES 5 A 55 LYS LYS LEU
ATOM 1 N GLU A 7 15.191 20.705 5.471 1.00 38.83
ATOM 2 CA GLU A 7 14.162 20.730 6.475 1.00 33.15
ATOM 3 C GLU A 7 14.746 21.133 7.820 1.00 20.72
ATOM 4 O GLU A 7 15.901 20.827 8.122 1.00 26.02
ATOM 5 CB GLU A 7 13.444 19.393 6.637 1.00 52.26
ATOM 6 CG GLU A 7 12.288 19.204 5.638 1.00 76.68
ATOM 7 CD GLU A 7 11.081 18.459 6.172 1.00 94.38
ATOM 8 OE1 GLU A 7 10.244 18.948 6.919 1.00100.00
ATOM 9 OE2 GLU A 7 10.981 17.244 5.682 1.00100.00
ATOM 10 N LEU A 8 13.967 21.964 8.495 1.00 21.34
ATOM 11 CA LEU A 8 14.317 22.428 9.805 1.00 25.70
ATOM 12 C LEU A 8 13.339 21.843 10.805 1.00 25.57
ATOM 13 O LEU A 8 12.147 21.718 10.524 1.00 29.88
ATOM 14 CB LEU A 8 14.219 23.962 9.879 1.00 26.56
ATOM 15 CG LEU A 8 15.045 24.619 8.784 1.00 27.51
ATOM 16 CD1 LEU A 8 14.895 26.138 8.875 1.00 30.70
ATOM 17 CD2 LEU A 8 16.493 24.215 8.999 1.00 29.29
ATOM 18 N VAL A 9 13.805 21.618 12.040 1.00 24.23
ATOM 19 CA VAL A 9 12.854 21.230 13.058 1.00 20.73
ATOM 20 C VAL A 9 13.140 22.108 14.267 1.00 15.52
ATOM 21 O VAL A 9 14.263 22.567 14.493 1.00 22.32
ATOM 22 CB VAL A 9 13.012 19.745 13.457 1.00 27.00
ATOM 23 CG1 VAL A 9 12.514 18.881 12.312 1.00 26.59
ATOM 24 CG2 VAL A 9 14.446 19.389 13.823 1.00 21.87
ATOM 25 N LEU A 10 12.141 22.214 15.051 1.00 19.27
ATOM 26 CA LEU A 10 12.275 22.955 16.291 1.00 21.59
ATOM 27 C LEU A 10 12.384 21.921 17.422 1.00 21.66
ATOM 28 O LEU A 10 11.508 21.069 17.525 1.00 21.74
ATOM 29 CB LEU A 10 10.922 23.734 16.486 1.00 22.58
ATOM 30 CG LEU A 10 10.653 24.229 17.915 1.00 20.72
ATOM 31 CD1 LEU A 10 11.702 25.247 18.284 1.00 23.17
ATOM 32 CD2 LEU A 10 9.287 24.890 17.997 1.00 23.93
ATOM 33 N ALA A 11 13.282 22.168 18.353 1.00 19.76
ATOM 34 CA ALA A 11 13.421 21.354 19.556 1.00 21.71
ATOM 35 C ALA A 11 12.266 21.667 20.517 1.00 28.80
ATOM 36 O ALA A 11 12.090 22.828 20.949 1.00 29.01
ATOM 37 CB ALA A 11 14.800 21.605 20.236 1.00 24.04
ATOM 38 N LEU A 12 11.422 20.689 20.795 1.00 20.59
ATOM 39 CA LEU A 12 10.373 20.966 21.742 1.00 24.62
ATOM 40 C LEU A 12 10.832 20.813 23.207 1.00 28.81
ATOM 41 O LEU A 12 10.221 21.351 24.133 1.00 28.22
ATOM 42 CB LEU A 12 9.112 20.143 21.463 1.00 21.00
ATOM 43 CG LEU A 12 8.680 20.155 20.013 1.00 26.95
ATOM 44 CD1 LEU A 12 7.602 19.120 19.771 1.00 27.87
ATOM 45 CD2 LEU A 12 8.070 21.491 19.607 1.00 31.27
ATOM 46 N TYR A 13 11.900 20.079 23.453 1.00 22.02
ATOM 47 CA TYR A 13 12.375 19.814 24.803 1.00 20.27
ATOM 48 C TYR A 13 13.837 19.737 24.803 1.00 22.60
ATOM 49 O TYR A 13 14.459 19.447 23.769 1.00 28.30
ATOM 50 CB TYR A 13 11.895 18.427 25.409 1.00 23.21
ATOM 51 CG TYR A 13 10.402 18.242 25.397 1.00 23.31
ATOM 52 CD1 TYR A 13 9.576 18.698 26.429 1.00 24.57
ATOM 53 CD2 TYR A 13 9.797 17.671 24.281 1.00 26.07
ATOM 54 CE1 TYR A 13 8.187 18.699 26.288 1.00 25.36
ATOM 55 CE2 TYR A 13 8.415 17.507 24.202 1.00 32.70
ATOM 56 CZ TYR A 13 7.601 18.079 25.182 1.00 33.30
ATOM 57 OH TYR A 13 6.228 17.955 25.054 1.00 38.03
ATOM 58 N ASP A 14 14.403 19.906 25.988 1.00 22.45
ATOM 59 CA ASP A 14 15.823 19.633 26.189 1.00 27.23
ATOM 60 C ASP A 14 16.070 18.134 25.990 1.00 33.32
ATOM 61 O ASP A 14 15.151 17.325 26.257 1.00 34.92
ATOM 62 CB ASP A 14 16.185 19.844 27.647 1.00 34.52
ATOM 63 CG ASP A 14 16.424 21.271 27.924 1.00 47.69
ATOM 64 OD1 ASP A 14 16.149 22.157 27.128 1.00 39.55
ATOM 65 OD2 ASP A 14 16.994 21.428 29.090 1.00 63.64
ATOM 66 N TYR A 15 17.230 17.797 25.445 1.00 26.10
ATOM 67 CA TYR A 15 17.596 16.393 25.263 1.00 27.53
ATOM 68 C TYR A 15 19.078 16.241 25.413 1.00 27.14
ATOM 69 O TYR A 15 19.848 16.802 24.637 1.00 27.90
ATOM 70 CB TYR A 15 17.125 15.737 23.959 1.00 27.01
ATOM 71 CG TYR A 15 17.353 14.238 23.946 1.00 24.48
ATOM 72 CD1 TYR A 15 16.505 13.385 24.652 1.00 25.83
ATOM 73 CD2 TYR A 15 18.480 13.711 23.311 1.00 24.05
ATOM 74 CE1 TYR A 15 16.857 12.039 24.780 1.00 27.74
ATOM 75 CE2 TYR A 15 18.834 12.365 23.408 1.00 27.51
ATOM 76 CZ TYR A 15 17.990 11.527 24.142 1.00 29.08
ATOM 77 OH TYR A 15 18.301 10.188 24.263 1.00 29.68
ATOM 78 N GLN A 16 19.511 15.464 26.421 1.00 24.45
ATOM 79 CA GLN A 16 20.928 15.243 26.628 1.00 29.10
ATOM 80 C GLN A 16 21.321 13.870 26.066 1.00 23.76
ATOM 81 O GLN A 16 20.746 12.825 26.346 1.00 26.46
ATOM 82 CB GLN A 16 21.256 15.401 28.135 1.00 43.80
ATOM 83 CG GLN A 16 20.734 16.732 28.789 1.00 63.80
ATOM 84 CD GLN A 16 19.206 16.968 28.865 1.00 78.09
ATOM 85 OE1 GLN A 16 18.375 16.025 28.926 1.00 86.37
ATOM 86 NE2 GLN A 16 18.801 18.247 28.883 1.00 72.70
ATOM 87 N GLU A 17 22.350 13.856 25.311 1.00 21.29
ATOM 88 CA GLU A 17 22.640 12.650 24.646 1.00 27.73
ATOM 89 C GLU A 17 22.943 11.555 25.629 1.00 31.21
ATOM 90 O GLU A 17 23.593 11.818 26.636 1.00 29.02
ATOM 91 CB GLU A 17 23.791 12.819 23.670 1.00 22.30
ATOM 92 CG GLU A 17 25.088 13.141 24.401 1.00 23.84
ATOM 93 CD GLU A 17 25.923 13.944 23.451 1.00 38.42
ATOM 94 OE1 GLU A 17 25.353 15.104 23.170 1.00 45.10
ATOM 95 OE2 GLU A 17 26.924 13.504 22.894 1.00 37.47
ATOM 96 N LYS A 18 22.565 10.342 25.278 1.00 23.90
ATOM 97 CA LYS A 18 22.881 9.226 26.183 1.00 35.09
ATOM 98 C LYS A 18 23.654 8.054 25.526 1.00 37.11
ATOM 99 O LYS A 18 23.916 7.005 26.095 1.00 31.61
ATOM 100 CB LYS A 18 21.626 8.802 26.927 1.00 39.56
ATOM 101 CG LYS A 18 21.295 9.747 28.075 1.00 52.91
ATOM 102 CD LYS A 18 19.832 9.656 28.521 1.00 65.34
ATOM 103 CE LYS A 18 19.291 10.915 29.234 1.00 73.13
ATOM 104 NZ LYS A 18 18.240 11.648 28.483 1.00 71.54
ATOM 105 N SER A 19 24.053 8.226 24.285 1.00 30.36
ATOM 106 CA SER A 19 24.660 7.160 23.549 1.00 26.36
ATOM 107 C SER A 19 25.535 7.779 22.477 1.00 29.48
ATOM 108 O SER A 19 25.418 8.972 22.153 1.00 23.67
ATOM 109 CB SER A 19 23.565 6.236 22.973 1.00 25.45
ATOM 110 OG SER A 19 23.649 6.293 21.578 1.00 31.09
ATOM 111 N PRO A 20 26.456 6.984 21.932 1.00 31.40
ATOM 112 CA PRO A 20 27.390 7.519 20.994 1.00 25.88
ATOM 113 C PRO A 20 26.810 8.235 19.795 1.00 26.13
ATOM 114 O PRO A 20 27.408 9.205 19.263 1.00 31.93
ATOM 115 CB PRO A 20 28.310 6.370 20.602 1.00 27.00
ATOM 116 CG PRO A 20 28.266 5.440 21.786 1.00 30.20
ATOM 117 CD PRO A 20 27.123 5.869 22.666 1.00 34.89
ATOM 118 N ARG A 21 25.707 7.704 19.328 1.00 25.29
ATOM 119 CA ARG A 21 25.254 8.256 18.107 1.00 26.36
ATOM 120 C ARG A 21 24.305 9.396 18.344 1.00 22.09
ATOM 121 O ARG A 21 23.679 9.820 17.374 1.00 22.07
ATOM 122 CB ARG A 21 24.598 7.159 17.285 1.00 32.00
ATOM 123 CG ARG A 21 23.540 6.529 18.149 1.00 37.45
ATOM 124 CD ARG A 21 22.755 5.434 17.456 1.00 40.80
ATOM 125 NE ARG A 21 21.685 4.964 18.326 1.00 47.00
ATOM 126 CZ ARG A 21 21.517 3.704 18.728 1.00 51.61
ATOM 127 NH1 ARG A 21 22.257 2.694 18.273 1.00 46.57
ATOM 128 NH2 ARG A 21 20.474 3.429 19.505 1.00 53.29
ATOM 129 N GLU A 22 24.084 9.763 19.615 1.00 18.27
ATOM 130 CA GLU A 22 23.074 10.778 19.941 1.00 18.98
ATOM 131 C GLU A 22 23.633 12.202 20.015 1.00 23.65
ATOM 132 O GLU A 22 24.811 12.408 20.231 1.00 25.60
ATOM 133 CB GLU A 22 22.440 10.442 21.291 1.00 18.01
ATOM 134 CG GLU A 22 21.416 9.335 21.113 1.00 22.13
ATOM 135 CD GLU A 22 20.829 8.900 22.408 1.00 24.46
ATOM 136 OE1 GLU A 22 20.827 9.564 23.428 1.00 26.36
ATOM 137 OE2 GLU A 22 20.379 7.698 22.322 1.00 25.98
ATOM 138 N VAL A 23 22.795 13.219 19.887 1.00 21.31
ATOM 139 CA VAL A 23 23.332 14.573 20.104 1.00 24.39
ATOM 140 C VAL A 23 22.542 15.272 21.192 1.00 23.00
ATOM 141 O VAL A 23 21.449 14.848 21.522 1.00 25.58
ATOM 142 CB VAL A 23 23.534 15.406 18.819 1.00 19.52
ATOM 143 CG1 VAL A 23 24.462 14.571 17.981 1.00 25.33
ATOM 144 CG2 VAL A 23 22.219 15.422 18.085 1.00 18.80
ATOM 145 N THR A 24 23.046 16.341 21.748 1.00 23.53
ATOM 146 CA THR A 24 22.281 17.030 22.776 1.00 21.27
ATOM 147 C THR A 24 21.601 18.204 22.143 1.00 19.50
ATOM 148 O THR A 24 22.216 18.838 21.304 1.00 25.38
ATOM 149 CB THR A 24 23.273 17.514 23.863 1.00 24.80
ATOM 150 OG1 THR A 24 23.737 16.370 24.556 1.00 25.78
ATOM 151 CG2 THR A 24 22.564 18.409 24.861 1.00 23.25
ATOM 152 N MET A 25 20.443 18.579 22.596 1.00 16.57
ATOM 153 CA MET A 25 19.806 19.795 22.088 1.00 18.58
ATOM 154 C MET A 25 19.086 20.447 23.230 1.00 27.89
ATOM 155 O MET A 25 18.811 19.749 24.211 1.00 30.55
ATOM 156 CB MET A 25 18.822 19.591 20.904 1.00 17.76
ATOM 157 CG MET A 25 17.571 18.888 21.354 1.00 22.20
ATOM 158 SD MET A 25 16.560 18.173 20.072 1.00 23.66
ATOM 159 CE MET A 25 15.265 17.384 21.026 1.00 18.97
ATOM 160 N LYS A 26 18.716 21.739 23.067 1.00 24.47
ATOM 161 CA LYS A 26 17.963 22.548 24.037 1.00 27.96
ATOM 162 C LYS A 26 16.670 22.962 23.422 1.00 24.11
ATOM 163 O LYS A 26 16.625 23.335 22.246 1.00 25.47
ATOM 164 CB LYS A 26 18.634 23.883 24.403 1.00 35.83
ATOM 165 CG LYS A 26 20.011 23.768 25.032 1.00 54.60
ATOM 166 CD LYS A 26 20.162 24.606 26.306 1.00 67.86
ATOM 167 CE LYS A 26 21.126 25.796 26.215 1.00 70.67
ATOM 168 NZ LYS A 26 20.430 27.100 26.268 1.00 71.42
ATOM 169 N LYS A 27 15.681 23.041 24.282 1.00 18.98
ATOM 170 CA LYS A 27 14.385 23.489 23.934 1.00 18.98
ATOM 171 C LYS A 27 14.488 24.821 23.179 1.00 24.14
ATOM 172 O LYS A 27 15.187 25.714 23.605 1.00 23.32
ATOM 173 CB LYS A 27 13.621 23.663 25.196 1.00 22.50
ATOM 174 CG LYS A 27 12.194 23.949 24.909 1.00 29.66
ATOM 175 CD LYS A 27 11.389 24.090 26.206 1.00 45.01
ATOM 176 CE LYS A 27 9.933 24.557 26.008 1.00 61.36
ATOM 177 NZ LYS A 27 8.912 23.571 26.435 1.00 70.77
ATOM 178 N GLY A 28 13.828 24.924 22.028 1.00 23.85
ATOM 179 CA GLY A 28 13.869 26.116 21.192 1.00 24.94
ATOM 180 C GLY A 28 14.977 26.119 20.153 1.00 27.69
ATOM 181 O GLY A 28 14.986 27.002 19.293 1.00 29.78
ATOM 182 N ASP A 29 15.914 25.160 20.207 1.00 23.52
ATOM 183 CA ASP A 29 16.903 25.004 19.144 1.00 17.61
ATOM 184 C ASP A 29 16.222 24.746 17.802 1.00 17.32
ATOM 185 O ASP A 29 15.226 24.041 17.687 1.00 21.89
ATOM 186 CB ASP A 29 18.013 23.952 19.383 1.00 14.00
ATOM 187 CG ASP A 29 18.935 24.348 20.434 1.00 24.56
ATOM 188 OD1 ASP A 29 19.013 25.488 20.818 1.00 33.65
ATOM 189 OD2 ASP A 29 19.790 23.416 20.753 1.00 25.71
ATOM 190 N ILE A 30 16.813 25.339 16.743 1.00 19.71
ATOM 191 CA ILE A 30 16.363 25.131 15.380 1.00 20.57
ATOM 192 C ILE A 30 17.413 24.181 14.758 1.00 20.68
ATOM 193 O ILE A 30 18.607 24.503 14.588 1.00 19.70
ATOM 194 CB ILE A 30 16.271 26.405 14.525 1.00 19.60
ATOM 195 CG1 ILE A 30 15.298 27.386 15.160 1.00 23.84
ATOM 196 CG2 ILE A 30 15.726 26.047 13.149 1.00 18.43
ATOM 197 CD1 ILE A 30 13.977 26.763 15.530 1.00 22.41
ATOM 198 N LEU A 31 16.958 22.964 14.420 1.00 19.90
ATOM 199 CA LEU A 31 17.940 21.959 13.964 1.00 19.22
ATOM 200 C LEU A 31 17.727 21.723 12.490 1.00 17.32
ATOM 201 O LEU A 31 16.595 21.885 12.016 1.00 23.56
ATOM 202 CB LEU A 31 17.715 20.579 14.676 1.00 20.14
ATOM 203 CG LEU A 31 17.681 20.782 16.185 1.00 30.04
ATOM 204 CD1 LEU A 31 17.214 19.599 17.032 1.00 33.73
ATOM 205 CD2 LEU A 31 19.076 21.165 16.559 1.00 30.10
ATOM 206 N THR A 32 18.776 21.229 11.841 1.00 20.95
ATOM 207 CA THR A 32 18.601 20.822 10.426 1.00 21.70
ATOM 208 C THR A 32 18.334 19.307 10.412 1.00 22.58
ATOM 209 O THR A 32 19.113 18.551 11.045 1.00 21.07
ATOM 210 CB THR A 32 19.892 21.093 9.658 1.00 29.57
ATOM 211 OG1 THR A 32 20.091 22.514 9.650 1.00 24.81
ATOM 212 CG2 THR A 32 19.826 20.440 8.258 1.00 28.54
ATOM 213 N LEU A 33 17.218 18.921 9.830 1.00 20.65
ATOM 214 CA LEU A 33 16.856 17.508 9.753 1.00 19.57
ATOM 215 C LEU A 33 17.676 16.823 8.663 1.00 25.82
ATOM 216 O LEU A 33 17.687 17.275 7.487 1.00 29.71
ATOM 217 CB LEU A 33 15.373 17.449 9.467 1.00 24.88
ATOM 218 CG LEU A 33 14.716 16.047 9.445 1.00 23.19
ATOM 219 CD1 LEU A 33 15.030 15.262 10.741 1.00 21.98
ATOM 220 CD2 LEU A 33 13.201 16.180 9.214 1.00 22.39
ATOM 221 N LEU A 34 18.453 15.795 9.072 1.00 19.75
ATOM 222 CA LEU A 34 19.272 14.972 8.153 1.00 17.63
ATOM 223 C LEU A 34 18.569 13.716 7.673 1.00 24.96
ATOM 224 O LEU A 34 18.598 13.369 6.490 1.00 27.53
ATOM 225 CB LEU A 34 20.648 14.592 8.666 1.00 17.76
ATOM 226 CG LEU A 34 21.517 15.767 9.049 1.00 31.74
ATOM 227 CD1 LEU A 34 22.937 15.264 9.319 1.00 33.77
ATOM 228 CD2 LEU A 34 21.498 16.770 7.894 1.00 36.62
ATOM 229 N ASN A 35 17.872 13.027 8.561 1.00 18.74
ATOM 230 CA ASN A 35 17.237 11.813 8.070 1.00 19.06
ATOM 231 C ASN A 35 16.107 11.526 8.987 1.00 17.85
ATOM 232 O ASN A 35 16.337 11.365 10.180 1.00 23.31
ATOM 233 CB ASN A 35 18.312 10.650 8.188 1.00 19.72
ATOM 234 CG ASN A 35 17.814 9.356 7.589 1.00 20.66
ATOM 235 OD1 ASN A 35 16.726 8.884 7.883 1.00 23.58
ATOM 236 ND2 ASN A 35 18.684 8.726 6.848 1.00 26.29
ATOM 237 N SER A 36 14.916 11.358 8.445 1.00 15.68
ATOM 238 CA SER A 36 13.783 11.070 9.288 1.00 21.65
ATOM 239 C SER A 36 13.107 9.754 8.883 1.00 18.87
ATOM 240 O SER A 36 11.910 9.617 9.027 1.00 20.10
ATOM 241 CB SER A 36 12.807 12.245 9.193 1.00 33.61
ATOM 242 OG SER A 36 12.538 12.495 7.815 1.00 30.09
ATOM 243 N THR A 37 13.894 8.826 8.320 1.00 18.63
ATOM 244 CA THR A 37 13.325 7.539 7.914 1.00 26.46
ATOM 245 C THR A 37 12.855 6.652 9.087 1.00 23.26
ATOM 246 O THR A 37 11.930 5.880 8.953 1.00 24.23
ATOM 247 CB THR A 37 14.322 6.770 7.022 1.00 19.42
ATOM 248 OG1 THR A 37 15.511 6.523 7.756 1.00 21.19
ATOM 249 CG2 THR A 37 14.620 7.560 5.742 1.00 18.81
ATOM 250 N ASN A 38 13.554 6.720 10.234 1.00 19.03
ATOM 251 CA ASN A 38 13.170 5.979 11.440 1.00 21.95
ATOM 252 C ASN A 38 12.043 6.665 12.197 1.00 27.42
ATOM 253 O ASN A 38 12.029 7.886 12.370 1.00 26.11
ATOM 254 CB ASN A 38 14.381 5.826 12.351 1.00 20.80
ATOM 255 CG ASN A 38 14.110 4.825 13.435 1.00 24.53
ATOM 256 OD1 ASN A 38 13.532 5.217 14.438 1.00 24.89
ATOM 257 ND2 ASN A 38 14.469 3.555 13.193 1.00 18.39
ATOM 258 N LYS A 39 11.064 5.906 12.610 1.00 22.82
ATOM 259 CA LYS A 39 9.934 6.491 13.294 1.00 26.59
ATOM 260 C LYS A 39 10.283 6.988 14.687 1.00 20.95
ATOM 261 O LYS A 39 9.691 7.896 15.212 1.00 24.99
ATOM 262 CB LYS A 39 8.770 5.549 13.367 1.00 38.24
ATOM 263 CG LYS A 39 8.239 5.381 14.767 1.00 58.65
ATOM 264 CD LYS A 39 7.495 4.058 14.983 1.00 70.43
ATOM 265 CE LYS A 39 7.466 3.625 16.452 1.00 69.17
ATOM 266 NZ LYS A 39 8.130 2.338 16.693 1.00 61.26
ATOM 267 N ASP A 40 11.312 6.499 15.276 1.00 19.91
ATOM 268 CA ASP A 40 11.516 6.952 16.607 1.00 22.98
ATOM 269 C ASP A 40 12.640 7.919 16.792 1.00 23.88
ATOM 270 O ASP A 40 12.660 8.601 17.833 1.00 25.31
ATOM 271 CB ASP A 40 11.732 5.771 17.570 1.00 30.47
ATOM 272 CG ASP A 40 10.493 4.876 17.618 1.00 36.12
ATOM 273 OD1 ASP A 40 9.317 5.470 17.809 1.00 29.40
ATOM 274 OD2 ASP A 40 10.602 3.711 17.372 1.00 36.52
ATOM 275 N TRP A 41 13.666 7.796 15.947 1.00 21.03
ATOM 276 CA TRP A 41 14.919 8.509 16.131 1.00 17.56
ATOM 277 C TRP A 41 15.221 9.260 14.878 1.00 25.16
ATOM 278 O TRP A 41 15.397 8.631 13.867 1.00 25.42
ATOM 279 CB TRP A 41 16.159 7.657 16.436 1.00 15.16
ATOM 280 CG TRP A 41 16.036 7.062 17.810 1.00 21.31
ATOM 281 CD1 TRP A 41 15.263 6.025 18.153 1.00 24.29
ATOM 282 CD2 TRP A 41 16.468 7.657 19.043 1.00 22.41
ATOM 283 NE1 TRP A 41 15.378 5.802 19.512 1.00 23.72
ATOM 284 CE2 TRP A 41 16.139 6.766 20.079 1.00 26.45
ATOM 285 CE3 TRP A 41 17.097 8.867 19.377 1.00 24.15
ATOM 286 CZ2 TRP A 41 16.434 7.050 21.428 1.00 31.55
ATOM 287 CZ3 TRP A 41 17.453 9.102 20.705 1.00 32.15
ATOM 288 CH2 TRP A 41 17.132 8.209 21.742 1.00 29.98
ATOM 289 N TRP A 42 15.428 10.572 14.967 1.00 21.81
ATOM 290 CA TRP A 42 15.782 11.379 13.799 1.00 18.18
ATOM 291 C TRP A 42 17.204 11.875 13.838 1.00 17.51
ATOM 292 O TRP A 42 17.682 12.285 14.907 1.00 20.24
ATOM 293 CB TRP A 42 14.735 12.529 13.607 1.00 19.65
ATOM 294 CG TRP A 42 13.386 12.108 13.114 1.00 21.19
ATOM 295 CD1 TRP A 42 12.961 10.844 12.716 1.00 18.08
ATOM 296 CD2 TRP A 42 12.322 13.010 12.857 1.00 21.79
ATOM 297 NE1 TRP A 42 11.655 10.909 12.319 1.00 19.36
ATOM 298 CE2 TRP A 42 11.254 12.234 12.342 1.00 22.66
ATOM 299 CE3 TRP A 42 12.185 14.389 13.052 1.00 23.32
ATOM 300 CZ2 TRP A 42 10.069 12.846 11.975 1.00 24.71
ATOM 301 CZ3 TRP A 42 10.998 14.996 12.715 1.00 24.36
ATOM 302 CH2 TRP A 42 9.952 14.203 12.215 1.00 28.11
ATOM 303 N LYS A 43 17.903 11.835 12.687 1.00 16.77
ATOM 304 CA LYS A 43 19.243 12.379 12.667 1.00 17.83
ATOM 305 C LYS A 43 19.183 13.856 12.270 1.00 23.21
ATOM 306 O LYS A 43 18.499 14.201 11.300 1.00 20.36
ATOM 307 CB LYS A 43 20.109 11.743 11.626 1.00 20.64
ATOM 308 CG LYS A 43 21.573 11.885 11.957 1.00 23.72
ATOM 309 CD LYS A 43 22.453 11.402 10.802 1.00 31.82
ATOM 310 CE LYS A 43 23.896 11.146 11.214 1.00 39.48
ATOM 311 NZ LYS A 43 24.864 11.162 10.110 1.00 47.06
ATOM 312 N VAL A 44 19.833 14.671 13.079 1.00 20.55
ATOM 313 CA VAL A 44 19.850 16.128 12.946 1.00 24.71
ATOM 314 C VAL A 44 21.268 16.669 13.110 1.00 27.17
ATOM 315 O VAL A 44 22.276 16.024 13.443 1.00 24.18
ATOM 316 CB VAL A 44 19.019 16.768 14.067 1.00 20.23
ATOM 317 CG1 VAL A 44 17.508 16.399 13.963 1.00 17.59
ATOM 318 CG2 VAL A 44 19.692 16.405 15.435 1.00 23.34
ATOM 319 N GLU A 45 21.353 17.936 12.812 1.00 26.15
ATOM 320 CA GLU A 45 22.589 18.734 12.934 1.00 27.87
ATOM 321 C GLU A 45 22.230 19.883 13.877 1.00 20.48
ATOM 322 O GLU A 45 21.181 20.529 13.719 1.00 22.67
ATOM 323 CB GLU A 45 23.047 19.289 11.571 1.00 25.60
ATOM 324 CG GLU A 45 24.354 20.067 11.663 1.00 36.22
ATOM 325 CD GLU A 45 24.858 20.427 10.284 1.00 46.63
ATOM 326 OE1 GLU A 45 24.182 21.032 9.438 1.00 45.83
ATOM 327 OE2 GLU A 45 26.084 20.000 10.104 1.00 47.84
ATOM 328 N VAL A 46 23.039 19.980 14.906 1.00 24.61
ATOM 329 CA VAL A 46 22.782 20.856 16.053 1.00 31.67
ATOM 330 C VAL A 46 24.009 21.661 16.117 1.00 32.03
ATOM 331 O VAL A 46 25.112 21.119 16.328 1.00 31.19
ATOM 332 CB VAL A 46 22.613 20.126 17.395 1.00 34.63
ATOM 333 CG1 VAL A 46 22.292 21.191 18.454 1.00 38.86
ATOM 334 CG2 VAL A 46 21.460 19.108 17.341 1.00 33.35
ATOM 335 N ASN A 47 23.771 22.900 15.699 1.00 48.79
ATOM 336 CA ASN A 47 24.781 23.775 15.193 1.00 56.59
ATOM 337 C ASN A 47 25.715 23.019 14.239 1.00 50.54
ATOM 338 O ASN A 47 25.473 22.844 13.040 1.00 52.42
ATOM 339 CB ASN A 47 25.615 24.569 16.205 1.00 64.81
ATOM 340 CG ASN A 47 26.231 25.717 15.413 1.00 74.08
ATOM 341 OD1 ASN A 47 27.411 25.685 14.973 1.00 74.78
ATOM 342 ND2 ASN A 47 25.333 26.632 15.023 1.00 76.53
ATOM 343 N ASP A 48 26.737 22.490 14.884 1.00 47.89
ATOM 344 CA ASP A 48 27.910 21.858 14.351 1.00 46.94
ATOM 345 C ASP A 48 27.959 20.354 14.547 1.00 52.47
ATOM 346 O ASP A 48 28.943 19.730 14.187 1.00 47.28
ATOM 347 CB ASP A 48 28.946 22.355 15.349 1.00 59.88
ATOM 348 CG ASP A 48 28.330 22.263 16.731 1.00 65.82
ATOM 349 OD1 ASP A 48 27.117 22.373 16.979 1.00 53.99
ATOM 350 OD2 ASP A 48 29.250 21.970 17.627 1.00 79.29
ATOM 351 N ARG A 49 27.062 19.785 15.348 1.00 50.21
ATOM 352 CA ARG A 49 27.171 18.356 15.617 1.00 44.41
ATOM 353 C ARG A 49 26.041 17.603 14.904 1.00 31.87
ATOM 354 O ARG A 49 24.953 18.201 14.792 1.00 33.55
ATOM 355 CB ARG A 49 27.079 18.155 17.137 1.00 53.48
ATOM 356 CG ARG A 49 28.433 18.248 17.849 1.00 63.42
ATOM 357 CD ARG A 49 28.389 17.869 19.335 1.00 70.27
ATOM 358 NE ARG A 49 28.579 16.420 19.603 1.00 70.57
ATOM 359 CZ ARG A 49 27.883 15.652 20.465 1.00 54.85
ATOM 360 NH1 ARG A 49 26.871 16.131 21.219 1.00 45.00
ATOM 361 NH2 ARG A 49 28.198 14.358 20.523 1.00 50.56
ATOM 362 N GLN A 50 26.264 16.323 14.471 1.00 27.26
ATOM 363 CA GLN A 50 25.194 15.509 13.832 1.00 28.99
ATOM 364 C GLN A 50 24.830 14.275 14.656 1.00 29.78
ATOM 365 O GLN A 50 25.693 13.640 15.162 1.00 32.14
ATOM 366 CB GLN A 50 25.615 14.940 12.480 1.00 33.37
ATOM 367 CG GLN A 50 26.211 15.948 11.489 1.00 45.14
ATOM 368 CD GLN A 50 26.246 15.354 10.097 1.00 52.46
ATOM 369 OE1 GLN A 50 26.153 14.117 9.915 1.00 55.85
ATOM 370 NE2 GLN A 50 26.234 16.246 9.120 1.00 54.92
ATOM 371 N GLY A 51 23.611 13.820 14.693 1.00 24.18
ATOM 372 CA GLY A 51 23.385 12.634 15.491 1.00 25.02
ATOM 373 C GLY A 51 21.903 12.427 15.723 1.00 24.07
ATOM 374 O GLY A 51 21.098 13.186 15.180 1.00 23.07
ATOM 375 N PHE A 52 21.507 11.413 16.525 1.00 20.03
ATOM 376 CA PHE A 52 20.100 11.193 16.741 1.00 16.79
ATOM 377 C PHE A 52 19.491 11.842 18.005 1.00 18.56
ATOM 378 O PHE A 52 20.174 12.069 18.993 1.00 22.51
ATOM 379 CB PHE A 52 19.764 9.710 16.733 1.00 23.47
ATOM 380 CG PHE A 52 20.178 9.096 15.428 1.00 28.60
ATOM 381 CD1 PHE A 52 21.507 8.667 15.252 1.00 30.30
ATOM 382 CD2 PHE A 52 19.216 8.946 14.417 1.00 22.20
ATOM 383 CE1 PHE A 52 21.924 8.099 14.045 1.00 24.01
ATOM 384 CE2 PHE A 52 19.601 8.304 13.233 1.00 23.44
ATOM 385 CZ PHE A 52 20.943 7.941 13.056 1.00 25.26
ATOM 386 N VAL A 53 18.248 12.263 17.856 1.00 19.05
ATOM 387 CA VAL A 53 17.405 12.684 18.923 1.00 18.00
ATOM 388 C VAL A 53 16.087 11.988 18.740 1.00 17.64
ATOM 389 O VAL A 53 15.775 11.552 17.627 1.00 21.28
ATOM 390 CB VAL A 53 17.274 14.200 19.004 1.00 20.16
ATOM 391 CG1 VAL A 53 18.666 14.824 19.087 1.00 17.99
ATOM 392 CG2 VAL A 53 16.514 14.735 17.789 1.00 22.24
ATOM 393 N PRO A 54 15.257 11.875 19.793 1.00 19.53
ATOM 394 CA PRO A 54 13.910 11.311 19.621 1.00 18.70
ATOM 395 C PRO A 54 13.015 12.192 18.676 1.00 27.03
ATOM 396 O PRO A 54 12.837 13.416 18.844 1.00 21.49
ATOM 397 CB PRO A 54 13.302 11.227 21.023 1.00 25.24
ATOM 398 CG PRO A 54 14.437 11.469 22.019 1.00 25.46
ATOM 399 CD PRO A 54 15.516 12.244 21.233 1.00 26.14
ATOM 400 N ALA A 55 12.415 11.521 17.680 1.00 19.74
ATOM 401 CA ALA A 55 11.545 12.130 16.742 1.00 15.92
ATOM 402 C ALA A 55 10.503 12.876 17.483 1.00 22.95
ATOM 403 O ALA A 55 9.978 13.833 16.912 1.00 25.64
ATOM 404 CB ALA A 55 10.840 11.174 15.772 1.00 17.54
ATOM 405 N ALA A 56 10.063 12.361 18.632 1.00 20.92
ATOM 406 CA ALA A 56 8.945 13.037 19.290 1.00 26.86
ATOM 407 C ALA A 56 9.370 14.369 19.926 1.00 23.49
ATOM 408 O ALA A 56 8.562 15.212 20.287 1.00 27.45
ATOM 409 CB ALA A 56 8.184 12.180 20.326 1.00 27.06
ATOM 410 N TYR A 57 10.628 14.579 20.123 1.00 21.59
ATOM 411 CA TYR A 57 10.841 15.802 20.847 1.00 22.58
ATOM 412 C TYR A 57 11.035 16.963 19.890 1.00 26.95
ATOM 413 O TYR A 57 11.554 17.981 20.323 1.00 25.37
ATOM 414 CB TYR A 57 12.144 15.597 21.610 1.00 21.44
ATOM 415 CG TYR A 57 12.023 14.644 22.776 1.00 19.99
ATOM 416 CD1 TYR A 57 10.870 13.870 22.906 1.00 22.17
ATOM 417 CD2 TYR A 57 13.031 14.581 23.740 1.00 26.13
ATOM 418 CE1 TYR A 57 10.778 12.961 23.961 1.00 25.03
ATOM 419 CE2 TYR A 57 12.941 13.665 24.792 1.00 30.80
ATOM 420 CZ TYR A 57 11.824 12.836 24.871 1.00 25.23
ATOM 421 OH TYR A 57 11.669 11.970 25.923 1.00 31.82
ATOM 422 N VAL A 58 10.811 16.713 18.580 1.00 23.94
ATOM 423 CA VAL A 58 11.047 17.731 17.574 1.00 25.72
ATOM 424 C VAL A 58 9.831 17.962 16.786 1.00 31.40
ATOM 425 O VAL A 58 8.999 17.093 16.702 1.00 26.03
ATOM 426 CB VAL A 58 12.254 17.567 16.657 1.00 20.72
ATOM 427 CG1 VAL A 58 13.442 17.383 17.575 1.00 26.39
ATOM 428 CG2 VAL A 58 12.157 16.366 15.730 1.00 24.52
ATOM 429 N LYS A 59 9.749 19.177 16.255 1.00 28.84
ATOM 430 CA LYS A 59 8.657 19.554 15.393 1.00 28.37
ATOM 431 C LYS A 59 9.170 20.091 14.060 1.00 32.13
ATOM 432 O LYS A 59 9.981 21.021 14.008 1.00 27.49
ATOM 433 CB LYS A 59 7.687 20.531 16.036 1.00 24.44
ATOM 434 CG LYS A 59 6.635 20.991 15.034 1.00 37.24
ATOM 435 CD LYS A 59 6.239 22.469 15.218 1.00 59.62
ATOM 436 CE LYS A 59 5.244 23.064 14.206 1.00 68.83
ATOM 437 NZ LYS A 59 4.908 22.130 13.121 1.00 77.40
ATOM 438 N LYS A 60 8.734 19.441 12.971 1.00 35.86
ATOM 439 CA LYS A 60 9.058 19.851 11.602 1.00 37.76
ATOM 440 C LYS A 60 8.540 21.267 11.266 1.00 34.19
ATOM 441 O LYS A 60 7.441 21.607 11.662 1.00 33.96
ATOM 442 CB LYS A 60 8.389 18.877 10.661 1.00 42.85
ATOM 443 CG LYS A 60 9.097 18.724 9.343 1.00 53.20
ATOM 444 CD LYS A 60 9.468 17.276 9.085 1.00 58.79
ATOM 445 CE LYS A 60 8.478 16.526 8.216 1.00 63.77
ATOM 446 NZ LYS A 60 8.859 15.113 8.027 1.00 71.14
ATOM 447 N LEU A 61 9.365 22.161 10.707 1.00 38.53
ATOM 448 CA LEU A 61 8.886 23.469 10.226 1.00 43.78
ATOM 449 C LEU A 61 8.984 23.478 8.675 1.00 50.96
ATOM 450 O LEU A 61 10.096 23.392 8.126 1.00 56.76
ATOM 451 CB LEU A 61 9.810 24.558 10.767 1.00 40.90
ATOM 452 CG LEU A 61 10.226 24.406 12.207 1.00 36.85
ATOM 453 CD1 LEU A 61 11.359 25.391 12.501 1.00 31.08
ATOM 454 CD2 LEU A 61 9.048 24.648 13.135 1.00 33.62
TER