1t7i.pdb

很多二维 三维几何计算算法 C++ 类库

ANISOU  119  CG1 ILE A  13     1886   1929   2239    -94   -157   -105       C  
ATOM    120  CG2 ILE A  13      33.784  28.693  23.776  1.00 16.70           C  
ANISOU  120  CG2 ILE A  13     1829   2243   2272    -76   -281     11       C  
ATOM    121  CD1 ILE A  13      34.968  29.978  21.191  1.00 15.96           C  
ANISOU  121  CD1 ILE A  13     1928   2058   2077   -126     82     32       C  
ATOM    122  N   ARG A  14      38.237  28.894  24.679  1.00 18.49           N  
ANISOU  122  N   ARG A  14     2100   2237   2687   -213   -265     96       N  
ATOM    123  CA  ARG A  14      39.606  29.129  24.338  1.00 20.05           C  
ANISOU  123  CA  ARG A  14     2247   2471   2898    -30    -71    243       C  
ATOM    124  C   ARG A  14      39.895  28.501  23.003  1.00 19.05           C  
ANISOU  124  C   ARG A  14     1945   2465   2828     78   -180    233       C  
ATOM    125  O   ARG A  14      39.702  27.306  22.812  1.00 19.81           O  
ANISOU  125  O   ARG A  14     2104   2268   3152    -38   -121    141       O  
ATOM    126  CB  ARG A  14      40.578  28.567  25.422  1.00 22.98           C  
ANISOU  126  CB  ARG A  14     2731   2918   3081     62   -128     26       C  
ATOM    127  CG  ARG A  14      42.033  28.954  25.172  1.00 27.65           C  
ANISOU  127  CG  ARG A  14     3157   3705   3643    -69      7    132       C  
ATOM    128  CD  ARG A  14      43.058  28.300  26.115  1.00 32.18           C  
ANISOU  128  CD  ARG A  14     3728   4402   4095     99   -184    113       C  
ATOM    129  NE  ARG A  14      43.744  27.183  25.458  1.00 36.20           N  
ANISOU  129  NE  ARG A  14     4624   4411   4716    172   -173    -23       N  
ATOM    130  CZ  ARG A  14      43.341  25.898  25.531  1.00 41.58           C  
ANISOU  130  CZ  ARG A  14     5292   5084   5422    -40    -77     62       C  
ATOM    131  NH1 ARG A  14      44.003  24.952  24.886  1.00 44.16           N  
ANISOU  131  NH1 ARG A  14     5631   5517   5627     39    -12    -24       N  
ATOM    132  NH2 ARG A  14      42.290  25.572  26.246  1.00 44.29           N  
ANISOU  132  NH2 ARG A  14     5495   5655   5676     77    -37    126       N  
ATOM    133  N   ILE A  15      40.358  29.306  22.076  1.00 19.43           N  
ANISOU  133  N   ILE A  15     2078   2387   2918     44    -39    207       N  
ATOM    134  CA  ILE A  15      40.671  28.861  20.757  1.00 18.39           C  
ANISOU  134  CA  ILE A  15     2010   2256   2719     75    -78    164       C  
ATOM    135  C   ILE A  15      41.915  29.646  20.290  1.00 21.70           C  
ANISOU  135  C   ILE A  15     2649   2457   3135    -50     84    147       C  
ATOM    136  O   ILE A  15      41.930  30.870  20.320  1.00 22.15           O  
ANISOU  136  O   ILE A  15     2493   2423   3498      5     76    239       O  
ATOM    137  CB  ILE A  15      39.412  29.053  19.766  1.00 20.25           C  
ANISOU  137  CB  ILE A  15     2364   2504   2823     32   -119    350       C  
ATOM    138  CG1 ILE A  15      39.800  28.658  18.358  1.00 20.60           C  
ANISOU  138  CG1 ILE A  15     2291   2455   3079     25      0     36       C  
ATOM    139  CG2 ILE A  15      38.851  30.490  19.837  1.00 21.18           C  
ANISOU  139  CG2 ILE A  15     2490   2746   2810     88     63    176       C  
ATOM    140  CD1 ILE A  15      38.683  28.751  17.327  1.00 21.65           C  
ANISOU  140  CD1 ILE A  15     2861   2788   2576    138      4    284       C  
ATOM    141  N   GLY A  16      42.988  28.933  20.033  1.00 20.73           N  
ANISOU  141  N   GLY A  16     2565   2614   2698   -162    253    197       N  
ATOM    142  CA  GLY A  16      44.269  29.560  19.588  1.00 21.67           C  
ANISOU  142  CA  GLY A  16     2546   2690   2996    -90    140     55       C  
ATOM    143  C   GLY A  16      44.881  30.485  20.615  1.00 22.64           C  
ANISOU  143  C   GLY A  16     2628   2882   3091    -66    111    114       C  
ATOM    144  O   GLY A  16      45.474  31.523  20.257  1.00 23.50           O  
ANISOU  144  O   GLY A  16     2604   2845   3480   -233    104     85       O  
ATOM    145  N   GLY A  17      44.704  30.167  21.891  1.00 22.50           N  
ANISOU  145  N   GLY A  17     2782   2834   2933    114   -111    -37       N  
ATOM    146  CA  GLY A  17      45.204  31.013  22.963  1.00 24.13           C  
ANISOU  146  CA  GLY A  17     2760   3188   3218     -7   -114   -164       C  
ATOM    147  C   GLY A  17      44.329  32.205  23.264  1.00 24.82           C  
ANISOU  147  C   GLY A  17     3030   3138   3262    -32   -123     -4       C  
ATOM    148  O   GLY A  17      44.626  32.986  24.172  1.00 26.21           O  
ANISOU  148  O   GLY A  17     2818   3442   3698     16   -242   -233       O  
ATOM    149  N   GLN A  18      43.250  32.379  22.490  1.00 24.20           N  
ANISOU  149  N   GLN A  18     2720   3115   3358    -69    -90    -16       N  
ATOM    150  CA  GLN A  18      42.363  33.514  22.680  1.00 23.77           C  
ANISOU  150  CA  GLN A  18     2886   2908   3235    -45    -89     87       C  
ATOM    151  C   GLN A  18      41.180  33.080  23.453  1.00 20.38           C  
ANISOU  151  C   GLN A  18     2455   2536   2752     -5   -297    171       C  
ATOM    152  O   GLN A  18      40.632  31.958  23.234  1.00 23.34           O  
ANISOU  152  O   GLN A  18     2935   2834   3097   -268   -116    115       O  
ATOM    153  CB  GLN A  18      41.925  34.104  21.341  1.00 24.54           C  
ANISOU  153  CB  GLN A  18     2974   3143   3204     12     36     55       C  
ATOM    154  CG  GLN A  18      42.454  35.522  21.084  1.00 29.98           C  
ANISOU  154  CG  GLN A  18     3790   3525   4076     34     26     16       C  
ATOM    155  CD  GLN A  18      41.801  36.211  19.885  1.00 33.48           C  
ANISOU  155  CD  GLN A  18     4117   4307   4295     19      0    105       C  
ATOM    156  OE1 GLN A  18      41.975  37.418  19.690  1.00 35.30           O  
ANISOU  156  OE1 GLN A  18     4345   4341   4724     57    -30     63       O  
ATOM    157  NE2 GLN A  18      41.051  35.455  19.094  1.00 34.31           N  
ANISOU  157  NE2 GLN A  18     4197   4338   4501    -60    -16    102       N  
ATOM    158  N   LEU A  19      40.728  33.939  24.307  1.00 19.98           N  
ANISOU  158  N   LEU A  19     2383   2650   2556   -110   -237    169       N  
ATOM    159  CA  LEU A  19      39.497  33.754  25.035  1.00 19.14           C  
ANISOU  159  CA  LEU A  19     2546   2253   2474   -181   -133     75       C  
ATOM    160  C   LEU A  19      38.381  34.536  24.326  1.00 19.33           C  
ANISOU  160  C   LEU A  19     2488   2253   2603   -212   -207    197       C  
ATOM    161  O   LEU A  19      38.515  35.721  24.036  1.00 20.02           O  
ANISOU  161  O   LEU A  19     2574   2155   2875   -307   -553    329       O  
ATOM    162  CB  LEU A  19      39.631  34.241  26.484  1.00 20.60           C  
ANISOU  162  CB  LEU A  19     2633   2755   2437   -205   -168    138       C  
ATOM    163  CG  LEU A  19      40.612  33.456  27.374  1.00 21.73           C  
ANISOU  163  CG  LEU A  19     2615   2953   2688   -163   -162     92       C  
ATOM    164  CD1 LEU A  19      40.508  33.937  28.818  1.00 22.81           C  
ANISOU  164  CD1 LEU A  19     2861   2956   2848   -185    -43   -145       C  
ATOM    165  CD2 LEU A  19      40.345  31.951  27.278  1.00 21.54           C  
ANISOU  165  CD2 LEU A  19     2480   2987   2716    -25   -440    216       C  
ATOM    166  N   LYS A  20      37.304  33.857  24.056  1.00 16.85           N  
ANISOU  166  N   LYS A  20     2220   2048   2134   -235   -448     21       N  
ATOM    167  CA  LYS A  20      36.109  34.468  23.403  1.00 16.34           C  
ANISOU  167  CA  LYS A  20     2188   2043   1976    -22   -239    105       C  
ATOM    168  C   LYS A  20      34.862  34.038  24.137  1.00 15.33           C  
ANISOU  168  C   LYS A  20     2066   1764   1995   -287   -251   -118       C  
ATOM    169  O   LYS A  20      34.871  33.051  24.799  1.00 17.48           O  
ANISOU  169  O   LYS A  20     2675   1669   2295     -6    -66    237       O  
ATOM    170  CB  LYS A  20      35.965  34.033  21.905  1.00 17.46           C  
ANISOU  170  CB  LYS A  20     2289   2051   2290     38   -221    -76       C  
ATOM    171  CG  LYS A  20      37.065  34.464  21.035  1.00 18.26           C  
ANISOU  171  CG  LYS A  20     2208   2726   2000      5   -632    249       C  
ATOM    172  CD  LYS A  20      36.970  33.801  19.681  1.00 21.51           C  
ANISOU  172  CD  LYS A  20     2821   3105   2246      2   -198    106       C  
ATOM    173  CE  LYS A  20      37.964  34.361  18.727  1.00 23.59           C  
ANISOU  173  CE  LYS A  20     3286   3372   2303    -53    -38   -106       C  
ATOM    174  NZ  LYS A  20      37.540  35.678  18.193  1.00 23.80           N  
ANISOU  174  NZ  LYS A  20     3072   3360   2609   -229   -111    162       N  
ATOM    175  N   GLU A  21      33.777  34.795  23.989  1.00 16.28           N  
ANISOU  175  N   GLU A  21     2182   1967   2033    -76   -263    167       N  
ATOM    176  CA  GLU A  21      32.488  34.392  24.456  1.00 17.47           C  
ANISOU  176  CA  GLU A  21     2236   2350   2051   -190   -376    172       C  
ATOM    177  C   GLU A  21      31.723  33.796  23.263  1.00 15.19           C  
ANISOU  177  C   GLU A  21     2078   2070   1624   -161   -245    123       C  
ATOM    178  O   GLU A  21      31.748  34.332  22.160  1.00 16.59           O  
ANISOU  178  O   GLU A  21     2616   2046   1641   -468   -370    286       O  
ATOM    179  CB  GLU A  21      31.715  35.596  24.974  1.00 17.55           C  
ANISOU  179  CB  GLU A  21     2358   2433   1877   -267   -442      1       C  
ATOM    180  CG  GLU A  21      32.227  36.206  26.231  1.00 24.34           C  
ANISOU  180  CG  GLU A  21     3119   3133   2993   -112   -460   -183       C  
ATOM    181  CD  GLU A  21      31.408  35.772  27.439  1.00 31.27           C  
ANISOU  181  CD  GLU A  21     4318   3957   3604   -138    -36   -117       C  
ATOM    182  OE1 GLU A  21      31.782  34.755  28.044  1.00 34.21           O  
ANISOU  182  OE1 GLU A  21     4631   4097   4268    320   -170   -135       O  
ATOM    183  OE2 GLU A  21      30.311  36.393  27.718  1.00 35.10           O  
ANISOU  183  OE2 GLU A  21     4688   4462   4183     25   -138    -59       O  
ATOM    184  N   ALA A  22      31.036  32.718  23.501  1.00 12.61           N  
ANISOU  184  N   ALA A  22     1656   1650   1482     12   -284    168       N  
ATOM    185  CA  ALA A  22      30.233  32.068  22.487  1.00 12.04           C  
ANISOU  185  CA  ALA A  22     1695   1406   1472   -153   -217    129       C  
ATOM    186  C   ALA A  22      28.955  31.552  23.064  1.00 12.60           C  
ANISOU  186  C   ALA A  22     1795   1594   1396   -151    -53     30       C  
ATOM    187  O   ALA A  22      28.867  31.243  24.227  1.00 14.48           O  
ANISOU  187  O   ALA A  22     1805   2243   1451   -142    -80    185       O  
ATOM    188  CB  ALA A  22      30.987  30.936  21.811  1.00 13.79           C  
ANISOU  188  CB  ALA A  22     1697   1928   1614   -236   -250     75       C  
ATOM    189  N   LEU A  23      27.961  31.404  22.200  1.00 12.24           N  
ANISOU  189  N   LEU A  23     1782   1691   1176   -138    -79    -11       N  
ATOM    190  CA  LEU A  23      26.661  30.968  22.554  1.00 11.83           C  
ANISOU  190  CA  LEU A  23     1736   1621   1138     75      9    -49       C  
ATOM    191  C   LEU A  23      26.480  29.487  22.282  1.00 12.65           C  
ANISOU  191  C   LEU A  23     1753   1685   1369    -66     20   -149       C  
ATOM    192  O   LEU A  23      26.667  29.022  21.168  1.00 13.20           O  
ANISOU  192  O   LEU A  23     1964   1800   1249     64    -11   -169       O  
ATOM    193  CB  LEU A  23      25.658  31.784  21.699  1.00 13.73           C  
ANISOU  193  CB  LEU A  23     1859   1991   1364    110     29   -139       C  
ATOM    194  CG  LEU A  23      24.178  31.589  21.919  1.00 14.67           C  
ANISOU  194  CG  LEU A  23     1915   1862   1796    102    -14     27       C  
ATOM    195  CD1 LEU A  23      23.743  32.109  23.249  1.00 16.90           C  
ANISOU  195  CD1 LEU A  23     2253   2425   1741    193     11    181       C  
ATOM    196  CD2 LEU A  23      23.387  32.254  20.783  1.00 14.56           C  
ANISOU  196  CD2 LEU A  23     1587   2131   1814    117   -344   -100       C  
ATOM    197  N   LEU A  24      26.074  28.733  23.303  1.00 12.22           N  
ANISOU  197  N   LEU A  24     1855   1673   1114      4    -69   -187       N  
ATOM    198  CA  LEU A  24      25.705  27.345  23.097  1.00 12.86           C  
ANISOU  198  CA  LEU A  24     1658   1638   1588     86     62   -207       C  
ATOM    199  C   LEU A  24      24.354  27.264  22.392  1.00 12.25           C  
ANISOU  199  C   LEU A  24     1574   1684   1393    -50     41   -275       C  
ATOM