CNRS Nantes University UFIP UFIP
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***  ANT1-IMM-Facing  ***

elNémo ID: 22021517104814522

Job options:

ID        	=	 22021517104814522
JOBID     	=	 ANT1-IMM-Facing
USERID    	=	 sureshv
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER ANT1-IMM-Facing

HEADER    MEMBRANE PROTEIN                        17-APR-18   6GCI
TITLE     STRUCTURE OF THE BONGKREKIC ACID-INHIBITED MITOCHONDRIAL
TITLE    2 ADP/ATP CARRIER
EXPDTA    X-RAY DIFFRACTION
REMARK   2 RESOLUTION.    3.30 ANGSTROMS
REMARK   3  R VALUE : 0.252000
REMARK   3  FREE R VALUE : 0.283000
REMARK   4 6GCI COMPLIES WITH FORMAT V. 3.30,
REMARK 200  TEMPERATURE           (KELVIN) : 100.00
REMARK 200  PH                             : NULL
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1  1   1.000000 0.000000 0.000000   0.000000
REMARK 350   BIOMT2  1   0.000000 1.000000 0.000000   0.000000
REMARK 350   BIOMT3  1   0.000000 0.000000 1.000000   0.000000
REMARK 888
REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC)
CRYST1   75.650   75.650  295.480  90.00  90.00 120.00 P 32 2 1      6
ATOM      1  N   GLY A  11     -48.987  29.985  -1.194  1.00271.91           N  
ANISOU    1  N   GLY A  11    29680  37189  36445  -1405   1931   -466
ATOM      2  CA  GLY A  11     -49.769  28.767  -1.154  1.00298.87           C  
ANISOU    2  CA  GLY A  11    37607  37982  37969    -72    101     19
ATOM      3  C   GLY A  11     -48.916  27.484  -1.294  1.00153.65           C  
ANISOU    3  C   GLY A  11    13277  24472  20630  -3955   3194  -3756
ATOM      4  O   GLY A  11     -49.492  26.396  -1.299  1.00175.71           O  
ANISOU    4  O   GLY A  11    15998  27520  23243  -4405   3198  -3763
ATOM      5  H1  GLY A  11     -49.583  30.781  -1.378  1.00  0.00           H  
ATOM      6  H2  GLY A  11     -48.563  30.161  -0.294  1.00  0.00           H  
ATOM      7  HA3 GLY A  11     -50.510  28.777  -1.954  1.00  0.00           H  
ATOM      8  HA2 GLY A  11     -50.339  28.714  -0.225  1.00  0.00           H  
ATOM      9  N   MET A  12     -47.579  27.591  -1.411  1.00150.35           N  
ANISOU    9  N   MET A  12    13464  23629  20032  -3817   3102  -3599
ATOM     10  CA  MET A  12     -46.629  26.480  -1.524  1.00150.34           C  
ANISOU   10  CA  MET A  12    14100  23392  19632  -4120   2999  -3419
ATOM     11  C   MET A  12     -45.973  26.147  -0.162  1.00149.03           C  
ANISOU   11  C   MET A  12    14460  22985  19179  -4290   3307  -3497
ATOM     12  O   MET A  12     -46.132  26.920   0.785  1.00148.27           O  
ANISOU   12  O   MET A  12    14245  22889  19200  -4135   3563  -3675
ATOM     13  CB  MET A  12     -45.575  26.854  -2.597  1.00  0.00           C  
ATOM     14  CG  MET A  12     -45.918  26.294  -3.982  1.00  0.00           C  
ATOM     15  SD  MET A  12     -44.742  26.773  -5.274  1.00  0.00           S  
ATOM     16  CE  MET A  12     -45.176  25.562  -6.550  1.00  0.00           C  
ATOM     17  H   MET A  12     -47.176  28.517  -1.396  1.00  0.00           H  
ATOM     18  HA  MET A  12     -47.171  25.593  -1.853  1.00  0.00           H  
ATOM     19  HB2 MET A  12     -45.466  27.938  -2.662  1.00  0.00           H  
ATOM     20  HB3 MET A  12     -44.580  26.499  -2.325  1.00  0.00           H  
ATOM     21  HG2 MET A  12     -45.949  25.206  -3.934  1.00  0.00           H  
ATOM     22  HG3 MET A  12     -46.912  26.623  -4.286  1.00  0.00           H  
ATOM     23  HE1 MET A  12     -44.560  25.715  -7.435  1.00  0.00           H  
ATOM     24  HE2 MET A  12     -45.011  24.548  -6.186  1.00  0.00           H  
ATOM     25  HE3 MET A  12     -46.224  25.666  -6.834  1.00  0.00           H  
ATOM     26  N   PRO A  13     -45.200  25.031  -0.091  1.00141.18           N  
ANISOU   26  N   PRO A  13    14057  21770  17815  -4590   3282  -3367
ATOM     27  CA  PRO A  13     -44.340  24.713   1.074  1.00139.48           C  
ANISOU   27  CA  PRO A  13    14339  21323  17333  -4733   3523  -3408
ATOM     28  C   PRO A  13     -43.289  25.800   1.394  1.00137.04           C  
ANISOU   28  C   PRO A  13    14199  20731  17139  -4306   3496  -3374
ATOM     29  O   PRO A  13     -42.951  26.582   0.504  1.00136.00           O  
ANISOU   29  O   PRO A  13    13874  20531  17269  -3905   3265  -3285
ATOM     30  CB  PRO A  13     -43.644  23.401   0.656  1.00139.53           C  
ANISOU   30  CB  PRO A  13    14906  21106  17003  -5015   3388  -3217
ATOM     31  CG  PRO A  13     -44.566  22.768  -0.368  1.00141.32           C  
ANISOU   31  CG  PRO A  13    14886  21558  17252  -5217   3230  -3181
ATOM     32  CD  PRO A  13     -45.135  23.970  -1.102  1.00142.29           C  
ANISOU   32  CD  PRO A  13    14451  21853  17759  -4819   3040  -3183
ATOM     33  HA  PRO A  13     -45.003  24.542   1.924  1.00  0.00           H  
ATOM     34  HB3 PRO A  13     -43.459  22.728   1.493  1.00  0.00           H  
ATOM     35  HB2 PRO A  13     -42.681  23.609   0.188  1.00  0.00           H  
ATOM     36  HG3 PRO A  13     -45.371  22.244   0.149  1.00  0.00           H  
ATOM     37  HG2 PRO A  13     -44.066  22.055  -1.023  1.00  0.00           H  
ATOM     38  HD2 PRO A  13     -44.466  24.267  -1.908  1.00  0.00           H  
ATOM     39  HD3 PRO A  13     -46.102  23.718  -1.535  1.00  0.00           H  
ATOM     40  N   PRO A  14     -42.737  25.800   2.631  1.00126.54           N  
ANISOU   40  N   PRO A  14    13252  19227  15602  -4402   3708  -3430
ATOM     41  CA  PRO A  14     -41.685  26.760   3.016  1.00124.47           C  
ANISOU   41  CA  PRO A  14    13162  18702  15430  -4031   3661  -3393
ATOM     42  C   PRO A  14     -40.377  26.598   2.220  1.00121.14           C  
ANISOU   42  C   PRO A  14    13107  17975  14944  -3848   3339  -3124
ATOM     43  O   PRO A  14     -39.736  27.601   1.921  1.00119.82           O  
ANISOU   43  O   PRO A  14    12979  17627  14920  -3500   3214  -3059
ATOM     44  CB  PRO A  14     -41.489  26.507   4.521  1.00125.87           C  
ANISOU   44  CB  PRO A  14    13682  18812  15333  -4291   3953  -3509
ATOM     45  CG  PRO A  14     -41.902  25.058   4.725  1.00126.85           C  
ANISOU   45  CG  PRO A  14    14090  18977  15129  -4769   4003  -3451
ATOM     46  CD  PRO A  14     -43.050  24.887   3.734  1.00128.98           C  
ANISOU   46  CD  PRO A  14    13895  19554  15558  -4875   3970  -3507
ATOM     47  HA  PRO A  14     -42.044  27.780   2.865  1.00  0.00           H  
ATOM     48  HB3 PRO A  14     -42.157  27.161   5.084  1.00  0.00           H  
ATOM     49  HB2 PRO A  14     -40.474  26.704   4.871  1.00  0.00           H  
ATOM     50  HG3 PRO A  14     -42.181  24.827   5.753  1.00  0.00           H  
ATOM     51  HG2 PRO A  14     -41.076  24.402   4.446  1.00  0.00           H  
ATOM     52  HD2 PRO A  14     -43.145  23.845   3.431  1.00  0.00           H  
ATOM     53  HD3 PRO A  14     -43.994  25.199   4.185  1.00  0.00           H  
ATOM     54  N   PHE A  15     -40.038  25.347   1.863  1.00113.24           N  
ANISOU   54  N   PHE A  15    12384  16916  13725  -4098   3223  -2980
ATOM     55  CA  PHE A  15     -38.844  24.991   1.101  1.00110.60           C  
ANISOU   55  CA  PHE A  15    12407  16308  13310  -3969   2966  -2751
ATOM     56  C   PHE A  15     -38.931  25.412  -0.375  1.00110.29           C  
ANISOU   56  C   PHE A  15    12106  16313  13485  -3736   2704  -2650
ATOM     57  O   PHE A  15     -37.960  25.962  -0.893  1.00108.34           O  
ANISOU   57  O   PHE A  15    11954  15877  13332  -3432   2524  -2525
ATOM     58  CB  PHE A  15     -38.604  23.473   1.239  1.00109.89           C  
ANISOU   58  CB  PHE A  15    12741  16110  12902  -4332   2980  -2662
ATOM     59  CG  PHE A  15     -37.299  22.968   0.646  1.00107.13           C  
ANISOU   59  CG  PHE A  15    12799  15446  12458  -4191   2772  -2451
ATOM     60  CD1 PHE A  15     -36.121  23.022   1.418  1.00105.59           C  
ANISOU   60  CD1 PHE A  15    12963  15009  12149  -4101   2774  -2372
ATOM     61  CD2 PHE A  15     -37.209  22.607  -0.716  1.00106.35           C  
ANISOU   61  CD2 PHE A  15    12714  15308  12387  -4155   2574  -2338
ATOM     62  CE1 PHE A  15     -34.906  22.651   0.862  1.00103.38           C  
ANISOU   62  CE1 PHE A  15    13002  14461  11816  -3948   2589  -2186
ATOM     63  CE2 PHE A  15     -35.980  22.257  -1.260  1.00104.14           C  
ANISOU   63  CE2 PHE A  15    12783  14748  12039  -4011   2419  -2170
ATOM     64  CZ  PHE A  15     -34.835  22.270  -0.472  1.00102.69           C  
ANISOU   64  CZ  PHE A  15    12910  14334  11772  -3897   2431  -2097
ATOM     65  H   PHE A  15     -40.628  24.579   2.148  1.00  0.00           H  
ATOM     66  HA  PHE A  15     -37.996  25.512   1.550  1.00  0.00           H  
ATOM     67  HB3 PHE A  15     -39.432  22.919   0.793  1.00  0.00           H  
ATOM     68  HB2 PHE A  15     -38.607  23.207   2.297  1.00  0.00           H  
ATOM     69  HD1 PHE A  15     -36.165  23.349   2.446  1.00  0.00           H  
ATOM     70  HD2 PHE A  15     -38.090  22.611  -1.341  1.00  0.00           H  
ATOM     71  HE1 PHE A  15     -34.010  22.676   1.462  1.00  0.00           H  
ATOM     72  HE2 PHE A  15     -35.912  21.979  -2.302  1.00  0.00           H  
ATOM     73  HZ  PHE A  15     -33.882  22.000  -0.903  1.00  0.00           H  
ATOM     74  N   VAL A  16     -40.075  25.129  -1.026  1.00103.63           N  
ANISOU   74  N   VAL A  16    10952  15726  12698  -3904   2670  -2694
ATOM     75  CA  VAL A  16     -40.281  25.376  -2.457  1.00102.88           C  
ANISOU   75  CA  VAL A  16    10634  15691  12764  -3738   2392  -2581
ATOM     76  C   VAL A  16     -40.358  26.881  -2.783  1.00102.33           C  
ANISOU   76  C   VAL A  16    10243  15622  13014  -3306   2283  -2582
ATOM     77  O   VAL A  16     -39.882  27.283  -3.843  1.00100.42           O  
ANISOU   77  O   VAL A  16    10032  15266  12857  -3083   2028  -2427
ATOM     78  CB  VAL A  16     -41.560  24.675  -2.997  1.00109.03           C  
ANISOU   78  CB  VAL A  16    11114  16781  13533  -4039   2373  -2638
ATOM     79  CG1 VAL A  16     -41.814  24.905  -4.503  1.00109.34           C  
ANISOU   79  CG1 VAL A  16    10992  16871  13682  -3912   2050  -2495
ATOM     80  CG2 VAL A  16     -41.525  23.158  -2.735  1.00108.68           C  
ANISOU   80  CG2 VAL A  16    11450  16693  13151  -4495   2499  -2643
ATOM     81  H   VAL A  16     -40.838  24.692  -0.532  1.00  0.00           H  
ATOM     82  HA  VAL A  16     -39.423  24.961  -2.987  1.00  0.00           H  
ATOM     83  HB  VAL A  16     -42.415  25.081  -2.456  1.00  0.00           H  
ATOM     84 HG11 VAL A  16     -42.681  24.338  -4.845  1.00  0.00           H  
ATOM     85 HG12 VAL A  16     -42.013  25.950  -4.737  1.00  0.00           H  
ATOM     86 HG13 VAL A  16     -40.958  24.590  -5.100  1.00  0.00           H  
ATOM     87 HG21 VAL A  16     -42.435  22.676  -3.093  1.00  0.00           H  
ATOM     88 HG22 VAL A  16     -40.681  22.691  -3.244  1.00  0.00           H  
ATOM     89 HG23 VAL A  16     -41.438  22.927  -1.675  1.00  0.00           H  
ATOM     90  N   VAL A  17     -40.887  27.691  -1.850  1.00104.12           N  
ANISOU   90  N   VAL A  17    10212  15947  13403  -3194   2488  -2759
ATOM     91  CA  VAL A  17     -40.876  29.150  -1.942  1.00104.21           C  
ANISOU   91  CA  VAL A  17     9961  15908  13725  -2771   2417  -2781
ATOM     92  C   VAL A  17     -39.443  29.724  -1.913  1.00101.88           C  
ANISOU   92  C   VAL A  17    10063  15271  13375  -2547   2302  -2638
ATOM     93  O   VAL A  17     -39.119  30.533  -2.779  1.00100.98           O  
ANISOU   93  O   VAL A  17     9900  15055  13412  -2279   2057  -2502
ATOM     94  CB  VAL A  17     -41.759  29.797  -0.838  1.00108.75           C  
ANISOU   94  CB  VAL A  17    10229  16629  14461  -2718   2718  -3036
ATOM     95  CG1 VAL A  17     -41.564  31.314  -0.661  1.00108.53           C  
ANISOU   95  CG1 VAL A  17    10113  16424  14697  -2283   2691  -3065
ATOM     96  CG2 VAL A  17     -43.249  29.512  -1.099  1.00110.15           C  
ANISOU   96  CG2 VAL A  17     9866  17183  14805  -2836   2771  -3163
ATOM     97  H   VAL A  17     -41.259  27.299  -0.995  1.00  0.00           H  
ATOM     98  HA  VAL A  17     -41.308  29.414  -2.910  1.00  0.00           H  
ATOM     99  HB  VAL A  17     -41.513  29.327   0.116  1.00  0.00           H  
ATOM    100 HG11 VAL A  17     -42.397  31.751  -0.113  1.00  0.00           H  
ATOM    101 HG12 VAL A  17     -40.659  31.536  -0.098  1.00  0.00           H  
ATOM    102 HG13 VAL A  17     -41.507  31.824  -1.623  1.00  0.00           H  
ATOM    103 HG21 VAL A  17     -43.871  29.864  -0.275  1.00  0.00           H  
ATOM    104 HG22 VAL A  17     -43.592  30.004  -2.009  1.00  0.00           H  
ATOM    105 HG23 VAL A  17     -43.441  28.446  -1.214  1.00  0.00           H  
ATOM    106  N   ASP A  18     -38.598  29.243  -0.982  1.00103.76           N  
ANISOU  106  N   ASP A  18    10702  15343  13380  -2686   2456  -2651
ATOM    107  CA  ASP A  18     -37.167  29.578  -0.893  1.00100.77           C  
ANISOU  107  CA  ASP A  18    10676  14672  12938  -2508   2348  -2519
ATOM    108  C   ASP A  18     -36.346  29.112  -2.109  1.00 98.94           C  
ANISOU  108  C   ASP A  18    10620  14333  12640  -2482   2090  -2308
ATOM    109  O   ASP A  18     -35.405  29.809  -2.489  1.00 97.31           O  
ANISOU  109  O   ASP A  18    10489  13965  12520  -2240   1929  -2195
ATOM    110  CB  ASP A  18     -36.502  29.074   0.408  1.00107.94           C  
ANISOU  110  CB  ASP A  18    11966  15455  13593  -2696   2522  -2549
ATOM    111  CG  ASP A  18     -37.181  29.503   1.713  1.00106.53           C  
ANISOU  111  CG  ASP A  18    11685  15373  13418  -2776   2809  -2771
ATOM    112  OD1 ASP A  18     -37.939  30.499   1.693  1.00106.11           O  
ANISOU  112  OD1 ASP A  18    11240  15459  13619  -2612   2890  -2920
ATOM    113  OD2 ASP A  18     -36.878  28.848   2.733  1.00105.39           O1-
ANISOU  113  OD2 ASP A  18    11854  15163  13025  -3000   2957  -2801
ATOM    114  H   ASP A  18     -38.938  28.587  -0.293  1.00  0.00           H  
ATOM    115  HA  ASP A  18     -37.100  30.667  -0.882  1.00  0.00           H  
ATOM    116  HB3 ASP A  18     -35.462  29.401   0.446  1.00  0.00           H  
ATOM    117  HB2 ASP A  18     -36.518  27.984   0.387  1.00  0.00           H  
ATOM    118  N   PHE A  19     -36.729  27.971  -2.712  1.00 91.31           N  
ANISOU  118  N   PHE A  19     9730  13453  11510  -2750   2065  -2265
ATOM    119  CA  PHE A  19     -36.142  27.440  -3.944  1.00 90.43           C  
ANISOU  119  CA  PHE A  19     9799  13246  11313  -2761   1857  -2096
ATOM    120  C   PHE A  19     -36.410  28.360  -5.144  1.00 91.50           C  
ANISOU  120  C   PHE A  19     9664  13439  11663  -2529   1628  -2018
ATOM    121  O   PHE A  19     -35.465  28.726  -5.841  1.00 90.60           O  
ANISOU  121  O   PHE A  19     9709  13156  11558  -2359   1476  -1885
ATOM    122  CB  PHE A  19     -36.612  25.981  -4.172  1.00 90.84           C  
ANISOU  122  CB  PHE A  19     9957  13394  11165  -3115   1893  -2103
ATOM    123  CG  PHE A  19     -36.086  25.280  -5.417  1.00 90.07           C  
ANISOU  123  CG  PHE A  19    10080  13186  10957  -3153   1714  -1959
ATOM    124  CD1 PHE A  19     -34.888  24.536  -5.365  1.00 89.06           C  
ANISOU  124  CD1 PHE A  19    10380  12816  10642  -3202   1742  -1882
ATOM    125  CD2 PHE A  19     -36.698  25.493  -6.672  1.00 90.56           C  
ANISOU  125  CD2 PHE A  19     9925  13387  11099  -3142   1519  -1904
ATOM    126  CE1 PHE A  19     -34.359  23.995  -6.531  1.00 88.53           C  
ANISOU  126  CE1 PHE A  19    10517  12642  10477  -3234   1621  -1781
ATOM    127  CE2 PHE A  19     -36.149  24.949  -7.825  1.00 89.99           C  
ANISOU  127  CE2 PHE A  19    10087  13213  10892  -3210   1382  -1792
ATOM    128  CZ  PHE A  19     -34.984  24.200  -7.753  1.00 89.00           C  
ANISOU  128  CZ  PHE A  19    10384  12844  10589  -3255   1455  -1746
ATOM    129  H   PHE A  19     -37.491  27.439  -2.314  1.00  0.00           H  
ATOM    130  HA  PHE A  19     -35.064  27.420  -3.807  1.00  0.00           H  
ATOM    131  HB3 PHE A  19     -37.699  25.951  -4.214  1.00  0.00           H  
ATOM    132  HB2 PHE A  19     -36.336  25.376  -3.308  1.00  0.00           H  
ATOM    133  HD1 PHE A  19     -34.374  24.394  -4.425  1.00  0.00           H  
ATOM    134  HD2 PHE A  19     -37.589  26.093  -6.744  1.00  0.00           H  
ATOM    135  HE1 PHE A  19     -33.443  23.431  -6.498  1.00  0.00           H  
ATOM    136  HE2 PHE A  19     -36.625  25.118  -8.779  1.00  0.00           H  
ATOM    137  HZ  PHE A  19     -34.554  23.784  -8.653  1.00  0.00           H  
ATOM    138  N   LEU A  20     -37.683  28.748  -5.329  1.00 95.33           N  
ANISOU  138  N   LEU A  20     9735  14162  12322  -2519   1602  -2095
ATOM    139  CA  LEU A  20     -38.124  29.666  -6.380  1.00 96.32           C  
ANISOU  139  CA  LEU A  20     9598  14347  12653  -2303   1348  -1999
ATOM    140  C   LEU A  20     -37.533  31.078  -6.213  1.00 95.46           C  
ANISOU  140  C   LEU A  20     9475  14056  12742  -1942   1297  -1970
ATOM    141  O   LEU A  20     -37.098  31.643  -7.214  1.00 94.68           O  
ANISOU  141  O   LEU A  20     9429  13851  12696  -1780   1066  -1815
ATOM    142  CB  LEU A  20     -39.671  29.698  -6.454  1.00 99.01           C  
ANISOU  142  CB  LEU A  20     9462  14999  13158  -2363   1323  -2088
ATOM    143  CG  LEU A  20     -40.288  28.764  -7.525  1.00100.36           C  
ANISOU  143  CG  LEU A  20     9598  15350  13183  -2655   1171  -2017
ATOM    144  CD1 LEU A  20     -40.065  27.264  -7.241  1.00 99.28           C  
ANISOU  144  CD1 LEU A  20     9754  15215  12754  -3040   1369  -2084
ATOM    145  CD2 LEU A  20     -41.779  29.092  -7.746  1.00104.44           C  
ANISOU  145  CD2 LEU A  20     9577  16194  13910  -2664   1080  -2076
ATOM    146  H   LEU A  20     -38.403  28.407  -4.706  1.00  0.00           H  
ATOM    147  HA  LEU A  20     -37.741  29.281  -7.327  1.00  0.00           H  
ATOM    148  HB3 LEU A  20     -39.990  30.711  -6.706  1.00  0.00           H  
ATOM    149  HB2 LEU A  20     -40.110  29.502  -5.474  1.00  0.00           H  
ATOM    150  HG  LEU A  20     -39.785  28.984  -8.469  1.00  0.00           H  
ATOM    151 HD11 LEU A  20     -39.500  26.798  -8.049  1.00  0.00           H  
ATOM    152 HD12 LEU A  20     -39.509  27.099  -6.323  1.00  0.00           H  
ATOM    153 HD13 LEU A  20     -40.995  26.706  -7.136  1.00  0.00           H  
ATOM    154 HD21 LEU A  20     -42.402  28.204  -7.854  1.00  0.00           H  
ATOM    155 HD22 LEU A  20     -42.193  29.672  -6.920  1.00  0.00           H  
ATOM    156 HD23 LEU A  20     -41.912  29.682  -8.653  1.00  0.00           H  
ATOM    157  N   MET A  21     -37.476  31.601  -4.973  1.00 97.49           N  
ANISOU  157  N   MET A  21     9712  14257  13071  -1849   1519  -2117
ATOM    158  CA  MET A  21     -36.847  32.889  -4.664  1.00 96.58           C  
ANISOU  158  CA  MET A  21     9627  13944  13126  -1536   1495  -2111
ATOM    159  C   MET A  21     -35.337  32.903  -4.949  1.00 93.35           C  
ANISOU  159  C   MET A  21     9616  13288  12564  -1504   1391  -1954
ATOM    160  O   MET A  21     -34.863  33.861  -5.556  1.00 92.47           O  
ANISOU  160  O   MET A  21     9531  13040  12564  -1293   1213  -1840
ATOM    161  CB  MET A  21     -37.108  33.309  -3.203  1.00101.43           C  
ANISOU  161  CB  MET A  21    10199  14546  13795  -1504   1784  -2322
ATOM    162  CG  MET A  21     -38.521  33.838  -2.924  1.00104.89           C  
ANISOU  162  CG  MET A  21    10181  15202  14469  -1433   1908  -2505
ATOM    163  SD  MET A  21     -38.692  34.674  -1.321  1.00106.50           S  
ANISOU  163  SD  MET A  21    10375  15318  14771  -1313   2248  -2765
ATOM    164  CE  MET A  21     -38.176  33.363  -0.183  1.00105.33           C  
ANISOU  164  CE  MET A  21    10634  15166  14220  -1721   2488  -2821
ATOM    165  H   MET A  21     -37.865  31.088  -4.192  1.00  0.00           H  
ATOM    166  HA  MET A  21     -37.298  33.633  -5.320  1.00  0.00           H  
ATOM    167  HB3 MET A  21     -36.403  34.088  -2.910  1.00  0.00           H  
ATOM    168  HB2 MET A  21     -36.911  32.459  -2.551  1.00  0.00           H  
ATOM    169  HG3 MET A  21     -39.256  33.038  -2.981  1.00  0.00           H  
ATOM    170  HG2 MET A  21     -38.800  34.560  -3.691  1.00  0.00           H  
ATOM    171  HE1 MET A  21     -38.441  33.621   0.841  1.00  0.00           H  
ATOM    172  HE2 MET A  21     -38.656  32.421  -0.439  1.00  0.00           H  
ATOM    173  HE3 MET A  21     -37.099  33.221  -0.235  1.00  0.00           H  
ATOM    174  N   GLY A  22     -34.621  31.845  -4.529  1.00 89.69           N  
ANISOU  174  N   GLY A  22     9452  12773  11853  -1717   1500  -1946
ATOM    175  CA  GLY A  22     -33.177  31.695  -4.715  1.00 87.73           C  
ANISOU  175  CA  GLY A  22     9546  12325  11464  -1702   1426  -1812
ATOM    176  C   GLY A  22     -32.803  31.507  -6.191  1.00 87.03           C  
ANISOU  176  C   GLY A  22     9502  12219  11346  -1691   1204  -1648
ATOM    177  O   GLY A  22     -31.762  32.005  -6.614  1.00 85.75           O  
ANISOU  177  O   GLY A  22     9481  11909  11192  -1566   1094  -1538
ATOM    178  H   GLY A  22     -35.091  31.100  -4.029  1.00  0.00           H  
ATOM    179  HA3 GLY A  22     -32.848  30.817  -4.161  1.00  0.00           H  
ATOM    180  HA2 GLY A  22     -32.645  32.553  -4.303  1.00  0.00           H  
ATOM    181  N   GLY A  23     -33.662  30.826  -6.970  1.00 82.05           N  
ANISOU  181  N   GLY A  23     8759  11752  10665  -1854   1146  -1638
ATOM    182  CA  GLY A  23     -33.472  30.581  -8.396  1.00 81.84           C  
ANISOU  182  CA  GLY A  23     8785  11736  10575  -1898    942  -1499
ATOM    183  C   GLY A  23     -33.734  31.852  -9.212  1.00 82.97           C  
ANISOU  183  C   GLY A  23     8763  11859  10902  -1676    728  -1402
ATOM    184  O   GLY A  23     -32.919  32.188 -10.070  1.00 81.93           O  
ANISOU  184  O   GLY A  23     8812  11599  10719  -1617    600  -1271
ATOM    185  H   GLY A  23     -34.493  30.431  -6.550  1.00  0.00           H  
ATOM    186  HA3 GLY A  23     -34.171  29.807  -8.712  1.00  0.00           H  
ATOM    187  HA2 GLY A  23     -32.466  30.205  -8.589  1.00  0.00           H  
ATOM    188  N   VAL A  24     -34.847  32.561  -8.945  1.00 77.29           N  
ANISOU  188  N   VAL A  24     7700  11264  10403  -1551    692  -1466
ATOM    189  CA  VAL A  24     -35.209  33.820  -9.607  1.00 78.32           C  
ANISOU  189  CA  VAL A  24     7659  11356  10744  -1306    465  -1366
ATOM    190  C   VAL A  24     -34.185  34.936  -9.332  1.00 78.15           C  
ANISOU  190  C   VAL A  24     7851  11070  10771  -1105    466  -1315
ATOM    191  O   VAL A  24     -33.778  35.613 -10.272  1.00 78.25           O  
ANISOU  191  O   VAL A  24     7983  10971  10776  -1032    264  -1154
ATOM    192  CB  VAL A  24     -36.641  34.296  -9.211  1.00 81.68           C  
ANISOU  192  CB  VAL A  24     7652  11944  11437  -1165    472  -1476
ATOM    193  CG1 VAL A  24     -36.977  35.769  -9.542  1.00 82.21           C  
ANISOU  193  CG1 VAL A  24     7572  11907  11757   -851    241  -1370
ATOM    194  CG2 VAL A  24     -37.706  33.389  -9.853  1.00 84.07           C  
ANISOU  194  CG2 VAL A  24     7712  12538  11691  -1390    417  -1498
ATOM    195  H   VAL A  24     -35.493  32.230  -8.238  1.00  0.00           H  
ATOM    196  HA  VAL A  24     -35.200  33.631 -10.683  1.00  0.00           H  
ATOM    197  HB  VAL A  24     -36.738  34.189  -8.129  1.00  0.00           H  
ATOM    198 HG11 VAL A  24     -38.025  35.985  -9.334  1.00  0.00           H  
ATOM    199 HG12 VAL A  24     -36.394  36.471  -8.945  1.00  0.00           H  
ATOM    200 HG13 VAL A  24     -36.798  35.989 -10.595  1.00  0.00           H  
ATOM    201 HG21 VAL A  24     -38.703  33.624  -9.479  1.00  0.00           H  
ATOM    202 HG22 VAL A  24     -37.721  33.509 -10.937  1.00  0.00           H  
ATOM    203 HG23 VAL A  24     -37.523  32.334  -9.650  1.00  0.00           H  
ATOM    204  N   SER A  25     -33.744  35.055  -8.068  1.00 81.66           N  
ANISOU  204  N   SER A  25     8366  11425  11236  -1058    694  -1451
ATOM    205  CA  SER A  25     -32.678  35.955  -7.631  1.00 80.09           C  
ANISOU  205  CA  SER A  25     8372  10994  11063   -917    726  -1433
ATOM    206  C   SER A  25     -31.335  35.690  -8.339  1.00 78.57           C  
ANISOU  206  C   SER A  25     8489  10696  10667  -1025    653  -1289
ATOM    207  O   SER A  25     -30.666  36.644  -8.732  1.00 77.87           O  
ANISOU  207  O   SER A  25     8529  10447  10610   -921    547  -1190
ATOM    208  CB  SER A  25     -32.546  35.849  -6.100  1.00 86.56           C  
ANISOU  208  CB  SER A  25     9232  11782  11875   -932    990  -1614
ATOM    209  OG  SER A  25     -31.508  36.668  -5.623  1.00 86.19           O  
ANISOU  209  OG  SER A  25     9423  11528  11798   -863   1013  -1590
ATOM    210  H   SER A  25     -34.134  34.457  -7.351  1.00  0.00           H  
ATOM    211  HA  SER A  25     -32.986  36.971  -7.883  1.00  0.00           H  
ATOM    212  HB3 SER A  25     -32.341  34.823  -5.794  1.00  0.00           H  
ATOM    213  HB2 SER A  25     -33.473  36.157  -5.613  1.00  0.00           H  
ATOM    214  HG  SER A  25     -31.343  36.465  -4.697  1.00  0.00           H  
ATOM    215  N   ALA A  26     -30.992  34.402  -8.511  1.00 72.56           N  
ANISOU  215  N   ALA A  26     7848  10018   9703  -1236    720  -1284
ATOM    216  CA  ALA A  26     -29.789  33.944  -9.199  1.00 71.29           C  
ANISOU  216  CA  ALA A  26     7948   9775   9366  -1329    686  -1176
ATOM    217  C   ALA A  26     -29.799  34.238 -10.704  1.00 72.37           C  
ANISOU  217  C   ALA A  26     8102   9913   9483  -1332    467  -1024
ATOM    218  O   ALA A  26     -28.768  34.656 -11.229  1.00 72.00           O  
ANISOU  218  O   ALA A  26     8227   9748   9383  -1313    407   -926
ATOM    219  CB  ALA A  26     -29.599  32.452  -8.921  1.00 71.67           C  
ANISOU  219  CB  ALA A  26     8108   9891   9233  -1526    811  -1220
ATOM    220  H   ALA A  26     -31.595  33.676  -8.148  1.00  0.00           H  
ATOM    221  HA  ALA A  26     -28.938  34.473  -8.770  1.00  0.00           H  
ATOM    222  HB1 ALA A  26     -28.726  32.045  -9.426  1.00  0.00           H  
ATOM    223  HB2 ALA A  26     -29.455  32.307  -7.853  1.00  0.00           H  
ATOM    224  HB3 ALA A  26     -30.460  31.859  -9.227  1.00  0.00           H  
ATOM    225  N   ALA A  27     -30.964  34.062 -11.354  1.00 70.25           N  
ANISOU  225  N   ALA A  27     7652   9793   9246  -1381    340  -1004
ATOM    226  CA  ALA A  27     -31.187  34.391 -12.760  1.00 71.04           C  
ANISOU  226  CA  ALA A  27     7767   9919   9306  -1415     99   -851
ATOM    227  C   ALA A  27     -31.086  35.898 -13.041  1.00 71.15           C  
ANISOU  227  C   ALA A  27     7784   9779   9470  -1206    -62   -743
ATOM    228  O   ALA A  27     -30.384  36.277 -13.976  1.00 71.01           O  
ANISOU  228  O   ALA A  27     7974   9664   9341  -1253   -167   -611
ATOM    229  CB  ALA A  27     -32.545  33.838 -13.214  1.00 73.10           C  
ANISOU  229  CB  ALA A  27     7782  10390   9603  -1496    -21   -858
ATOM    230  H   ALA A  27     -31.762  33.701 -10.847  1.00  0.00           H  
ATOM    231  HA  ALA A  27     -30.412  33.892 -13.345  1.00  0.00           H  
ATOM    232  HB1 ALA A  27     -32.754  34.103 -14.251  1.00  0.00           H  
ATOM    233  HB2 ALA A  27     -32.553  32.752 -13.151  1.00  0.00           H  
ATOM    234  HB3 ALA A  27     -33.364  34.214 -12.600  1.00  0.00           H  
ATOM    235  N   VAL A  28     -31.741  36.722 -12.202  1.00 71.78           N  
ANISOU  235  N   VAL A  28     7660   9817   9795   -986    -51   -813
ATOM    236  CA  VAL A  28     -31.694  38.187 -12.267  1.00 72.22           C  
ANISOU  236  CA  VAL A  28     7732   9680  10028   -758   -188   -732
ATOM    237  C   VAL A  28     -30.275  38.740 -12.032  1.00 70.69           C  
ANISOU  237  C   VAL A  28     7839   9291   9729   -785   -103   -701
ATOM    238  O   VAL A  28     -29.868  39.650 -12.751  1.00 71.10           O  
ANISOU  238  O   VAL A  28     8055   9202   9760   -762   -262   -553
ATOM    239  CB  VAL A  28     -32.690  38.845 -11.264  1.00 75.07           C  
ANISOU  239  CB  VAL A  28     7830  10018  10675   -514   -115   -871
ATOM    240  CG1 VAL A  28     -32.526  40.371 -11.078  1.00 75.66           C  
ANISOU  240  CG1 VAL A  28     7966   9843  10938   -267   -252   -791
ATOM    241  CG2 VAL A  28     -34.146  38.565 -11.677  1.00 75.50           C  
ANISOU  241  CG2 VAL A  28     7526  10307  10855   -494   -192   -910
ATOM    242  H   VAL A  28     -32.302  36.330 -11.457  1.00  0.00           H  
ATOM    243  HA  VAL A  28     -31.997  38.475 -13.276  1.00  0.00           H  
ATOM    244  HB  VAL A  28     -32.536  38.381 -10.288  1.00  0.00           H  
ATOM    245 HG11 VAL A  28     -33.303  40.769 -10.424  1.00  0.00           H  
ATOM    246 HG12 VAL A  28     -31.573  40.633 -10.624  1.00  0.00           H  
ATOM    247 HG13 VAL A  28     -32.598  40.894 -12.032  1.00  0.00           H  
ATOM    248 HG21 VAL A  28     -34.846  38.902 -10.911  1.00  0.00           H  
ATOM    249 HG22 VAL A  28     -34.396  39.081 -12.605  1.00  0.00           H  
ATOM    250 HG23 VAL A  28     -34.334  37.506 -11.843  1.00  0.00           H  
ATOM    251  N   SER A  29     -29.538  38.158 -11.071  1.00 68.84           N  
ANISOU  251  N   SER A  29     7678   9058   9418   -855    138   -832
ATOM    252  CA  SER A  29     -28.155  38.518 -10.772  1.00 67.23           C  
ANISOU  252  CA  SER A  29     7706   8711   9126   -892    226   -820
ATOM    253  C   SER A  29     -27.179  38.162 -11.911  1.00 66.33           C  
ANISOU  253  C   SER A  29     7788   8603   8810  -1060    160   -687
ATOM    254  O   SER A  29     -26.314  38.980 -12.226  1.00 66.62           O  
ANISOU  254  O   SER A  29     7989   8506   8816  -1068    107   -600
ATOM    255  CB  SER A  29     -27.737  37.865  -9.446  1.00 71.31           C  
ANISOU  255  CB  SER A  29     8236   9264   9596   -944    460   -972
ATOM    256  OG  SER A  29     -26.437  38.282  -9.095  1.00 71.70           O  
ANISOU  256  OG  SER A  29     8482   9218   9544  -1007    516   -942
ATOM    257  H   SER A  29     -29.943  37.424 -10.505  1.00  0.00           H  
ATOM    258  HA  SER A  29     -28.123  39.601 -10.633  1.00  0.00           H  
ATOM    259  HB3 SER A  29     -27.760  36.779  -9.535  1.00  0.00           H  
ATOM    260  HB2 SER A  29     -28.416  38.145  -8.641  1.00  0.00           H  
ATOM    261  HG  SER A  29     -26.112  37.743  -8.366  1.00  0.00           H  
ATOM    262  N   LYS A  30     -27.343  36.971 -12.517  1.00 67.73           N  
ANISOU  262  N   LYS A  30     7959   8930   8843  -1211    178   -683
ATOM    263  CA  LYS A  30     -26.523  36.516 -13.642  1.00 67.26           C  
ANISOU  263  CA  LYS A  30     8088   8885   8582  -1380    163   -593
ATOM    264  C   LYS A  30     -26.704  37.336 -14.915  1.00 69.14           C  
ANISOU  264  C   LYS A  30     8406   9076   8790  -1404    -65   -428
ATOM    265  O   LYS A  30     -25.699  37.700 -15.518  1.00 69.15           O  
ANISOU  265  O   LYS A  30     8594   8993   8687  -1484    -75   -346
ATOM    266  CB  LYS A  30     -26.730  35.014 -13.932  1.00 69.69           C  
ANISOU  266  CB  LYS A  30     8400   9334   8744  -1535    248   -648
ATOM    267  CG  LYS A  30     -25.677  34.133 -13.258  1.00 69.05           C  
ANISOU  267  CG  LYS A  30     8414   9241   8580  -1585    465   -736
ATOM    268  CD  LYS A  30     -24.263  34.306 -13.838  1.00 69.19           C  
ANISOU  268  CD  LYS A  30     8593   9195   8500  -1639    510   -679
ATOM    269  CE  LYS A  30     -23.246  33.475 -13.063  1.00 69.07           C  
ANISOU  269  CE  LYS A  30     8614   9164   8466  -1625    699   -760
ATOM    270  NZ  LYS A  30     -21.867  33.767 -13.488  1.00 69.36           N1+
ANISOU  270  NZ  LYS A  30     8744   9166   8445  -1664    757   -718
ATOM    271  H   LYS A  30     -28.064  36.337 -12.199  1.00  0.00           H  
ATOM    272  HA  LYS A  30     -25.497  36.688 -13.318  1.00  0.00           H  
ATOM    273  HB3 LYS A  30     -26.663  34.812 -15.003  1.00  0.00           H  
ATOM    274  HB2 LYS A  30     -27.738  34.707 -13.652  1.00  0.00           H  
ATOM    275  HG3 LYS A  30     -25.977  33.089 -13.352  1.00  0.00           H  
ATOM    276  HG2 LYS A  30     -25.663  34.367 -12.194  1.00  0.00           H  
ATOM    277  HD3 LYS A  30     -23.947  35.347 -13.828  1.00  0.00           H  
ATOM    278  HD2 LYS A  30     -24.263  34.001 -14.885  1.00  0.00           H  
ATOM    279  HE3 LYS A  30     -23.459  32.415 -13.207  1.00  0.00           H  
ATOM    280  HE2 LYS A  30     -23.322  33.677 -11.993  1.00  0.00           H  
ATOM    281  HZ1 LYS A  30     -21.246  33.175 -12.950  1.00  0.00           H  
ATOM    282  HZ2 LYS A  30     -21.758  33.570 -14.472  1.00  0.00           H  
ATOM    283  HZ3 LYS A  30     -21.651  34.737 -13.307  1.00  0.00           H  
ATOM    284  N   THR A  31     -27.965  37.616 -15.279  1.00 73.50           N  
ANISOU  284  N   THR A  31     8808   9688   9432  -1343   -258   -374
ATOM    285  CA  THR A  31     -28.323  38.469 -16.413  1.00 75.89           C  
ANISOU  285  CA  THR A  31     9179   9944   9711  -1354   -535   -188
ATOM    286  C   THR A  31     -27.927  39.947 -16.189  1.00 76.65           C  
ANISOU  286  C   THR A  31     9384   9812   9927  -1207   -616   -105
ATOM    287  O   THR A  31     -27.594  40.610 -17.167  1.00 77.95           O  
ANISOU  287  O   THR A  31     9761   9885   9971  -1304   -758     54
ATOM    288  CB  THR A  31     -29.842  38.402 -16.728  1.00 91.12           C  
ANISOU  288  CB  THR A  31    10866  12002  11754  -1287   -736   -154
ATOM    289  OG1 THR A  31     -30.629  38.812 -15.626  1.00 91.07           O  
ANISOU  289  OG1 THR A  31    10607  11988  12008  -1063   -653   -284
ATOM    290  CG2 THR A  31     -30.320  37.012 -17.179  1.00 91.18           C  
ANISOU  290  CG2 THR A  31    10831  12225  11588  -1507   -698   -204
ATOM    291  H   THR A  31     -28.734  37.259 -14.728  1.00  0.00           H  
ATOM    292  HA  THR A  31     -27.781  38.114 -17.289  1.00  0.00           H  
ATOM    293  HB  THR A  31     -30.066  39.100 -17.537  1.00  0.00           H  
ATOM    294  HG1 THR A  31     -30.632  38.104 -14.975  1.00  0.00           H  
ATOM    295 HG21 THR A  31     -31.408  36.966 -17.231  1.00  0.00           H  
ATOM    296 HG22 THR A  31     -29.946  36.786 -18.177  1.00  0.00           H  
ATOM    297 HG23 THR A  31     -29.982  36.220 -16.514  1.00  0.00           H  
ATOM    298  N   ALA A  32     -27.904  40.430 -14.933  1.00 78.14           N  
ANISOU  298  N   ALA A  32     9468   9898  10324  -1008   -506   -219
ATOM    299  CA  ALA A  32     -27.436  41.776 -14.591  1.00 78.82           C  
ANISOU  299  CA  ALA A  32     9687   9738  10522   -880   -554   -170
ATOM    300  C   ALA A  32     -25.913  41.945 -14.750  1.00 77.77           C  
ANISOU  300  C   ALA A  32     9822   9528  10198  -1069   -453   -130
ATOM    301  O   ALA A  32     -25.482  42.957 -15.302  1.00 78.90           O  
ANISOU  301  O   ALA A  32    10175   9523  10282  -1125   -595     21
ATOM    302  CB  ALA A  32     -27.882  42.135 -13.165  1.00 78.83           C  
ANISOU  302  CB  ALA A  32     9540   9667  10745   -675   -405   -343
ATOM    303  H   ALA A  32     -28.213  39.851 -14.165  1.00  0.00           H  
ATOM    304  HA  ALA A  32     -27.917  42.482 -15.270  1.00  0.00           H  
ATOM    305  HB1 ALA A  32     -27.515  43.119 -12.871  1.00  0.00           H  
ATOM    306  HB2 ALA A  32     -28.969  42.163 -13.093  1.00  0.00           H  
ATOM    307  HB3 ALA A  32     -27.518  41.415 -12.433  1.00  0.00           H  
ATOM    308  N   ALA A  33     -25.139  40.949 -14.286  1.00 81.19           N  
ANISOU  308  N   ALA A  33    10246  10071  10533  -1177   -218   -257
ATOM    309  CA  ALA A  33     -23.673  40.925 -14.341  1.00 80.40           C  
ANISOU  309  CA  ALA A  33    10324   9946  10280  -1346    -99   -244
ATOM    310  C   ALA A  33     -23.096  40.410 -15.679  1.00 80.50           C  
ANISOU  310  C   ALA A  33    10462  10065  10059  -1570   -106   -156
ATOM    311  O   ALA A  33     -21.883  40.501 -15.873  1.00 79.68           O  
ANISOU  311  O   ALA A  33    10476   9965   9831  -1719      9   -151
ATOM    312  CB  ALA A  33     -23.162  40.076 -13.166  1.00 78.48           C  
ANISOU  312  CB  ALA A  33     9992   9782  10047  -1343    127   -403
ATOM    313  H   ALA A  33     -25.576  40.157 -13.833  1.00  0.00           H  
ATOM    314  HA  ALA A  33     -23.303  41.941 -14.199  1.00  0.00           H  
ATOM    315  HB1 ALA A  33     -22.072  40.061 -13.126  1.00  0.00           H  
ATOM    316  HB2 ALA A  33     -23.514  40.473 -12.213  1.00  0.00           H  
ATOM    317  HB3 ALA A  33     -23.507  39.044 -13.240  1.00  0.00           H  
ATOM    318  N   ALA A  34     -23.962  39.888 -16.567  1.00 86.52           N  
ANISOU  318  N   ALA A  34    11197  10920  10755  -1613   -235    -92
ATOM    319  CA  ALA A  34     -23.639  39.302 -17.870  1.00 87.11           C  
ANISOU  319  CA  ALA A  34    11410  11105  10584  -1847   -224    -36
ATOM    320  C   ALA A  34     -22.795  40.160 -18.836  1.00 87.86           C  
ANISOU  320  C   ALA A  34    11758  11109  10515  -2026   -289    106
ATOM    321  O   ALA A  34     -21.798  39.625 -19.322  1.00 88.08           O  
ANISOU  321  O   ALA A  34    11882  11218  10367  -2215   -111     64
ATOM    322  CB  ALA A  34     -24.935  38.870 -18.567  1.00 88.77           C  
ANISOU  322  CB  ALA A  34    11557  11420  10751  -1875   -393     16
ATOM    323  H   ALA A  34     -24.938  39.850 -16.310  1.00  0.00           H  
ATOM    324  HA  ALA A  34     -23.067  38.397 -17.657  1.00  0.00           H  
ATOM    325  HB1 ALA A  34     -24.736  38.366 -19.513  1.00  0.00           H  
ATOM    326  HB2 ALA A  34     -25.510  38.193 -17.947  1.00  0.00           H  
ATOM    327  HB3 ALA A  34     -25.585  39.714 -18.772  1.00  0.00           H  
ATOM    328  N   PRO A  35     -23.165  41.438 -19.118  1.00 86.29           N  
ANISOU  328  N   PRO A  35    11680  10742  10364  -1983   -526    268
ATOM    329  CA  PRO A  35     -22.420  42.256 -20.094  1.00 87.98           C  
ANISOU  329  CA  PRO A  35    12180  10872  10376  -2212   -579    411
ATOM    330  C   PRO A  35     -20.992  42.624 -19.661  1.00 86.84           C  
ANISOU  330  C   PRO A  35    12101  10691  10205  -2308   -358    338
ATOM    331  O   PRO A  35     -20.121  42.732 -20.523  1.00 87.38           O  
ANISOU  331  O   PRO A  35    12344  10800  10055  -2568   -272    380
ATOM    332  CB  PRO A  35     -23.304  43.502 -20.290  1.00 91.18           C  
ANISOU  332  CB  PRO A  35    12693  11065  10887  -2090   -898    600
ATOM    333  CG  PRO A  35     -24.075  43.630 -18.994  1.00 90.52           C  
ANISOU  333  CG  PRO A  35    12361  10921  11112  -1766   -920    504
ATOM    334  CD  PRO A  35     -24.338  42.176 -18.634  1.00 88.43           C  
ANISOU  334  CD  PRO A  35    11847  10884  10867  -1732   -755    334
ATOM    335  HA  PRO A  35     -22.342  41.714 -21.035  1.00  0.00           H  
ATOM    336  HB3 PRO A  35     -24.025  43.327 -21.087  1.00  0.00           H  
ATOM    337  HB2 PRO A  35     -22.748  44.407 -20.541  1.00  0.00           H  
ATOM    338  HG3 PRO A  35     -24.986  44.222 -19.087  1.00  0.00           H  
ATOM    339  HG2 PRO A  35     -23.447  44.096 -18.236  1.00  0.00           H  
ATOM    340  HD2 PRO A  35     -24.525  42.093 -17.569  1.00  0.00           H  
ATOM    341  HD3 PRO A  35     -25.220  41.829 -19.167  1.00  0.00           H  
ATOM    342  N   ILE A  36     -20.773  42.776 -18.344  1.00 85.30           N  
ANISOU  342  N   ILE A  36    11756  10442  10211  -2128   -258    220
ATOM    343  CA  ILE A  36     -19.470  43.088 -17.764  1.00 84.84           C  
ANISOU  343  CA  ILE A  36    11732  10370  10134  -2230    -77    155
ATOM    344  C   ILE A  36     -18.526  41.869 -17.837  1.00 84.23           C  
ANISOU  344  C   ILE A  36    11549  10516   9937  -2356    170     36
ATOM    345  O   ILE A  36     -17.358  42.051 -18.177  1.00 84.61           O  
ANISOU  345  O   ILE A  36    11680  10621   9847  -2568    295     42
ATOM    346  CB  ILE A  36     -19.572  43.570 -16.283  1.00 88.85           C  
ANISOU  346  CB  ILE A  36    12136  10759  10863  -2030    -52     60
ATOM    347  CG1 ILE A  36     -20.615  44.703 -16.108  1.00 89.71           C  
ANISOU  347  CG1 ILE A  36    12351  10615  11122  -1864   -275    155
ATOM    348  CG2 ILE A  36     -18.211  44.067 -15.748  1.00 89.17           C  
ANISOU  348  CG2 ILE A  36    12223  10800  10858  -2182     95     13
ATOM    349  CD1 ILE A  36     -22.016  44.217 -15.704  1.00 89.08           C  
ANISOU  349  CD1 ILE A  36    12068  10545  11235  -1590   -362    104
ATOM    350  H   ILE A  36     -21.537  42.663 -17.693  1.00  0.00           H  
ATOM    351  HA  ILE A  36     -19.025  43.893 -18.353  1.00  0.00           H  
ATOM    352  HB  ILE A  36     -19.877  42.729 -15.657  1.00  0.00           H  
ATOM    353 HG13 ILE A  36     -20.672  45.313 -17.011  1.00  0.00           H  
ATOM    354 HG12 ILE A  36     -20.288  45.388 -15.325  1.00  0.00           H  
ATOM    355 HG21 ILE A  36     -18.289  44.373 -14.704  1.00  0.00           H  
ATOM    356 HG22 ILE A  36     -17.437  43.304 -15.792  1.00  0.00           H  
ATOM    357 HG23 ILE A  36     -17.855  44.925 -16.318  1.00  0.00           H  
ATOM    358 HD11 ILE A  36     -22.773  44.961 -15.952  1.00  0.00           H  
ATOM    359 HD12 ILE A  36     -22.293  43.289 -16.201  1.00  0.00           H  
ATOM    360 HD13 ILE A  36     -22.069  44.042 -14.629  1.00  0.00           H  
ATOM    361  N   GLU A  37     -19.053  40.656 -17.576  1.00 79.20           N  
ANISOU  361  N   GLU A  37    10737  10001   9354  -2234    244    -71
ATOM    362  CA  GLU A  37     -18.313  39.394 -17.687  1.00 78.98           C  
ANISOU  362  CA  GLU A  37    10626  10145   9238  -2312    473   -185
ATOM    363  C   GLU A  37     -17.974  39.064 -19.148  1.00 79.02           C  
ANISOU  363  C   GLU A  37    10796  10224   9002  -2553    514   -133
ATOM    364  O   GLU A  37     -16.865  38.601 -19.407  1.00 79.13           O  
ANISOU  364  O   GLU A  37    10800  10347   8921  -2680    728   -209
ATOM    365  CB  GLU A  37     -19.089  38.269 -16.956  1.00  0.00           C  
ATOM    366  CG  GLU A  37     -18.307  36.962 -16.659  1.00  0.00           C  
ATOM    367  CD  GLU A  37     -18.026  36.055 -17.862  1.00  0.00           C  
ATOM    368  OE1 GLU A  37     -18.998  35.748 -18.588  1.00  0.00           O  
ATOM    369  OE2 GLU A  37     -16.845  35.681 -18.030  1.00  0.00           O1-
ATOM    370  H   GLU A  37     -20.025  40.581 -17.308  1.00  0.00           H  
ATOM    371  HA  GLU A  37     -17.362  39.529 -17.172  1.00  0.00           H  
ATOM    372  HB2 GLU A  37     -19.446  38.659 -16.002  1.00  0.00           H  
ATOM    373  HB3 GLU A  37     -19.996  38.031 -17.515  1.00  0.00           H  
ATOM    374  HG2 GLU A  37     -17.367  37.205 -16.161  1.00  0.00           H  
ATOM    375  HG3 GLU A  37     -18.877  36.368 -15.945  1.00  0.00           H  
ATOM    376  N   ARG A  38     -18.902  39.362 -20.073  1.00 84.17           N  
ANISOU  376  N   ARG A  38    11604  10823   9555  -2623    305     -3
ATOM    377  CA  ARG A  38     -18.717  39.188 -21.510  1.00 84.87           C  
ANISOU  377  CA  ARG A  38    11901  10976   9370  -2893    314     61
ATOM    378  C   ARG A  38     -17.559  40.032 -22.065  1.00 85.65           C  
ANISOU  378  C   ARG A  38    12161  11058   9326  -3126    405    113
ATOM    379  O   ARG A  38     -16.714  39.483 -22.767  1.00 86.21           O  
ANISOU  379  O   ARG A  38    12291  11254   9212  -3334    622     41
ATOM    380  CB  ARG A  38     -20.050  39.453 -22.241  1.00 90.59           C  
ANISOU  380  CB  ARG A  38    12759  11639  10020  -2921      7    225
ATOM    381  CG  ARG A  38     -19.980  39.334 -23.774  1.00 92.48           C  
ANISOU  381  CG  ARG A  38    13259  11947   9934  -3241    -14    306
ATOM    382  CD  ARG A  38     -19.745  37.900 -24.261  1.00 92.34           C  
ANISOU  382  CD  ARG A  38    13220  12097   9770  -3354    230    137
ATOM    383  NE  ARG A  38     -19.449  37.862 -25.697  1.00 94.37           N  
ANISOU  383  NE  ARG A  38    13762  12414   9682  -3695    226    201
ATOM    384  CZ  ARG A  38     -19.359  36.743 -26.432  1.00 95.05           C  
ANISOU  384  CZ  ARG A  38    13921  12620   9574  -3859    410     71
ATOM    385  NH1 ARG A  38     -19.586  35.536 -25.893  1.00 93.62           N  
ANISOU  385  NH1 ARG A  38    13554  12494   9522  -3699    606   -119
ATOM    386  NH2 ARG A  38     -19.028  36.838 -27.726  1.00 97.04           N1+
ANISOU  386  NH2 ARG A  38    14465  12921   9485  -4199    402    130
ATOM    387  H   ARG A  38     -19.798  39.727 -19.778  1.00  0.00           H  
ATOM    388  HA  ARG A  38     -18.453  38.138 -21.650  1.00  0.00           H  
ATOM    389  HB3 ARG A  38     -20.404  40.454 -21.993  1.00  0.00           H  
ATOM    390  HB2 ARG A  38     -20.807  38.765 -21.861  1.00  0.00           H  
ATOM    391  HG3 ARG A  38     -19.301  40.048 -24.235  1.00  0.00           H  
ATOM    392  HG2 ARG A  38     -20.966  39.612 -24.135  1.00  0.00           H  
ATOM    393  HD3 ARG A  38     -20.697  37.374 -24.174  1.00  0.00           H  
ATOM    394  HD2 ARG A  38     -19.024  37.343 -23.664  1.00  0.00           H  
ATOM    395  HE  ARG A  38     -19.241  38.751 -26.129  1.00  0.00           H  
ATOM    396 HH12 ARG A  38     -19.495  34.695 -26.443  1.00  0.00           H  
ATOM    397 HH11 ARG A  38     -19.853  35.463 -24.921  1.00  0.00           H  
ATOM    398 HH22 ARG A  38     -18.924  36.008 -28.290  1.00  0.00           H  
ATOM    399 HH21 ARG A  38     -18.826  37.740 -28.135  1.00  0.00           H  
ATOM    400  N   ILE A  39     -17.517  41.327 -21.711  1.00 84.69           N  
ANISOU  400  N   ILE A  39    12120  10776   9281  -3105    253    229
ATOM    401  CA  ILE A  39     -16.440  42.241 -22.097  1.00 85.14           C  
ANISOU  401  CA  ILE A  39    12350  10805   9195  -3362    327    289
ATOM    402  C   ILE A  39     -15.094  41.888 -21.426  1.00 84.84           C  
ANISOU  402  C   ILE A  39    12104  10909   9224  -3379    623    121
ATOM    403  O   ILE A  39     -14.060  42.011 -22.081  1.00 85.08           O  
ANISOU  403  O   ILE A  39    12190  11043   9095  -3635    807     94
ATOM    404  CB  ILE A  39     -16.819  43.724 -21.810  1.00 87.72           C  
ANISOU  404  CB  ILE A  39    12838  10886   9606  -3325     90    447
ATOM    405  CG1 ILE A  39     -17.988  44.170 -22.719  1.00 88.36           C  
ANISOU  405  CG1 ILE A  39    13115  10821   9638  -3289   -235    640
ATOM    406  CG2 ILE A  39     -15.657  44.730 -21.949  1.00 88.60           C  
ANISOU  406  CG2 ILE A  39    13134  10971   9558  -3632    189    497
ATOM    407  CD1 ILE A  39     -18.645  45.489 -22.286  1.00 89.29           C  
ANISOU  407  CD1 ILE A  39    13437  10650   9839  -3237   -481    811
ATOM    408  H   ILE A  39     -18.249  41.713 -21.130  1.00  0.00           H  
ATOM    409  HA  ILE A  39     -16.297  42.141 -23.175  1.00  0.00           H  
ATOM    410  HB  ILE A  39     -17.172  43.773 -20.778  1.00  0.00           H  
ATOM    411 HG13 ILE A  39     -18.761  43.402 -22.753  1.00  0.00           H  
ATOM    412 HG12 ILE A  39     -17.632  44.265 -23.746  1.00  0.00           H  
ATOM    413 HG21 ILE A  39     -16.018  45.750 -21.823  1.00  0.00           H  
ATOM    414 HG22 ILE A  39     -14.884  44.581 -21.195  1.00  0.00           H  
ATOM    415 HG23 ILE A  39     -15.190  44.669 -22.931  1.00  0.00           H  
ATOM    416 HD11 ILE A  39     -19.729  45.435 -22.391  1.00  0.00           H  
ATOM    417 HD12 ILE A  39     -18.436  45.728 -21.243  1.00  0.00           H  
ATOM    418 HD13 ILE A  39     -18.291  46.319 -22.896  1.00  0.00           H  
ATOM    419  N   LYS A  40     -15.132  41.405 -20.168  1.00 84.22           N  
ANISOU  419  N   LYS A  40    11775  10848   9377  -3113    664      9
ATOM    420  CA  LYS A  40     -13.957  40.916 -19.439  1.00 83.96           C  
ANISOU  420  CA  LYS A  40    11520  10952   9430  -3095    894   -131
ATOM    421  C   LYS A  40     -13.325  39.687 -20.123  1.00 84.36           C  
ANISOU  421  C   LYS A  40    11488  11195   9369  -3183   1148   -250
ATOM    422  O   LYS A  40     -12.106  39.656 -20.268  1.00 85.29           O  
ANISOU  422  O   LYS A  40    11508  11446   9452  -3317   1355   -322
ATOM    423  CB  LYS A  40     -14.328  40.617 -17.969  1.00 86.70           C  
ANISOU  423  CB  LYS A  40    11652  11274  10015  -2802    863   -212
ATOM    424  CG  LYS A  40     -13.110  40.377 -17.052  1.00 86.22           C  
ANISOU  424  CG  LYS A  40    11384  11322  10055  -2788   1012   -307
ATOM    425  CD  LYS A  40     -13.464  39.730 -15.701  1.00 84.31           C  
ANISOU  425  CD  LYS A  40    10957  11079   9999  -2523    995   -389
ATOM    426  CE  LYS A  40     -13.754  38.221 -15.789  1.00 83.06           C  
ANISOU  426  CE  LYS A  40    10670  11038   9851  -2410   1140   -488
ATOM    427  NZ  LYS A  40     -12.553  37.457 -16.171  1.00 83.74           N1+
ANISOU  427  NZ  LYS A  40    10604  11290   9923  -2484   1350   -563
ATOM    428  H   LYS A  40     -16.018  41.338 -19.685  1.00  0.00           H  
ATOM    429  HA  LYS A  40     -13.217  41.718 -19.444  1.00  0.00           H  
ATOM    430  HB3 LYS A  40     -15.005  39.765 -17.934  1.00  0.00           H  
ATOM    431  HB2 LYS A  40     -14.886  41.457 -17.555  1.00  0.00           H  
ATOM    432  HG3 LYS A  40     -12.634  41.340 -16.861  1.00  0.00           H  
ATOM    433  HG2 LYS A  40     -12.349  39.779 -17.551  1.00  0.00           H  
ATOM    434  HD3 LYS A  40     -14.331  40.235 -15.278  1.00  0.00           H  
ATOM    435  HD2 LYS A  40     -12.652  39.904 -14.994  1.00  0.00           H  
ATOM    436  HE3 LYS A  40     -14.555  38.014 -16.500  1.00  0.00           H  
ATOM    437  HE2 LYS A  40     -14.095  37.858 -14.819  1.00  0.00           H  
ATOM    438  HZ1 LYS A  40     -12.775  36.472 -16.205  1.00  0.00           H  
ATOM    439  HZ2 LYS A  40     -12.231  37.750 -17.084  1.00  0.00           H  
ATOM    440  HZ3 LYS A  40     -11.819  37.613 -15.496  1.00  0.00           H  
ATOM    441  N   LEU A  41     -14.166  38.734 -20.563  1.00 85.42           N  
ANISOU  441  N   LEU A  41    11659  11344   9452  -3115   1139   -281
ATOM    442  CA  LEU A  41     -13.785  37.536 -21.314  1.00 86.52           C  
ANISOU  442  CA  LEU A  41    11765  11625   9482  -3187   1393   -414
ATOM    443  C   LEU A  41     -13.178  37.875 -22.689  1.00 88.88           C  
ANISOU  443  C   LEU A  41    12276  11984   9508  -3529   1495   -379
ATOM    444  O   LEU A  41     -12.133  37.320 -23.027  1.00 90.38           O  
ANISOU  444  O   LEU A  41    12391  12316   9635  -3650   1778   -501
ATOM    445  CB  LEU A  41     -15.025  36.618 -21.446  1.00  0.00           C  
ATOM    446  CG  LEU A  41     -14.794  35.239 -22.111  1.00  0.00           C  
ATOM    447  CD1 LEU A  41     -14.082  34.262 -21.154  1.00  0.00           C  
ATOM    448  CD2 LEU A  41     -16.109  34.651 -22.665  1.00  0.00           C  
ATOM    449  H   LEU A  41     -15.157  38.836 -20.382  1.00  0.00           H  
ATOM    450  HA  LEU A  41     -13.024  37.017 -20.730  1.00  0.00           H  
ATOM    451  HB2 LEU A  41     -15.473  36.460 -20.464  1.00  0.00           H  
ATOM    452  HB3 LEU A  41     -15.779  37.158 -22.019  1.00  0.00           H  
ATOM    453  HG  LEU A  41     -14.142  35.371 -22.974  1.00  0.00           H  
ATOM    454 HD11 LEU A  41     -13.325  33.687 -21.684  1.00  0.00           H  
ATOM    455 HD12 LEU A  41     -13.583  34.778 -20.334  1.00  0.00           H  
ATOM    456 HD13 LEU A  41     -14.772  33.550 -20.701  1.00  0.00           H  
ATOM    457 HD21 LEU A  41     -16.264  33.614 -22.366  1.00  0.00           H  
ATOM    458 HD22 LEU A  41     -16.983  35.212 -22.329  1.00  0.00           H  
ATOM    459 HD23 LEU A  41     -16.112  34.671 -23.755  1.00  0.00           H  
ATOM    460  N   LEU A  42     -13.834  38.782 -23.438  1.00 97.95           N  
ANISOU  460  N   LEU A  42    13691  13027  10500  -3684   1263   -210
ATOM    461  CA  LEU A  42     -13.414  39.241 -24.767  1.00100.65           C  
ANISOU  461  CA  LEU A  42    14301  13405  10534  -4053   1320   -143
ATOM    462  C   LEU A  42     -12.027  39.899 -24.765  1.00102.35           C  
ANISOU  462  C   LEU A  42    14468  13707  10712  -4253   1526   -179
ATOM    463  O   LEU A  42     -11.219  39.571 -25.630  1.00104.64           O  
ANISOU  463  O   LEU A  42    14808  14144  10806  -4508   1796   -274
ATOM    464  CB  LEU A  42     -14.455  40.222 -25.351  1.00101.12           C  
ANISOU  464  CB  LEU A  42    14658  13298  10466  -4158    965     95
ATOM    465  CG  LEU A  42     -15.748  39.564 -25.875  1.00101.30           C  
ANISOU  465  CG  LEU A  42    14795  13297  10398  -4121    770    153
ATOM    466  CD1 LEU A  42     -16.837  40.631 -26.086  1.00103.15           C  
ANISOU  466  CD1 LEU A  42    15290  13371  10532  -4209    402    408
ATOM    467  CD2 LEU A  42     -15.499  38.732 -27.151  1.00102.82           C  
ANISOU  467  CD2 LEU A  42    15113  13638  10317  -4365    997     38
ATOM    468  H   LEU A  42     -14.695  39.181 -23.086  1.00  0.00           H  
ATOM    469  HA  LEU A  42     -13.349  38.362 -25.410  1.00  0.00           H  
ATOM    470  HB3 LEU A  42     -14.017  40.798 -26.169  1.00  0.00           H  
ATOM    471  HB2 LEU A  42     -14.706  40.958 -24.585  1.00  0.00           H  
ATOM    472  HG  LEU A  42     -16.117  38.870 -25.122  1.00  0.00           H  
ATOM    473 HD11 LEU A  42     -17.551  40.351 -26.859  1.00  0.00           H  
ATOM    474 HD12 LEU A  42     -17.399  40.790 -25.168  1.00  0.00           H  
ATOM    475 HD13 LEU A  42     -16.405  41.593 -26.360  1.00  0.00           H  
ATOM    476 HD21 LEU A  42     -16.085  39.083 -28.000  1.00  0.00           H  
ATOM    477 HD22 LEU A  42     -14.454  38.760 -27.461  1.00  0.00           H  
ATOM    478 HD23 LEU A  42     -15.758  37.685 -26.987  1.00  0.00           H  
ATOM    479  N   VAL A  43     -11.777  40.792 -23.792  1.00108.41           N  
ANISOU  479  N   VAL A  43    15126  14400  11664  -4155   1424   -125
ATOM    480  CA  VAL A  43     -10.504  41.496 -23.635  1.00110.02           C  
ANISOU  480  CA  VAL A  43    15262  14700  11840  -4370   1595   -154
ATOM    481  C   VAL A  43      -9.391  40.589 -23.067  1.00110.28           C  
ANISOU  481  C   VAL A  43    14921  14954  12025  -4259   1904   -365
ATOM    482  O   VAL A  43      -8.242  40.749 -23.477  1.00112.44           O  
ANISOU  482  O   VAL A  43    15114  15403  12204  -4491   2162   -450
ATOM    483  CB  VAL A  43     -10.667  42.768 -22.749  1.00110.26           C  
ANISOU  483  CB  VAL A  43    15329  14564  12002  -4330   1375    -31
ATOM    484  CG1 VAL A  43      -9.350  43.460 -22.335  1.00111.11           C  
ANISOU  484  CG1 VAL A  43    15371  14791  12056  -4608   1551    -63
ATOM    485  CG2 VAL A  43     -11.572  43.805 -23.442  1.00110.13           C  
ANISOU  485  CG2 VAL A  43    15678  14295  11869  -4398   1060    185
ATOM    486  H   VAL A  43     -12.498  41.012 -23.117  1.00  0.00           H  
ATOM    487  HA  VAL A  43     -10.182  41.820 -24.627  1.00  0.00           H  
ATOM    488  HB  VAL A  43     -11.173  42.471 -21.828  1.00  0.00           H  
ATOM    489 HG11 VAL A  43      -9.548  44.393 -21.806  1.00  0.00           H  
ATOM    490 HG12 VAL A  43      -8.753  42.845 -21.662  1.00  0.00           H  
ATOM    491 HG13 VAL A  43      -8.739  43.701 -23.205  1.00  0.00           H  
ATOM    492 HG21 VAL A  43     -11.747  44.671 -22.804  1.00  0.00           H  
ATOM    493 HG22 VAL A  43     -11.125  44.162 -24.371  1.00  0.00           H  
ATOM    494 HG23 VAL A  43     -12.546  43.390 -23.690  1.00  0.00           H  
ATOM    495  N   GLN A  44      -9.733  39.648 -22.168  1.00117.19           N  
ANISOU  495  N   GLN A  44    15563  15822  13144  -3906   1875   -444
ATOM    496  CA  GLN A  44      -8.784  38.702 -21.573  1.00116.98           C  
ANISOU  496  CA  GLN A  44    15184  15973  13289  -3750   2119   -618
ATOM    497  C   GLN A  44      -8.237  37.683 -22.591  1.00117.84           C  
ANISOU  497  C   GLN A  44    15266  16226  13282  -3826   2433   -776
ATOM    498  O   GLN A  44      -7.034  37.423 -22.583  1.00118.91           O  
ANISOU  498  O   GLN A  44    15160  16547  13473  -3867   2702   -907
ATOM    499  CB  GLN A  44      -9.437  38.008 -20.356  1.00121.17           C  
ANISOU  499  CB  GLN A  44    15537  16432  14072  -3372   1995   -647
ATOM    500  CG  GLN A  44      -8.520  37.024 -19.593  1.00121.05           C  
ANISOU  500  CG  GLN A  44    15175  16567  14251  -3172   2192   -793
ATOM    501  CD  GLN A  44      -9.225  36.287 -18.450  1.00121.79           C  
ANISOU  501  CD  GLN A  44    15170  16566  14538  -2834   2067   -808
ATOM    502  OE1 GLN A  44     -10.388  36.539 -18.140  1.00122.46           O  
ANISOU  502  OE1 GLN A  44    15419  16496  14614  -2756   1862   -731
ATOM    503  NE2 GLN A  44      -8.506  35.363 -17.812  1.00121.62           N  
ANISOU  503  NE2 GLN A  44    14874  16641  14695  -2634   2188   -905
ATOM    504  H   GLN A  44     -10.694  39.571 -21.861  1.00  0.00           H  
ATOM    505  HA  GLN A  44      -7.935  39.281 -21.202  1.00  0.00           H  
ATOM    506  HB3 GLN A  44     -10.339  37.488 -20.685  1.00  0.00           H  
ATOM    507  HB2 GLN A  44      -9.762  38.775 -19.653  1.00  0.00           H  
ATOM    508  HG3 GLN A  44      -7.664  37.563 -19.187  1.00  0.00           H  
ATOM    509  HG2 GLN A  44      -8.120  36.267 -20.264  1.00  0.00           H  
ATOM    510 HE22 GLN A  44      -8.913  34.838 -17.052  1.00  0.00           H  
ATOM    511 HE21 GLN A  44      -7.556  35.171 -18.094  1.00  0.00           H  
ATOM    512  N   ASN A  45      -9.128  37.126 -23.429  1.00112.28           N  
ANISOU  512  N   ASN A  45    14802  15440  12420  -3851   2404   -772
ATOM    513  CA  ASN A  45      -8.825  36.023 -24.349  1.00114.11           C  
ANISOU  513  CA  ASN A  45    15065  15774  12517  -3933   2711   -941
ATOM    514  C   ASN A  45      -8.800  36.486 -25.820  1.00116.98           C  
ANISOU  514  C   ASN A  45    15759  16169  12517  -4344   2793   -908
ATOM    515  O   ASN A  45      -9.053  35.666 -26.701  1.00118.68           O  
ANISOU  515  O   ASN A  45    16186  16361  12544  -4428   2857   -962
ATOM    516  CB  ASN A  45      -9.827  34.858 -24.116  1.00117.15           C  
ANISOU  516  CB  ASN A  45    15478  16062  12972  -3680   2674  -1009
ATOM    517  CG  ASN A  45      -9.748  34.203 -22.729  1.00114.27           C  
ANISOU  517  CG  ASN A  45    14808  15677  12933  -3301   2653  -1067
ATOM    518  OD1 ASN A  45      -8.796  34.397 -21.977  1.00113.91           O  
ANISOU  518  OD1 ASN A  45    14495  15722  13064  -3217   2708  -1085
ATOM    519  ND2 ASN A  45     -10.749  33.388 -22.394  1.00112.53           N  
ANISOU  519  ND2 ASN A  45    14636  15343  12777  -3096   2563  -1088
ATOM    520  H   ASN A  45     -10.099  37.404 -23.377  1.00  0.00           H  
ATOM    521  HA  ASN A  45      -7.823  35.639 -24.148  1.00  0.00           H  
ATOM    522  HB3 ASN A  45      -9.635  34.055 -24.829  1.00  0.00           H  
ATOM    523  HB2 ASN A  45     -10.847  35.198 -24.300  1.00  0.00           H  
ATOM    524 HD22 ASN A  45     -10.737  32.921 -21.499  1.00  0.00           H  
ATOM    525 HD21 ASN A  45     -11.516  33.228 -23.030  1.00  0.00           H  
ATOM    526  N   GLN A  46      -8.453  37.760 -26.083  1.00110.60           N  
ANISOU  526  N   GLN A  46    15023  15411  11589  -4629   2787   -815
ATOM    527  CA  GLN A  46      -8.310  38.305 -27.441  1.00111.83           C  
ANISOU  527  CA  GLN A  46    15525  15596  11369  -5067   2858   -762
ATOM    528  C   GLN A  46      -7.126  37.718 -28.236  1.00113.22           C  
ANISOU  528  C   GLN A  46    15605  15999  11414  -5288   3330   -989
ATOM    529  O   GLN A  46      -7.225  37.616 -29.456  1.00114.24           O  
ANISOU  529  O   GLN A  46    16027  16160  11219  -5588   3473  -1030
ATOM    530  CB  GLN A  46      -8.248  39.848 -27.403  1.00110.84           C  
ANISOU  530  CB  GLN A  46    15596  15381  11139  -5310   2621   -539
ATOM    531  CG  GLN A  46      -7.034  40.449 -26.668  1.00111.38           C  
ANISOU  531  CG  GLN A  46    15383  15543  11394  -5315   2702   -562
ATOM    532  CD  GLN A  46      -7.069  41.975 -26.708  1.00112.20           C  
ANISOU  532  CD  GLN A  46    15773  15529  11331  -5627   2499   -352
ATOM    533  OE1 GLN A  46      -6.728  42.577 -27.721  1.00115.18           O  
ANISOU  533  OE1 GLN A  46    16351  15989  11424  -6049   2655   -335
ATOM    534  NE2 GLN A  46      -7.478  42.612 -25.612  1.00109.77           N  
ANISOU  534  NE2 GLN A  46    15511  15009  11189  -5435   2158   -193
ATOM    535  H   GLN A  46      -8.257  38.392 -25.319  1.00  0.00           H  
ATOM    536  HA  GLN A  46      -9.219  38.041 -27.985  1.00  0.00           H  
ATOM    537  HB3 GLN A  46      -9.165  40.233 -26.959  1.00  0.00           H  
ATOM    538  HB2 GLN A  46      -8.249  40.218 -28.429  1.00  0.00           H  
ATOM    539  HG3 GLN A  46      -6.103  40.130 -27.137  1.00  0.00           H  
ATOM    540  HG2 GLN A  46      -6.991  40.100 -25.637  1.00  0.00           H  
ATOM    541 HE22 GLN A  46      -7.509  43.620 -25.588  1.00  0.00           H  
ATOM    542 HE21 GLN A  46      -7.740  42.082 -24.789  1.00  0.00           H  
ATOM    543  N   ASP A  47      -6.039  37.341 -27.540  1.00114.79           N  
ANISOU  543  N   ASP A  47    15391  16361  11861  -5140   3571  -1142
ATOM    544  CA  ASP A  47      -4.822  36.764 -28.126  1.00118.11           C  
ANISOU  544  CA  ASP A  47    15642  17015  12218  -5302   4043  -1381
ATOM    545  C   ASP A  47      -5.024  35.330 -28.632  1.00118.61           C  
ANISOU  545  C   ASP A  47    15734  17067  12267  -5140   4286  -1590
ATOM    546  O   ASP A  47      -4.539  35.007 -29.717  1.00121.88           O  
ANISOU  546  O   ASP A  47    16313  17579  12416  -5427   4608  -1739
ATOM    547  CB  ASP A  47      -3.614  36.834 -27.166  1.00123.82           C  
ANISOU  547  CB  ASP A  47    15861  17924  13260  -5139   4189  -1473
ATOM    548  CG  ASP A  47      -3.340  38.249 -26.656  1.00123.31           C  
ANISOU  548  CG  ASP A  47    15794  17867  13190  -5344   3964  -1284
ATOM    549  OD1 ASP A  47      -3.167  39.131 -27.522  1.00125.27           O  
ANISOU  549  OD1 ASP A  47    16273  18179  13146  -5797   4047  -1229
ATOM    550  OD2 ASP A  47      -3.252  38.422 -25.422  1.00120.86           O1-
ANISOU  550  OD2 ASP A  47    15287  17484  13149  -5069   3702  -1188
ATOM    551  H   ASP A  47      -6.028  37.471 -26.539  1.00  0.00           H  
ATOM    552  HA  ASP A  47      -4.575  37.368 -29.002  1.00  0.00           H  
ATOM    553  HB3 ASP A  47      -2.707  36.452 -27.635  1.00  0.00           H  
ATOM    554  HB2 ASP A  47      -3.801  36.190 -26.305  1.00  0.00           H  
ATOM    555  N   GLU A  48      -5.772  34.516 -27.866  1.00112.51           N  
ANISOU  555  N   GLU A  48    14851  16156  11743  -4720   4134  -1602
ATOM    556  CA  GLU A  48      -6.184  33.167 -28.260  1.00112.96           C  
ANISOU  556  CA  GLU A  48    14980  16150  11789  -4559   4330  -1789
ATOM    557  C   GLU A  48      -7.194  33.186 -29.424  1.00113.84           C  
ANISOU  557  C   GLU A  48    15588  16165  11500  -4876   4250  -1735
ATOM    558  O   GLU A  48      -7.148  32.288 -30.264  1.00115.81           O  
ANISOU  558  O   GLU A  48    15990  16414  11599  -4942   4521  -1929
ATOM    559  CB  GLU A  48      -6.720  32.411 -27.026  1.00  0.00           C  
ATOM    560  CG  GLU A  48      -7.101  30.941 -27.307  1.00  0.00           C  
ATOM    561  CD  GLU A  48      -7.649  30.227 -26.074  1.00  0.00           C  
ATOM    562  OE1 GLU A  48      -6.926  30.198 -25.055  1.00  0.00           O  
ATOM    563  OE2 GLU A  48      -8.787  29.716 -26.179  1.00  0.00           O1-
ATOM    564  H   GLU A  48      -6.138  34.857 -26.989  1.00  0.00           H  
ATOM    565  HA  GLU A  48      -5.293  32.640 -28.607  1.00  0.00           H  
ATOM    566  HB2 GLU A  48      -5.964  32.440 -26.240  1.00  0.00           H  
ATOM    567  HB3 GLU A  48      -7.587  32.940 -26.624  1.00  0.00           H  
ATOM    568  HG2 GLU A  48      -7.852  30.876 -28.094  1.00  0.00           H  
ATOM    569  HG3 GLU A  48      -6.229  30.392 -27.663  1.00  0.00           H  
ATOM    570  N   MET A  49      -8.050  34.223 -29.476  1.00111.24           N  
ANISOU  570  N   MET A  49    15518  15749  11000  -5071   3869  -1470
ATOM    571  CA  MET A  49      -8.954  34.490 -30.595  1.00112.39           C  
ANISOU  571  CA  MET A  49    16127  15816  10761  -5391   3704  -1358
ATOM    572  C   MET A  49      -8.200  34.865 -31.879  1.00116.47           C  
ANISOU  572  C   MET A  49    16881  16473  10899  -5882   3988  -1422
ATOM    573  O   MET A  49      -8.588  34.373 -32.933  1.00118.67           O  
ANISOU  573  O   MET A  49    17488  16752  10848  -6145   4095  -1491
ATOM    574  CB  MET A  49      -9.976  35.581 -30.223  1.00114.19           C  
ANISOU  574  CB  MET A  49    16507  15893  10986  -5379   3186  -1043
ATOM    575  CG  MET A  49     -11.029  35.122 -29.207  1.00110.50           C  
ANISOU  575  CG  MET A  49    15874  15292  10820  -4958   2913   -990
ATOM    576  SD  MET A  49     -12.043  36.459 -28.524  1.00107.89           S  
ANISOU  576  SD  MET A  49    15628  14796  10568  -4892   2368   -657
ATOM    577  CE  MET A  49     -13.159  36.747 -29.923  1.00109.41           C  
ANISOU  577  CE  MET A  49    16313  14933  10326  -5266   2124   -484
ATOM    578  H   MET A  49      -8.033  34.917 -28.741  1.00  0.00           H  
ATOM    579  HA  MET A  49      -9.506  33.571 -30.805  1.00  0.00           H  
ATOM    580  HB3 MET A  49     -10.497  35.906 -31.124  1.00  0.00           H  
ATOM    581  HB2 MET A  49      -9.469  36.468 -29.848  1.00  0.00           H  
ATOM    582  HG3 MET A  49     -10.559  34.596 -28.378  1.00  0.00           H  
ATOM    583  HG2 MET A  49     -11.698  34.403 -29.674  1.00  0.00           H  
ATOM    584  HE1 MET A  49     -13.852  37.555 -29.691  1.00  0.00           H  
ATOM    585  HE2 MET A  49     -12.603  37.020 -30.817  1.00  0.00           H  
ATOM    586  HE3 MET A  49     -13.737  35.848 -30.140  1.00  0.00           H  
ATOM    587  N   ILE A  50      -7.131  35.675 -31.784  1.00109.08           N  
ANISOU  587  N   ILE A  50    15787  15668   9991  -6036   4129  -1414
ATOM    588  CA  ILE A  50      -6.275  36.024 -32.924  1.00109.34           C  
ANISOU  588  CA  ILE A  50    16022  15860   9663  -6531   4449  -1498
ATOM    589  C   ILE A  50      -5.474  34.820 -33.468  1.00109.91           C  
ANISOU  589  C   ILE A  50    15954  16075   9732  -6504   4996  -1863
ATOM    590  O   ILE A  50      -5.335  34.705 -34.686  1.00111.51           O  
ANISOU  590  O   ILE A  50    16472  16348   9549  -6894   5258  -1980
ATOM    591  CB  ILE A  50      -5.356  37.252 -32.626  1.00110.23           C  
ANISOU  591  CB  ILE A  50    15981  16083   9819  -6719   4466  -1403
ATOM    592  CG1 ILE A  50      -6.205  38.546 -32.535  1.00110.60           C  
ANISOU  592  CG1 ILE A  50    16305  15934   9784  -6815   3944  -1046
ATOM    593  CG2 ILE A  50      -4.197  37.472 -33.626  1.00111.81           C  
ANISOU  593  CG2 ILE A  50    16304  16494   9684  -7219   4895  -1550
ATOM    594  CD1 ILE A  50      -5.488  39.740 -31.886  1.00109.89           C  
ANISOU  594  CD1 ILE A  50    16167  15898   9690  -7052   3915   -926
ATOM    595  H   ILE A  50      -6.871  36.067 -30.889  1.00  0.00           H  
ATOM    596  HA  ILE A  50      -6.941  36.311 -33.733  1.00  0.00           H  
ATOM    597  HB  ILE A  50      -4.909  37.087 -31.644  1.00  0.00           H  
ATOM    598 HG13 ILE A  50      -7.120  38.359 -31.975  1.00  0.00           H  
ATOM    599 HG12 ILE A  50      -6.532  38.835 -33.534  1.00  0.00           H  
ATOM    600 HG21 ILE A  50      -3.631  38.372 -33.387  1.00  0.00           H  
ATOM    601 HG22 ILE A  50      -3.480  36.651 -33.613  1.00  0.00           H  
ATOM    602 HG23 ILE A  50      -4.570  37.580 -34.645  1.00  0.00           H  
ATOM    603 HD11 ILE A  50      -6.202  40.386 -31.374  1.00  0.00           H  
ATOM    604 HD12 ILE A  50      -4.752  39.417 -31.148  1.00  0.00           H  
ATOM    605 HD13 ILE A  50      -4.975  40.345 -32.633  1.00  0.00           H  
ATOM    606  N   LYS A  51      -5.035  33.913 -32.576  1.00118.18           N  
ANISOU  606  N   LYS A  51    16558  17145  11200  -6039   5153  -2038
ATOM    607  CA  LYS A  51      -4.431  32.626 -32.934  1.00119.90           C  
ANISOU  607  CA  LYS A  51    16608  17450  11498  -5909   5653  -2387
ATOM    608  C   LYS A  51      -5.409  31.686 -33.669  1.00119.84           C  
ANISOU  608  C   LYS A  51    17005  17289  11240  -5970   5674  -2475
ATOM    609  O   LYS A  51      -5.025  31.091 -34.675  1.00121.81           O  
ANISOU  609  O   LYS A  51    17441  17614  11230  -6225   6089  -2717
ATOM    610  CB  LYS A  51      -3.811  31.973 -31.675  1.00128.22           C  
ANISOU  610  CB  LYS A  51    17118  18513  13086  -5350   5713  -2494
ATOM    611  CG  LYS A  51      -3.284  30.542 -31.906  1.00128.72           C  
ANISOU  611  CG  LYS A  51    17074  18522  13312  -5042   6071  -2799
ATOM    612  CD  LYS A  51      -2.455  29.990 -30.738  1.00129.49           C  
ANISOU  612  CD  LYS A  51    16592  18719  13891  -4599   6288  -2957
ATOM    613  CE  LYS A  51      -2.026  28.528 -30.952  1.00129.62           C  
ANISOU  613  CE  LYS A  51    16540  18689  14022  -4366   6747  -3299
ATOM    614  NZ  LYS A  51      -1.205  28.363 -32.166  1.00126.50           N1+
ANISOU  614  NZ  LYS A  51    16241  18473  13348  -4740   7285  -3571
ATOM    615  H   LYS A  51      -5.171  34.084 -31.589  1.00  0.00           H  
ATOM    616  HA  LYS A  51      -3.613  32.841 -33.624  1.00  0.00           H  
ATOM    617  HB3 LYS A  51      -4.545  31.944 -30.870  1.00  0.00           H  
ATOM    618  HB2 LYS A  51      -2.998  32.607 -31.319  1.00  0.00           H  
ATOM    619  HG3 LYS A  51      -2.686  30.534 -32.817  1.00  0.00           H  
ATOM    620  HG2 LYS A  51      -4.122  29.866 -32.079  1.00  0.00           H  
ATOM    621  HD3 LYS A  51      -3.034  30.063 -29.817  1.00  0.00           H  
ATOM    622  HD2 LYS A  51      -1.572  30.613 -30.590  1.00  0.00           H  
ATOM    623  HE3 LYS A  51      -2.904  27.886 -31.031  1.00  0.00           H  
ATOM    624  HE2 LYS A  51      -1.453  28.180 -30.092  1.00  0.00           H  
ATOM    625  HZ1 LYS A  51      -0.944  27.393 -32.269  1.00  0.00           H  
ATOM    626  HZ2 LYS A  51      -1.737  28.655 -32.974  1.00  0.00           H  
ATOM    627  HZ3 LYS A  51      -0.372  28.930 -32.091  1.00  0.00           H  
ATOM    628  N   ALA A  52      -6.644  31.580 -33.152  1.00113.37           N  
ANISOU  628  N   ALA A  52    16324  16268  10485  -5765   5237  -2288
ATOM    629  CA  ALA A  52      -7.717  30.745 -33.694  1.00112.86           C  
ANISOU  629  CA  ALA A  52    16622  16063  10199  -5826   5194  -2346
ATOM    630  C   ALA A  52      -8.419  31.333 -34.937  1.00112.52           C  
ANISOU  630  C   ALA A  52    17098  16023   9633  -6358   5008  -2185
ATOM    631  O   ALA A  52      -9.212  30.622 -35.553  1.00112.02           O  
ANISOU  631  O   ALA A  52    17372  15877   9315  -6504   4969  -2229
ATOM    632  CB  ALA A  52      -8.732  30.477 -32.571  1.00110.21           C  
ANISOU  632  CB  ALA A  52    16188  15542  10145  -5419   4811  -2216
ATOM    633  H   ALA A  52      -6.869  32.093 -32.309  1.00  0.00           H  
ATOM    634  HA  ALA A  52      -7.288  29.787 -33.993  1.00  0.00           H  
ATOM    635  HB1 ALA A  52      -9.558  29.852 -32.914  1.00  0.00           H  
ATOM    636  HB2 ALA A  52      -8.261  29.963 -31.733  1.00  0.00           H  
ATOM    637  HB3 ALA A  52      -9.154  31.408 -32.189  1.00  0.00           H  
ATOM    638  N   GLY A  53      -8.130  32.600 -35.283  1.00109.95           N  
ANISOU  638  N   GLY A  53    16849  15784   9142  -6657   4882  -1992
ATOM    639  CA  GLY A  53      -8.715  33.305 -36.425  1.00110.84           C  
ANISOU  639  CA  GLY A  53    17462  15891   8759  -7168   4669  -1796
ATOM    640  C   GLY A  53     -10.126  33.853 -36.143  1.00108.47           C  
ANISOU  640  C   GLY A  53    17348  15426   8439  -7102   4051  -1460
ATOM    641  O   GLY A  53     -10.808  34.245 -37.088  1.00109.10           O  
ANISOU  641  O   GLY A  53    17861  15477   8117  -7465   3834  -1314
ATOM    642  H   GLY A  53      -7.468  33.119 -34.723  1.00  0.00           H  
ATOM    643  HA3 GLY A  53      -8.743  32.652 -37.299  1.00  0.00           H  
ATOM    644  HA2 GLY A  53      -8.064  34.142 -36.679  1.00  0.00           H  
ATOM    645  N   ARG A  54     -10.570  33.886 -34.872  1.00107.69           N  
ANISOU  645  N   ARG A  54    16920  15229   8768  -6647   3763  -1339
ATOM    646  CA  ARG A  54     -11.847  34.462 -34.434  1.00105.66           C  
ANISOU  646  CA  ARG A  54    16742  14821   8584  -6502   3198  -1044
ATOM    647  C   ARG A  54     -11.832  36.001 -34.325  1.00105.75           C  
ANISOU  647  C   ARG A  54    16843  14787   8549  -6644   2882   -748
ATOM    648  O   ARG A  54     -12.910  36.594 -34.279  1.00105.39           O  
ANISOU  648  O   ARG A  54    17023  14629   8394  -6706   2433   -480
ATOM    649  CB  ARG A  54     -12.281  33.853 -33.083  1.00114.72           C  
ANISOU  649  CB  ARG A  54    17514  15880  10195  -5964   3080  -1082
ATOM    650  CG  ARG A  54     -12.365  32.315 -33.060  1.00114.81           C  
ANISOU  650  CG  ARG A  54    17508  15877  10239  -5825   3319  -1336
ATOM    651  CD  ARG A  54     -13.117  31.770 -31.831  1.00117.02           C  
ANISOU  651  CD  ARG A  54    17553  16042  10867  -5396   3085  -1300
ATOM    652  NE  ARG A  54     -12.383  31.981 -30.573  1.00118.74           N  
ANISOU  652  NE  ARG A  54    17359  16256  11501  -5022   3128  -1313
ATOM    653  CZ  ARG A  54     -11.850  31.038 -29.776  1.00119.74           C  
ANISOU  653  CZ  ARG A  54    17209  16353  11935  -4667   3322  -1489
ATOM    654  NH1 ARG A  54     -11.962  29.734 -30.064  1.00119.25           N  
ANISOU  654  NH1 ARG A  54    17246  16234  11829  -4618   3512  -1681
ATOM    655  NH2 ARG A  54     -11.191  31.408 -28.669  1.00121.34           N1+
ANISOU  655  NH2 ARG A  54    17059  16566  12480  -4371   3309  -1466
ATOM    656  H   ARG A  54      -9.949  33.577 -34.137  1.00  0.00           H  
ATOM    657  HA  ARG A  54     -12.607  34.204 -35.173  1.00  0.00           H  
ATOM    658  HB3 ARG A  54     -13.267  34.255 -32.842  1.00  0.00           H  
ATOM    659  HB2 ARG A  54     -11.618  34.186 -32.285  1.00  0.00           H  
ATOM    660  HG3 ARG A  54     -11.341  31.940 -33.053  1.00  0.00           H  
ATOM    661  HG2 ARG A  54     -12.824  31.916 -33.966  1.00  0.00           H  
ATOM    662  HD3 ARG A  54     -13.496  30.759 -31.976  1.00  0.00           H  
ATOM    663  HD2 ARG A  54     -14.008  32.384 -31.699  1.00  0.00           H  
ATOM    664  HE  ARG A  54     -12.263  32.946 -30.305  1.00  0.00           H  
ATOM    665 HH12 ARG A  54     -11.543  29.039 -29.462  1.00  0.00           H  
ATOM    666 HH11 ARG A  54     -12.442  29.440 -30.902  1.00  0.00           H  
ATOM    667 HH22 ARG A  54     -10.762  30.717 -28.068  1.00  0.00           H  
ATOM    668 HH21 ARG A  54     -11.091  32.384 -28.431  1.00  0.00           H  
ATOM    669  N   LEU A  55     -10.640  36.618 -34.276  1.00107.96           N  
ANISOU  669  N   LEU A  55    16958  15151   8911  -6706   3110   -795
ATOM    670  CA  LEU A  55     -10.446  38.067 -34.197  1.00108.08           C  
ANISOU  670  CA  LEU A  55    17099  15104   8861  -6886   2856   -533
ATOM    671  C   LEU A  55      -9.253  38.454 -35.086  1.00109.64           C  
ANISOU  671  C   LEU A  55    17491  15453   8715  -7386   3201   -607
ATOM    672  O   LEU A  55      -8.305  37.678 -35.189  1.00110.98           O  
ANISOU  672  O   LEU A  55    17501  15800   8865  -7450   3694   -905
ATOM    673  CB  LEU A  55     -10.262  38.456 -32.708  1.00107.58           C  
ANISOU  673  CB  LEU A  55    16638  14985   9253  -6491   2743   -490
ATOM    674  CG  LEU A  55     -10.128  39.964 -32.396  1.00107.50           C  
ANISOU  674  CG  LEU A  55    16756  14841   9247  -6590   2416   -210
ATOM    675  CD1 LEU A  55     -11.345  40.783 -32.881  1.00107.11           C  
ANISOU  675  CD1 LEU A  55    17128  14604   8963  -6732   1947     93
ATOM    676  CD2 LEU A  55      -9.844  40.188 -30.895  1.00108.35           C  
ANISOU  676  CD2 LEU A  55    16493  14873   9800  -6165   2282   -191
ATOM    677  H   LEU A  55      -9.794  36.069 -34.340  1.00  0.00           H  
ATOM    678  HA  LEU A  55     -11.327  38.567 -34.601  1.00  0.00           H  
ATOM    679  HB3 LEU A  55      -9.389  37.930 -32.319  1.00  0.00           H  
ATOM    680  HB2 LEU A  55     -11.110  38.073 -32.143  1.00  0.00           H  
ATOM    681  HG  LEU A  55      -9.249  40.329 -32.928  1.00  0.00           H  
ATOM    682 HD11 LEU A  55     -11.686  41.506 -32.140  1.00  0.00           H  
ATOM    683 HD12 LEU A  55     -11.092  41.348 -33.778  1.00  0.00           H  
ATOM    684 HD13 LEU A  55     -12.198  40.148 -33.121  1.00  0.00           H  
ATOM    685 HD21 LEU A  55      -8.976  40.835 -30.759  1.00  0.00           H  
ATOM    686 HD22 LEU A  55     -10.680  40.651 -30.373  1.00  0.00           H  
ATOM    687 HD23 LEU A  55      -9.630  39.253 -30.375  1.00  0.00           H  
ATOM    688  N   ASP A  56      -9.325  39.636 -35.722  1.00115.45           N  
ANISOU  688  N   ASP A  56    18584  16112   9170  -7748   2959   -343
ATOM    689  CA  ASP A  56      -8.307  40.129 -36.666  1.00112.84           C  
ANISOU  689  CA  ASP A  56    18491  15926   8458  -8293   3283   -398
ATOM    690  C   ASP A  56      -7.409  41.233 -36.092  1.00112.73           C  
ANISOU  690  C   ASP A  56    18330  15939   8565  -8393   3340   -330
ATOM    691  O   ASP A  56      -6.301  41.403 -36.600  1.00110.25           O  
ANISOU  691  O   ASP A  56    18017  15820   8054  -8769   3752   -481
ATOM    692  CB  ASP A  56      -8.907  40.593 -38.015  1.00111.15           C  
ANISOU  692  CB  ASP A  56    18886  15629   7717  -8772   3033   -167
ATOM    693  CG  ASP A  56      -9.666  39.505 -38.782  1.00159.69           C  
ANISOU  693  CG  ASP A  56    25251  21876  13547  -8967   3238   -347
ATOM    694  OD1 ASP A  56      -9.309  38.317 -38.619  1.00128.19           O  
ANISOU  694  OD1 ASP A  56    20976  18040   9692  -8824   3705   -700
ATOM    695  OD2 ASP A  56     -10.521  39.896 -39.605  1.00276.04           O1-
ANISOU  695  OD2 ASP A  56    36270  35799  32815  -1886   1539    965
ATOM    696  H   ASP A  56     -10.148  40.210 -35.616  1.00  0.00           H  
ATOM    697  HA  ASP A  56      -7.619  39.314 -36.901  1.00  0.00           H  
ATOM    698  HB3 ASP A  56      -8.123  40.975 -38.670  1.00  0.00           H  
ATOM    699  HB2 ASP A  56      -9.599  41.414 -37.819  1.00  0.00           H  
ATOM    700  N   ARG A  57      -7.865  41.956 -35.057  1.00116.24           N  
ANISOU  700  N   ARG A  57    18671  16191   9305  -8099   2942   -112
ATOM    701  CA  ARG A  57      -7.074  42.999 -34.404  1.00116.64           C  
ANISOU  701  CA  ARG A  57    18585  16243   9492  -8176   2967    -51
ATOM    702  C   ARG A  57      -7.555  43.209 -32.967  1.00112.46           C  
ANISOU  702  C   ARG A  57    17734  15555   9440  -7645   2668     26
ATOM    703  O   ARG A  57      -8.735  43.020 -32.669  1.00109.62           O  
ANISOU  703  O   ARG A  57    17414  15017   9220  -7318   2317    147
ATOM    704  CB  ARG A  57      -7.074  44.310 -35.231  1.00115.63           C  
ANISOU  704  CB  ARG A  57    18973  15993   8968  -8701   2789    218
ATOM    705  CG  ARG A  57      -8.441  44.999 -35.402  1.00114.91           C  
ANISOU  705  CG  ARG A  57    19314  15590   8757  -8664   2217    569
ATOM    706  CD  ARG A  57      -8.367  46.211 -36.344  1.00299.79           C  
ANISOU  706  CD  ARG A  57    37977  37972  37956    -21     27     30
ATOM    707  NE  ARG A  57      -9.624  46.971 -36.362  1.00300.00           N  
ANISOU  707  NE  ARG A  57    37995  37995  37995      0      0      0
ATOM    708  CZ  ARG A  57      -9.973  47.944 -35.502  1.00178.79           C  
ANISOU  708  CZ  ARG A  57    28313  22924  16695  -8794   1081   1411
ATOM    709  NH1 ARG A  57      -9.142  48.348 -34.530  1.00115.04           N  
ANISOU  709  NH1 ARG A  57    19944  14852   8912  -8667   1229   1313
ATOM    710  NH2 ARG A  57     -11.176  48.520 -35.617  1.00203.70           N1+
ANISOU  710  NH2 ARG A  57    31778  25789  19828  -8660    555   1723
ATOM    711  H   ARG A  57      -8.774  41.766 -34.661  1.00  0.00           H  
ATOM    712  HA  ARG A  57      -6.043  42.642 -34.337  1.00  0.00           H  
ATOM    713  HB3 ARG A  57      -6.651  44.111 -36.216  1.00  0.00           H  
ATOM    714  HB2 ARG A  57      -6.388  45.016 -34.760  1.00  0.00           H  
ATOM    715  HG3 ARG A  57      -8.914  45.263 -34.456  1.00  0.00           H  
ATOM    716  HG2 ARG A  57      -9.093  44.263 -35.874  1.00  0.00           H  
ATOM    717  HD3 ARG A  57      -8.318  45.810 -37.357  1.00  0.00           H  
ATOM    718  HD2 ARG A  57      -7.471  46.820 -36.224  1.00  0.00           H  
ATOM    719  HE  ARG A  57     -10.299  46.681 -37.056  1.00  0.00           H  
ATOM    720 HH12 ARG A  57      -9.416  49.077 -33.888  1.00  0.00           H  
ATOM    721 HH11 ARG A  57      -8.230  47.923 -34.439  1.00  0.00           H  
ATOM    722 HH22 ARG A  57     -11.459  49.248 -34.977  1.00  0.00           H  
ATOM    723 HH21 ARG A  57     -11.815  48.232 -36.344  1.00  0.00           H  
ATOM    724  N   ARG A  58      -6.604  43.630 -32.120  1.00122.96           N  
ANISOU  724  N   ARG A  58    18728  16980  11013  -7581   2829    -63
ATOM    725  CA  ARG A  58      -6.779  43.908 -30.697  1.00121.89           C  
ANISOU  725  CA  ARG A  58    18272  16733  11308  -7136   2614    -29
ATOM    726  C   ARG A  58      -7.822  45.000 -30.402  1.00121.21           C  
ANISOU  726  C   ARG A  58    18497  16312  11248  -7060   2112    279
ATOM    727  O   ARG A  58      -8.064  45.875 -31.237  1.00121.85           O  
ANISOU  727  O   ARG A  58    19042  16243  11012  -7401   1927    495
ATOM    728  CB  ARG A  58      -5.423  44.350 -30.106  1.00132.04           C  
ANISOU  728  CB  ARG A  58    19208  18207  12753  -7227   2880   -160
ATOM    729  CG  ARG A  58      -4.275  43.334 -30.261  1.00133.91           C  
ANISOU  729  CG  ARG A  58    19053  18790  13037  -7260   3388   -474
ATOM    730  CD  ARG A  58      -2.996  43.785 -29.534  1.00135.02           C  
ANISOU  730  CD  ARG A  58    18822  19124  13353  -7351   3576   -564
ATOM    731  NE  ARG A  58      -3.125  43.663 -28.074  1.00131.54           N  
ANISOU  731  NE  ARG A  58    18044  18611  13323  -6900   3359   -548
ATOM    732  CZ  ARG A  58      -2.708  42.609 -27.353  1.00130.60           C  
ANISOU  732  CZ  ARG A  58    17420  18674  13526  -6551   3534   -744
ATOM    733  NH1 ARG A  58      -1.990  41.633 -27.922  1.00132.95           N  
ANISOU  733  NH1 ARG A  58    17462  19231  13823  -6568   3943   -984
ATOM    734  NH2 ARG A  58      -3.023  42.520 -26.056  1.00127.52           N1+
ANISOU  734  NH2 ARG A  58    16789  18201  13459  -6187   3304   -704
ATOM    735  H   ARG A  58      -5.669  43.772 -32.474  1.00  0.00           H  
ATOM    736  HA  ARG A  58      -7.102  42.978 -30.228  1.00  0.00           H  
ATOM    737  HB3 ARG A  58      -5.551  44.574 -29.046  1.00  0.00           H  
ATOM    738  HB2 ARG A  58      -5.121  45.290 -30.572  1.00  0.00           H  
ATOM    739  HG3 ARG A  58      -4.060  43.081 -31.300  1.00  0.00           H  
ATOM    740  HG2 ARG A  58      -4.621  42.412 -29.792  1.00  0.00           H  
ATOM    741  HD3 ARG A  58      -2.920  44.864 -29.672  1.00  0.00           H  
ATOM    742  HD2 ARG A  58      -2.076  43.381 -29.957  1.00  0.00           H  
ATOM    743  HE  ARG A  58      -3.679  44.372 -27.615  1.00  0.00           H  
ATOM    744 HH12 ARG A  58      -1.854  40.755 -27.433  1.00  0.00           H  
ATOM    745 HH11 ARG A  58      -1.739  41.691 -28.897  1.00  0.00           H  
ATOM    746 HH22 ARG A  58      -2.749  41.703 -25.527  1.00  0.00           H  
ATOM    747 HH21 ARG A  58      -3.572  43.238 -25.606  1.00  0.00           H  
ATOM    748  N   TYR A  59      -8.367  44.947 -29.179  1.00119.96           N  
ANISOU  748  N   TYR A  59    18084  16028  11465  -6614   1904    295
ATOM    749  CA  TYR A  59      -9.168  46.017 -28.593  1.00118.88           C  
ANISOU  749  CA  TYR A  59    18171  15571  11429  -6475   1474    541
ATOM    750  C   TYR A  59      -8.221  47.064 -27.991  1.00119.96           C  
ANISOU  750  C   TYR A  59    18294  15657  11628  -6642   1501    575
ATOM    751  O   TYR A  59      -7.491  46.746 -27.051  1.00118.44           O  
ANISOU  751  O   TYR A  59    17706  15601  11694  -6471   1659    413
ATOM    752  CB  TYR A  59     -10.101  45.434 -27.513  1.00115.27           C  
ANISOU  752  CB  TYR A  59    17459  15012  11327  -5933   1269    515
ATOM    753  CG  TYR A  59     -11.055  44.366 -28.013  1.00113.94           C  
ANISOU  753  CG  TYR A  59    17290  14889  11114  -5769   1222    479
ATOM    754  CD1 TYR A  59     -12.140  44.722 -28.840  1.00114.45           C  
ANISOU  754  CD1 TYR A  59    17708  14785  10991  -5836    901    692
ATOM    755  CD2 TYR A  59     -10.867  43.016 -27.649  1.00112.30           C  
ANISOU  755  CD2 TYR A  59    16730  14876  11063  -5537   1469    242
ATOM    756  CE1 TYR A  59     -13.049  43.738 -29.274  1.00113.40           C  
ANISOU  756  CE1 TYR A  59    17566  14707  10812  -5711    835    660
ATOM    757  CE2 TYR A  59     -11.764  42.030 -28.100  1.00111.25           C  
ANISOU  757  CE2 TYR A  59    16620  14765  10886  -5404   1420    204
ATOM    758  CZ  TYR A  59     -12.860  42.391 -28.907  1.00111.78           C  
ANISOU  758  CZ  TYR A  59    17029  14692  10749  -5511   1108    408
ATOM    759  OH  TYR A  59     -13.740  41.439 -29.332  1.00110.89           O  
ANISOU  759  OH  TYR A  59    16932  14621  10581  -5416   1046    369
ATOM    760  H   TYR A  59      -8.107  44.195 -28.554  1.00  0.00           H  
ATOM    761  HA  TYR A  59      -9.785  46.485 -29.362  1.00  0.00           H  
ATOM    762  HB3 TYR A  59     -10.697  46.236 -27.076  1.00  0.00           H  
ATOM    763  HB2 TYR A  59      -9.516  45.017 -26.691  1.00  0.00           H  
ATOM    764  HD1 TYR A  59     -12.290  45.754 -29.126  1.00  0.00           H  
ATOM    765  HD2 TYR A  59     -10.037  42.730 -27.020  1.00  0.00           H  
ATOM    766  HE1 TYR A  59     -13.898  44.020 -29.876  1.00  0.00           H  
ATOM    767  HE2 TYR A  59     -11.611  40.998 -27.821  1.00  0.00           H  
ATOM    768  HH  TYR A  59     -13.509  40.556 -29.034  1.00  0.00           H  
ATOM    769  N   ASN A  60      -8.258  48.290 -28.538  1.00130.20           N  
ANISOU  769  N   ASN A  60    20035  16751  12683  -6986   1328    793
ATOM    770  CA  ASN A  60      -7.470  49.440 -28.066  1.00130.74           C  
ANISOU  770  CA  ASN A  60    20173  16735  12768  -7214   1338    842
ATOM    771  C   ASN A  60      -8.098  50.164 -26.850  1.00130.65           C  
ANISOU  771  C   ASN A  60    20147  16416  13079  -6837   1017    935
ATOM    772  O   ASN A  60      -7.624  51.238 -26.482  1.00131.12           O  
ANISOU  772  O   ASN A  60    20409  16289  13123  -7025    929   1031
ATOM    773  CB  ASN A  60      -7.119  50.378 -29.254  1.00155.35           C  
ANISOU  773  CB  ASN A  60    23826  19727  15472  -7772   1294   1042
ATOM    774  CG  ASN A  60      -8.301  50.954 -30.045  1.00155.29           C  
ANISOU  774  CG  ASN A  60    24301  19427  15275  -7765    920   1313
ATOM    775  OD1 ASN A  60      -9.447  50.886 -29.618  1.00154.36           O  
ANISOU  775  OD1 ASN A  60    24122  19162  15366  -7325    647   1373
ATOM    776  ND2 ASN A  60      -8.021  51.542 -31.210  1.00293.03           N  
ANISOU  776  ND2 ASN A  60    37368  36771  37198   -877    707    988
ATOM    777  H   ASN A  60      -8.899  48.480 -29.297  1.00  0.00           H  
ATOM    778  HA  ASN A  60      -6.516  49.043 -27.714  1.00  0.00           H  
ATOM    779  HB3 ASN A  60      -6.499  49.821 -29.958  1.00  0.00           H  
ATOM    780  HB2 ASN A  60      -6.500  51.207 -28.908  1.00  0.00           H  
ATOM    781 HD22 ASN A  60      -8.766  51.951 -31.756  1.00  0.00           H  
ATOM    782 HD21 ASN A  60      -7.070  51.603 -31.542  1.00  0.00           H  
ATOM    783  N   GLY A  61      -9.126  49.557 -26.236  1.00122.58           N  
ANISOU  783  N   GLY A  61    18892  15350  12333  -6337    878    886
ATOM    784  CA  GLY A  61      -9.767  50.045 -25.024  1.00122.18           C  
ANISOU  784  CA  GLY A  61    18788  15041  12595  -5951    623    930
ATOM    785  C   GLY A  61     -10.998  49.178 -24.739  1.00121.26           C  
ANISOU  785  C   GLY A  61    18540  14855  12679  -5487    431    932
ATOM    786  O   GLY A  61     -11.556  48.546 -25.638  1.00121.39           O  
ANISOU  786  O   GLY A  61    18679  14899  12544  -5501    354   1004
ATOM    787  H   GLY A  61      -9.473  48.685 -26.607  1.00  0.00           H  
ATOM    788  HA3 GLY A  61     -10.079  51.083 -25.151  1.00  0.00           H  
ATOM    789  HA2 GLY A  61      -9.066  49.999 -24.189  1.00  0.00           H  
ATOM    790  N   ILE A  62     -11.443  49.192 -23.472  1.00114.25           N  
ANISOU  790  N   ILE A  62    17410  13887  12113  -5105    356    851
ATOM    791  CA  ILE A  62     -12.683  48.561 -23.006  1.00111.38           C  
ANISOU  791  CA  ILE A  62    16881  13468  11969  -4663    194    832
ATOM    792  C   ILE A  62     -13.952  49.198 -23.615  1.00112.21           C  
ANISOU  792  C   ILE A  62    17328  13283  12024  -4590   -162   1070
ATOM    793  O   ILE A  62     -14.894  48.473 -23.937  1.00111.25           O  
ANISOU  793  O   ILE A  62    17162  13212  11897  -4434   -278   1104
ATOM    794  CB  ILE A  62     -12.784  48.569 -21.448  1.00110.10           C  
ANISOU  794  CB  ILE A  62    16433  13264  12134  -4323    200    697
ATOM    795  CG1 ILE A  62     -14.064  47.871 -20.934  1.00111.87           C  
ANISOU  795  CG1 ILE A  62    16536  13393  12576  -3898     13    697
ATOM    796  CG2 ILE A  62     -12.635  49.970 -20.817  1.00109.80           C  
ANISOU  796  CG2 ILE A  62    16589  12981  12149  -4419    119    752
ATOM    797  CD1 ILE A  62     -14.029  47.465 -19.455  1.00111.90           C  
ANISOU  797  CD1 ILE A  62    16214  13443  12859  -3581     85    523
ATOM    798  H   ILE A  62     -10.933  49.718 -22.776  1.00  0.00           H  
ATOM    799  HA  ILE A  62     -12.652  47.520 -23.334  1.00  0.00           H  
ATOM    800  HB  ILE A  62     -11.940  47.974 -21.095  1.00  0.00           H  
ATOM    801 HG13 ILE A  62     -14.208  46.970 -21.525  1.00  0.00           H  
ATOM    802 HG12 ILE A  62     -14.941  48.495 -21.104  1.00  0.00           H  
ATOM    803 HG21 ILE A  62     -12.579  49.907 -19.730  1.00  0.00           H  
ATOM    804 HG22 ILE A  62     -11.726  50.472 -21.147  1.00  0.00           H  
ATOM    805 HG23 ILE A  62     -13.479  50.616 -21.059  1.00  0.00           H  
ATOM    806 HD11 ILE A  62     -14.859  46.797 -19.222  1.00  0.00           H  
ATOM    807 HD12 ILE A  62     -13.106  46.943 -19.207  1.00  0.00           H  
ATOM    808 HD13 ILE A  62     -14.114  48.333 -18.802  1.00  0.00           H  
ATOM    809  N   ILE A  63     -13.928  50.527 -23.810  1.00117.53           N  
ANISOU  809  N   ILE A  63    18350  13651  12655  -4715   -344   1240
ATOM    810  CA  ILE A  63     -14.978  51.275 -24.497  1.00118.49           C  
ANISOU  810  CA  ILE A  63    18814  13460  12747  -4631   -714   1494
ATOM    811  C   ILE A  63     -15.036  50.960 -26.007  1.00119.50           C  
ANISOU  811  C   ILE A  63    19172  13705  12528  -4932   -769   1635
ATOM    812  O   ILE A  63     -16.138  50.904 -26.544  1.00120.05           O  
ANISOU  812  O   ILE A  63    19332  13684  12598  -4773  -1054   1788
ATOM    813  CB  ILE A  63     -14.845  52.810 -24.260  1.00123.52           C  
ANISOU  813  CB  ILE A  63    19819  13702  13410  -4710   -882   1643
ATOM    814  CG1 ILE A  63     -16.006  53.651 -24.848  1.00126.17           C  
ANISOU  814  CG1 ILE A  63    20520  13676  13741  -4580  -1302   1932
ATOM    815  CG2 ILE A  63     -13.495  53.389 -24.733  1.00125.78           C  
ANISOU  815  CG2 ILE A  63    20325  14045  13421  -5228   -672   1644
ATOM    816  CD1 ILE A  63     -17.405  53.227 -24.371  1.00124.30           C  
ANISOU  816  CD1 ILE A  63    20027  13378  13824  -4038  -1541   1938
ATOM    817  H   ILE A  63     -13.121  51.058 -23.519  1.00  0.00           H  
ATOM    818  HA  ILE A  63     -15.926  50.950 -24.063  1.00  0.00           H  
ATOM    819  HB  ILE A  63     -14.880  52.955 -23.180  1.00  0.00           H  
ATOM    820 HG13 ILE A  63     -15.976  53.629 -25.938  1.00  0.00           H  
ATOM    821 HG12 ILE A  63     -15.859  54.697 -24.578  1.00  0.00           H  
ATOM    822 HG21 ILE A  63     -13.397  54.434 -24.440  1.00  0.00           H  
ATOM    823 HG22 ILE A  63     -12.649  52.855 -24.298  1.00  0.00           H  
ATOM    824 HG23 ILE A  63     -13.392  53.347 -25.818  1.00  0.00           H  
ATOM    825 HD11 ILE A  63     -18.111  54.052 -24.458  1.00  0.00           H  
ATOM    826 HD12 ILE A  63     -17.794  52.399 -24.963  1.00  0.00           H  
ATOM    827 HD13 ILE A  63     -17.393  52.914 -23.327  1.00  0.00           H  
ATOM    828  N   ASP A  64     -13.884  50.676 -26.648  1.00120.14           N  
ANISOU  828  N   ASP A  64    19315  14016  12317  -5367   -483   1567
ATOM    829  CA  ASP A  64     -13.829  50.190 -28.031  1.00122.42           C  
ANISOU  829  CA  ASP A  64    19836  14441  12235  -5706   -473   1662
ATOM    830  C   ASP A  64     -14.395  48.761 -28.155  1.00120.14           C  
ANISOU  830  C   ASP A  64    19252  14421  11976  -5528   -380   1518
ATOM    831  O   ASP A  64     -15.083  48.487 -29.134  1.00121.68           O  
ANISOU  831  O   ASP A  64    19648  14640  11946  -5649   -535   1643
ATOM    832  CB  ASP A  64     -12.415  50.281 -28.645  1.00127.63           C  
ANISOU  832  CB  ASP A  64    20629  15280  12585  -6229   -147   1597
ATOM    833  CG  ASP A  64     -12.366  49.874 -30.126  1.00128.24           C  
ANISOU  833  CG  ASP A  64    20960  15511  12254  -6603    -93   1663
ATOM    834  OD1 ASP A  64     -12.996  50.586 -30.938  1.00129.54           O  
ANISOU  834  OD1 ASP A  64    21582  15453  12184  -6790   -404   1941
ATOM    835  OD2 ASP A  64     -11.681  48.871 -30.426  1.00127.28           O1-
ANISOU  835  OD2 ASP A  64    20595  15719  12046  -6701    251   1440
ATOM    836  H   ASP A  64     -13.007  50.717 -26.151  1.00  0.00           H  
ATOM    837  HA  ASP A  64     -14.473  50.846 -28.619  1.00  0.00           H  
ATOM    838  HB3 ASP A  64     -11.723  49.647 -28.089  1.00  0.00           H  
ATOM    839  HB2 ASP A  64     -12.012  51.289 -28.550  1.00  0.00           H  
ATOM    840  N   CYS A  65     -14.129  47.896 -27.158  1.00112.14           N  
ANISOU  840  N   CYS A  65    17791  13595  11220  -5261   -143   1266
ATOM    841  CA  CYS A  65     -14.675  46.538 -27.067  1.00110.79           C  
ANISOU  841  CA  CYS A  65    17335  13640  11120  -5054    -49   1113
ATOM    842  C   CYS A  65     -16.215  46.537 -26.999  1.00110.39           C  
ANISOU  842  C   CYS A  65    17319  13421  11204  -4748   -441   1269
ATOM    843  O   CYS A  65     -16.842  45.749 -27.708  1.00110.68           O  
ANISOU  843  O   CYS A  65    17407  13559  11087  -4797   -530   1306
ATOM    844  CB  CYS A  65     -14.021  45.735 -25.919  1.00106.17           C  
ANISOU  844  CB  CYS A  65    16308  13219  10814  -4807    226    854
ATOM    845  SG  CYS A  65     -14.584  44.008 -25.855  1.00102.85           S  
ANISOU  845  SG  CYS A  65    15560  13037  10482  -4569    385    647
ATOM    846  H   CYS A  65     -13.535  48.191 -26.396  1.00  0.00           H  
ATOM    847  HA  CYS A  65     -14.414  46.041 -28.001  1.00  0.00           H  
ATOM    848  HB3 CYS A  65     -14.225  46.195 -24.954  1.00  0.00           H  
ATOM    849  HB2 CYS A  65     -12.938  45.729 -26.037  1.00  0.00           H  
ATOM    850  HG  CYS A  65     -13.847  43.657 -24.798  1.00  0.00           H  
ATOM    851  N   PHE A  66     -16.786  47.473 -26.218  1.00115.57           N  
ANISOU  851  N   PHE A  66    17972  13814  12127  -4466   -681   1367
ATOM    852  CA  PHE A  66     -18.218  47.764 -26.188  1.00115.68           C  
ANISOU  852  CA  PHE A  66    17985  13656  12312  -4153  -1054   1517
ATOM    853  C   PHE A  66     -18.726  48.234 -27.562  1.00119.05           C  
ANISOU  853  C   PHE A  66    18807  13977  12447  -4393  -1366   1798
ATOM    854  O   PHE A  66     -19.571  47.555 -28.139  1.00119.22           O  
ANISOU  854  O   PHE A  66    18797  14129  12373  -4386  -1503   1842
ATOM    855  CB  PHE A  66     -18.535  48.774 -25.061  1.00118.14           C  
ANISOU  855  CB  PHE A  66    18260  13678  12951  -3837  -1204   1552
ATOM    856  CG  PHE A  66     -20.003  49.139 -24.891  1.00118.31           C  
ANISOU  856  CG  PHE A  66    18219  13533  13202  -3469  -1564   1682
ATOM    857  CD1 PHE A  66     -20.601  50.131 -25.701  1.00121.79           C  
ANISOU  857  CD1 PHE A  66    18988  13732  13555  -3502  -1946   1975
ATOM    858  CD2 PHE A  66     -20.821  48.388 -24.020  1.00115.26           C  
ANISOU  858  CD2 PHE A  66    17437  13237  13119  -3095  -1527   1517
ATOM    859  CE1 PHE A  66     -21.961  50.389 -25.598  1.00122.34           C  
ANISOU  859  CE1 PHE A  66    18944  13671  13867  -3136  -2290   2096
ATOM    860  CE2 PHE A  66     -22.173  48.682 -23.910  1.00115.75           C  
ANISOU  860  CE2 PHE A  66    17391  13177  13412  -2757  -1839   1621
ATOM    861  CZ  PHE A  66     -22.739  49.678 -24.695  1.00119.33           C  
ANISOU  861  CZ  PHE A  66    18127  13406  13805  -2764  -2221   1907
ATOM    862  H   PHE A  66     -16.196  48.076 -25.661  1.00  0.00           H  
ATOM    863  HA  PHE A  66     -18.733  46.831 -25.946  1.00  0.00           H  
ATOM    864  HB3 PHE A  66     -17.975  49.695 -25.215  1.00  0.00           H  
ATOM    865  HB2 PHE A  66     -18.175  48.374 -24.113  1.00  0.00           H  
ATOM    866  HD1 PHE A  66     -20.005  50.694 -26.404  1.00  0.00           H  
ATOM    867  HD2 PHE A  66     -20.398  47.595 -23.422  1.00  0.00           H  
ATOM    868  HE1 PHE A  66     -22.412  51.150 -26.217  1.00  0.00           H  
ATOM    869  HE2 PHE A  66     -22.790  48.129 -23.218  1.00  0.00           H  
ATOM    870  HZ  PHE A  66     -23.791  49.900 -24.605  1.00  0.00           H  
ATOM    871  N   ARG A  67     -18.183  49.360 -28.063  1.00127.98           N  
ANISOU  871  N   ARG A  67    20336  14878  13414  -4641  -1479   1990
ATOM    872  CA  ARG A  67     -18.567  50.007 -29.324  1.00131.81           C  
ANISOU  872  CA  ARG A  67    21270  15212  13600  -4899  -1806   2297
ATOM    873  C   ARG A  67     -18.521  49.082 -30.547  1.00132.52           C  
ANISOU  873  C   ARG A  67    21431  15590  13331  -5216  -1725   2280
ATOM    874  O   ARG A  67     -19.410  49.186 -31.382  1.00134.67           O  
ANISOU  874  O   ARG A  67    21881  15825  13464  -5248  -2067   2491
ATOM    875  CB  ARG A  67     -17.687  51.253 -29.568  1.00153.67           C  
ANISOU  875  CB  ARG A  67    24476  17756  16157  -5254  -1795   2444
ATOM    876  CG  ARG A  67     -17.987  52.417 -28.610  1.00154.66           C  
ANISOU  876  CG  ARG A  67    24678  17502  16583  -4992  -1949   2519
ATOM    877  CD  ARG A  67     -19.220  53.234 -29.016  1.00152.74           C  
ANISOU  877  CD  ARG A  67    24748  16873  16414  -4800  -2463   2851
ATOM    878  NE  ARG A  67     -19.644  54.123 -27.928  1.00155.24           N  
ANISOU  878  NE  ARG A  67    24904  16900  17181  -4309  -2589   2817
ATOM    879  CZ  ARG A  67     -20.594  55.068 -28.014  1.00154.30           C  
ANISOU  879  CZ  ARG A  67    24949  16418  17262  -3996  -3007   3051
ATOM    880  NH1 ARG A  67     -21.226  55.320 -29.169  1.00150.43           N  
ANISOU  880  NH1 ARG A  67    24797  15804  16556  -4125  -3391   3373
ATOM    881  NH2 ARG A  67     -20.920  55.766 -26.919  1.00155.38           N1+
ANISOU  881  NH2 ARG A  67    24913  16312  17815  -3551  -3045   2964
ATOM    882  H   ARG A  67     -17.464  49.835 -27.531  1.00  0.00           H  
ATOM    883  HA  ARG A  67     -19.603  50.324 -29.201  1.00  0.00           H  
ATOM    884  HB3 ARG A  67     -17.802  51.613 -30.593  1.00  0.00           H  
ATOM    885  HB2 ARG A  67     -16.640  50.964 -29.476  1.00  0.00           H  
ATOM    886  HG3 ARG A  67     -17.132  53.088 -28.700  1.00  0.00           H  
ATOM    887  HG2 ARG A  67     -18.028  52.123 -27.564  1.00  0.00           H  
ATOM    888  HD3 ARG A  67     -20.029  52.624 -29.419  1.00  0.00           H  
ATOM    889  HD2 ARG A  67     -18.915  53.915 -29.811  1.00  0.00           H  
ATOM    890  HE  ARG A  67     -19.209  53.957 -27.032  1.00  0.00           H  
ATOM    891 HH12 ARG A  67     -21.942  56.031 -29.222  1.00  0.00           H  
ATOM    892 HH11 ARG A  67     -20.990  54.794 -29.997  1.00  0.00           H  
ATOM    893 HH22 ARG A  67     -21.633  56.480 -26.962  1.00  0.00           H  
ATOM    894 HH21 ARG A  67     -20.455  55.588 -26.041  1.00  0.00           H  
ATOM    895  N   ARG A  68     -17.523  48.188 -30.617  1.00125.51           N  
ANISOU  895  N   ARG A  68    20388  14990  12310  -5432  -1276   2020
ATOM    896  CA  ARG A  68     -17.345  47.230 -31.704  1.00125.20           C  
ANISOU  896  CA  ARG A  68    20427  15224  11919  -5761  -1098   1940
ATOM    897  C   ARG A  68     -18.434  46.143 -31.703  1.00124.74           C  
ANISOU  897  C   ARG A  68    20117  15317  11961  -5518  -1206   1868
ATOM    898  O   ARG A  68     -19.175  46.037 -32.679  1.00125.79           O  
ANISOU  898  O   ARG A  68    20472  15466  11856  -5671  -1481   2041
ATOM    899  CB  ARG A  68     -15.915  46.654 -31.632  1.00114.38           C  
ANISOU  899  CB  ARG A  68    18895  14094  10469  -5973   -562   1650
ATOM    900  CG  ARG A  68     -15.521  45.784 -32.840  1.00114.16           C  
ANISOU  900  CG  ARG A  68    19023  14315  10039  -6378   -313   1550
ATOM    901  CD  ARG A  68     -14.142  45.121 -32.707  1.00113.94           C  
ANISOU  901  CD  ARG A  68    18783  14517   9994  -6530    223   1255
ATOM    902  NE  ARG A  68     -13.069  46.078 -32.388  1.00114.82           N  
ANISOU  902  NE  ARG A  68    19104  14568   9956  -6861    339   1322
ATOM    903  CZ  ARG A  68     -11.753  45.805 -32.414  1.00115.25           C  
ANISOU  903  CZ  ARG A  68    19051  14839   9899  -7129    789   1111
ATOM    904  NH1 ARG A  68     -11.303  44.592 -32.765  1.00114.98           N  
ANISOU  904  NH1 ARG A  68    18716  15070   9901  -7068   1163    821
ATOM    905  NH2 ARG A  68     -10.874  46.750 -32.064  1.00115.52           N1+
ANISOU  905  NH2 ARG A  68    19273  14823   9795  -7457    874   1183
ATOM    906  H   ARG A  68     -16.815  48.176 -29.894  1.00  0.00           H  
ATOM    907  HA  ARG A  68     -17.431  47.780 -32.643  1.00  0.00           H  
ATOM    908  HB3 ARG A  68     -15.781  46.087 -30.708  1.00  0.00           H  
ATOM    909  HB2 ARG A  68     -15.217  47.491 -31.577  1.00  0.00           H  
ATOM    910  HG3 ARG A  68     -15.620  46.310 -33.791  1.00  0.00           H  
ATOM    911  HG2 ARG A  68     -16.240  44.966 -32.879  1.00  0.00           H  
ATOM    912  HD3 ARG A  68     -13.880  44.768 -33.704  1.00  0.00           H  
ATOM    913  HD2 ARG A  68     -14.157  44.236 -32.073  1.00  0.00           H  
ATOM    914  HE  ARG A  68     -13.361  46.991 -32.067  1.00  0.00           H  
ATOM    915 HH12 ARG A  68     -10.316  44.369 -32.734  1.00  0.00           H  
ATOM    916 HH11 ARG A  68     -11.961  43.871 -33.023  1.00  0.00           H  
ATOM    917 HH22 ARG A  68      -9.884  46.545 -32.040  1.00  0.00           H  
ATOM    918 HH21 ARG A  68     -11.203  47.631 -31.670  1.00  0.00           H  
ATOM    919  N   THR A  69     -18.512  45.369 -30.607  1.00120.47           N  
ANISOU  919  N   THR A  69    19136  14893  11743  -5180   -995   1620
ATOM    920  CA  THR A  69     -19.418  44.223 -30.469  1.00118.68           C  
ANISOU  920  CA  THR A  69    18654  14822  11615  -4976  -1036   1515
ATOM    921  C   THR A  69     -20.914  44.606 -30.452  1.00119.51           C  
ANISOU  921  C   THR A  69    18778  14789  11841  -4754  -1545   1759
ATOM    922  O   THR A  69     -21.713  43.870 -31.033  1.00120.86           O  
ANISOU  922  O   THR A  69    19033  15074  11815  -4884  -1731   1837
ATOM    923  CB  THR A  69     -19.100  43.397 -29.194  1.00112.14           C  
ANISOU  923  CB  THR A  69    17385  14092  11131  -4645   -742   1234
ATOM    924  OG1 THR A  69     -19.318  44.127 -27.998  1.00110.92           O  
ANISOU  924  OG1 THR A  69    17089  13739  11315  -4327   -867   1282
ATOM    925  CG2 THR A  69     -17.665  42.845 -29.192  1.00111.59           C  
ANISOU  925  CG2 THR A  69    17251  14193  10957  -4838   -263    996
ATOM    926  H   THR A  69     -17.889  45.540 -29.831  1.00  0.00           H  
ATOM    927  HA  THR A  69     -19.258  43.579 -31.337  1.00  0.00           H  
ATOM    928  HB  THR A  69     -19.777  42.542 -29.157  1.00  0.00           H  
ATOM    929  HG1 THR A  69     -18.585  44.740 -27.873  1.00  0.00           H  
ATOM    930 HG21 THR A  69     -17.473  42.266 -28.293  1.00  0.00           H  
ATOM    931 HG22 THR A  69     -17.504  42.185 -30.045  1.00  0.00           H  
ATOM    932 HG23 THR A  69     -16.914  43.633 -29.243  1.00  0.00           H  
ATOM    933  N   THR A  70     -21.259  45.751 -29.836  1.00118.72           N  
ANISOU  933  N   THR A  70    18609  14444  12055  -4437  -1769   1879
ATOM    934  CA  THR A  70     -22.634  46.250 -29.763  1.00120.48           C  
ANISOU  934  CA  THR A  70    18786  14516  12473  -4153  -2238   2097
ATOM    935  C   THR A  70     -23.097  46.971 -31.043  1.00125.19           C  
ANISOU  935  C   THR A  70    19805  15005  12755  -4426  -2627   2427
ATOM    936  O   THR A  70     -24.297  46.944 -31.308  1.00127.13           O  
ANISOU  936  O   THR A  70    20003  15285  13014  -4332  -2991   2583
ATOM    937  CB  THR A  70     -22.860  47.216 -28.571  1.00106.14           C  
ANISOU  937  CB  THR A  70    16834  12436  11058  -3763  -2325   2116
ATOM    938  OG1 THR A  70     -22.172  48.446 -28.709  1.00106.29           O  
ANISOU  938  OG1 THR A  70    17218  12213  10953  -3954  -2342   2257
ATOM    939  CG2 THR A  70     -22.531  46.585 -27.214  1.00105.25           C  
ANISOU  939  CG2 THR A  70    16338  12426  11225  -3521  -1975   1813
ATOM    940  H   THR A  70     -20.551  46.308 -29.377  1.00  0.00           H  
ATOM    941  HA  THR A  70     -23.289  45.392 -29.612  1.00  0.00           H  
ATOM    942  HB  THR A  70     -23.919  47.477 -28.544  1.00  0.00           H  
ATOM    943  HG1 THR A  70     -21.236  48.284 -28.550  1.00  0.00           H  
ATOM    944 HG21 THR A  70     -22.653  47.311 -26.412  1.00  0.00           H  
ATOM    945 HG22 THR A  70     -23.211  45.758 -27.021  1.00  0.00           H  
ATOM    946 HG23 THR A  70     -21.515  46.196 -27.160  1.00  0.00           H  
ATOM    947  N   ALA A  71     -22.186  47.587 -31.821  1.00131.95           N  
ANISOU  947  N   ALA A  71    21072  15738  13323  -4777  -2573   2544
ATOM    948  CA  ALA A  71     -22.557  48.254 -33.075  1.00133.86           C  
ANISOU  948  CA  ALA A  71    21771  15847  13242  -5057  -2969   2888
ATOM    949  C   ALA A  71     -22.895  47.267 -34.201  1.00133.92           C  
ANISOU  949  C   ALA A  71    21904  16123  12856  -5404  -3016   2908
ATOM    950  O   ALA A  71     -23.822  47.540 -34.962  1.00135.62           O  
ANISOU  950  O   ALA A  71    22317  16283  12929  -5466  -3479   3194
ATOM    951  CB  ALA A  71     -21.460  49.220 -33.539  1.00137.49           C  
ANISOU  951  CB  ALA A  71    22672  16122  13446  -5412  -2866   2997
ATOM    952  H   ALA A  71     -21.208  47.596 -31.567  1.00  0.00           H  
ATOM    953  HA  ALA A  71     -23.451  48.854 -32.889  1.00  0.00           H  
ATOM    954  HB1 ALA A  71     -21.720  49.684 -34.491  1.00  0.00           H  
ATOM    955  HB2 ALA A  71     -21.324  50.029 -32.822  1.00  0.00           H  
ATOM    956  HB3 ALA A  71     -20.507  48.708 -33.677  1.00  0.00           H  
ATOM    957  N   ASP A  72     -22.150  46.151 -34.279  1.00131.10           N  
ANISOU  957  N   ASP A  72    21438  16044  12329  -5620  -2560   2611
ATOM    958  CA  ASP A  72     -22.317  45.129 -35.317  1.00132.68           C  
ANISOU  958  CA  ASP A  72    21815  16479  12119  -5993  -2567   2604
ATOM    959  C   ASP A  72     -23.584  44.277 -35.129  1.00131.18           C  
ANISOU  959  C   ASP A  72    21314  16436  12093  -5749  -2809   2587
ATOM    960  O   ASP A  72     -24.341  44.131 -36.088  1.00133.80           O  
ANISOU  960  O   ASP A  72    21848  16812  12177  -5939  -3195   2810
ATOM    961  CB  ASP A  72     -21.069  44.229 -35.509  1.00  0.00           C  
ATOM    962  CG  ASP A  72     -19.757  44.972 -35.806  1.00  0.00           C  
ATOM    963  OD1 ASP A  72     -19.820  46.150 -36.224  1.00  0.00           O  
ATOM    964  OD2 ASP A  72     -18.702  44.316 -35.671  1.00  0.00           O1-
ATOM    965  H   ASP A  72     -21.387  46.012 -33.632  1.00  0.00           H  
ATOM    966  HA  ASP A  72     -22.452  45.665 -36.259  1.00  0.00           H  
ATOM    967  HB2 ASP A  72     -20.921  43.650 -34.597  1.00  0.00           H  
ATOM    968  HB3 ASP A  72     -21.249  43.526 -36.324  1.00  0.00           H  
ATOM    969  N   GLU A  73     -23.788  43.734 -33.916  1.00126.66           N  
ANISOU  969  N   GLU A  73    20260  15944  11921  -5357  -2599   2333
ATOM    970  CA  GLU A  73     -24.827  42.736 -33.622  1.00126.83           C  
ANISOU  970  CA  GLU A  73    19952  16140  12099  -5161  -2733   2255
ATOM    971  C   GLU A  73     -25.930  43.239 -32.670  1.00127.30           C  
ANISOU  971  C   GLU A  73    19629  16086  12653  -4637  -3058   2351
ATOM    972  O   GLU A  73     -26.778  42.440 -32.270  1.00127.45           O  
ANISOU  972  O   GLU A  73    19320  16268  12837  -4467  -3125   2256
ATOM    973  CB  GLU A  73     -24.136  41.462 -33.075  1.00  0.00           C  
ATOM    974  CG  GLU A  73     -23.265  40.704 -34.099  1.00  0.00           C  
ATOM    975  CD  GLU A  73     -24.052  40.157 -35.293  1.00  0.00           C  
ATOM    976  OE1 GLU A  73     -25.110  39.535 -35.048  1.00  0.00           O  
ATOM    977  OE2 GLU A  73     -23.576  40.362 -36.430  1.00  0.00           O1-
ATOM    978  H   GLU A  73     -23.129  43.920 -33.174  1.00  0.00           H  
ATOM    979  HA  GLU A  73     -25.363  42.470 -34.534  1.00  0.00           H  
ATOM    980  HB2 GLU A  73     -23.495  41.744 -32.240  1.00  0.00           H  
ATOM    981  HB3 GLU A  73     -24.870  40.769 -32.659  1.00  0.00           H  
ATOM    982  HG2 GLU A  73     -22.462  41.349 -34.460  1.00  0.00           H  
ATOM    983  HG3 GLU A  73     -22.778  39.861 -33.608  1.00  0.00           H  
ATOM    984  N   GLY A  74     -25.925  44.537 -32.325  1.00125.01           N  
ANISOU  984  N   GLY A  74    19391  15521  12587  -4404  -3240   2522
ATOM    985  CA  GLY A  74     -26.880  45.142 -31.394  1.00125.02           C  
ANISOU  985  CA  GLY A  74    19044  15388  13069  -3895  -3501   2586
ATOM    986  C   GLY A  74     -26.432  44.931 -29.939  1.00120.60           C  
ANISOU  986  C   GLY A  74    18158  14792  12873  -3575  -3118   2302
ATOM    987  O   GLY A  74     -25.509  44.164 -29.658  1.00117.40           O  
ANISOU  987  O   GLY A  74    17729  14512  12367  -3724  -2676   2050
ATOM    988  H   GLY A  74     -25.200  45.141 -32.689  1.00  0.00           H  
ATOM    989  HA3 GLY A  74     -27.881  44.731 -31.536  1.00  0.00           H  
ATOM    990  HA2 GLY A  74     -26.941  46.211 -31.604  1.00  0.00           H  
ATOM    991  N   LEU A  75     -27.101  45.628 -29.005  1.00111.78           N  
ANISOU  991  N   LEU A  75    16787  13500  12184  -3128  -3283   2336
ATOM    992  CA  LEU A  75     -26.783  45.627 -27.571  1.00107.99           C  
ANISOU  992  CA  LEU A  75    16021  12969  12041  -2829  -2951   2079
ATOM    993  C   LEU A  75     -26.930  44.243 -26.901  1.00104.70           C  
ANISOU  993  C   LEU A  75    15252  12838  11691  -2789  -2657   1794
ATOM    994  O   LEU A  75     -26.164  43.941 -25.986  1.00101.33           O  
ANISOU  994  O   LEU A  75    14716  12435  11351  -2741  -2281   1562
ATOM    995  CB  LEU A  75     -27.650  46.696 -26.866  1.00108.20           C  
ANISOU  995  CB  LEU A  75    15864  12753  12495  -2371  -3195   2165
ATOM    996  CG  LEU A  75     -27.068  47.226 -25.536  1.00105.86           C  
ANISOU  996  CG  LEU A  75    15480  12269  12471  -2135  -2914   1984
ATOM    997  CD1 LEU A  75     -25.783  48.051 -25.761  1.00106.49           C  
ANISOU  997  CD1 LEU A  75    15965  12160  12338  -2395  -2783   2043
ATOM    998  CD2 LEU A  75     -28.127  48.002 -24.724  1.00107.47           C  
ANISOU  998  CD2 LEU A  75    15516  12231  13087  -1683  -3155   2056
ATOM    999  H   LEU A  75     -27.850  46.243 -29.290  1.00  0.00           H  
ATOM   1000  HA  LEU A  75     -25.733  45.914 -27.492  1.00  0.00           H  
ATOM   1001  HB3 LEU A  75     -28.646  46.281 -26.701  1.00  0.00           H  
ATOM   1002  HB2 LEU A  75     -27.800  47.550 -27.529  1.00  0.00           H  
ATOM   1003  HG  LEU A  75     -26.793  46.364 -24.928  1.00  0.00           H  
ATOM   1004 HD11 LEU A  75     -25.832  49.039 -25.305  1.00  0.00           H  
ATOM   1005 HD12 LEU A  75     -24.923  47.546 -25.328  1.00  0.00           H  
ATOM   1006 HD13 LEU A  75     -25.568  48.204 -26.818  1.00  0.00           H  
ATOM   1007 HD21 LEU A  75     -28.181  47.624 -23.703  1.00  0.00           H  
ATOM   1008 HD22 LEU A  75     -27.916  49.070 -24.662  1.00  0.00           H  
ATOM   1009 HD23 LEU A  75     -29.125  47.907 -25.153  1.00  0.00           H  
ATOM   1010  N   MET A  76     -27.861  43.417 -27.416  1.00 99.49           N  
ANISOU 1010  N   MET A  76    14439  12393  10971  -2836  -2838   1820
ATOM   1011  CA  MET A  76     -28.128  42.030 -27.013  1.00 96.86           C  
ANISOU 1011  CA  MET A  76    13820  12320  10664  -2844  -2594   1571
ATOM   1012  C   MET A  76     -26.912  41.083 -27.124  1.00 94.33           C  
ANISOU 1012  C   MET A  76    13657  12103  10083  -3129  -2156   1362
ATOM   1013  O   MET A  76     -26.869  40.087 -26.403  1.00 91.61           O  
ANISOU 1013  O   MET A  76    13086  11875   9846  -3046  -1863   1121
ATOM   1014  CB  MET A  76     -29.340  41.519 -27.828  1.00  0.00           C  
ATOM   1015  CG  MET A  76     -29.842  40.099 -27.492  1.00  0.00           C  
ATOM   1016  SD  MET A  76     -30.408  39.842 -25.786  1.00  0.00           S  
ATOM   1017  CE  MET A  76     -31.996  40.714 -25.842  1.00  0.00           C  
ATOM   1018  H   MET A  76     -28.424  43.756 -28.182  1.00  0.00           H  
ATOM   1019  HA  MET A  76     -28.418  42.063 -25.962  1.00  0.00           H  
ATOM   1020  HB2 MET A  76     -30.170  42.216 -27.708  1.00  0.00           H  
ATOM   1021  HB3 MET A  76     -29.091  41.549 -28.890  1.00  0.00           H  
ATOM   1022  HG2 MET A  76     -30.668  39.847 -28.157  1.00  0.00           H  
ATOM   1023  HG3 MET A  76     -29.069  39.361 -27.708  1.00  0.00           H  
ATOM   1024  HE1 MET A  76     -32.504  40.624 -24.882  1.00  0.00           H  
ATOM   1025  HE2 MET A  76     -31.847  41.773 -26.051  1.00  0.00           H  
ATOM   1026  HE3 MET A  76     -32.639  40.291 -26.614  1.00  0.00           H  
ATOM   1027  N   ALA A  77     -25.933  41.424 -27.984  1.00 92.87           N  
ANISOU 1027  N   ALA A  77    13854  11864   9568  -3453  -2099   1451
ATOM   1028  CA  ALA A  77     -24.668  40.708 -28.179  1.00 92.12           C  
ANISOU 1028  CA  ALA A  77    13905  11867   9229  -3724  -1672   1253
ATOM   1029  C   ALA A  77     -23.789  40.584 -26.918  1.00 89.82           C  
ANISOU 1029  C   ALA A  77    13402  11536   9191  -3505  -1309   1028
ATOM   1030  O   ALA A  77     -22.973  39.664 -26.855  1.00 88.85           O  
ANISOU 1030  O   ALA A  77    13257  11528   8974  -3616   -948    818
ATOM   1031  CB  ALA A  77     -23.887  41.405 -29.301  1.00 94.65           C  
ANISOU 1031  CB  ALA A  77    14649  12117   9198  -4083  -1687   1401
ATOM   1032  H   ALA A  77     -26.040  42.268 -28.531  1.00  0.00           H  
ATOM   1033  HA  ALA A  77     -24.916  39.698 -28.508  1.00  0.00           H  
ATOM   1034  HB1 ALA A  77     -22.992  40.848 -29.578  1.00  0.00           H  
ATOM   1035  HB2 ALA A  77     -24.506  41.502 -30.192  1.00  0.00           H  
ATOM   1036  HB3 ALA A  77     -23.570  42.407 -29.008  1.00  0.00           H  
ATOM   1037  N   LEU A  78     -23.989  41.479 -25.933  1.00 88.94           N  
ANISOU 1037  N   LEU A  78    13140  11254   9399  -3191  -1414   1073
ATOM   1038  CA  LEU A  78     -23.335  41.441 -24.623  1.00 87.76           C  
ANISOU 1038  CA  LEU A  78    12803  11055   9487  -2988  -1133    890
ATOM   1039  C   LEU A  78     -23.841  40.301 -23.712  1.00 86.71           C  
ANISOU 1039  C   LEU A  78    12354  11071   9522  -2812   -964    678
ATOM   1040  O   LEU A  78     -23.128  39.925 -22.784  1.00 85.70           O  
ANISOU 1040  O   LEU A  78    12103  10967   9493  -2734   -674    498
ATOM   1041  CB  LEU A  78     -23.538  42.783 -23.899  1.00 84.78           C  
ANISOU 1041  CB  LEU A  78    12398  10435   9379  -2725  -1310    994
ATOM   1042  CG  LEU A  78     -22.962  44.028 -24.592  1.00 84.03           C  
ANISOU 1042  CG  LEU A  78    12642  10135   9151  -2888  -1422   1180
ATOM   1043  CD1 LEU A  78     -23.449  45.294 -23.871  1.00 84.46           C  
ANISOU 1043  CD1 LEU A  78    12686   9920   9484  -2599  -1652   1292
ATOM   1044  CD2 LEU A  78     -21.425  44.001 -24.698  1.00 83.95           C  
ANISOU 1044  CD2 LEU A  78    12729  10156   9014  -3095  -1081   1056
ATOM   1045  H   LEU A  78     -24.674  42.211 -26.064  1.00  0.00           H  
ATOM   1046  HA  LEU A  78     -22.268  41.295 -24.786  1.00  0.00           H  
ATOM   1047  HB3 LEU A  78     -23.070  42.716 -22.923  1.00  0.00           H  
ATOM   1048  HB2 LEU A  78     -24.603  42.927 -23.722  1.00  0.00           H  
ATOM   1049  HG  LEU A  78     -23.372  44.060 -25.600  1.00  0.00           H  
ATOM   1050 HD11 LEU A  78     -23.339  46.163 -24.513  1.00  0.00           H  
ATOM   1051 HD12 LEU A  78     -24.502  45.228 -23.594  1.00  0.00           H  
ATOM   1052 HD13 LEU A  78     -22.877  45.481 -22.962  1.00  0.00           H  
ATOM   1053 HD21 LEU A  78     -20.980  44.953 -24.408  1.00  0.00           H  
ATOM   1054 HD22 LEU A  78     -20.981  43.230 -24.067  1.00  0.00           H  
ATOM   1055 HD23 LEU A  78     -21.114  43.804 -25.725  1.00  0.00           H  
ATOM   1056  N   TRP A  79     -25.047  39.774 -23.980  1.00 92.74           N  
ANISOU 1056  N   TRP A  79    12988  11939  10309  -2767  -1155    707
ATOM   1057  CA  TRP A  79     -25.664  38.664 -23.248  1.00 91.85           C  
ANISOU 1057  CA  TRP A  79    12598  11963  10338  -2635  -1007    517
ATOM   1058  C   TRP A  79     -25.464  37.298 -23.933  1.00 90.88           C  
ANISOU 1058  C   TRP A  79    12568  12014   9949  -2900   -838    405
ATOM   1059  O   TRP A  79     -26.158  36.348 -23.568  1.00 90.62           O  
ANISOU 1059  O   TRP A  79    12375  12103   9954  -2879   -836    315
ATOM   1060  CB  TRP A  79     -27.155  38.981 -22.996  1.00 89.78           C  
ANISOU 1060  CB  TRP A  79    12085  11723  10306  -2413  -1291    586
ATOM   1061  CG  TRP A  79     -27.409  40.020 -21.947  1.00 89.44           C  
ANISOU 1061  CG  TRP A  79    11876  11513  10593  -2084  -1338    589
ATOM   1062  CD1 TRP A  79     -27.622  39.746 -20.642  1.00 87.90           C  
ANISOU 1062  CD1 TRP A  79    11423  11329  10647  -1857  -1164    413
ATOM   1063  CD2 TRP A  79     -27.399  41.478 -22.052  1.00 90.88           C  
ANISOU 1063  CD2 TRP A  79    12176  11475  10880  -1959  -1567    770
ATOM   1064  NE1 TRP A  79     -27.761  40.922 -19.941  1.00 88.24           N  
ANISOU 1064  NE1 TRP A  79    11412  11178  10936  -1603  -1246    452
ATOM   1065  CE2 TRP A  79     -27.626  42.024 -20.752  1.00 90.12           C  
ANISOU 1065  CE2 TRP A  79    11878  11258  11105  -1646  -1496    670
ATOM   1066  CE3 TRP A  79     -27.219  42.402 -23.107  1.00 93.05           C  
ANISOU 1066  CE3 TRP A  79    12741  11625  10991  -2097  -1824   1010
ATOM   1067  CZ2 TRP A  79     -27.663  43.408 -20.507  1.00 91.49           C  
ANISOU 1067  CZ2 TRP A  79    12130  11174  11459  -1450  -1659    785
ATOM   1068  CZ3 TRP A  79     -27.264  43.793 -22.875  1.00 94.36           C  
ANISOU 1068  CZ3 TRP A  79    12989  11528  11336  -1900  -2007   1147
ATOM   1069  CH2 TRP A  79     -27.480  44.298 -21.579  1.00 93.49           C  
ANISOU 1069  CH2 TRP A  79    12673  11286  11564  -1571  -1918   1027
ATOM   1070  H   TRP A  79     -25.578  40.127 -24.765  1.00  0.00           H  
ATOM   1071  HA  TRP A  79     -25.192  38.550 -22.271  1.00  0.00           H  
ATOM   1072  HB3 TRP A  79     -27.693  38.091 -22.669  1.00  0.00           H  
ATOM   1073  HB2 TRP A  79     -27.639  39.292 -23.922  1.00  0.00           H  
ATOM   1074  HD1 TRP A  79     -27.662  38.751 -20.222  1.00  0.00           H  
ATOM   1075  HE1 TRP A  79     -27.900  40.941 -18.936  1.00  0.00           H  
ATOM   1076  HE3 TRP A  79     -27.038  42.035 -24.105  1.00  0.00           H  
ATOM   1077  HZ2 TRP A  79     -27.829  43.781 -19.507  1.00  0.00           H  
ATOM   1078  HZ3 TRP A  79     -27.126  44.480 -23.693  1.00  0.00           H  
ATOM   1079  HH2 TRP A  79     -27.505  45.364 -21.410  1.00  0.00           H  
ATOM   1080  N   ARG A  80     -24.516  37.191 -24.883  1.00 96.65           N  
ANISOU 1080  N   ARG A  80    13564  12751  10406  -3164   -676    396
ATOM   1081  CA  ARG A  80     -24.188  35.930 -25.550  1.00 97.28           C  
ANISOU 1081  CA  ARG A  80    13759  12965  10236  -3407   -476    261
ATOM   1082  C   ARG A  80     -23.565  34.913 -24.573  1.00 95.62           C  
ANISOU 1082  C   ARG A  80    13384  12776  10171  -3261   -127     22
ATOM   1083  O   ARG A  80     -22.571  35.224 -23.916  1.00 94.53           O  
ANISOU 1083  O   ARG A  80    13170  12566  10180  -3117     50    -38
ATOM   1084  CB  ARG A  80     -23.299  36.187 -26.786  1.00111.80           C  
ANISOU 1084  CB  ARG A  80    15934  14815  11731  -3743   -380    302
ATOM   1085  CG  ARG A  80     -22.990  34.903 -27.587  1.00113.20           C  
ANISOU 1085  CG  ARG A  80    16273  15115  11624  -4016   -183    156
ATOM   1086  CD  ARG A  80     -22.249  35.132 -28.913  1.00115.34           C  
ANISOU 1086  CD  ARG A  80    16892  15407  11525  -4381    -88    192
ATOM   1087  NE  ARG A  80     -23.099  35.769 -29.932  1.00117.77           N  
ANISOU 1087  NE  ARG A  80    17422  15734  11593  -4614   -472    432
ATOM   1088  CZ  ARG A  80     -23.152  37.077 -30.244  1.00118.45           C  
ANISOU 1088  CZ  ARG A  80    17638  15721  11646  -4649   -732    671
ATOM   1089  NH1 ARG A  80     -22.394  37.986 -29.614  1.00116.64           N  
ANISOU 1089  NH1 ARG A  80    17347  15371  11599  -4490   -632    687
ATOM   1090  NH2 ARG A  80     -23.980  37.484 -31.216  1.00121.10           N1+
ANISOU 1090  NH2 ARG A  80    18182  16071  11761  -4853  -1111    904
ATOM   1091  H   ARG A  80     -23.968  38.000 -25.141  1.00  0.00           H  
ATOM   1092  HA  ARG A  80     -25.131  35.518 -25.919  1.00  0.00           H  
ATOM   1093  HB3 ARG A  80     -22.365  36.662 -26.481  1.00  0.00           H  
ATOM   1094  HB2 ARG A  80     -23.809  36.901 -27.433  1.00  0.00           H  
ATOM   1095  HG3 ARG A  80     -23.947  34.436 -27.823  1.00  0.00           H  
ATOM   1096  HG2 ARG A  80     -22.443  34.170 -26.994  1.00  0.00           H  
ATOM   1097  HD3 ARG A  80     -21.848  34.187 -29.279  1.00  0.00           H  
ATOM   1098  HD2 ARG A  80     -21.385  35.774 -28.751  1.00  0.00           H  
ATOM   1099  HE  ARG A  80     -23.727  35.145 -30.419  1.00  0.00           H  
ATOM   1100 HH12 ARG A  80     -22.445  38.962 -29.869  1.00  0.00           H  
ATOM   1101 HH11 ARG A  80     -21.790  37.703 -28.857  1.00  0.00           H  
ATOM   1102 HH22 ARG A  80     -24.028  38.458 -31.478  1.00  0.00           H  
ATOM   1103 HH21 ARG A  80     -24.555  36.820 -31.714  1.00  0.00           H  
ATOM   1104  N   GLY A  81     -24.173  33.717 -24.526  1.00 98.04           N  
ANISOU 1104  N   GLY A  81    13643  13175  10430  -3312    -67    -95
ATOM   1105  CA  GLY A  81     -23.750  32.596 -23.689  1.00 97.02           C  
ANISOU 1105  CA  GLY A  81    13410  13055  10400  -3207    223   -305
ATOM   1106  C   GLY A  81     -24.339  32.647 -22.269  1.00 95.63           C  
ANISOU 1106  C   GLY A  81    12954  12858  10523  -2928    181   -342
ATOM   1107  O   GLY A  81     -24.052  31.743 -21.485  1.00 94.81           O  
ANISOU 1107  O   GLY A  81    12780  12741  10504  -2835    401   -493
ATOM   1108  H   GLY A  81     -24.987  33.562 -25.103  1.00  0.00           H  
ATOM   1109  HA3 GLY A  81     -22.661  32.553 -23.627  1.00  0.00           H  
ATOM   1110  HA2 GLY A  81     -24.073  31.670 -24.165  1.00  0.00           H  
ATOM   1111  N   ASN A  82     -25.146  33.669 -21.921  1.00 88.27           N  
ANISOU 1111  N   ASN A  82    11873  11914   9753  -2792    -93   -206
ATOM   1112  CA  ASN A  82     -25.703  33.831 -20.575  1.00 88.01           C  
ANISOU 1112  CA  ASN A  82    11575  11860  10004  -2531   -109   -252
ATOM   1113  C   ASN A  82     -26.805  32.810 -20.231  1.00 87.91           C  
ANISOU 1113  C   ASN A  82    11425  11958  10018  -2555   -107   -346
ATOM   1114  O   ASN A  82     -26.914  32.458 -19.059  1.00 87.22           O  
ANISOU 1114  O   ASN A  82    11193  11856  10089  -2410     35   -460
ATOM   1115  CB  ASN A  82     -26.181  35.283 -20.354  1.00 93.34           C  
ANISOU 1115  CB  ASN A  82    12136  12468  10863  -2359   -365   -107
ATOM   1116  CG  ASN A  82     -26.468  35.582 -18.877  1.00 91.83           C  
ANISOU 1116  CG  ASN A  82    11718  12220  10951  -2092   -292   -193
ATOM   1117  OD1 ASN A  82     -27.619  35.760 -18.492  1.00 90.37           O  
ANISOU 1117  OD1 ASN A  82    11320  12085  10932  -1967   -419   -195
ATOM   1118  ND2 ASN A  82     -25.428  35.608 -18.041  1.00 92.33           N  
ANISOU 1118  ND2 ASN A  82    11814  12200  11068  -2016    -76   -276
ATOM   1119  H   ASN A  82     -25.358  34.398 -22.589  1.00  0.00           H  
ATOM   1120  HA  ASN A  82     -24.898  33.635 -19.863  1.00  0.00           H  
ATOM   1121  HB3 ASN A  82     -27.068  35.495 -20.953  1.00  0.00           H  
ATOM   1122  HB2 ASN A  82     -25.412  35.982 -20.687  1.00  0.00           H  
ATOM   1123 HD22 ASN A  82     -25.574  35.820 -17.064  1.00  0.00           H  
ATOM   1124 HD21 ASN A  82     -24.489  35.464 -18.381  1.00  0.00           H  
ATOM   1125  N   THR A  83     -27.568  32.322 -21.225  1.00 81.49           N  
ANISOU 1125  N   THR A  83    10673  11259   9031  -2767   -257   -302
ATOM   1126  CA  THR A  83     -28.599  31.295 -21.025  1.00 82.23           C  
ANISOU 1126  CA  THR A  83    10643  11478   9121  -2851   -260   -392
ATOM   1127  C   THR A  83     -28.028  29.975 -20.464  1.00 81.54           C  
ANISOU 1127  C   THR A  83    10641  11341   8998  -2873     67   -583
ATOM   1128  O   THR A  83     -28.645  29.398 -19.571  1.00 81.26           O  
ANISOU 1128  O   THR A  83    10444  11335   9094  -2796    132   -670
ATOM   1129  CB  THR A  83     -29.369  30.980 -22.335  1.00 81.50           C  
ANISOU 1129  CB  THR A  83    10658  11519   8791  -3138   -469   -313
ATOM   1130  OG1 THR A  83     -29.908  32.180 -22.854  1.00 83.38           O  
ANISOU 1130  OG1 THR A  83    10828  11777   9075  -3086   -805   -107
ATOM   1131  CG2 THR A  83     -30.521  29.964 -22.197  1.00 82.26           C  
ANISOU 1131  CG2 THR A  83    10607  11767   8881  -3261   -504   -396
ATOM   1132  H   THR A  83     -27.452  32.663 -22.169  1.00  0.00           H  
ATOM   1133  HA  THR A  83     -29.310  31.687 -20.295  1.00  0.00           H  
ATOM   1134  HB  THR A  83     -28.667  30.603 -23.081  1.00  0.00           H  
ATOM   1135  HG1 THR A  83     -30.509  31.962 -23.571  1.00  0.00           H  
ATOM   1136 HG21 THR A  83     -31.074  29.868 -23.132  1.00  0.00           H  
ATOM   1137 HG22 THR A  83     -30.160  28.968 -21.940  1.00  0.00           H  
ATOM   1138 HG23 THR A  83     -31.227  30.272 -21.424  1.00  0.00           H  
ATOM   1139  N   ALA A  84     -26.827  29.585 -20.934  1.00 83.07           N  
ANISOU 1139  N   ALA A  84    11083  11450   9031  -2963    277   -644
ATOM   1140  CA  ALA A  84     -26.047  28.448 -20.438  1.00 81.91           C  
ANISOU 1140  CA  ALA A  84    11035  11218   8870  -2944    577   -808
ATOM   1141  C   ALA A  84     -25.599  28.604 -18.972  1.00 81.06           C  
ANISOU 1141  C   ALA A  84    10760  11033   9006  -2675    678   -844
ATOM   1142  O   ALA A  84     -25.626  27.623 -18.229  1.00 80.44           O  
ANISOU 1142  O   ALA A  84    10673  10917   8972  -2639    816   -947
ATOM   1143  CB  ALA A  84     -24.833  28.228 -21.351  1.00 83.86           C  
ANISOU 1143  CB  ALA A  84    11528  11392   8941  -3043    775   -861
ATOM   1144  H   ALA A  84     -26.376  30.145 -21.643  1.00  0.00           H  
ATOM   1145  HA  ALA A  84     -26.671  27.559 -20.523  1.00  0.00           H  
ATOM   1146  HB1 ALA A  84     -24.268  27.345 -21.049  1.00  0.00           H  
ATOM   1147  HB2 ALA A  84     -25.142  28.076 -22.386  1.00  0.00           H  
ATOM   1148  HB3 ALA A  84     -24.151  29.078 -21.330  1.00  0.00           H  
ATOM   1149  N   ASN A  85     -25.226  29.835 -18.578  1.00 79.48           N  
ANISOU 1149  N   ASN A  85    10457  10799   8943  -2510    602   -756
ATOM   1150  CA  ASN A  85     -24.865  30.179 -17.200  1.00 78.82           C  
ANISOU 1150  CA  ASN A  85    10230  10649   9068  -2283    678   -786
ATOM   1151  C   ASN A  85     -26.084  30.241 -16.274  1.00 79.15           C  
ANISOU 1151  C   ASN A  85    10070  10746   9257  -2202    585   -803
ATOM   1152  O   ASN A  85     -25.929  29.882 -15.113  1.00 78.49           O  
ANISOU 1152  O   ASN A  85     9918  10622   9281  -2088    698   -875
ATOM   1153  CB  ASN A  85     -24.080  31.509 -17.168  1.00 95.31           C  
ANISOU 1153  CB  ASN A  85    12296  12681  11236  -2176    625   -698
ATOM   1154  CG  ASN A  85     -22.654  31.375 -17.706  1.00 95.92           C  
ANISOU 1154  CG  ASN A  85    12518  12717  11209  -2230    798   -724
ATOM   1155  OD1 ASN A  85     -21.927  30.463 -17.316  1.00 96.36           O  
ANISOU 1155  OD1 ASN A  85    12626  12745  11241  -2218    999   -831
ATOM   1156  ND2 ASN A  85     -22.233  32.300 -18.570  1.00 96.17           N  
ANISOU 1156  ND2 ASN A  85    12619  12739  11182  -2292    726   -628
ATOM   1157  H   ASN A  85     -25.237  30.595 -19.243  1.00  0.00           H  
ATOM   1158  HA  ASN A  85     -24.213  29.375 -16.852  1.00  0.00           H  
ATOM   1159  HB3 ASN A  85     -23.977  31.844 -16.134  1.00  0.00           H  
ATOM   1160  HB2 ASN A  85     -24.623  32.298 -17.689  1.00  0.00           H  
ATOM   1161 HD22 ASN A  85     -21.291  32.260 -18.932  1.00  0.00           H  
ATOM   1162 HD21 ASN A  85     -22.847  33.040 -18.878  1.00  0.00           H  
ATOM   1163  N   VAL A  86     -27.260  30.654 -16.776  1.00 72.66           N  
ANISOU 1163  N   VAL A  86     9146  10028   8433  -2271    383   -742
ATOM   1164  CA  VAL A  86     -28.496  30.703 -15.995  1.00 72.66           C  
ANISOU 1164  CA  VAL A  86     8908  10113   8588  -2200    315   -777
ATOM   1165  C   VAL A  86     -29.088  29.299 -15.740  1.00 73.50           C  
ANISOU 1165  C   VAL A  86     9047  10287   8591  -2370    436   -890
ATOM   1166  O   VAL A  86     -29.532  29.067 -14.621  1.00 73.49           O  
ANISOU 1166  O   VAL A  86     8926  10308   8691  -2318    526   -974
ATOM   1167  CB  VAL A  86     -29.555  31.660 -16.620  1.00 75.87           C  
ANISOU 1167  CB  VAL A  86     9142  10609   9076  -2171     35   -660
ATOM   1168  CG1 VAL A  86     -30.974  31.555 -16.016  1.00 76.68           C  
ANISOU 1168  CG1 VAL A  86     8948  10836   9350  -2106    -11   -722
ATOM   1169  CG2 VAL A  86     -29.089  33.126 -16.519  1.00 75.12           C  
ANISOU 1169  CG2 VAL A  86     9055  10391   9095  -1990    -69   -551
ATOM   1170  H   VAL A  86     -27.318  30.963 -17.737  1.00  0.00           H  
ATOM   1171  HA  VAL A  86     -28.243  31.115 -15.015  1.00  0.00           H  
ATOM   1172  HB  VAL A  86     -29.636  31.421 -17.682  1.00  0.00           H  
ATOM   1173 HG11 VAL A  86     -31.628  32.330 -16.417  1.00  0.00           H  
ATOM   1174 HG12 VAL A  86     -31.448  30.600 -16.242  1.00  0.00           H  
ATOM   1175 HG13 VAL A  86     -30.952  31.674 -14.932  1.00  0.00           H  
ATOM   1176 HG21 VAL A  86     -29.760  33.791 -17.063  1.00  0.00           H  
ATOM   1177 HG22 VAL A  86     -29.063  33.461 -15.482  1.00  0.00           H  
ATOM   1178 HG23 VAL A  86     -28.091  33.271 -16.929  1.00  0.00           H  
ATOM   1179  N   ILE A  87     -29.037  28.368 -16.714  1.00 76.96           N  
ANISOU 1179  N   ILE A  87     9686  10742   8813  -2590    462   -905
ATOM   1180  CA  ILE A  87     -29.477  26.975 -16.508  1.00 77.45           C  
ANISOU 1180  CA  ILE A  87     9836  10832   8758  -2778    584  -1016
ATOM   1181  C   ILE A  87     -28.534  26.146 -15.605  1.00 76.83           C  
ANISOU 1181  C   ILE A  87     9906  10591   8696  -2686    832  -1107
ATOM   1182  O   ILE A  87     -28.978  25.145 -15.044  1.00 77.09           O  
ANISOU 1182  O   ILE A  87     9998  10606   8686  -2785    943  -1194
ATOM   1183  CB  ILE A  87     -29.696  26.189 -17.835  1.00 82.02           C  
ANISOU 1183  CB  ILE A  87    10617  11460   9085  -3067    543  -1022
ATOM   1184  CG1 ILE A  87     -28.413  25.981 -18.671  1.00 81.93           C  
ANISOU 1184  CG1 ILE A  87    10906  11295   8926  -3090    712  -1052
ATOM   1185  CG2 ILE A  87     -30.835  26.816 -18.661  1.00 82.99           C  
ANISOU 1185  CG2 ILE A  87    10592  11757   9184  -3164    245   -899
ATOM   1186  CD1 ILE A  87     -28.589  25.082 -19.902  1.00 83.39           C  
ANISOU 1186  CD1 ILE A  87    11360  11498   8826  -3392    725  -1088
ATOM   1187  H   ILE A  87     -28.672  28.604 -17.628  1.00  0.00           H  
ATOM   1188  HA  ILE A  87     -30.439  27.012 -15.992  1.00  0.00           H  
ATOM   1189  HB  ILE A  87     -30.046  25.193 -17.559  1.00  0.00           H  
ATOM   1190 HG13 ILE A  87     -27.608  25.561 -18.068  1.00  0.00           H  
ATOM   1191 HG12 ILE A  87     -28.069  26.956 -18.993  1.00  0.00           H  
ATOM   1192 HG21 ILE A  87     -31.084  26.208 -19.530  1.00  0.00           H  
ATOM   1193 HG22 ILE A  87     -31.743  26.908 -18.065  1.00  0.00           H  
ATOM   1194 HG23 ILE A  87     -30.580  27.812 -19.019  1.00  0.00           H  
ATOM   1195 HD11 ILE A  87     -27.634  24.652 -20.205  1.00  0.00           H  
ATOM   1196 HD12 ILE A  87     -29.276  24.259 -19.702  1.00  0.00           H  
ATOM   1197 HD13 ILE A  87     -28.978  25.649 -20.748  1.00  0.00           H  
ATOM   1198  N   ARG A  88     -27.273  26.586 -15.461  1.00 81.61           N  
ANISOU 1198  N   ARG A  88    10568  11079   9362  -2508    904  -1078
ATOM   1199  CA  ARG A  88     -26.310  26.053 -14.499  1.00 81.52           C  
ANISOU 1199  CA  ARG A  88    10653  10925   9395  -2385   1093  -1137
ATOM   1200  C   ARG A  88     -26.547  26.645 -13.098  1.00 80.75           C  
ANISOU 1200  C   ARG A  88    10374  10838   9470  -2230   1078  -1135
ATOM   1201  O   ARG A  88     -26.577  25.896 -12.123  1.00 80.99           O  
ANISOU 1201  O   ARG A  88    10447  10821   9504  -2237   1179  -1194
ATOM   1202  CB  ARG A  88     -24.884  26.328 -15.032  1.00 87.88           C  
ANISOU 1202  CB  ARG A  88    11566  11632  10191  -2282   1182  -1116
ATOM   1203  CG  ARG A  88     -23.728  26.013 -14.057  1.00 87.48           C  
ANISOU 1203  CG  ARG A  88    11550  11457  10232  -2110   1326  -1148
ATOM   1204  CD  ARG A  88     -22.347  26.373 -14.625  1.00 87.25           C  
ANISOU 1204  CD  ARG A  88    11534  11381  10237  -1993   1397  -1124
ATOM   1205  NE  ARG A  88     -22.187  27.825 -14.812  1.00 86.85           N  
ANISOU 1205  NE  ARG A  88    11365  11410  10225  -1981   1268  -1039
ATOM   1206  CZ  ARG A  88     -21.987  28.733 -13.843  1.00 86.05           C  
ANISOU 1206  CZ  ARG A  88    11117  11319  10257  -1857   1186   -985
ATOM   1207  NH1 ARG A  88     -21.880  28.377 -12.556  1.00 85.69           N  
ANISOU 1207  NH1 ARG A  88    11016  11234  10308  -1748   1218  -1009
ATOM   1208  NH2 ARG A  88     -21.883  30.026 -14.168  1.00 85.77           N1+
ANISOU 1208  NH2 ARG A  88    11024  11320  10245  -1861   1070   -906
ATOM   1209  H   ARG A  88     -26.976  27.400 -15.982  1.00  0.00           H  
ATOM   1210  HA  ARG A  88     -26.438  24.970 -14.435  1.00  0.00           H  
ATOM   1211  HB3 ARG A  88     -24.814  27.378 -15.317  1.00  0.00           H  
ATOM   1212  HB2 ARG A  88     -24.742  25.761 -15.952  1.00  0.00           H  
ATOM   1213  HG3 ARG A  88     -23.744  24.978 -13.713  1.00  0.00           H  
ATOM   1214  HG2 ARG A  88     -23.872  26.622 -13.166  1.00  0.00           H  
ATOM   1215  HD3 ARG A  88     -22.289  25.969 -15.636  1.00  0.00           H  
ATOM   1216  HD2 ARG A  88     -21.528  25.910 -14.073  1.00  0.00           H  
ATOM   1217  HE  ARG A  88     -22.265  28.155 -15.763  1.00  0.00           H  
ATOM   1218 HH12 ARG A  88     -21.622  29.066 -11.853  1.00  0.00           H  
ATOM   1219 HH11 ARG A  88     -21.956  27.407 -12.290  1.00  0.00           H  
ATOM   1220 HH22 ARG A  88     -21.735  30.701 -13.423  1.00  0.00           H  
ATOM   1221 HH21 ARG A  88     -21.916  30.322 -15.135  1.00  0.00           H  
ATOM   1222  N   TYR A  89     -26.682  27.979 -13.031  1.00 76.64           N  
ANISOU 1222  N   TYR A  89     9684  10364   9073  -2108    956  -1069
ATOM   1223  CA  TYR A  89     -26.653  28.753 -11.793  1.00 76.47           C  
ANISOU 1223  CA  TYR A  89     9513  10336   9207  -1958    955  -1080
ATOM   1224  C   TYR A  89     -28.007  28.828 -11.065  1.00 76.99           C  
ANISOU 1224  C   TYR A  89     9410  10510   9333  -2007    942  -1145
ATOM   1225  O   TYR A  89     -27.995  28.935  -9.839  1.00 76.65           O  
ANISOU 1225  O   TYR A  89     9340  10441   9341  -1959   1038  -1204
ATOM   1226  CB  TYR A  89     -26.093  30.147 -12.119  1.00 77.40           C  
ANISOU 1226  CB  TYR A  89     9543  10439   9427  -1831    834   -998
ATOM   1227  CG  TYR A  89     -25.695  31.001 -10.937  1.00 76.86           C  
ANISOU 1227  CG  TYR A  89     9414  10304   9485  -1677    871  -1012
ATOM   1228  CD1 TYR A  89     -26.363  32.213 -10.682  1.00 76.67           C  
ANISOU 1228  CD1 TYR A  89     9232  10293   9607  -1573    788  -1014
ATOM   1229  CD2 TYR A  89     -24.614  30.609 -10.123  1.00 76.65           C  
ANISOU 1229  CD2 TYR A  89     9492  10197   9436  -1634    979  -1023
ATOM   1230  CE1 TYR A  89     -25.923  33.057  -9.647  1.00 76.38           C  
ANISOU 1230  CE1 TYR A  89     9178  10180   9662  -1460    834  -1044
ATOM   1231  CE2 TYR A  89     -24.196  31.435  -9.066  1.00 76.23           C  
ANISOU 1231  CE2 TYR A  89     9399  10095   9470  -1532    995  -1034
ATOM   1232  CZ  TYR A  89     -24.838  32.668  -8.841  1.00 76.20           C  
ANISOU 1232  CZ  TYR A  89     9275  10095   9582  -1460    930  -1050
ATOM   1233  OH  TYR A  89     -24.421  33.478  -7.831  1.00 76.09           O  
ANISOU 1233  OH  TYR A  89     9260  10021   9630  -1389    958  -1077
ATOM   1234  H   TYR A  89     -26.648  28.522 -13.884  1.00  0.00           H  
ATOM   1235  HA  TYR A  89     -25.949  28.267 -11.117  1.00  0.00           H  
ATOM   1236  HB3 TYR A  89     -26.791  30.696 -12.753  1.00  0.00           H  
ATOM   1237  HB2 TYR A  89     -25.177  30.030 -12.700  1.00  0.00           H  
ATOM   1238  HD1 TYR A  89     -27.195  32.513 -11.301  1.00  0.00           H  
ATOM   1239  HD2 TYR A  89     -24.094  29.681 -10.312  1.00  0.00           H  
ATOM   1240  HE1 TYR A  89     -26.423  33.999  -9.478  1.00  0.00           H  
ATOM   1241  HE2 TYR A  89     -23.375  31.121  -8.441  1.00  0.00           H  
ATOM   1242  HH  TYR A  89     -23.827  33.031  -7.214  1.00  0.00           H  
ATOM   1243  N   PHE A  90     -29.133  28.741 -11.803  1.00 75.94           N  
ANISOU 1243  N   PHE A  90     9154  10511   9190  -2114    825  -1136
ATOM   1244  CA  PHE A  90     -30.493  28.678 -11.253  1.00 76.82           C  
ANISOU 1244  CA  PHE A  90     9040  10767   9380  -2166    814  -1206
ATOM   1245  C   PHE A  90     -30.681  27.505 -10.270  1.00 77.14           C  
ANISOU 1245  C   PHE A  90     9173  10802   9335  -2303    997  -1310
ATOM   1246  O   PHE A  90     -30.975  27.801  -9.117  1.00 77.31           O  
ANISOU 1246  O   PHE A  90     9072  10857   9446  -2256   1081  -1382
ATOM   1247  CB  PHE A  90     -31.567  28.728 -12.375  1.00 84.53           C  
ANISOU 1247  CB  PHE A  90     9882  11912  10325  -2307    642  -1168
ATOM   1248  CG  PHE A  90     -33.035  28.744 -11.945  1.00 85.70           C  
ANISOU 1248  CG  PHE A  90     9713  12250  10598  -2337    614  -1238
ATOM   1249  CD1 PHE A  90     -33.786  29.932 -12.075  1.00 86.26           C  
ANISOU 1249  CD1 PHE A  90     9492  12409  10873  -2166    445  -1192
ATOM   1250  CD2 PHE A  90     -33.662  27.615 -11.368  1.00 86.54           C  
ANISOU 1250  CD2 PHE A  90     9810  12443  10630  -2533    766  -1354
ATOM   1251  CE1 PHE A  90     -35.103  29.986 -11.638  1.00 87.84           C  
ANISOU 1251  CE1 PHE A  90     9345  12804  11224  -2169    439  -1276
ATOM   1252  CE2 PHE A  90     -34.971  27.696 -10.910  1.00 87.95           C  
ANISOU 1252  CE2 PHE A  90     9660  12824  10931  -2575    775  -1439
ATOM   1253  CZ  PHE A  90     -35.688  28.877 -11.044  1.00 88.72           C  
ANISOU 1253  CZ  PHE A  90     9422  13033  11255  -2383    615  -1406
ATOM   1254  H   PHE A  90     -29.064  28.677 -12.811  1.00  0.00           H  
ATOM   1255  HA  PHE A  90     -30.621  29.595 -10.674  1.00  0.00           H  
ATOM   1256  HB3 PHE A  90     -31.429  27.918 -13.088  1.00  0.00           H  
ATOM   1257  HB2 PHE A  90     -31.401  29.640 -12.949  1.00  0.00           H  
ATOM   1258  HD1 PHE A  90     -33.337  30.811 -12.508  1.00  0.00           H  
ATOM   1259  HD2 PHE A  90     -33.131  26.681 -11.266  1.00  0.00           H  
ATOM   1260  HE1 PHE A  90     -35.664  30.904 -11.739  1.00  0.00           H  
ATOM   1261  HE2 PHE A  90     -35.435  26.834 -10.454  1.00  0.00           H  
ATOM   1262  HZ  PHE A  90     -36.706  28.932 -10.688  1.00  0.00           H  
ATOM   1263  N   PRO A  91     -30.488  26.225 -10.689  1.00 77.71           N  
ANISOU 1263  N   PRO A  91     9478  10823   9227  -2488   1070  -1327
ATOM   1264  CA  PRO A  91     -30.662  25.078  -9.776  1.00 77.50           C  
ANISOU 1264  CA  PRO A  91     9570  10766   9111  -2635   1229  -1412
ATOM   1265  C   PRO A  91     -29.635  25.024  -8.635  1.00 76.60           C  
ANISOU 1265  C   PRO A  91     9588  10495   9023  -2493   1340  -1412
ATOM   1266  O   PRO A  91     -30.001  24.611  -7.537  1.00 76.64           O  
ANISOU 1266  O   PRO A  91     9591  10515   9013  -2563   1440  -1473
ATOM   1267  CB  PRO A  91     -30.564  23.845 -10.689  1.00 80.46           C  
ANISOU 1267  CB  PRO A  91    10208  11069   9295  -2836   1263  -1419
ATOM   1268  CG  PRO A  91     -29.709  24.308 -11.856  1.00 79.73           C  
ANISOU 1268  CG  PRO A  91    10207  10895   9191  -2718   1190  -1343
ATOM   1269  CD  PRO A  91     -30.157  25.753 -12.037  1.00 79.63           C  
ANISOU 1269  CD  PRO A  91     9918  11013   9325  -2585   1027  -1281
ATOM   1270  HA  PRO A  91     -31.659  25.110  -9.333  1.00  0.00           H  
ATOM   1271  HB3 PRO A  91     -31.560  23.582 -11.047  1.00  0.00           H  
ATOM   1272  HB2 PRO A  91     -30.152  22.962 -10.199  1.00  0.00           H  
ATOM   1273  HG3 PRO A  91     -29.834  23.701 -12.753  1.00  0.00           H  
ATOM   1274  HG2 PRO A  91     -28.657  24.276 -11.574  1.00  0.00           H  
ATOM   1275  HD2 PRO A  91     -29.389  26.333 -12.543  1.00  0.00           H  
ATOM   1276  HD3 PRO A  91     -31.059  25.775 -12.649  1.00  0.00           H  
ATOM   1277  N   THR A  92     -28.395  25.472  -8.904  1.00 74.50           N  
ANISOU 1277  N   THR A  92     9419  10097   8788  -2312   1315  -1340
ATOM   1278  CA  THR A  92     -27.304  25.570  -7.934  1.00 73.85           C  
ANISOU 1278  CA  THR A  92     9441   9883   8737  -2169   1373  -1315
ATOM   1279  C   THR A  92     -27.672  26.485  -6.750  1.00 73.77           C  
ANISOU 1279  C   THR A  92     9264   9937   8827  -2099   1380  -1351
ATOM   1280  O   THR A  92     -27.670  26.013  -5.613  1.00 74.06           O  
ANISOU 1280  O   THR A  92     9388   9941   8811  -2157   1469  -1388
ATOM   1281  CB  THR A  92     -26.005  26.100  -8.604  1.00 89.30           C  
ANISOU 1281  CB  THR A  92    11445  11755  10730  -2012   1327  -1240
ATOM   1282  OG1 THR A  92     -25.518  25.123  -9.502  1.00 89.81           O  
ANISOU 1282  OG1 THR A  92    11698  11739  10689  -2080   1376  -1239
ATOM   1283  CG2 THR A  92     -24.857  26.479  -7.653  1.00 88.73           C  
ANISOU 1283  CG2 THR A  92    11410  11590  10714  -1859   1345  -1201
ATOM   1284  H   THR A  92     -28.185  25.801  -9.836  1.00  0.00           H  
ATOM   1285  HA  THR A  92     -27.115  24.568  -7.542  1.00  0.00           H  
ATOM   1286  HB  THR A  92     -26.243  26.978  -9.203  1.00  0.00           H  
ATOM   1287  HG1 THR A  92     -26.085  25.105 -10.279  1.00  0.00           H  
ATOM   1288 HG21 THR A  92     -23.927  26.649  -8.197  1.00  0.00           H  
ATOM   1289 HG22 THR A  92     -25.069  27.391  -7.095  1.00  0.00           H  
ATOM   1290 HG23 THR A  92     -24.687  25.681  -6.934  1.00  0.00           H  
ATOM   1291  N   GLN A  93     -28.018  27.750  -7.045  1.00 73.59           N  
ANISOU 1291  N   GLN A  93     9034   9990   8938  -1985   1292  -1343
ATOM   1292  CA  GLN A  93     -28.420  28.731  -6.041  1.00 73.65           C  
ANISOU 1292  CA  GLN A  93     8898  10032   9054  -1902   1320  -1400
ATOM   1293  C   GLN A  93     -29.806  28.474  -5.440  1.00 74.73           C  
ANISOU 1293  C   GLN A  93     8894  10305   9197  -2030   1407  -1513
ATOM   1294  O   GLN A  93     -29.967  28.683  -4.242  1.00 75.15           O  
ANISOU 1294  O   GLN A  93     8936  10363   9256  -2041   1516  -1593
ATOM   1295  CB  GLN A  93     -28.314  30.156  -6.606  1.00 77.42           C  
ANISOU 1295  CB  GLN A  93     9226  10509   9682  -1732   1204  -1360
ATOM   1296  CG  GLN A  93     -26.882  30.676  -6.841  1.00 76.68           C  
ANISOU 1296  CG  GLN A  93     9263  10289   9583  -1626   1157  -1272
ATOM   1297  CD  GLN A  93     -26.054  30.846  -5.561  1.00 76.70           C  
ANISOU 1297  CD  GLN A  93     9366  10219   9559  -1603   1235  -1296
ATOM   1298  OE1 GLN A  93     -25.577  29.873  -4.985  1.00 76.84           O  
ANISOU 1298  OE1 GLN A  93     9536  10191   9470  -1662   1288  -1279
ATOM   1299  NE2 GLN A  93     -25.855  32.090  -5.125  1.00 76.66           N  
ANISOU 1299  NE2 GLN A  93     9295  10189   9643  -1520   1232  -1335
ATOM   1300  H   GLN A  93     -28.018  28.066  -8.006  1.00  0.00           H  
ATOM   1301  HA  GLN A  93     -27.720  28.641  -5.219  1.00  0.00           H  
ATOM   1302  HB3 GLN A  93     -28.833  30.856  -5.949  1.00  0.00           H  
ATOM   1303  HB2 GLN A  93     -28.856  30.177  -7.551  1.00  0.00           H  
ATOM   1304  HG3 GLN A  93     -26.945  31.635  -7.354  1.00  0.00           H  
ATOM   1305  HG2 GLN A  93     -26.348  30.006  -7.515  1.00  0.00           H  
ATOM   1306 HE22 GLN A  93     -25.294  32.260  -4.303  1.00  0.00           H  
ATOM   1307 HE21 GLN A  93     -26.231  32.877  -5.633  1.00  0.00           H  
ATOM   1308  N   ALA A  94     -30.767  27.983  -6.239  1.00 68.26           N  
ANISOU 1308  N   ALA A  94     7974   9607   8353  -2161   1373  -1529
ATOM   1309  CA  ALA A  94     -32.098  27.593  -5.767  1.00 69.41           C  
ANISOU 1309  CA  ALA A  94     7951   9919   8502  -2321   1470  -1646
ATOM   1310  C   ALA A  94     -32.041  26.535  -4.654  1.00 69.76           C  
ANISOU 1310  C   ALA A  94     8221   9907   8378  -2502   1635  -1698
ATOM   1311  O   ALA A  94     -32.671  26.734  -3.616  1.00 70.36           O  
ANISOU 1311  O   ALA A  94     8230  10037   8466  -2542   1764  -1796
ATOM   1312  CB  ALA A  94     -32.951  27.105  -6.942  1.00 71.81           C  
ANISOU 1312  CB  ALA A  94     8130  10371   8782  -2469   1380  -1637
ATOM   1313  H   ALA A  94     -30.582  27.837  -7.224  1.00  0.00           H  
ATOM   1314  HA  ALA A  94     -32.574  28.484  -5.354  1.00  0.00           H  
ATOM   1315  HB1 ALA A  94     -33.943  26.810  -6.612  1.00  0.00           H  
ATOM   1316  HB2 ALA A  94     -33.093  27.889  -7.683  1.00  0.00           H  
ATOM   1317  HB3 ALA A  94     -32.501  26.246  -7.439  1.00  0.00           H  
ATOM   1318  N   LEU A  95     -31.216  25.490  -4.850  1.00 64.90           N  
ANISOU 1318  N   LEU A  95     7899   9154   7605  -2595   1635  -1628
ATOM   1319  CA  LEU A  95     -30.912  24.497  -3.821  1.00 65.31           C  
ANISOU 1319  CA  LEU A  95     8220   9101   7493  -2747   1756  -1640
ATOM   1320  C   LEU A  95     -30.188  25.112  -2.610  1.00 64.63           C  
ANISOU 1320  C   LEU A  95     8208   8928   7420  -2626   1791  -1629
ATOM   1321  O   LEU A  95     -30.620  24.844  -1.494  1.00 65.58           O  
ANISOU 1321  O   LEU A  95     8421   9058   7437  -2773   1907  -1686
ATOM   1322  CB  LEU A  95     -30.102  23.316  -4.407  1.00 65.19           C  
ANISOU 1322  CB  LEU A  95     8515   8902   7351  -2789   1730  -1555
ATOM   1323  CG  LEU A  95     -30.875  22.356  -5.336  1.00 66.25           C  
ANISOU 1323  CG  LEU A  95     8705   9079   7388  -3003   1734  -1582
ATOM   1324  CD1 LEU A  95     -29.907  21.396  -6.061  1.00 66.32           C  
ANISOU 1324  CD1 LEU A  95     9071   8849   7279  -3014   1747  -1519
ATOM   1325  CD2 LEU A  95     -32.011  21.602  -4.604  1.00 67.61           C  
ANISOU 1325  CD2 LEU A  95     8841   9384   7464  -3295   1847  -1680
ATOM   1326  H   LEU A  95     -30.717  25.398  -5.725  1.00  0.00           H  
ATOM   1327  HA  LEU A  95     -31.867  24.121  -3.453  1.00  0.00           H  
ATOM   1328  HB3 LEU A  95     -29.707  22.709  -3.593  1.00  0.00           H  
ATOM   1329  HB2 LEU A  95     -29.233  23.718  -4.931  1.00  0.00           H  
ATOM   1330  HG  LEU A  95     -31.340  22.966  -6.107  1.00  0.00           H  
ATOM   1331 HD11 LEU A  95     -29.988  21.514  -7.142  1.00  0.00           H  
ATOM   1332 HD12 LEU A  95     -28.865  21.583  -5.799  1.00  0.00           H  
ATOM   1333 HD13 LEU A  95     -30.106  20.349  -5.838  1.00  0.00           H  
ATOM   1334 HD21 LEU A  95     -31.856  20.524  -4.577  1.00  0.00           H  
ATOM   1335 HD22 LEU A  95     -32.123  21.924  -3.570  1.00  0.00           H  
ATOM   1336 HD23 LEU A  95     -32.971  21.766  -5.090  1.00  0.00           H  
ATOM   1337  N   ASN A  96     -29.144  25.935  -2.830  1.00 64.96           N  
ANISOU 1337  N   ASN A  96     8222   8893   7566  -2393   1692  -1559
ATOM   1338  CA  ASN A  96     -28.333  26.558  -1.770  1.00 64.67           C  
ANISOU 1338  CA  ASN A  96     8261   8781   7529  -2299   1701  -1543
ATOM   1339  C   ASN A  96     -29.145  27.421  -0.791  1.00 65.45           C  
ANISOU 1339  C   ASN A  96     8207   8993   7667  -2345   1812  -1676
ATOM   1340  O   ASN A  96     -28.966  27.268   0.415  1.00 65.88           O  
ANISOU 1340  O   ASN A  96     8413   9013   7607  -2440   1891  -1703
ATOM   1341  CB  ASN A  96     -27.214  27.416  -2.399  1.00 66.44           C  
ANISOU 1341  CB  ASN A  96     8438   8936   7868  -2074   1577  -1458
ATOM   1342  CG  ASN A  96     -25.965  26.668  -2.846  1.00 65.78           C  
ANISOU 1342  CG  ASN A  96     8546   8714   7732  -2006   1510  -1339
ATOM   1343  OD1 ASN A  96     -25.568  25.687  -2.229  1.00 66.07           O  
ANISOU 1343  OD1 ASN A  96     8798   8655   7651  -2080   1535  -1297
ATOM   1344  ND2 ASN A  96     -25.288  27.177  -3.872  1.00 65.09           N  
ANISOU 1344  ND2 ASN A  96     8382   8609   7741  -1857   1424  -1281
ATOM   1345  H   ASN A  96     -28.842  26.108  -3.780  1.00  0.00           H  
ATOM   1346  HA  ASN A  96     -27.899  25.715  -1.229  1.00  0.00           H  
ATOM   1347  HB3 ASN A  96     -26.820  28.082  -1.649  1.00  0.00           H  
ATOM   1348  HB2 ASN A  96     -27.604  28.061  -3.180  1.00  0.00           H  
ATOM   1349 HD22 ASN A  96     -24.422  26.728  -4.152  1.00  0.00           H  
ATOM   1350 HD21 ASN A  96     -25.586  28.025  -4.337  1.00  0.00           H  
ATOM   1351  N   PHE A  97     -30.010  28.304  -1.314  1.00 68.86           N  
ANISOU 1351  N   PHE A  97     8349   9555   8261  -2273   1816  -1759
ATOM   1352  CA  PHE A  97     -30.866  29.178  -0.512  1.00 69.88           C  
ANISOU 1352  CA  PHE A  97     8303   9776   8472  -2263   1942  -1908
ATOM   1353  C   PHE A  97     -31.990  28.434   0.227  1.00 71.36           C  
ANISOU 1353  C   PHE A  97     8465  10097   8551  -2514   2129  -2037
ATOM   1354  O   PHE A  97     -32.233  28.741   1.395  1.00 72.07           O  
ANISOU 1354  O   PHE A  97     8625  10197   8562  -2606   2281  -2140
ATOM   1355  CB  PHE A  97     -31.404  30.336  -1.375  1.00 73.79           C  
ANISOU 1355  CB  PHE A  97     8490  10338   9208  -2061   1869  -1942
ATOM   1356  CG  PHE A  97     -30.434  31.495  -1.542  1.00 72.68           C  
ANISOU 1356  CG  PHE A  97     8406  10051   9160  -1845   1751  -1864
ATOM   1357  CD1 PHE A  97     -30.414  32.535  -0.591  1.00 72.87           C  
ANISOU 1357  CD1 PHE A  97     8436  10013   9237  -1764   1831  -1956
ATOM   1358  CD2 PHE A  97     -29.434  31.477  -2.536  1.00 71.64           C  
ANISOU 1358  CD2 PHE A  97     8348   9838   9035  -1756   1579  -1710
ATOM   1359  CE1 PHE A  97     -29.502  33.577  -0.709  1.00 71.92           C  
ANISOU 1359  CE1 PHE A  97     8394   9752   9182  -1607   1722  -1884
ATOM   1360  CE2 PHE A  97     -28.513  32.507  -2.622  1.00 70.76           C  
ANISOU 1360  CE2 PHE A  97     8296   9603   8988  -1602   1483  -1639
ATOM   1361  CZ  PHE A  97     -28.563  33.568  -1.732  1.00 70.93           C  
ANISOU 1361  CZ  PHE A  97     8322   9562   9065  -1533   1546  -1721
ATOM   1362  H   PHE A  97     -30.098  28.381  -2.320  1.00  0.00           H  
ATOM   1363  HA  PHE A  97     -30.243  29.621   0.269  1.00  0.00           H  
ATOM   1364  HB3 PHE A  97     -32.326  30.734  -0.946  1.00  0.00           H  
ATOM   1365  HB2 PHE A  97     -31.680  29.961  -2.361  1.00  0.00           H  
ATOM   1366  HD1 PHE A  97     -31.132  32.539   0.214  1.00  0.00           H  
ATOM   1367  HD2 PHE A  97     -29.366  30.674  -3.243  1.00  0.00           H  
ATOM   1368  HE1 PHE A  97     -29.517  34.391   0.000  1.00  0.00           H  
ATOM   1369  HE2 PHE A  97     -27.757  32.490  -3.390  1.00  0.00           H  
ATOM   1370  HZ  PHE A  97     -27.848  34.372  -1.822  1.00  0.00           H  
ATOM   1371  N   ALA A  98     -32.618  27.452  -0.446  1.00 76.96           N  
ANISOU 1371  N   ALA A  98     9101  10912   9230  -2660   2124  -2035
ATOM   1372  CA  ALA A  98     -33.657  26.598   0.131  1.00 78.80           C  
ANISOU 1372  CA  ALA A  98     9307  11291   9343  -2950   2302  -2153
ATOM   1373  C   ALA A  98     -33.131  25.686   1.244  1.00 78.99           C  
ANISOU 1373  C   ALA A  98     9713  11188   9112  -3152   2396  -2124
ATOM   1374  O   ALA A  98     -33.754  25.620   2.304  1.00 80.43           O  
ANISOU 1374  O   ALA A  98     9912  11449   9198  -3327   2586  -2251
ATOM   1375  CB  ALA A  98     -34.329  25.776  -0.974  1.00 79.28           C  
ANISOU 1375  CB  ALA A  98     9290  11451   9381  -3097   2236  -2120
ATOM   1376  H   ALA A  98     -32.362  27.256  -1.404  1.00  0.00           H  
ATOM   1377  HA  ALA A  98     -34.406  27.251   0.576  1.00  0.00           H  
ATOM   1378  HB1 ALA A  98     -35.189  25.228  -0.588  1.00  0.00           H  
ATOM   1379  HB2 ALA A  98     -34.691  26.427  -1.764  1.00  0.00           H  
ATOM   1380  HB3 ALA A  98     -33.643  25.059  -1.426  1.00  0.00           H  
ATOM   1381  N   PHE A  99     -31.978  25.036   1.000  1.00 84.95           N  
ANISOU 1381  N   PHE A  99    10772  11741   9765  -3109   2260  -1958
ATOM   1382  CA  PHE A  99     -31.282  24.224   1.992  1.00 85.07           C  
ANISOU 1382  CA  PHE A  99    11165  11604   9553  -3259   2290  -1887
ATOM   1383  C   PHE A  99     -30.714  25.024   3.166  1.00 84.95           C  
ANISOU 1383  C   PHE A  99    11219  11548   9509  -3192   2318  -1908
ATOM   1384  O   PHE A  99     -30.781  24.510   4.277  1.00 86.02           O  
ANISOU 1384  O   PHE A  99    11580  11664   9440  -3413   2420  -1930
ATOM   1385  CB  PHE A  99     -30.220  23.292   1.364  1.00 86.72           C  
ANISOU 1385  CB  PHE A  99    11646  11599   9707  -3179   2132  -1708
ATOM   1386  CG  PHE A  99     -30.782  22.011   0.772  1.00 87.50           C  
ANISOU 1386  CG  PHE A  99    11880  11671   9694  -3391   2163  -1697
ATOM   1387  CD1 PHE A  99     -30.695  21.741  -0.611  1.00 87.08           C  
ANISOU 1387  CD1 PHE A  99    11729  11624   9735  -3314   2080  -1672
ATOM   1388  CD2 PHE A  99     -31.431  21.080   1.610  1.00 88.88           C  
ANISOU 1388  CD2 PHE A  99    12322  11802   9645  -3697   2274  -1710
ATOM   1389  CE1 PHE A  99     -31.256  20.581  -1.127  1.00 87.96           C  
ANISOU 1389  CE1 PHE A  99    12000  11699   9723  -3540   2112  -1674
ATOM   1390  CE2 PHE A  99     -31.992  19.930   1.073  1.00 89.76           C  
ANISOU 1390  CE2 PHE A  99    12595  11868   9643  -3921   2306  -1704
ATOM   1391  CZ  PHE A  99     -31.909  19.684  -0.292  1.00 89.31           C  
ANISOU 1391  CZ  PHE A  99    12431  11817   9685  -3841   2227  -1694
ATOM   1392  H   PHE A  99     -31.526  25.129   0.098  1.00  0.00           H  
ATOM   1393  HA  PHE A  99     -32.041  23.582   2.439  1.00  0.00           H  
ATOM   1394  HB3 PHE A  99     -29.510  22.983   2.130  1.00  0.00           H  
ATOM   1395  HB2 PHE A  99     -29.627  23.825   0.622  1.00  0.00           H  
ATOM   1396  HD1 PHE A  99     -30.177  22.417  -1.271  1.00  0.00           H  
ATOM   1397  HD2 PHE A  99     -31.501  21.264   2.672  1.00  0.00           H  
ATOM   1398  HE1 PHE A  99     -31.170  20.362  -2.180  1.00  0.00           H  
ATOM   1399  HE2 PHE A  99     -32.491  19.222   1.717  1.00  0.00           H  
ATOM   1400  HZ  PHE A  99     -32.339  18.783  -0.704  1.00  0.00           H  
ATOM   1401  N   ARG A 100     -30.217  26.257   2.941  1.00 96.20           N  
ANISOU 1401  N   ARG A 100    12479  12960  11111  -2929   2233  -1905
ATOM   1402  CA  ARG A 100     -29.745  27.138   4.016  1.00 96.36           C  
ANISOU 1402  CA  ARG A 100    12583  12942  11086  -2900   2263  -1940
ATOM   1403  C   ARG A 100     -30.840  27.408   5.049  1.00 97.90           C  
ANISOU 1403  C   ARG A 100    12711  13276  11209  -3098   2509  -2146
ATOM   1404  O   ARG A 100     -30.624  27.096   6.214  1.00 98.73           O  
ANISOU 1404  O   ARG A 100    13064  13344  11103  -3277   2582  -2163
ATOM   1405  CB  ARG A 100     -29.164  28.455   3.466  1.00103.79           C  
ANISOU 1405  CB  ARG A 100    13356  13848  12231  -2621   2156  -1929
ATOM   1406  CG  ARG A 100     -28.840  29.510   4.557  1.00104.29           C  
ANISOU 1406  CG  ARG A 100    13479  13902  12246  -2646   2245  -2033
ATOM   1407  CD  ARG A 100     -28.355  30.830   3.975  1.00103.41           C  
ANISOU 1407  CD  ARG A 100    13243  13732  12315  -2410   2155  -2035
ATOM   1408  NE  ARG A 100     -29.407  31.573   3.276  1.00103.42           N  
ANISOU 1408  NE  ARG A 100    12931  13804  12559  -2247   2204  -2142
ATOM   1409  CZ  ARG A 100     -30.191  32.518   3.815  1.00104.21           C  
ANISOU 1409  CZ  ARG A 100    12888  13947  12762  -2208   2367  -2333
ATOM   1410  NH1 ARG A 100     -30.044  32.923   5.080  1.00105.25           N  
ANISOU 1410  NH1 ARG A 100    13176  14071  12744  -2360   2530  -2461
ATOM   1411  NH2 ARG A 100     -31.136  33.084   3.063  1.00104.12           N1+
ANISOU 1411  NH2 ARG A 100    12580  13980  13000  -2018   2369  -2400
ATOM   1412  H   ARG A 100     -30.178  26.627   2.001  1.00  0.00           H  
ATOM   1413  HA  ARG A 100     -28.934  26.612   4.523  1.00  0.00           H  
ATOM   1414  HB3 ARG A 100     -29.868  28.888   2.755  1.00  0.00           H  
ATOM   1415  HB2 ARG A 100     -28.260  28.229   2.898  1.00  0.00           H  
ATOM   1416  HG3 ARG A 100     -28.150  29.138   5.315  1.00  0.00           H  
ATOM   1417  HG2 ARG A 100     -29.762  29.760   5.083  1.00  0.00           H  
ATOM   1418  HD3 ARG A 100     -27.729  30.518   3.152  1.00  0.00           H  
ATOM   1419  HD2 ARG A 100     -27.730  31.424   4.639  1.00  0.00           H  
ATOM   1420  HE  ARG A 100     -29.590  31.283   2.326  1.00  0.00           H  
ATOM   1421 HH12 ARG A 100     -30.650  33.634   5.456  1.00  0.00           H  
ATOM   1422 HH11 ARG A 100     -29.231  32.629   5.613  1.00  0.00           H  
ATOM   1423 HH22 ARG A 100     -31.291  32.773   2.116  1.00  0.00           H  
ATOM   1424 HH21 ARG A 100     -31.729  33.800   3.452  1.00  0.00           H  
ATOM   1425  N   ASP A 101     -31.976  27.962   4.598  1.00102.85           N  
ANISOU 1425  N   ASP A 101    12996  14072  12009  -3069   2636  -2306
ATOM   1426  CA  ASP A 101     -33.135  28.266   5.442  1.00104.83           C  
ANISOU 1426  CA  ASP A 101    13111  14485  12233  -3236   2911  -2538
ATOM   1427  C   ASP A 101     -33.779  27.022   6.078  1.00106.47           C  
ANISOU 1427  C   ASP A 101    13528  14757  12168  -3617   3059  -2563
ATOM   1428  O   ASP A 101     -34.293  27.141   7.190  1.00108.07           O  
ANISOU 1428  O   ASP A 101    13823  15026  12212  -3834   3278  -2707
ATOM   1429  CB  ASP A 101     -34.175  29.160   4.732  1.00110.74           C  
ANISOU 1429  CB  ASP A 101    13397  15406  13272  -3077   2980  -2682
ATOM   1430  CG  ASP A 101     -33.632  30.531   4.301  1.00110.96           C  
ANISOU 1430  CG  ASP A 101    13252  15348  13559  -2720   2865  -2680
ATOM   1431  OD1 ASP A 101     -32.751  31.068   5.009  1.00111.10           O  
ANISOU 1431  OD1 ASP A 101    13433  15244  13535  -2660   2890  -2709
ATOM   1432  OD2 ASP A 101     -34.179  31.088   3.328  1.00111.23           O1-
ANISOU 1432  OD2 ASP A 101    13014  15430  13819  -2526   2740  -2642
ATOM   1433  H   ASP A 101     -32.070  28.187   3.617  1.00  0.00           H  
ATOM   1434  HA  ASP A 101     -32.746  28.842   6.283  1.00  0.00           H  
ATOM   1435  HB3 ASP A 101     -35.050  29.316   5.363  1.00  0.00           H  
ATOM   1436  HB2 ASP A 101     -34.507  28.635   3.835  1.00  0.00           H  
ATOM   1437  N   LYS A 102     -33.671  25.851   5.419  1.00101.85           N  
ANISOU 1437  N   LYS A 102    13059  14133  11506  -3718   2946  -2423
ATOM   1438  CA  LYS A 102     -34.006  24.558   6.013  1.00102.67           C  
ANISOU 1438  CA  LYS A 102    13420  14253  11336  -4096   3064  -2421
ATOM   1439  C   LYS A 102     -33.066  24.221   7.180  1.00102.57           C  
ANISOU 1439  C   LYS A 102    13859  14060  11055  -4221   3025  -2311
ATOM   1440  O   LYS A 102     -33.558  24.151   8.301  1.00103.84           O  
ANISOU 1440  O   LYS A 102    14146  14293  11017  -4493   3225  -2427
ATOM   1441  CB  LYS A 102     -34.059  23.437   4.955  1.00105.95           C  
ANISOU 1441  CB  LYS A 102    13903  14622  11731  -4168   2944  -2298
ATOM   1442  CG  LYS A 102     -34.476  22.070   5.534  1.00106.06           C  
ANISOU 1442  CG  LYS A 102    14212  14633  11454  -4591   3076  -2301
ATOM   1443  CD  LYS A 102     -34.470  20.942   4.499  1.00106.07           C  
ANISOU 1443  CD  LYS A 102    14381  14511  11410  -4652   2942  -2166
ATOM   1444  CE  LYS A 102     -34.813  19.589   5.139  1.00106.21           C  
ANISOU 1444  CE  LYS A 102    14789  14449  11117  -5073   3043  -2133
ATOM   1445  NZ  LYS A 102     -34.762  18.500   4.152  1.00106.22           N1+
ANISOU 1445  NZ  LYS A 102    14968  14308  11082  -5140   2931  -2027
ATOM   1446  H   LYS A 102     -33.257  25.832   4.497  1.00  0.00           H  
ATOM   1447  HA  LYS A 102     -35.015  24.651   6.423  1.00  0.00           H  
ATOM   1448  HB3 LYS A 102     -33.089  23.337   4.472  1.00  0.00           H  
ATOM   1449  HB2 LYS A 102     -34.760  23.722   4.171  1.00  0.00           H  
ATOM   1450  HG3 LYS A 102     -35.469  22.155   5.975  1.00  0.00           H  
ATOM   1451  HG2 LYS A 102     -33.808  21.781   6.346  1.00  0.00           H  
ATOM   1452  HD3 LYS A 102     -33.489  20.888   4.025  1.00  0.00           H  
ATOM   1453  HD2 LYS A 102     -35.184  21.169   3.707  1.00  0.00           H  
ATOM   1454  HE3 LYS A 102     -35.811  19.622   5.580  1.00  0.00           H  
ATOM   1455  HE2 LYS A 102     -34.113  19.362   5.944  1.00  0.00           H  
ATOM   1456  HZ1 LYS A 102     -34.997  17.626   4.601  1.00  0.00           H  
ATOM   1457  HZ2 LYS A 102     -35.423  18.683   3.410  1.00  0.00           H  
ATOM   1458  HZ3 LYS A 102     -33.831  18.438   3.765  1.00  0.00           H  
ATOM   1459  N   PHE A 103     -31.754  24.052   6.912  1.00102.51           N  
ANISOU 1459  N   PHE A 103    14069  13834  11044  -4026   2772  -2096
ATOM   1460  CA  PHE A 103     -30.714  23.758   7.909  1.00102.21           C  
ANISOU 1460  CA  PHE A 103    14437  13627  10772  -4114   2673  -1955
ATOM   1461  C   PHE A 103     -30.676  24.748   9.087  1.00102.45           C  
ANISOU 1461  C   PHE A 103    14471  13732  10725  -4177   2795  -2087
ATOM   1462  O   PHE A 103     -30.523  24.318  10.224  1.00103.24           O  
ANISOU 1462  O   PHE A 103    14900  13791  10536  -4446   2844  -2064
ATOM   1463  CB  PHE A 103     -29.314  23.627   7.256  1.00105.28           C  
ANISOU 1463  CB  PHE A 103    14934  13815  11254  -3823   2379  -1727
ATOM   1464  CG  PHE A 103     -29.048  22.334   6.496  1.00105.27           C  
ANISOU 1464  CG  PHE A 103    15095  13666  11239  -3815   2265  -1577
ATOM   1465  CD1 PHE A 103     -29.061  21.096   7.173  1.00105.31           C  
ANISOU 1465  CD1 PHE A 103    15519  13487  11006  -3991   2195  -1425
ATOM   1466  CD2 PHE A 103     -28.784  22.346   5.109  1.00105.30           C  
ANISOU 1466  CD2 PHE A 103    14863  13692  11457  -3630   2222  -1583
ATOM   1467  CE1 PHE A 103     -28.838  19.917   6.473  1.00105.29           C  
ANISOU 1467  CE1 PHE A 103    15695  13307  11003  -3965   2106  -1301
ATOM   1468  CE2 PHE A 103     -28.589  21.156   4.423  1.00105.23           C  
ANISOU 1468  CE2 PHE A 103    15034  13527  11422  -3632   2141  -1469
ATOM   1469  CZ  PHE A 103     -28.616  19.946   5.102  1.00105.31           C  
ANISOU 1469  CZ  PHE A 103    15459  13336  11217  -3787   2092  -1337
ATOM   1470  H   PHE A 103     -31.429  24.159   5.959  1.00  0.00           H  
ATOM   1471  HA  PHE A 103     -30.963  22.792   8.345  1.00  0.00           H  
ATOM   1472  HB3 PHE A 103     -28.547  23.687   8.030  1.00  0.00           H  
ATOM   1473  HB2 PHE A 103     -29.133  24.478   6.597  1.00  0.00           H  
ATOM   1474  HD1 PHE A 103     -29.247  21.059   8.237  1.00  0.00           H  
ATOM   1475  HD2 PHE A 103     -28.709  23.279   4.574  1.00  0.00           H  
ATOM   1476  HE1 PHE A 103     -28.849  18.972   6.995  1.00  0.00           H  
ATOM   1477  HE2 PHE A 103     -28.391  21.171   3.361  1.00  0.00           H  
ATOM   1478  HZ  PHE A 103     -28.450  19.025   4.562  1.00  0.00           H  
ATOM   1479  N   LYS A 104     -30.884  26.041   8.804  1.00103.65           N  
ANISOU 1479  N   LYS A 104    14287  13979  11117  -3948   2852  -2231
ATOM   1480  CA  LYS A 104     -30.950  27.126   9.783  1.00104.22           C  
ANISOU 1480  CA  LYS A 104    14345  14108  11147  -3988   3006  -2403
ATOM   1481  C   LYS A 104     -32.156  26.999  10.733  1.00105.37           C  
ANISOU 1481  C   LYS A 104    14522  14412  11100  -4342   3336  -2621
ATOM   1482  O   LYS A 104     -32.031  27.378  11.896  1.00105.78           O  
ANISOU 1482  O   LYS A 104    14816  14461  10916  -4555   3450  -2694
ATOM   1483  CB  LYS A 104     -30.936  28.453   9.004  1.00102.28           C  
ANISOU 1483  CB  LYS A 104    13721  13907  11233  -3662   3020  -2526
ATOM   1484  CG  LYS A 104     -30.658  29.716   9.826  1.00102.38           C  
ANISOU 1484  CG  LYS A 104    13810  13863  11227  -3602   3047  -2611
ATOM   1485  CD  LYS A 104     -30.601  30.952   8.914  1.00102.39           C  
ANISOU 1485  CD  LYS A 104    13483  13851  11570  -3256   3015  -2686
ATOM   1486  CE  LYS A 104     -29.965  32.163   9.598  1.00102.36           C  
ANISOU 1486  CE  LYS A 104    13607  13729  11554  -3171   2959  -2708
ATOM   1487  NZ  LYS A 104     -29.972  33.337   8.715  1.00102.43           N1+
ANISOU 1487  NZ  LYS A 104    13346  13685  11886  -2844   2909  -2757
ATOM   1488  H   LYS A 104     -30.993  26.320   7.836  1.00  0.00           H  
ATOM   1489  HA  LYS A 104     -30.051  27.078  10.399  1.00  0.00           H  
ATOM   1490  HB3 LYS A 104     -31.863  28.565   8.440  1.00  0.00           H  
ATOM   1491  HB2 LYS A 104     -30.132  28.398   8.272  1.00  0.00           H  
ATOM   1492  HG3 LYS A 104     -29.708  29.598  10.350  1.00  0.00           H  
ATOM   1493  HG2 LYS A 104     -31.422  29.855  10.591  1.00  0.00           H  
ATOM   1494  HD3 LYS A 104     -31.615  31.203   8.596  1.00  0.00           H  
ATOM   1495  HD2 LYS A 104     -30.049  30.721   8.002  1.00  0.00           H  
ATOM   1496  HE3 LYS A 104     -28.932  31.940   9.853  1.00  0.00           H  
ATOM   1497  HE2 LYS A 104     -30.492  32.405  10.521  1.00  0.00           H  
ATOM   1498  HZ1 LYS A 104     -29.577  34.126   9.205  1.00  0.00           H  
ATOM   1499  HZ2 LYS A 104     -29.408  33.143   7.896  1.00  0.00           H  
ATOM   1500  HZ3 LYS A 104     -30.920  33.549   8.438  1.00  0.00           H  
ATOM   1501  N   ALA A 105     -33.265  26.418  10.241  1.00113.93           N  
ANISOU 1501  N   ALA A 105    15366  15652  12271  -4434   3491  -2726
ATOM   1502  CA  ALA A 105     -34.429  26.033  11.036  1.00117.27           C  
ANISOU 1502  CA  ALA A 105    15773  16261  12522  -4799   3825  -2939
ATOM   1503  C   ALA A 105     -34.251  24.686  11.767  1.00118.75           C  
ANISOU 1503  C   ALA A 105    16443  16360  12315  -5191   3807  -2797
ATOM   1504  O   ALA A 105     -34.851  24.532  12.831  1.00121.69           O  
ANISOU 1504  O   ALA A 105    16980  16827  12430  -5542   4060  -2941
ATOM   1505  CB  ALA A 105     -35.680  26.014  10.143  1.00119.48           C  
ANISOU 1505  CB  ALA A 105    15614  16751  13029  -4778   3954  -3072
ATOM   1506  H   ALA A 105     -33.286  26.137   9.270  1.00  0.00           H  
ATOM   1507  HA  ALA A 105     -34.588  26.798  11.799  1.00  0.00           H  
ATOM   1508  HB1 ALA A 105     -36.575  25.801  10.727  1.00  0.00           H  
ATOM   1509  HB2 ALA A 105     -35.829  26.981   9.660  1.00  0.00           H  
ATOM   1510  HB3 ALA A 105     -35.614  25.261   9.359  1.00  0.00           H  
ATOM   1511  N   MET A 106     -33.430  23.754  11.230  1.00122.42           N  
ANISOU 1511  N   MET A 106    17156  16630  12728  -5134   3519  -2521
ATOM   1512  CA  MET A 106     -33.076  22.486  11.893  1.00124.03           C  
ANISOU 1512  CA  MET A 106    17865  16684  12575  -5461   3450  -2344
ATOM   1513  C   MET A 106     -32.260  22.728  13.175  1.00124.95           C  
ANISOU 1513  C   MET A 106    18343  16705  12429  -5580   3398  -2282
ATOM   1514  O   MET A 106     -32.570  22.128  14.203  1.00127.91           O  
ANISOU 1514  O   MET A 106    19061  17086  12455  -5985   3527  -2294
ATOM   1515  CB  MET A 106     -32.291  21.513  10.976  1.00126.66           C  
ANISOU 1515  CB  MET A 106    18381  16789  12956  -5300   3146  -2068
ATOM   1516  CG  MET A 106     -32.926  21.092   9.639  1.00127.47           C  
ANISOU 1516  CG  MET A 106    18139  16959  13334  -5126   3132  -2103
ATOM   1517  SD  MET A 106     -34.521  20.230   9.685  1.00125.35           S  
ANISOU 1517  SD  MET A 106    17811  16851  12967  -5520   3359  -2227
ATOM   1518  CE  MET A 106     -35.677  21.618   9.520  1.00123.69           C  
ANISOU 1518  CE  MET A 106    17069  17030  12899  -5605   3717  -2586
ATOM   1519  H   MET A 106     -32.987  23.939  10.341  1.00  0.00           H  
ATOM   1520  HA  MET A 106     -34.007  21.996  12.184  1.00  0.00           H  
ATOM   1521  HB3 MET A 106     -32.086  20.601  11.538  1.00  0.00           H  
ATOM   1522  HB2 MET A 106     -31.308  21.930  10.758  1.00  0.00           H  
ATOM   1523  HG3 MET A 106     -32.229  20.419   9.140  1.00  0.00           H  
ATOM   1524  HG2 MET A 106     -33.017  21.936   8.973  1.00  0.00           H  
ATOM   1525  HE1 MET A 106     -36.699  21.244   9.460  1.00  0.00           H  
ATOM   1526  HE2 MET A 106     -35.612  22.286  10.376  1.00  0.00           H  
ATOM   1527  HE3 MET A 106     -35.468  22.186   8.614  1.00  0.00           H  
ATOM   1528  N   PHE A 107     -31.267  23.633  13.091  1.00124.76           N  
ANISOU 1528  N   PHE A 107    18251  16607  12547  -5268   3215  -2223
ATOM   1529  CA  PHE A 107     -30.551  24.197  14.235  1.00125.70           C  
ANISOU 1529  CA  PHE A 107    18684  16663  12415  -5397   3154  -2180
ATOM   1530  C   PHE A 107     -31.498  25.028  15.118  1.00128.26           C  
ANISOU 1530  C   PHE A 107    18910  17182  12639  -5626   3529  -2504
ATOM   1531  O   PHE A 107     -31.663  24.706  16.293  1.00131.09           O  
ANISOU 1531  O   PHE A 107    19613  17567  12628  -6028   3670  -2547
ATOM   1532  CB  PHE A 107     -29.327  25.014  13.758  1.00125.79           C  
ANISOU 1532  CB  PHE A 107    18615  16562  12617  -5025   2862  -2041
ATOM   1533  CG  PHE A 107     -28.086  24.200  13.417  1.00124.70           C  
ANISOU 1533  CG  PHE A 107    18690  16217  12473  -4870   2492  -1710
ATOM   1534  CD1 PHE A 107     -27.003  24.147  14.320  1.00124.69           C  
ANISOU 1534  CD1 PHE A 107    19029  16095  12252  -4937   2243  -1507
ATOM   1535  CD2 PHE A 107     -28.029  23.408  12.251  1.00123.73           C  
ANISOU 1535  CD2 PHE A 107    18410  16022  12581  -4639   2385  -1607
ATOM   1536  CE1 PHE A 107     -25.884  23.377  14.025  1.00123.77           C  
ANISOU 1536  CE1 PHE A 107    19055  15791  12181  -4741   1897  -1206
ATOM   1537  CE2 PHE A 107     -26.902  22.650  11.968  1.00122.75           C  
ANISOU 1537  CE2 PHE A 107    18461  15696  12483  -4458   2073  -1328
ATOM   1538  CZ  PHE A 107     -25.831  22.638  12.850  1.00122.82           C  
ANISOU 1538  CZ  PHE A 107    18770  15587  12307  -4492   1832  -1129
ATOM   1539  H   PHE A 107     -31.063  24.051  12.192  1.00  0.00           H  
ATOM   1540  HA  PHE A 107     -30.185  23.373  14.851  1.00  0.00           H  
ATOM   1541  HB3 PHE A 107     -29.048  25.748  14.515  1.00  0.00           H  
ATOM   1542  HB2 PHE A 107     -29.599  25.597  12.876  1.00  0.00           H  
ATOM   1543  HD1 PHE A 107     -27.029  24.720  15.233  1.00  0.00           H  
ATOM   1544  HD2 PHE A 107     -28.856  23.376  11.568  1.00  0.00           H  
ATOM   1545  HE1 PHE A 107     -25.052  23.356  14.713  1.00  0.00           H  
ATOM   1546  HE2 PHE A 107     -26.863  22.060  11.064  1.00  0.00           H  
ATOM   1547  HZ  PHE A 107     -24.957  22.044  12.628  1.00  0.00           H  
ATOM   1548  N   GLY A 108     -32.144  26.037  14.506  1.00127.94           N  
ANISOU 1548  N   GLY A 108    18412  17270  12930  -5369   3692  -2729
ATOM   1549  CA  GLY A 108     -33.200  26.846  15.113  1.00129.43           C  
ANISOU 1549  CA  GLY A 108    18405  17639  13135  -5480   4075  -3076
ATOM   1550  C   GLY A 108     -32.687  27.769  16.227  1.00130.35           C  
ANISOU 1550  C   GLY A 108    18802  17707  13018  -5617   4129  -3156
ATOM   1551  O   GLY A 108     -33.463  28.105  17.123  1.00132.31           O  
ANISOU 1551  O   GLY A 108    19153  18076  13043  -5940   4468  -3398
ATOM   1552  H   GLY A 108     -31.950  26.225  13.531  1.00  0.00           H  
ATOM   1553  HA3 GLY A 108     -33.982  26.192  15.504  1.00  0.00           H  
ATOM   1554  HA2 GLY A 108     -33.660  27.458  14.336  1.00  0.00           H  
ATOM   1555  N   TYR A 109     -31.394  28.142  16.204  1.00124.02           N  
ANISOU 1555  N   TYR A 109    18125  16743  12253  -5401   3808  -2966
ATOM   1556  CA  TYR A 109     -30.763  28.926  17.265  1.00124.01           C  
ANISOU 1556  CA  TYR A 109    18410  16697  12010  -5560   3822  -3028
ATOM   1557  C   TYR A 109     -31.268  30.376  17.290  1.00124.40           C  
ANISOU 1557  C   TYR A 109    18191  16810  12266  -5413   4109  -3361
ATOM   1558  O   TYR A 109     -31.472  30.978  16.234  1.00124.51           O  
ANISOU 1558  O   TYR A 109    17797  16829  12683  -5040   4116  -3432
ATOM   1559  CB  TYR A 109     -29.221  28.892  17.131  1.00125.19           C  
ANISOU 1559  CB  TYR A 109    18766  16677  12122  -5409   3377  -2717
ATOM   1560  CG  TYR A 109     -28.488  27.585  17.420  1.00124.97           C  
ANISOU 1560  CG  TYR A 109    19097  16546  11839  -5568   3068  -2378
ATOM   1561  CD1 TYR A 109     -27.081  27.604  17.464  1.00126.42           C  
ANISOU 1561  CD1 TYR A 109    19476  16603  11954  -5476   2671  -2101
ATOM   1562  CD2 TYR A 109     -29.156  26.363  17.651  1.00123.28           C  
ANISOU 1562  CD2 TYR A 109    19012  16351  11476  -5793   3159  -2327
ATOM   1563  CE1 TYR A 109     -26.344  26.430  17.704  1.00126.26           C  
ANISOU 1563  CE1 TYR A 109    19755  16465  11753  -5554   2364  -1777
ATOM   1564  CE2 TYR A 109     -28.425  25.180  17.878  1.00123.06           C  
ANISOU 1564  CE2 TYR A 109    19336  16178  11243  -5900   2861  -2004
ATOM   1565  CZ  TYR A 109     -27.018  25.212  17.902  1.00124.60           C  
ANISOU 1565  CZ  TYR A 109    19706  16234  11401  -5756   2459  -1727
ATOM   1566  OH  TYR A 109     -26.306  24.067  18.108  1.00124.29           O  
ANISOU 1566  OH  TYR A 109    20002  16033  11188  -5818   2148  -1401
ATOM   1567  H   TYR A 109     -30.797  27.834  15.452  1.00  0.00           H  
ATOM   1568  HA  TYR A 109     -31.047  28.451  18.202  1.00  0.00           H  
ATOM   1569  HB3 TYR A 109     -28.797  29.622  17.823  1.00  0.00           H  
ATOM   1570  HB2 TYR A 109     -28.933  29.229  16.134  1.00  0.00           H  
ATOM   1571  HD1 TYR A 109     -26.563  28.532  17.310  1.00  0.00           H  
ATOM   1572  HD2 TYR A 109     -30.232  26.311  17.662  1.00  0.00           H  
ATOM   1573  HE1 TYR A 109     -25.265  26.465  17.724  1.00  0.00           H  
ATOM   1574  HE2 TYR A 109     -28.954  24.252  18.037  1.00  0.00           H  
ATOM   1575  HH  TYR A 109     -26.862  23.295  18.233  1.00  0.00           H  
ATOM   1576  N   LYS A 110     -31.403  30.908  18.511  1.00123.78           N  
ANISOU 1576  N   LYS A 110    18367  16767  11896  -5722   4353  -3568
ATOM   1577  CA  LYS A 110     -31.632  32.323  18.783  1.00123.24           C  
ANISOU 1577  CA  LYS A 110    18145  16712  11971  -5615   4640  -3900
ATOM   1578  C   LYS A 110     -30.366  32.881  19.443  1.00123.44           C  
ANISOU 1578  C   LYS A 110    18507  16589  11804  -5664   4402  -3795
ATOM   1579  O   LYS A 110     -29.815  32.237  20.337  1.00121.96           O  
ANISOU 1579  O   LYS A 110    18766  16389  11186  -6034   4280  -3656
ATOM   1580  CB  LYS A 110     -32.862  32.492  19.700  1.00  0.00           C  
ATOM   1581  CG  LYS A 110     -34.201  32.215  18.997  1.00  0.00           C  
ATOM   1582  CD  LYS A 110     -35.407  32.408  19.930  1.00  0.00           C  
ATOM   1583  CE  LYS A 110     -36.750  32.260  19.199  1.00  0.00           C  
ATOM   1584  NZ  LYS A 110     -37.890  32.477  20.106  1.00  0.00           N1+
ATOM   1585  H   LYS A 110     -31.181  30.334  19.317  1.00  0.00           H  
ATOM   1586  HA  LYS A 110     -31.811  32.871  17.855  1.00  0.00           H  
ATOM   1587  HB2 LYS A 110     -32.768  31.851  20.572  1.00  0.00           H  
ATOM   1588  HB3 LYS A 110     -32.887  33.516  20.075  1.00  0.00           H  
ATOM   1589  HG2 LYS A 110     -34.297  32.878  18.136  1.00  0.00           H  
ATOM   1590  HG3 LYS A 110     -34.207  31.198  18.602  1.00  0.00           H  
ATOM   1591  HD2 LYS A 110     -35.351  31.680  20.740  1.00  0.00           H  
ATOM   1592  HD3 LYS A 110     -35.352  33.392  20.399  1.00  0.00           H  
ATOM   1593  HE2 LYS A 110     -36.815  32.981  18.383  1.00  0.00           H  
ATOM   1594  HE3 LYS A 110     -36.833  31.266  18.757  1.00  0.00           H  
ATOM   1595  HZ1 LYS A 110     -38.753  32.386  19.588  1.00  0.00           H  
ATOM   1596  HZ2 LYS A 110     -37.872  31.793  20.848  1.00  0.00           H  
ATOM   1597  HZ3 LYS A 110     -37.836  33.405  20.501  1.00  0.00           H  
ATOM   1598  N   LYS A 111     -29.944  34.076  18.994  1.00105.88           N  
ANISOU 1598  N   LYS A 111    16086  14252   9891  -5306   4289  -3823
ATOM   1599  CA  LYS A 111     -28.745  34.785  19.458  1.00106.71           C  
ANISOU 1599  CA  LYS A 111    16469  14226   9847  -5347   4047  -3725
ATOM   1600  C   LYS A 111     -28.708  35.019  20.984  1.00108.04           C  
ANISOU 1600  C   LYS A 111    17100  14422   9528  -5834   4236  -3886
ATOM   1601  O   LYS A 111     -27.644  34.874  21.582  1.00108.25           O  
ANISOU 1601  O   LYS A 111    17494  14416   9219  -6078   3930  -3648
ATOM   1602  CB  LYS A 111     -28.598  36.105  18.660  1.00  0.00           C  
ATOM   1603  CG  LYS A 111     -29.662  37.177  18.982  1.00  0.00           C  
ATOM   1604  CD  LYS A 111     -29.529  38.467  18.168  1.00  0.00           C  
ATOM   1605  CE  LYS A 111     -30.548  39.521  18.633  1.00  0.00           C  
ATOM   1606  NZ  LYS A 111     -30.396  40.785  17.896  1.00  0.00           N1+
ATOM   1607  H   LYS A 111     -30.458  34.530  18.253  1.00  0.00           H  
ATOM   1608  HA  LYS A 111     -27.890  34.154  19.213  1.00  0.00           H  
ATOM   1609  HB2 LYS A 111     -27.613  36.528  18.867  1.00  0.00           H  
ATOM   1610  HB3 LYS A 111     -28.603  35.885  17.591  1.00  0.00           H  
ATOM   1611  HG2 LYS A 111     -30.661  36.762  18.843  1.00  0.00           H  
ATOM   1612  HG3 LYS A 111     -29.589  37.458  20.031  1.00  0.00           H  
ATOM   1613  HD2 LYS A 111     -28.516  38.860  18.268  1.00  0.00           H  
ATOM   1614  HD3 LYS A 111     -29.675  38.249  17.109  1.00  0.00           H  
ATOM   1615  HE2 LYS A 111     -31.565  39.152  18.498  1.00  0.00           H  
ATOM   1616  HE3 LYS A 111     -30.421  39.726  19.698  1.00  0.00           H  
ATOM   1617  HZ1 LYS A 111     -31.076  41.453  18.231  1.00  0.00           H  
ATOM   1618  HZ2 LYS A 111     -29.467  41.152  18.045  1.00  0.00           H  
ATOM   1619  HZ3 LYS A 111     -30.541  40.623  16.910  1.00  0.00           H  
ATOM   1620  N   ASP A 112     -29.873  35.346  21.573  1.00 91.40           N  
ANISOU 1620  N   ASP A 112    14959  12393   7376  -5984   4744  -4285
ATOM   1621  CA  ASP A 112     -30.055  35.611  23.002  1.00 95.65           C  
ANISOU 1621  CA  ASP A 112    15893  12971   7480  -6445   5058  -4544
ATOM   1622  C   ASP A 112     -30.212  34.337  23.842  1.00299.33           C  
ANISOU 1622  C   ASP A 112    37982  37974  37774     17     54    -69
ATOM   1623  O   ASP A 112     -29.746  34.333  24.981  1.00299.66           O  
ANISOU 1623  O   ASP A 112    37990  37985  37884      8     24    -35
ATOM   1624  CB  ASP A 112     -31.230  36.577  23.291  1.00  0.00           C  
ATOM   1625  CG  ASP A 112     -31.090  37.957  22.640  1.00  0.00           C  
ATOM   1626  OD1 ASP A 112     -29.960  38.492  22.663  1.00  0.00           O  
ATOM   1627  OD2 ASP A 112     -32.135  38.500  22.220  1.00  0.00           O1-
ATOM   1628  H   ASP A 112     -30.698  35.445  21.001  1.00  0.00           H  
ATOM   1629  HA  ASP A 112     -29.144  36.096  23.361  1.00  0.00           H  
ATOM   1630  HB2 ASP A 112     -32.149  36.121  22.920  1.00  0.00           H  
ATOM   1631  HB3 ASP A 112     -31.363  36.722  24.363  1.00  0.00           H  
ATOM   1632  N   LYS A 113     -30.857  33.290  23.296  1.00285.35           N  
ANISOU 1632  N   LYS A 113    37194  36981  34247   -321   1064  -1013
ATOM   1633  CA  LYS A 113     -31.098  32.038  24.023  1.00293.10           C  
ANISOU 1633  CA  LYS A 113    37817  37862  35685    154    643   -555
ATOM   1634  C   LYS A 113     -29.830  31.173  24.149  1.00291.73           C  
ANISOU 1634  C   LYS A 113    37777  37750  35317     60    636   -609
ATOM   1635  O   LYS A 113     -29.648  30.537  25.186  1.00293.51           O  
ANISOU 1635  O   LYS A 113    37882  37900  35741    104    506   -465
ATOM   1636  CB  LYS A 113     -32.251  31.254  23.355  1.00  0.00           C  
ATOM   1637  CG  LYS A 113     -32.714  30.014  24.150  1.00  0.00           C  
ATOM   1638  CD  LYS A 113     -33.866  29.232  23.499  1.00  0.00           C  
ATOM   1639  CE  LYS A 113     -35.228  29.934  23.594  1.00  0.00           C  
ATOM   1640  NZ  LYS A 113     -36.302  29.070  23.075  1.00  0.00           N1+
ATOM   1641  H   LYS A 113     -31.197  33.342  22.348  1.00  0.00           H  
ATOM   1642  HA  LYS A 113     -31.422  32.294  25.034  1.00  0.00           H  
ATOM   1643  HB2 LYS A 113     -33.100  31.923  23.216  1.00  0.00           H  
ATOM   1644  HB3 LYS A 113     -31.934  30.934  22.363  1.00  0.00           H  
ATOM   1645  HG2 LYS A 113     -31.880  29.321  24.265  1.00  0.00           H  
ATOM   1646  HG3 LYS A 113     -32.995  30.308  25.161  1.00  0.00           H  
ATOM   1647  HD2 LYS A 113     -33.623  29.046  22.452  1.00  0.00           H  
ATOM   1648  HD3 LYS A 113     -33.928  28.249  23.969  1.00  0.00           H  
ATOM   1649  HE2 LYS A 113     -35.454  30.178  24.633  1.00  0.00           H  
ATOM   1650  HE3 LYS A 113     -35.222  30.871  23.037  1.00  0.00           H  
ATOM   1651  HZ1 LYS A 113     -37.191  29.541  23.160  1.00  0.00           H  
ATOM   1652  HZ2 LYS A 113     -36.121  28.850  22.106  1.00  0.00           H  
ATOM   1653  HZ3 LYS A 113     -36.326  28.214  23.610  1.00  0.00           H  
ATOM   1654  N   ASP A 114     -29.008  31.147  23.086  1.00274.19           N  
ANISOU 1654  N   ASP A 114    36283  35489  32406  -1487   1319  -1212
ATOM   1655  CA  ASP A 114     -27.925  30.172  22.890  1.00274.21           C  
ANISOU 1655  CA  ASP A 114    36357  35433  32397  -1594   1149  -1083
ATOM   1656  C   ASP A 114     -26.527  30.815  22.847  1.00274.06           C  
ANISOU 1656  C   ASP A 114    36411  35346  32375  -1658    992  -1101
ATOM   1657  O   ASP A 114     -25.542  30.077  22.829  1.00274.03           O  
ANISOU 1657  O   ASP A 114    36457  35303  32356  -1734    857   -984
ATOM   1658  CB  ASP A 114     -28.161  29.309  21.625  1.00273.98           C  
ANISOU 1658  CB  ASP A 114    36275  35368  32457  -1677   1183  -1014
ATOM   1659  CG  ASP A 114     -29.578  28.732  21.523  1.00273.84           C  
ANISOU 1659  CG  ASP A 114    36174  35419  32453  -1651   1344   -999
ATOM   1660  OD1 ASP A 114     -30.055  28.174  22.535  1.00274.27           O  
ANISOU 1660  OD1 ASP A 114    36239  35536  32434  -1580   1361   -939
ATOM   1661  OD2 ASP A 114     -30.148  28.818  20.416  1.00273.35           O1-
ANISOU 1661  OD2 ASP A 114    36025  35356  32480  -1694   1455  -1043
ATOM   1662  H   ASP A 114     -29.242  31.703  22.274  1.00  0.00           H  
ATOM   1663  HA  ASP A 114     -27.898  29.487  23.739  1.00  0.00           H  
ATOM   1664  HB3 ASP A 114     -27.449  28.485  21.568  1.00  0.00           H  
ATOM   1665  HB2 ASP A 114     -27.984  29.927  20.742  1.00  0.00           H  
ATOM   1666  N   GLY A 115     -26.449  32.157  22.842  1.00262.64           N  
ANISOU 1666  N   GLY A 115    35511  33908  30373  -2587   1445  -1569
ATOM   1667  CA  GLY A 115     -25.202  32.917  22.761  1.00261.81           C  
ANISOU 1667  CA  GLY A 115    35519  33740  30215  -2720   1294  -1579
ATOM   1668  C   GLY A 115     -24.834  33.174  21.293  1.00188.45           C  
ANISOU 1668  C   GLY A 115    28045  24471  19088  -6111   2784  -2740
ATOM   1669  O   GLY A 115     -25.127  32.363  20.412  1.00107.70           O  
ANISOU 1669  O   GLY A 115    17574  14244   9102  -5871   2734  -2612
ATOM   1670  H   GLY A 115     -27.305  32.694  22.860  1.00  0.00           H  
ATOM   1671  HA3 GLY A 115     -24.383  32.397  23.262  1.00  0.00           H  
ATOM   1672  HA2 GLY A 115     -25.346  33.865  23.280  1.00  0.00           H  
ATOM   1673  N   TYR A 116     -24.179  34.321  21.042  1.00153.98           N  
ANISOU 1673  N   TYR A 116    23578  20047  14881  -5955   2716  -2816
ATOM   1674  CA  TYR A 116     -23.845  34.813  19.702  1.00155.80           C  
ANISOU 1674  CA  TYR A 116    23399  20216  15583  -5491   2590  -2755
ATOM   1675  C   TYR A 116     -22.864  33.919  18.921  1.00157.48           C  
ANISOU 1675  C   TYR A 116    23489  20420  15926  -5279   2157  -2363
ATOM   1676  O   TYR A 116     -23.070  33.734  17.723  1.00158.91           O  
ANISOU 1676  O   TYR A 116    23334  20583  16463  -4935   2152  -2315
ATOM   1677  CB  TYR A 116     -23.348  36.274  19.782  1.00154.02           C  
ANISOU 1677  CB  TYR A 116    23179  19913  15427  -5448   2578  -2890
ATOM   1678  CG  TYR A 116     -22.942  36.872  18.443  1.00152.01           C  
ANISOU 1678  CG  TYR A 116    22546  19586  15625  -5012   2446  -2820
ATOM   1679  CD1 TYR A 116     -23.927  37.381  17.571  1.00151.97           C  
ANISOU 1679  CD1 TYR A 116    22232  19532  15979  -4712   2726  -3035
ATOM   1680  CD2 TYR A 116     -21.589  36.865  18.040  1.00151.79           C  
ANISOU 1680  CD2 TYR A 116    22462  19549  15662  -4909   2037  -2534
ATOM   1681  CE1 TYR A 116     -23.563  37.867  16.300  1.00151.91           C  
ANISOU 1681  CE1 TYR A 116    21917  19451  16353  -4341   2590  -2952
ATOM   1682  CE2 TYR A 116     -21.227  37.338  16.764  1.00151.69           C  
ANISOU 1682  CE2 TYR A 116    22125  19477  16032  -4549   1936  -2474
ATOM   1683  CZ  TYR A 116     -22.215  37.836  15.892  1.00151.72           C  
ANISOU 1683  CZ  TYR A 116    21874  19416  16357  -4277   2208  -2677
ATOM   1684  OH  TYR A 116     -21.867  38.285  14.653  1.00151.65           O  
ANISOU 1684  OH  TYR A 116    21587  19342  16693  -3952   2098  -2604
ATOM   1685  H   TYR A 116     -23.964  34.944  21.807  1.00  0.00           H  
ATOM   1686  HA  TYR A 116     -24.780  34.828  19.139  1.00  0.00           H  
ATOM   1687  HB3 TYR A 116     -22.497  36.339  20.462  1.00  0.00           H  
ATOM   1688  HB2 TYR A 116     -24.127  36.903  20.217  1.00  0.00           H  
ATOM   1689  HD1 TYR A 116     -24.966  37.383  17.867  1.00  0.00           H  
ATOM   1690  HD2 TYR A 116     -20.828  36.469  18.696  1.00  0.00           H  
ATOM   1691  HE1 TYR A 116     -24.320  38.253  15.633  1.00  0.00           H  
ATOM   1692  HE2 TYR A 116     -20.192  37.310  16.457  1.00  0.00           H  
ATOM   1693  HH  TYR A 116     -20.926  38.215  14.476  1.00  0.00           H  
ATOM   1694  N   ALA A 117     -21.827  33.393  19.596  1.00140.10           N  
ANISOU 1694  N   ALA A 117    21546  18231  13455  -5468   1793  -2088
ATOM   1695  CA  ALA A 117     -20.804  32.538  18.985  1.00138.10           C  
ANISOU 1695  CA  ALA A 117    21163  17961  13348  -5239   1384  -1723
ATOM   1696  C   ALA A 117     -21.357  31.191  18.493  1.00137.12           C  
ANISOU 1696  C   ALA A 117    20986  17817  13297  -5135   1424  -1614
ATOM   1697  O   ALA A 117     -20.949  30.732  17.426  1.00134.45           O  
ANISOU 1697  O   ALA A 117    20377  17442  13268  -4798   1282  -1463
ATOM   1698  CB  ALA A 117     -19.656  32.326  19.982  1.00141.56           C  
ANISOU 1698  CB  ALA A 117    21889  18426  13473  -5476    991  -1461
ATOM   1699  H   ALA A 117     -21.720  33.592  20.579  1.00  0.00           H  
ATOM   1700  HA  ALA A 117     -20.404  33.067  18.118  1.00  0.00           H  
ATOM   1701  HB1 ALA A 117     -18.867  31.708  19.550  1.00  0.00           H  
ATOM   1702  HB2 ALA A 117     -19.205  33.277  20.265  1.00  0.00           H  
ATOM   1703  HB3 ALA A 117     -20.001  31.837  20.893  1.00  0.00           H  
ATOM   1704  N   LYS A 118     -22.303  30.614  19.255  1.00125.54           N  
ANISOU 1704  N   LYS A 118    19789  16373  11539  -5446   1643  -1709
ATOM   1705  CA  LYS A 118     -23.043  29.409  18.884  1.00125.63           C  
ANISOU 1705  CA  LYS A 118    19796  16361  11577  -5421   1721  -1634
ATOM   1706  C   LYS A 118     -24.024  29.674  17.734  1.00125.25           C  
ANISOU 1706  C   LYS A 118    19341  16337  11911  -5136   2008  -1844
ATOM   1707  O   LYS A 118     -24.114  28.841  16.835  1.00125.21           O  
ANISOU 1707  O   LYS A 118    19175  16292  12106  -4924   1932  -1711
ATOM   1708  CB  LYS A 118     -23.788  28.846  20.113  1.00  0.00           C  
ATOM   1709  CG  LYS A 118     -22.885  28.433  21.292  1.00  0.00           C  
ATOM   1710  CD  LYS A 118     -21.904  27.294  20.958  1.00  0.00           C  
ATOM   1711  CE  LYS A 118     -21.095  26.802  22.169  1.00  0.00           C  
ATOM   1712  NZ  LYS A 118     -20.167  27.833  22.666  1.00  0.00           N1+
ATOM   1713  H   LYS A 118     -22.598  31.069  20.106  1.00  0.00           H  
ATOM   1714  HA  LYS A 118     -22.330  28.663  18.530  1.00  0.00           H  
ATOM   1715  HB2 LYS A 118     -24.507  29.587  20.463  1.00  0.00           H  
ATOM   1716  HB3 LYS A 118     -24.382  27.980  19.813  1.00  0.00           H  
ATOM   1717  HG2 LYS A 118     -22.340  29.304  21.656  1.00  0.00           H  
ATOM   1718  HG3 LYS A 118     -23.525  28.120  22.118  1.00  0.00           H  
ATOM   1719  HD2 LYS A 118     -22.459  26.454  20.538  1.00  0.00           H  
ATOM   1720  HD3 LYS A 118     -21.209  27.613  20.181  1.00  0.00           H  
ATOM   1721  HE2 LYS A 118     -21.763  26.498  22.976  1.00  0.00           H  
ATOM   1722  HE3 LYS A 118     -20.512  25.924  21.890  1.00  0.00           H  
ATOM   1723  HZ1 LYS A 118     -19.648  27.468  23.452  1.00  0.00           H  
ATOM   1724  HZ2 LYS A 118     -19.525  28.093  21.931  1.00  0.00           H  
ATOM   1725  HZ3 LYS A 118     -20.691  28.645  22.958  1.00  0.00           H  
ATOM   1726  N   TRP A 119     -24.709  30.831  17.763  1.00114.78           N  
ANISOU 1726  N   TRP A 119    17851  15064  10694  -5117   2319  -2163
ATOM   1727  CA  TRP A 119     -25.623  31.289  16.716  1.00114.62           C  
ANISOU 1727  CA  TRP A 119    17426  15073  11050  -4834   2566  -2361
ATOM   1728  C   TRP A 119     -24.929  31.530  15.362  1.00114.29           C  
ANISOU 1728  C   TRP A 119    17074  14969  11382  -4416   2309  -2189
ATOM   1729  O   TRP A 119     -25.451  31.086  14.340  1.00114.15           O  
ANISOU 1729  O   TRP A 119    16815  14957  11597  -4210   2331  -2153
ATOM   1730  CB  TRP A 119     -26.409  32.512  17.219  1.00114.60           C  
ANISOU 1730  CB  TRP A 119    17347  15107  11088  -4880   2920  -2723
ATOM   1731  CG  TRP A 119     -27.347  33.123  16.226  1.00113.21           C  
ANISOU 1731  CG  TRP A 119    16743  14957  11316  -4566   3140  -2914
ATOM   1732  CD1 TRP A 119     -28.568  32.640  15.914  1.00113.75           C  
ANISOU 1732  CD1 TRP A 119    16610  15128  11483  -4570   3406  -3060
ATOM   1733  CD2 TRP A 119     -27.117  34.244  15.323  1.00111.86           C  
ANISOU 1733  CD2 TRP A 119    16300  14711  11491  -4221   3097  -2973
ATOM   1734  NE1 TRP A 119     -29.119  33.389  14.897  1.00112.65           N  
ANISOU 1734  NE1 TRP A 119    16068  14989  11743  -4227   3505  -3193
ATOM   1735  CE2 TRP A 119     -28.265  34.391  14.485  1.00111.53           C  
ANISOU 1735  CE2 TRP A 119    15897  14725  11755  -4006   3322  -3141
ATOM   1736  CE3 TRP A 119     -26.047  35.147  15.118  1.00110.82           C  
ANISOU 1736  CE3 TRP A 119    16199  14474  11436  -4090   2877  -2889
ATOM   1737  CZ2 TRP A 119     -28.346  35.383  13.494  1.00110.48           C  
ANISOU 1737  CZ2 TRP A 119    15461  14522  11994  -3650   3314  -3209
ATOM   1738  CZ3 TRP A 119     -26.121  36.150  14.133  1.00109.77           C  
ANISOU 1738  CZ3 TRP A 119    15784  14265  11657  -3763   2902  -2974
ATOM   1739  CH2 TRP A 119     -27.265  36.264  13.319  1.00109.58           C  
ANISOU 1739  CH2 TRP A 119    15430  14277  11930  -3537   3107  -3122
ATOM   1740  H   TRP A 119     -24.592  31.455  18.550  1.00  0.00           H  
ATOM   1741  HA  TRP A 119     -26.357  30.505  16.539  1.00  0.00           H  
ATOM   1742  HB3 TRP A 119     -25.722  33.291  17.549  1.00  0.00           H  
ATOM   1743  HB2 TRP A 119     -26.988  32.229  18.099  1.00  0.00           H  
ATOM   1744  HD1 TRP A 119     -29.012  31.783  16.392  1.00  0.00           H  
ATOM   1745  HE1 TRP A 119     -30.031  33.188  14.510  1.00  0.00           H  
ATOM   1746  HE3 TRP A 119     -25.158  35.065  15.727  1.00  0.00           H  
ATOM   1747  HZ2 TRP A 119     -29.224  35.465  12.870  1.00  0.00           H  
ATOM   1748  HZ3 TRP A 119     -25.294  36.830  13.997  1.00  0.00           H  
ATOM   1749  HH2 TRP A 119     -27.306  37.022  12.556  1.00  0.00           H  
ATOM   1750  N   MET A 120     -23.751  32.179  15.391  1.00104.83           N  
ANISOU 1750  N   MET A 120    15896  13721  10213  -4330   2070  -2085
ATOM   1751  CA  MET A 120     -22.864  32.380  14.243  1.00104.74           C  
ANISOU 1751  CA  MET A 120    15622  13664  10509  -3989   1830  -1920
ATOM   1752  C   MET A 120     -22.363  31.050  13.657  1.00105.19           C  
ANISOU 1752  C   MET A 120    15679  13696  10593  -3885   1591  -1639
ATOM   1753  O   MET A 120     -22.360  30.903  12.436  1.00106.19           O  
ANISOU 1753  O   MET A 120    15548  13801  10997  -3608   1551  -1579
ATOM   1754  CB  MET A 120     -21.699  33.308  14.657  1.00110.56           C  
ANISOU 1754  CB  MET A 120    16429  14379  11200  -4013   1623  -1858
ATOM   1755  CG  MET A 120     -20.640  33.577  13.568  1.00112.59           C  
ANISOU 1755  CG  MET A 120    16425  14610  11745  -3709   1396  -1698
ATOM   1756  SD  MET A 120     -19.179  34.476  14.136  1.00112.44           S  
ANISOU 1756  SD  MET A 120    16515  14601  11606  -3830   1130  -1602
ATOM   1757  CE  MET A 120     -18.274  33.104  14.899  1.00111.95           C  
ANISOU 1757  CE  MET A 120    16652  14585  11298  -3964    774  -1270
ATOM   1758  H   MET A 120     -23.411  32.534  16.276  1.00  0.00           H  
ATOM   1759  HA  MET A 120     -23.445  32.884  13.470  1.00  0.00           H  
ATOM   1760  HB3 MET A 120     -21.207  32.893  15.537  1.00  0.00           H  
ATOM   1761  HB2 MET A 120     -22.111  34.265  14.979  1.00  0.00           H  
ATOM   1762  HG3 MET A 120     -21.073  34.162  12.765  1.00  0.00           H  
ATOM   1763  HG2 MET A 120     -20.286  32.656  13.110  1.00  0.00           H  
ATOM   1764  HE1 MET A 120     -17.322  33.458  15.295  1.00  0.00           H  
ATOM   1765  HE2 MET A 120     -18.847  32.670  15.718  1.00  0.00           H  
ATOM   1766  HE3 MET A 120     -18.073  32.324  14.164  1.00  0.00           H  
ATOM   1767  N   ALA A 121     -21.991  30.100  14.535  1.00100.35           N  
ANISOU 1767  N   ALA A 121    15378  13068   9681  -4115   1442  -1472
ATOM   1768  CA  ALA A 121     -21.617  28.733  14.169  1.00100.37           C  
ANISOU 1768  CA  ALA A 121    15440  13003   9692  -4025   1231  -1212
ATOM   1769  C   ALA A 121     -22.774  27.930  13.549  1.00 99.73           C  
ANISOU 1769  C   ALA A 121    15258  12915   9719  -3979   1462  -1307
ATOM   1770  O   ALA A 121     -22.509  27.075  12.708  1.00 99.34           O  
ANISOU 1770  O   ALA A 121    15111  12797   9835  -3775   1349  -1161
ATOM   1771  CB  ALA A 121     -21.039  28.007  15.393  1.00103.83           C  
ANISOU 1771  CB  ALA A 121    16279  13407   9763  -4311   1045  -1030
ATOM   1772  H   ALA A 121     -22.009  30.305  15.525  1.00  0.00           H  
ATOM   1773  HA  ALA A 121     -20.825  28.799  13.422  1.00  0.00           H  
ATOM   1774  HB1 ALA A 121     -20.711  27.000  15.132  1.00  0.00           H  
ATOM   1775  HB2 ALA A 121     -20.172  28.538  15.788  1.00  0.00           H  
ATOM   1776  HB3 ALA A 121     -21.767  27.917  16.197  1.00  0.00           H  
ATOM   1777  N   GLY A 122     -24.024  28.249  13.929  1.00 98.69           N  
ANISOU 1777  N   GLY A 122    15134  12863   9502  -4173   1794  -1565
ATOM   1778  CA  GLY A 122     -25.241  27.691  13.346  1.00 98.48           C  
ANISOU 1778  CA  GLY A 122    14959  12877   9581  -4167   2036  -1691
ATOM   1779  C   GLY A 122     -25.451  28.212  11.916  1.00 96.42           C  
ANISOU 1779  C   GLY A 122    14300  12627   9706  -3813   2040  -1732
ATOM   1780  O   GLY A 122     -25.845  27.432  11.052  1.00 95.70           O  
ANISOU 1780  O   GLY A 122    14115  12513   9733  -3713   2024  -1662
ATOM   1781  H   GLY A 122     -24.149  28.951  14.647  1.00  0.00           H  
ATOM   1782  HA3 GLY A 122     -26.094  27.981  13.960  1.00  0.00           H  
ATOM   1783  HA2 GLY A 122     -25.195  26.600  13.350  1.00  0.00           H  
ATOM   1784  N   ASN A 123     -25.144  29.498  11.655  1.00 90.13           N  
ANISOU 1784  N   ASN A 123    13306  11849   9090  -3640   2046  -1835
ATOM   1785  CA  ASN A 123     -25.223  30.128  10.329  1.00 87.60           C  
ANISOU 1785  CA  ASN A 123    12639  11528   9117  -3319   2029  -1862
ATOM   1786  C   ASN A 123     -24.139  29.590   9.374  1.00 85.69           C  
ANISOU 1786  C   ASN A 123    12358  11210   8990  -3113   1751  -1612
ATOM   1787  O   ASN A 123     -24.450  29.302   8.218  1.00 84.29           O  
ANISOU 1787  O   ASN A 123    12005  11030   8992  -2954   1754  -1583
ATOM   1788  CB  ASN A 123     -25.124  31.673  10.433  1.00 79.92           C  
ANISOU 1788  CB  ASN A 123    11544  10552   8270  -3218   2085  -2010
ATOM   1789  CG  ASN A 123     -26.160  32.340  11.347  1.00 82.30           C  
ANISOU 1789  CG  ASN A 123    11886  10908   8477  -3394   2391  -2291
ATOM   1790  OD1 ASN A 123     -27.211  31.778  11.642  1.00 83.87           O  
ANISOU 1790  OD1 ASN A 123    12087  11190   8590  -3554   2615  -2419
ATOM   1791  ND2 ASN A 123     -25.869  33.560  11.798  1.00 83.03           N  
ANISOU 1791  ND2 ASN A 123    12015  10953   8578  -3385   2426  -2408
ATOM   1792  H   ASN A 123     -24.836  30.092  12.412  1.00  0.00           H  
ATOM   1793  HA  ASN A 123     -26.190  29.879   9.886  1.00  0.00           H  
ATOM   1794  HB3 ASN A 123     -25.251  32.112   9.443  1.00  0.00           H  
ATOM   1795  HB2 ASN A 123     -24.128  31.962  10.772  1.00  0.00           H  
ATOM   1796 HD22 ASN A 123     -26.513  34.037  12.414  1.00  0.00           H  
ATOM   1797 HD21 ASN A 123     -24.984  33.998  11.574  1.00  0.00           H  
ATOM   1798  N   LEU A 124     -22.900  29.445   9.883  1.00 84.14           N  
ANISOU 1798  N   LEU A 124    12327  10961   8680  -3131   1513  -1433
ATOM   1799  CA  LEU A 124     -21.747  28.861   9.188  1.00 82.72           C  
ANISOU 1799  CA  LEU A 124    12094  10718   8617  -2925   1255  -1202
ATOM   1800  C   LEU A 124     -21.971  27.384   8.820  1.00 82.60           C  
ANISOU 1800  C   LEU A 124    12181  10632   8572  -2919   1237  -1088
ATOM   1801  O   LEU A 124     -21.690  27.005   7.684  1.00 81.50           O  
ANISOU 1801  O   LEU A 124    11883  10456   8629  -2709   1200  -1033
ATOM   1802  CB  LEU A 124     -20.481  29.010  10.066  1.00 83.06           C  
ANISOU 1802  CB  LEU A 124    12274  10749   8538  -2970    998  -1036
ATOM   1803  CG  LEU A 124     -19.910  30.444  10.171  1.00 82.87           C  
ANISOU 1803  CG  LEU A 124    12164  10777   8544  -2984    970  -1120
ATOM   1804  CD1 LEU A 124     -18.987  30.569  11.396  1.00 83.49           C  
ANISOU 1804  CD1 LEU A 124    12443  10875   8403  -3154    741   -984
ATOM   1805  CD2 LEU A 124     -19.163  30.866   8.891  1.00 81.29           C  
ANISOU 1805  CD2 LEU A 124    11677  10582   8629  -2722    902  -1091
ATOM   1806  H   LEU A 124     -22.734  29.732  10.839  1.00  0.00           H  
ATOM   1807  HA  LEU A 124     -21.598  29.400   8.253  1.00  0.00           H  
ATOM   1808  HB3 LEU A 124     -19.689  28.352   9.704  1.00  0.00           H  
ATOM   1809  HB2 LEU A 124     -20.719  28.645  11.065  1.00  0.00           H  
ATOM   1810  HG  LEU A 124     -20.735  31.142  10.318  1.00  0.00           H  
ATOM   1811 HD11 LEU A 124     -18.385  31.478  11.357  1.00  0.00           H  
ATOM   1812 HD12 LEU A 124     -19.564  30.603  12.318  1.00  0.00           H  
ATOM   1813 HD13 LEU A 124     -18.306  29.720  11.469  1.00  0.00           H  
ATOM   1814 HD21 LEU A 124     -19.582  31.774   8.460  1.00  0.00           H  
ATOM   1815 HD22 LEU A 124     -18.108  31.055   9.079  1.00  0.00           H  
ATOM   1816 HD23 LEU A 124     -19.195  30.085   8.134  1.00  0.00           H  
ATOM   1817  N   ALA A 125     -22.496  26.594   9.774  1.00 78.39           N  
ANISOU 1817  N   ALA A 125    11937  10070   7779  -3173   1282  -1068
ATOM   1818  CA  ALA A 125     -22.832  25.180   9.594  1.00 78.46           C  
ANISOU 1818  CA  ALA A 125    12114   9979   7718  -3221   1279   -967
ATOM   1819  C   ALA A 125     -23.954  24.952   8.572  1.00 78.57           C  
ANISOU 1819  C   ALA A 125    11929  10034   7891  -3168   1480  -1107
ATOM   1820  O   ALA A 125     -23.837  24.034   7.763  1.00 78.42           O  
ANISOU 1820  O   ALA A 125    11912   9921   7964  -3045   1421  -1011
ATOM   1821  CB  ALA A 125     -23.208  24.556  10.947  1.00 82.35           C  
ANISOU 1821  CB  ALA A 125    12966  10450   7874  -3567   1333   -955
ATOM   1822  H   ALA A 125     -22.685  26.978  10.691  1.00  0.00           H  
ATOM   1823  HA  ALA A 125     -21.938  24.672   9.226  1.00  0.00           H  
ATOM   1824  HB1 ALA A 125     -23.486  23.507  10.835  1.00  0.00           H  
ATOM   1825  HB2 ALA A 125     -22.369  24.594  11.642  1.00  0.00           H  
ATOM   1826  HB3 ALA A 125     -24.050  25.073  11.409  1.00  0.00           H  
ATOM   1827  N   SER A 126     -24.992  25.805   8.607  1.00 81.10           N  
ANISOU 1827  N   SER A 126    12069  10494   8252  -3251   1712  -1336
ATOM   1828  CA  SER A 126     -26.128  25.771   7.682  1.00 81.21           C  
ANISOU 1828  CA  SER A 126    11843  10588   8424  -3213   1887  -1477
ATOM   1829  C   SER A 126     -25.735  26.126   6.244  1.00 79.58           C  
ANISOU 1829  C   SER A 126    11384  10359   8494  -2902   1771  -1420
ATOM   1830  O   SER A 126     -26.263  25.521   5.312  1.00 79.33           O  
ANISOU 1830  O   SER A 126    11293  10310   8538  -2861   1786  -1401
ATOM   1831  CB  SER A 126     -27.223  26.734   8.168  1.00 82.71           C  
ANISOU 1831  CB  SER A 126    11854  10933   8637  -3316   2134  -1729
ATOM   1832  OG  SER A 126     -27.777  26.248   9.368  1.00 85.20           O  
ANISOU 1832  OG  SER A 126    12404  11290   8679  -3643   2292  -1808
ATOM   1833  H   SER A 126     -25.014  26.531   9.311  1.00  0.00           H  
ATOM   1834  HA  SER A 126     -26.524  24.755   7.670  1.00  0.00           H  
ATOM   1835  HB3 SER A 126     -28.028  26.812   7.436  1.00  0.00           H  
ATOM   1836  HB2 SER A 126     -26.833  27.740   8.326  1.00  0.00           H  
ATOM   1837  HG  SER A 126     -27.163  26.443  10.084  1.00  0.00           H  
ATOM   1838  N   GLY A 127     -24.799  27.078   6.105  1.00 75.54           N  
ANISOU 1838  N   GLY A 127    10752   9846   8103  -2724   1662  -1395
ATOM   1839  CA  GLY A 127     -24.270  27.535   4.830  1.00 74.04           C  
ANISOU 1839  CA  GLY A 127    10351   9639   8141  -2465   1556  -1337
ATOM   1840  C   GLY A 127     -23.426  26.448   4.159  1.00 73.25           C  
ANISOU 1840  C   GLY A 127    10352   9427   8052  -2364   1417  -1162
ATOM   1841  O   GLY A 127     -23.602  26.191   2.969  1.00 72.99           O  
ANISOU 1841  O   GLY A 127    10214   9384   8136  -2266   1435  -1162
ATOM   1842  H   GLY A 127     -24.429  27.526   6.933  1.00  0.00           H  
ATOM   1843  HA3 GLY A 127     -23.629  28.391   5.026  1.00  0.00           H  
ATOM   1844  HA2 GLY A 127     -25.089  27.853   4.185  1.00  0.00           H  
ATOM   1845  N   GLY A 128     -22.532  25.807   4.930  1.00 71.14           N  
ANISOU 1845  N   GLY A 128    10302   9072   7658  -2394   1280  -1018
ATOM   1846  CA  GLY A 128     -21.627  24.770   4.441  1.00 70.81           C  
ANISOU 1846  CA  GLY A 128    10373   8891   7640  -2267   1144   -848
ATOM   1847  C   GLY A 128     -22.393  23.484   4.108  1.00 71.20           C  
ANISOU 1847  C   GLY A 128    10573   8851   7630  -2354   1241   -858
ATOM   1848  O   GLY A 128     -22.114  22.873   3.076  1.00 70.92           O  
ANISOU 1848  O   GLY A 128    10496   8738   7712  -2208   1231   -825
ATOM   1849  H   GLY A 128     -22.441  26.069   5.902  1.00  0.00           H  
ATOM   1850  HA3 GLY A 128     -20.881  24.561   5.208  1.00  0.00           H  
ATOM   1851  HA2 GLY A 128     -21.095  25.131   3.560  1.00  0.00           H  
ATOM   1852  N   ALA A 129     -23.371  23.101   4.950  1.00 71.22           N  
ANISOU 1852  N   ALA A 129    10762   8864   7432  -2624   1354   -918
ATOM   1853  CA  ALA A 129     -24.254  21.952   4.740  1.00 72.29           C  
ANISOU 1853  CA  ALA A 129    11065   8927   7475  -2783   1463   -941
ATOM   1854  C   ALA A 129     -25.117  22.087   3.478  1.00 71.79           C  
ANISOU 1854  C   ALA A 129    10755   8958   7562  -2741   1585  -1072
ATOM   1855  O   ALA A 129     -25.246  21.110   2.744  1.00 71.92           O  
ANISOU 1855  O   ALA A 129    10869   8869   7587  -2736   1596  -1042
ATOM   1856  CB  ALA A 129     -25.138  21.741   5.978  1.00 74.20           C  
ANISOU 1856  CB  ALA A 129    11492   9224   7476  -3119   1596  -1017
ATOM   1857  H   ALA A 129     -23.543  23.640   5.788  1.00  0.00           H  
ATOM   1858  HA  ALA A 129     -23.623  21.069   4.620  1.00  0.00           H  
ATOM   1859  HB1 ALA A 129     -25.804  20.887   5.847  1.00  0.00           H  
ATOM   1860  HB2 ALA A 129     -24.533  21.543   6.863  1.00  0.00           H  
ATOM   1861  HB3 ALA A 129     -25.758  22.615   6.185  1.00  0.00           H  
ATOM   1862  N   ALA A 130     -25.646  23.298   3.228  1.00 72.72           N  
ANISOU 1862  N   ALA A 130    10575   9263   7793  -2714   1665  -1211
ATOM   1863  CA  ALA A 130     -26.399  23.638   2.023  1.00 72.70           C  
ANISOU 1863  CA  ALA A 130    10315   9370   7936  -2670   1738  -1316
ATOM   1864  C   ALA A 130     -25.550  23.602   0.744  1.00 71.53           C  
ANISOU 1864  C   ALA A 130    10105   9140   7933  -2436   1624  -1227
ATOM   1865  O   ALA A 130     -26.047  23.126  -0.274  1.00 71.72           O  
ANISOU 1865  O   ALA A 130    10112   9157   7981  -2463   1657  -1251
ATOM   1866  CB  ALA A 130     -27.048  25.014   2.198  1.00 72.99           C  
ANISOU 1866  CB  ALA A 130    10066   9582   8084  -2639   1811  -1455
ATOM   1867  H   ALA A 130     -25.500  24.051   3.888  1.00  0.00           H  
ATOM   1868  HA  ALA A 130     -27.193  22.898   1.912  1.00  0.00           H  
ATOM   1869  HB1 ALA A 130     -27.663  25.262   1.334  1.00  0.00           H  
ATOM   1870  HB2 ALA A 130     -27.693  25.027   3.074  1.00  0.00           H  
ATOM   1871  HB3 ALA A 130     -26.307  25.805   2.319  1.00  0.00           H  
ATOM   1872  N   GLY A 131     -24.288  24.060   0.836  1.00 64.22           N  
ANISOU 1872  N   GLY A 131     9159   8160   7084  -2240   1499  -1132
ATOM   1873  CA  GLY A 131     -23.302  24.033  -0.245  1.00 63.15           C  
ANISOU 1873  CA  GLY A 131     8955   7958   7079  -2025   1415  -1057
ATOM   1874  C   GLY A 131     -22.955  22.600  -0.648  1.00 63.66           C  
ANISOU 1874  C   GLY A 131     9241   7852   7094  -2015   1415   -989
ATOM   1875  O   GLY A 131     -22.996  22.273  -1.833  1.00 63.46           O  
ANISOU 1875  O   GLY A 131     9188   7806   7118  -1985   1459  -1022
ATOM   1876  H   GLY A 131     -23.976  24.444   1.718  1.00  0.00           H  
ATOM   1877  HA3 GLY A 131     -22.389  24.513   0.103  1.00  0.00           H  
ATOM   1878  HA2 GLY A 131     -23.655  24.588  -1.110  1.00  0.00           H  
ATOM   1879  N   ALA A 132     -22.640  21.753   0.346  1.00 65.98           N  
ANISOU 1879  N   ALA A 132     9788   8013   7270  -2071   1372   -902
ATOM   1880  CA  ALA A 132     -22.305  20.341   0.176  1.00 66.50           C  
ANISOU 1880  CA  ALA A 132    10126   7858   7283  -2054   1364   -826
ATOM   1881  C   ALA A 132     -23.471  19.494  -0.360  1.00 67.67           C  
ANISOU 1881  C   ALA A 132    10388   7985   7339  -2265   1503   -924
ATOM   1882  O   ALA A 132     -23.226  18.596  -1.165  1.00 67.86           O  
ANISOU 1882  O   ALA A 132    10533   7862   7388  -2206   1532   -920
ATOM   1883  CB  ALA A 132     -21.795  19.786   1.513  1.00 68.87           C  
ANISOU 1883  CB  ALA A 132    10694   8024   7451  -2106   1265   -697
ATOM   1884  H   ALA A 132     -22.621  22.099   1.298  1.00  0.00           H  
ATOM   1885  HA  ALA A 132     -21.494  20.284  -0.551  1.00  0.00           H  
ATOM   1886  HB1 ALA A 132     -21.524  18.733   1.428  1.00  0.00           H  
ATOM   1887  HB2 ALA A 132     -20.907  20.326   1.844  1.00  0.00           H  
ATOM   1888  HB3 ALA A 132     -22.547  19.875   2.298  1.00  0.00           H  
ATOM   1889  N   THR A 133     -24.708  19.815   0.063  1.00 73.29           N  
ANISOU 1889  N   THR A 133    11052   8848   7945  -2518   1598  -1024
ATOM   1890  CA  THR A 133     -25.926  19.170  -0.427  1.00 74.46           C  
ANISOU 1890  CA  THR A 133    11260   9026   8006  -2757   1721  -1124
ATOM   1891  C   THR A 133     -26.205  19.537  -1.894  1.00 73.96           C  
ANISOU 1891  C   THR A 133    10969   9061   8070  -2672   1735  -1195
ATOM   1892  O   THR A 133     -26.375  18.628  -2.700  1.00 74.54           O  
ANISOU 1892  O   THR A 133    11193   9021   8107  -2722   1771  -1208
ATOM   1893  CB  THR A 133     -27.182  19.517   0.415  1.00 67.21           C  
ANISOU 1893  CB  THR A 133    10262   8297   6978  -3032   1829  -1230
ATOM   1894  OG1 THR A 133     -26.978  19.119   1.755  1.00 68.07           O  
ANISOU 1894  OG1 THR A 133    10601   8327   6936  -3137   1818  -1163
ATOM   1895  CG2 THR A 133     -28.473  18.825  -0.055  1.00 68.53           C  
ANISOU 1895  CG2 THR A 133    10468   8522   7049  -3313   1947  -1328
ATOM   1896  H   THR A 133     -24.829  20.562   0.733  1.00  0.00           H  
ATOM   1897  HA  THR A 133     -25.773  18.090  -0.375  1.00  0.00           H  
ATOM   1898  HB  THR A 133     -27.341  20.597   0.421  1.00  0.00           H  
ATOM   1899  HG1 THR A 133     -26.282  19.667   2.134  1.00  0.00           H  
ATOM   1900 HG21 THR A 133     -29.284  19.006   0.649  1.00  0.00           H  
ATOM   1901 HG22 THR A 133     -28.800  19.188  -1.028  1.00  0.00           H  
ATOM   1902 HG23 THR A 133     -28.336  17.746  -0.129  1.00  0.00           H  
ATOM   1903  N   SER A 134     -26.192  20.842  -2.225  1.00 73.56           N  
ANISOU 1903  N   SER A 134    10591   9203   8154  -2556   1703  -1239
ATOM   1904  CA  SER A 134     -26.420  21.359  -3.580  1.00 73.18           C  
ANISOU 1904  CA  SER A 134    10343   9254   8209  -2492   1688  -1284
ATOM   1905  C   SER A 134     -25.422  20.808  -4.606  1.00 73.34           C  
ANISOU 1905  C   SER A 134    10513   9099   8254  -2348   1666  -1228
ATOM   1906  O   SER A 134     -25.833  20.471  -5.715  1.00 73.35           O  
ANISOU 1906  O   SER A 134    10583   9082   8206  -2451   1710  -1276
ATOM   1907  CB  SER A 134     -26.346  22.891  -3.574  1.00 80.88           C  
ANISOU 1907  CB  SER A 134    11011  10389   9332  -2341   1627  -1298
ATOM   1908  OG  SER A 134     -27.375  23.404  -2.764  1.00 81.28           O  
ANISOU 1908  OG  SER A 134    10923  10582   9379  -2444   1675  -1374
ATOM   1909  H   SER A 134     -26.022  21.538  -1.510  1.00  0.00           H  
ATOM   1910  HA  SER A 134     -27.421  21.054  -3.889  1.00  0.00           H  
ATOM   1911  HB3 SER A 134     -26.473  23.296  -4.578  1.00  0.00           H  
ATOM   1912  HB2 SER A 134     -25.381  23.237  -3.201  1.00  0.00           H  
ATOM   1913  HG  SER A 134     -27.050  23.441  -1.858  1.00  0.00           H  
ATOM   1914  N   LEU A 135     -24.152  20.677  -4.181  1.00 66.43           N  
ANISOU 1914  N   LEU A 135     9705   8092   7442  -2132   1609  -1134
ATOM   1915  CA  LEU A 135     -23.069  20.045  -4.927  1.00 66.21           C  
ANISOU 1915  CA  LEU A 135     9780   7900   7476  -1946   1611  -1092
ATOM   1916  C   LEU A 135     -23.377  18.578  -5.246  1.00 67.51           C  
ANISOU 1916  C   LEU A 135    10259   7859   7531  -2056   1692  -1114
ATOM   1917  O   LEU A 135     -23.261  18.188  -6.402  1.00 68.10           O  
ANISOU 1917  O   LEU A 135    10401   7862   7613  -2033   1759  -1165
ATOM   1918  CB  LEU A 135     -21.750  20.173  -4.143  1.00 63.81           C  
ANISOU 1918  CB  LEU A 135     9460   7516   7269  -1709   1520   -982
ATOM   1919  CG  LEU A 135     -20.503  19.843  -4.988  1.00 63.34           C  
ANISOU 1919  CG  LEU A 135     9425   7323   7319  -1480   1537   -954
ATOM   1920  CD1 LEU A 135     -20.157  20.988  -5.946  1.00 62.99           C  
ANISOU 1920  CD1 LEU A 135     9125   7435   7374  -1396   1548   -993
ATOM   1921  CD2 LEU A 135     -19.302  19.474  -4.112  1.00 62.56           C  
ANISOU 1921  CD2 LEU A 135     9368   7109   7295  -1280   1436   -832
ATOM   1922  H   LEU A 135     -23.912  20.998  -3.252  1.00  0.00           H  
ATOM   1923  HA  LEU A 135     -22.962  20.573  -5.873  1.00  0.00           H  
ATOM   1924  HB3 LEU A 135     -21.800  19.522  -3.269  1.00  0.00           H  
ATOM   1925  HB2 LEU A 135     -21.648  21.181  -3.746  1.00  0.00           H  
ATOM   1926  HG  LEU A 135     -20.702  18.962  -5.594  1.00  0.00           H  
ATOM   1927 HD11 LEU A 135     -19.081  21.069  -6.067  1.00  0.00           H  
ATOM   1928 HD12 LEU A 135     -20.593  20.818  -6.930  1.00  0.00           H  
ATOM   1929 HD13 LEU A 135     -20.519  21.952  -5.588  1.00  0.00           H  
ATOM   1930 HD21 LEU A 135     -18.724  18.662  -4.555  1.00  0.00           H  
ATOM   1931 HD22 LEU A 135     -18.634  20.323  -3.988  1.00  0.00           H  
ATOM   1932 HD23 LEU A 135     -19.609  19.150  -3.120  1.00  0.00           H  
ATOM   1933  N   LEU A 136     -23.812  17.810  -4.235  1.00 66.79           N  
ANISOU 1933  N   LEU A 136    10389   7670   7319  -2211   1700  -1086
ATOM   1934  CA  LEU A 136     -24.202  16.407  -4.378  1.00 67.94           C  
ANISOU 1934  CA  LEU A 136    10888   7585   7340  -2351   1777  -1102
ATOM   1935  C   LEU A 136     -25.343  16.181  -5.394  1.00 68.43           C  
ANISOU 1935  C   LEU A 136    10937   7748   7316  -2593   1869  -1229
ATOM   1936  O   LEU A 136     -25.358  15.128  -6.025  1.00 69.11           O  
ANISOU 1936  O   LEU A 136    11267   7647   7343  -2642   1944  -1270
ATOM   1937  CB  LEU A 136     -24.514  15.832  -2.976  1.00 68.31           C  
ANISOU 1937  CB  LEU A 136    11176   7542   7239  -2538   1764  -1043
ATOM   1938  CG  LEU A 136     -24.779  14.312  -2.910  1.00 69.08           C  
ANISOU 1938  CG  LEU A 136    11704   7344   7199  -2679   1822  -1026
ATOM   1939  CD1 LEU A 136     -23.532  13.488  -3.297  1.00 69.28           C  
ANISOU 1939  CD1 LEU A 136    11926   7060   7336  -2359   1773   -931
ATOM   1940  CD2 LEU A 136     -25.316  13.924  -1.521  1.00 69.60           C  
ANISOU 1940  CD2 LEU A 136    11973   7382   7089  -2926   1814   -975
ATOM   1941  H   LEU A 136     -23.902  18.206  -3.309  1.00  0.00           H  
ATOM   1942  HA  LEU A 136     -23.326  15.890  -4.771  1.00  0.00           H  
ATOM   1943  HB3 LEU A 136     -25.384  16.344  -2.568  1.00  0.00           H  
ATOM   1944  HB2 LEU A 136     -23.690  16.070  -2.301  1.00  0.00           H  
ATOM   1945  HG  LEU A 136     -25.570  14.056  -3.614  1.00  0.00           H  
ATOM   1946 HD11 LEU A 136     -23.258  12.762  -2.532  1.00  0.00           H  
ATOM   1947 HD12 LEU A 136     -23.706  12.937  -4.222  1.00  0.00           H  
ATOM   1948 HD13 LEU A 136     -22.656  14.115  -3.458  1.00  0.00           H  
ATOM   1949 HD21 LEU A 136     -25.140  12.873  -1.289  1.00  0.00           H  
ATOM   1950 HD22 LEU A 136     -24.854  14.518  -0.732  1.00  0.00           H  
ATOM   1951 HD23 LEU A 136     -26.393  14.088  -1.467  1.00  0.00           H  
ATOM   1952  N   PHE A 137     -26.234  17.171  -5.581  1.00 71.93           N  
ANISOU 1952  N   PHE A 137    11091   8477   7760  -2732   1855  -1290
ATOM   1953  CA  PHE A 137     -27.287  17.141  -6.598  1.00 72.73           C  
ANISOU 1953  CA  PHE A 137    11143   8712   7781  -2976   1900  -1392
ATOM   1954  C   PHE A 137     -26.833  17.558  -8.014  1.00 72.29           C  
ANISOU 1954  C   PHE A 137    10951   8723   7793  -2868   1878  -1423
ATOM   1955  O   PHE A 137     -27.297  16.940  -8.972  1.00 73.22           O  
ANISOU 1955  O   PHE A 137    11192   8825   7801  -3058   1923  -1493
ATOM   1956  CB  PHE A 137     -28.505  17.971  -6.133  1.00 74.25           C  
ANISOU 1956  CB  PHE A 137    11052   9193   7966  -3156   1883  -1441
ATOM   1957  CG  PHE A 137     -29.420  17.266  -5.144  1.00 75.32           C  
ANISOU 1957  CG  PHE A 137    11348   9319   7951  -3441   1960  -1470
ATOM   1958  CD1 PHE A 137     -30.352  16.310  -5.598  1.00 76.71           C  
ANISOU 1958  CD1 PHE A 137    11580   9577   7988  -3785   2023  -1556
ATOM   1959  CD2 PHE A 137     -29.259  17.447  -3.755  1.00 75.18           C  
ANISOU 1959  CD2 PHE A 137    11420   9234   7910  -3404   1968  -1412
ATOM   1960  CE1 PHE A 137     -31.126  15.603  -4.686  1.00 77.82           C  
ANISOU 1960  CE1 PHE A 137    11859   9734   7976  -4093   2114  -1590
ATOM   1961  CE2 PHE A 137     -30.027  16.719  -2.857  1.00 76.38           C  
ANISOU 1961  CE2 PHE A 137    11735   9393   7895  -3710   2055  -1441
ATOM   1962  CZ  PHE A 137     -30.962  15.804  -3.321  1.00 77.65           C  
ANISOU 1962  CZ  PHE A 137    11941   9638   7925  -4054   2138  -1533
ATOM   1963  H   PHE A 137     -26.166  18.012  -5.025  1.00  0.00           H  
ATOM   1964  HA  PHE A 137     -27.632  16.110  -6.698  1.00  0.00           H  
ATOM   1965  HB3 PHE A 137     -29.118  18.248  -6.992  1.00  0.00           H  
ATOM   1966  HB2 PHE A 137     -28.168  18.912  -5.696  1.00  0.00           H  
ATOM   1967  HD1 PHE A 137     -30.469  16.126  -6.656  1.00  0.00           H  
ATOM   1968  HD2 PHE A 137     -28.563  18.177  -3.387  1.00  0.00           H  
ATOM   1969  HE1 PHE A 137     -31.848  14.881  -5.040  1.00  0.00           H  
ATOM   1970  HE2 PHE A 137     -29.908  16.874  -1.795  1.00  0.00           H  
ATOM   1971  HZ  PHE A 137     -31.561  15.243  -2.619  1.00  0.00           H  
ATOM   1972  N   VAL A 138     -25.988  18.600  -8.137  1.00 76.86           N  
ANISOU 1972  N   VAL A 138    11296   9383   8525  -2609   1809  -1374
ATOM   1973  CA  VAL A 138     -25.722  19.281  -9.416  1.00 76.54           C  
ANISOU 1973  CA  VAL A 138    11121   9434   8528  -2543   1783  -1394
ATOM   1974  C   VAL A 138     -24.354  18.945 -10.059  1.00 76.31           C  
ANISOU 1974  C   VAL A 138    11238   9209   8546  -2330   1854  -1385
ATOM   1975  O   VAL A 138     -24.155  19.291 -11.222  1.00 76.49           O  
ANISOU 1975  O   VAL A 138    11261   9267   8536  -2359   1885  -1431
ATOM   1976  CB  VAL A 138     -25.849  20.829  -9.238  1.00 76.30           C  
ANISOU 1976  CB  VAL A 138    10740   9629   8621  -2443   1671  -1356
ATOM   1977  CG1 VAL A 138     -24.622  21.515  -8.603  1.00 75.08           C  
ANISOU 1977  CG1 VAL A 138    10508   9423   8597  -2186   1640  -1282
ATOM   1978  CG2 VAL A 138     -26.232  21.557 -10.542  1.00 76.28           C  
ANISOU 1978  CG2 VAL A 138    10614   9751   8617  -2467   1613  -1365
ATOM   1979  H   VAL A 138     -25.639  19.061  -7.307  1.00  0.00           H  
ATOM   1980  HA  VAL A 138     -26.474  18.976 -10.146  1.00  0.00           H  
ATOM   1981  HB  VAL A 138     -26.678  20.992  -8.547  1.00  0.00           H  
ATOM   1982 HG11 VAL A 138     -24.864  22.529  -8.284  1.00  0.00           H  
ATOM   1983 HG12 VAL A 138     -24.271  20.970  -7.729  1.00  0.00           H  
ATOM   1984 HG13 VAL A 138     -23.788  21.588  -9.301  1.00  0.00           H  
ATOM   1985 HG21 VAL A 138     -26.438  22.611 -10.350  1.00  0.00           H  
ATOM   1986 HG22 VAL A 138     -25.441  21.514 -11.290  1.00  0.00           H  
ATOM   1987 HG23 VAL A 138     -27.133  21.130 -10.982  1.00  0.00           H  
ATOM   1988  N   TYR A 139     -23.428  18.300  -9.328  1.00 76.14           N  
ANISOU 1988  N   TYR A 139    11336   8995   8597  -2131   1879  -1331
ATOM   1989  CA  TYR A 139     -22.047  18.069  -9.778  1.00 76.16           C  
ANISOU 1989  CA  TYR A 139    11414   8832   8692  -1889   1951  -1328
ATOM   1990  C   TYR A 139     -21.918  17.175 -11.027  1.00 77.14           C  
ANISOU 1990  C   TYR A 139    11754   8833   8724  -1977   2094  -1439
ATOM   1991  O   TYR A 139     -21.106  17.488 -11.899  1.00 77.05           O  
ANISOU 1991  O   TYR A 139    11654   8865   8757  -1880   2153  -1478
ATOM   1992  CB  TYR A 139     -21.201  17.545  -8.605  1.00 74.18           C  
ANISOU 1992  CB  TYR A 139    11312   8360   8513  -1700   1937  -1248
ATOM   1993  CG  TYR A 139     -19.713  17.462  -8.863  1.00 74.25           C  
ANISOU 1993  CG  TYR A 139    11243   8278   8691  -1382   1966  -1220
ATOM   1994  CD1 TYR A 139     -18.899  18.569  -8.560  1.00 73.56           C  
ANISOU 1994  CD1 TYR A 139    10866   8344   8739  -1209   1862  -1138
ATOM   1995  CD2 TYR A 139     -19.141  16.299  -9.411  1.00 75.13           C  
ANISOU 1995  CD2 TYR A 139    11562   8150   8834  -1258   2107  -1285
ATOM   1996  CE1 TYR A 139     -17.517  18.513  -8.795  1.00 73.68           C  
ANISOU 1996  CE1 TYR A 139    10761   8313   8919   -935   1889  -1116
ATOM   1997  CE2 TYR A 139     -17.753  16.238  -9.643  1.00 75.23           C  
ANISOU 1997  CE2 TYR A 139    11454   8098   9031   -945   2152  -1273
ATOM   1998  CZ  TYR A 139     -16.942  17.344  -9.324  1.00 74.51           C  
ANISOU 1998  CZ  TYR A 139    11034   8199   9076   -791   2037  -1184
ATOM   1999  OH  TYR A 139     -15.600  17.295  -9.537  1.00 74.68           O  
ANISOU 1999  OH  TYR A 139    10889   8198   9287   -504   2077  -1174
ATOM   2000  H   TYR A 139     -23.633  18.049  -8.369  1.00  0.00           H  
ATOM   2001  HA  TYR A 139     -21.645  19.047 -10.052  1.00  0.00           H  
ATOM   2002  HB3 TYR A 139     -21.569  16.578  -8.258  1.00  0.00           H  
ATOM   2003  HB2 TYR A 139     -21.303  18.232  -7.770  1.00  0.00           H  
ATOM   2004  HD1 TYR A 139     -19.330  19.474  -8.165  1.00  0.00           H  
ATOM   2005  HD2 TYR A 139     -19.780  15.467  -9.666  1.00  0.00           H  
ATOM   2006  HE1 TYR A 139     -16.907  19.376  -8.583  1.00  0.00           H  
ATOM   2007  HE2 TYR A 139     -17.315  15.349 -10.070  1.00  0.00           H  
ATOM   2008  HH  TYR A 139     -15.307  16.487  -9.972  1.00  0.00           H  
ATOM   2009  N   SER A 140     -22.737  16.113 -11.113  1.00 81.27           N  
ANISOU 2009  N   SER A 140    12577   9201   9102  -2183   2163  -1499
ATOM   2010  CA  SER A 140     -22.827  15.234 -12.283  1.00 82.69           C  
ANISOU 2010  CA  SER A 140    13017   9235   9168  -2295   2315  -1625
ATOM   2011  C   SER A 140     -23.340  15.944 -13.548  1.00 82.75           C  
ANISOU 2011  C   SER A 140    12875   9487   9079  -2479   2296  -1683
ATOM   2012  O   SER A 140     -22.871  15.625 -14.640  1.00 83.41           O  
ANISOU 2012  O   SER A 140    13044   9518   9131  -2452   2417  -1767
ATOM   2013  CB  SER A 140     -23.677  14.000 -11.931  1.00 86.90           C  
ANISOU 2013  CB  SER A 140    13915   9569   9536  -2546   2375  -1678
ATOM   2014  OG  SER A 140     -25.014  14.339 -11.619  1.00 86.08           O  
ANISOU 2014  OG  SER A 140    13719   9698   9292  -2884   2287  -1687
ATOM   2015  H   SER A 140     -23.392  15.922 -10.367  1.00  0.00           H  
ATOM   2016  HA  SER A 140     -21.817  14.882 -12.500  1.00  0.00           H  
ATOM   2017  HB3 SER A 140     -23.231  13.465 -11.096  1.00  0.00           H  
ATOM   2018  HB2 SER A 140     -23.699  13.310 -12.774  1.00  0.00           H  
ATOM   2019  HG  SER A 140     -25.477  13.545 -11.342  1.00  0.00           H  
ATOM   2020  N   LEU A 141     -24.263  16.907 -13.371  1.00 79.50           N  
ANISOU 2020  N   LEU A 141    12235   9342   8630  -2653   2144  -1636
ATOM   2021  CA  LEU A 141     -24.803  17.750 -14.435  1.00 79.28           C  
ANISOU 2021  CA  LEU A 141    12051   9550   8523  -2811   2070  -1652
ATOM   2022  C   LEU A 141     -23.740  18.708 -14.992  1.00 78.65           C  
ANISOU 2022  C   LEU A 141    11799   9532   8551  -2589   2076  -1618
ATOM   2023  O   LEU A 141     -23.654  18.837 -16.211  1.00 79.20           O  
ANISOU 2023  O   LEU A 141    11921   9653   8516  -2692   2116  -1668
ATOM   2024  CB  LEU A 141     -26.056  18.497 -13.919  1.00 78.16           C  
ANISOU 2024  CB  LEU A 141    11647   9664   8387  -2954   1893  -1591
ATOM   2025  CG  LEU A 141     -26.826  19.323 -14.976  1.00 79.34           C  
ANISOU 2025  CG  LEU A 141    11643  10047   8455  -3129   1765  -1582
ATOM   2026  CD1 LEU A 141     -27.536  18.421 -16.010  1.00 78.57           C  
ANISOU 2026  CD1 LEU A 141    11747   9964   8140  -3482   1780  -1665
ATOM   2027  CD2 LEU A 141     -27.783  20.331 -14.302  1.00 80.62           C  
ANISOU 2027  CD2 LEU A 141    11440  10442   8750  -3068   1586  -1495
ATOM   2028  H   LEU A 141     -24.592  17.104 -12.436  1.00  0.00           H  
ATOM   2029  HA  LEU A 141     -25.106  17.093 -15.251  1.00  0.00           H  
ATOM   2030  HB3 LEU A 141     -25.748  19.172 -13.123  1.00  0.00           H  
ATOM   2031  HB2 LEU A 141     -26.742  17.788 -13.452  1.00  0.00           H  
ATOM   2032  HG  LEU A 141     -26.106  19.929 -15.524  1.00  0.00           H  
ATOM   2033 HD11 LEU A 141     -27.120  18.580 -17.006  1.00  0.00           H  
ATOM   2034 HD12 LEU A 141     -27.418  17.362 -15.779  1.00  0.00           H  
ATOM   2035 HD13 LEU A 141     -28.607  18.609 -16.076  1.00  0.00           H  
ATOM   2036 HD21 LEU A 141     -28.802  20.273 -14.681  1.00  0.00           H  
ATOM   2037 HD22 LEU A 141     -27.843  20.179 -13.224  1.00  0.00           H  
ATOM   2038 HD23 LEU A 141     -27.440  21.355 -14.458  1.00  0.00           H  
ATOM   2039  N   ASP A 142     -22.930  19.318 -14.107  1.00 83.60           N  
ANISOU 2039  N   ASP A 142    12242  10160   9364  -2320   2040  -1538
ATOM   2040  CA  ASP A 142     -21.807  20.188 -14.469  1.00 83.38           C  
ANISOU 2040  CA  ASP A 142    12042  10199   9439  -2136   2049  -1505
ATOM   2041  C   ASP A 142     -20.751  19.441 -15.308  1.00 83.98           C  
ANISOU 2041  C   ASP A 142    12297  10112   9501  -2051   2255  -1603
ATOM   2042  O   ASP A 142     -20.342  19.958 -16.347  1.00 84.28           O  
ANISOU 2042  O   ASP A 142    12295  10236   9491  -2086   2311  -1637
ATOM   2043  CB  ASP A 142     -21.171  20.854 -13.227  1.00 90.38           C  
ANISOU 2043  CB  ASP A 142    12715  11112  10515  -1898   1965  -1406
ATOM   2044  CG  ASP A 142     -20.088  21.885 -13.573  1.00 90.56           C  
ANISOU 2044  CG  ASP A 142    12545  11222  10640  -1742   1968  -1369
ATOM   2045  OD1 ASP A 142     -20.431  22.851 -14.289  1.00 90.70           O  
ANISOU 2045  OD1 ASP A 142    12441  11405  10618  -1843   1884  -1339
ATOM   2046  OD2 ASP A 142     -18.955  21.712 -13.074  1.00 90.49           O1-
ANISOU 2046  OD2 ASP A 142    12506  11121  10755  -1527   2045  -1364
ATOM   2047  H   ASP A 142     -23.071  19.162 -13.117  1.00  0.00           H  
ATOM   2048  HA  ASP A 142     -22.222  20.979 -15.097  1.00  0.00           H  
ATOM   2049  HB3 ASP A 142     -20.729  20.090 -12.586  1.00  0.00           H  
ATOM   2050  HB2 ASP A 142     -21.927  21.342 -12.611  1.00  0.00           H  
ATOM   2051  N   TYR A 143     -20.386  18.221 -14.869  1.00 81.30           N  
ANISOU 2051  N   TYR A 143    12171   9527   9191  -1951   2375  -1654
ATOM   2052  CA  TYR A 143     -19.510  17.295 -15.588  1.00 82.82           C  
ANISOU 2052  CA  TYR A 143    12550   9524   9395  -1837   2603  -1775
ATOM   2053  C   TYR A 143     -20.036  16.938 -16.992  1.00 84.36           C  
ANISOU 2053  C   TYR A 143    12958   9734   9362  -2118   2722  -1908
ATOM   2054  O   TYR A 143     -19.269  17.001 -17.952  1.00 85.34           O  
ANISOU 2054  O   TYR A 143    13077   9880   9466  -2087   2875  -1993
ATOM   2055  CB  TYR A 143     -19.259  16.041 -14.715  1.00 87.92           C  
ANISOU 2055  CB  TYR A 143    13436   9862  10106  -1693   2678  -1794
ATOM   2056  CG  TYR A 143     -18.564  14.881 -15.414  1.00 90.26           C  
ANISOU 2056  CG  TYR A 143    13998   9897  10399  -1601   2935  -1950
ATOM   2057  CD1 TYR A 143     -17.156  14.831 -15.477  1.00 90.94           C  
ANISOU 2057  CD1 TYR A 143    13969   9886  10698  -1255   3062  -1977
ATOM   2058  CD2 TYR A 143     -19.327  13.866 -16.030  1.00 91.96           C  
ANISOU 2058  CD2 TYR A 143    14583   9948  10409  -1855   3055  -2080
ATOM   2059  CE1 TYR A 143     -16.516  13.777 -16.157  1.00 93.31           C  
ANISOU 2059  CE1 TYR A 143    14503   9925  11026  -1132   3327  -2143
ATOM   2060  CE2 TYR A 143     -18.688  12.819 -16.719  1.00 94.38           C  
ANISOU 2060  CE2 TYR A 143    15173   9972  10714  -1763   3317  -2247
ATOM   2061  CZ  TYR A 143     -17.282  12.772 -16.782  1.00 95.06           C  
ANISOU 2061  CZ  TYR A 143    15129   9954  11034  -1382   3464  -2284
ATOM   2062  OH  TYR A 143     -16.660  11.745 -17.429  1.00 97.75           O  
ANISOU 2062  OH  TYR A 143    15733  10002  11404  -1253   3750  -2470
ATOM   2063  H   TYR A 143     -20.765  17.884 -13.994  1.00  0.00           H  
ATOM   2064  HA  TYR A 143     -18.552  17.802 -15.719  1.00  0.00           H  
ATOM   2065  HB3 TYR A 143     -20.209  15.664 -14.335  1.00  0.00           H  
ATOM   2066  HB2 TYR A 143     -18.685  16.317 -13.829  1.00  0.00           H  
ATOM   2067  HD1 TYR A 143     -16.565  15.604 -15.008  1.00  0.00           H  
ATOM   2068  HD2 TYR A 143     -20.406  13.895 -15.986  1.00  0.00           H  
ATOM   2069  HE1 TYR A 143     -15.438  13.745 -16.197  1.00  0.00           H  
ATOM   2070  HE2 TYR A 143     -19.284  12.047 -17.181  1.00  0.00           H  
ATOM   2071  HH  TYR A 143     -15.724  11.692 -17.223  1.00  0.00           H  
ATOM   2072  N   ALA A 144     -21.328  16.575 -17.077  1.00 85.82           N  
ANISOU 2072  N   ALA A 144    13329   9917   9360  -2416   2658  -1932
ATOM   2073  CA  ALA A 144     -21.975  16.138 -18.312  1.00 86.63           C  
ANISOU 2073  CA  ALA A 144    13665  10041   9208  -2742   2732  -2049
ATOM   2074  C   ALA A 144     -22.140  17.261 -19.350  1.00 86.21           C  
ANISOU 2074  C   ALA A 144    13434  10261   9061  -2882   2634  -2009
ATOM   2075  O   ALA A 144     -21.881  17.016 -20.528  1.00 87.23           O  
ANISOU 2075  O   ALA A 144    13727  10375   9043  -3001   2788  -2119
ATOM   2076  CB  ALA A 144     -23.315  15.466 -17.985  1.00 86.98           C  
ANISOU 2076  CB  ALA A 144    13879  10078   9092  -3046   2637  -2056
ATOM   2077  H   ALA A 144     -21.893  16.540 -16.239  1.00  0.00           H  
ATOM   2078  HA  ALA A 144     -21.324  15.380 -18.742  1.00  0.00           H  
ATOM   2079  HB1 ALA A 144     -23.766  15.032 -18.877  1.00  0.00           H  
ATOM   2080  HB2 ALA A 144     -23.181  14.654 -17.269  1.00  0.00           H  
ATOM   2081  HB3 ALA A 144     -24.027  16.173 -17.555  1.00  0.00           H  
ATOM   2082  N   ARG A 145     -22.511  18.473 -18.891  1.00 86.49           N  
ANISOU 2082  N   ARG A 145    13162  10527   9175  -2866   2394  -1856
ATOM   2083  CA  ARG A 145     -22.566  19.696 -19.701  1.00 86.08           C  
ANISOU 2083  CA  ARG A 145    12955  10704   9049  -2975   2267  -1786
ATOM   2084  C   ARG A 145     -21.188  20.091 -20.255  1.00 86.50           C  
ANISOU 2084  C   ARG A 145    12984  10737   9145  -2827   2438  -1828
ATOM   2085  O   ARG A 145     -21.114  20.480 -21.419  1.00 87.44           O  
ANISOU 2085  O   ARG A 145    13208  10937   9077  -3023   2482  -1868
ATOM   2086  CB  ARG A 145     -23.139  20.869 -18.877  1.00 99.35           C  
ANISOU 2086  CB  ARG A 145    14314  12567  10866  -2898   2011  -1626
ATOM   2087  CG  ARG A 145     -24.650  20.805 -18.598  1.00 99.36           C  
ANISOU 2087  CG  ARG A 145    14266  12673  10812  -3089   1831  -1587
ATOM   2088  CD  ARG A 145     -25.138  22.094 -17.910  1.00 98.05           C  
ANISOU 2088  CD  ARG A 145    13768  12698  10789  -2997   1597  -1446
ATOM   2089  NE  ARG A 145     -26.502  21.992 -17.368  1.00 97.89           N  
ANISOU 2089  NE  ARG A 145    13618  12783  10791  -3103   1459  -1423
ATOM   2090  CZ  ARG A 145     -27.644  21.797 -18.050  1.00 98.76           C  
ANISOU 2090  CZ  ARG A 145    13742  13028  10754  -3382   1338  -1430
ATOM   2091  NH1 ARG A 145     -27.660  21.664 -19.383  1.00 99.82           N  
ANISOU 2091  NH1 ARG A 145    14055  13194  10677  -3602   1323  -1453
ATOM   2092  NH2 ARG A 145     -28.800  21.746 -17.375  1.00 98.65           N1+
ANISOU 2092  NH2 ARG A 145    13558  13134  10792  -3464   1237  -1420
ATOM   2093  H   ARG A 145     -22.715  18.586 -17.906  1.00  0.00           H  
ATOM   2094  HA  ARG A 145     -23.226  19.504 -20.549  1.00  0.00           H  
ATOM   2095  HB3 ARG A 145     -22.951  21.803 -19.412  1.00  0.00           H  
ATOM   2096  HB2 ARG A 145     -22.593  20.953 -17.935  1.00  0.00           H  
ATOM   2097  HG3 ARG A 145     -24.964  19.911 -18.060  1.00  0.00           H  
ATOM   2098  HG2 ARG A 145     -25.123  20.741 -19.577  1.00  0.00           H  
ATOM   2099  HD3 ARG A 145     -25.210  22.882 -18.661  1.00  0.00           H  
ATOM   2100  HD2 ARG A 145     -24.427  22.449 -17.164  1.00  0.00           H  
ATOM   2101  HE  ARG A 145     -26.565  22.080 -16.364  1.00  0.00           H  
ATOM   2102 HH12 ARG A 145     -28.529  21.524 -19.878  1.00  0.00           H  
ATOM   2103 HH11 ARG A 145     -26.796  21.713 -19.902  1.00  0.00           H  
ATOM   2104 HH22 ARG A 145     -29.673  21.605 -17.863  1.00  0.00           H  
ATOM   2105 HH21 ARG A 145     -28.812  21.861 -16.372  1.00  0.00           H  
ATOM   2106  N   THR A 146     -20.136  19.966 -19.424  1.00 86.50           N  
ANISOU 2106  N   THR A 146    12852  10636   9378  -2503   2537  -1822
ATOM   2107  CA  THR A 146     -18.748  20.245 -19.797  1.00 86.89           C  
ANISOU 2107  CA  THR A 146    12822  10676   9514  -2332   2723  -1874
ATOM   2108  C   THR A 146     -18.241  19.288 -20.892  1.00 88.59           C  
ANISOU 2108  C   THR A 146    13324  10759   9578  -2437   3010  -2069
ATOM   2109  O   THR A 146     -17.706  19.778 -21.885  1.00 89.28           O  
ANISOU 2109  O   THR A 146    13431  10952   9542  -2563   3116  -2120
ATOM   2110  CB  THR A 146     -17.790  20.181 -18.575  1.00 94.82           C  
ANISOU 2110  CB  THR A 146    13642  11589  10796  -1980   2749  -1834
ATOM   2111  OG1 THR A 146     -18.108  21.236 -17.690  1.00 92.34           O  
ANISOU 2111  OG1 THR A 146    13070  11424  10592  -1921   2507  -1671
ATOM   2112  CG2 THR A 146     -16.284  20.278 -18.886  1.00 96.61           C  
ANISOU 2112  CG2 THR A 146    13778  11791  11139  -1787   2981  -1921
ATOM   2113  H   THR A 146     -20.286  19.647 -18.477  1.00  0.00           H  
ATOM   2114  HA  THR A 146     -18.717  21.258 -20.203  1.00  0.00           H  
ATOM   2115  HB  THR A 146     -17.961  19.255 -18.027  1.00  0.00           H  
ATOM   2116  HG1 THR A 146     -18.952  21.043 -17.268  1.00  0.00           H  
ATOM   2117 HG21 THR A 146     -15.701  20.364 -17.968  1.00  0.00           H  
ATOM   2118 HG22 THR A 146     -15.919  19.394 -19.409  1.00  0.00           H  
ATOM   2119 HG23 THR A 146     -16.063  21.151 -19.502  1.00  0.00           H  
ATOM   2120  N   ARG A 147     -18.461  17.967 -20.731  1.00 92.88           N  
ANISOU 2120  N   ARG A 147    14118  11062  10109  -2410   3143  -2182
ATOM   2121  CA  ARG A 147     -18.111  16.953 -21.734  1.00 95.20           C  
ANISOU 2121  CA  ARG A 147    14735  11175  10263  -2499   3446  -2397
ATOM   2122  C   ARG A 147     -18.818  17.158 -23.081  1.00 96.48           C  
ANISOU 2122  C   ARG A 147    15097  11471  10088  -2911   3451  -2459
ATOM   2123  O   ARG A 147     -18.166  17.003 -24.112  1.00 98.37           O  
ANISOU 2123  O   ARG A 147    15465  11705  10208  -2991   3700  -2608
ATOM   2124  CB  ARG A 147     -18.409  15.528 -21.214  1.00 95.52           C  
ANISOU 2124  CB  ARG A 147    15065  10914  10314  -2461   3526  -2480
ATOM   2125  CG  ARG A 147     -17.457  14.977 -20.135  1.00 95.62           C  
ANISOU 2125  CG  ARG A 147    15013  10694  10625  -2036   3646  -2494
ATOM   2126  CD  ARG A 147     -15.994  14.796 -20.583  1.00 98.15           C  
ANISOU 2126  CD  ARG A 147    15270  10954  11068  -1807   3948  -2643
ATOM   2127  NE  ARG A 147     -15.834  13.837 -21.690  1.00101.54           N  
ANISOU 2127  NE  ARG A 147    16079  11170  11332  -1935   4261  -2887
ATOM   2128  CZ  ARG A 147     -15.708  12.504 -21.581  1.00104.18           C  
ANISOU 2128  CZ  ARG A 147    16680  11144  11760  -1751   4447  -3012
ATOM   2129  NH1 ARG A 147     -15.784  11.889 -20.394  1.00103.80           N  
ANISOU 2129  NH1 ARG A 147    16564  10917  11959  -1441   4322  -2891
ATOM   2130  NH2 ARG A 147     -15.488  11.774 -22.682  1.00107.53           N1+
ANISOU 2130  NH2 ARG A 147    17470  11365  12019  -1886   4754  -3257
ATOM   2131  H   ARG A 147     -18.913  17.633 -19.890  1.00  0.00           H  
ATOM   2132  HA  ARG A 147     -17.045  17.059 -21.929  1.00  0.00           H  
ATOM   2133  HB3 ARG A 147     -18.392  14.826 -22.049  1.00  0.00           H  
ATOM   2134  HB2 ARG A 147     -19.430  15.501 -20.834  1.00  0.00           H  
ATOM   2135  HG3 ARG A 147     -17.844  13.994 -19.864  1.00  0.00           H  
ATOM   2136  HG2 ARG A 147     -17.494  15.563 -19.217  1.00  0.00           H  
ATOM   2137  HD3 ARG A 147     -15.331  14.581 -19.745  1.00  0.00           H  
ATOM   2138  HD2 ARG A 147     -15.634  15.741 -20.985  1.00  0.00           H  
ATOM   2139  HE  ARG A 147     -15.829  14.241 -22.615  1.00  0.00           H  
ATOM   2140 HH12 ARG A 147     -15.680  10.887 -20.323  1.00  0.00           H  
ATOM   2141 HH11 ARG A 147     -15.985  12.421 -19.559  1.00  0.00           H  
ATOM   2142 HH22 ARG A 147     -15.378  10.772 -22.618  1.00  0.00           H  
ATOM   2143 HH21 ARG A 147     -15.415  12.219 -23.586  1.00  0.00           H  
ATOM   2144  N   LEU A 148     -20.111  17.520 -23.050  1.00 97.93           N  
ANISOU 2144  N   LEU A 148    15297  11792  10122  -3178   3172  -2343
ATOM   2145  CA  LEU A 148     -20.913  17.769 -24.246  1.00 99.01           C  
ANISOU 2145  CA  LEU A 148    15608  12080   9931  -3592   3086  -2356
ATOM   2146  C   LEU A 148     -20.497  19.053 -24.989  1.00 98.84           C  
ANISOU 2146  C   LEU A 148    15439  12271   9844  -3649   3040  -2280
ATOM   2147  O   LEU A 148     -20.514  19.055 -26.218  1.00100.90           O  
ANISOU 2147  O   LEU A 148    15931  12570   9836  -3920   3165  -2379
ATOM   2148  CB  LEU A 148     -22.408  17.783 -23.861  1.00 96.78           C  
ANISOU 2148  CB  LEU A 148    15279  11926   9569  -3807   2764  -2225
ATOM   2149  CG  LEU A 148     -23.372  17.598 -25.052  1.00 96.44           C  
ANISOU 2149  CG  LEU A 148    15522  11949   9172  -4261   2706  -2287
ATOM   2150  CD1 LEU A 148     -23.193  16.231 -25.743  1.00 96.16           C  
ANISOU 2150  CD1 LEU A 148    15902  11647   8987  -4382   3013  -2523
ATOM   2151  CD2 LEU A 148     -24.824  17.803 -24.603  1.00 96.52           C  
ANISOU 2151  CD2 LEU A 148    15404  12114   9154  -4441   2387  -2158
ATOM   2152  H   LEU A 148     -20.584  17.622 -22.161  1.00  0.00           H  
ATOM   2153  HA  LEU A 148     -20.731  16.930 -24.920  1.00  0.00           H  
ATOM   2154  HB3 LEU A 148     -22.634  18.711 -23.334  1.00  0.00           H  
ATOM   2155  HB2 LEU A 148     -22.608  16.988 -23.143  1.00  0.00           H  
ATOM   2156  HG  LEU A 148     -23.165  18.376 -25.787  1.00  0.00           H  
ATOM   2157 HD11 LEU A 148     -24.145  15.758 -25.977  1.00  0.00           H  
ATOM   2158 HD12 LEU A 148     -22.652  16.341 -26.684  1.00  0.00           H  
ATOM   2159 HD13 LEU A 148     -22.633  15.531 -25.123  1.00  0.00           H  
ATOM   2160 HD21 LEU A 148     -25.491  17.908 -25.460  1.00  0.00           H  
ATOM   2161 HD22 LEU A 148     -25.164  16.956 -24.012  1.00  0.00           H  
ATOM   2162 HD23 LEU A 148     -24.933  18.697 -23.989  1.00  0.00           H  
ATOM   2163  N   ALA A 149     -20.104  20.098 -24.239  1.00 93.73           N  
ANISOU 2163  N   ALA A 149    14442  11749   9424  -3419   2872  -2110
ATOM   2164  CA  ALA A 149     -19.604  21.368 -24.769  1.00 93.36           C  
ANISOU 2164  CA  ALA A 149    14254  11881   9339  -3461   2815  -2016
ATOM   2165  C   ALA A 149     -18.225  21.240 -25.437  1.00 95.60           C  
ANISOU 2165  C   ALA A 149    14620  12116   9587  -3424   3176  -2184
ATOM   2166  O   ALA A 149     -18.017  21.837 -26.492  1.00 97.07           O  
ANISOU 2166  O   ALA A 149    14933  12414   9535  -3680   3231  -2203
ATOM   2167  CB  ALA A 149     -19.566  22.411 -23.644  1.00 91.48           C  
ANISOU 2167  CB  ALA A 149    13661  11724   9375  -3197   2614  -1839
ATOM   2168  H   ALA A 149     -20.136  20.023 -23.231  1.00  0.00           H  
ATOM   2169  HA  ALA A 149     -20.309  21.715 -25.526  1.00  0.00           H  
ATOM   2170  HB1 ALA A 149     -19.197  23.372 -24.006  1.00  0.00           H  
ATOM   2171  HB2 ALA A 149     -20.562  22.579 -23.234  1.00  0.00           H  
ATOM   2172  HB3 ALA A 149     -18.920  22.096 -22.823  1.00  0.00           H  
ATOM   2173  N   ASN A 150     -17.325  20.443 -24.834  1.00 99.88           N  
ANISOU 2173  N   ASN A 150    15089  12495  10364  -3110   3419  -2304
ATOM   2174  CA  ASN A 150     -15.998  20.125 -25.376  1.00101.74           C  
ANISOU 2174  CA  ASN A 150    15338  12686  10632  -3014   3790  -2487
ATOM   2175  C   ASN A 150     -16.092  19.252 -26.638  1.00104.04           C  
ANISOU 2175  C   ASN A 150    16025  12884  10623  -3296   4056  -2707
ATOM   2176  O   ASN A 150     -15.323  19.472 -27.574  1.00105.81           O  
ANISOU 2176  O   ASN A 150    16318  13174  10712  -3420   4317  -2837
ATOM   2177  CB  ASN A 150     -15.138  19.414 -24.303  1.00110.51           C  
ANISOU 2177  CB  ASN A 150    16269  13629  12092  -2582   3943  -2549
ATOM   2178  CG  ASN A 150     -14.829  20.260 -23.061  1.00107.58           C  
ANISOU 2178  CG  ASN A 150    15539  13340  11998  -2321   3690  -2347
ATOM   2179  OD1 ASN A 150     -14.919  21.486 -23.080  1.00105.96           O  
ANISOU 2179  OD1 ASN A 150    15143  13336  11783  -2398   3493  -2191
ATOM   2180  ND2 ASN A 150     -14.454  19.596 -21.966  1.00107.07           N  
ANISOU 2180  ND2 ASN A 150    15408  13100  12172  -2016   3688  -2344
ATOM   2181  H   ASN A 150     -17.564  20.007 -23.953  1.00  0.00           H  
ATOM   2182  HA  ASN A 150     -15.518  21.067 -25.648  1.00  0.00           H  
ATOM   2183  HB3 ASN A 150     -14.179  19.126 -24.736  1.00  0.00           H  
ATOM   2184  HB2 ASN A 150     -15.627  18.490 -23.989  1.00  0.00           H  
ATOM   2185 HD22 ASN A 150     -14.236  20.104 -21.122  1.00  0.00           H  
ATOM   2186 HD21 ASN A 150     -14.380  18.589 -21.976  1.00  0.00           H  
ATOM   2187  N   ASP A 151     -17.058  18.316 -26.652  1.00104.41           N  
ANISOU 2187  N   ASP A 151    16343  12779  10550  -3425   4007  -2760
ATOM   2188  CA  ASP A 151     -17.384  17.459 -27.792  1.00104.79           C  
ANISOU 2188  CA  ASP A 151    16817  12719  10279  -3740   4235  -2974
ATOM   2189  C   ASP A 151     -18.000  18.265 -28.956  1.00104.93           C  
ANISOU 2189  C   ASP A 151    16978  12968   9922  -4193   4080  -2899
ATOM   2190  O   ASP A 151     -17.731  17.945 -30.111  1.00105.21           O  
ANISOU 2190  O   ASP A 151    17307  12995   9673  -4464   4338  -3081
ATOM   2191  CB  ASP A 151     -18.316  16.300 -27.368  1.00104.27           C  
ANISOU 2191  CB  ASP A 151    16996  12447  10174  -3800   4170  -3018
ATOM   2192  CG  ASP A 151     -18.457  15.204 -28.426  1.00106.37           C  
ANISOU 2192  CG  ASP A 151    17727  12526  10161  -4062   4471  -3282
ATOM   2193  OD1 ASP A 151     -17.405  14.763 -28.936  1.00108.27           O  
ANISOU 2193  OD1 ASP A 151    18061  12586  10489  -3875   4867  -3506
ATOM   2194  OD2 ASP A 151     -19.602  14.750 -28.637  1.00106.71           O1-
ANISOU 2194  OD2 ASP A 151    18037  12604   9902  -4458   4314  -3274
ATOM   2195  H   ASP A 151     -17.637  18.192 -25.832  1.00  0.00           H  
ATOM   2196  HA  ASP A 151     -16.441  17.037 -28.143  1.00  0.00           H  
ATOM   2197  HB3 ASP A 151     -19.306  16.696 -27.140  1.00  0.00           H  
ATOM   2198  HB2 ASP A 151     -17.960  15.828 -26.453  1.00  0.00           H  
ATOM   2199  N   ALA A 152     -18.790  19.305 -28.636  1.00107.78           N  
ANISOU 2199  N   ALA A 152    17136  13531  10285  -4269   3659  -2630
ATOM   2200  CA  ALA A 152     -19.382  20.222 -29.608  1.00108.41           C  
ANISOU 2200  CA  ALA A 152    17321  13827  10043  -4659   3433  -2501
ATOM   2201  C   ALA A 152     -18.348  21.145 -30.275  1.00109.22           C  
ANISOU 2201  C   ALA A 152    17377  14048  10074  -4705   3603  -2512
ATOM   2202  O   ALA A 152     -18.489  21.414 -31.465  1.00111.52           O  
ANISOU 2202  O   ALA A 152    17944  14427  10001  -5087   3655  -2553
ATOM   2203  CB  ALA A 152     -20.498  21.038 -28.938  1.00105.96           C  
ANISOU 2203  CB  ALA A 152    16770  13667   9825  -4645   2957  -2219
ATOM   2204  H   ALA A 152     -18.997  19.489 -27.663  1.00  0.00           H  
ATOM   2205  HA  ALA A 152     -19.843  19.620 -30.393  1.00  0.00           H  
ATOM   2206  HB1 ALA A 152     -20.974  21.712 -29.651  1.00  0.00           H  
ATOM   2207  HB2 ALA A 152     -21.275  20.384 -28.542  1.00  0.00           H  
ATOM   2208  HB3 ALA A 152     -20.120  21.641 -28.114  1.00  0.00           H  
ATOM   2209  N   LYS A 153     -17.323  21.583 -29.520  1.00114.03           N  
ANISOU 2209  N   LYS A 153    17654  14665  11006  -4350   3696  -2480
ATOM   2210  CA  LYS A 153     -16.201  22.376 -30.033  1.00114.92           C  
ANISOU 2210  CA  LYS A 153    17684  14901  11081  -4391   3881  -2499
ATOM   2211  C   LYS A 153     -15.276  21.573 -30.959  1.00118.84           C  
ANISOU 2211  C   LYS A 153    18415  15321  11416  -4503   4370  -2804
ATOM   2212  O   LYS A 153     -14.873  22.106 -31.994  1.00121.07           O  
ANISOU 2212  O   LYS A 153    18889  15724  11388  -4841   4496  -2850
ATOM   2213  CB  LYS A 153     -15.399  22.990 -28.870  1.00118.64           C  
ANISOU 2213  CB  LYS A 153    17732  15405  11940  -4002   3863  -2407
ATOM   2214  CG  LYS A 153     -16.107  24.173 -28.196  1.00118.47           C  
ANISOU 2214  CG  LYS A 153    17510  15496  12006  -3975   3418  -2110
ATOM   2215  CD  LYS A 153     -15.276  24.759 -27.047  1.00118.47           C  
ANISOU 2215  CD  LYS A 153    17126  15531  12355  -3639   3400  -2027
ATOM   2216  CE  LYS A 153     -15.993  25.906 -26.324  1.00118.14           C  
ANISOU 2216  CE  LYS A 153    16903  15530  12454  -3540   2980  -1774
ATOM   2217  NZ  LYS A 153     -15.159  26.452 -25.239  1.00118.16           N1+
ANISOU 2217  NZ  LYS A 153    16571  15564  12760  -3257   2964  -1704
ATOM   2218  H   LYS A 153     -17.283  21.330 -28.542  1.00  0.00           H  
ATOM   2219  HA  LYS A 153     -16.619  23.193 -30.624  1.00  0.00           H  
ATOM   2220  HB3 LYS A 153     -14.443  23.358 -29.246  1.00  0.00           H  
ATOM   2221  HB2 LYS A 153     -15.156  22.220 -28.135  1.00  0.00           H  
ATOM   2222  HG3 LYS A 153     -17.082  23.861 -27.824  1.00  0.00           H  
ATOM   2223  HG2 LYS A 153     -16.301  24.950 -28.936  1.00  0.00           H  
ATOM   2224  HD3 LYS A 153     -14.321  25.113 -27.437  1.00  0.00           H  
ATOM   2225  HD2 LYS A 153     -15.042  23.968 -26.332  1.00  0.00           H  
ATOM   2226  HE3 LYS A 153     -16.935  25.556 -25.900  1.00  0.00           H  
ATOM   2227  HE2 LYS A 153     -16.230  26.708 -27.023  1.00  0.00           H  
ATOM   2228  HZ1 LYS A 153     -15.655  27.200 -24.774  1.00  0.00           H  
ATOM   2229  HZ2 LYS A 153     -14.954  25.722 -24.572  1.00  0.00           H  
ATOM   2230  HZ3 LYS A 153     -14.295  26.809 -25.622  1.00  0.00           H  
ATOM   2231  N   SER A 154     -14.983  20.311 -30.594  1.00124.90           N  
ANISOU 2231  N   SER A 154    19199  15878  12380  -4235   4650  -3017
ATOM   2232  CA  SER A 154     -14.222  19.385 -31.433  1.00126.18           C  
ANISOU 2232  CA  SER A 154    19595  15927  12419  -4302   5153  -3344
ATOM   2233  C   SER A 154     -14.979  19.030 -32.727  1.00126.20           C  
ANISOU 2233  C   SER A 154    20091  15938  11921  -4826   5185  -3441
ATOM   2234  O   SER A 154     -14.372  19.090 -33.793  1.00126.96           O  
ANISOU 2234  O   SER A 154    20395  16100  11744  -5099   5502  -3618
ATOM   2235  CB  SER A 154     -13.765  18.157 -30.613  1.00131.96           C  
ANISOU 2235  CB  SER A 154    20304  16378  13456  -3907   5387  -3528
ATOM   2236  OG  SER A 154     -14.810  17.244 -30.351  1.00131.48           O  
ANISOU 2236  OG  SER A 154    20514  16145  13296  -4004   5211  -3515
ATOM   2237  H   SER A 154     -15.345  19.935 -29.728  1.00  0.00           H  
ATOM   2238  HA  SER A 154     -13.312  19.913 -31.729  1.00  0.00           H  
ATOM   2239  HB3 SER A 154     -13.320  18.471 -29.668  1.00  0.00           H  
ATOM   2240  HB2 SER A 154     -12.988  17.622 -31.160  1.00  0.00           H  
ATOM   2241  HG  SER A 154     -14.455  16.482 -29.887  1.00  0.00           H  
ATOM   2242  N   ALA A 155     -16.293  18.756 -32.614  1.00131.18           N  
ANISOU 2242  N   ALA A 155    20895  16528  12420  -4995   4837  -3313
ATOM   2243  CA  ALA A 155     -17.205  18.482 -33.727  1.00128.96           C  
ANISOU 2243  CA  ALA A 155    21064  16274  11663  -5515   4768  -3362
ATOM   2244  C   ALA A 155     -17.388  19.654 -34.703  1.00127.83           C  
ANISOU 2244  C   ALA A 155    21005  16393  11172  -5918   4581  -3197
ATOM   2245  O   ALA A 155     -17.507  19.410 -35.903  1.00125.30           O  
ANISOU 2245  O   ALA A 155    21085  16110  10413  -6365   4726  -3327
ATOM   2246  CB  ALA A 155     -18.558  18.009 -33.180  1.00127.62           C  
ANISOU 2246  CB  ALA A 155    20940  16056  11493  -5572   4387  -3219
ATOM   2247  H   ALA A 155     -16.701  18.701 -31.689  1.00  0.00           H  
ATOM   2248  HA  ALA A 155     -16.779  17.663 -34.300  1.00  0.00           H  
ATOM   2249  HB1 ALA A 155     -19.257  17.781 -33.985  1.00  0.00           H  
ATOM   2250  HB2 ALA A 155     -18.435  17.100 -32.593  1.00  0.00           H  
ATOM   2251  HB3 ALA A 155     -19.021  18.762 -32.541  1.00  0.00           H  
ATOM   2252  N   LYS A 156     -17.364  20.895 -34.187  1.00121.36           N  
ANISOU 2252  N   LYS A 156    19835  15736  10540  -5765   4258  -2911
ATOM   2253  CA  LYS A 156     -17.393  22.129 -34.977  1.00121.20           C  
ANISOU 2253  CA  LYS A 156    19879  15930  10243  -6092   4038  -2711
ATOM   2254  C   LYS A 156     -16.119  22.317 -35.827  1.00120.49           C  
ANISOU 2254  C   LYS A 156    19949  15889   9943  -6282   4494  -2920
ATOM   2255  O   LYS A 156     -16.213  22.832 -36.940  1.00119.03           O  
ANISOU 2255  O   LYS A 156    20107  15813   9303  -6762   4473  -2904
ATOM   2256  CB  LYS A 156     -17.662  23.319 -34.029  1.00123.88           C  
ANISOU 2256  CB  LYS A 156    19818  16371  10879  -5830   3661  -2400
ATOM   2257  CG  LYS A 156     -17.757  24.695 -34.712  1.00123.89           C  
ANISOU 2257  CG  LYS A 156    19930  16549  10594  -6168   3323  -2137
ATOM   2258  CD  LYS A 156     -18.070  25.821 -33.717  1.00122.26           C  
ANISOU 2258  CD  LYS A 156    19369  16393  10692  -5898   2897  -1829
ATOM   2259  CE  LYS A 156     -18.111  27.199 -34.391  1.00123.51           C  
ANISOU 2259  CE  LYS A 156    19590  16674  10664  -6122   2690  -1598
ATOM   2260  NZ  LYS A 156     -18.335  28.271 -33.408  1.00120.57           N1+
ANISOU 2260  NZ  LYS A 156    18853  16303  10656  -5786   2429  -1375
ATOM   2261  H   LYS A 156     -17.290  21.011 -33.185  1.00  0.00           H  
ATOM   2262  HA  LYS A 156     -18.237  22.056 -35.666  1.00  0.00           H  
ATOM   2263  HB3 LYS A 156     -16.887  23.357 -33.263  1.00  0.00           H  
ATOM   2264  HB2 LYS A 156     -18.599  23.138 -33.501  1.00  0.00           H  
ATOM   2265  HG3 LYS A 156     -18.523  24.665 -35.487  1.00  0.00           H  
ATOM   2266  HG2 LYS A 156     -16.818  24.930 -35.215  1.00  0.00           H  
ATOM   2267  HD3 LYS A 156     -17.319  25.821 -32.925  1.00  0.00           H  
ATOM   2268  HD2 LYS A 156     -19.026  25.620 -33.232  1.00  0.00           H  
ATOM   2269  HE3 LYS A 156     -18.904  27.231 -35.140  1.00  0.00           H  
ATOM   2270  HE2 LYS A 156     -17.172  27.395 -34.908  1.00  0.00           H  
ATOM   2271  HZ1 LYS A 156     -18.358  29.162 -33.882  1.00  0.00           H  
ATOM   2272  HZ2 LYS A 156     -19.216  28.118 -32.938  1.00  0.00           H  
ATOM   2273  HZ3 LYS A 156     -17.587  28.269 -32.730  1.00  0.00           H  
ATOM   2274  N   GLY A 157     -14.970  21.854 -35.302  1.00104.39           N  
ANISOU 2274  N   GLY A 157    17670  13772   8223  -5924   4905  -3124
ATOM   2275  CA  GLY A 157     -13.673  21.853 -35.978  1.00107.88           C  
ANISOU 2275  CA  GLY A 157    18182  14268   8540  -6043   5413  -3371
ATOM   2276  C   GLY A 157     -13.481  20.640 -36.909  1.00112.15           C  
ANISOU 2276  C   GLY A 157    19098  14665   8848  -6218   5903  -3754
ATOM   2277  O   GLY A 157     -12.385  20.476 -37.444  1.00115.13           O  
ANISOU 2277  O   GLY A 157    19451  15053   9242  -6187   6409  -4021
ATOM   2278  H   GLY A 157     -14.993  21.438 -34.381  1.00  0.00           H  
ATOM   2279  HA3 GLY A 157     -12.892  21.835 -35.217  1.00  0.00           H  
ATOM   2280  HA2 GLY A 157     -13.537  22.773 -36.548  1.00  0.00           H  
ATOM   2281  N   GLY A 158     -14.510  19.794 -37.100  1.00 77.52           N  
ANISOU 2281  N   GLY A 158    15053  10146   4254  -6405   5774  -3796
ATOM   2282  CA  GLY A 158     -14.482  18.629 -37.986  1.00296.03           C  
ANISOU 2282  CA  GLY A 158    37855  37931  36692     95    428   -290
ATOM   2283  C   GLY A 158     -13.957  17.358 -37.295  1.00295.81           C  
ANISOU 2283  C   GLY A 158    37841  37899  36653    122    455   -360
ATOM   2284  O   GLY A 158     -13.842  16.327 -37.957  1.00297.26           O  
ANISOU 2284  O   GLY A 158    37901  37919  37125     85    286   -258
ATOM   2285  H   GLY A 158     -15.383  19.975 -36.624  1.00  0.00           H  
ATOM   2286  HA3 GLY A 158     -13.887  18.832 -38.878  1.00  0.00           H  
ATOM   2287  HA2 GLY A 158     -15.500  18.438 -38.326  1.00  0.00           H  
ATOM   2288  N   GLY A 159     -13.655  17.411 -35.986  1.00276.63           N  
ANISOU 2288  N   GLY A 159    36628  36102  32379   -419   2052  -1487
ATOM   2289  CA  GLY A 159     -13.231  16.274 -35.169  1.00276.96           C  
ANISOU 2289  CA  GLY A 159    36652  36080  32500   -243   2100  -1656
ATOM   2290  C   GLY A 159     -14.399  15.306 -34.928  1.00276.69           C  
ANISOU 2290  C   GLY A 159    36736  35895  32499   -314   1953  -1746
ATOM   2291  O   GLY A 159     -15.568  15.675 -35.049  1.00276.37           O  
ANISOU 2291  O   GLY A 159    36745  35786  32479   -524   1811  -1641
ATOM   2292  H   GLY A 159     -13.796  18.282 -35.491  1.00  0.00           H  
ATOM   2293  HA3 GLY A 159     -12.870  16.643 -34.209  1.00  0.00           H  
ATOM   2294  HA2 GLY A 159     -12.400  15.756 -35.652  1.00  0.00           H  
ATOM   2295  N   ALA A 160     -14.067  14.052 -34.581  1.00254.18           N  
ANISOU 2295  N   ALA A 160    35086  32436  29055  -1635   3453  -2799
ATOM   2296  CA  ALA A 160     -15.034  12.983 -34.334  1.00254.10           C  
ANISOU 2296  CA  ALA A 160    35237  32255  29054  -1672   3297  -2866
ATOM   2297  C   ALA A 160     -15.879  13.241 -33.077  1.00251.61           C  
ANISOU 2297  C   ALA A 160    35059  31734  28809  -1992   3349  -2860
ATOM   2298  O   ALA A 160     -15.328  13.541 -32.017  1.00251.22           O  
ANISOU 2298  O   ALA A 160    34929  31593  28931  -1931   3518  -2892
ATOM   2299  CB  ALA A 160     -14.290  11.644 -34.229  1.00255.95           C  
ANISOU 2299  CB  ALA A 160    35425  32419  29405  -1246   3303  -3048
ATOM   2300  H   ALA A 160     -13.094  13.802 -34.482  1.00  0.00           H  
ATOM   2301  HA  ALA A 160     -15.697  12.929 -35.200  1.00  0.00           H  
ATOM   2302  HB1 ALA A 160     -14.984  10.820 -34.056  1.00  0.00           H  
ATOM   2303  HB2 ALA A 160     -13.747  11.425 -35.149  1.00  0.00           H  
ATOM   2304  HB3 ALA A 160     -13.569  11.649 -33.410  1.00  0.00           H  
ATOM   2305  N   ARG A 161     -17.202  13.110 -33.239  1.00231.79           N  
ANISOU 2305  N   ARG A 161    33768  28740  25560  -3585   4293  -3445
ATOM   2306  CA  ARG A 161     -18.196  13.325 -32.192  1.00144.32           C  
ANISOU 2306  CA  ARG A 161    23873  17105  13857  -5167   5333  -4031
ATOM   2307  C   ARG A 161     -18.348  12.053 -31.342  1.00143.85           C  
ANISOU 2307  C   ARG A 161    23922  16673  14062  -4850   5479  -4150
ATOM   2308  O   ARG A 161     -18.306  10.951 -31.893  1.00231.66           O  
ANISOU 2308  O   ARG A 161    34001  28192  25828  -3322   4337  -3638
ATOM   2309  CB  ARG A 161     -19.515  13.731 -32.883  1.00129.38           C  
ANISOU 2309  CB  ARG A 161    22194  15394  11569  -5702   4964  -3894
ATOM   2310  CG  ARG A 161     -20.402  14.685 -32.068  1.00126.93           C  
ANISOU 2310  CG  ARG A 161    21481  15365  11383  -5660   4452  -3536
ATOM   2311  CD  ARG A 161     -21.558  15.225 -32.928  1.00125.74           C  
ANISOU 2311  CD  ARG A 161    21483  15468  10823  -6190   4109  -3396
ATOM   2312  NE  ARG A 161     -22.007  16.548 -32.478  1.00127.39           N  
ANISOU 2312  NE  ARG A 161    21290  15962  11152  -6111   3694  -3073
ATOM   2313  CZ  ARG A 161     -22.776  17.389 -33.193  1.00126.50           C  
ANISOU 2313  CZ  ARG A 161    21203  16103  10758  -6476   3334  -2881
ATOM   2314  NH1 ARG A 161     -23.249  17.050 -34.401  1.00124.89           N  
ANISOU 2314  NH1 ARG A 161    21402  15939  10110  -6982   3316  -2971
ATOM   2315  NH2 ARG A 161     -23.069  18.596 -32.694  1.00128.71           N1+
ANISOU 2315  NH2 ARG A 161    21118  16589  11198  -6339   2977  -2595
ATOM   2316  H   ARG A 161     -17.565  12.843 -34.142  1.00  0.00           H  
ATOM   2317  HA  ARG A 161     -17.863  14.144 -31.550  1.00  0.00           H  
ATOM   2318  HB3 ARG A 161     -20.078  12.858 -33.218  1.00  0.00           H  
ATOM   2319  HB2 ARG A 161     -19.251  14.274 -33.792  1.00  0.00           H  
ATOM   2320  HG3 ARG A 161     -19.823  15.505 -31.642  1.00  0.00           H  
ATOM   2321  HG2 ARG A 161     -20.804  14.124 -31.223  1.00  0.00           H  
ATOM   2322  HD3 ARG A 161     -22.427  14.578 -32.805  1.00  0.00           H  
ATOM   2323  HD2 ARG A 161     -21.308  15.218 -33.990  1.00  0.00           H  
ATOM   2324  HE  ARG A 161     -21.726  16.814 -31.544  1.00  0.00           H  
ATOM   2325 HH12 ARG A 161     -23.824  17.689 -34.930  1.00  0.00           H  
ATOM   2326 HH11 ARG A 161     -23.038  16.140 -34.786  1.00  0.00           H  
ATOM   2327 HH22 ARG A 161     -23.644  19.241 -33.216  1.00  0.00           H  
ATOM   2328 HH21 ARG A 161     -22.723  18.869 -31.785  1.00  0.00           H  
ATOM   2329  N   GLN A 162     -18.512  12.229 -30.024  1.00127.09           N  
ANISOU 2329  N   GLN A 162    21482  14546  12261  -4544   5181  -3923
ATOM   2330  CA  GLN A 162     -18.632  11.143 -29.049  1.00127.08           C  
ANISOU 2330  CA  GLN A 162    21581  14202  12503  -4258   5245  -3974
ATOM   2331  C   GLN A 162     -20.066  10.925 -28.555  1.00127.44           C  
ANISOU 2331  C   GLN A 162    21727  14266  12429  -4518   4889  -3819
ATOM   2332  O   GLN A 162     -20.402   9.784 -28.237  1.00127.13           O  
ANISOU 2332  O   GLN A 162    22012  13918  12373  -4547   4987  -3931
ATOM   2333  CB  GLN A 162     -17.696  11.421 -27.849  1.00127.30           C  
ANISOU 2333  CB  GLN A 162    21176  14183  13010  -3674   5238  -3859
ATOM   2334  CG  GLN A 162     -16.208  11.138 -28.129  1.00129.44           C  
ANISOU 2334  CG  GLN A 162    21415  14279  13488  -3321   5678  -4085
ATOM   2335  CD  GLN A 162     -15.910   9.649 -28.334  1.00133.44           C  
ANISOU 2335  CD  GLN A 162    22360  14336  14004  -3232   6015  -4354
ATOM   2336  OE1 GLN A 162     -16.471   8.793 -27.652  1.00132.81           O  
ANISOU 2336  OE1 GLN A 162    22505  14012  13946  -3235   5887  -4310
ATOM   2337  NE2 GLN A 162     -15.004   9.333 -29.260  1.00250.80           N  
ANISOU 2337  NE2 GLN A 162    35216  30563  29512  -1171   3692  -3426
ATOM   2338  H   GLN A 162     -18.505  13.169 -29.642  1.00  0.00           H  
ATOM   2339  HA  GLN A 162     -18.335  10.201 -29.511  1.00  0.00           H  
ATOM   2340  HB3 GLN A 162     -18.006  10.831 -26.984  1.00  0.00           H  
ATOM   2341  HB2 GLN A 162     -17.807  12.458 -27.533  1.00  0.00           H  
ATOM   2342  HG3 GLN A 162     -15.611  11.485 -27.286  1.00  0.00           H  
ATOM   2343  HG2 GLN A 162     -15.880  11.712 -28.997  1.00  0.00           H  
ATOM   2344 HE22 GLN A 162     -14.771   8.366 -29.430  1.00  0.00           H  
ATOM   2345 HE21 GLN A 162     -14.558  10.056 -29.807  1.00  0.00           H  
ATOM   2346  N   PHE A 163     -20.862  12.003 -28.462  1.00116.57           N  
ANISOU 2346  N   PHE A 163    20067  13238  10987  -4694   4488  -3565
ATOM   2347  CA  PHE A 163     -22.172  11.982 -27.810  1.00115.04           C  
ANISOU 2347  CA  PHE A 163    19860  13117  10732  -4904   4145  -3408
ATOM   2348  C   PHE A 163     -23.206  12.699 -28.685  1.00115.01           C  
ANISOU 2348  C   PHE A 163    19847  13451  10399  -5377   3846  -3293
ATOM   2349  O   PHE A 163     -22.898  13.737 -29.272  1.00114.26           O  
ANISOU 2349  O   PHE A 163    19574  13598  10242  -5415   3762  -3204
ATOM   2350  CB  PHE A 163     -22.073  12.696 -26.445  1.00108.41           C  
ANISOU 2350  CB  PHE A 163    18574  12348  10271  -4516   3901  -3172
ATOM   2351  CG  PHE A 163     -20.922  12.262 -25.557  1.00108.16           C  
ANISOU 2351  CG  PHE A 163    18420  12073  10604  -3989   4120  -3215
ATOM   2352  CD1 PHE A 163     -20.887  10.964 -25.006  1.00109.51           C  
ANISOU 2352  CD1 PHE A 163    18862  11864  10883  -3826   4301  -3331
ATOM   2353  CD2 PHE A 163     -19.827  13.129 -25.353  1.00107.03           C  
ANISOU 2353  CD2 PHE A 163    17913  12071  10684  -3671   4145  -3140
ATOM   2354  CE1 PHE A 163     -19.799  10.572 -24.238  1.00109.61           C  
ANISOU 2354  CE1 PHE A 163    18762  11649  11236  -3327   4479  -3359
ATOM   2355  CE2 PHE A 163     -18.756  12.721 -24.571  1.00107.35           C  
ANISOU 2355  CE2 PHE A 163    17820  11910  11056  -3200   4335  -3181
ATOM   2356  CZ  PHE A 163     -18.747  11.449 -24.013  1.00108.43           C  
ANISOU 2356  CZ  PHE A 163    18209  11678  11311  -3016   4489  -3284
ATOM   2357  H   PHE A 163     -20.514  12.916 -28.731  1.00  0.00           H  
ATOM   2358  HA  PHE A 163     -22.500  10.955 -27.645  1.00  0.00           H  
ATOM   2359  HB3 PHE A 163     -22.999  12.540 -25.889  1.00  0.00           H  
ATOM   2360  HB2 PHE A 163     -21.996  13.773 -26.596  1.00  0.00           H  
ATOM   2361  HD1 PHE A 163     -21.701  10.274 -25.181  1.00  0.00           H  
ATOM   2362  HD2 PHE A 163     -19.822  14.115 -25.794  1.00  0.00           H  
ATOM   2363  HE1 PHE A 163     -19.769   9.582 -23.813  1.00  0.00           H  
ATOM   2364  HE2 PHE A 163     -17.927  13.393 -24.403  1.00  0.00           H  
ATOM   2365  HZ  PHE A 163     -17.916  11.128 -23.406  1.00  0.00           H  
ATOM   2366  N   ASN A 164     -24.434  12.156 -28.702  1.00124.08           N  
ANISOU 2366  N   ASN A 164    21177  14621  11345  -5741   3662  -3278
ATOM   2367  CA  ASN A 164     -25.613  12.790 -29.303  1.00123.79           C  
ANISOU 2367  CA  ASN A 164    21084  14923  11026  -6186   3304  -3137
ATOM   2368  C   ASN A 164     -26.157  13.918 -28.410  1.00126.03           C  
ANISOU 2368  C   ASN A 164    20824  15482  11578  -5971   2919  -2844
ATOM   2369  O   ASN A 164     -26.397  15.011 -28.920  1.00126.58           O  
ANISOU 2369  O   ASN A 164    20663  15823  11608  -6011   2693  -2683
ATOM   2370  CB  ASN A 164     -26.699  11.721 -29.568  1.00  0.00           C  
ATOM   2371  CG  ASN A 164     -26.414  10.877 -30.812  1.00  0.00           C  
ATOM   2372  OD1 ASN A 164     -26.839  11.232 -31.910  1.00  0.00           O  
ATOM   2373  ND2 ASN A 164     -25.705   9.759 -30.646  1.00  0.00           N  
ATOM   2374  H   ASN A 164     -24.590  11.274 -28.228  1.00  0.00           H  
ATOM   2375  HA  ASN A 164     -25.282  13.199 -30.261  1.00  0.00           H  
ATOM   2376  HB2 ASN A 164     -26.849  11.082 -28.695  1.00  0.00           H  
ATOM   2377  HB3 ASN A 164     -27.657  12.211 -29.747  1.00  0.00           H  
ATOM   2378 HD22 ASN A 164     -25.495   9.169 -31.437  1.00  0.00           H  
ATOM   2379 HD21 ASN A 164     -25.360   9.500 -29.729  1.00  0.00           H  
ATOM   2380  N   GLY A 165     -26.343  13.636 -27.111  1.00118.01           N  
ANISOU 2380  N   GLY A 165    19635  14371  10833  -5732   2869  -2785
ATOM   2381  CA  GLY A 165     -26.890  14.589 -26.146  1.00114.63           C  
ANISOU 2381  CA  GLY A 165    18721  14168  10667  -5517   2562  -2549
ATOM   2382  C   GLY A 165     -26.366  14.256 -24.746  1.00112.57           C  
ANISOU 2382  C   GLY A 165    18310  13712  10751  -5095   2664  -2529
ATOM   2383  O   GLY A 165     -25.495  13.400 -24.587  1.00113.47           O  
ANISOU 2383  O   GLY A 165    18652  13517  10947  -4889   2965  -2673
ATOM   2384  H   GLY A 165     -26.089  12.725 -26.758  1.00  0.00           H  
ATOM   2385  HA3 GLY A 165     -27.979  14.532 -26.159  1.00  0.00           H  
ATOM   2386  HA2 GLY A 165     -26.605  15.613 -26.392  1.00  0.00           H  
ATOM   2387  N   LEU A 166     -26.910  14.949 -23.726  1.00104.76           N  
ANISOU 2387  N   LEU A 166    16941  12898   9967  -4963   2413  -2351
ATOM   2388  CA  LEU A 166     -26.563  14.774 -22.307  1.00102.98           C  
ANISOU 2388  CA  LEU A 166    16566  12524  10038  -4608   2463  -2306
ATOM   2389  C   LEU A 166     -26.794  13.342 -21.810  1.00104.51           C  
ANISOU 2389  C   LEU A 166    17098  12437  10174  -4713   2623  -2426
ATOM   2390  O   LEU A 166     -25.934  12.813 -21.113  1.00104.23           O  
ANISOU 2390  O   LEU A 166    17164  12125  10314  -4411   2800  -2464
ATOM   2391  CB  LEU A 166     -27.369  15.751 -21.414  1.00 98.84           C  
ANISOU 2391  CB  LEU A 166    15610  12259   9687  -4530   2177  -2121
ATOM   2392  CG  LEU A 166     -26.822  17.192 -21.343  1.00 97.81           C  
ANISOU 2392  CG  LEU A 166    15122  12293   9747  -4246   2053  -1981
ATOM   2393  CD1 LEU A 166     -27.795  18.112 -20.574  1.00 98.00           C  
ANISOU 2393  CD1 LEU A 166    14766  12549   9921  -4204   1792  -1833
ATOM   2394  CD2 LEU A 166     -25.394  17.247 -20.756  1.00 97.31           C  
ANISOU 2394  CD2 LEU A 166    15038  12028   9906  -3844   2246  -1998
ATOM   2395  H   LEU A 166     -27.612  15.648 -23.923  1.00  0.00           H  
ATOM   2396  HA  LEU A 166     -25.495  14.975 -22.209  1.00  0.00           H  
ATOM   2397  HB3 LEU A 166     -27.404  15.374 -20.390  1.00  0.00           H  
ATOM   2398  HB2 LEU A 166     -28.407  15.763 -21.752  1.00  0.00           H  
ATOM   2399  HG  LEU A 166     -26.776  17.571 -22.364  1.00  0.00           H  
ATOM   2400 HD11 LEU A 166     -28.039  18.995 -21.167  1.00  0.00           H  
ATOM   2401 HD12 LEU A 166     -28.737  17.613 -20.344  1.00  0.00           H  
ATOM   2402 HD13 LEU A 166     -27.390  18.464 -19.625  1.00  0.00           H  
ATOM   2403 HD21 LEU A 166     -25.285  17.993 -19.970  1.00  0.00           H  
ATOM   2404 HD22 LEU A 166     -25.094  16.292 -20.327  1.00  0.00           H  
ATOM   2405 HD23 LEU A 166     -24.668  17.496 -21.530  1.00  0.00           H  
ATOM   2406  N   ILE A 167     -27.922  12.732 -22.206  1.00100.69           N  
ANISOU 2406  N   ILE A 167    16800  12018   9439  -5151   2548  -2480
ATOM   2407  CA  ILE A 167     -28.298  11.367 -21.831  1.00102.72           C  
ANISOU 2407  CA  ILE A 167    17420  12003   9604  -5323   2689  -2592
ATOM   2408  C   ILE A 167     -27.302  10.314 -22.370  1.00104.91           C  
ANISOU 2408  C   ILE A 167    18145  11885   9829  -5216   3022  -2781
ATOM   2409  O   ILE A 167     -27.075   9.315 -21.692  1.00105.73           O  
ANISOU 2409  O   ILE A 167    18490  11651  10033  -5059   3182  -2834
ATOM   2410  CB  ILE A 167     -29.733  11.016 -22.327  1.00109.75           C  
ANISOU 2410  CB  ILE A 167    18399  13087  10215  -5870   2530  -2615
ATOM   2411  CG1 ILE A 167     -30.774  12.104 -21.958  1.00109.84           C  
ANISOU 2411  CG1 ILE A 167    17886  13544  10306  -5933   2190  -2432
ATOM   2412  CG2 ILE A 167     -30.223   9.627 -21.860  1.00109.96           C  
ANISOU 2412  CG2 ILE A 167    18757  12858  10166  -6069   2644  -2700
ATOM   2413  CD1 ILE A 167     -30.840  12.473 -20.467  1.00111.87           C  
ANISOU 2413  CD1 ILE A 167    17771  13860  10873  -5627   2107  -2300
ATOM   2414  H   ILE A 167     -28.578  13.230 -22.790  1.00  0.00           H  
ATOM   2415  HA  ILE A 167     -28.279  11.307 -20.741  1.00  0.00           H  
ATOM   2416  HB  ILE A 167     -29.708  10.985 -23.418  1.00  0.00           H  
ATOM   2417 HG13 ILE A 167     -31.763  11.794 -22.296  1.00  0.00           H  
ATOM   2418 HG12 ILE A 167     -30.560  13.012 -22.523  1.00  0.00           H  
ATOM   2419 HG21 ILE A 167     -31.256   9.454 -22.162  1.00  0.00           H  
ATOM   2420 HG22 ILE A 167     -29.636   8.817 -22.291  1.00  0.00           H  
ATOM   2421 HG23 ILE A 167     -30.175   9.528 -20.776  1.00  0.00           H  
ATOM   2422 HD11 ILE A 167     -31.757  13.020 -20.248  1.00  0.00           H  
ATOM   2423 HD12 ILE A 167     -30.825  11.591 -19.827  1.00  0.00           H  
ATOM   2424 HD13 ILE A 167     -30.003  13.110 -20.179  1.00  0.00           H  
ATOM   2425  N   ASP A 168     -26.682  10.592 -23.533  1.00 98.20           N  
ANISOU 2425  N   ASP A 168    17398  11069   8844  -5267   3132  -2876
ATOM   2426  CA  ASP A 168     -25.615   9.787 -24.131  1.00 99.05           C  
ANISOU 2426  CA  ASP A 168    17900  10817   8917  -5145   3490  -3087
ATOM   2427  C   ASP A 168     -24.290   9.929 -23.345  1.00 99.13           C  
ANISOU 2427  C   ASP A 168    17747  10626   9291  -4570   3635  -3055
ATOM   2428  O   ASP A 168     -23.591   8.928 -23.191  1.00 99.95           O  
ANISOU 2428  O   ASP A 168    18161  10340   9476  -4377   3897  -3193
ATOM   2429  CB  ASP A 168     -25.437  10.131 -25.631  1.00104.43           C  
ANISOU 2429  CB  ASP A 168    18712  11617   9349  -5364   3590  -3203
ATOM   2430  CG  ASP A 168     -24.712   9.074 -26.478  1.00107.91           C  
ANISOU 2430  CG  ASP A 168    19659  11678   9662  -5386   3993  -3483
ATOM   2431  OD1 ASP A 168     -24.366   7.998 -25.943  1.00108.83           O  
ANISOU 2431  OD1 ASP A 168    20046  11417   9888  -5236   4171  -3578
ATOM   2432  OD2 ASP A 168     -24.548   9.364 -27.683  1.00110.01           O1-
ANISOU 2432  OD2 ASP A 168    20074  12011   9712  -5562   4137  -3611
ATOM   2433  H   ASP A 168     -26.903  11.452 -24.014  1.00  0.00           H  
ATOM   2434  HA  ASP A 168     -25.934   8.746 -24.055  1.00  0.00           H  
ATOM   2435  HB3 ASP A 168     -24.885  11.066 -25.723  1.00  0.00           H  
ATOM   2436  HB2 ASP A 168     -26.422  10.284 -26.075  1.00  0.00           H  
ATOM   2437  N   VAL A 169     -23.988  11.134 -22.813  1.00 87.55           N  
ANISOU 2437  N   VAL A 169    15800   9417   8050  -4298   3449  -2868
ATOM   2438  CA  VAL A 169     -22.846  11.364 -21.915  1.00 86.10           C  
ANISOU 2438  CA  VAL A 169    15394   9110   8211  -3777   3528  -2806
ATOM   2439  C   VAL A 169     -22.994  10.560 -20.611  1.00 85.74           C  
ANISOU 2439  C   VAL A 169    15465   8801   8313  -3622   3514  -2758
ATOM   2440  O   VAL A 169     -22.071   9.826 -20.266  1.00 86.63           O  
ANISOU 2440  O   VAL A 169    15741   8583   8592  -3307   3709  -2826
ATOM   2441  CB  VAL A 169     -22.619  12.857 -21.527  1.00 82.14           C  
ANISOU 2441  CB  VAL A 169    14388   8942   7879  -3591   3313  -2617
ATOM   2442  CG1 VAL A 169     -21.414  13.061 -20.585  1.00 80.76           C  
ANISOU 2442  CG1 VAL A 169    14002   8646   8036  -3097   3389  -2562
ATOM   2443  CG2 VAL A 169     -22.440  13.769 -22.747  1.00 82.49           C  
ANISOU 2443  CG2 VAL A 169    14363   9224   7756  -3767   3315  -2646
ATOM   2444  H   VAL A 169     -24.600  11.921 -22.975  1.00  0.00           H  
ATOM   2445  HA  VAL A 169     -21.950  11.007 -22.423  1.00  0.00           H  
ATOM   2446  HB  VAL A 169     -23.494  13.226 -20.996  1.00  0.00           H  
ATOM   2447 HG11 VAL A 169     -21.176  14.117 -20.500  1.00  0.00           H  
ATOM   2448 HG12 VAL A 169     -21.604  12.694 -19.576  1.00  0.00           H  
ATOM   2449 HG13 VAL A 169     -20.522  12.560 -20.965  1.00  0.00           H  
ATOM   2450 HG21 VAL A 169     -22.427  14.816 -22.447  1.00  0.00           H  
ATOM   2451 HG22 VAL A 169     -21.497  13.565 -23.248  1.00  0.00           H  
ATOM   2452 HG23 VAL A 169     -23.241  13.650 -23.472  1.00  0.00           H  
ATOM   2453  N   TYR A 170     -24.168  10.668 -19.958  1.00 81.97           N  
ANISOU 2453  N   TYR A 170    14912   8469   7765  -3858   3286  -2642
ATOM   2454  CA  TYR A 170     -24.545   9.886 -18.778  1.00 81.81           C  
ANISOU 2454  CA  TYR A 170    15029   8234   7821  -3812   3252  -2584
ATOM   2455  C   TYR A 170     -24.459   8.373 -19.017  1.00 84.77           C  
ANISOU 2455  C   TYR A 170    15959   8186   8065  -3929   3486  -2757
ATOM   2456  O   TYR A 170     -23.821   7.699 -18.217  1.00 85.18           O  
ANISOU 2456  O   TYR A 170    16189   7891   8285  -3629   3591  -2751
ATOM   2457  CB  TYR A 170     -25.951  10.291 -18.283  1.00 82.06           C  
ANISOU 2457  CB  TYR A 170    14882   8552   7747  -4139   3007  -2473
ATOM   2458  CG  TYR A 170     -25.971  11.467 -17.324  1.00 78.85           C  
ANISOU 2458  CG  TYR A 170    13990   8415   7554  -3907   2803  -2290
ATOM   2459  CD1 TYR A 170     -25.756  11.249 -15.948  1.00 77.70           C  
ANISOU 2459  CD1 TYR A 170    13797   8156   7568  -3712   2755  -2184
ATOM   2460  CD2 TYR A 170     -26.227  12.774 -17.784  1.00 77.16           C  
ANISOU 2460  CD2 TYR A 170    13397   8556   7364  -3908   2651  -2221
ATOM   2461  CE1 TYR A 170     -25.796  12.326 -15.043  1.00 74.99           C  
ANISOU 2461  CE1 TYR A 170    13039   8052   7401  -3522   2586  -2036
ATOM   2462  CE2 TYR A 170     -26.261  13.854 -16.884  1.00 74.48           C  
ANISOU 2462  CE2 TYR A 170    12644   8434   7220  -3701   2477  -2068
ATOM   2463  CZ  TYR A 170     -26.056  13.627 -15.511  1.00 73.44           C  
ANISOU 2463  CZ  TYR A 170    12471   8191   7243  -3510   2457  -1988
ATOM   2464  OH  TYR A 170     -26.139  14.660 -14.630  1.00 71.08           O  
ANISOU 2464  OH  TYR A 170    11799   8090   7117  -3323   2308  -1859
ATOM   2465  H   TYR A 170     -24.872  11.299 -20.317  1.00  0.00           H  
ATOM   2466  HA  TYR A 170     -23.822  10.130 -17.998  1.00  0.00           H  
ATOM   2467  HB3 TYR A 170     -26.401   9.460 -17.737  1.00  0.00           H  
ATOM   2468  HB2 TYR A 170     -26.622  10.474 -19.123  1.00  0.00           H  
ATOM   2469  HD1 TYR A 170     -25.574  10.250 -15.582  1.00  0.00           H  
ATOM   2470  HD2 TYR A 170     -26.425  12.960 -18.822  1.00  0.00           H  
ATOM   2471  HE1 TYR A 170     -25.644  12.152 -13.988  1.00  0.00           H  
ATOM   2472  HE2 TYR A 170     -26.468  14.850 -17.248  1.00  0.00           H  
ATOM   2473  HH  TYR A 170     -26.331  15.501 -15.049  1.00  0.00           H  
ATOM   2474  N   ARG A 171     -25.048   7.881 -20.121  1.00 83.28           N  
ANISOU 2474  N   ARG A 171    16060   8005   7580  -4344   3568  -2911
ATOM   2475  CA  ARG A 171     -25.054   6.469 -20.507  1.00 83.30           C  
ANISOU 2475  CA  ARG A 171    16637   7586   7427  -4507   3796  -3093
ATOM   2476  C   ARG A 171     -23.646   5.877 -20.687  1.00 83.95           C  
ANISOU 2476  C   ARG A 171    16899   7286   7713  -4055   4077  -3209
ATOM   2477  O   ARG A 171     -23.373   4.826 -20.110  1.00 84.78           O  
ANISOU 2477  O   ARG A 171    17263   6998   7953  -3837   4160  -3204
ATOM   2478  CB  ARG A 171     -25.939   6.286 -21.762  1.00  0.00           C  
ATOM   2479  CG  ARG A 171     -25.989   4.864 -22.364  1.00  0.00           C  
ATOM   2480  CD  ARG A 171     -26.679   3.813 -21.479  1.00  0.00           C  
ATOM   2481  NE  ARG A 171     -28.125   4.055 -21.367  1.00  0.00           N  
ATOM   2482  CZ  ARG A 171     -28.968   3.417 -20.537  1.00  0.00           C  
ATOM   2483  NH1 ARG A 171     -28.536   2.454 -19.710  1.00  0.00           N  
ATOM   2484  NH2 ARG A 171     -30.265   3.749 -20.539  1.00  0.00           N1+
ATOM   2485  H   ARG A 171     -25.549   8.508 -20.738  1.00  0.00           H  
ATOM   2486  HA  ARG A 171     -25.529   5.936 -19.681  1.00  0.00           H  
ATOM   2487  HB2 ARG A 171     -26.953   6.615 -21.533  1.00  0.00           H  
ATOM   2488  HB3 ARG A 171     -25.578   6.959 -22.541  1.00  0.00           H  
ATOM   2489  HG2 ARG A 171     -26.586   4.959 -23.272  1.00  0.00           H  
ATOM   2490  HG3 ARG A 171     -25.016   4.508 -22.706  1.00  0.00           H  
ATOM   2491  HD2 ARG A 171     -26.434   2.795 -21.782  1.00  0.00           H  
ATOM   2492  HD3 ARG A 171     -26.306   3.924 -20.461  1.00  0.00           H  
ATOM   2493  HE  ARG A 171     -28.502   4.752 -21.994  1.00  0.00           H  
ATOM   2494 HH12 ARG A 171     -29.176   1.979 -19.090  1.00  0.00           H  
ATOM   2495 HH11 ARG A 171     -27.560   2.196 -19.705  1.00  0.00           H  
ATOM   2496 HH22 ARG A 171     -30.915   3.281 -19.924  1.00  0.00           H  
ATOM   2497 HH21 ARG A 171     -30.606   4.472 -21.156  1.00  0.00           H  
ATOM   2498  N   LYS A 172     -22.789   6.560 -21.464  1.00 93.66           N  
ANISOU 2498  N   LYS A 172    17966   8638   8982  -3897   4213  -3300
ATOM   2499  CA  LYS A 172     -21.436   6.105 -21.782  1.00 92.89           C  
ANISOU 2499  CA  LYS A 172    17984   8230   9081  -3479   4522  -3450
ATOM   2500  C   LYS A 172     -20.479   6.131 -20.576  1.00 94.00           C  
ANISOU 2500  C   LYS A 172    17874   8222   9620  -2915   4465  -3294
ATOM   2501  O   LYS A 172     -19.739   5.166 -20.390  1.00 92.89           O  
ANISOU 2501  O   LYS A 172    18019   7641   9636  -2622   4652  -3377
ATOM   2502  CB  LYS A 172     -20.895   6.906 -22.988  1.00  0.00           C  
ATOM   2503  CG  LYS A 172     -19.462   6.553 -23.443  1.00  0.00           C  
ATOM   2504  CD  LYS A 172     -19.273   5.073 -23.825  1.00  0.00           C  
ATOM   2505  CE  LYS A 172     -17.832   4.746 -24.236  1.00  0.00           C  
ATOM   2506  NZ  LYS A 172     -17.684   3.317 -24.562  1.00  0.00           N1+
ATOM   2507  H   LYS A 172     -23.088   7.421 -21.906  1.00  0.00           H  
ATOM   2508  HA  LYS A 172     -21.534   5.064 -22.095  1.00  0.00           H  
ATOM   2509  HB2 LYS A 172     -21.572   6.773 -23.834  1.00  0.00           H  
ATOM   2510  HB3 LYS A 172     -20.932   7.968 -22.745  1.00  0.00           H  
ATOM   2511  HG2 LYS A 172     -19.209   7.175 -24.303  1.00  0.00           H  
ATOM   2512  HG3 LYS A 172     -18.747   6.828 -22.667  1.00  0.00           H  
ATOM   2513  HD2 LYS A 172     -19.549   4.429 -22.991  1.00  0.00           H  
ATOM   2514  HD3 LYS A 172     -19.954   4.824 -24.641  1.00  0.00           H  
ATOM   2515  HE2 LYS A 172     -17.539   5.340 -25.102  1.00  0.00           H  
ATOM   2516  HE3 LYS A 172     -17.144   4.991 -23.426  1.00  0.00           H  
ATOM   2517  HZ1 LYS A 172     -16.727   3.128 -24.825  1.00  0.00           H  
ATOM   2518  HZ2 LYS A 172     -17.927   2.759 -23.756  1.00  0.00           H  
ATOM   2519  HZ3 LYS A 172     -18.295   3.081 -25.331  1.00  0.00           H  
ATOM   2520  N   THR A 173     -20.514   7.212 -19.780  1.00 88.84           N  
ANISOU 2520  N   THR A 173    16718   7916   9123  -2773   4197  -3066
ATOM   2521  CA  THR A 173     -19.656   7.381 -18.602  1.00 87.50           C  
ANISOU 2521  CA  THR A 173    16292   7655   9300  -2281   4107  -2904
ATOM   2522  C   THR A 173     -20.107   6.525 -17.394  1.00 88.27           C  
ANISOU 2522  C   THR A 173    16693   7422   9422  -2266   4014  -2808
ATOM   2523  O   THR A 173     -19.240   6.111 -16.626  1.00 89.61           O  
ANISOU 2523  O   THR A 173    16924   7285   9840  -1858   4050  -2757
ATOM   2524  CB  THR A 173     -19.550   8.866 -18.172  1.00 96.28           C  
ANISOU 2524  CB  THR A 173    16842   9207  10534  -2186   3855  -2704
ATOM   2525  OG1 THR A 173     -20.803   9.386 -17.773  1.00 94.24           O  
ANISOU 2525  OG1 THR A 173    16513   9224  10071  -2581   3628  -2607
ATOM   2526  CG2 THR A 173     -18.945   9.754 -19.275  1.00 95.76           C  
ANISOU 2526  CG2 THR A 173    16486   9394  10506  -2101   3960  -2774
ATOM   2527  H   THR A 173     -21.150   7.971 -19.987  1.00  0.00           H  
ATOM   2528  HA  THR A 173     -18.651   7.052 -18.872  1.00  0.00           H  
ATOM   2529  HB  THR A 173     -18.898   8.937 -17.300  1.00  0.00           H  
ATOM   2530  HG1 THR A 173     -21.333   9.544 -18.562  1.00  0.00           H  
ATOM   2531 HG21 THR A 173     -18.929  10.803 -18.986  1.00  0.00           H  
ATOM   2532 HG22 THR A 173     -17.915   9.459 -19.480  1.00  0.00           H  
ATOM   2533 HG23 THR A 173     -19.493   9.685 -20.214  1.00  0.00           H  
ATOM   2534  N   LEU A 174     -21.412   6.200 -17.289  1.00 86.10           N  
ANISOU 2534  N   LEU A 174    16615   7211   8888  -2722   3892  -2781
ATOM   2535  CA  LEU A 174     -21.932   5.191 -16.356  1.00 86.73           C  
ANISOU 2535  CA  LEU A 174    17027   6984   8942  -2788   3819  -2695
ATOM   2536  C   LEU A 174     -21.539   3.766 -16.770  1.00 89.97           C  
ANISOU 2536  C   LEU A 174    18003   6849   9333  -2715   4075  -2866
ATOM   2537  O   LEU A 174     -21.241   2.956 -15.896  1.00 90.95           O  
ANISOU 2537  O   LEU A 174    18370   6588   9600  -2468   4063  -2783
ATOM   2538  CB  LEU A 174     -23.471   5.279 -16.239  1.00 82.46           C  
ANISOU 2538  CB  LEU A 174    16542   6673   8117  -3338   3658  -2652
ATOM   2539  CG  LEU A 174     -23.968   6.430 -15.339  1.00 81.99           C  
ANISOU 2539  CG  LEU A 174    16046   6993   8115  -3369   3392  -2448
ATOM   2540  CD1 LEU A 174     -25.466   6.724 -15.572  1.00 81.88           C  
ANISOU 2540  CD1 LEU A 174    15985   7289   7836  -3905   3279  -2463
ATOM   2541  CD2 LEU A 174     -23.645   6.175 -13.852  1.00 82.04           C  
ANISOU 2541  CD2 LEU A 174    16153   6762   8258  -3159   3300  -2288
ATOM   2542  H   LEU A 174     -22.081   6.601 -17.932  1.00  0.00           H  
ATOM   2543  HA  LEU A 174     -21.492   5.377 -15.376  1.00  0.00           H  
ATOM   2544  HB3 LEU A 174     -23.877   4.349 -15.838  1.00  0.00           H  
ATOM   2545  HB2 LEU A 174     -23.893   5.357 -17.241  1.00  0.00           H  
ATOM   2546  HG  LEU A 174     -23.424   7.326 -15.640  1.00  0.00           H  
ATOM   2547 HD11 LEU A 174     -25.616   7.773 -15.827  1.00  0.00           H  
ATOM   2548 HD12 LEU A 174     -25.878   6.136 -16.393  1.00  0.00           H  
ATOM   2549 HD13 LEU A 174     -26.081   6.513 -14.696  1.00  0.00           H  
ATOM   2550 HD21 LEU A 174     -24.488   6.373 -13.190  1.00  0.00           H  
ATOM   2551 HD22 LEU A 174     -23.329   5.147 -13.670  1.00  0.00           H  
ATOM   2552 HD23 LEU A 174     -22.832   6.822 -13.528  1.00  0.00           H  
ATOM   2553  N   ALA A 175     -21.539   3.483 -18.084  1.00 93.43           N  
ANISOU 2553  N   ALA A 175    18675   7235   9587  -2933   4303  -3102
ATOM   2554  CA  ALA A 175     -21.159   2.182 -18.633  1.00 97.92           C  
ANISOU 2554  CA  ALA A 175    19819   7270  10117  -2895   4584  -3305
ATOM   2555  C   ALA A 175     -19.662   1.866 -18.473  1.00 99.34           C  
ANISOU 2555  C   ALA A 175    19945   7133  10666  -2249   4757  -3341
ATOM   2556  O   ALA A 175     -19.327   0.697 -18.286  1.00102.78           O  
ANISOU 2556  O   ALA A 175    20828   7035  11189  -2056   4900  -3407
ATOM   2557  CB  ALA A 175     -21.585   2.101 -20.106  1.00101.13           C  
ANISOU 2557  CB  ALA A 175    20469   7742  10214  -3311   4792  -3562
ATOM   2558  H   ALA A 175     -21.816   4.189 -18.752  1.00  0.00           H  
ATOM   2559  HA  ALA A 175     -21.714   1.416 -18.088  1.00  0.00           H  
ATOM   2560  HB1 ALA A 175     -21.309   1.141 -20.545  1.00  0.00           H  
ATOM   2561  HB2 ALA A 175     -22.666   2.202 -20.206  1.00  0.00           H  
ATOM   2562  HB3 ALA A 175     -21.121   2.884 -20.706  1.00  0.00           H  
ATOM   2563  N   SER A 176     -18.801   2.897 -18.535  1.00104.08           N  
ANISOU 2563  N   SER A 176    20004   8049  11491  -1914   4737  -3292
ATOM   2564  CA  SER A 176     -17.350   2.758 -18.419  1.00105.36           C  
ANISOU 2564  CA  SER A 176    20040   7972  12020  -1310   4904  -3337
ATOM   2565  C   SER A 176     -16.851   2.797 -16.962  1.00104.10           C  
ANISOU 2565  C   SER A 176    19639   7744  12170   -884   4646  -3061
ATOM   2566  O   SER A 176     -16.046   1.941 -16.598  1.00106.35           O  
ANISOU 2566  O   SER A 176    20106   7596  12707   -458   4729  -3063
ATOM   2567  CB  SER A 176     -16.658   3.795 -19.335  1.00105.29           C  
ANISOU 2567  CB  SER A 176    19603   8317  12087  -1188   5059  -3455
ATOM   2568  OG  SER A 176     -16.739   5.123 -18.857  1.00100.72           O  
ANISOU 2568  OG  SER A 176    18481   8248  11540  -1226   4787  -3250
ATOM   2569  H   SER A 176     -19.146   3.831 -18.708  1.00  0.00           H  
ATOM   2570  HA  SER A 176     -17.076   1.780 -18.819  1.00  0.00           H  
ATOM   2571  HB3 SER A 176     -17.078   3.756 -20.341  1.00  0.00           H  
ATOM   2572  HB2 SER A 176     -15.601   3.545 -19.432  1.00  0.00           H  
ATOM   2573  HG  SER A 176     -16.100   5.226 -18.143  1.00  0.00           H  
ATOM   2574  N   ASP A 177     -17.304   3.792 -16.177  1.00110.50           N  
ANISOU 2574  N   ASP A 177    20049   8966  12971   -984   4332  -2826
ATOM   2575  CA  ASP A 177     -16.728   4.151 -14.871  1.00108.78           C  
ANISOU 2575  CA  ASP A 177    19582   8730  13018   -610   4077  -2564
ATOM   2576  C   ASP A 177     -17.753   4.148 -13.721  1.00106.62           C  
ANISOU 2576  C   ASP A 177    19404   8526  12580   -904   3781  -2342
ATOM   2577  O   ASP A 177     -17.338   4.254 -12.566  1.00105.25           O  
ANISOU 2577  O   ASP A 177    19118   8294  12578   -646   3563  -2120
ATOM   2578  CB  ASP A 177     -16.030   5.534 -14.890  1.00111.90           C  
ANISOU 2578  CB  ASP A 177    19335   9557  13625   -349   3994  -2486
ATOM   2579  CG  ASP A 177     -14.986   5.788 -15.984  1.00111.88           C  
ANISOU 2579  CG  ASP A 177    19153   9613  13743   -149   4297  -2713
ATOM   2580  OD1 ASP A 177     -14.450   4.810 -16.549  1.00112.28           O  
ANISOU 2580  OD1 ASP A 177    19512   9263  13887     59   4570  -2900
ATOM   2581  OD2 ASP A 177     -14.695   6.985 -16.193  1.00112.85           O1-
ANISOU 2581  OD2 ASP A 177    18843  10170  13864   -206   4276  -2711
ATOM   2582  H   ASP A 177     -17.974   4.450 -16.554  1.00  0.00           H  
ATOM   2583  HA  ASP A 177     -15.975   3.413 -14.588  1.00  0.00           H  
ATOM   2584  HB3 ASP A 177     -15.560   5.727 -13.927  1.00  0.00           H  
ATOM   2585  HB2 ASP A 177     -16.814   6.273 -15.040  1.00  0.00           H  
ATOM   2586  N   GLY A 178     -19.058   4.048 -14.028  1.00100.83           N  
ANISOU 2586  N   GLY A 178    18862   7931  11517  -1446   3773  -2402
ATOM   2587  CA  GLY A 178     -20.130   4.092 -13.034  1.00100.52           C  
ANISOU 2587  CA  GLY A 178    18904   7984  11307  -1770   3541  -2230
ATOM   2588  C   GLY A 178     -20.363   5.523 -12.530  1.00 99.73           C  
ANISOU 2588  C   GLY A 178    18265   8388  11241  -1804   3307  -2067
ATOM   2589  O   GLY A 178     -20.030   6.504 -13.200  1.00 99.27           O  
ANISOU 2589  O   GLY A 178    17791   8669  11256  -1721   3320  -2107
ATOM   2590  H   GLY A 178     -19.335   3.960 -14.996  1.00  0.00           H  
ATOM   2591  HA3 GLY A 178     -19.892   3.432 -12.198  1.00  0.00           H  
ATOM   2592  HA2 GLY A 178     -21.056   3.722 -13.470  1.00  0.00           H  
ATOM   2593  N   ILE A 179     -20.967   5.620 -11.335  1.00 96.29           N  
ANISOU 2593  N   ILE A 179    17857   7988  10741  -1942   3107  -1890
ATOM   2594  CA  ILE A 179     -21.271   6.871 -10.634  1.00 92.54           C  
ANISOU 2594  CA  ILE A 179    16909   7966  10285  -1997   2900  -1750
ATOM   2595  C   ILE A 179     -20.009   7.682 -10.248  1.00 90.33           C  
ANISOU 2595  C   ILE A 179    16209   7810  10301  -1518   2817  -1650
ATOM   2596  O   ILE A 179     -20.080   8.907 -10.198  1.00 87.47           O  
ANISOU 2596  O   ILE A 179    15412   7850   9973  -1535   2727  -1618
ATOM   2597  CB  ILE A 179     -22.134   6.585  -9.365  1.00 96.15           C  
ANISOU 2597  CB  ILE A 179    17529   8404  10597  -2254   2739  -1598
ATOM   2598  CG1 ILE A 179     -22.809   7.839  -8.764  1.00 96.32           C  
ANISOU 2598  CG1 ILE A 179    17096   8905  10598  -2390   2572  -1506
ATOM   2599  CG2 ILE A 179     -21.380   5.818  -8.257  1.00 96.66           C  
ANISOU 2599  CG2 ILE A 179    17881   8066  10778  -1968   2653  -1437
ATOM   2600  CD1 ILE A 179     -23.768   8.545  -9.733  1.00 95.82           C  
ANISOU 2600  CD1 ILE A 179    16818   9210  10379  -2752   2608  -1630
ATOM   2601  H   ILE A 179     -21.231   4.775 -10.850  1.00  0.00           H  
ATOM   2602  HA  ILE A 179     -21.848   7.484 -11.328  1.00  0.00           H  
ATOM   2603  HB  ILE A 179     -22.944   5.928  -9.686  1.00  0.00           H  
ATOM   2604 HG13 ILE A 179     -22.059   8.544  -8.407  1.00  0.00           H  
ATOM   2605 HG12 ILE A 179     -23.379   7.550  -7.880  1.00  0.00           H  
ATOM   2606 HG21 ILE A 179     -22.064   5.508  -7.466  1.00  0.00           H  
ATOM   2607 HG22 ILE A 179     -20.907   4.915  -8.644  1.00  0.00           H  
ATOM   2608 HG23 ILE A 179     -20.606   6.428  -7.790  1.00  0.00           H  
ATOM   2609 HD11 ILE A 179     -24.529   9.103  -9.187  1.00  0.00           H  
ATOM   2610 HD12 ILE A 179     -23.234   9.248 -10.372  1.00  0.00           H  
ATOM   2611 HD13 ILE A 179     -24.284   7.835 -10.380  1.00  0.00           H  
ATOM   2612  N   ALA A 180     -18.867   6.998 -10.049  1.00 91.85           N  
ANISOU 2612  N   ALA A 180    16532   7657  10712  -1097   2845  -1605
ATOM   2613  CA  ALA A 180     -17.560   7.607  -9.789  1.00 90.77           C  
ANISOU 2613  CA  ALA A 180    15999   7623  10868   -643   2762  -1510
ATOM   2614  C   ALA A 180     -17.002   8.424 -10.970  1.00 89.27           C  
ANISOU 2614  C   ALA A 180    15455   7712  10752   -576   2915  -1665
ATOM   2615  O   ALA A 180     -16.233   9.353 -10.728  1.00 86.94           O  
ANISOU 2615  O   ALA A 180    14718   7718  10599   -411   2811  -1587
ATOM   2616  CB  ALA A 180     -16.571   6.504  -9.388  1.00 95.58           C  
ANISOU 2616  CB  ALA A 180    16837   7778  11700   -215   2779  -1455
ATOM   2617  H   ALA A 180     -18.877   5.992 -10.127  1.00  0.00           H  
ATOM   2618  HA  ALA A 180     -17.672   8.288  -8.943  1.00  0.00           H  
ATOM   2619  HB1 ALA A 180     -15.589   6.918  -9.155  1.00  0.00           H  
ATOM   2620  HB2 ALA A 180     -16.917   5.970  -8.502  1.00  0.00           H  
ATOM   2621  HB3 ALA A 180     -16.442   5.773 -10.187  1.00  0.00           H  
ATOM   2622  N   GLY A 181     -17.407   8.086 -12.209  1.00 88.90           N  
ANISOU 2622  N   GLY A 181    15631   7570  10579   -748   3158  -1881
ATOM   2623  CA  GLY A 181     -17.033   8.816 -13.422  1.00 88.85           C  
ANISOU 2623  CA  GLY A 181    15376   7809  10573   -765   3329  -2044
ATOM   2624  C   GLY A 181     -17.781  10.150 -13.532  1.00 86.07           C  
ANISOU 2624  C   GLY A 181    14682   7931  10090  -1048   3189  -1993
ATOM   2625  O   GLY A 181     -17.203  11.125 -14.009  1.00 85.04           O  
ANISOU 2625  O   GLY A 181    14196   8065  10051   -942   3213  -2013
ATOM   2626  H   GLY A 181     -18.046   7.311 -12.325  1.00  0.00           H  
ATOM   2627  HA3 GLY A 181     -17.303   8.224 -14.293  1.00  0.00           H  
ATOM   2628  HA2 GLY A 181     -15.954   8.977 -13.459  1.00  0.00           H  
ATOM   2629  N   LEU A 182     -19.042  10.197 -13.070  1.00 81.95           N  
ANISOU 2629  N   LEU A 182    14259   7514   9365  -1402   3042  -1925
ATOM   2630  CA  LEU A 182     -19.870  11.404 -13.018  1.00 80.59           C  
ANISOU 2630  CA  LEU A 182    13768   7765   9087  -1656   2890  -1869
ATOM   2631  C   LEU A 182     -19.440  12.362 -11.897  1.00 79.76           C  
ANISOU 2631  C   LEU A 182    13293   7861   9153  -1448   2684  -1687
ATOM   2632  O   LEU A 182     -19.444  13.574 -12.109  1.00 78.96           O  
ANISOU 2632  O   LEU A 182    12847   8079   9074  -1474   2607  -1659
ATOM   2633  CB  LEU A 182     -21.343  10.996 -12.822  1.00 78.67           C  
ANISOU 2633  CB  LEU A 182    13735   7563   8591  -2094   2828  -1879
ATOM   2634  CG  LEU A 182     -21.975  10.280 -14.030  1.00 81.29           C  
ANISOU 2634  CG  LEU A 182    14426   7755   8705  -2395   3000  -2059
ATOM   2635  CD1 LEU A 182     -23.364   9.754 -13.648  1.00 81.50           C  
ANISOU 2635  CD1 LEU A 182    14623   7837   8506  -2824   2919  -2052
ATOM   2636  CD2 LEU A 182     -22.048  11.199 -15.263  1.00 81.29           C  
ANISOU 2636  CD2 LEU A 182    14256   7993   8637  -2490   3069  -2164
ATOM   2637  H   LEU A 182     -19.458   9.359 -12.691  1.00  0.00           H  
ATOM   2638  HA  LEU A 182     -19.767  11.940 -13.962  1.00  0.00           H  
ATOM   2639  HB3 LEU A 182     -21.936  11.880 -12.593  1.00  0.00           H  
ATOM   2640  HB2 LEU A 182     -21.425  10.357 -11.944  1.00  0.00           H  
ATOM   2641  HG  LEU A 182     -21.368   9.412 -14.290  1.00  0.00           H  
ATOM   2642 HD11 LEU A 182     -23.850   9.270 -14.492  1.00  0.00           H  
ATOM   2643 HD12 LEU A 182     -23.299   9.023 -12.844  1.00  0.00           H  
ATOM   2644 HD13 LEU A 182     -24.012  10.560 -13.304  1.00  0.00           H  
ATOM   2645 HD21 LEU A 182     -22.902  10.967 -15.898  1.00  0.00           H  
ATOM   2646 HD22 LEU A 182     -22.128  12.249 -14.982  1.00  0.00           H  
ATOM   2647 HD23 LEU A 182     -21.151  11.098 -15.872  1.00  0.00           H  
ATOM   2648  N   TYR A 183     -19.068  11.792 -10.738  1.00 84.84           N  
ANISOU 2648  N   TYR A 183    14036   8300   9900  -1255   2588  -1560
ATOM   2649  CA  TYR A 183     -18.614  12.506  -9.545  1.00 83.21           C  
ANISOU 2649  CA  TYR A 183    13537   8253   9827  -1082   2387  -1387
ATOM   2650  C   TYR A 183     -17.083  12.457  -9.413  1.00 83.43           C  
ANISOU 2650  C   TYR A 183    13392   8191  10117   -649   2392  -1341
ATOM   2651  O   TYR A 183     -16.563  12.314  -8.305  1.00 82.77           O  
ANISOU 2651  O   TYR A 183    13250   8048  10151   -450   2226  -1181
ATOM   2652  CB  TYR A 183     -19.359  11.963  -8.306  1.00 85.51           C  
ANISOU 2652  CB  TYR A 183    14059   8412  10020  -1211   2247  -1259
ATOM   2653  CG  TYR A 183     -20.824  12.357  -8.249  1.00 84.47           C  
ANISOU 2653  CG  TYR A 183    13936   8491   9669  -1627   2212  -1287
ATOM   2654  CD1 TYR A 183     -21.793  11.606  -8.941  1.00 84.56           C  
ANISOU 2654  CD1 TYR A 183    14211   8429   9488  -1943   2333  -1412
ATOM   2655  CD2 TYR A 183     -21.224  13.490  -7.510  1.00 83.16           C  
ANISOU 2655  CD2 TYR A 183    13495   8609   9494  -1708   2067  -1201
ATOM   2656  CE1 TYR A 183     -23.147  11.978  -8.895  1.00 83.41           C  
ANISOU 2656  CE1 TYR A 183    14009   8517   9167  -2319   2294  -1440
ATOM   2657  CE2 TYR A 183     -22.580  13.866  -7.462  1.00 82.01           C  
ANISOU 2657  CE2 TYR A 183    13301   8675   9185  -2057   2053  -1243
ATOM   2658  CZ  TYR A 183     -23.542  13.109  -8.160  1.00 82.19           C  
ANISOU 2658  CZ  TYR A 183    13545   8647   9037  -2357   2159  -1357
ATOM   2659  OH  TYR A 183     -24.858  13.460  -8.142  1.00 81.30           O  
ANISOU 2659  OH  TYR A 183    13341   8770   8782  -2701   2138  -1399
ATOM   2660  H   TYR A 183     -19.105  10.785 -10.658  1.00  0.00           H  
ATOM   2661  HA  TYR A 183     -18.866  13.556  -9.636  1.00  0.00           H  
ATOM   2662  HB3 TYR A 183     -18.903  12.343  -7.390  1.00  0.00           H  
ATOM   2663  HB2 TYR A 183     -19.269  10.877  -8.252  1.00  0.00           H  
ATOM   2664  HD1 TYR A 183     -21.506  10.745  -9.519  1.00  0.00           H  
ATOM   2665  HD2 TYR A 183     -20.490  14.076  -6.984  1.00  0.00           H  
ATOM   2666  HE1 TYR A 183     -23.885  11.406  -9.437  1.00  0.00           H  
ATOM   2667  HE2 TYR A 183     -22.872  14.740  -6.900  1.00  0.00           H  
ATOM   2668  HH  TYR A 183     -25.055  14.155  -7.503  1.00  0.00           H  
ATOM   2669  N   ARG A 184     -16.377  12.588 -10.549  1.00 89.75           N  
ANISOU 2669  N   ARG A 184    14100   8999  11004   -519   2581  -1480
ATOM   2670  CA  ARG A 184     -14.920  12.535 -10.604  1.00 90.48           C  
ANISOU 2670  CA  ARG A 184    13984   9028  11364   -108   2624  -1466
ATOM   2671  C   ARG A 184     -14.307  13.855 -10.107  1.00 89.55           C  
ANISOU 2671  C   ARG A 184    13421   9239  11365    -11   2443  -1337
ATOM   2672  O   ARG A 184     -14.579  14.905 -10.689  1.00 88.69           O  
ANISOU 2672  O   ARG A 184    13103   9430  11166   -213   2432  -1366
ATOM   2673  CB  ARG A 184     -14.489  12.163 -12.038  1.00 99.48           C  
ANISOU 2673  CB  ARG A 184    15141  10118  12540    -42   2917  -1680
ATOM   2674  CG  ARG A 184     -12.993  11.832 -12.208  1.00101.73           C  
ANISOU 2674  CG  ARG A 184    15303  10228  13120    410   3027  -1709
ATOM   2675  CD  ARG A 184     -12.550  10.517 -11.535  1.00104.14           C  
ANISOU 2675  CD  ARG A 184    15917  10108  13544    663   2971  -1630
ATOM   2676  NE  ARG A 184     -13.160   9.337 -12.168  1.00106.84           N  
ANISOU 2676  NE  ARG A 184    16755  10093  13745    537   3181  -1789
ATOM   2677  CZ  ARG A 184     -13.244   8.107 -11.632  1.00109.64           C  
ANISOU 2677  CZ  ARG A 184    17486  10005  14169    716   3181  -1755
ATOM   2678  NH1 ARG A 184     -12.768   7.842 -10.406  1.00110.31           N  
ANISOU 2678  NH1 ARG A 184    17498   9950  14465   1047   2961  -1548
ATOM   2679  NH2 ARG A 184     -13.810   7.123 -12.341  1.00112.28           N1+
ANISOU 2679  NH2 ARG A 184    18292  10020  14351    554   3389  -1920
ATOM   2680  H   ARG A 184     -16.859  12.712 -11.428  1.00  0.00           H  
ATOM   2681  HA  ARG A 184     -14.608  11.735  -9.933  1.00  0.00           H  
ATOM   2682  HB3 ARG A 184     -14.757  12.973 -12.719  1.00  0.00           H  
ATOM   2683  HB2 ARG A 184     -15.070  11.302 -12.369  1.00  0.00           H  
ATOM   2684  HG3 ARG A 184     -12.339  12.659 -11.931  1.00  0.00           H  
ATOM   2685  HG2 ARG A 184     -12.848  11.700 -13.282  1.00  0.00           H  
ATOM   2686  HD3 ARG A 184     -12.938  10.510 -10.519  1.00  0.00           H  
ATOM   2687  HD2 ARG A 184     -11.467  10.441 -11.438  1.00  0.00           H  
ATOM   2688  HE  ARG A 184     -13.498   9.470 -13.111  1.00  0.00           H  
ATOM   2689 HH12 ARG A 184     -12.832   6.912 -10.018  1.00  0.00           H  
ATOM   2690 HH11 ARG A 184     -12.339   8.577  -9.864  1.00  0.00           H  
ATOM   2691 HH22 ARG A 184     -13.880   6.189 -11.962  1.00  0.00           H  
ATOM   2692 HH21 ARG A 184     -14.152   7.297 -13.276  1.00  0.00           H  
ATOM   2693  N   GLY A 185     -13.506  13.769  -9.032  1.00 91.33           N  
ANISOU 2693  N   GLY A 185    13535   9388  11777    277   2280  -1183
ATOM   2694  CA  GLY A 185     -12.882  14.923  -8.383  1.00 89.68           C  
ANISOU 2694  CA  GLY A 185    12940   9457  11678    367   2081  -1045
ATOM   2695  C   GLY A 185     -13.813  15.592  -7.354  1.00 86.93           C  
ANISOU 2695  C   GLY A 185    12602   9276  11150     89   1882   -934
ATOM   2696  O   GLY A 185     -13.592  16.759  -7.029  1.00 84.92           O  
ANISOU 2696  O   GLY A 185    12058   9316  10892      2   1800   -905
ATOM   2697  H   GLY A 185     -13.337  12.865  -8.615  1.00  0.00           H  
ATOM   2698  HA3 GLY A 185     -12.565  15.660  -9.124  1.00  0.00           H  
ATOM   2699  HA2 GLY A 185     -11.980  14.589  -7.869  1.00  0.00           H  
ATOM   2700  N   PHE A 186     -14.848  14.888  -6.857  1.00 86.31           N  
ANISOU 2700  N   PHE A 186    12872   9001  10921    -62   1818   -879
ATOM   2701  CA  PHE A 186     -15.844  15.411  -5.912  1.00 85.14           C  
ANISOU 2701  CA  PHE A 186    12764   8997  10587   -353   1681   -809
ATOM   2702  C   PHE A 186     -15.295  15.770  -4.513  1.00 84.84           C  
ANISOU 2702  C   PHE A 186    12590   9043  10600   -261   1441   -627
ATOM   2703  O   PHE A 186     -15.854  16.659  -3.879  1.00 84.12           O  
ANISOU 2703  O   PHE A 186    12356   9188  10418   -446   1355   -604
ATOM   2704  CB  PHE A 186     -17.041  14.434  -5.842  1.00 84.33           C  
ANISOU 2704  CB  PHE A 186    13081   8671  10288   -589   1725   -829
ATOM   2705  CG  PHE A 186     -18.203  14.835  -4.943  1.00 83.29           C  
ANISOU 2705  CG  PHE A 186    12987   8698   9961   -913   1636   -792
ATOM   2706  CD1 PHE A 186     -19.182  15.729  -5.423  1.00 82.77           C  
ANISOU 2706  CD1 PHE A 186    12804   8864   9779  -1182   1715   -908
ATOM   2707  CD2 PHE A 186     -18.244  14.444  -3.586  1.00 83.43           C  
ANISOU 2707  CD2 PHE A 186    13164   8628   9906   -952   1478   -643
ATOM   2708  CE1 PHE A 186     -20.218  16.138  -4.595  1.00 82.53           C  
ANISOU 2708  CE1 PHE A 186    12780   8980   9597  -1459   1662   -896
ATOM   2709  CE2 PHE A 186     -19.274  14.888  -2.766  1.00 82.95           C  
ANISOU 2709  CE2 PHE A 186    13140   8718   9658  -1266   1443   -639
ATOM   2710  CZ  PHE A 186     -20.262  15.725  -3.271  1.00 82.63           C  
ANISOU 2710  CZ  PHE A 186    12946   8912   9537  -1504   1548   -775
ATOM   2711  H   PHE A 186     -15.002  13.943  -7.180  1.00  0.00           H  
ATOM   2712  HA  PHE A 186     -16.223  16.338  -6.345  1.00  0.00           H  
ATOM   2713  HB3 PHE A 186     -16.698  13.439  -5.557  1.00  0.00           H  
ATOM   2714  HB2 PHE A 186     -17.452  14.333  -6.847  1.00  0.00           H  
ATOM   2715  HD1 PHE A 186     -19.141  16.082  -6.442  1.00  0.00           H  
ATOM   2716  HD2 PHE A 186     -17.475  13.802  -3.181  1.00  0.00           H  
ATOM   2717  HE1 PHE A 186     -20.985  16.793  -4.979  1.00  0.00           H  
ATOM   2718  HE2 PHE A 186     -19.306  14.584  -1.730  1.00  0.00           H  
ATOM   2719  HZ  PHE A 186     -21.061  16.065  -2.629  1.00  0.00           H  
ATOM   2720  N   GLY A 187     -14.228  15.086  -4.060  1.00 87.86           N  
ANISOU 2720  N   GLY A 187    13040   9223  11119     15   1329   -502
ATOM   2721  CA  GLY A 187     -13.618  15.243  -2.733  1.00 87.52           C  
ANISOU 2721  CA  GLY A 187    12916   9234  11105     95   1066   -306
ATOM   2722  C   GLY A 187     -13.072  16.661  -2.462  1.00 85.33           C  
ANISOU 2722  C   GLY A 187    12231   9302  10889     89    969   -284
ATOM   2723  O   GLY A 187     -13.530  17.286  -1.504  1.00 83.80           O  
ANISOU 2723  O   GLY A 187    12028   9264  10549   -128    852   -231
ATOM   2724  H   GLY A 187     -13.827  14.377  -4.656  1.00  0.00           H  
ATOM   2725  HA3 GLY A 187     -12.798  14.531  -2.641  1.00  0.00           H  
ATOM   2726  HA2 GLY A 187     -14.349  14.974  -1.969  1.00  0.00           H  
ATOM   2727  N   PRO A 188     -12.152  17.212  -3.288  1.00 84.19           N  
ANISOU 2727  N   PRO A 188    11754   9285  10950    303   1029   -335
ATOM   2728  CA  PRO A 188     -11.704  18.611  -3.141  1.00 82.59           C  
ANISOU 2728  CA  PRO A 188    11190   9400  10790    260    931   -309
ATOM   2729  C   PRO A 188     -12.773  19.660  -3.508  1.00 79.14           C  
ANISOU 2729  C   PRO A 188    10757   9137  10175    -57   1032   -425
ATOM   2730  O   PRO A 188     -12.684  20.783  -3.014  1.00 77.88           O  
ANISOU 2730  O   PRO A 188    10462   9176   9955   -196    922   -389
ATOM   2731  CB  PRO A 188     -10.465  18.699  -4.045  1.00 85.79           C  
ANISOU 2731  CB  PRO A 188    11284   9881  11431    512   1049   -380
ATOM   2732  CG  PRO A 188     -10.698  17.638  -5.109  1.00 87.44           C  
ANISOU 2732  CG  PRO A 188    11704   9853  11667    601   1285   -512
ATOM   2733  CD  PRO A 188     -11.391  16.523  -4.333  1.00 88.51           C  
ANISOU 2733  CD  PRO A 188    12243   9694  11691    572   1207   -431
ATOM   2734  HA  PRO A 188     -11.400  18.797  -2.110  1.00  0.00           H  
ATOM   2735  HB3 PRO A 188      -9.578  18.444  -3.464  1.00  0.00           H  
ATOM   2736  HB2 PRO A 188     -10.296  19.689  -4.469  1.00  0.00           H  
ATOM   2737  HG3 PRO A 188      -9.784  17.317  -5.609  1.00  0.00           H  
ATOM   2738  HG2 PRO A 188     -11.374  18.031  -5.869  1.00  0.00           H  
ATOM   2739  HD2 PRO A 188     -11.993  15.909  -4.998  1.00  0.00           H  
ATOM   2740  HD3 PRO A 188     -10.654  15.877  -3.855  1.00  0.00           H  
ATOM   2741  N   SER A 189     -13.772  19.273  -4.324  1.00 79.54           N  
ANISOU 2741  N   SER A 189    10980   9100  10141   -173   1228   -560
ATOM   2742  CA  SER A 189     -14.916  20.116  -4.677  1.00 77.20           C  
ANISOU 2742  CA  SER A 189    10681   8957   9696   -451   1303   -659
ATOM   2743  C   SER A 189     -15.840  20.355  -3.473  1.00 76.62           C  
ANISOU 2743  C   SER A 189    10733   8919   9458   -666   1188   -604
ATOM   2744  O   SER A 189     -16.219  21.502  -3.243  1.00 75.42           O  
ANISOU 2744  O   SER A 189    10431   8960   9265   -795   1145   -619
ATOM   2745  CB  SER A 189     -15.715  19.495  -5.838  1.00 81.29           C  
ANISOU 2745  CB  SER A 189    11355   9382  10150   -539   1505   -800
ATOM   2746  OG  SER A 189     -14.916  19.361  -6.991  1.00 82.81           O  
ANISOU 2746  OG  SER A 189    11412   9587  10464   -386   1642   -879
ATOM   2747  H   SER A 189     -13.780  18.334  -4.695  1.00  0.00           H  
ATOM   2748  HA  SER A 189     -14.536  21.086  -5.002  1.00  0.00           H  
ATOM   2749  HB3 SER A 189     -16.564  20.131  -6.094  1.00  0.00           H  
ATOM   2750  HB2 SER A 189     -16.129  18.525  -5.574  1.00  0.00           H  
ATOM   2751  HG  SER A 189     -14.453  18.517  -6.957  1.00  0.00           H  
ATOM   2752  N   VAL A 190     -16.170  19.284  -2.724  1.00 74.20           N  
ANISOU 2752  N   VAL A 190    10715   8415   9064   -698   1143   -537
ATOM   2753  CA  VAL A 190     -17.039  19.347  -1.547  1.00 74.10           C  
ANISOU 2753  CA  VAL A 190    10837   8439   8878   -922   1059   -493
ATOM   2754  C   VAL A 190     -16.356  19.990  -0.321  1.00 74.19           C  
ANISOU 2754  C   VAL A 190    10749   8555   8887   -897    861   -367
ATOM   2755  O   VAL A 190     -17.045  20.636   0.467  1.00 73.70           O  
ANISOU 2755  O   VAL A 190    10682   8623   8697  -1103    840   -391
ATOM   2756  CB  VAL A 190     -17.685  17.975  -1.187  1.00 79.79           C  
ANISOU 2756  CB  VAL A 190    11941   8909   9468  -1022   1097   -470
ATOM   2757  CG1 VAL A 190     -16.731  16.935  -0.576  1.00 82.54           C  
ANISOU 2757  CG1 VAL A 190    12465   9009   9889   -795    964   -313
ATOM   2758  CG2 VAL A 190     -18.926  18.128  -0.287  1.00 79.11           C  
ANISOU 2758  CG2 VAL A 190    12005   8887   9167  -1337   1098   -484
ATOM   2759  H   VAL A 190     -15.839  18.364  -2.985  1.00  0.00           H  
ATOM   2760  HA  VAL A 190     -17.861  20.000  -1.819  1.00  0.00           H  
ATOM   2761  HB  VAL A 190     -18.041  17.546  -2.124  1.00  0.00           H  
ATOM   2762 HG11 VAL A 190     -17.257  16.003  -0.367  1.00  0.00           H  
ATOM   2763 HG12 VAL A 190     -15.931  16.692  -1.266  1.00  0.00           H  
ATOM   2764 HG13 VAL A 190     -16.286  17.273   0.360  1.00  0.00           H  
ATOM   2765 HG21 VAL A 190     -19.432  17.172  -0.155  1.00  0.00           H  
ATOM   2766 HG22 VAL A 190     -18.669  18.502   0.704  1.00  0.00           H  
ATOM   2767 HG23 VAL A 190     -19.648  18.815  -0.726  1.00  0.00           H  
ATOM   2768  N   ALA A 191     -15.019  19.874  -0.228  1.00 76.55           N  
ANISOU 2768  N   ALA A 191    10939   8816   9332   -651    724   -249
ATOM   2769  CA  ALA A 191     -14.193  20.591   0.745  1.00 76.61           C  
ANISOU 2769  CA  ALA A 191    10830   8950   9328   -651    512   -126
ATOM   2770  C   ALA A 191     -14.094  22.098   0.441  1.00 74.70           C  
ANISOU 2770  C   ALA A 191    10298   8972   9111   -746    548   -219
ATOM   2771  O   ALA A 191     -14.116  22.903   1.370  1.00 74.48           O  
ANISOU 2771  O   ALA A 191    10282   9059   8957   -932    484   -219
ATOM   2772  CB  ALA A 191     -12.796  19.958   0.788  1.00 80.33           C  
ANISOU 2772  CB  ALA A 191    11194   9347   9979   -354    346     22
ATOM   2773  H   ALA A 191     -14.523  19.314  -0.908  1.00  0.00           H  
ATOM   2774  HA  ALA A 191     -14.642  20.464   1.731  1.00  0.00           H  
ATOM   2775  HB1 ALA A 191     -12.171  20.433   1.545  1.00  0.00           H  
ATOM   2776  HB2 ALA A 191     -12.854  18.897   1.030  1.00  0.00           H  
ATOM   2777  HB3 ALA A 191     -12.284  20.052  -0.171  1.00  0.00           H  
ATOM   2778  N   GLY A 192     -14.014  22.454  -0.852  1.00 77.58           N  
ANISOU 2778  N   GLY A 192    10444   9409   9623   -634    671   -309
ATOM   2779  CA  GLY A 192     -13.951  23.837  -1.320  1.00 77.10           C  
ANISOU 2779  CA  GLY A 192    10146   9558   9592   -718    715   -391
ATOM   2780  C   GLY A 192     -15.295  24.552  -1.142  1.00 77.54           C  
ANISOU 2780  C   GLY A 192    10283   9667   9512   -947    804   -498
ATOM   2781  O   GLY A 192     -15.303  25.722  -0.765  1.00 77.37           O  
ANISOU 2781  O   GLY A 192    10159   9778   9462  -1054    766   -525
ATOM   2782  H   GLY A 192     -13.982  21.734  -1.561  1.00  0.00           H  
ATOM   2783  HA3 GLY A 192     -13.684  23.837  -2.377  1.00  0.00           H  
ATOM   2784  HA2 GLY A 192     -13.173  24.388  -0.795  1.00  0.00           H  
ATOM   2785  N   ILE A 193     -16.416  23.853  -1.395  1.00 71.76           N  
ANISOU 2785  N   ILE A 193     9734   8829   8702  -1024    923   -564
ATOM   2786  CA  ILE A 193     -17.758  24.431  -1.356  1.00 72.32           C  
ANISOU 2786  CA  ILE A 193     9831   8972   8676  -1220   1011   -672
ATOM   2787  C   ILE A 193     -18.349  24.507   0.067  1.00 72.76           C  
ANISOU 2787  C   ILE A 193    10027   9034   8586  -1381    957   -653
ATOM   2788  O   ILE A 193     -19.136  25.418   0.304  1.00 73.23           O  
ANISOU 2788  O   ILE A 193    10030   9196   8598  -1515   1010   -744
ATOM   2789  CB  ILE A 193     -18.734  23.676  -2.312  1.00 75.93           C  
ANISOU 2789  CB  ILE A 193    10389   9362   9099  -1283   1154   -760
ATOM   2790  CG1 ILE A 193     -19.847  24.584  -2.873  1.00 75.71           C  
ANISOU 2790  CG1 ILE A 193    10288   9456   9020  -1453   1227   -871
ATOM   2791  CG2 ILE A 193     -19.373  22.420  -1.694  1.00 75.75           C  
ANISOU 2791  CG2 ILE A 193    10647   9157   8977  -1326   1168   -719
ATOM   2792  CD1 ILE A 193     -19.330  25.717  -3.779  1.00 76.08           C  
ANISOU 2792  CD1 ILE A 193    10121   9627   9160  -1412   1218   -906
ATOM   2793  H   ILE A 193     -16.348  22.896  -1.716  1.00  0.00           H  
ATOM   2794  HA  ILE A 193     -17.671  25.461  -1.693  1.00  0.00           H  
ATOM   2795  HB  ILE A 193     -18.151  23.336  -3.169  1.00  0.00           H  
ATOM   2796 HG13 ILE A 193     -20.448  24.991  -2.062  1.00  0.00           H  
ATOM   2797 HG12 ILE A 193     -20.534  23.973  -3.461  1.00  0.00           H  
ATOM   2798 HG21 ILE A 193     -19.829  21.790  -2.454  1.00  0.00           H  
ATOM   2799 HG22 ILE A 193     -18.631  21.833  -1.167  1.00  0.00           H  
ATOM   2800 HG23 ILE A 193     -20.147  22.673  -0.972  1.00  0.00           H  
ATOM   2801 HD11 ILE A 193     -19.773  26.675  -3.511  1.00  0.00           H  
ATOM   2802 HD12 ILE A 193     -18.248  25.830  -3.750  1.00  0.00           H  
ATOM   2803 HD13 ILE A 193     -19.577  25.518  -4.821  1.00  0.00           H  
ATOM   2804  N   VAL A 194     -17.959  23.606   0.993  1.00 68.35           N  
ANISOU 2804  N   VAL A 194     9657   8359   7952  -1369    853   -537
ATOM   2805  CA  VAL A 194     -18.369  23.686   2.403  1.00 69.10           C  
ANISOU 2805  CA  VAL A 194     9926   8466   7864  -1569    811   -520
ATOM   2806  C   VAL A 194     -17.685  24.869   3.125  1.00 68.84           C  
ANISOU 2806  C   VAL A 194     9754   8571   7831  -1594    703   -504
ATOM   2807  O   VAL A 194     -18.326  25.507   3.959  1.00 69.65           O  
ANISOU 2807  O   VAL A 194     9908   8747   7811  -1782    754   -586
ATOM   2808  CB  VAL A 194     -18.126  22.357   3.185  1.00 72.99           C  
ANISOU 2808  CB  VAL A 194    10719   8778   8235  -1595    716   -385
ATOM   2809  CG1 VAL A 194     -16.649  22.013   3.429  1.00 73.17           C  
ANISOU 2809  CG1 VAL A 194    10713   8746   8341  -1393    493   -204
ATOM   2810  CG2 VAL A 194     -18.863  22.288   4.533  1.00 73.24           C  
ANISOU 2810  CG2 VAL A 194    10969   8829   8030  -1876    739   -406
ATOM   2811  H   VAL A 194     -17.328  22.856   0.744  1.00  0.00           H  
ATOM   2812  HA  VAL A 194     -19.444  23.873   2.414  1.00  0.00           H  
ATOM   2813  HB  VAL A 194     -18.535  21.555   2.569  1.00  0.00           H  
ATOM   2814 HG11 VAL A 194     -16.541  21.009   3.839  1.00  0.00           H  
ATOM   2815 HG12 VAL A 194     -16.108  22.038   2.493  1.00  0.00           H  
ATOM   2816 HG13 VAL A 194     -16.166  22.704   4.119  1.00  0.00           H  
ATOM   2817 HG21 VAL A 194     -18.655  21.348   5.045  1.00  0.00           H  
ATOM   2818 HG22 VAL A 194     -18.575  23.095   5.206  1.00  0.00           H  
ATOM   2819 HG23 VAL A 194     -19.938  22.330   4.394  1.00  0.00           H  
ATOM   2820  N   VAL A 195     -16.432  25.180   2.737  1.00 64.96           N  
ANISOU 2820  N   VAL A 195     9077   8124   7482  -1417    581   -422
ATOM   2821  CA  VAL A 195     -15.699  26.369   3.171  1.00 64.61           C  
ANISOU 2821  CA  VAL A 195     8888   8215   7446  -1454    468   -403
ATOM   2822  C   VAL A 195     -16.283  27.643   2.537  1.00 64.68           C  
ANISOU 2822  C   VAL A 195     8754   8316   7504  -1514    606   -556
ATOM   2823  O   VAL A 195     -16.555  28.590   3.272  1.00 65.24           O  
ANISOU 2823  O   VAL A 195     8861   8443   7483  -1666    622   -627
ATOM   2824  CB  VAL A 195     -14.178  26.270   2.843  1.00 64.78           C  
ANISOU 2824  CB  VAL A 195     8716   8278   7620  -1261    313   -278
ATOM   2825  CG1 VAL A 195     -13.379  27.587   2.989  1.00 64.93           C  
ANISOU 2825  CG1 VAL A 195     8564   8457   7650  -1339    221   -282
ATOM   2826  CG2 VAL A 195     -13.512  25.189   3.712  1.00 66.75           C  
ANISOU 2826  CG2 VAL A 195     9099   8426   7839  -1172    129   -103
ATOM   2827  H   VAL A 195     -15.971  24.603   2.047  1.00  0.00           H  
ATOM   2828  HA  VAL A 195     -15.810  26.456   4.254  1.00  0.00           H  
ATOM   2829  HB  VAL A 195     -14.076  25.948   1.805  1.00  0.00           H  
ATOM   2830 HG11 VAL A 195     -12.314  27.418   2.832  1.00  0.00           H  
ATOM   2831 HG12 VAL A 195     -13.680  28.342   2.263  1.00  0.00           H  
ATOM   2832 HG13 VAL A 195     -13.501  28.012   3.985  1.00  0.00           H  
ATOM   2833 HG21 VAL A 195     -12.470  25.042   3.429  1.00  0.00           H  
ATOM   2834 HG22 VAL A 195     -13.533  25.463   4.767  1.00  0.00           H  
ATOM   2835 HG23 VAL A 195     -14.013  24.226   3.617  1.00  0.00           H  
ATOM   2836  N   TYR A 196     -16.485  27.636   1.205  1.00 67.76           N  
ANISOU 2836  N   TYR A 196     9008   8708   8031  -1399    707   -607
ATOM   2837  CA  TYR A 196     -17.012  28.782   0.466  1.00 66.58           C  
ANISOU 2837  CA  TYR A 196     8731   8626   7939  -1435    802   -720
ATOM   2838  C   TYR A 196     -18.429  29.172   0.896  1.00 65.71           C  
ANISOU 2838  C   TYR A 196     8708   8513   7747  -1572    918   -844
ATOM   2839  O   TYR A 196     -18.615  30.315   1.298  1.00 65.42           O  
ANISOU 2839  O   TYR A 196     8638   8519   7701  -1645    935   -919
ATOM   2840  CB  TYR A 196     -16.959  28.560  -1.055  1.00 68.04           C  
ANISOU 2840  CB  TYR A 196     8792   8810   8249  -1316    877   -737
ATOM   2841  CG  TYR A 196     -17.450  29.766  -1.835  1.00 68.42           C  
ANISOU 2841  CG  TYR A 196     8742   8910   8344  -1358    940   -824
ATOM   2842  CD1 TYR A 196     -16.665  30.935  -1.864  1.00 68.34           C  
ANISOU 2842  CD1 TYR A 196     8631   8958   8377  -1380    884   -818
ATOM   2843  CD2 TYR A 196     -18.707  29.749  -2.475  1.00 68.88           C  
ANISOU 2843  CD2 TYR A 196     8821   8953   8399  -1390   1038   -905
ATOM   2844  CE1 TYR A 196     -17.102  32.063  -2.575  1.00 68.71           C  
ANISOU 2844  CE1 TYR A 196     8629   9010   8466  -1410    923   -881
ATOM   2845  CE2 TYR A 196     -19.151  30.882  -3.181  1.00 69.03           C  
ANISOU 2845  CE2 TYR A 196     8751   9005   8474  -1405   1059   -961
ATOM   2846  CZ  TYR A 196     -18.327  32.021  -3.258  1.00 68.92           C  
ANISOU 2846  CZ  TYR A 196     8668   9012   8506  -1404   1001   -945
ATOM   2847  OH  TYR A 196     -18.677  33.080  -4.029  1.00 69.06           O  
ANISOU 2847  OH  TYR A 196     8636   9023   8582  -1408   1003   -982
ATOM   2848  H   TYR A 196     -16.233  26.823   0.658  1.00  0.00           H  
ATOM   2849  HA  TYR A 196     -16.357  29.625   0.697  1.00  0.00           H  
ATOM   2850  HB3 TYR A 196     -17.554  27.691  -1.332  1.00  0.00           H  
ATOM   2851  HB2 TYR A 196     -15.942  28.337  -1.374  1.00  0.00           H  
ATOM   2852  HD1 TYR A 196     -15.725  30.969  -1.339  1.00  0.00           H  
ATOM   2853  HD2 TYR A 196     -19.329  28.867  -2.438  1.00  0.00           H  
ATOM   2854  HE1 TYR A 196     -16.490  32.951  -2.618  1.00  0.00           H  
ATOM   2855  HE2 TYR A 196     -20.097  30.859  -3.700  1.00  0.00           H  
ATOM   2856  HH  TYR A 196     -19.564  33.024  -4.418  1.00  0.00           H  
ATOM   2857  N   ARG A 197     -19.384  28.230   0.802  1.00 65.29           N  
ANISOU 2857  N   ARG A 197     8760   8408   7639  -1612   1007   -877
ATOM   2858  CA  ARG A 197     -20.781  28.451   1.174  1.00 66.09           C  
ANISOU 2858  CA  ARG A 197     8890   8541   7679  -1746   1133  -1007
ATOM   2859  C   ARG A 197     -20.985  28.628   2.679  1.00 66.80           C  
ANISOU 2859  C   ARG A 197     9116   8645   7619  -1903   1136  -1040
ATOM   2860  O   ARG A 197     -21.911  29.342   3.057  1.00 67.47           O  
ANISOU 2860  O   ARG A 197     9163   8781   7691  -1990   1246  -1176
ATOM   2861  CB  ARG A 197     -21.704  27.367   0.594  1.00 54.17           C  
ANISOU 2861  CB  ARG A 197     7451   6998   6133  -1798   1229  -1039
ATOM   2862  CG  ARG A 197     -21.728  27.357  -0.942  1.00 53.93           C  
ANISOU 2862  CG  ARG A 197     7292   6978   6220  -1699   1254  -1052
ATOM   2863  CD  ARG A 197     -22.513  28.534  -1.541  1.00 53.95           C  
ANISOU 2863  CD  ARG A 197     7103   7068   6329  -1669   1271  -1130
ATOM   2864  NE  ARG A 197     -22.354  28.587  -2.994  1.00 53.71           N  
ANISOU 2864  NE  ARG A 197     6982   7045   6379  -1591   1258  -1109
ATOM   2865  CZ  ARG A 197     -22.542  29.666  -3.767  1.00 53.60           C  
ANISOU 2865  CZ  ARG A 197     6828   7081   6458  -1549   1237  -1135
ATOM   2866  NH1 ARG A 197     -22.837  30.866  -3.259  1.00 53.66           N  
ANISOU 2866  NH1 ARG A 197     6756   7116   6516  -1546   1236  -1194
ATOM   2867  NH2 ARG A 197     -22.431  29.549  -5.089  1.00 53.51           N1+
ANISOU 2867  NH2 ARG A 197     6776   7076   6478  -1515   1217  -1104
ATOM   2868  H   ARG A 197     -19.150  27.299   0.480  1.00  0.00           H  
ATOM   2869  HA  ARG A 197     -21.079  29.381   0.712  1.00  0.00           H  
ATOM   2870  HB3 ARG A 197     -22.725  27.527   0.941  1.00  0.00           H  
ATOM   2871  HB2 ARG A 197     -21.406  26.393   0.980  1.00  0.00           H  
ATOM   2872  HG3 ARG A 197     -22.278  26.462  -1.224  1.00  0.00           H  
ATOM   2873  HG2 ARG A 197     -20.739  27.248  -1.384  1.00  0.00           H  
ATOM   2874  HD3 ARG A 197     -22.274  29.481  -1.061  1.00  0.00           H  
ATOM   2875  HD2 ARG A 197     -23.581  28.371  -1.393  1.00  0.00           H  
ATOM   2876  HE  ARG A 197     -22.231  27.691  -3.456  1.00  0.00           H  
ATOM   2877 HH12 ARG A 197     -22.946  31.652  -3.892  1.00  0.00           H  
ATOM   2878 HH11 ARG A 197     -22.930  31.004  -2.264  1.00  0.00           H  
ATOM   2879 HH22 ARG A 197     -22.596  30.360  -5.677  1.00  0.00           H  
ATOM   2880 HH21 ARG A 197     -22.216  28.640  -5.501  1.00  0.00           H  
ATOM   2881  N   GLY A 198     -20.093  28.044   3.499  1.00 68.02           N  
ANISOU 2881  N   GLY A 198     9425   8753   7666  -1934   1013   -917
ATOM   2882  CA  GLY A 198     -20.044  28.254   4.942  1.00 69.37           C  
ANISOU 2882  CA  GLY A 198     9765   8939   7652  -2116    989   -926
ATOM   2883  C   GLY A 198     -19.738  29.720   5.253  1.00 69.31           C  
ANISOU 2883  C   GLY A 198     9665   8999   7672  -2144    982  -1005
ATOM   2884  O   GLY A 198     -20.505  30.347   5.975  1.00 69.74           O  
ANISOU 2884  O   GLY A 198     9772   9082   7646  -2283   1112  -1152
ATOM   2885  H   GLY A 198     -19.363  27.468   3.102  1.00  0.00           H  
ATOM   2886  HA3 GLY A 198     -19.276  27.619   5.383  1.00  0.00           H  
ATOM   2887  HA2 GLY A 198     -20.997  27.979   5.388  1.00  0.00           H  
ATOM   2888  N   LEU A 199     -18.668  30.278   4.663  1.00 69.39           N  
ANISOU 2888  N   LEU A 199     9531   9029   7807  -2014    854   -926
ATOM   2889  CA  LEU A 199     -18.278  31.679   4.823  1.00 69.58           C  
ANISOU 2889  CA  LEU A 199     9490   9093   7856  -2055    831   -987
ATOM   2890  C   LEU A 199     -19.229  32.660   4.113  1.00 69.77           C  
ANISOU 2890  C   LEU A 199     9397   9106   8007  -2002    988  -1141
ATOM   2891  O   LEU A 199     -19.494  33.721   4.667  1.00 70.40           O  
ANISOU 2891  O   LEU A 199     9512   9174   8062  -2082   1057  -1261
ATOM   2892  CB  LEU A 199     -16.828  31.869   4.332  1.00 66.16           C  
ANISOU 2892  CB  LEU A 199     8928   8702   7509  -1968    653   -854
ATOM   2893  CG  LEU A 199     -15.762  31.157   5.193  1.00 65.76           C  
ANISOU 2893  CG  LEU A 199     8937   8673   7375  -1975    453   -680
ATOM   2894  CD1 LEU A 199     -14.389  31.194   4.500  1.00 65.17           C  
ANISOU 2894  CD1 LEU A 199     8657   8674   7432  -1870    309   -573
ATOM   2895  CD2 LEU A 199     -15.692  31.701   6.632  1.00 66.83           C  
ANISOU 2895  CD2 LEU A 199     9287   8824   7282  -2198    381   -679
ATOM   2896  H   LEU A 199     -18.075  29.715   4.066  1.00  0.00           H  
ATOM   2897  HA  LEU A 199     -18.321  31.914   5.887  1.00  0.00           H  
ATOM   2898  HB3 LEU A 199     -16.585  32.932   4.293  1.00  0.00           H  
ATOM   2899  HB2 LEU A 199     -16.765  31.510   3.304  1.00  0.00           H  
ATOM   2900  HG  LEU A 199     -16.038  30.106   5.267  1.00  0.00           H  
ATOM   2901 HD11 LEU A 199     -13.801  30.314   4.760  1.00  0.00           H  
ATOM   2902 HD12 LEU A 199     -14.484  31.204   3.414  1.00  0.00           H  
ATOM   2903 HD13 LEU A 199     -13.813  32.075   4.787  1.00  0.00           H  
ATOM   2904 HD21 LEU A 199     -14.666  31.883   6.955  1.00  0.00           H  
ATOM   2905 HD22 LEU A 199     -16.230  32.643   6.735  1.00  0.00           H  
ATOM   2906 HD23 LEU A 199     -16.130  30.993   7.336  1.00  0.00           H  
ATOM   2907  N   TYR A 200     -19.739  32.298   2.926  1.00 66.10           N  
ANISOU 2907  N   TYR A 200     8811   8632   7670  -1873   1043  -1139
ATOM   2908  CA  TYR A 200     -20.653  33.105   2.115  1.00 65.50           C  
ANISOU 2908  CA  TYR A 200     8614   8549   7724  -1807   1153  -1254
ATOM   2909  C   TYR A 200     -21.993  33.366   2.819  1.00 66.55           C  
ANISOU 2909  C   TYR A 200     8794   8688   7802  -1905   1317  -1424
ATOM   2910  O   TYR A 200     -22.356  34.521   3.016  1.00 67.32           O  
ANISOU 2910  O   TYR A 200     8904   8758   7916  -1933   1376  -1536
ATOM   2911  CB  TYR A 200     -20.817  32.438   0.737  1.00 60.06           C  
ANISOU 2911  CB  TYR A 200     7825   7867   7127  -1699   1162  -1206
ATOM   2912  CG  TYR A 200     -21.882  32.971  -0.203  1.00 60.12           C  
ANISOU 2912  CG  TYR A 200     7697   7882   7265  -1628   1226  -1287
ATOM   2913  CD1 TYR A 200     -21.580  34.027  -1.087  1.00 59.68           C  
ANISOU 2913  CD1 TYR A 200     7556   7799   7322  -1541   1164  -1259
ATOM   2914  CD2 TYR A 200     -23.157  32.368  -0.243  1.00 60.59           C  
ANISOU 2914  CD2 TYR A 200     7711   7981   7331  -1657   1329  -1370
ATOM   2915  CE1 TYR A 200     -22.538  34.453  -2.026  1.00 59.64           C  
ANISOU 2915  CE1 TYR A 200     7438   7787   7434  -1464   1179  -1298
ATOM   2916  CE2 TYR A 200     -24.116  32.806  -1.174  1.00 60.57           C  
ANISOU 2916  CE2 TYR A 200     7551   8002   7460  -1579   1349  -1423
ATOM   2917  CZ  TYR A 200     -23.802  33.832  -2.079  1.00 60.00           C  
ANISOU 2917  CZ  TYR A 200     7412   7884   7501  -1471   1260  -1377
ATOM   2918  OH  TYR A 200     -24.726  34.194  -3.013  1.00 60.00           O  
ANISOU 2918  OH  TYR A 200     7274   7895   7628  -1387   1239  -1399
ATOM   2919  H   TYR A 200     -19.452  31.417   2.518  1.00  0.00           H  
ATOM   2920  HA  TYR A 200     -20.162  34.061   1.947  1.00  0.00           H  
ATOM   2921  HB3 TYR A 200     -21.063  31.400   0.905  1.00  0.00           H  
ATOM   2922  HB2 TYR A 200     -19.861  32.440   0.210  1.00  0.00           H  
ATOM   2923  HD1 TYR A 200     -20.606  34.493  -1.068  1.00  0.00           H  
ATOM   2924  HD2 TYR A 200     -23.393  31.552   0.423  1.00  0.00           H  
ATOM   2925  HE1 TYR A 200     -22.285  35.245  -2.713  1.00  0.00           H  
ATOM   2926  HE2 TYR A 200     -25.081  32.329  -1.231  1.00  0.00           H  
ATOM   2927  HH  TYR A 200     -24.492  35.003  -3.481  1.00  0.00           H  
ATOM   2928  N   PHE A 201     -22.691  32.292   3.207  1.00 70.77           N  
ANISOU 2928  N   PHE A 201     9368   9257   8266  -1973   1406  -1451
ATOM   2929  CA  PHE A 201     -23.963  32.384   3.916  1.00 71.71           C  
ANISOU 2929  CA  PHE A 201     9498   9416   8333  -2087   1592  -1623
ATOM   2930  C   PHE A 201     -23.805  32.730   5.395  1.00 72.50           C  
ANISOU 2930  C   PHE A 201     9786   9507   8254  -2259   1640  -1690
ATOM   2931  O   PHE A 201     -24.578  33.540   5.903  1.00 73.11           O  
ANISOU 2931  O   PHE A 201     9841   9589   8349  -2297   1793  -1869
ATOM   2932  CB  PHE A 201     -24.718  31.061   3.761  1.00 70.05           C  
ANISOU 2932  CB  PHE A 201     9315   9252   8050  -2178   1666  -1619
ATOM   2933  CG  PHE A 201     -25.271  30.798   2.377  1.00 69.55           C  
ANISOU 2933  CG  PHE A 201     9069   9220   8136  -2065   1660  -1604
ATOM   2934  CD1 PHE A 201     -26.083  31.765   1.748  1.00 69.54           C  
ANISOU 2934  CD1 PHE A 201     8845   9257   8318  -1945   1699  -1696
ATOM   2935  CD2 PHE A 201     -25.125  29.528   1.780  1.00 69.23           C  
ANISOU 2935  CD2 PHE A 201     9099   9163   8043  -2091   1615  -1503
ATOM   2936  CE1 PHE A 201     -26.742  31.450   0.575  1.00 69.21           C  
ANISOU 2936  CE1 PHE A 201     8648   9261   8388  -1871   1665  -1668
ATOM   2937  CE2 PHE A 201     -25.775  29.245   0.589  1.00 69.02           C  
ANISOU 2937  CE2 PHE A 201     8931   9172   8121  -2030   1611  -1500
ATOM   2938  CZ  PHE A 201     -26.586  30.204  -0.007  1.00 69.01           C  
ANISOU 2938  CZ  PHE A 201     8703   9235   8284  -1931   1624  -1576
ATOM   2939  H   PHE A 201     -22.337  31.361   3.029  1.00  0.00           H  
ATOM   2940  HA  PHE A 201     -24.551  33.192   3.479  1.00  0.00           H  
ATOM   2941  HB3 PHE A 201     -25.538  30.993   4.475  1.00  0.00           H  
ATOM   2942  HB2 PHE A 201     -24.045  30.253   4.024  1.00  0.00           H  
ATOM   2943  HD1 PHE A 201     -26.254  32.730   2.199  1.00  0.00           H  
ATOM   2944  HD2 PHE A 201     -24.516  28.767   2.242  1.00  0.00           H  
ATOM   2945  HE1 PHE A 201     -27.381  32.181   0.116  1.00  0.00           H  
ATOM   2946  HE2 PHE A 201     -25.652  28.267   0.149  1.00  0.00           H  
ATOM   2947  HZ  PHE A 201     -27.115  30.007  -0.926  1.00  0.00           H  
ATOM   2948  N   GLY A 202     -22.806  32.116   6.048  1.00 75.52           N  
ANISOU 2948  N   GLY A 202    10358   9872   8466  -2360   1507  -1551
ATOM   2949  CA  GLY A 202     -22.563  32.248   7.477  1.00 76.47           C  
ANISOU 2949  CA  GLY A 202    10700   9993   8363  -2570   1516  -1587
ATOM   2950  C   GLY A 202     -22.151  33.669   7.841  1.00 76.66           C  
ANISOU 2950  C   GLY A 202    10727   9992   8410  -2577   1510  -1673
ATOM   2951  O   GLY A 202     -22.823  34.270   8.673  1.00 77.89           O  
ANISOU 2951  O   GLY A 202    10971  10146   8478  -2708   1683  -1859
ATOM   2952  H   GLY A 202     -22.199  31.482   5.547  1.00  0.00           H  
ATOM   2953  HA3 GLY A 202     -21.783  31.564   7.794  1.00  0.00           H  
ATOM   2954  HA2 GLY A 202     -23.466  31.977   8.019  1.00  0.00           H  
ATOM   2955  N   MET A 203     -21.103  34.222   7.202  1.00 75.94           N  
ANISOU 2955  N   MET A 203    10540   9874   8439  -2446   1338  -1559
ATOM   2956  CA  MET A 203     -20.641  35.588   7.471  1.00 76.54           C  
ANISOU 2956  CA  MET A 203    10649   9908   8525  -2484   1317  -1629
ATOM   2957  C   MET A 203     -21.621  36.671   7.010  1.00 77.04           C  
ANISOU 2957  C   MET A 203    10618   9905   8750  -2387   1508  -1829
ATOM   2958  O   MET A 203     -21.695  37.695   7.682  1.00 78.39           O  
ANISOU 2958  O   MET A 203    10910  10019   8856  -2488   1607  -1980
ATOM   2959  CB  MET A 203     -19.229  35.854   6.911  1.00 81.41           C  
ANISOU 2959  CB  MET A 203    11175  10531   9227  -2401   1097  -1460
ATOM   2960  CG  MET A 203     -18.148  34.912   7.462  1.00 81.37           C  
ANISOU 2960  CG  MET A 203    11250  10593   9073  -2492    885  -1272
ATOM   2961  SD  MET A 203     -17.906  35.061   9.255  1.00 80.98           S  
ANISOU 2961  SD  MET A 203    11500  10561   8708  -2809    877  -1337
ATOM   2962  CE  MET A 203     -16.539  33.901   9.494  1.00 81.23           C  
ANISOU 2962  CE  MET A 203    11596  10666   8602  -2852    579  -1058
ATOM   2963  H   MET A 203     -20.601  33.704   6.494  1.00  0.00           H  
ATOM   2964  HA  MET A 203     -20.580  35.689   8.556  1.00  0.00           H  
ATOM   2965  HB3 MET A 203     -18.937  36.874   7.160  1.00  0.00           H  
ATOM   2966  HB2 MET A 203     -19.235  35.836   5.824  1.00  0.00           H  
ATOM   2967  HG3 MET A 203     -17.200  35.122   6.967  1.00  0.00           H  
ATOM   2968  HG2 MET A 203     -18.393  33.876   7.234  1.00  0.00           H  
ATOM   2969  HE1 MET A 203     -16.271  33.851  10.549  1.00  0.00           H  
ATOM   2970  HE2 MET A 203     -16.821  32.904   9.164  1.00  0.00           H  
ATOM   2971  HE3 MET A 203     -15.665  34.221   8.928  1.00  0.00           H  
ATOM   2972  N   TYR A 204     -22.389  36.431   5.931  1.00 74.67           N  
ANISOU 2972  N   TYR A 204    10116   9604   8651  -2196   1559  -1835
ATOM   2973  CA  TYR A 204     -23.442  37.353   5.502  1.00 75.08           C  
ANISOU 2973  CA  TYR A 204    10050   9589   8886  -2066   1709  -2004
ATOM   2974  C   TYR A 204     -24.553  37.487   6.556  1.00 75.79           C  
ANISOU 2974  C   TYR A 204    10198   9698   8900  -2173   1957  -2231
ATOM   2975  O   TYR A 204     -24.790  38.597   7.024  1.00 76.68           O  
ANISOU 2975  O   TYR A 204    10362   9718   9056  -2165   2082  -2403
ATOM   2976  CB  TYR A 204     -23.993  36.974   4.115  1.00 73.99           C  
ANISOU 2976  CB  TYR A 204     9682   9478   8952  -1868   1682  -1945
ATOM   2977  CG  TYR A 204     -25.037  37.944   3.601  1.00 74.36           C  
ANISOU 2977  CG  TYR A 204     9581   9457   9215  -1701   1792  -2089
ATOM   2978  CD1 TYR A 204     -24.638  39.226   3.172  1.00 74.58           C  
ANISOU 2978  CD1 TYR A 204     9596   9351   9391  -1566   1702  -2060
ATOM   2979  CD2 TYR A 204     -26.402  37.592   3.593  1.00 74.81           C  
ANISOU 2979  CD2 TYR A 204     9502   9584   9338  -1676   1976  -2247
ATOM   2980  CE1 TYR A 204     -25.601  40.157   2.750  1.00 75.04           C  
ANISOU 2980  CE1 TYR A 204     9526   9316   9668  -1378   1771  -2168
ATOM   2981  CE2 TYR A 204     -27.363  38.520   3.152  1.00 75.26           C  
ANISOU 2981  CE2 TYR A 204     9380   9584   9631  -1483   2058  -2371
ATOM   2982  CZ  TYR A 204     -26.963  39.805   2.733  1.00 75.38           C  
ANISOU 2982  CZ  TYR A 204     9402   9437   9802  -1317   1943  -2323
ATOM   2983  OH  TYR A 204     -27.891  40.714   2.319  1.00 76.06           O  
ANISOU 2983  OH  TYR A 204     9326   9435  10137  -1097   1996  -2426
ATOM   2984  H   TYR A 204     -22.293  35.568   5.414  1.00  0.00           H  
ATOM   2985  HA  TYR A 204     -22.983  38.338   5.405  1.00  0.00           H  
ATOM   2986  HB3 TYR A 204     -24.409  35.965   4.131  1.00  0.00           H  
ATOM   2987  HB2 TYR A 204     -23.186  36.963   3.385  1.00  0.00           H  
ATOM   2988  HD1 TYR A 204     -23.595  39.504   3.189  1.00  0.00           H  
ATOM   2989  HD2 TYR A 204     -26.715  36.613   3.924  1.00  0.00           H  
ATOM   2990  HE1 TYR A 204     -25.287  41.144   2.454  1.00  0.00           H  
ATOM   2991  HE2 TYR A 204     -28.404  38.235   3.133  1.00  0.00           H  
ATOM   2992  HH  TYR A 204     -28.800  40.394   2.409  1.00  0.00           H  
ATOM   2993  N   ASP A 205     -25.167  36.357   6.940  1.00 82.21           N  
ANISOU 2993  N   ASP A 205    11018  10621   9595  -2287   2045  -2243
ATOM   2994  CA  ASP A 205     -26.221  36.291   7.957  1.00 81.37           C  
ANISOU 2994  CA  ASP A 205    10944  10567   9405  -2420   2314  -2467
ATOM   2995  C   ASP A 205     -25.781  36.711   9.367  1.00 81.92           C  
ANISOU 2995  C   ASP A 205    11302  10606   9219  -2664   2388  -2564
ATOM   2996  O   ASP A 205     -26.622  37.216  10.108  1.00 83.61           O  
ANISOU 2996  O   ASP A 205    11554  10825   9387  -2756   2650  -2806
ATOM   2997  CB  ASP A 205     -26.894  34.904   8.039  1.00 91.39           C  
ANISOU 2997  CB  ASP A 205    12182  11964  10579  -2532   2373  -2431
ATOM   2998  CG  ASP A 205     -27.535  34.419   6.738  1.00 91.95           C  
ANISOU 2998  CG  ASP A 205    11973  12089  10875  -2345   2343  -2383
ATOM   2999  OD1 ASP A 205     -27.976  35.273   5.936  1.00 92.04           O  
ANISOU 2999  OD1 ASP A 205    11758  12080  11133  -2143   2399  -2485
ATOM   3000  OD2 ASP A 205     -27.703  33.184   6.637  1.00 92.20           O1-
ANISOU 3000  OD2 ASP A 205    12027  12173  10834  -2403   2255  -2241
ATOM   3001  H   ASP A 205     -24.906  35.476   6.516  1.00  0.00           H  
ATOM   3002  HA  ASP A 205     -26.984  37.012   7.655  1.00  0.00           H  
ATOM   3003  HB3 ASP A 205     -27.658  34.903   8.816  1.00  0.00           H  
ATOM   3004  HB2 ASP A 205     -26.135  34.176   8.327  1.00  0.00           H  
ATOM   3005  N   SER A 206     -24.503  36.492   9.717  1.00 79.91           N  
ANISOU 3005  N   SER A 206    11242  10332   8790  -2781   2163  -2382
ATOM   3006  CA  SER A 206     -23.968  36.804  11.041  1.00 81.50           C  
ANISOU 3006  CA  SER A 206    11741  10519   8707  -3053   2176  -2438
ATOM   3007  C   SER A 206     -23.626  38.289  11.215  1.00 82.14           C  
ANISOU 3007  C   SER A 206    11893  10478   8838  -3036   2192  -2555
ATOM   3008  O   SER A 206     -23.843  38.819  12.303  1.00 84.14           O  
ANISOU 3008  O   SER A 206    12380  10700   8890  -3256   2327  -2723
ATOM   3009  CB  SER A 206     -22.733  35.940  11.333  1.00 81.84           C  
ANISOU 3009  CB  SER A 206    11940  10608   8546  -3185   1894  -2174
ATOM   3010  OG  SER A 206     -23.114  34.583  11.407  1.00 81.53           O  
ANISOU 3010  OG  SER A 206    11902  10636   8438  -3222   1895  -2078
ATOM   3011  H   SER A 206     -23.871  36.048   9.063  1.00  0.00           H  
ATOM   3012  HA  SER A 206     -24.726  36.558  11.783  1.00  0.00           H  
ATOM   3013  HB3 SER A 206     -22.285  36.220  12.288  1.00  0.00           H  
ATOM   3014  HB2 SER A 206     -21.967  36.068  10.568  1.00  0.00           H  
ATOM   3015  HG  SER A 206     -23.110  34.234  10.509  1.00  0.00           H  
ATOM   3016  N   ILE A 207     -23.106  38.928  10.153  1.00 77.69           N  
ANISOU 3016  N   ILE A 207    11164   9835   8521  -2804   2063  -2475
ATOM   3017  CA  ILE A 207     -22.636  40.315  10.187  1.00 78.31           C  
ANISOU 3017  CA  ILE A 207    11335   9768   8652  -2796   2063  -2568
ATOM   3018  C   ILE A 207     -23.748  41.315   9.798  1.00 79.20           C  
ANISOU 3018  C   ILE A 207    11328   9750   9012  -2586   2308  -2803
ATOM   3019  O   ILE A 207     -23.689  42.455  10.253  1.00 80.60           O  
ANISOU 3019  O   ILE A 207    11668   9782   9176  -2636   2433  -2986
ATOM   3020  CB  ILE A 207     -21.385  40.517   9.275  1.00 75.85           C  
ANISOU 3020  CB  ILE A 207    10953   9438   8430  -2714   1775  -2335
ATOM   3021  CG1 ILE A 207     -20.221  39.590   9.713  1.00 75.29           C  
ANISOU 3021  CG1 ILE A 207    10975   9499   8132  -2906   1537  -2122
ATOM   3022  CG2 ILE A 207     -20.866  41.972   9.216  1.00 76.99           C  
ANISOU 3022  CG2 ILE A 207    11202   9412   8638  -2719   1771  -2421
ATOM   3023  CD1 ILE A 207     -19.106  39.440   8.666  1.00 74.01           C  
ANISOU 3023  CD1 ILE A 207    10621   9401   8097  -2763   1293  -1869
ATOM   3024  H   ILE A 207     -22.954  38.428   9.287  1.00  0.00           H  
ATOM   3025  HA  ILE A 207     -22.332  40.561  11.207  1.00  0.00           H  
ATOM   3026  HB  ILE A 207     -21.673  40.240   8.260  1.00  0.00           H  
ATOM   3027 HG13 ILE A 207     -20.581  38.589   9.947  1.00  0.00           H  
ATOM   3028 HG12 ILE A 207     -19.793  39.963  10.645  1.00  0.00           H  
ATOM   3029 HG21 ILE A 207     -19.971  42.055   8.600  1.00  0.00           H  
ATOM   3030 HG22 ILE A 207     -21.593  42.658   8.786  1.00  0.00           H  
ATOM   3031 HG23 ILE A 207     -20.613  42.338  10.211  1.00  0.00           H  
ATOM   3032 HD11 ILE A 207     -18.555  38.513   8.823  1.00  0.00           H  
ATOM   3033 HD12 ILE A 207     -19.503  39.423   7.651  1.00  0.00           H  
ATOM   3034 HD13 ILE A 207     -18.389  40.259   8.733  1.00  0.00           H  
ATOM   3035  N   LYS A 208     -24.758  40.886   9.015  1.00 80.19           N  
ANISOU 3035  N   LYS A 208    11182   9925   9363  -2359   2375  -2805
ATOM   3036  CA  LYS A 208     -25.894  41.717   8.592  1.00 80.70           C  
ANISOU 3036  CA  LYS A 208    11078   9878   9704  -2116   2560  -2997
ATOM   3037  C   LYS A 208     -26.684  42.406   9.726  1.00 81.85           C  
ANISOU 3037  C   LYS A 208    11359   9950   9790  -2207   2885  -3322
ATOM   3038  O   LYS A 208     -26.815  43.623   9.645  1.00 82.93           O  
ANISOU 3038  O   LYS A 208    11536   9884  10090  -2063   2969  -3464
ATOM   3039  CB  LYS A 208     -26.793  40.938   7.610  1.00 83.30           C  
ANISOU 3039  CB  LYS A 208    11088  10331  10232  -1925   2579  -2954
ATOM   3040  CG  LYS A 208     -27.962  41.742   7.005  1.00 83.80           C  
ANISOU 3040  CG  LYS A 208    10925  10286  10628  -1622   2683  -3089
ATOM   3041  CD  LYS A 208     -28.716  40.944   5.930  1.00 83.14           C  
ANISOU 3041  CD  LYS A 208    10516  10346  10729  -1455   2620  -2993
ATOM   3042  CE  LYS A 208     -29.652  39.873   6.512  1.00 83.55           C  
ANISOU 3042  CE  LYS A 208    10427  10607  10711  -1575   2835  -3128
ATOM   3043  NZ  LYS A 208     -30.037  38.885   5.492  1.00 86.23           N1+
ANISOU 3043  NZ  LYS A 208    10554  11110  11101  -1542   2696  -2956
ATOM   3044  H   LYS A 208     -24.746  39.938   8.663  1.00  0.00           H  
ATOM   3045  HA  LYS A 208     -25.454  42.532   8.018  1.00  0.00           H  
ATOM   3046  HB3 LYS A 208     -27.157  40.028   8.086  1.00  0.00           H  
ATOM   3047  HB2 LYS A 208     -26.177  40.616   6.773  1.00  0.00           H  
ATOM   3048  HG3 LYS A 208     -27.568  42.656   6.557  1.00  0.00           H  
ATOM   3049  HG2 LYS A 208     -28.662  42.060   7.779  1.00  0.00           H  
ATOM   3050  HD3 LYS A 208     -27.990  40.476   5.267  1.00  0.00           H  
ATOM   3051  HD2 LYS A 208     -29.288  41.630   5.303  1.00  0.00           H  
ATOM   3052  HE3 LYS A 208     -30.547  40.342   6.923  1.00  0.00           H  
ATOM   3053  HE2 LYS A 208     -29.174  39.328   7.325  1.00  0.00           H  
ATOM   3054  HZ1 LYS A 208     -30.725  38.248   5.865  1.00  0.00           H  
ATOM   3055  HZ2 LYS A 208     -30.414  39.354   4.674  1.00  0.00           H  
ATOM   3056  HZ3 LYS A 208     -29.220  38.364   5.206  1.00  0.00           H  
ATOM   3057  N   PRO A 209     -27.140  41.701  10.789  1.00 89.83           N  
ANISOU 3057  N   PRO A 209    12470  11094  10566  -2448   3083  -3455
ATOM   3058  CA  PRO A 209     -27.825  42.385  11.905  1.00 93.47           C  
ANISOU 3058  CA  PRO A 209    13056  11481  10978  -2532   3429  -3794
ATOM   3059  C   PRO A 209     -26.916  43.300  12.749  1.00 94.86           C  
ANISOU 3059  C   PRO A 209    13603  11488  10952  -2730   3418  -3870
ATOM   3060  O   PRO A 209     -27.428  44.229  13.371  1.00 97.90           O  
ANISOU 3060  O   PRO A 209    14101  11715  11380  -2712   3685  -4159
ATOM   3061  CB  PRO A 209     -28.416  41.238  12.735  1.00 95.80           C  
ANISOU 3061  CB  PRO A 209    13391  11990  11018  -2802   3611  -3870
ATOM   3062  CG  PRO A 209     -27.499  40.060  12.460  1.00 93.31           C  
ANISOU 3062  CG  PRO A 209    13167  11790  10498  -2959   3300  -3550
ATOM   3063  CD  PRO A 209     -27.115  40.252  10.998  1.00 90.17           C  
ANISOU 3063  CD  PRO A 209    12538  11345  10379  -2660   3027  -3321
ATOM   3064  HA  PRO A 209     -28.640  43.000  11.519  1.00  0.00           H  
ATOM   3065  HB3 PRO A 209     -29.420  41.012  12.371  1.00  0.00           H  
ATOM   3066  HB2 PRO A 209     -28.500  41.460  13.800  1.00  0.00           H  
ATOM   3067  HG3 PRO A 209     -27.977  39.104  12.660  1.00  0.00           H  
ATOM   3068  HG2 PRO A 209     -26.608  40.133  13.085  1.00  0.00           H  
ATOM   3069  HD2 PRO A 209     -26.152  39.789  10.804  1.00  0.00           H  
ATOM   3070  HD3 PRO A 209     -27.857  39.790  10.346  1.00  0.00           H  
ATOM   3071  N   VAL A 210     -25.598  43.031  12.743  1.00 99.38           N  
ANISOU 3071  N   VAL A 210    14355  12095  11309  -2920   3112  -3619
ATOM   3072  CA  VAL A 210     -24.592  43.796  13.475  1.00 99.45           C  
ANISOU 3072  CA  VAL A 210    14714  11995  11079  -3176   3040  -3648
ATOM   3073  C   VAL A 210     -24.324  45.176  12.835  1.00 99.97           C  
ANISOU 3073  C   VAL A 210    14801  11803  11379  -2979   3010  -3702
ATOM   3074  O   VAL A 210     -24.239  46.152  13.580  1.00100.19           O  
ANISOU 3074  O   VAL A 210    15079  11651  11336  -3082   3197  -3941
ATOM   3075  CB  VAL A 210     -23.252  43.006  13.602  1.00 99.72           C  
ANISOU 3075  CB  VAL A 210    14858  12177  10852  -3410   2690  -3339
ATOM   3076  CG1 VAL A 210     -22.104  43.787  14.276  1.00100.75           C  
ANISOU 3076  CG1 VAL A 210    15302  12224  10755  -3680   2560  -3336
ATOM   3077  CG2 VAL A 210     -23.459  41.667  14.335  1.00100.38           C  
ANISOU 3077  CG2 VAL A 210    15006  12463  10673  -3629   2721  -3290
ATOM   3078  H   VAL A 210     -25.251  42.257  12.194  1.00  0.00           H  
ATOM   3079  HA  VAL A 210     -24.975  43.968  14.483  1.00  0.00           H  
ATOM   3080  HB  VAL A 210     -22.900  42.759  12.603  1.00  0.00           H  
ATOM   3081 HG11 VAL A 210     -21.229  43.153  14.420  1.00  0.00           H  
ATOM   3082 HG12 VAL A 210     -21.777  44.638  13.679  1.00  0.00           H  
ATOM   3083 HG13 VAL A 210     -22.405  44.160  15.256  1.00  0.00           H  
ATOM   3084 HG21 VAL A 210     -22.528  41.104  14.401  1.00  0.00           H  
ATOM   3085 HG22 VAL A 210     -23.824  41.824  15.351  1.00  0.00           H  
ATOM   3086 HG23 VAL A 210     -24.179  41.032  13.820  1.00  0.00           H  
ATOM   3087  N   VAL A 211     -24.199  45.236  11.494  1.00 97.43           N  
ANISOU 3087  N   VAL A 211    14248  11448  11322  -2711   2798  -3495
ATOM   3088  CA  VAL A 211     -23.763  46.443  10.779  1.00 97.73           C  
ANISOU 3088  CA  VAL A 211    14340  11238  11554  -2557   2716  -3487
ATOM   3089  C   VAL A 211     -24.887  47.134   9.970  1.00 98.67           C  
ANISOU 3089  C   VAL A 211    14280  11169  12043  -2180   2896  -3646
ATOM   3090  O   VAL A 211     -24.863  48.362   9.892  1.00100.42           O  
ANISOU 3090  O   VAL A 211    14672  11107  12375  -2099   2970  -3782
ATOM   3091  CB  VAL A 211     -22.541  46.161   9.855  1.00 96.03           C  
ANISOU 3091  CB  VAL A 211    14025  11091  11370  -2538   2361  -3154
ATOM   3092  CG1 VAL A 211     -21.369  45.531  10.628  1.00 95.88           C  
ANISOU 3092  CG1 VAL A 211    14184  11229  11018  -2892   2171  -3014
ATOM   3093  CG2 VAL A 211     -22.837  45.371   8.569  1.00 94.94           C  
ANISOU 3093  CG2 VAL A 211    13541  11114  11419  -2300   2263  -2973
ATOM   3094  H   VAL A 211     -24.284  44.391  10.946  1.00  0.00           H  
ATOM   3095  HA  VAL A 211     -23.425  47.188  11.502  1.00  0.00           H  
ATOM   3096  HB  VAL A 211     -22.166  47.132   9.528  1.00  0.00           H  
ATOM   3097 HG11 VAL A 211     -20.478  45.452  10.004  1.00  0.00           H  
ATOM   3098 HG12 VAL A 211     -21.104  46.131  11.499  1.00  0.00           H  
ATOM   3099 HG13 VAL A 211     -21.613  44.528  10.979  1.00  0.00           H  
ATOM   3100 HG21 VAL A 211     -21.925  44.973   8.123  1.00  0.00           H  
ATOM   3101 HG22 VAL A 211     -23.517  44.539   8.743  1.00  0.00           H  
ATOM   3102 HG23 VAL A 211     -23.277  46.027   7.823  1.00  0.00           H  
ATOM   3103  N   LEU A 212     -25.866  46.380   9.429  1.00103.54           N  
ANISOU 3103  N   LEU A 212    14559  11930  12849  -1956   2950  -3623
ATOM   3104  CA  LEU A 212     -27.078  46.932   8.802  1.00104.54           C  
ANISOU 3104  CA  LEU A 212    14443  11928  13348  -1578   3077  -3742
ATOM   3105  C   LEU A 212     -28.171  47.036   9.878  1.00107.66           C  
ANISOU 3105  C   LEU A 212    14811  12318  13775  -1558   3471  -4096
ATOM   3106  O   LEU A 212     -28.937  46.092  10.073  1.00107.85           O  
ANISOU 3106  O   LEU A 212    14574  12558  13847  -1516   3612  -4162
ATOM   3107  CB  LEU A 212     -27.558  46.070   7.599  1.00102.00           C  
ANISOU 3107  CB  LEU A 212    13757  11783  13214  -1370   2899  -3521
ATOM   3108  CG  LEU A 212     -26.937  46.404   6.228  1.00101.91           C  
ANISOU 3108  CG  LEU A 212    13696  11639  13385  -1179   2611  -3279
ATOM   3109  CD1 LEU A 212     -25.418  46.201   6.190  1.00101.66           C  
ANISOU 3109  CD1 LEU A 212    13922  11581  13123  -1428   2389  -3089
ATOM   3110  CD2 LEU A 212     -27.637  45.601   5.114  1.00101.58           C  
ANISOU 3110  CD2 LEU A 212    13310  11781  13506   -997   2469  -3098
ATOM   3111  H   LEU A 212     -25.855  45.376   9.548  1.00  0.00           H  
ATOM   3112  HA  LEU A 212     -26.881  47.937   8.427  1.00  0.00           H  
ATOM   3113  HB3 LEU A 212     -28.633  46.215   7.484  1.00  0.00           H  
ATOM   3114  HB2 LEU A 212     -27.442  45.009   7.795  1.00  0.00           H  
ATOM   3115  HG  LEU A 212     -27.126  47.453   6.016  1.00  0.00           H  
ATOM   3116 HD11 LEU A 212     -25.052  46.000   5.183  1.00  0.00           H  
ATOM   3117 HD12 LEU A 212     -24.903  47.092   6.549  1.00  0.00           H  
ATOM   3118 HD13 LEU A 212     -25.132  45.355   6.813  1.00  0.00           H  
ATOM   3119 HD21 LEU A 212     -28.036  46.264   4.347  1.00  0.00           H  
ATOM   3120 HD22 LEU A 212     -26.961  44.899   4.628  1.00  0.00           H  
ATOM   3121 HD23 LEU A 212     -28.475  45.014   5.490  1.00  0.00           H  
ATOM   3122  N   VAL A 213     -28.209  48.191  10.557  1.00111.92           N  
ANISOU 3122  N   VAL A 213    15638  12612  14277  -1612   3663  -4338
ATOM   3123  CA  VAL A 213     -29.180  48.509  11.602  1.00115.67           C  
ANISOU 3123  CA  VAL A 213    16138  13044  14768  -1608   4081  -4718
ATOM   3124  C   VAL A 213     -29.696  49.949  11.404  1.00119.07           C  
ANISOU 3124  C   VAL A 213    16591  13103  15547  -1257   4218  -4915
ATOM   3125  O   VAL A 213     -29.020  50.768  10.777  1.00118.77           O  
ANISOU 3125  O   VAL A 213    16696  12820  15612  -1149   3982  -4756
ATOM   3126  CB  VAL A 213     -28.541  48.324  13.013  1.00117.88           C  
ANISOU 3126  CB  VAL A 213    16809  13391  14591  -2081   4228  -4859
ATOM   3127  CG1 VAL A 213     -27.512  49.404  13.405  1.00119.47           C  
ANISOU 3127  CG1 VAL A 213    17439  13283  14670  -2222   4239  -4971
ATOM   3128  CG2 VAL A 213     -29.591  48.160  14.127  1.00118.40           C  
ANISOU 3128  CG2 VAL A 213    16811  13607  14570  -2184   4645  -5179
ATOM   3129  H   VAL A 213     -27.539  48.917  10.347  1.00  0.00           H  
ATOM   3130  HA  VAL A 213     -30.044  47.847  11.510  1.00  0.00           H  
ATOM   3131  HB  VAL A 213     -27.993  47.380  12.981  1.00  0.00           H  
ATOM   3132 HG11 VAL A 213     -27.008  49.138  14.335  1.00  0.00           H  
ATOM   3133 HG12 VAL A 213     -26.741  49.510  12.641  1.00  0.00           H  
ATOM   3134 HG13 VAL A 213     -27.973  50.380  13.556  1.00  0.00           H  
ATOM   3135 HG21 VAL A 213     -29.115  47.904  15.074  1.00  0.00           H  
ATOM   3136 HG22 VAL A 213     -30.163  49.074  14.288  1.00  0.00           H  
ATOM   3137 HG23 VAL A 213     -30.294  47.360  13.891  1.00  0.00           H  
ATOM   3138  N   GLY A 214     -30.903  50.223  11.927  1.00128.20           N  
ANISOU 3138  N   GLY A 214    17591  14227  16893  -1074   4595  -5249
ATOM   3139  CA  GLY A 214     -31.590  51.507  11.787  1.00132.12           C  
ANISOU 3139  CA  GLY A 214    18070  14368  17762   -689   4779  -5480
ATOM   3140  C   GLY A 214     -32.171  51.606  10.364  1.00131.03           C  
ANISOU 3140  C   GLY A 214    17529  14185  18071   -217   4549  -5281
ATOM   3141  O   GLY A 214     -32.927  50.711   9.981  1.00129.92           O  
ANISOU 3141  O   GLY A 214    16959  14345  18060   -102   4536  -5216
ATOM   3142  H   GLY A 214     -31.401  49.496  12.419  1.00  0.00           H  
ATOM   3143  HA3 GLY A 214     -30.922  52.324  12.057  1.00  0.00           H  
ATOM   3144  HA2 GLY A 214     -32.415  51.537  12.498  1.00  0.00           H  
ATOM   3145  N   PRO A 215     -31.846  52.656   9.571  1.00133.87           N  
ANISOU 3145  N   PRO A 215    18043  14178  18645     27   4337  -5158
ATOM   3146  CA  PRO A 215     -32.344  52.792   8.186  1.00133.37           C  
ANISOU 3146  CA  PRO A 215    17632  14065  18977    455   4065  -4926
ATOM   3147  C   PRO A 215     -31.751  51.774   7.190  1.00129.86           C  
ANISOU 3147  C   PRO A 215    17019  13922  18401    321   3680  -4524
ATOM   3148  O   PRO A 215     -32.329  51.576   6.121  1.00129.33           O  
ANISOU 3148  O   PRO A 215    16605  13937  18598    602   3476  -4338
ATOM   3149  CB  PRO A 215     -31.968  54.236   7.817  1.00136.69           C  
ANISOU 3149  CB  PRO A 215    18389  13985  19560    646   3944  -4894
ATOM   3150  CG  PRO A 215     -30.705  54.513   8.618  1.00136.07           C  
ANISOU 3150  CG  PRO A 215    18828  13798  19073    200   3983  -4944
ATOM   3151  CD  PRO A 215     -30.948  53.759   9.923  1.00136.33           C  
ANISOU 3151  CD  PRO A 215    18872  14098  18827   -105   4326  -5217
ATOM   3152  HA  PRO A 215     -33.431  52.685   8.165  1.00  0.00           H  
ATOM   3153  HB3 PRO A 215     -32.763  54.909   8.142  1.00  0.00           H  
ATOM   3154  HB2 PRO A 215     -31.825  54.395   6.747  1.00  0.00           H  
ATOM   3155  HG3 PRO A 215     -30.506  55.575   8.764  1.00  0.00           H  
ATOM   3156  HG2 PRO A 215     -29.848  54.079   8.102  1.00  0.00           H  
ATOM   3157  HD2 PRO A 215     -30.002  53.421  10.349  1.00  0.00           H  
ATOM   3158  HD3 PRO A 215     -31.448  54.400  10.650  1.00  0.00           H  
ATOM   3159  N   LEU A 216     -30.624  51.144   7.563  1.00124.72           N  
ANISOU 3159  N   LEU A 216    16606  13438  17343   -105   3584  -4398
ATOM   3160  CA  LEU A 216     -29.902  50.161   6.760  1.00120.99           C  
ANISOU 3160  CA  LEU A 216    16015  13219  16735   -239   3250  -4044
ATOM   3161  C   LEU A 216     -30.504  48.744   6.813  1.00119.89           C  
ANISOU 3161  C   LEU A 216    15552  13488  16513   -337   3321  -4035
ATOM   3162  O   LEU A 216     -30.082  47.906   6.017  1.00116.96           O  
ANISOU 3162  O   LEU A 216    15076  13327  16036   -437   3071  -3761
ATOM   3163  CB  LEU A 216     -28.426  50.144   7.207  1.00116.66           C  
ANISOU 3163  CB  LEU A 216    15847  12656  15824   -622   3089  -3897
ATOM   3164  CG  LEU A 216     -27.653  51.459   6.969  1.00117.09           C  
ANISOU 3164  CG  LEU A 216    16271  12333  15887   -633   3007  -3890
ATOM   3165  CD1 LEU A 216     -26.237  51.369   7.575  1.00116.86           C  
ANISOU 3165  CD1 LEU A 216    16567  12365  15470  -1070   2912  -3810
ATOM   3166  CD2 LEU A 216     -27.624  51.868   5.480  1.00117.64           C  
ANISOU 3166  CD2 LEU A 216    16260  12231  16206   -367   2717  -3635
ATOM   3167  H   LEU A 216     -30.213  51.362   8.460  1.00  0.00           H  
ATOM   3168  HA  LEU A 216     -29.943  50.479   5.722  1.00  0.00           H  
ATOM   3169  HB3 LEU A 216     -27.897  49.354   6.680  1.00  0.00           H  
ATOM   3170  HB2 LEU A 216     -28.383  49.884   8.264  1.00  0.00           H  
ATOM   3171  HG  LEU A 216     -28.169  52.250   7.514  1.00  0.00           H  
ATOM   3172 HD11 LEU A 216     -26.032  52.233   8.207  1.00  0.00           H  
ATOM   3173 HD12 LEU A 216     -26.113  50.482   8.199  1.00  0.00           H  
ATOM   3174 HD13 LEU A 216     -25.457  51.327   6.815  1.00  0.00           H  
ATOM   3175 HD21 LEU A 216     -26.647  52.237   5.165  1.00  0.00           H  
ATOM   3176 HD22 LEU A 216     -27.875  51.036   4.822  1.00  0.00           H  
ATOM   3177 HD23 LEU A 216     -28.342  52.664   5.286  1.00  0.00           H  
ATOM   3178  N   ALA A 217     -31.470  48.496   7.718  1.00124.19           N  
ANISOU 3178  N   ALA A 217    15949  14140  17095   -324   3672  -4336
ATOM   3179  CA  ALA A 217     -32.124  47.199   7.920  1.00122.84           C  
ANISOU 3179  CA  ALA A 217    15501  14349  16822   -464   3763  -4341
ATOM   3180  C   ALA A 217     -32.881  46.658   6.690  1.00121.89           C  
ANISOU 3180  C   ALA A 217    14947  14392  16974   -203   3547  -4139
ATOM   3181  O   ALA A 217     -32.864  45.447   6.474  1.00119.38           O  
ANISOU 3181  O   ALA A 217    14513  14343  16502   -374   3413  -3957
ATOM   3182  CB  ALA A 217     -33.064  47.303   9.131  1.00127.37           C  
ANISOU 3182  CB  ALA A 217    16000  14999  17395   -511   4210  -4726
ATOM   3183  H   ALA A 217     -31.774  49.242   8.328  1.00  0.00           H  
ATOM   3184  HA  ALA A 217     -31.340  46.480   8.164  1.00  0.00           H  
ATOM   3185  HB1 ALA A 217     -33.545  46.347   9.343  1.00  0.00           H  
ATOM   3186  HB2 ALA A 217     -32.515  47.598  10.027  1.00  0.00           H  
ATOM   3187  HB3 ALA A 217     -33.850  48.042   8.966  1.00  0.00           H  
ATOM   3188  N   ASN A 218     -33.502  47.558   5.906  1.00124.07           N  
ANISOU 3188  N   ASN A 218    15015  14481  17643    203   3491  -4156
ATOM   3189  CA  ASN A 218     -34.245  47.236   4.678  1.00123.28           C  
ANISOU 3189  CA  ASN A 218    14511  14520  17808    456   3260  -3964
ATOM   3190  C   ASN A 218     -33.491  47.673   3.403  1.00120.96           C  
ANISOU 3190  C   ASN A 218    14349  14041  17569    572   2849  -3627
ATOM   3191  O   ASN A 218     -33.985  47.395   2.309  1.00119.88           O  
ANISOU 3191  O   ASN A 218    13938  14032  17579    714   2608  -3422
ATOM   3192  CB  ASN A 218     -35.641  47.907   4.720  1.00  0.00           C  
ATOM   3193  CG  ASN A 218     -36.526  47.422   5.873  1.00  0.00           C  
ATOM   3194  OD1 ASN A 218     -36.512  48.000   6.957  1.00  0.00           O  
ATOM   3195  ND2 ASN A 218     -37.309  46.366   5.639  1.00  0.00           N  
ATOM   3196  H   ASN A 218     -33.473  48.534   6.163  1.00  0.00           H  
ATOM   3197  HA  ASN A 218     -34.390  46.157   4.601  1.00  0.00           H  
ATOM   3198  HB2 ASN A 218     -35.536  48.991   4.791  1.00  0.00           H  
ATOM   3199  HB3 ASN A 218     -36.179  47.718   3.789  1.00  0.00           H  
ATOM   3200 HD22 ASN A 218     -37.912  46.015   6.369  1.00  0.00           H  
ATOM   3201 HD21 ASN A 218     -37.303  45.910   4.739  1.00  0.00           H  
ATOM   3202  N   ASN A 219     -32.337  48.353   3.546  1.00111.71           N  
ANISOU 3202  N   ASN A 219    13600  12583  16261    477   2774  -3574
ATOM   3203  CA  ASN A 219     -31.536  48.904   2.447  1.00109.49           C  
ANISOU 3203  CA  ASN A 219    13495  12108  15999    536   2425  -3278
ATOM   3204  C   ASN A 219     -30.896  47.801   1.578  1.00105.34           C  
ANISOU 3204  C   ASN A 219    12901  11847  15278    339   2167  -2983
ATOM   3205  O   ASN A 219     -30.329  46.847   2.114  1.00103.92           O  
ANISOU 3205  O   ASN A 219    12735  11912  14836     58   2248  -2994
ATOM   3206  CB  ASN A 219     -30.478  49.861   3.042  1.00109.09           C  
ANISOU 3206  CB  ASN A 219    13907  11756  15785    380   2439  -3307
ATOM   3207  CG  ASN A 219     -29.767  50.747   2.011  1.00109.16           C  
ANISOU 3207  CG  ASN A 219    14108  11518  15850    456   2123  -3041
ATOM   3208  OD1 ASN A 219     -28.944  50.270   1.235  1.00108.92           O  
ANISOU 3208  OD1 ASN A 219    14073  11631  15681    317   1874  -2771
ATOM   3209  ND2 ASN A 219     -30.059  52.048   2.012  1.00109.45           N  
ANISOU 3209  ND2 ASN A 219    14344  11161  16081    665   2143  -3123
ATOM   3210  H   ASN A 219     -31.974  48.506   4.475  1.00  0.00           H  
ATOM   3211  HA  ASN A 219     -32.199  49.486   1.802  1.00  0.00           H  
ATOM   3212  HB3 ASN A 219     -29.732  49.304   3.611  1.00  0.00           H  
ATOM   3213  HB2 ASN A 219     -30.977  50.523   3.751  1.00  0.00           H  
ATOM   3214 HD22 ASN A 219     -29.604  52.669   1.358  1.00  0.00           H  
ATOM   3215 HD21 ASN A 219     -30.731  52.423   2.666  1.00  0.00           H  
ATOM   3216  N   PHE A 220     -30.990  47.987   0.250  1.00 89.60           N  
ANISOU 3216  N   PHE A 220    10863   9777  13402    484   1859  -2722
ATOM   3217  CA  PHE A 220     -30.491  47.063  -0.766  1.00 87.68           C  
ANISOU 3217  CA  PHE A 220    10558   9752  13006    334   1619  -2452
ATOM   3218  C   PHE A 220     -28.997  47.241  -1.085  1.00 87.46           C  
ANISOU 3218  C   PHE A 220    10862   9621  12746    112   1462  -2269
ATOM   3219  O   PHE A 220     -28.303  46.237  -1.236  1.00 86.30           O  
ANISOU 3219  O   PHE A 220    10733   9689  12367   -127   1423  -2168
ATOM   3220  CB  PHE A 220     -31.359  47.196  -2.035  1.00 89.64           C  
ANISOU 3220  CB  PHE A 220    10554  10010  13495    592   1380  -2282
ATOM   3221  CG  PHE A 220     -30.947  46.309  -3.197  1.00 89.14           C  
ANISOU 3221  CG  PHE A 220    10432  10163  13274    437   1150  -2027
ATOM   3222  CD1 PHE A 220     -29.996  46.752  -4.143  1.00 88.58           C  
ANISOU 3222  CD1 PHE A 220    10594   9964  13097    359    914  -1788
ATOM   3223  CD2 PHE A 220     -31.371  44.966  -3.231  1.00 89.15           C  
ANISOU 3223  CD2 PHE A 220    10153  10488  13233    361   1182  -2035
ATOM   3224  CE1 PHE A 220     -29.532  45.884  -5.122  1.00 87.93           C  
ANISOU 3224  CE1 PHE A 220    10467  10076  12868    216    734  -1579
ATOM   3225  CE2 PHE A 220     -30.909  44.123  -4.229  1.00 88.62           C  
ANISOU 3225  CE2 PHE A 220    10062  10593  13017    216    986  -1819
ATOM   3226  CZ  PHE A 220     -29.994  44.577  -5.170  1.00 87.95           C  
ANISOU 3226  CZ  PHE A 220    10209  10378  12829    153    772  -1600
ATOM   3227  H   PHE A 220     -31.468  48.805  -0.097  1.00  0.00           H  
ATOM   3228  HA  PHE A 220     -30.623  46.045  -0.393  1.00  0.00           H  
ATOM   3229  HB3 PHE A 220     -31.371  48.233  -2.373  1.00  0.00           H  
ATOM   3230  HB2 PHE A 220     -32.393  46.955  -1.783  1.00  0.00           H  
ATOM   3231  HD1 PHE A 220     -29.617  47.763  -4.102  1.00  0.00           H  
ATOM   3232  HD2 PHE A 220     -32.051  44.592  -2.481  1.00  0.00           H  
ATOM   3233  HE1 PHE A 220     -28.807  46.226  -5.845  1.00  0.00           H  
ATOM   3234  HE2 PHE A 220     -31.246  43.103  -4.264  1.00  0.00           H  
ATOM   3235  HZ  PHE A 220     -29.629  43.907  -5.935  1.00  0.00           H  
ATOM   3236  N   LEU A 221     -28.533  48.497  -1.220  1.00 84.52           N  
ANISOU 3236  N   LEU A 221    10740   8925  12450    194   1362  -2213
ATOM   3237  CA  LEU A 221     -27.148  48.831  -1.572  1.00 82.97           C  
ANISOU 3237  CA  LEU A 221    10849   8631  12047    -35   1218  -2044
ATOM   3238  C   LEU A 221     -26.152  48.383  -0.488  1.00 81.84           C  
ANISOU 3238  C   LEU A 221    10858   8609  11628   -346   1367  -2145
ATOM   3239  O   LEU A 221     -25.109  47.831  -0.830  1.00 79.64           O  
ANISOU 3239  O   LEU A 221    10649   8467  11142   -575   1259  -1992
ATOM   3240  CB  LEU A 221     -27.043  50.343  -1.889  1.00  0.00           C  
ATOM   3241  CG  LEU A 221     -25.645  50.850  -2.324  1.00  0.00           C  
ATOM   3242  CD1 LEU A 221     -25.123  50.145  -3.595  1.00  0.00           C  
ATOM   3243  CD2 LEU A 221     -25.629  52.387  -2.463  1.00  0.00           C  
ATOM   3244  H   LEU A 221     -29.155  49.277  -1.065  1.00  0.00           H  
ATOM   3245  HA  LEU A 221     -26.912  48.274  -2.480  1.00  0.00           H  
ATOM   3246  HB2 LEU A 221     -27.763  50.591  -2.671  1.00  0.00           H  
ATOM   3247  HB3 LEU A 221     -27.360  50.902  -1.008  1.00  0.00           H  
ATOM   3248  HG  LEU A 221     -24.947  50.623  -1.518  1.00  0.00           H  
ATOM   3249 HD11 LEU A 221     -24.654  50.836  -4.296  1.00  0.00           H  
ATOM   3250 HD12 LEU A 221     -24.373  49.397  -3.339  1.00  0.00           H  
ATOM   3251 HD13 LEU A 221     -25.920  49.635  -4.136  1.00  0.00           H  
ATOM   3252 HD21 LEU A 221     -24.790  52.817  -1.915  1.00  0.00           H  
ATOM   3253 HD22 LEU A 221     -25.542  52.713  -3.500  1.00  0.00           H  
ATOM   3254 HD23 LEU A 221     -26.537  52.842  -2.067  1.00  0.00           H  
ATOM   3255  N   ALA A 222     -26.525  48.574   0.788  1.00 89.29           N  
ANISOU 3255  N   ALA A 222    11833   9523  12568   -355   1617  -2406
ATOM   3256  CA  ALA A 222     -25.793  48.094   1.958  1.00 89.27           C  
ANISOU 3256  CA  ALA A 222    11988   9639  12291   -659   1751  -2510
ATOM   3257  C   ALA A 222     -25.742  46.559   2.047  1.00 86.86           C  
ANISOU 3257  C   ALA A 222    11489   9682  11831   -796   1735  -2427
ATOM   3258  O   ALA A 222     -24.692  46.023   2.399  1.00 85.48           O  
ANISOU 3258  O   ALA A 222    11420   9632  11427  -1040   1659  -2323
ATOM   3259  CB  ALA A 222     -26.422  48.701   3.220  1.00 92.79           C  
ANISOU 3259  CB  ALA A 222    12518   9970  12769   -633   2038  -2821
ATOM   3260  H   ALA A 222     -27.401  49.046   0.976  1.00  0.00           H  
ATOM   3261  HA  ALA A 222     -24.766  48.459   1.880  1.00  0.00           H  
ATOM   3262  HB1 ALA A 222     -25.878  48.402   4.115  1.00  0.00           H  
ATOM   3263  HB2 ALA A 222     -26.405  49.790   3.178  1.00  0.00           H  
ATOM   3264  HB3 ALA A 222     -27.461  48.392   3.340  1.00  0.00           H  
ATOM   3265  N   SER A 223     -26.850  45.885   1.681  1.00 87.21           N  
ANISOU 3265  N   SER A 223    11245   9878  12014   -634   1791  -2463
ATOM   3266  CA  SER A 223     -26.943  44.425   1.584  1.00 85.36           C  
ANISOU 3266  CA  SER A 223    10843   9943  11648   -755   1783  -2391
ATOM   3267  C   SER A 223     -26.044  43.854   0.475  1.00 82.76           C  
ANISOU 3267  C   SER A 223    10520   9696  11229   -830   1542  -2123
ATOM   3268  O   SER A 223     -25.369  42.854   0.704  1.00 81.75           O  
ANISOU 3268  O   SER A 223    10439   9725  10898  -1026   1519  -2050
ATOM   3269  CB  SER A 223     -28.411  43.997   1.374  1.00 93.31           C  
ANISOU 3269  CB  SER A 223    11532  11081  12840   -577   1871  -2476
ATOM   3270  OG  SER A 223     -29.151  44.125   2.569  1.00 96.44           O  
ANISOU 3270  OG  SER A 223    11889  11441  13313   -523   2140  -2751
ATOM   3271  H   SER A 223     -27.672  46.401   1.400  1.00  0.00           H  
ATOM   3272  HA  SER A 223     -26.590  43.992   2.522  1.00  0.00           H  
ATOM   3273  HB3 SER A 223     -28.470  42.955   1.061  1.00  0.00           H  
ATOM   3274  HB2 SER A 223     -28.895  44.578   0.593  1.00  0.00           H  
ATOM   3275  HG  SER A 223     -29.438  45.040   2.655  1.00  0.00           H  
ATOM   3276  N   PHE A 224     -26.020  44.520  -0.692  1.00 73.42           N  
ANISOU 3276  N   PHE A 224     9310   8394  10193   -679   1367  -1980
ATOM   3277  CA  PHE A 224     -25.157  44.178  -1.820  1.00 72.11           C  
ANISOU 3277  CA  PHE A 224     9163   8297   9940   -759   1167  -1746
ATOM   3278  C   PHE A 224     -23.661  44.361  -1.522  1.00 71.63           C  
ANISOU 3278  C   PHE A 224     9324   8203   9691   -979   1126  -1682
ATOM   3279  O   PHE A 224     -22.880  43.480  -1.868  1.00 70.47           O  
ANISOU 3279  O   PHE A 224     9154   8216   9408  -1110   1055  -1557
ATOM   3280  CB  PHE A 224     -25.618  44.920  -3.094  1.00 73.27           C  
ANISOU 3280  CB  PHE A 224     9281   8300  10256   -582    991  -1612
ATOM   3281  CG  PHE A 224     -24.682  44.786  -4.283  1.00 72.34           C  
ANISOU 3281  CG  PHE A 224     9245   8221  10018   -706    816  -1392
ATOM   3282  CD1 PHE A 224     -23.746  45.802  -4.571  1.00 73.17           C  
ANISOU 3282  CD1 PHE A 224     9581   8145  10076   -795    732  -1308
ATOM   3283  CD2 PHE A 224     -24.607  43.566  -4.986  1.00 70.95           C  
ANISOU 3283  CD2 PHE A 224     8932   8265   9762   -763    759  -1286
ATOM   3284  CE1 PHE A 224     -22.803  45.611  -5.570  1.00 72.55           C  
ANISOU 3284  CE1 PHE A 224     9565   8125   9874   -938    605  -1123
ATOM   3285  CE2 PHE A 224     -23.649  43.393  -5.976  1.00 70.42           C  
ANISOU 3285  CE2 PHE A 224     8943   8236   9578   -886    638  -1111
ATOM   3286  CZ  PHE A 224     -22.748  44.410  -6.263  1.00 71.19           C  
ANISOU 3286  CZ  PHE A 224     9242   8175   9631   -974    569  -1034
ATOM   3287  H   PHE A 224     -26.618  45.328  -0.816  1.00  0.00           H  
ATOM   3288  HA  PHE A 224     -25.289  43.112  -2.017  1.00  0.00           H  
ATOM   3289  HB3 PHE A 224     -25.774  45.978  -2.881  1.00  0.00           H  
ATOM   3290  HB2 PHE A 224     -26.592  44.534  -3.394  1.00  0.00           H  
ATOM   3291  HD1 PHE A 224     -23.755  46.726  -4.010  1.00  0.00           H  
ATOM   3292  HD2 PHE A 224     -25.282  42.760  -4.743  1.00  0.00           H  
ATOM   3293  HE1 PHE A 224     -22.099  46.397  -5.797  1.00  0.00           H  
ATOM   3294  HE2 PHE A 224     -23.600  42.460  -6.514  1.00  0.00           H  
ATOM   3295  HZ  PHE A 224     -21.996  44.268  -7.025  1.00  0.00           H  
ATOM   3296  N   LEU A 225     -23.290  45.480  -0.879  1.00 66.22           N  
ANISOU 3296  N   LEU A 225     8844   7314   9004  -1020   1172  -1773
ATOM   3297  CA  LEU A 225     -21.908  45.779  -0.504  1.00 66.26           C  
ANISOU 3297  CA  LEU A 225     9043   7304   8828  -1259   1122  -1719
ATOM   3298  C   LEU A 225     -21.373  44.845   0.592  1.00 65.79           C  
ANISOU 3298  C   LEU A 225     8970   7450   8579  -1440   1192  -1767
ATOM   3299  O   LEU A 225     -20.220  44.432   0.491  1.00 65.15           O  
ANISOU 3299  O   LEU A 225     8887   7503   8365  -1594   1093  -1638
ATOM   3300  CB  LEU A 225     -21.775  47.257  -0.085  1.00 65.99           C  
ANISOU 3300  CB  LEU A 225     9264   6988   8821  -1291   1156  -1818
ATOM   3301  CG  LEU A 225     -21.855  48.260  -1.258  1.00 66.48           C  
ANISOU 3301  CG  LEU A 225     9412   6811   9036  -1156   1034  -1714
ATOM   3302  CD1 LEU A 225     -21.943  49.707  -0.736  1.00 67.61           C  
ANISOU 3302  CD1 LEU A 225     9840   6640   9209  -1182   1088  -1830
ATOM   3303  CD2 LEU A 225     -20.716  48.085  -2.284  1.00 66.24           C  
ANISOU 3303  CD2 LEU A 225     9376   6877   8914  -1285    860  -1484
ATOM   3304  H   LEU A 225     -23.984  46.177  -0.639  1.00  0.00           H  
ATOM   3305  HA  LEU A 225     -21.288  45.605  -1.385  1.00  0.00           H  
ATOM   3306  HB3 LEU A 225     -20.824  47.413   0.428  1.00  0.00           H  
ATOM   3307  HB2 LEU A 225     -22.549  47.480   0.652  1.00  0.00           H  
ATOM   3308  HG  LEU A 225     -22.784  48.066  -1.791  1.00  0.00           H  
ATOM   3309 HD11 LEU A 225     -22.651  50.287  -1.326  1.00  0.00           H  
ATOM   3310 HD12 LEU A 225     -22.277  49.750   0.301  1.00  0.00           H  
ATOM   3311 HD13 LEU A 225     -20.983  50.222  -0.781  1.00  0.00           H  
ATOM   3312 HD21 LEU A 225     -20.228  49.027  -2.532  1.00  0.00           H  
ATOM   3313 HD22 LEU A 225     -19.939  47.408  -1.928  1.00  0.00           H  
ATOM   3314 HD23 LEU A 225     -21.105  47.676  -3.217  1.00  0.00           H  
ATOM   3315  N   LEU A 226     -22.218  44.479   1.575  1.00 70.00           N  
ANISOU 3315  N   LEU A 226     9477   8019   9101  -1418   1359  -1944
ATOM   3316  CA  LEU A 226     -21.888  43.469   2.582  1.00 69.84           C  
ANISOU 3316  CA  LEU A 226     9477   8180   8878  -1601   1413  -1974
ATOM   3317  C   LEU A 226     -21.727  42.073   1.962  1.00 68.72           C  
ANISOU 3317  C   LEU A 226     9165   8247   8699  -1593   1319  -1811
ATOM   3318  O   LEU A 226     -20.776  41.375   2.309  1.00 68.34           O  
ANISOU 3318  O   LEU A 226     9150   8318   8498  -1741   1237  -1712
ATOM   3319  CB  LEU A 226     -22.933  43.473   3.720  1.00 69.72           C  
ANISOU 3319  CB  LEU A 226     9477   8167   8848  -1598   1634  -2200
ATOM   3320  CG  LEU A 226     -22.659  42.446   4.846  1.00 69.11           C  
ANISOU 3320  CG  LEU A 226     9481   8254   8524  -1823   1684  -2226
ATOM   3321  CD1 LEU A 226     -21.261  42.616   5.472  1.00 69.32           C  
ANISOU 3321  CD1 LEU A 226     9695   8290   8355  -2051   1551  -2139
ATOM   3322  CD2 LEU A 226     -23.768  42.475   5.907  1.00 69.23           C  
ANISOU 3322  CD2 LEU A 226     9571   8243   8491  -1873   1929  -2473
ATOM   3323  H   LEU A 226     -23.152  44.867   1.611  1.00  0.00           H  
ATOM   3324  HA  LEU A 226     -20.922  43.752   3.004  1.00  0.00           H  
ATOM   3325  HB3 LEU A 226     -23.922  43.286   3.298  1.00  0.00           H  
ATOM   3326  HB2 LEU A 226     -22.980  44.473   4.155  1.00  0.00           H  
ATOM   3327  HG  LEU A 226     -22.698  41.445   4.415  1.00  0.00           H  
ATOM   3328 HD11 LEU A 226     -21.258  42.379   6.532  1.00  0.00           H  
ATOM   3329 HD12 LEU A 226     -20.539  41.948   5.003  1.00  0.00           H  
ATOM   3330 HD13 LEU A 226     -20.887  43.635   5.366  1.00  0.00           H  
ATOM   3331 HD21 LEU A 226     -24.118  41.463   6.113  1.00  0.00           H  
ATOM   3332 HD22 LEU A 226     -23.426  42.901   6.849  1.00  0.00           H  
ATOM   3333 HD23 LEU A 226     -24.632  43.058   5.585  1.00  0.00           H  
ATOM   3334  N   GLY A 227     -22.622  41.727   1.021  1.00 78.24           N  
ANISOU 3334  N   GLY A 227    10193   9484  10049  -1419   1321  -1782
ATOM   3335  CA  GLY A 227     -22.553  40.510   0.220  1.00 77.58           C  
ANISOU 3335  CA  GLY A 227     9976   9564   9935  -1410   1249  -1647
ATOM   3336  C   GLY A 227     -21.253  40.460  -0.594  1.00 76.92           C  
ANISOU 3336  C   GLY A 227     9914   9496   9817  -1458   1096  -1472
ATOM   3337  O   GLY A 227     -20.646  39.401  -0.664  1.00 76.61           O  
ANISOU 3337  O   GLY A 227     9830   9586   9692  -1512   1052  -1376
ATOM   3338  H   GLY A 227     -23.384  42.359   0.812  1.00  0.00           H  
ATOM   3339  HA3 GLY A 227     -23.405  40.481  -0.459  1.00  0.00           H  
ATOM   3340  HA2 GLY A 227     -22.624  39.637   0.869  1.00  0.00           H  
ATOM   3341  N   TRP A 228     -20.799  41.596  -1.156  1.00 83.69           N  
ANISOU 3341  N   TRP A 228    10848  10212  10738  -1445   1027  -1436
ATOM   3342  CA  TRP A 228     -19.574  41.719  -1.951  1.00 83.70           C  
ANISOU 3342  CA  TRP A 228    10873  10228  10701  -1526    905  -1285
ATOM   3343  C   TRP A 228     -18.313  41.522  -1.099  1.00 83.73           C  
ANISOU 3343  C   TRP A 228    10921  10336  10556  -1707    878  -1259
ATOM   3344  O   TRP A 228     -17.456  40.739  -1.503  1.00 83.33           O  
ANISOU 3344  O   TRP A 228    10776  10427  10460  -1742    823  -1149
ATOM   3345  CB  TRP A 228     -19.605  43.056  -2.722  1.00 94.13           C  
ANISOU 3345  CB  TRP A 228    12315  11348  12102  -1508    850  -1266
ATOM   3346  CG  TRP A 228     -18.628  43.298  -3.842  1.00 94.16           C  
ANISOU 3346  CG  TRP A 228    12334  11377  12064  -1604    745  -1110
ATOM   3347  CD1 TRP A 228     -17.605  42.503  -4.238  1.00 94.28           C  
ANISOU 3347  CD1 TRP A 228    12272  11572  11980  -1728    717  -1022
ATOM   3348  CD2 TRP A 228     -18.621  44.425  -4.772  1.00 93.94           C  
ANISOU 3348  CD2 TRP A 228    12408  11189  12095  -1588    663  -1027
ATOM   3349  NE1 TRP A 228     -16.959  43.065  -5.317  1.00 94.12           N  
ANISOU 3349  NE1 TRP A 228    12282  11534  11945  -1806    653   -906
ATOM   3350  CE2 TRP A 228     -17.551  44.247  -5.701  1.00 93.90           C  
ANISOU 3350  CE2 TRP A 228    12389  11293  11995  -1741    610   -899
ATOM   3351  CE3 TRP A 228     -19.426  45.574  -4.937  1.00 93.67           C  
ANISOU 3351  CE3 TRP A 228    12480  10920  12190  -1452    627  -1044
ATOM   3352  CZ2 TRP A 228     -17.296  45.159  -6.740  1.00 93.60           C  
ANISOU 3352  CZ2 TRP A 228    12468  11144  11951  -1803    530   -787
ATOM   3353  CZ3 TRP A 228     -19.190  46.492  -5.981  1.00 93.42           C  
ANISOU 3353  CZ3 TRP A 228    12573  10755  12166  -1486    513   -911
ATOM   3354  CH2 TRP A 228     -18.128  46.285  -6.883  1.00 93.38           C  
ANISOU 3354  CH2 TRP A 228    12581  10872  12029  -1683    468   -781
ATOM   3355  H   TRP A 228     -21.354  42.438  -1.070  1.00  0.00           H  
ATOM   3356  HA  TRP A 228     -19.578  40.916  -2.687  1.00  0.00           H  
ATOM   3357  HB3 TRP A 228     -19.530  43.893  -2.028  1.00  0.00           H  
ATOM   3358  HB2 TRP A 228     -20.586  43.152  -3.189  1.00  0.00           H  
ATOM   3359  HD1 TRP A 228     -17.344  41.553  -3.801  1.00  0.00           H  
ATOM   3360  HE1 TRP A 228     -16.172  42.624  -5.771  1.00  0.00           H  
ATOM   3361  HE3 TRP A 228     -20.245  45.741  -4.253  1.00  0.00           H  
ATOM   3362  HZ2 TRP A 228     -16.482  44.991  -7.429  1.00  0.00           H  
ATOM   3363  HZ3 TRP A 228     -19.824  47.359  -6.087  1.00  0.00           H  
ATOM   3364  HH2 TRP A 228     -17.950  46.991  -7.680  1.00  0.00           H  
ATOM   3365  N   CYS A 229     -18.252  42.155   0.086  1.00 72.44           N  
ANISOU 3365  N   CYS A 229     9625   8847   9051  -1814    920  -1366
ATOM   3366  CA  CYS A 229     -17.185  41.971   1.080  1.00 72.91           C  
ANISOU 3366  CA  CYS A 229     9728   9021   8955  -2004    860  -1335
ATOM   3367  C   CYS A 229     -17.047  40.502   1.516  1.00 72.12           C  
ANISOU 3367  C   CYS A 229     9525   9085   8793  -1978    852  -1283
ATOM   3368  O   CYS A 229     -15.932  39.984   1.564  1.00 71.97           O  
ANISOU 3368  O   CYS A 229     9431   9195   8718  -2040    750  -1167
ATOM   3369  CB  CYS A 229     -17.406  42.841   2.333  1.00 74.60           C  
ANISOU 3369  CB  CYS A 229    10140   9136   9067  -2148    915  -1477
ATOM   3370  SG  CYS A 229     -17.252  44.599   1.927  1.00 75.81           S  
ANISOU 3370  SG  CYS A 229    10480   9011   9313  -2142    966  -1584
ATOM   3371  H   CYS A 229     -18.995  42.791   0.347  1.00  0.00           H  
ATOM   3372  HA  CYS A 229     -16.243  42.264   0.612  1.00  0.00           H  
ATOM   3373  HB3 CYS A 229     -16.668  42.610   3.103  1.00  0.00           H  
ATOM   3374  HB2 CYS A 229     -18.389  42.665   2.770  1.00  0.00           H  
ATOM   3375  HG  CYS A 229     -17.500  45.052   3.159  1.00  0.00           H  
ATOM   3376  N   VAL A 230     -18.196  39.862   1.781  1.00 71.47           N  
ANISOU 3376  N   VAL A 230     9443   8991   8720  -1897    961  -1374
ATOM   3377  CA  VAL A 230     -18.305  38.463   2.169  1.00 71.37           C  
ANISOU 3377  CA  VAL A 230     9390   9096   8630  -1895    968  -1335
ATOM   3378  C   VAL A 230     -17.916  37.490   1.038  1.00 70.52           C  
ANISOU 3378  C   VAL A 230     9137   9072   8584  -1796    895  -1190
ATOM   3379  O   VAL A 230     -17.185  36.545   1.319  1.00 70.32           O  
ANISOU 3379  O   VAL A 230     9091   9137   8491  -1827    816  -1093
ATOM   3380  CB  VAL A 230     -19.731  38.160   2.707  1.00 68.89           C  
ANISOU 3380  CB  VAL A 230     9092   8759   8324  -1849   1124  -1471
ATOM   3381  CG1 VAL A 230     -20.102  36.674   2.772  1.00 68.24           C  
ANISOU 3381  CG1 VAL A 230     8969   8775   8184  -1837   1128  -1407
ATOM   3382  CG2 VAL A 230     -19.930  38.789   4.097  1.00 70.41           C  
ANISOU 3382  CG2 VAL A 230     9451   8903   8398  -1990   1220  -1623
ATOM   3383  H   VAL A 230     -19.070  40.369   1.718  1.00  0.00           H  
ATOM   3384  HA  VAL A 230     -17.598  38.299   2.985  1.00  0.00           H  
ATOM   3385  HB  VAL A 230     -20.455  38.635   2.044  1.00  0.00           H  
ATOM   3386 HG11 VAL A 230     -20.978  36.533   3.398  1.00  0.00           H  
ATOM   3387 HG12 VAL A 230     -20.335  36.282   1.782  1.00  0.00           H  
ATOM   3388 HG13 VAL A 230     -19.301  36.077   3.209  1.00  0.00           H  
ATOM   3389 HG21 VAL A 230     -20.969  38.725   4.413  1.00  0.00           H  
ATOM   3390 HG22 VAL A 230     -19.322  38.287   4.850  1.00  0.00           H  
ATOM   3391 HG23 VAL A 230     -19.655  39.843   4.111  1.00  0.00           H  
ATOM   3392  N   THR A 231     -18.359  37.745  -0.206  1.00 72.11           N  
ANISOU 3392  N   THR A 231     9251   9237   8911  -1680    915  -1173
ATOM   3393  CA  THR A 231     -18.036  36.919  -1.376  1.00 71.65           C  
ANISOU 3393  CA  THR A 231     9083   9246   8895  -1607    879  -1065
ATOM   3394  C   THR A 231     -16.556  37.047  -1.808  1.00 71.48           C  
ANISOU 3394  C   THR A 231     9013   9287   8857  -1670    791   -967
ATOM   3395  O   THR A 231     -15.975  36.056  -2.249  1.00 71.15           O  
ANISOU 3395  O   THR A 231     8892   9333   8810  -1633    767   -892
ATOM   3396  CB  THR A 231     -18.939  37.236  -2.603  1.00 83.59           C  
ANISOU 3396  CB  THR A 231    10546  10708  10505  -1517    903  -1069
ATOM   3397  OG1 THR A 231     -20.300  37.253  -2.229  1.00 83.71           O  
ANISOU 3397  OG1 THR A 231    10570  10673  10564  -1466    975  -1176
ATOM   3398  CG2 THR A 231     -18.900  36.171  -3.703  1.00 83.06           C  
ANISOU 3398  CG2 THR A 231    10405  10711  10441  -1462    912  -1003
ATOM   3399  H   THR A 231     -18.965  38.539  -0.368  1.00  0.00           H  
ATOM   3400  HA  THR A 231     -18.205  35.877  -1.096  1.00  0.00           H  
ATOM   3401  HB  THR A 231     -18.686  38.213  -3.017  1.00  0.00           H  
ATOM   3402  HG1 THR A 231     -20.449  38.000  -1.639  1.00  0.00           H  
ATOM   3403 HG21 THR A 231     -19.500  36.465  -4.565  1.00  0.00           H  
ATOM   3404 HG22 THR A 231     -17.894  35.946  -4.056  1.00  0.00           H  
ATOM   3405 HG23 THR A 231     -19.341  35.257  -3.315  1.00  0.00           H  
ATOM   3406  N   THR A 232     -15.958  38.239  -1.615  1.00 75.00           N  
ANISOU 3406  N   THR A 232     9508   9690   9300  -1769    749   -975
ATOM   3407  CA  THR A 232     -14.532  38.509  -1.819  1.00 74.96           C  
ANISOU 3407  CA  THR A 232     9432   9777   9272  -1873    668   -891
ATOM   3408  C   THR A 232     -13.659  37.742  -0.806  1.00 74.85           C  
ANISOU 3408  C   THR A 232     9361   9887   9191  -1911    591   -840
ATOM   3409  O   THR A 232     -12.745  37.036  -1.228  1.00 74.42           O  
ANISOU 3409  O   THR A 232     9159   9944   9174  -1852    560   -757
ATOM   3410  CB  THR A 232     -14.202  40.026  -1.703  1.00 78.38           C  
ANISOU 3410  CB  THR A 232     9974  10123   9682  -2022    637   -923
ATOM   3411  OG1 THR A 232     -14.863  40.726  -2.737  1.00 78.42           O  
ANISOU 3411  OG1 THR A 232    10040   9994   9760  -1968    676   -935
ATOM   3412  CG2 THR A 232     -12.708  40.403  -1.778  1.00 78.76           C  
ANISOU 3412  CG2 THR A 232     9935  10301   9691  -2183    551   -846
ATOM   3413  H   THR A 232     -16.505  39.009  -1.254  1.00  0.00           H  
ATOM   3414  HA  THR A 232     -14.265  38.170  -2.823  1.00  0.00           H  
ATOM   3415  HB  THR A 232     -14.602  40.414  -0.766  1.00  0.00           H  
ATOM   3416  HG1 THR A 232     -15.809  40.702  -2.558  1.00  0.00           H  
ATOM   3417 HG21 THR A 232     -12.580  41.485  -1.813  1.00  0.00           H  
ATOM   3418 HG22 THR A 232     -12.152  40.047  -0.911  1.00  0.00           H  
ATOM   3419 HG23 THR A 232     -12.242  39.985  -2.671  1.00  0.00           H  
ATOM   3420  N   GLY A 233     -13.976  37.872   0.496  1.00 75.32           N  
ANISOU 3420  N   GLY A 233     9546   9919   9153  -2003    562   -893
ATOM   3421  CA  GLY A 233     -13.230  37.252   1.592  1.00 75.42           C  
ANISOU 3421  CA  GLY A 233     9547  10037   9072  -2065    448   -826
ATOM   3422  C   GLY A 233     -13.393  35.725   1.605  1.00 74.67           C  
ANISOU 3422  C   GLY A 233     9393   9976   9003  -1911    449   -760
ATOM   3423  O   GLY A 233     -12.401  35.017   1.775  1.00 74.19           O  
ANISOU 3423  O   GLY A 233     9205  10017   8966  -1866    342   -647
ATOM   3424  H   GLY A 233     -14.754  38.464   0.757  1.00  0.00           H  
ATOM   3425  HA3 GLY A 233     -13.594  37.655   2.537  1.00  0.00           H  
ATOM   3426  HA2 GLY A 233     -12.173  37.515   1.516  1.00  0.00           H  
ATOM   3427  N   ALA A 234     -14.623  35.223   1.380  1.00 75.90           N  
ANISOU 3427  N   ALA A 234     9632  10041   9165  -1827    571   -831
ATOM   3428  CA  ALA A 234     -14.937  33.796   1.258  1.00 75.41           C  
ANISOU 3428  CA  ALA A 234     9571   9974   9107  -1710    592   -784
ATOM   3429  C   ALA A 234     -14.288  33.149   0.029  1.00 74.78           C  
ANISOU 3429  C   ALA A 234     9330   9934   9149  -1567    597   -710
ATOM   3430  O   ALA A 234     -13.839  32.010   0.132  1.00 74.26           O  
ANISOU 3430  O   ALA A 234     9235   9882   9099  -1472    551   -629
ATOM   3431  CB  ALA A 234     -16.459  33.586   1.203  1.00 74.70           C  
ANISOU 3431  CB  ALA A 234     9581   9804   8998  -1695    732   -890
ATOM   3432  H   ALA A 234     -15.404  35.855   1.256  1.00  0.00           H  
ATOM   3433  HA  ALA A 234     -14.556  33.295   2.148  1.00  0.00           H  
ATOM   3434  HB1 ALA A 234     -16.710  32.526   1.138  1.00  0.00           H  
ATOM   3435  HB2 ALA A 234     -16.947  33.980   2.095  1.00  0.00           H  
ATOM   3436  HB3 ALA A 234     -16.903  34.075   0.335  1.00  0.00           H  
ATOM   3437  N   GLY A 235     -14.237  33.893  -1.090  1.00 77.51           N  
ANISOU 3437  N   GLY A 235     9592  10284   9573  -1556    657   -740
ATOM   3438  CA  GLY A 235     -13.648  33.458  -2.353  1.00 77.16           C  
ANISOU 3438  CA  GLY A 235     9411  10286   9620  -1456    697   -695
ATOM   3439  C   GLY A 235     -12.126  33.315  -2.241  1.00 77.14           C  
ANISOU 3439  C   GLY A 235     9250  10401   9658  -1442    600   -607
ATOM   3440  O   GLY A 235     -11.586  32.366  -2.800  1.00 76.77           O  
ANISOU 3440  O   GLY A 235     9103  10383   9683  -1306    615   -561
ATOM   3441  H   GLY A 235     -14.645  34.818  -1.081  1.00  0.00           H  
ATOM   3442  HA3 GLY A 235     -13.883  34.193  -3.123  1.00  0.00           H  
ATOM   3443  HA2 GLY A 235     -14.088  32.511  -2.665  1.00  0.00           H  
ATOM   3444  N   ILE A 236     -11.454  34.221  -1.506  1.00 78.33           N  
ANISOU 3444  N   ILE A 236     9373  10620   9770  -1585    500   -590
ATOM   3445  CA  ILE A 236     -10.020  34.160  -1.197  1.00 79.65           C  
ANISOU 3445  CA  ILE A 236     9349  10937   9976  -1604    379   -503
ATOM   3446  C   ILE A 236      -9.682  32.987  -0.253  1.00 79.81           C  
ANISOU 3446  C   ILE A 236     9364  10970   9990  -1497    255   -414
ATOM   3447  O   ILE A 236      -8.693  32.294  -0.492  1.00 80.40           O  
ANISOU 3447  O   ILE A 236     9241  11136  10172  -1369    197   -334
ATOM   3448  CB  ILE A 236      -9.513  35.501  -0.574  1.00 83.66           C  
ANISOU 3448  CB  ILE A 236     9876  11509  10404  -1832    276   -507
ATOM   3449  CG1 ILE A 236      -9.533  36.637  -1.624  1.00 84.05           C  
ANISOU 3449  CG1 ILE A 236     9958  11517  10461  -1945    378   -573
ATOM   3450  CG2 ILE A 236      -8.115  35.442   0.090  1.00 85.01           C  
ANISOU 3450  CG2 ILE A 236     9818  11872  10610  -1873    119   -407
ATOM   3451  CD1 ILE A 236      -9.514  38.047  -1.014  1.00 85.40           C  
ANISOU 3451  CD1 ILE A 236    10188  11713  10548  -2189    293   -589
ATOM   3452  H   ILE A 236     -11.963  34.988  -1.087  1.00  0.00           H  
ATOM   3453  HA  ILE A 236      -9.484  33.994  -2.134  1.00  0.00           H  
ATOM   3454  HB  ILE A 236     -10.222  35.774   0.208  1.00  0.00           H  
ATOM   3455 HG13 ILE A 236     -10.412  36.555  -2.261  1.00  0.00           H  
ATOM   3456 HG12 ILE A 236      -8.683  36.523  -2.299  1.00  0.00           H  
ATOM   3457 HG21 ILE A 236      -7.803  36.423   0.448  1.00  0.00           H  
ATOM   3458 HG22 ILE A 236      -8.093  34.785   0.959  1.00  0.00           H  
ATOM   3459 HG23 ILE A 236      -7.358  35.094  -0.614  1.00  0.00           H  
ATOM   3460 HD11 ILE A 236      -9.944  38.771  -1.707  1.00  0.00           H  
ATOM   3461 HD12 ILE A 236     -10.092  38.096  -0.091  1.00  0.00           H  
ATOM   3462 HD13 ILE A 236      -8.497  38.370  -0.792  1.00  0.00           H  
ATOM   3463  N   ALA A 237     -10.520  32.781   0.779  1.00 77.75           N  
ANISOU 3463  N   ALA A 237     9326  10612   9606  -1548    220   -428
ATOM   3464  CA  ALA A 237     -10.375  31.725   1.781  1.00 79.12           C  
ANISOU 3464  CA  ALA A 237     9565  10768   9731  -1484     82   -326
ATOM   3465  C   ALA A 237     -10.580  30.304   1.227  1.00 79.04           C  
ANISOU 3465  C   ALA A 237     9556  10662   9813  -1259    154   -294
ATOM   3466  O   ALA A 237      -9.886  29.389   1.670  1.00 80.90           O  
ANISOU 3466  O   ALA A 237     9743  10896  10098  -1127     27   -177
ATOM   3467  CB  ALA A 237     -11.349  32.001   2.934  1.00 77.53           C  
ANISOU 3467  CB  ALA A 237     9633  10489   9337  -1649     60   -367
ATOM   3468  H   ALA A 237     -11.306  33.405   0.907  1.00  0.00           H  
ATOM   3469  HA  ALA A 237      -9.359  31.780   2.178  1.00  0.00           H  
ATOM   3470  HB1 ALA A 237     -11.294  31.227   3.700  1.00  0.00           H  
ATOM   3471  HB2 ALA A 237     -11.126  32.954   3.414  1.00  0.00           H  
ATOM   3472  HB3 ALA A 237     -12.377  32.045   2.576  1.00  0.00           H  
ATOM   3473  N   SER A 238     -11.500  30.150   0.260  1.00 87.12           N  
ANISOU 3473  N   SER A 238    10647  11595  10860  -1218    345   -396
ATOM   3474  CA  SER A 238     -11.785  28.889  -0.426  1.00 86.99           C  
ANISOU 3474  CA  SER A 238    10676  11468  10906  -1045    436   -391
ATOM   3475  C   SER A 238     -10.867  28.618  -1.635  1.00 87.42           C  
ANISOU 3475  C   SER A 238    10516  11574  11125   -891    524   -399
ATOM   3476  O   SER A 238     -10.944  27.519  -2.186  1.00 87.54           O  
ANISOU 3476  O   SER A 238    10572  11486  11201   -738    615   -408
ATOM   3477  CB  SER A 238     -13.275  28.868  -0.829  1.00 83.57           C  
ANISOU 3477  CB  SER A 238    10429  10928  10394  -1110    588   -498
ATOM   3478  OG  SER A 238     -13.545  29.698  -1.945  1.00 83.73           O  
ANISOU 3478  OG  SER A 238    10376  10993  10447  -1166    697   -589
ATOM   3479  H   SER A 238     -12.050  30.945  -0.039  1.00  0.00           H  
ATOM   3480  HA  SER A 238     -11.633  28.071   0.281  1.00  0.00           H  
ATOM   3481  HB3 SER A 238     -13.908  29.169   0.005  1.00  0.00           H  
ATOM   3482  HB2 SER A 238     -13.568  27.851  -1.090  1.00  0.00           H  
ATOM   3483  HG  SER A 238     -14.464  29.583  -2.198  1.00  0.00           H  
ATOM   3484  N   TYR A 239     -10.043  29.604  -2.044  1.00 93.83           N  
ANISOU 3484  N   TYR A 239    11116  12538  11997   -948    514   -405
ATOM   3485  CA  TYR A 239      -9.235  29.532  -3.263  1.00 94.59           C  
ANISOU 3485  CA  TYR A 239    11005  12707  12228   -845    638   -436
ATOM   3486  C   TYR A 239      -8.149  28.427  -3.311  1.00 96.17           C  
ANISOU 3486  C   TYR A 239    11046  12912  12583   -604    607   -371
ATOM   3487  O   TYR A 239      -7.981  27.860  -4.389  1.00 96.69           O  
ANISOU 3487  O   TYR A 239    11080  12925  12733   -471    781   -437
ATOM   3488  CB  TYR A 239      -8.648  30.910  -3.646  1.00104.71           C  
ANISOU 3488  CB  TYR A 239    12103  14158  13522  -1001    635   -452
ATOM   3489  CG  TYR A 239      -8.270  30.999  -5.112  1.00104.72           C  
ANISOU 3489  CG  TYR A 239    11984  14212  13593   -979    832   -526
ATOM   3490  CD1 TYR A 239      -9.230  31.381  -6.073  1.00104.75           C  
ANISOU 3490  CD1 TYR A 239    12138  14152  13512  -1093    958   -602
ATOM   3491  CD2 TYR A 239      -6.982  30.616  -5.528  1.00104.55           C  
ANISOU 3491  CD2 TYR A 239    11700  14305  13720   -843    894   -522
ATOM   3492  CE1 TYR A 239      -8.910  31.340  -7.445  1.00104.63           C  
ANISOU 3492  CE1 TYR A 239    12054  14183  13517  -1110   1135   -664
ATOM   3493  CE2 TYR A 239      -6.667  30.560  -6.896  1.00103.85           C  
ANISOU 3493  CE2 TYR A 239    11522  14268  13669   -848   1111   -611
ATOM   3494  CZ  TYR A 239      -7.633  30.912  -7.857  1.00103.98           C  
ANISOU 3494  CZ  TYR A 239    11732  14216  13559  -1000   1230   -679
ATOM   3495  OH  TYR A 239      -7.330  30.833  -9.184  1.00103.29           O  
ANISOU 3495  OH  TYR A 239    11598  14177  13470  -1036   1442   -763
ATOM   3496  H   TYR A 239     -10.029  30.483  -1.545  1.00  0.00           H  
ATOM   3497  HA  TYR A 239      -9.949  29.279  -4.050  1.00  0.00           H  
ATOM   3498  HB3 TYR A 239      -7.788  31.157  -3.022  1.00  0.00           H  
ATOM   3499  HB2 TYR A 239      -9.369  31.699  -3.463  1.00  0.00           H  
ATOM   3500  HD1 TYR A 239     -10.222  31.672  -5.761  1.00  0.00           H  
ATOM   3501  HD2 TYR A 239      -6.252  30.313  -4.796  1.00  0.00           H  
ATOM   3502  HE1 TYR A 239      -9.652  31.614  -8.180  1.00  0.00           H  
ATOM   3503  HE2 TYR A 239      -5.688  30.220  -7.195  1.00  0.00           H  
ATOM   3504  HH  TYR A 239      -6.423  30.552  -9.335  1.00  0.00           H  
ATOM   3505  N   PRO A 240      -7.468  28.075  -2.192  1.00 90.97           N  
ANISOU 3505  N   PRO A 240    10290  12305  11970   -531    394   -245
ATOM   3506  CA  PRO A 240      -6.519  26.941  -2.186  1.00 93.73           C  
ANISOU 3506  CA  PRO A 240    10461  12642  12511   -249    363   -181
ATOM   3507  C   PRO A 240      -7.145  25.578  -2.524  1.00 93.67           C  
ANISOU 3507  C   PRO A 240    10683  12385  12525    -61    476   -207
ATOM   3508  O   PRO A 240      -6.521  24.799  -3.243  1.00 95.28           O  
ANISOU 3508  O   PRO A 240    10768  12542  12891    156    615   -254
ATOM   3509  CB  PRO A 240      -5.912  26.962  -0.774  1.00 97.48           C  
ANISOU 3509  CB  PRO A 240    10865  13191  12982   -243     57    -14
ATOM   3510  CG  PRO A 240      -6.049  28.408  -0.338  1.00 96.14           C  
ANISOU 3510  CG  PRO A 240    10722  13155  12650   -548    -26    -25
ATOM   3511  CD  PRO A 240      -7.390  28.815  -0.932  1.00 92.95           C  
ANISOU 3511  CD  PRO A 240    10580  12631  12105   -697    164   -156
ATOM   3512  HA  PRO A 240      -5.738  27.168  -2.914  1.00  0.00           H  
ATOM   3513  HB3 PRO A 240      -4.877  26.621  -0.757  1.00  0.00           H  
ATOM   3514  HB2 PRO A 240      -6.480  26.324  -0.094  1.00  0.00           H  
ATOM   3515  HG3 PRO A 240      -5.254  28.992  -0.801  1.00  0.00           H  
ATOM   3516  HG2 PRO A 240      -5.991  28.548   0.742  1.00  0.00           H  
ATOM   3517  HD2 PRO A 240      -8.202  28.493  -0.281  1.00  0.00           H  
ATOM   3518  HD3 PRO A 240      -7.449  29.896  -1.056  1.00  0.00           H  
ATOM   3519  N   LEU A 241      -8.378  25.342  -2.043  1.00 83.89           N  
ANISOU 3519  N   LEU A 241     9776  10983  11114   -167    448   -199
ATOM   3520  CA  LEU A 241      -9.169  24.149  -2.348  1.00 83.93           C  
ANISOU 3520  CA  LEU A 241    10037  10746  11106    -51    558   -230
ATOM   3521  C   LEU A 241      -9.722  24.155  -3.784  1.00 82.57           C  
ANISOU 3521  C   LEU A 241     9882  10545  10944    -68    832   -393
ATOM   3522  O   LEU A 241      -9.863  23.072  -4.347  1.00 83.67           O  
ANISOU 3522  O   LEU A 241    10146  10510  11133     75    963   -442
ATOM   3523  CB  LEU A 241     -10.290  23.988  -1.298  1.00 79.18           C  
ANISOU 3523  CB  LEU A 241     9767  10017  10299   -216    478   -192
ATOM   3524  CG  LEU A 241      -9.768  23.602   0.106  1.00 79.24           C  
ANISOU 3524  CG  LEU A 241     9853   9995  10258   -199    211    -19
ATOM   3525  CD1 LEU A 241     -10.857  23.747   1.187  1.00 79.11           C  
ANISOU 3525  CD1 LEU A 241    10173   9871  10014   -407    186    -12
ATOM   3526  CD2 LEU A 241      -9.118  22.202   0.128  1.00 79.52           C  
ANISOU 3526  CD2 LEU A 241     9875   9882  10459    102    121     95
ATOM   3527  H   LEU A 241      -8.831  26.040  -1.470  1.00  0.00           H  
ATOM   3528  HA  LEU A 241      -8.506  23.285  -2.283  1.00  0.00           H  
ATOM   3529  HB3 LEU A 241     -11.003  23.228  -1.625  1.00  0.00           H  
ATOM   3530  HB2 LEU A 241     -10.851  24.921  -1.243  1.00  0.00           H  
ATOM   3531  HG  LEU A 241      -8.993  24.322   0.372  1.00  0.00           H  
ATOM   3532 HD11 LEU A 241     -10.448  24.219   2.081  1.00  0.00           H  
ATOM   3533 HD12 LEU A 241     -11.687  24.372   0.859  1.00  0.00           H  
ATOM   3534 HD13 LEU A 241     -11.276  22.788   1.489  1.00  0.00           H  
ATOM   3535 HD21 LEU A 241      -9.447  21.601   0.977  1.00  0.00           H  
ATOM   3536 HD22 LEU A 241      -9.345  21.631  -0.773  1.00  0.00           H  
ATOM   3537 HD23 LEU A 241      -8.033  22.282   0.198  1.00  0.00           H  
ATOM   3538  N   ASP A 242      -9.962  25.346  -4.371  1.00 87.32           N  
ANISOU 3538  N   ASP A 242    10379  11306  11492   -250    910   -471
ATOM   3539  CA  ASP A 242     -10.264  25.522  -5.798  1.00 86.38           C  
ANISOU 3539  CA  ASP A 242    10274  11188  11358   -301   1138   -606
ATOM   3540  C   ASP A 242      -9.053  25.155  -6.679  1.00 88.61           C  
ANISOU 3540  C   ASP A 242    10314  11543  11811   -133   1270   -652
ATOM   3541  O   ASP A 242      -9.241  24.511  -7.708  1.00 89.10           O  
ANISOU 3541  O   ASP A 242    10447  11527  11880    -90   1480   -763
ATOM   3542  CB  ASP A 242     -10.770  26.949  -6.133  1.00 89.25           C  
ANISOU 3542  CB  ASP A 242    10629  11674  11609   -542   1149   -649
ATOM   3543  CG  ASP A 242     -11.147  27.155  -7.609  1.00 89.64           C  
ANISOU 3543  CG  ASP A 242    10683  11747  11629   -613   1347   -758
ATOM   3544  OD1 ASP A 242     -11.912  26.318  -8.135  1.00 89.99           O  
ANISOU 3544  OD1 ASP A 242    10930  11674  11587   -653   1439   -820
ATOM   3545  OD2 ASP A 242     -10.698  28.170  -8.185  1.00 90.06           O1-
ANISOU 3545  OD2 ASP A 242    10545  11944  11732   -651   1408   -779
ATOM   3546  H   ASP A 242      -9.837  26.195  -3.837  1.00  0.00           H  
ATOM   3547  HA  ASP A 242     -11.070  24.825  -6.035  1.00  0.00           H  
ATOM   3548  HB3 ASP A 242      -9.990  27.670  -5.895  1.00  0.00           H  
ATOM   3549  HB2 ASP A 242     -11.621  27.221  -5.509  1.00  0.00           H  
ATOM   3550  N   THR A 243      -7.839  25.557  -6.265  1.00 87.31           N  
ANISOU 3550  N   THR A 243     9857  11541  11778    -55   1158   -579
ATOM   3551  CA  THR A 243      -6.604  25.256  -6.986  1.00 89.83           C  
ANISOU 3551  CA  THR A 243     9878  11964  12288    116   1292   -631
ATOM   3552  C   THR A 243      -6.281  23.755  -6.979  1.00 91.17           C  
ANISOU 3552  C   THR A 243    10118  11923  12598    421   1354   -639
ATOM   3553  O   THR A 243      -5.991  23.230  -8.049  1.00 93.01           O  
ANISOU 3553  O   THR A 243    10336  12102  12900    522   1606   -774
ATOM   3554  CB  THR A 243      -5.392  26.053  -6.445  1.00101.08           C  
ANISOU 3554  CB  THR A 243    10957  13632  13817    102   1125   -540
ATOM   3555  OG1 THR A 243      -5.659  27.416  -6.691  1.00 98.84           O  
ANISOU 3555  OG1 THR A 243    10656  13503  13394   -199   1124   -564
ATOM   3556  CG2 THR A 243      -4.036  25.709  -7.095  1.00104.24           C  
ANISOU 3556  CG2 THR A 243    10992  14165  14450    305   1251   -589
ATOM   3557  H   THR A 243      -7.751  26.129  -5.435  1.00  0.00           H  
ATOM   3558  HA  THR A 243      -6.759  25.551  -8.027  1.00  0.00           H  
ATOM   3559  HB  THR A 243      -5.308  25.929  -5.365  1.00  0.00           H  
ATOM   3560  HG1 THR A 243      -5.027  27.951  -6.199  1.00  0.00           H  
ATOM   3561 HG21 THR A 243      -3.278  26.454  -6.861  1.00  0.00           H  
ATOM   3562 HG22 THR A 243      -3.657  24.744  -6.757  1.00  0.00           H  
ATOM   3563 HG23 THR A 243      -4.123  25.674  -8.181  1.00  0.00           H  
ATOM   3564  N   VAL A 244      -6.413  23.083  -5.821  1.00 94.62           N  
ANISOU 3564  N   VAL A 244    10685  12216  13051    546   1136   -503
ATOM   3565  CA  VAL A 244      -6.270  21.627  -5.708  1.00 97.20           C  
ANISOU 3565  CA  VAL A 244    11149  12281  13501    839   1154   -481
ATOM   3566  C   VAL A 244      -7.358  20.859  -6.495  1.00 95.94           C  
ANISOU 3566  C   VAL A 244    11345  11892  13215    776   1388   -620
ATOM   3567  O   VAL A 244      -7.027  19.852  -7.118  1.00 98.22           O  
ANISOU 3567  O   VAL A 244    11686  12008  13624    989   1567   -709
ATOM   3568  CB  VAL A 244      -6.252  21.160  -4.222  1.00 99.02           C  
ANISOU 3568  CB  VAL A 244    11515  12393  13713    915    839   -279
ATOM   3569  CG1 VAL A 244      -6.313  19.631  -4.019  1.00 99.63           C  
ANISOU 3569  CG1 VAL A 244    11736  12176  13945   1246    838   -235
ATOM   3570  CG2 VAL A 244      -5.009  21.698  -3.491  1.00 99.65           C  
ANISOU 3570  CG2 VAL A 244    11265  12725  13872    914    578   -136
ATOM   3571  H   VAL A 244      -6.660  23.580  -4.975  1.00  0.00           H  
ATOM   3572  HA  VAL A 244      -5.307  21.363  -6.151  1.00  0.00           H  
ATOM   3573  HB  VAL A 244      -7.125  21.587  -3.725  1.00  0.00           H  
ATOM   3574 HG11 VAL A 244      -6.150  19.375  -2.972  1.00  0.00           H  
ATOM   3575 HG12 VAL A 244      -7.280  19.213  -4.300  1.00  0.00           H  
ATOM   3576 HG13 VAL A 244      -5.545  19.124  -4.603  1.00  0.00           H  
ATOM   3577 HG21 VAL A 244      -5.033  21.428  -2.437  1.00  0.00           H  
ATOM   3578 HG22 VAL A 244      -4.092  21.286  -3.915  1.00  0.00           H  
ATOM   3579 HG23 VAL A 244      -4.934  22.783  -3.547  1.00  0.00           H  
ATOM   3580  N   ARG A 245      -8.603  21.373  -6.507  1.00103.42           N  
ANISOU 3580  N   ARG A 245    12525  12843  13928    482   1389   -647
ATOM   3581  CA  ARG A 245      -9.726  20.857  -7.299  1.00102.36           C  
ANISOU 3581  CA  ARG A 245    12711  12536  13646    362   1570   -766
ATOM   3582  C   ARG A 245      -9.436  20.885  -8.809  1.00103.53           C  
ANISOU 3582  C   ARG A 245    12783  12733  13821    355   1849   -938
ATOM   3583  O   ARG A 245      -9.443  19.826  -9.431  1.00105.31           O  
ANISOU 3583  O   ARG A 245    13167  12761  14087    482   2028  -1037
ATOM   3584  CB  ARG A 245     -11.012  21.630  -6.931  1.00102.08           C  
ANISOU 3584  CB  ARG A 245    12840  12560  13387     55   1490   -753
ATOM   3585  CG  ARG A 245     -12.281  21.250  -7.718  1.00101.65           C  
ANISOU 3585  CG  ARG A 245    13072  12376  13174   -105   1645   -866
ATOM   3586  CD  ARG A 245     -13.422  22.263  -7.531  1.00100.34           C  
ANISOU 3586  CD  ARG A 245    12948  12337  12839   -383   1588   -874
ATOM   3587  NE  ARG A 245     -13.196  23.502  -8.291  1.00 99.96           N  
ANISOU 3587  NE  ARG A 245    12689  12498  12794   -479   1627   -913
ATOM   3588  CZ  ARG A 245     -13.705  23.778  -9.503  1.00100.30           C  
ANISOU 3588  CZ  ARG A 245    12778  12584  12747   -620   1759  -1010
ATOM   3589  NH1 ARG A 245     -14.536  22.930 -10.123  1.00101.00           N  
ANISOU 3589  NH1 ARG A 245    13100  12541  12733   -693   1866  -1089
ATOM   3590  NH2 ARG A 245     -13.380  24.932 -10.093  1.00100.11           N1+
ANISOU 3590  NH2 ARG A 245    12591  12732  12716   -715   1771  -1019
ATOM   3591  H   ARG A 245      -8.798  22.201  -5.959  1.00  0.00           H  
ATOM   3592  HA  ARG A 245      -9.870  19.815  -7.009  1.00  0.00           H  
ATOM   3593  HB3 ARG A 245     -10.835  22.693  -7.066  1.00  0.00           H  
ATOM   3594  HB2 ARG A 245     -11.221  21.493  -5.870  1.00  0.00           H  
ATOM   3595  HG3 ARG A 245     -12.587  20.224  -7.523  1.00  0.00           H  
ATOM   3596  HG2 ARG A 245     -12.041  21.284  -8.779  1.00  0.00           H  
ATOM   3597  HD3 ARG A 245     -13.366  22.608  -6.498  1.00  0.00           H  
ATOM   3598  HD2 ARG A 245     -14.421  21.844  -7.640  1.00  0.00           H  
ATOM   3599  HE  ARG A 245     -12.573  24.185  -7.877  1.00  0.00           H  
ATOM   3600 HH12 ARG A 245     -14.935  23.159 -11.023  1.00  0.00           H  
ATOM   3601 HH11 ARG A 245     -14.795  22.063  -9.675  1.00  0.00           H  
ATOM   3602 HH22 ARG A 245     -13.749  25.182 -10.998  1.00  0.00           H  
ATOM   3603 HH21 ARG A 245     -12.793  25.589  -9.581  1.00  0.00           H  
ATOM   3604  N   ARG A 246      -9.167  22.085  -9.355  1.00109.72           N  
ANISOU 3604  N   ARG A 246    13361  13764  14565    187   1894   -978
ATOM   3605  CA  ARG A 246      -8.828  22.322 -10.763  1.00110.90           C  
ANISOU 3605  CA  ARG A 246    13445  13996  14695    118   2155  -1133
ATOM   3606  C   ARG A 246      -7.619  21.500 -11.242  1.00114.19           C  
ANISOU 3606  C   ARG A 246    13687  14368  15330    404   2336  -1216
ATOM   3607  O   ARG A 246      -7.660  20.984 -12.357  1.00115.90           O  
ANISOU 3607  O   ARG A 246    14041  14471  15525    428   2596  -1375
ATOM   3608  CB  ARG A 246      -8.545  23.824 -10.986  1.00120.67           C  
ANISOU 3608  CB  ARG A 246    14471  15505  15876    -94   2122  -1116
ATOM   3609  CG  ARG A 246      -9.785  24.734 -10.986  1.00119.34           C  
ANISOU 3609  CG  ARG A 246    14482  15364  15499   -371   2012  -1080
ATOM   3610  CD  ARG A 246      -9.380  26.217 -10.967  1.00119.08           C  
ANISOU 3610  CD  ARG A 246    14254  15550  15441   -538   1933  -1031
ATOM   3611  NE  ARG A 246     -10.496  27.119 -11.278  1.00118.37           N  
ANISOU 3611  NE  ARG A 246    14334  15471  15169   -781   1889  -1028
ATOM   3612  CZ  ARG A 246     -10.807  27.577 -12.505  1.00119.07           C  
ANISOU 3612  CZ  ARG A 246    14463  15631  15147   -960   2005  -1085
ATOM   3613  NH1 ARG A 246     -10.073  27.249 -13.579  1.00120.71           N  
ANISOU 3613  NH1 ARG A 246    14560  15920  15385   -954   2211  -1172
ATOM   3614  NH2 ARG A 246     -11.867  28.380 -12.658  1.00118.29           N1+
ANISOU 3614  NH2 ARG A 246    14515  15525  14906  -1146   1916  -1054
ATOM   3615  H   ARG A 246      -9.176  22.906  -8.762  1.00  0.00           H  
ATOM   3616  HA  ARG A 246      -9.694  22.031 -11.361  1.00  0.00           H  
ATOM   3617  HB3 ARG A 246      -8.052  23.962 -11.950  1.00  0.00           H  
ATOM   3618  HB2 ARG A 246      -7.831  24.169 -10.235  1.00  0.00           H  
ATOM   3619  HG3 ARG A 246     -10.326  24.532 -10.062  1.00  0.00           H  
ATOM   3620  HG2 ARG A 246     -10.478  24.505 -11.796  1.00  0.00           H  
ATOM   3621  HD3 ARG A 246      -8.453  26.442 -11.497  1.00  0.00           H  
ATOM   3622  HD2 ARG A 246      -9.176  26.456  -9.923  1.00  0.00           H  
ATOM   3623  HE  ARG A 246     -11.053  27.404 -10.481  1.00  0.00           H  
ATOM   3624 HH12 ARG A 246     -10.314  27.597 -14.495  1.00  0.00           H  
ATOM   3625 HH11 ARG A 246      -9.273  26.642 -13.473  1.00  0.00           H  
ATOM   3626 HH22 ARG A 246     -12.118  28.732 -13.570  1.00  0.00           H  
ATOM   3627 HH21 ARG A 246     -12.423  28.643 -11.857  1.00  0.00           H  
ATOM   3628  N   ARG A 247      -6.584  21.385 -10.389  1.00120.72           N  
ANISOU 3628  N   ARG A 247    14217  15279  16371    625   2194  -1113
ATOM   3629  CA  ARG A 247      -5.344  20.670 -10.685  1.00124.68           C  
ANISOU 3629  CA  ARG A 247    14472  15763  17139    950   2335  -1177
ATOM   3630  C   ARG A 247      -5.518  19.139 -10.715  1.00126.74           C  
ANISOU 3630  C   ARG A 247    15012  15669  17473   1201   2434  -1231
ATOM   3631  O   ARG A 247      -4.844  18.488 -11.512  1.00129.63           O  
ANISOU 3631  O   ARG A 247    15317  15957  17980   1393   2707  -1390
ATOM   3632  CB  ARG A 247      -4.254  21.096  -9.679  1.00130.67           C  
ANISOU 3632  CB  ARG A 247    14855  16691  18103   1122   2085  -1017
ATOM   3633  CG  ARG A 247      -2.810  20.961 -10.190  1.00131.58           C  
ANISOU 3633  CG  ARG A 247    14530  16973  18491   1353   2253  -1104
ATOM   3634  CD  ARG A 247      -2.380  22.118 -11.114  1.00130.96           C  
ANISOU 3634  CD  ARG A 247    14228  17196  18333   1086   2460  -1229
ATOM   3635  NE  ARG A 247      -2.279  23.407 -10.402  1.00130.23           N  
ANISOU 3635  NE  ARG A 247    13996  17353  18133    817   2221  -1095
ATOM   3636  CZ  ARG A 247      -1.179  23.901  -9.807  1.00130.72           C  
ANISOU 3636  CZ  ARG A 247    13651  17662  18355    865   2059  -1000
ATOM   3637  NH1 ARG A 247      -0.018  23.233  -9.839  1.00131.96           N  
ANISOU 3637  NH1 ARG A 247    13454  17871  18812   1201   2090  -1010
ATOM   3638  NH2 ARG A 247      -1.233  25.083  -9.178  1.00129.87           N1+
ANISOU 3638  NH2 ARG A 247    13483  17748  18113    579   1862   -898
ATOM   3639  H   ARG A 247      -6.630  21.843  -9.488  1.00  0.00           H  
ATOM   3640  HA  ARG A 247      -5.030  20.967 -11.687  1.00  0.00           H  
ATOM   3641  HB3 ARG A 247      -4.379  20.541  -8.747  1.00  0.00           H  
ATOM   3642  HB2 ARG A 247      -4.384  22.141  -9.418  1.00  0.00           H  
ATOM   3643  HG3 ARG A 247      -2.578  19.979 -10.603  1.00  0.00           H  
ATOM   3644  HG2 ARG A 247      -2.191  21.050  -9.299  1.00  0.00           H  
ATOM   3645  HD3 ARG A 247      -3.205  22.304 -11.801  1.00  0.00           H  
ATOM   3646  HD2 ARG A 247      -1.529  21.879 -11.753  1.00  0.00           H  
ATOM   3647  HE  ARG A 247      -3.141  23.925 -10.315  1.00  0.00           H  
ATOM   3648 HH12 ARG A 247       0.833  23.629  -9.450  1.00  0.00           H  
ATOM   3649 HH11 ARG A 247       0.036  22.345 -10.314  1.00  0.00           H  
ATOM   3650 HH22 ARG A 247      -0.398  25.459  -8.746  1.00  0.00           H  
ATOM   3651 HH21 ARG A 247      -2.092  25.610  -9.137  1.00  0.00           H  
ATOM   3652  N   MET A 248      -6.429  18.597  -9.885  1.00135.00           N  
ANISOU 3652  N   MET A 248    16385  16493  18415   1182   2238  -1113
ATOM   3653  CA  MET A 248      -6.796  17.177  -9.890  1.00137.01           C  
ANISOU 3653  CA  MET A 248    16969  16376  18713   1381   2310  -1145
ATOM   3654  C   MET A 248      -7.725  16.795 -11.055  1.00136.72           C  
ANISOU 3654  C   MET A 248    17276  16192  18481   1185   2592  -1342
ATOM   3655  O   MET A 248      -7.594  15.685 -11.568  1.00139.61           O  
ANISOU 3655  O   MET A 248    17836  16285  18925   1370   2789  -1461
ATOM   3656  CB  MET A 248      -7.433  16.774  -8.546  1.00138.35           C  
ANISOU 3656  CB  MET A 248    17389  16369  18811   1379   2006   -945
ATOM   3657  CG  MET A 248      -6.410  16.573  -7.418  1.00140.79           C  
ANISOU 3657  CG  MET A 248    17469  16669  19354   1692   1752   -759
ATOM   3658  SD  MET A 248      -7.097  15.722  -5.976  1.00140.96           S  
ANISOU 3658  SD  MET A 248    17914  16342  19303   1760   1470   -549
ATOM   3659  CE  MET A 248      -7.061  14.009  -6.570  1.00144.20           C  
ANISOU 3659  CE  MET A 248    18684  16296  19809   2006   1753   -706
ATOM   3660  H   MET A 248      -6.939  19.190  -9.244  1.00  0.00           H  
ATOM   3661  HA  MET A 248      -5.886  16.587 -10.021  1.00  0.00           H  
ATOM   3662  HB3 MET A 248      -7.995  15.847  -8.669  1.00  0.00           H  
ATOM   3663  HB2 MET A 248      -8.170  17.519  -8.243  1.00  0.00           H  
ATOM   3664  HG3 MET A 248      -6.005  17.530  -7.095  1.00  0.00           H  
ATOM   3665  HG2 MET A 248      -5.559  15.992  -7.774  1.00  0.00           H  
ATOM   3666  HE1 MET A 248      -7.435  13.340  -5.795  1.00  0.00           H  
ATOM   3667  HE2 MET A 248      -7.683  13.887  -7.456  1.00  0.00           H  
ATOM   3668  HE3 MET A 248      -6.041  13.712  -6.815  1.00  0.00           H  
ATOM   3669  N   MET A 249      -8.623  17.708 -11.463  1.00145.17           N  
ANISOU 3669  N   MET A 249    18427  17430  19300    816   2604  -1377
ATOM   3670  CA  MET A 249      -9.524  17.522 -12.608  1.00144.29           C  
ANISOU 3670  CA  MET A 249    18628  17222  18972    581   2825  -1544
ATOM   3671  C   MET A 249      -8.863  17.797 -13.974  1.00145.86           C  
ANISOU 3671  C   MET A 249    18686  17556  19178    543   3133  -1738
ATOM   3672  O   MET A 249      -9.513  17.574 -14.996  1.00146.42           O  
ANISOU 3672  O   MET A 249    19016  17562  19053    333   3330  -1887
ATOM   3673  CB  MET A 249     -10.771  18.406 -12.440  1.00143.41           C  
ANISOU 3673  CB  MET A 249    18656  17232  18601    216   2675  -1481
ATOM   3674  CG  MET A 249     -11.664  18.038 -11.245  1.00142.16           C  
ANISOU 3674  CG  MET A 249    18666  16957  18392    189   2427  -1327
ATOM   3675  SD  MET A 249     -13.309  18.798 -11.281  1.00138.91           S  
ANISOU 3675  SD  MET A 249    18396  16683  17703   -219   2308  -1300
ATOM   3676  CE  MET A 249     -12.933  20.492 -11.806  1.00136.83           C  
ANISOU 3676  CE  MET A 249    17803  16759  17428   -347   2316  -1313
ATOM   3677  H   MET A 249      -8.689  18.594 -10.980  1.00  0.00           H  
ATOM   3678  HA  MET A 249      -9.854  16.482 -12.630  1.00  0.00           H  
ATOM   3679  HB3 MET A 249     -11.382  18.365 -13.343  1.00  0.00           H  
ATOM   3680  HB2 MET A 249     -10.445  19.443 -12.340  1.00  0.00           H  
ATOM   3681  HG3 MET A 249     -11.187  18.300 -10.304  1.00  0.00           H  
ATOM   3682  HG2 MET A 249     -11.812  16.958 -11.215  1.00  0.00           H  
ATOM   3683  HE1 MET A 249     -13.856  21.067 -11.855  1.00  0.00           H  
ATOM   3684  HE2 MET A 249     -12.248  20.974 -11.109  1.00  0.00           H  
ATOM   3685  HE3 MET A 249     -12.492  20.508 -12.802  1.00  0.00           H  
ATOM   3686  N   MET A 250      -7.593  18.246 -13.983  1.00156.27           N  
ANISOU 3686  N   MET A 250    19598  19070  20707    724   3179  -1739
ATOM   3687  CA  MET A 250      -6.789  18.544 -15.176  1.00157.42           C  
ANISOU 3687  CA  MET A 250    19557  19385  20871    680   3487  -1923
ATOM   3688  C   MET A 250      -6.509  17.326 -16.091  1.00159.67           C  
ANISOU 3688  C   MET A 250    20032  19422  21213    845   3840  -2152
ATOM   3689  O   MET A 250      -6.049  17.520 -17.216  1.00160.99           O  
ANISOU 3689  O   MET A 250    20085  19711  21371    792   4149  -2340
ATOM   3690  CB  MET A 250      -5.497  19.259 -14.716  1.00  0.00           C  
ATOM   3691  CG  MET A 250      -4.664  19.897 -15.841  1.00  0.00           C  
ATOM   3692  SD  MET A 250      -3.294  20.926 -15.253  1.00  0.00           S  
ATOM   3693  CE  MET A 250      -2.642  21.473 -16.854  1.00  0.00           C  
ATOM   3694  H   MET A 250      -7.132  18.406 -13.098  1.00  0.00           H  
ATOM   3695  HA  MET A 250      -7.369  19.254 -15.768  1.00  0.00           H  
ATOM   3696  HB2 MET A 250      -5.751  20.041 -14.000  1.00  0.00           H  
ATOM   3697  HB3 MET A 250      -4.869  18.552 -14.174  1.00  0.00           H  
ATOM   3698  HG2 MET A 250      -4.231  19.128 -16.479  1.00  0.00           H  
ATOM   3699  HG3 MET A 250      -5.306  20.512 -16.472  1.00  0.00           H  
ATOM   3700  HE1 MET A 250      -1.779  22.123 -16.705  1.00  0.00           H  
ATOM   3701  HE2 MET A 250      -2.331  20.617 -17.452  1.00  0.00           H  
ATOM   3702  HE3 MET A 250      -3.401  22.028 -17.406  1.00  0.00           H  
ATOM   3703  N   THR A 251      -6.831  16.109 -15.616  1.00165.97           N  
ANISOU 3703  N   THR A 251    21152  19863  22046   1014   3809  -2146
ATOM   3704  CA  THR A 251      -6.742  14.814 -16.301  1.00166.53           C  
ANISOU 3704  CA  THR A 251    21484  19614  22175   1191   4124  -2359
ATOM   3705  C   THR A 251      -7.391  14.754 -17.703  1.00165.85           C  
ANISOU 3705  C   THR A 251    21683  19542  21790    839   4436  -2591
ATOM   3706  O   THR A 251      -6.901  14.006 -18.549  1.00166.32           O  
ANISOU 3706  O   THR A 251    21789  19490  21913    955   4805  -2832
ATOM   3707  CB  THR A 251      -7.409  13.714 -15.426  1.00  0.00           C  
ATOM   3708  OG1 THR A 251      -6.796  13.705 -14.152  1.00  0.00           O  
ATOM   3709  CG2 THR A 251      -7.370  12.276 -15.978  1.00  0.00           C  
ATOM   3710  H   THR A 251      -7.188  16.051 -14.673  1.00  0.00           H  
ATOM   3711  HA  THR A 251      -5.681  14.583 -16.416  1.00  0.00           H  
ATOM   3712  HB  THR A 251      -8.454  13.983 -15.260  1.00  0.00           H  
ATOM   3713  HG1 THR A 251      -7.148  12.970 -13.644  1.00  0.00           H  
ATOM   3714 HG21 THR A 251      -7.749  11.564 -15.244  1.00  0.00           H  
ATOM   3715 HG22 THR A 251      -7.985  12.162 -16.870  1.00  0.00           H  
ATOM   3716 HG23 THR A 251      -6.352  11.979 -16.232  1.00  0.00           H  
ATOM   3717  N   SER A 252      -8.451  15.553 -17.943  1.00159.54           N  
ANISOU 3717  N   SER A 252    21064  18884  20669    414   4283  -2518
ATOM   3718  CA  SER A 252      -9.187  15.623 -19.214  1.00159.61           C  
ANISOU 3718  CA  SER A 252    21351  18940  20351     25   4483  -2682
ATOM   3719  C   SER A 252      -8.368  16.510 -20.134  1.00160.45           C  
ANISOU 3719  C   SER A 252    21208  19324  20430    -79   4735  -2816
ATOM   3720  O   SER A 252      -8.082  16.182 -21.284  1.00162.10           O  
ANISOU 3720  O   SER A 252    21466  19451  20672     -1   5109  -3056
ATOM   3721  CB  SER A 252     -10.592  16.219 -18.950  1.00  0.00           C  
ATOM   3722  OG  SER A 252     -11.430  16.128 -20.087  1.00  0.00           O  
ATOM   3723  H   SER A 252      -8.783  16.156 -17.203  1.00  0.00           H  
ATOM   3724  HA  SER A 252      -9.296  14.619 -19.631  1.00  0.00           H  
ATOM   3725  HXT SER A 252      -8.036  17.457 -19.704  1.00  0.00           H  
ATOM   3726  HB2 SER A 252     -11.083  15.678 -18.140  1.00  0.00           H  
ATOM   3727  HB3 SER A 252     -10.534  17.263 -18.633  1.00  0.00           H  
ATOM   3728  HG  SER A 252     -12.268  16.549 -19.884  1.00  0.00           H  
ATOM   3729  N   LYS A 257      -1.799  12.779 -12.549  1.00164.50           N  
ANISOU 3729  N   LYS A 257    19719  19076  23707   3403   3587  -1899
ATOM   3730  CA  LYS A 257      -0.528  13.390 -12.102  1.00167.64           C  
ANISOU 3730  CA  LYS A 257    19481  19801  24415   3647   3453  -1802
ATOM   3731  C   LYS A 257      -0.425  13.388 -10.552  1.00167.73           C  
ANISOU 3731  C   LYS A 257    19421  19789  24518   3794   2933  -1457
ATOM   3732  O   LYS A 257       0.695  13.482 -10.049  1.00170.87           O  
ANISOU 3732  O   LYS A 257    19335  20354  25234   4107   2764  -1344
ATOM   3733  CB  LYS A 257      -0.323  14.817 -12.670  1.00  0.00           C  
ATOM   3734  CG  LYS A 257      -0.201  14.904 -14.208  1.00  0.00           C  
ATOM   3735  CD  LYS A 257       1.025  14.206 -14.828  1.00  0.00           C  
ATOM   3736  CE  LYS A 257       2.370  14.815 -14.401  1.00  0.00           C  
ATOM   3737  NZ  LYS A 257       3.496  14.171 -15.098  1.00  0.00           N1+
ATOM   3738  H1  LYS A 257      -1.895  12.857 -13.552  1.00  0.00           H  
ATOM   3739  H2  LYS A 257      -1.806  11.788 -12.351  1.00  0.00           H  
ATOM   3740  HA  LYS A 257       0.297  12.768 -12.450  1.00  0.00           H  
ATOM   3741  HB2 LYS A 257      -1.171  15.437 -12.372  1.00  0.00           H  
ATOM   3742  HB3 LYS A 257       0.550  15.289 -12.216  1.00  0.00           H  
ATOM   3743  HG2 LYS A 257      -1.105  14.495 -14.660  1.00  0.00           H  
ATOM   3744  HG3 LYS A 257      -0.189  15.955 -14.497  1.00  0.00           H  
ATOM   3745  HD2 LYS A 257       1.007  13.142 -14.589  1.00  0.00           H  
ATOM   3746  HD3 LYS A 257       0.936  14.261 -15.914  1.00  0.00           H  
ATOM   3747  HE2 LYS A 257       2.388  15.883 -14.622  1.00  0.00           H  
ATOM   3748  HE3 LYS A 257       2.520  14.704 -13.326  1.00  0.00           H  
ATOM   3749  HZ1 LYS A 257       4.364  14.594 -14.800  1.00  0.00           H  
ATOM   3750  HZ2 LYS A 257       3.512  13.186 -14.877  1.00  0.00           H  
ATOM   3751  HZ3 LYS A 257       3.391  14.291 -16.095  1.00  0.00           H  
ATOM   3752  N   TYR A 258      -1.556  13.295  -9.824  1.00165.24           N  
ANISOU 3752  N   TYR A 258    19582  19284  23919   3552   2680  -1291
ATOM   3753  CA  TYR A 258      -1.625  13.248  -8.361  1.00165.23           C  
ANISOU 3753  CA  TYR A 258    19621  19240  23918   3605   2196   -966
ATOM   3754  C   TYR A 258      -2.651  12.201  -7.911  1.00164.76           C  
ANISOU 3754  C   TYR A 258    20184  18716  23703   3600   2079   -869
ATOM   3755  O   TYR A 258      -3.669  12.010  -8.577  1.00162.26           O  
ANISOU 3755  O   TYR A 258    20294  18240  23118   3318   2284  -1011
ATOM   3756  CB  TYR A 258      -2.003  14.636  -7.798  1.00160.65           C  
ANISOU 3756  CB  TYR A 258    18910  19048  23083   3176   1961   -834
ATOM   3757  CG  TYR A 258      -0.955  15.719  -7.982  1.00162.07           C  
ANISOU 3757  CG  TYR A 258    18476  19685  23419   3171   1949   -843
ATOM   3758  CD1 TYR A 258       0.321  15.560  -7.402  1.00166.40           C  
ANISOU 3758  CD1 TYR A 258    18584  20358  24282   3504   1700   -683
ATOM   3759  CD2 TYR A 258      -1.246  16.887  -8.719  1.00159.51           C  
ANISOU 3759  CD2 TYR A 258    18017  19673  22917   2810   2165   -998
ATOM   3760  CE1 TYR A 258       1.302  16.554  -7.570  1.00168.16           C  
ANISOU 3760  CE1 TYR A 258    18226  21025  24643   3463   1692   -697
ATOM   3761  CE2 TYR A 258      -0.270  17.893  -8.865  1.00160.95           C  
ANISOU 3761  CE2 TYR A 258    17661  20270  23221   2761   2163  -1007
ATOM   3762  CZ  TYR A 258       1.005  17.727  -8.288  1.00165.32           C  
ANISOU 3762  CZ  TYR A 258    17764  20962  24088   3075   1933   -863
ATOM   3763  OH  TYR A 258       1.954  18.699  -8.422  1.00167.20           O  
ANISOU 3763  OH  TYR A 258    17460  21633  24437   2986   1928   -874
ATOM   3764  H   TYR A 258      -2.438  13.213 -10.309  1.00  0.00           H  
ATOM   3765  HA  TYR A 258      -0.656  12.945  -7.959  1.00  0.00           H  
ATOM   3766  HB3 TYR A 258      -2.168  14.551  -6.723  1.00  0.00           H  
ATOM   3767  HB2 TYR A 258      -2.953  14.968  -8.220  1.00  0.00           H  
ATOM   3768  HD1 TYR A 258       0.556  14.672  -6.833  1.00  0.00           H  
ATOM   3769  HD2 TYR A 258      -2.221  17.021  -9.165  1.00  0.00           H  
ATOM   3770  HE1 TYR A 258       2.283  16.410  -7.148  1.00  0.00           H  
ATOM   3771  HE2 TYR A 258      -0.505  18.789  -9.420  1.00  0.00           H  
ATOM   3772  HH  TYR A 258       1.637  19.470  -8.898  1.00  0.00           H  
ATOM   3773  N   LYS A 259      -2.365  11.573  -6.759  1.00163.36           N  
ANISOU 3773  N   LYS A 259    20058  18338  23673   3879   1723   -612
ATOM   3774  CA  LYS A 259      -3.220  10.586  -6.102  1.00163.45           C  
ANISOU 3774  CA  LYS A 259    20660  17908  23535   3866   1555   -470
ATOM   3775  C   LYS A 259      -3.603  11.132  -4.723  1.00161.04           C  
ANISOU 3775  C   LYS A 259    20414  17754  23021   3616   1119   -179
ATOM   3776  O   LYS A 259      -2.737  11.215  -3.857  1.00163.34           O  
ANISOU 3776  O   LYS A 259    20359  18214  23490   3810    803     28
ATOM   3777  CB  LYS A 259      -2.458   9.250  -5.970  1.00  0.00           C  
ATOM   3778  CG  LYS A 259      -2.181   8.561  -7.316  1.00  0.00           C  
ATOM   3779  CD  LYS A 259      -1.472   7.208  -7.138  1.00  0.00           C  
ATOM   3780  CE  LYS A 259      -1.152   6.502  -8.463  1.00  0.00           C  
ATOM   3781  NZ  LYS A 259      -2.374   6.112  -9.189  1.00  0.00           N1+
ATOM   3782  H   LYS A 259      -1.514  11.805  -6.264  1.00  0.00           H  
ATOM   3783  HA  LYS A 259      -4.132  10.412  -6.677  1.00  0.00           H  
ATOM   3784  HB2 LYS A 259      -1.517   9.403  -5.439  1.00  0.00           H  
ATOM   3785  HB3 LYS A 259      -3.046   8.568  -5.355  1.00  0.00           H  
ATOM   3786  HG2 LYS A 259      -3.123   8.424  -7.847  1.00  0.00           H  
ATOM   3787  HG3 LYS A 259      -1.566   9.208  -7.941  1.00  0.00           H  
ATOM   3788  HD2 LYS A 259      -0.542   7.362  -6.588  1.00  0.00           H  
ATOM   3789  HD3 LYS A 259      -2.081   6.553  -6.513  1.00  0.00           H  
ATOM   3790  HE2 LYS A 259      -0.546   7.147  -9.101  1.00  0.00           H  
ATOM   3791  HE3 LYS A 259      -0.566   5.603  -8.271  1.00  0.00           H  
ATOM   3792  HZ1 LYS A 259      -2.122   5.647 -10.049  1.00  0.00           H  
ATOM   3793  HZ2 LYS A 259      -2.921   5.486  -8.617  1.00  0.00           H  
ATOM   3794  HZ3 LYS A 259      -2.918   6.937  -9.400  1.00  0.00           H  
ATOM   3795  N   SER A 260      -4.888  11.493  -4.558  1.00153.54           N  
ANISOU 3795  N   SER A 260    19875  16775  21688   3164   1112   -177
ATOM   3796  CA  SER A 260      -5.489  12.148  -3.385  1.00151.25           C  
ANISOU 3796  CA  SER A 260    19698  16633  21137   2844    777     42
ATOM   3797  C   SER A 260      -5.143  13.649  -3.308  1.00148.26           C  
ANISOU 3797  C   SER A 260    18834  16768  20730   2648    697     46
ATOM   3798  O   SER A 260      -4.065  14.071  -3.732  1.00149.25           O  
ANISOU 3798  O   SER A 260    18474  17121  21111   2866    742     -1
ATOM   3799  CB  SER A 260      -5.169  11.391  -2.069  1.00154.28           C  
ANISOU 3799  CB  SER A 260    20248  16774  21598   3073    386    342
ATOM   3800  OG  SER A 260      -5.907  11.899  -0.975  1.00152.32           O  
ANISOU 3800  OG  SER A 260    20152  16663  21061   2727     95    532
ATOM   3801  H   SER A 260      -5.517  11.370  -5.338  1.00  0.00           H  
ATOM   3802  HA  SER A 260      -6.566  12.077  -3.550  1.00  0.00           H  
ATOM   3803  HB3 SER A 260      -4.115  11.466  -1.805  1.00  0.00           H  
ATOM   3804  HB2 SER A 260      -5.400  10.330  -2.174  1.00  0.00           H  
ATOM   3805  HG  SER A 260      -5.720  11.359  -0.203  1.00  0.00           H  
ATOM   3806  N   SER A 261      -6.085  14.430  -2.752  1.00142.01           N  
ANISOU 3806  N   SER A 261    18182  16150  19627   2225    598     89
ATOM   3807  CA  SER A 261      -5.979  15.879  -2.570  1.00138.96           C  
ANISOU 3807  CA  SER A 261    17445  16192  19160   1980    530     85
ATOM   3808  C   SER A 261      -4.885  16.313  -1.578  1.00141.62           C  
ANISOU 3808  C   SER A 261    17436  16725  19649   2134    186    298
ATOM   3809  O   SER A 261      -4.363  17.415  -1.731  1.00140.85           O  
ANISOU 3809  O   SER A 261    16934  16981  19601   2047    174    267
ATOM   3810  CB  SER A 261      -7.370  16.446  -2.212  1.00138.17           C  
ANISOU 3810  CB  SER A 261    17627  16162  18707   1532    503     80
ATOM   3811  OG  SER A 261      -7.770  16.109  -0.898  1.00136.38           O  
ANISOU 3811  OG  SER A 261    17653  15840  18325   1431    203    292
ATOM   3812  H   SER A 261      -6.932  14.008  -2.399  1.00  0.00           H  
ATOM   3813  HA  SER A 261      -5.698  16.300  -3.536  1.00  0.00           H  
ATOM   3814  HB3 SER A 261      -8.123  16.097  -2.919  1.00  0.00           H  
ATOM   3815  HB2 SER A 261      -7.362  17.532  -2.284  1.00  0.00           H  
ATOM   3816  HG  SER A 261      -8.622  16.516  -0.722  1.00  0.00           H  
ATOM   3817  N   ILE A 262      -4.541  15.446  -0.610  1.00140.29           N  
ANISOU 3817  N   ILE A 262    17437  16328  19538   2340   -107    524
ATOM   3818  CA  ILE A 262      -3.501  15.692   0.389  1.00143.26           C  
ANISOU 3818  CA  ILE A 262    17510  16884  20036   2473   -491    760
ATOM   3819  C   ILE A 262      -2.085  15.592  -0.220  1.00146.50           C  
ANISOU 3819  C   ILE A 262    17373  17438  20851   2872   -429    710
ATOM   3820  O   ILE A 262      -1.236  16.410   0.132  1.00147.34           O  
ANISOU 3820  O   ILE A 262    17030  17910  21044   2835   -584    767
ATOM   3821  CB  ILE A 262      -3.623  14.733   1.615  1.00148.53           C  
ANISOU 3821  CB  ILE A 262    18559  17258  20618   2550   -849   1039
ATOM   3822  CG1 ILE A 262      -4.996  14.887   2.322  1.00145.43           C  
ANISOU 3822  CG1 ILE A 262    18679  16778  19802   2095   -863   1058
ATOM   3823  CG2 ILE A 262      -2.497  14.933   2.657  1.00152.60           C  
ANISOU 3823  CG2 ILE A 262    18753  17987  21242   2665  -1288   1301
ATOM   3824  CD1 ILE A 262      -6.106  13.977   1.773  1.00143.93           C  
ANISOU 3824  CD1 ILE A 262    19001  16200  19485   2044   -622    952
ATOM   3825  H   ILE A 262      -5.024  14.561  -0.545  1.00  0.00           H  
ATOM   3826  HA  ILE A 262      -3.625  16.715   0.752  1.00  0.00           H  
ATOM   3827  HB  ILE A 262      -3.541  13.705   1.256  1.00  0.00           H  
ATOM   3828 HG13 ILE A 262      -5.321  15.928   2.291  1.00  0.00           H  
ATOM   3829 HG12 ILE A 262      -4.897  14.653   3.382  1.00  0.00           H  
ATOM   3830 HG21 ILE A 262      -2.642  14.287   3.523  1.00  0.00           H  
ATOM   3831 HG22 ILE A 262      -1.512  14.687   2.261  1.00  0.00           H  
ATOM   3832 HG23 ILE A 262      -2.468  15.963   3.015  1.00  0.00           H  
ATOM   3833 HD11 ILE A 262      -6.955  13.955   2.456  1.00  0.00           H  
ATOM   3834 HD12 ILE A 262      -6.478  14.319   0.809  1.00  0.00           H  
ATOM   3835 HD13 ILE A 262      -5.757  12.951   1.657  1.00  0.00           H  
ATOM   3836  N   ASP A 263      -1.872  14.642  -1.151  1.00149.53           N  
ANISOU 3836  N   ASP A 263    17789  17556  21471   3218   -170    575
ATOM   3837  CA  ASP A 263      -0.635  14.517  -1.931  1.00153.07           C  
ANISOU 3837  CA  ASP A 263    17700  18142  22317   3604    -42    481
ATOM   3838  C   ASP A 263      -0.487  15.697  -2.907  1.00150.01           C  
ANISOU 3838  C   ASP A 263    16962  18139  21897   3361    270    239
ATOM   3839  O   ASP A 263       0.593  16.274  -2.971  1.00152.06           O  
ANISOU 3839  O   ASP A 263    16668  18718  22389   3489    257    223
ATOM   3840  CB  ASP A 263      -0.559  13.175  -2.694  1.00159.29           C  
ANISOU 3840  CB  ASP A 263    18649  18514  23359   4036    191    371
ATOM   3841  CG  ASP A 263       0.785  12.879  -3.379  1.00162.64           C  
ANISOU 3841  CG  ASP A 263    18507  19066  24222   4469    377    238
ATOM   3842  OD1 ASP A 263       1.827  13.327  -2.853  1.00164.15           O  
ANISOU 3842  OD1 ASP A 263    18143  19636  24592   4541    179    336
ATOM   3843  OD2 ASP A 263       0.748  12.144  -4.390  1.00164.38           O1-
ANISOU 3843  OD2 ASP A 263    18840  19012  24606   4724    728     29
ATOM   3844  H   ASP A 263      -2.620  14.011  -1.402  1.00  0.00           H  
ATOM   3845  HA  ASP A 263       0.196  14.559  -1.223  1.00  0.00           H  
ATOM   3846  HB3 ASP A 263      -1.318  13.206  -3.475  1.00  0.00           H  
ATOM   3847  HB2 ASP A 263      -0.802  12.345  -2.029  1.00  0.00           H  
ATOM   3848  N   ALA A 264      -1.580  16.063  -3.605  1.00142.52           N  
ANISOU 3848  N   ALA A 264    16327  17170  20655   2996    534     64
ATOM   3849  CA  ALA A 264      -1.640  17.223  -4.497  1.00139.58           C  
ANISOU 3849  CA  ALA A 264    15699  17132  20203   2723    799   -137
ATOM   3850  C   ALA A 264      -1.308  18.544  -3.780  1.00138.33           C  
ANISOU 3850  C   ALA A 264    15243  17363  19952   2462    529     -3
ATOM   3851  O   ALA A 264      -0.537  19.332  -4.319  1.00139.39           O  
ANISOU 3851  O   ALA A 264    14929  17826  20205   2425    616    -81
ATOM   3852  CB  ALA A 264      -3.021  17.292  -5.165  1.00136.05           C  
ANISOU 3852  CB  ALA A 264    15683  16557  19451   2394   1055   -302
ATOM   3853  H   ALA A 264      -2.434  15.530  -3.505  1.00  0.00           H  
ATOM   3854  HA  ALA A 264      -0.892  17.074  -5.277  1.00  0.00           H  
ATOM   3855  HB1 ALA A 264      -3.067  18.099  -5.897  1.00  0.00           H  
ATOM   3856  HB2 ALA A 264      -3.258  16.365  -5.686  1.00  0.00           H  
ATOM   3857  HB3 ALA A 264      -3.810  17.464  -4.434  1.00  0.00           H  
ATOM   3858  N   PHE A 265      -1.836  18.718  -2.556  1.00135.21           N  
ANISOU 3858  N   PHE A 265    15107  16921  19347   2280    203    196
ATOM   3859  CA  PHE A 265      -1.555  19.847  -1.671  1.00134.08           C  
ANISOU 3859  CA  PHE A 265    14771  17094  19080   2013    -72    326
ATOM   3860  C   PHE A 265      -0.072  19.901  -1.256  1.00138.54           C  
ANISOU 3860  C   PHE A 265    14804  17900  19935   2259   -301    455
ATOM   3861  O   PHE A 265       0.565  20.927  -1.485  1.00138.53           O  
ANISOU 3861  O   PHE A 265    14405  18253  19979   2111   -266    396
ATOM   3862  CB  PHE A 265      -2.514  19.793  -0.460  1.00136.33           C  
ANISOU 3862  CB  PHE A 265    15490  17222  19089   1813   -352    504
ATOM   3863  CG  PHE A 265      -2.465  20.977   0.491  1.00136.35           C  
ANISOU 3863  CG  PHE A 265    15410  17506  18891   1469   -588    599
ATOM   3864  CD1 PHE A 265      -3.297  22.094   0.262  1.00135.28           C  
ANISOU 3864  CD1 PHE A 265    15461  17453  18487   1082   -448    477
ATOM   3865  CD2 PHE A 265      -1.499  21.043   1.518  1.00137.11           C  
ANISOU 3865  CD2 PHE A 265    15255  17775  19067   1530   -962    811
ATOM   3866  CE1 PHE A 265      -3.208  23.209   1.083  1.00134.93           C  
ANISOU 3866  CE1 PHE A 265    15374  17633  18259    769   -643    543
ATOM   3867  CE2 PHE A 265      -1.416  22.174   2.320  1.00136.69           C  
ANISOU 3867  CE2 PHE A 265    15160  17972  18802   1177  -1170    882
ATOM   3868  CZ  PHE A 265      -2.272  23.248   2.108  1.00135.66           C  
ANISOU 3868  CZ  PHE A 265    15243  17894  18408    802   -994    738
ATOM   3869  H   PHE A 265      -2.469  18.019  -2.191  1.00  0.00           H  
ATOM   3870  HA  PHE A 265      -1.778  20.758  -2.230  1.00  0.00           H  
ATOM   3871  HB3 PHE A 265      -2.344  18.881   0.113  1.00  0.00           H  
ATOM   3872  HB2 PHE A 265      -3.539  19.723  -0.825  1.00  0.00           H  
ATOM   3873  HD1 PHE A 265      -4.014  22.086  -0.544  1.00  0.00           H  
ATOM   3874  HD2 PHE A 265      -0.822  20.218   1.684  1.00  0.00           H  
ATOM   3875  HE1 PHE A 265      -3.856  24.056   0.913  1.00  0.00           H  
ATOM   3876  HE2 PHE A 265      -0.681  22.220   3.110  1.00  0.00           H  
ATOM   3877  HZ  PHE A 265      -2.200  24.124   2.736  1.00  0.00           H  
ATOM   3878  N   ARG A 266       0.448  18.794  -0.691  1.00140.98           N  
ANISOU 3878  N   ARG A 266    15106  18013  20447   2632   -538    634
ATOM   3879  CA  ARG A 266       1.833  18.656  -0.224  1.00145.81           C  
ANISOU 3879  CA  ARG A 266    15199  18836  21368   2919   -811    789
ATOM   3880  C   ARG A 266       2.893  18.796  -1.328  1.00148.32           C  
ANISOU 3880  C   ARG A 266    14960  19385  22010   3129   -507    588
ATOM   3881  O   ARG A 266       3.937  19.390  -1.065  1.00150.25           O  
ANISOU 3881  O   ARG A 266    14684  20008  22395   3102   -647    637
ATOM   3882  CB  ARG A 266       2.016  17.318   0.518  1.00157.93           C  
ANISOU 3882  CB  ARG A 266    16891  20040  23077   3331  -1102   1016
ATOM   3883  CG  ARG A 266       1.579  17.383   1.988  1.00156.29           C  
ANISOU 3883  CG  ARG A 266    17070  19737  22578   3112  -1532   1290
ATOM   3884  CD  ARG A 266       1.839  16.063   2.727  1.00161.57           C  
ANISOU 3884  CD  ARG A 266    17887  20083  23419   3516  -1862   1549
ATOM   3885  NE  ARG A 266       1.862  16.253   4.184  1.00160.75           N  
ANISOU 3885  NE  ARG A 266    17930  20051  23096   3317  -2369   1857
ATOM   3886  CZ  ARG A 266       2.938  16.645   4.890  1.00165.25           C  
ANISOU 3886  CZ  ARG A 266    18063  20915  23809   3400  -2768   2066
ATOM   3887  NH1 ARG A 266       4.121  16.867   4.296  1.00170.93           N  
ANISOU 3887  NH1 ARG A 266    18125  21898  24921   3697  -2713   1999
ATOM   3888  NH2 ARG A 266       2.831  16.818   6.213  1.00164.36           N1+
ANISOU 3888  NH2 ARG A 266    18163  20848  23438   3166  -3221   2339
ATOM   3889  H   ARG A 266      -0.143  17.984  -0.559  1.00  0.00           H  
ATOM   3890  HA  ARG A 266       1.999  19.461   0.493  1.00  0.00           H  
ATOM   3891  HB3 ARG A 266       3.076  17.055   0.523  1.00  0.00           H  
ATOM   3892  HB2 ARG A 266       1.515  16.506  -0.012  1.00  0.00           H  
ATOM   3893  HG3 ARG A 266       0.506  17.581   1.993  1.00  0.00           H  
ATOM   3894  HG2 ARG A 266       2.048  18.217   2.513  1.00  0.00           H  
ATOM   3895  HD3 ARG A 266       2.677  15.483   2.338  1.00  0.00           H  
ATOM   3896  HD2 ARG A 266       0.954  15.444   2.574  1.00  0.00           H  
ATOM   3897  HE  ARG A 266       0.980  16.134   4.662  1.00  0.00           H  
ATOM   3898 HH12 ARG A 266       4.923  17.159   4.834  1.00  0.00           H  
ATOM   3899 HH11 ARG A 266       4.213  16.739   3.298  1.00  0.00           H  
ATOM   3900 HH22 ARG A 266       3.629  17.110   6.758  1.00  0.00           H  
ATOM   3901 HH21 ARG A 266       1.951  16.652   6.680  1.00  0.00           H  
ATOM   3902  N   GLN A 267       2.620  18.261  -2.526  1.00144.26           N  
ANISOU 3902  N   GLN A 267    14558  18656  21598   3306    -84    355
ATOM   3903  CA  GLN A 267       3.529  18.335  -3.667  1.00147.05           C  
ANISOU 3903  CA  GLN A 267    14424  19206  22241   3496    265    131
ATOM   3904  C   GLN A 267       3.555  19.721  -4.324  1.00143.81           C  
ANISOU 3904  C   GLN A 267    13812  19177  21651   3055    478    -31
ATOM   3905  O   GLN A 267       4.625  20.127  -4.772  1.00146.57           O  
ANISOU 3905  O   GLN A 267    13625  19849  22218   3113    614   -131
ATOM   3906  CB  GLN A 267       3.178  17.246  -4.697  1.00  0.00           C  
ATOM   3907  CG  GLN A 267       3.430  15.797  -4.227  1.00  0.00           C  
ATOM   3908  CD  GLN A 267       4.886  15.334  -4.324  1.00  0.00           C  
ATOM   3909  OE1 GLN A 267       5.820  16.093  -4.071  1.00  0.00           O  
ATOM   3910  NE2 GLN A 267       5.085  14.059  -4.662  1.00  0.00           N  
ATOM   3911  H   GLN A 267       1.756  17.752  -2.670  1.00  0.00           H  
ATOM   3912  HA  GLN A 267       4.539  18.148  -3.300  1.00  0.00           H  
ATOM   3913  HB2 GLN A 267       2.122  17.349  -4.950  1.00  0.00           H  
ATOM   3914  HB3 GLN A 267       3.721  17.420  -5.627  1.00  0.00           H  
ATOM   3915  HG2 GLN A 267       3.101  15.661  -3.198  1.00  0.00           H  
ATOM   3916  HG3 GLN A 267       2.816  15.129  -4.833  1.00  0.00           H  
ATOM   3917 HE22 GLN A 267       6.022  13.691  -4.727  1.00  0.00           H  
ATOM   3918 HE21 GLN A 267       4.296  13.448  -4.822  1.00  0.00           H  
ATOM   3919  N   ILE A 268       2.415  20.435  -4.348  1.00137.18           N  
ANISOU 3919  N   ILE A 268    13388  18306  20429   2620    505    -55
ATOM   3920  CA  ILE A 268       2.338  21.799  -4.878  1.00134.39           C  
ANISOU 3920  CA  ILE A 268    12901  18269  19893   2199    677   -186
ATOM   3921  C   ILE A 268       2.977  22.827  -3.922  1.00135.08           C  
ANISOU 3921  C   ILE A 268    12666  18707  19951   1987    328    -14
ATOM   3922  O   ILE A 268       3.735  23.665  -4.402  1.00136.00           O  
ANISOU 3922  O   ILE A 268    12380  19169  20125   1822    439   -100
ATOM   3923  CB  ILE A 268       0.889  22.226  -5.261  1.00131.26           C  
ANISOU 3923  CB  ILE A 268    13041  17700  19132   1846    834   -279
ATOM   3924  CG1 ILE A 268       0.380  21.401  -6.468  1.00131.21           C  
ANISOU 3924  CG1 ILE A 268    13265  17446  19145   1975   1236   -497
ATOM   3925  CG2 ILE A 268       0.727  23.730  -5.581  1.00128.52           C  
ANISOU 3925  CG2 ILE A 268    12605  17652  18575   1398    885   -338
ATOM   3926  CD1 ILE A 268      -1.146  21.447  -6.651  1.00126.31           C  
ANISOU 3926  CD1 ILE A 268    13182  16615  18194   1690   1337   -559
ATOM   3927  H   ILE A 268       1.561  20.044  -3.973  1.00  0.00           H  
ATOM   3928  HA  ILE A 268       2.924  21.824  -5.800  1.00  0.00           H  
ATOM   3929  HB  ILE A 268       0.246  22.001  -4.408  1.00  0.00           H  
ATOM   3930 HG13 ILE A 268       0.680  20.358  -6.373  1.00  0.00           H  
ATOM   3931 HG12 ILE A 268       0.866  21.754  -7.378  1.00  0.00           H  
ATOM   3932 HG21 ILE A 268      -0.266  23.952  -5.968  1.00  0.00           H  
ATOM   3933 HG22 ILE A 268       0.870  24.359  -4.702  1.00  0.00           H  
ATOM   3934 HG23 ILE A 268       1.443  24.047  -6.339  1.00  0.00           H  
ATOM   3935 HD11 ILE A 268      -1.516  20.502  -7.051  1.00  0.00           H  
ATOM   3936 HD12 ILE A 268      -1.665  21.622  -5.708  1.00  0.00           H  
ATOM   3937 HD13 ILE A 268      -1.437  22.240  -7.340  1.00  0.00           H  
ATOM   3938  N   ILE A 269       2.727  22.730  -2.602  1.00134.96           N  
ANISOU 3938  N   ILE A 269    12846  18608  19825   1958    -83    223
ATOM   3939  CA  ILE A 269       3.365  23.616  -1.614  1.00135.75           C  
ANISOU 3939  CA  ILE A 269    12698  19025  19856   1720   -437    389
ATOM   3940  C   ILE A 269       4.878  23.372  -1.439  1.00141.41           C  
ANISOU 3940  C   ILE A 269    12762  20031  20937   1994   -571    457
ATOM   3941  O   ILE A 269       5.577  24.302  -1.041  1.00142.68           O  
ANISOU 3941  O   ILE A 269    12562  20564  21085   1749   -710    496
ATOM   3942  CB  ILE A 269       2.686  23.601  -0.212  1.00137.19           C  
ANISOU 3942  CB  ILE A 269    13277  19051  19797   1592   -838    619
ATOM   3943  CG1 ILE A 269       2.749  22.253   0.541  1.00140.63           C  
ANISOU 3943  CG1 ILE A 269    13796  19231  20407   2006  -1099    816
ATOM   3944  CG2 ILE A 269       1.241  24.106  -0.323  1.00131.86           C  
ANISOU 3944  CG2 ILE A 269    13172  18155  18775   1290   -694    534
ATOM   3945  CD1 ILE A 269       3.904  22.117   1.546  1.00145.66           C  
ANISOU 3945  CD1 ILE A 269    14033  20093  21216   2147  -1559   1069
ATOM   3946  H   ILE A 269       2.094  22.026  -2.246  1.00  0.00           H  
ATOM   3947  HA  ILE A 269       3.264  24.630  -1.999  1.00  0.00           H  
ATOM   3948  HB  ILE A 269       3.200  24.342   0.403  1.00  0.00           H  
ATOM   3949 HG13 ILE A 269       2.806  21.451  -0.185  1.00  0.00           H  
ATOM   3950 HG12 ILE A 269       1.818  22.084   1.083  1.00  0.00           H  
ATOM   3951 HG21 ILE A 269       0.788  24.238   0.660  1.00  0.00           H  
ATOM   3952 HG22 ILE A 269       1.220  25.070  -0.828  1.00  0.00           H  
ATOM   3953 HG23 ILE A 269       0.609  23.426  -0.891  1.00  0.00           H  
ATOM   3954 HD11 ILE A 269       3.740  21.262   2.201  1.00  0.00           H  
ATOM   3955 HD12 ILE A 269       4.859  21.962   1.046  1.00  0.00           H  
ATOM   3956 HD13 ILE A 269       3.992  23.002   2.176  1.00  0.00           H  
ATOM   3957  N   ALA A 270       5.359  22.159  -1.765  1.00149.34           N  
ANISOU 3957  N   ALA A 270    13614  20858  22270   2500   -534    470
ATOM   3958  CA  ALA A 270       6.778  21.809  -1.729  1.00155.43           C  
ANISOU 3958  CA  ALA A 270    13731  21884  23441   2837   -665    536
ATOM   3959  C   ALA A 270       7.524  22.206  -3.013  1.00157.34           C  
ANISOU 3959  C   ALA A 270    13494  22390  23898   2870   -219    265
ATOM   3960  O   ALA A 270       8.641  22.711  -2.909  1.00161.27           O  
ANISOU 3960  O   ALA A 270    13386  23295  24595   2857   -311    286
ATOM   3961  CB  ALA A 270       6.929  20.305  -1.457  1.00159.74           C  
ANISOU 3961  CB  ALA A 270    14330  22098  24267   3395   -834    676
ATOM   3962  H   ALA A 270       4.724  21.433  -2.066  1.00  0.00           H  
ATOM   3963  HA  ALA A 270       7.250  22.334  -0.896  1.00  0.00           H  
ATOM   3964  HB1 ALA A 270       7.979  20.009  -1.437  1.00  0.00           H  
ATOM   3965  HB2 ALA A 270       6.501  20.039  -0.490  1.00  0.00           H  
ATOM   3966  HB3 ALA A 270       6.431  19.706  -2.221  1.00  0.00           H  
ATOM   3967  N   LYS A 271       6.916  21.964  -4.190  1.00156.69           N  
ANISOU 3967  N   LYS A 271    13677  22100  23758   2875    257     10
ATOM   3968  CA  LYS A 271       7.557  22.171  -5.494  1.00158.68           C  
ANISOU 3968  CA  LYS A 271    13539  22574  24176   2885    724   -267
ATOM   3969  C   LYS A 271       7.398  23.605  -6.035  1.00155.24           C  
ANISOU 3969  C   LYS A 271    13136  22411  23436   2315    926   -399
ATOM   3970  O   LYS A 271       8.274  24.047  -6.777  1.00157.25           O  
ANISOU 3970  O   LYS A 271    12988  22953  23805   2235   1242   -587
ATOM   3971  CB  LYS A 271       7.021  21.124  -6.497  1.00  0.00           C  
ATOM   3972  CG  LYS A 271       7.798  21.058  -7.829  1.00  0.00           C  
ATOM   3973  CD  LYS A 271       7.338  19.928  -8.769  1.00  0.00           C  
ATOM   3974  CE  LYS A 271       5.913  20.091  -9.326  1.00  0.00           C  
ATOM   3975  NZ  LYS A 271       5.773  21.315 -10.136  1.00  0.00           N1+
ATOM   3976  H   LYS A 271       6.001  21.534  -4.205  1.00  0.00           H  
ATOM   3977  HA  LYS A 271       8.628  21.989  -5.382  1.00  0.00           H  
ATOM   3978  HB2 LYS A 271       7.077  20.138  -6.033  1.00  0.00           H  
ATOM   3979  HB3 LYS A 271       5.965  21.314  -6.690  1.00  0.00           H  
ATOM   3980  HG2 LYS A 271       7.732  22.009  -8.357  1.00  0.00           H  
ATOM   3981  HG3 LYS A 271       8.857  20.916  -7.610  1.00  0.00           H  
ATOM   3982  HD2 LYS A 271       8.042  19.846  -9.598  1.00  0.00           H  
ATOM   3983  HD3 LYS A 271       7.401  18.977  -8.238  1.00  0.00           H  
ATOM   3984  HE2 LYS A 271       5.661  19.234  -9.951  1.00  0.00           H  
ATOM   3985  HE3 LYS A 271       5.181  20.113  -8.517  1.00  0.00           H  
ATOM   3986  HZ1 LYS A 271       4.824  21.393 -10.474  1.00  0.00           H  
ATOM   3987  HZ2 LYS A 271       5.985  22.121  -9.566  1.00  0.00           H  
ATOM   3988  HZ3 LYS A 271       6.410  21.281 -10.919  1.00  0.00           H  
ATOM   3989  N   GLU A 272       6.300  24.295  -5.680  1.00156.67           N  
ANISOU 3989  N   GLU A 272    13795  22495  23236   1925    761   -309
ATOM   3990  CA  GLU A 272       5.971  25.636  -6.178  1.00153.45           C  
ANISOU 3990  CA  GLU A 272    13475  22287  22541   1404    924   -415
ATOM   3991  C   GLU A 272       5.919  26.690  -5.055  1.00151.90           C  
ANISOU 3991  C   GLU A 272    13282  22289  22143   1039    534   -228
ATOM   3992  O   GLU A 272       6.165  27.861  -5.345  1.00152.37           O  
ANISOU 3992  O   GLU A 272    13107  22665  22122    684    587   -278
ATOM   3993  CB  GLU A 272       4.619  25.603  -6.921  1.00151.52           C  
ANISOU 3993  CB  GLU A 272    13834  21729  22008   1235   1175   -539
ATOM   3994  CG  GLU A 272       4.530  24.628  -8.111  1.00150.99           C  
ANISOU 3994  CG  GLU A 272    13829  21494  22045   1451   1619   -768
ATOM   3995  CD  GLU A 272       3.145  24.596  -8.771  1.00150.61           C  
ANISOU 3995  CD  GLU A 272    14356  21188  21683   1219   1832   -877
ATOM   3996  OE1 GLU A 272       2.353  25.543  -8.565  1.00149.44           O  
ANISOU 3996  OE1 GLU A 272    14451  21082  21248    830   1730   -827
ATOM   3997  OE2 GLU A 272       2.887  23.595  -9.473  1.00150.37           O1-
ANISOU 3997  OE2 GLU A 272    14532  20906  21696   1428   2098  -1017
ATOM   3998  H   GLU A 272       5.610  23.866  -5.078  1.00  0.00           H  
ATOM   3999  HA  GLU A 272       6.727  25.975  -6.889  1.00  0.00           H  
ATOM   4000  HB3 GLU A 272       4.402  26.609  -7.283  1.00  0.00           H  
ATOM   4001  HB2 GLU A 272       3.834  25.355  -6.212  1.00  0.00           H  
ATOM   4002  HG3 GLU A 272       4.766  23.615  -7.783  1.00  0.00           H  
ATOM   4003  HG2 GLU A 272       5.269  24.896  -8.866  1.00  0.00           H  
ATOM   4004  N   GLY A 273       5.609  26.277  -3.814  1.00148.60           N  
ANISOU 4004  N   GLY A 273    13163  21675  21624   1097    166    -25
ATOM   4005  CA  GLY A 273       5.470  27.168  -2.659  1.00147.48           C  
ANISOU 4005  CA  GLY A 273    13101  21676  21259    747   -198    141
ATOM   4006  C   GLY A 273       3.989  27.369  -2.309  1.00142.23           C  
ANISOU 4006  C   GLY A 273    13082  20703  20257    544   -262    175
ATOM   4007  O   GLY A 273       3.095  27.019  -3.079  1.00139.04           O  
ANISOU 4007  O   GLY A 273    13035  20028  19767    596      4     52
ATOM   4008  H   GLY A 273       5.405  25.301  -3.658  1.00  0.00           H  
ATOM   4009  HA3 GLY A 273       5.930  28.141  -2.835  1.00  0.00           H  
ATOM   4010  HA2 GLY A 273       5.992  26.729  -1.809  1.00  0.00           H  
ATOM   4011  N   VAL A 274       3.734  27.953  -1.126  1.00135.38           N  
ANISOU 4011  N   VAL A 274    12363  19887  19188    294   -603    330
ATOM   4012  CA  VAL A 274       2.390  28.263  -0.621  1.00130.92           C  
ANISOU 4012  CA  VAL A 274    12379  19055  18309     90   -646    344
ATOM   4013  C   VAL A 274       1.685  29.367  -1.440  1.00127.24           C  
ANISOU 4013  C   VAL A 274    12109  18590  17647   -246   -359    167
ATOM   4014  O   VAL A 274       0.469  29.292  -1.613  1.00123.84           O  
ANISOU 4014  O   VAL A 274    12117  17907  17032   -322   -239    104
ATOM   4015  CB  VAL A 274       2.433  28.676   0.882  1.00134.58           C  
ANISOU 4015  CB  VAL A 274    12959  19589  18587   -129  -1056    530
ATOM   4016  CG1 VAL A 274       1.094  29.184   1.462  1.00130.48           C  
ANISOU 4016  CG1 VAL A 274    13018  18813  17746   -359  -1038    503
ATOM   4017  CG2 VAL A 274       2.952  27.518   1.755  1.00138.96           C  
ANISOU 4017  CG2 VAL A 274    13367  20121  19311    196  -1390    743
ATOM   4018  H   VAL A 274       4.503  28.204  -0.522  1.00  0.00           H  
ATOM   4019  HA  VAL A 274       1.785  27.359  -0.708  1.00  0.00           H  
ATOM   4020  HB  VAL A 274       3.150  29.493   0.986  1.00  0.00           H  
ATOM   4021 HG11 VAL A 274       1.163  29.336   2.539  1.00  0.00           H  
ATOM   4022 HG12 VAL A 274       0.799  30.142   1.034  1.00  0.00           H  
ATOM   4023 HG13 VAL A 274       0.290  28.470   1.281  1.00  0.00           H  
ATOM   4024 HG21 VAL A 274       3.003  27.805   2.805  1.00  0.00           H  
ATOM   4025 HG22 VAL A 274       2.300  26.647   1.681  1.00  0.00           H  
ATOM   4026 HG23 VAL A 274       3.954  27.206   1.461  1.00  0.00           H  
ATOM   4027  N   LYS A 275       2.466  30.327  -1.968  1.00128.46           N  
ANISOU 4027  N   LYS A 275    11925  19036  17849   -449   -259     94
ATOM   4028  CA  LYS A 275       2.014  31.437  -2.814  1.00126.30           C  
ANISOU 4028  CA  LYS A 275    11815  18777  17397   -783    -12    -51
ATOM   4029  C   LYS A 275       1.335  30.999  -4.125  1.00124.61           C  
ANISOU 4029  C   LYS A 275    11788  18361  17198   -645    349   -207
ATOM   4030  O   LYS A 275       0.440  31.705  -4.592  1.00121.56           O  
ANISOU 4030  O   LYS A 275    11752  17824  16612   -846    485   -283
ATOM   4031  CB  LYS A 275       3.212  32.356  -3.134  1.00  0.00           C  
ATOM   4032  CG  LYS A 275       3.806  33.068  -1.907  1.00  0.00           C  
ATOM   4033  CD  LYS A 275       4.964  34.007  -2.283  1.00  0.00           C  
ATOM   4034  CE  LYS A 275       5.558  34.730  -1.067  1.00  0.00           C  
ATOM   4035  NZ  LYS A 275       6.664  35.620  -1.460  1.00  0.00           N1+
ATOM   4036  H   LYS A 275       3.459  30.292  -1.791  1.00  0.00           H  
ATOM   4037  HA  LYS A 275       1.279  32.006  -2.240  1.00  0.00           H  
ATOM   4038  HB2 LYS A 275       3.992  31.782  -3.637  1.00  0.00           H  
ATOM   4039  HB3 LYS A 275       2.895  33.121  -3.845  1.00  0.00           H  
ATOM   4040  HG2 LYS A 275       3.023  33.638  -1.404  1.00  0.00           H  
ATOM   4041  HG3 LYS A 275       4.161  32.331  -1.185  1.00  0.00           H  
ATOM   4042  HD2 LYS A 275       5.744  33.433  -2.784  1.00  0.00           H  
ATOM   4043  HD3 LYS A 275       4.611  34.742  -3.008  1.00  0.00           H  
ATOM   4044  HE2 LYS A 275       4.792  35.324  -0.567  1.00  0.00           H  
ATOM   4045  HE3 LYS A 275       5.931  34.007  -0.340  1.00  0.00           H  
ATOM   4046  HZ1 LYS A 275       7.034  36.082  -0.641  1.00  0.00           H  
ATOM   4047  HZ2 LYS A 275       7.396  35.078  -1.898  1.00  0.00           H  
ATOM   4048  HZ3 LYS A 275       6.325  36.314  -2.112  1.00  0.00           H  
ATOM   4049  N   SER A 276       1.758  29.850  -4.686  1.00129.69           N  
ANISOU 4049  N   SER A 276    12199  18995  18081   -298    496   -252
ATOM   4050  CA  SER A 276       1.230  29.296  -5.934  1.00128.53           C  
ANISOU 4050  CA  SER A 276    12212  18673  17949   -173    850   -413
ATOM   4051  C   SER A 276      -0.232  28.820  -5.837  1.00124.98           C  
ANISOU 4051  C   SER A 276    12293  17876  17319   -148    857   -414
ATOM   4052  O   SER A 276      -0.935  28.882  -6.845  1.00123.11           O  
ANISOU 4052  O   SER A 276    12300  17523  16954   -260   1095   -534
ATOM   4053  CB  SER A 276       2.166  28.183  -6.441  1.00137.92           C  
ANISOU 4053  CB  SER A 276    13074  19884  19447    231    990   -466
ATOM   4054  OG  SER A 276       1.927  26.947  -5.799  1.00139.51           O  
ANISOU 4054  OG  SER A 276    13328  19910  19769    555    740   -323
ATOM   4055  H   SER A 276       2.476  29.304  -4.231  1.00  0.00           H  
ATOM   4056  HA  SER A 276       1.262  30.103  -6.669  1.00  0.00           H  
ATOM   4057  HB3 SER A 276       3.211  28.464  -6.311  1.00  0.00           H  
ATOM   4058  HB2 SER A 276       2.014  28.036  -7.511  1.00  0.00           H  
ATOM   4059  HG  SER A 276       2.292  26.249  -6.353  1.00  0.00           H  
ATOM   4060  N   LEU A 277      -0.663  28.386  -4.635  1.00123.10           N  
ANISOU 4060  N   LEU A 277    12231  17484  17057    -25    592   -276
ATOM   4061  CA  LEU A 277      -2.047  28.002  -4.342  1.00120.21           C  
ANISOU 4061  CA  LEU A 277    12340  16811  16522    -19    602   -280
ATOM   4062  C   LEU A 277      -3.021  29.176  -4.503  1.00116.94           C  
ANISOU 4062  C   LEU A 277    12201  16374  15857   -367    648   -333
ATOM   4063  O   LEU A 277      -4.126  28.967  -4.991  1.00114.96           O  
ANISOU 4063  O   LEU A 277    12241  15943  15495   -400    810   -418
ATOM   4064  CB  LEU A 277      -2.184  27.438  -2.911  1.00118.72           C  
ANISOU 4064  CB  LEU A 277    12296  16500  16313     96    291   -109
ATOM   4065  CG  LEU A 277      -1.413  26.138  -2.611  1.00122.14           C  
ANISOU 4065  CG  LEU A 277    12531  16887  16989    475    168     -7
ATOM   4066  CD1 LEU A 277      -1.571  25.777  -1.122  1.00122.28           C  
ANISOU 4066  CD1 LEU A 277    12746  16799  16915    493   -185    190
ATOM   4067  CD2 LEU A 277      -1.874  24.973  -3.505  1.00122.10           C  
ANISOU 4067  CD2 LEU A 277    12662  16636  17095    749    431   -118
ATOM   4068  H   LEU A 277      -0.017  28.356  -3.858  1.00  0.00           H  
ATOM   4069  HA  LEU A 277      -2.339  27.233  -5.052  1.00  0.00           H  
ATOM   4070  HB3 LEU A 277      -3.241  27.258  -2.705  1.00  0.00           H  
ATOM   4071  HB2 LEU A 277      -1.878  28.204  -2.196  1.00  0.00           H  
ATOM   4072  HG  LEU A 277      -0.351  26.302  -2.801  1.00  0.00           H  
ATOM   4073 HD11 LEU A 277      -1.618  24.700  -0.960  1.00  0.00           H  
ATOM   4074 HD12 LEU A 277      -0.738  26.167  -0.539  1.00  0.00           H  
ATOM   4075 HD13 LEU A 277      -2.478  26.204  -0.693  1.00  0.00           H  
ATOM   4076 HD21 LEU A 277      -1.437  24.025  -3.189  1.00  0.00           H  
ATOM   4077 HD22 LEU A 277      -2.959  24.862  -3.484  1.00  0.00           H  
ATOM   4078 HD23 LEU A 277      -1.582  25.134  -4.541  1.00  0.00           H  
ATOM   4079  N   PHE A 278      -2.584  30.380  -4.102  1.00119.73           N  
ANISOU 4079  N   PHE A 278    12461  16904  16126   -623    494   -282
ATOM   4080  CA  PHE A 278      -3.376  31.607  -4.151  1.00117.06           C  
ANISOU 4080  CA  PHE A 278    12379  16525  15575   -933    521   -328
ATOM   4081  C   PHE A 278      -3.350  32.315  -5.519  1.00117.44           C  
ANISOU 4081  C   PHE A 278    12413  16625  15586  -1092    772   -447
ATOM   4082  O   PHE A 278      -4.112  33.265  -5.688  1.00117.37           O  
ANISOU 4082  O   PHE A 278    12664  16513  15417  -1286    811   -484
ATOM   4083  CB  PHE A 278      -2.909  32.556  -3.029  1.00119.12           C  
ANISOU 4083  CB  PHE A 278    12599  16919  15741  -1170    275   -243
ATOM   4084  CG  PHE A 278      -3.156  32.032  -1.625  1.00120.94           C  
ANISOU 4084  CG  PHE A 278    12951  17075  15927  -1093     17   -123
ATOM   4085  CD1 PHE A 278      -4.436  32.134  -1.040  1.00121.81           C  
ANISOU 4085  CD1 PHE A 278    13441  16988  15854  -1185    -24   -132
ATOM   4086  CD2 PHE A 278      -2.154  31.296  -0.958  1.00122.02           C  
ANISOU 4086  CD2 PHE A 278    12817  17343  16203   -932   -186      0
ATOM   4087  CE1 PHE A 278      -4.672  31.577   0.211  1.00123.66           C  
ANISOU 4087  CE1 PHE A 278    13818  17158  16011  -1156   -243    -26
ATOM   4088  CE2 PHE A 278      -2.413  30.736   0.285  1.00123.98           C  
ANISOU 4088  CE2 PHE A 278    13215  17514  16378   -887   -447    132
ATOM   4089  CZ  PHE A 278      -3.664  30.884   0.871  1.00124.76           C  
ANISOU 4089  CZ  PHE A 278    13728  17415  16259  -1017   -466    116
ATOM   4090  H   PHE A 278      -1.651  30.468  -3.725  1.00  0.00           H  
ATOM   4091  HA  PHE A 278      -4.419  31.360  -3.952  1.00  0.00           H  
ATOM   4092  HB3 PHE A 278      -3.418  33.518  -3.116  1.00  0.00           H  
ATOM   4093  HB2 PHE A 278      -1.845  32.771  -3.141  1.00  0.00           H  
ATOM   4094  HD1 PHE A 278      -5.232  32.648  -1.556  1.00  0.00           H  
ATOM   4095  HD2 PHE A 278      -1.183  31.176  -1.413  1.00  0.00           H  
ATOM   4096  HE1 PHE A 278      -5.649  31.668   0.663  1.00  0.00           H  
ATOM   4097  HE2 PHE A 278      -1.642  30.179   0.796  1.00  0.00           H  
ATOM   4098  HZ  PHE A 278      -3.859  30.445   1.838  1.00  0.00           H  
ATOM   4099  N   LYS A 279      -2.493  31.880  -6.463  1.00119.32           N  
ANISOU 4099  N   LYS A 279    12358  17012  15967  -1008    947   -507
ATOM   4100  CA  LYS A 279      -2.340  32.518  -7.775  1.00118.90           C  
ANISOU 4100  CA  LYS A 279    12305  17026  15844  -1206   1188   -613
ATOM   4101  C   LYS A 279      -3.612  32.392  -8.635  1.00117.80           C  
ANISOU 4101  C   LYS A 279    12536  16656  15568  -1220   1333   -681
ATOM   4102  O   LYS A 279      -4.119  31.286  -8.817  1.00117.31           O  
ANISOU 4102  O   LYS A 279    12596  16433  15545   -998   1394   -709
ATOM   4103  CB  LYS A 279      -1.105  31.948  -8.504  1.00  0.00           C  
ATOM   4104  CG  LYS A 279      -0.751  32.720  -9.795  1.00  0.00           C  
ATOM   4105  CD  LYS A 279       0.490  32.186 -10.531  1.00  0.00           C  
ATOM   4106  CE  LYS A 279       0.290  30.828 -11.225  1.00  0.00           C  
ATOM   4107  NZ  LYS A 279      -0.701  30.905 -12.313  1.00  0.00           N1+
ATOM   4108  H   LYS A 279      -1.902  31.082  -6.276  1.00  0.00           H  
ATOM   4109  HA  LYS A 279      -2.151  33.578  -7.590  1.00  0.00           H  
ATOM   4110  HB2 LYS A 279      -0.247  31.992  -7.832  1.00  0.00           H  
ATOM   4111  HB3 LYS A 279      -1.266  30.891  -8.723  1.00  0.00           H  
ATOM   4112  HG2 LYS A 279      -1.596  32.732 -10.483  1.00  0.00           H  
ATOM   4113  HG3 LYS A 279      -0.572  33.764  -9.534  1.00  0.00           H  
ATOM   4114  HD2 LYS A 279       0.816  32.924 -11.265  1.00  0.00           H  
ATOM   4115  HD3 LYS A 279       1.313  32.099  -9.821  1.00  0.00           H  
ATOM   4116  HE2 LYS A 279       1.237  30.492 -11.650  1.00  0.00           H  
ATOM   4117  HE3 LYS A 279      -0.019  30.066 -10.509  1.00  0.00           H  
ATOM   4118  HZ1 LYS A 279      -0.789  30.000 -12.753  1.00  0.00           H  
ATOM   4119  HZ2 LYS A 279      -1.595  31.184 -11.936  1.00  0.00           H  
ATOM   4120  HZ3 LYS A 279      -0.398  31.582 -12.999  1.00  0.00           H  
ATOM   4121  N   GLY A 280      -4.071  33.537  -9.163  1.00124.03           N  
ANISOU 4121  N   GLY A 280    13496  17433  16196  -1493   1386   -704
ATOM   4122  CA  GLY A 280      -5.292  33.649  -9.959  1.00123.56           C  
ANISOU 4122  CA  GLY A 280    13771  17178  15998  -1539   1474   -745
ATOM   4123  C   GLY A 280      -6.497  34.070  -9.103  1.00121.89           C  
ANISOU 4123  C   GLY A 280    13835  16787  15690  -1571   1288   -688
ATOM   4124  O   GLY A 280      -7.601  34.154  -9.641  1.00121.07           O  
ANISOU 4124  O   GLY A 280    13980  16527  15495  -1580   1322   -711
ATOM   4125  H   GLY A 280      -3.575  34.396  -8.973  1.00  0.00           H  
ATOM   4126  HA3 GLY A 280      -5.520  32.717 -10.479  1.00  0.00           H  
ATOM   4127  HA2 GLY A 280      -5.132  34.405 -10.728  1.00  0.00           H  
ATOM   4128  N   ALA A 281      -6.305  34.345  -7.796  1.00127.41           N  
ANISOU 4128  N   ALA A 281    14477  17524  16407  -1600   1095   -621
ATOM   4129  CA  ALA A 281      -7.353  34.783  -6.870  1.00127.94           C  
ANISOU 4129  CA  ALA A 281    14786  17440  16387  -1641    941   -590
ATOM   4130  C   ALA A 281      -7.988  36.144  -7.201  1.00127.71           C  
ANISOU 4130  C   ALA A 281    14978  17308  16239  -1840    947   -607
ATOM   4131  O   ALA A 281      -9.110  36.369  -6.765  1.00128.07           O  
ANISOU 4131  O   ALA A 281    15241  17188  16232  -1810    908   -620
ATOM   4132  CB  ALA A 281      -6.815  34.784  -5.430  1.00128.58           C  
ANISOU 4132  CB  ALA A 281    14767  17605  16482  -1678    744   -525
ATOM   4133  H   ALA A 281      -5.386  34.223  -7.394  1.00  0.00           H  
ATOM   4134  HA  ALA A 281      -8.157  34.048  -6.918  1.00  0.00           H  
ATOM   4135  HB1 ALA A 281      -7.549  35.181  -4.728  1.00  0.00           H  
ATOM   4136  HB2 ALA A 281      -6.586  33.770  -5.102  1.00  0.00           H  
ATOM   4137  HB3 ALA A 281      -5.909  35.385  -5.339  1.00  0.00           H  
ATOM   4138  N   GLY A 282      -7.304  37.016  -7.963  1.00121.87           N  
ANISOU 4138  N   GLY A 282    14177  16664  15465  -2041    997   -605
ATOM   4139  CA  GLY A 282      -7.812  38.343  -8.329  1.00121.73           C  
ANISOU 4139  CA  GLY A 282    14385  16526  15340  -2236    982   -598
ATOM   4140  C   GLY A 282      -8.971  38.290  -9.341  1.00120.69           C  
ANISOU 4140  C   GLY A 282    14470  16232  15156  -2179   1043   -613
ATOM   4141  O   GLY A 282      -9.765  39.230  -9.391  1.00120.67           O  
ANISOU 4141  O   GLY A 282    14681  16065  15103  -2232    968   -598
ATOM   4142  H   GLY A 282      -6.384  36.765  -8.294  1.00  0.00           H  
ATOM   4143  HA3 GLY A 282      -6.996  38.920  -8.765  1.00  0.00           H  
ATOM   4144  HA2 GLY A 282      -8.134  38.876  -7.433  1.00  0.00           H  
ATOM   4145  N   ALA A 283      -9.089  37.200 -10.123  1.00117.62           N  
ANISOU 4145  N   ALA A 283    14025  15882  14783  -2069   1174   -645
ATOM   4146  CA  ALA A 283     -10.137  36.993 -11.126  1.00117.15           C  
ANISOU 4146  CA  ALA A 283    14162  15699  14651  -2049   1217   -653
ATOM   4147  C   ALA A 283     -11.549  36.802 -10.541  1.00116.48           C  
ANISOU 4147  C   ALA A 283    14227  15452  14580  -1922   1108   -652
ATOM   4148  O   ALA A 283     -12.521  37.046 -11.257  1.00116.35           O  
ANISOU 4148  O   ALA A 283    14379  15318  14510  -1959   1060   -630
ATOM   4149  CB  ALA A 283      -9.756  35.788 -12.000  1.00118.46           C  
ANISOU 4149  CB  ALA A 283    14255  15936  14819  -1967   1389   -709
ATOM   4150  H   ALA A 283      -8.424  36.446 -10.017  1.00  0.00           H  
ATOM   4151  HA  ALA A 283     -10.166  37.877 -11.765  1.00  0.00           H  
ATOM   4152  HB1 ALA A 283     -10.485  35.627 -12.795  1.00  0.00           H  
ATOM   4153  HB2 ALA A 283      -8.786  35.938 -12.474  1.00  0.00           H  
ATOM   4154  HB3 ALA A 283      -9.699  34.870 -11.413  1.00  0.00           H  
ATOM   4155  N   ASN A 284     -11.639  36.397  -9.259  1.00102.66           N  
ANISOU 4155  N   ASN A 284    12408  13702  12897  -1779   1066   -673
ATOM   4156  CA  ASN A 284     -12.895  36.162  -8.540  1.00101.75           C  
ANISOU 4156  CA  ASN A 284    12412  13461  12787  -1682    996   -692
ATOM   4157  C   ASN A 284     -13.739  37.424  -8.274  1.00101.77           C  
ANISOU 4157  C   ASN A 284    12556  13340  12771  -1753    905   -685
ATOM   4158  O   ASN A 284     -14.870  37.266  -7.828  1.00101.27           O  
ANISOU 4158  O   ASN A 284    12575  13182  12722  -1675    876   -713
ATOM   4159  CB  ASN A 284     -12.638  35.351  -7.240  1.00  0.00           C  
ATOM   4160  CG  ASN A 284     -12.034  36.090  -6.030  1.00  0.00           C  
ATOM   4161  OD1 ASN A 284     -11.771  37.291  -6.057  1.00  0.00           O  
ATOM   4162  ND2 ASN A 284     -11.789  35.353  -4.947  1.00  0.00           N  
ATOM   4163  H   ASN A 284     -10.791  36.255  -8.727  1.00  0.00           H  
ATOM   4164  HA  ASN A 284     -13.535  35.546  -9.174  1.00  0.00           H  
ATOM   4165  HB2 ASN A 284     -13.594  34.952  -6.900  1.00  0.00           H  
ATOM   4166  HB3 ASN A 284     -12.012  34.487  -7.468  1.00  0.00           H  
ATOM   4167 HD22 ASN A 284     -11.384  35.786  -4.130  1.00  0.00           H  
ATOM   4168 HD21 ASN A 284     -11.987  34.363  -4.937  1.00  0.00           H  
ATOM   4169  N   ILE A 285     -13.186  38.628  -8.506  1.00 90.55           N  
ANISOU 4169  N   ILE A 285    11159  11918  11328  -1900    867   -653
ATOM   4170  CA  ILE A 285     -13.816  39.925  -8.240  1.00 90.75           C  
ANISOU 4170  CA  ILE A 285    11349  11783  11347  -1964    784   -645
ATOM   4171  C   ILE A 285     -15.194  40.119  -8.905  1.00 90.22           C  
ANISOU 4171  C   ILE A 285    11400  11585  11294  -1880    753   -634
ATOM   4172  O   ILE A 285     -16.080  40.690  -8.269  1.00 89.91           O  
ANISOU 4172  O   ILE A 285    11446  11409  11306  -1814    695   -664
ATOM   4173  CB  ILE A 285     -12.841  41.098  -8.590  1.00  0.00           C  
ATOM   4174  CG1 ILE A 285     -11.866  41.313  -7.409  1.00  0.00           C  
ATOM   4175  CG2 ILE A 285     -13.486  42.444  -9.006  1.00  0.00           C  
ATOM   4176  CD1 ILE A 285     -10.694  42.259  -7.711  1.00  0.00           C  
ATOM   4177  H   ILE A 285     -12.236  38.667  -8.850  1.00  0.00           H  
ATOM   4178  HA  ILE A 285     -14.003  39.948  -7.164  1.00  0.00           H  
ATOM   4179  HB  ILE A 285     -12.243  40.775  -9.443  1.00  0.00           H  
ATOM   4180 HG12 ILE A 285     -12.418  41.700  -6.551  1.00  0.00           H  
ATOM   4181 HG13 ILE A 285     -11.457  40.353  -7.089  1.00  0.00           H  
ATOM   4182 HG21 ILE A 285     -12.732  43.201  -9.218  1.00  0.00           H  
ATOM   4183 HG22 ILE A 285     -14.078  42.354  -9.917  1.00  0.00           H  
ATOM   4184 HG23 ILE A 285     -14.130  42.837  -8.219  1.00  0.00           H  
ATOM   4185 HD11 ILE A 285      -9.852  42.052  -7.050  1.00  0.00           H  
ATOM   4186 HD12 ILE A 285     -10.342  42.145  -8.736  1.00  0.00           H  
ATOM   4187 HD13 ILE A 285     -10.978  43.301  -7.564  1.00  0.00           H  
ATOM   4188  N   LEU A 286     -15.356  39.619 -10.142  1.00 88.64           N  
ANISOU 4188  N   LEU A 286    11202  11429  11049  -1886    786   -596
ATOM   4189  CA  LEU A 286     -16.610  39.725 -10.889  1.00 88.46           C  
ANISOU 4189  CA  LEU A 286    11275  11299  11036  -1820    712   -567
ATOM   4190  C   LEU A 286     -17.615  38.613 -10.542  1.00 87.82           C  
ANISOU 4190  C   LEU A 286    11116  11243  11007  -1667    731   -633
ATOM   4191  O   LEU A 286     -18.819  38.861 -10.605  1.00 87.56           O  
ANISOU 4191  O   LEU A 286    11106  11123  11038  -1576    658   -643
ATOM   4192  CB  LEU A 286     -16.305  39.788 -12.397  1.00 89.66           C  
ANISOU 4192  CB  LEU A 286    11507  11478  11082  -1936    711   -488
ATOM   4193  CG  LEU A 286     -17.228  40.776 -13.136  1.00 89.76           C  
ANISOU 4193  CG  LEU A 286    11681  11334  11088  -1947    557   -395
ATOM   4194  CD1 LEU A 286     -16.963  42.242 -12.727  1.00 90.02           C  
ANISOU 4194  CD1 LEU A 286    11838  11201  11163  -1995    480   -359
ATOM   4195  CD2 LEU A 286     -17.160  40.569 -14.653  1.00 89.76           C  
ANISOU 4195  CD2 LEU A 286    11787  11380  10939  -2097    549   -309
ATOM   4196  H   LEU A 286     -14.588  39.149 -10.600  1.00  0.00           H  
ATOM   4197  HA  LEU A 286     -17.087  40.661 -10.592  1.00  0.00           H  
ATOM   4198  HB3 LEU A 286     -16.383  38.788 -12.827  1.00  0.00           H  
ATOM   4199  HB2 LEU A 286     -15.273  40.097 -12.571  1.00  0.00           H  
ATOM   4200  HG  LEU A 286     -18.252  40.534 -12.844  1.00  0.00           H  
ATOM   4201 HD11 LEU A 286     -16.676  42.869 -13.569  1.00  0.00           H  
ATOM   4202 HD12 LEU A 286     -17.854  42.686 -12.283  1.00  0.00           H  
ATOM   4203 HD13 LEU A 286     -16.161  42.327 -11.993  1.00  0.00           H  
ATOM   4204 HD21 LEU A 286     -18.161  40.644 -15.072  1.00  0.00           H  
ATOM   4205 HD22 LEU A 286     -16.530  41.302 -15.155  1.00  0.00           H  
ATOM   4206 HD23 LEU A 286     -16.770  39.585 -14.916  1.00  0.00           H  
ATOM   4207  N   ARG A 287     -17.115  37.442 -10.105  1.00 82.91           N  
ANISOU 4207  N   ARG A 287    10400  10735  10366  -1638    830   -680
ATOM   4208  CA  ARG A 287     -17.901  36.425  -9.397  1.00 82.52           C  
ANISOU 4208  CA  ARG A 287    10307  10705  10343  -1533    862   -743
ATOM   4209  C   ARG A 287     -18.394  36.939  -8.027  1.00 82.40           C  
ANISOU 4209  C   ARG A 287    10287  10624  10397  -1473    831   -800
ATOM   4210  O   ARG A 287     -19.486  36.565  -7.602  1.00 82.45           O  
ANISOU 4210  O   ARG A 287    10276  10609  10441  -1406    830   -853
ATOM   4211  CB  ARG A 287     -17.071  35.123  -9.289  1.00 75.81           C  
ANISOU 4211  CB  ARG A 287     9398   9943   9464  -1514    965   -766
ATOM   4212  CG  ARG A 287     -17.705  34.039  -8.399  1.00 75.52           C  
ANISOU 4212  CG  ARG A 287     9358   9902   9436  -1436    999   -822
ATOM   4213  CD  ARG A 287     -17.002  32.674  -8.472  1.00 75.53           C  
ANISOU 4213  CD  ARG A 287     9335   9942   9421  -1393   1085   -829
ATOM   4214  NE  ARG A 287     -15.859  32.584  -7.551  1.00 75.33           N  
ANISOU 4214  NE  ARG A 287     9245   9944   9433  -1355   1063   -809
ATOM   4215  CZ  ARG A 287     -14.559  32.426  -7.851  1.00 75.54           C  
ANISOU 4215  CZ  ARG A 287     9174  10039   9490  -1341   1092   -779
ATOM   4216  NH1 ARG A 287     -14.107  32.463  -9.112  1.00 75.97           N  
ANISOU 4216  NH1 ARG A 287     9200  10136   9530  -1376   1178   -783
ATOM   4217  NH2 ARG A 287     -13.692  32.216  -6.852  1.00 75.31           N1+
ANISOU 4217  NH2 ARG A 287     9065  10052   9499  -1308   1034   -747
ATOM   4218  H   ARG A 287     -16.113  37.316 -10.083  1.00  0.00           H  
ATOM   4219  HA  ARG A 287     -18.783  36.210 -10.002  1.00  0.00           H  
ATOM   4220  HB3 ARG A 287     -16.067  35.325  -8.921  1.00  0.00           H  
ATOM   4221  HB2 ARG A 287     -16.946  34.730 -10.299  1.00  0.00           H  
ATOM   4222  HG3 ARG A 287     -18.766  33.942  -8.606  1.00  0.00           H  
ATOM   4223  HG2 ARG A 287     -17.651  34.385  -7.366  1.00  0.00           H  
ATOM   4224  HD3 ARG A 287     -16.612  32.542  -9.480  1.00  0.00           H  
ATOM   4225  HD2 ARG A 287     -17.694  31.847  -8.331  1.00  0.00           H  
ATOM   4226  HE  ARG A 287     -16.115  32.591  -6.573  1.00  0.00           H  
ATOM   4227 HH12 ARG A 287     -13.126  32.331  -9.313  1.00  0.00           H  
ATOM   4228 HH11 ARG A 287     -14.753  32.617  -9.873  1.00  0.00           H  
ATOM   4229 HH22 ARG A 287     -12.713  32.063  -7.046  1.00  0.00           H  
ATOM   4230 HH21 ARG A 287     -14.017  32.161  -5.897  1.00  0.00           H  
ATOM   4231  N   GLY A 288     -17.585  37.815  -7.404  1.00 85.15           N  
ANISOU 4231  N   GLY A 288    10651  10951  10750  -1524    814   -798
ATOM   4232  CA  GLY A 288     -17.836  38.553  -6.171  1.00 85.11           C  
ANISOU 4232  CA  GLY A 288    10685  10875  10778  -1513    799   -864
ATOM   4233  C   GLY A 288     -19.120  39.381  -6.261  1.00 85.23           C  
ANISOU 4233  C   GLY A 288    10750  10760  10874  -1441    765   -902
ATOM   4234  O   GLY A 288     -19.918  39.362  -5.328  1.00 85.23           O  
ANISOU 4234  O   GLY A 288    10746  10722  10914  -1384    807   -999
ATOM   4235  H   GLY A 288     -16.691  38.004  -7.838  1.00  0.00           H  
ATOM   4236  HA3 GLY A 288     -17.000  39.230  -5.998  1.00  0.00           H  
ATOM   4237  HA2 GLY A 288     -17.858  37.875  -5.327  1.00  0.00           H  
ATOM   4238  N   VAL A 289     -19.323  40.060  -7.403  1.00 68.64           N  
ANISOU 4238  N   VAL A 289     8693   8590   8796  -1441    692   -826
ATOM   4239  CA  VAL A 289     -20.522  40.831  -7.729  1.00 68.51           C  
ANISOU 4239  CA  VAL A 289     8706   8440   8885  -1333    625   -835
ATOM   4240  C   VAL A 289     -21.756  39.935  -7.952  1.00 67.97           C  
ANISOU 4240  C   VAL A 289     8509   8453   8863  -1231    642   -878
ATOM   4241  O   VAL A 289     -22.823  40.269  -7.440  1.00 67.85           O  
ANISOU 4241  O   VAL A 289     8434   8397   8949  -1127    672   -973
ATOM   4242  CB  VAL A 289     -20.288  41.716  -8.991  1.00 68.92           C  
ANISOU 4242  CB  VAL A 289     8865   8395   8926  -1376    508   -708
ATOM   4243  CG1 VAL A 289     -21.555  42.358  -9.600  1.00 68.95           C  
ANISOU 4243  CG1 VAL A 289     8874   8263   9062  -1222    400   -690
ATOM   4244  CG2 VAL A 289     -19.242  42.806  -8.703  1.00 69.26           C  
ANISOU 4244  CG2 VAL A 289     9048   8344   8923  -1508    500   -679
ATOM   4245  H   VAL A 289     -18.614  40.027  -8.120  1.00  0.00           H  
ATOM   4246  HA  VAL A 289     -20.735  41.488  -6.883  1.00  0.00           H  
ATOM   4247  HB  VAL A 289     -19.863  41.085  -9.771  1.00  0.00           H  
ATOM   4248 HG11 VAL A 289     -21.296  43.063 -10.389  1.00  0.00           H  
ATOM   4249 HG12 VAL A 289     -22.213  41.615 -10.053  1.00  0.00           H  
ATOM   4250 HG13 VAL A 289     -22.129  42.898  -8.849  1.00  0.00           H  
ATOM   4251 HG21 VAL A 289     -19.032  43.400  -9.593  1.00  0.00           H  
ATOM   4252 HG22 VAL A 289     -19.588  43.486  -7.924  1.00  0.00           H  
ATOM   4253 HG23 VAL A 289     -18.294  42.380  -8.374  1.00  0.00           H  
ATOM   4254  N   ALA A 290     -21.592  38.818  -8.685  1.00 64.65           N  
ANISOU 4254  N   ALA A 290     8049   8152   8365  -1279    637   -821
ATOM   4255  CA  ALA A 290     -22.663  37.860  -8.966  1.00 64.68           C  
ANISOU 4255  CA  ALA A 290     7946   8248   8381  -1237    644   -853
ATOM   4256  C   ALA A 290     -23.231  37.218  -7.690  1.00 64.99           C  
ANISOU 4256  C   ALA A 290     7911   8332   8451  -1202    759   -983
ATOM   4257  O   ALA A 290     -24.437  37.298  -7.479  1.00 65.11           O  
ANISOU 4257  O   ALA A 290     7828   8345   8567  -1120    764  -1055
ATOM   4258  CB  ALA A 290     -22.180  36.797  -9.965  1.00 63.82           C  
ANISOU 4258  CB  ALA A 290     7861   8244   8145  -1337    666   -801
ATOM   4259  H   ALA A 290     -20.683  38.604  -9.071  1.00  0.00           H  
ATOM   4260  HA  ALA A 290     -23.473  38.414  -9.446  1.00  0.00           H  
ATOM   4261  HB1 ALA A 290     -22.981  36.101 -10.217  1.00  0.00           H  
ATOM   4262  HB2 ALA A 290     -21.845  37.260 -10.894  1.00  0.00           H  
ATOM   4263  HB3 ALA A 290     -21.349  36.214  -9.567  1.00  0.00           H  
ATOM   4264  N   GLY A 291     -22.354  36.670  -6.831  1.00 63.91           N  
ANISOU 4264  N   GLY A 291     7821   8230   8230  -1265    847  -1010
ATOM   4265  CA  GLY A 291     -22.719  36.064  -5.549  1.00 63.54           C  
ANISOU 4265  CA  GLY A 291     7758   8217   8166  -1274    948  -1113
ATOM   4266  C   GLY A 291     -23.386  37.067  -4.600  1.00 64.38           C  
ANISOU 4266  C   GLY A 291     7846   8252   8362  -1217    982  -1216
ATOM   4267  O   GLY A 291     -24.416  36.749  -4.006  1.00 64.67           O  
ANISOU 4267  O   GLY A 291     7798   8334   8441  -1193   1056  -1315
ATOM   4268  H   GLY A 291     -21.369  36.671  -7.068  1.00  0.00           H  
ATOM   4269  HA3 GLY A 291     -21.814  35.693  -5.071  1.00  0.00           H  
ATOM   4270  HA2 GLY A 291     -23.378  35.211  -5.716  1.00  0.00           H  
ATOM   4271  N   ALA A 292     -22.830  38.286  -4.500  1.00 61.42           N  
ANISOU 4271  N   ALA A 292     7551   7763   8020  -1206    941  -1204
ATOM   4272  CA  ALA A 292     -23.366  39.396  -3.710  1.00 61.91           C  
ANISOU 4272  CA  ALA A 292     7640   7710   8174  -1145    988  -1317
ATOM   4273  C   ALA A 292     -24.776  39.832  -4.120  1.00 62.05           C  
ANISOU 4273  C   ALA A 292     7523   7698   8355   -993    979  -1367
ATOM   4274  O   ALA A 292     -25.592  40.134  -3.248  1.00 62.85           O  
ANISOU 4274  O   ALA A 292     7554   7802   8523   -942   1097  -1515
ATOM   4275  CB  ALA A 292     -22.422  40.585  -3.856  1.00 64.20           C  
ANISOU 4275  CB  ALA A 292     8068   7858   8468  -1174    921  -1271
ATOM   4276  H   ALA A 292     -21.982  38.484  -5.014  1.00  0.00           H  
ATOM   4277  HA  ALA A 292     -23.389  39.086  -2.663  1.00  0.00           H  
ATOM   4278  HB1 ALA A 292     -22.756  41.430  -3.261  1.00  0.00           H  
ATOM   4279  HB2 ALA A 292     -21.431  40.304  -3.521  1.00  0.00           H  
ATOM   4280  HB3 ALA A 292     -22.333  40.920  -4.889  1.00  0.00           H  
ATOM   4281  N   GLY A 293     -25.023  39.831  -5.441  1.00 67.20           N  
ANISOU 4281  N   GLY A 293     8132   8336   9067   -931    839  -1246
ATOM   4282  CA  GLY A 293     -26.300  40.159  -6.056  1.00 67.21           C  
ANISOU 4282  CA  GLY A 293     7972   8332   9231   -779    774  -1255
ATOM   4283  C   GLY A 293     -27.372  39.127  -5.690  1.00 67.53           C  
ANISOU 4283  C   GLY A 293     7821   8556   9283   -792    869  -1352
ATOM   4284  O   GLY A 293     -28.499  39.534  -5.432  1.00 68.19           O  
ANISOU 4284  O   GLY A 293     7738   8649   9523   -669    922  -1464
ATOM   4285  H   GLY A 293     -24.274  39.582  -6.073  1.00  0.00           H  
ATOM   4286  HA3 GLY A 293     -26.176  40.184  -7.138  1.00  0.00           H  
ATOM   4287  HA2 GLY A 293     -26.622  41.155  -5.749  1.00  0.00           H  
ATOM   4288  N   VAL A 294     -27.038  37.822  -5.614  1.00 64.39           N  
ANISOU 4288  N   VAL A 294     7447   8296   8722   -944    913  -1325
ATOM   4289  CA  VAL A 294     -28.014  36.789  -5.245  1.00 65.00           C  
ANISOU 4289  CA  VAL A 294     7390   8536   8771  -1012   1012  -1413
ATOM   4290  C   VAL A 294     -28.437  36.882  -3.765  1.00 65.96           C  
ANISOU 4290  C   VAL A 294     7468   8676   8918  -1020   1200  -1593
ATOM   4291  O   VAL A 294     -29.610  36.663  -3.485  1.00 66.56           O  
ANISOU 4291  O   VAL A 294     7361   8869   9060  -1019   1282  -1697
ATOM   4292  CB  VAL A 294     -27.555  35.324  -5.495  1.00 68.94           C  
ANISOU 4292  CB  VAL A 294     7992   9119   9082  -1174   1030  -1350
ATOM   4293  CG1 VAL A 294     -28.730  34.324  -5.442  1.00 69.00           C  
ANISOU 4293  CG1 VAL A 294     7885   9278   9054  -1272   1108  -1424
ATOM   4294  CG2 VAL A 294     -26.851  35.152  -6.838  1.00 68.85           C  
ANISOU 4294  CG2 VAL A 294     8050   9089   9022  -1188    886  -1199
ATOM   4295  H   VAL A 294     -26.092  37.520  -5.807  1.00  0.00           H  
ATOM   4296  HA  VAL A 294     -28.898  36.960  -5.860  1.00  0.00           H  
ATOM   4297  HB  VAL A 294     -26.846  35.027  -4.720  1.00  0.00           H  
ATOM   4298 HG11 VAL A 294     -28.399  33.302  -5.622  1.00  0.00           H  
ATOM   4299 HG12 VAL A 294     -29.243  34.324  -4.483  1.00  0.00           H  
ATOM   4300 HG13 VAL A 294     -29.476  34.559  -6.199  1.00  0.00           H  
ATOM   4301 HG21 VAL A 294     -26.842  34.108  -7.143  1.00  0.00           H  
ATOM   4302 HG22 VAL A 294     -27.342  35.722  -7.622  1.00  0.00           H  
ATOM   4303 HG23 VAL A 294     -25.818  35.472  -6.763  1.00  0.00           H  
ATOM   4304  N   LEU A 295     -27.514  37.240  -2.853  1.00 67.95           N  
ANISOU 4304  N   LEU A 295     7888   8829   9103  -1054   1273  -1636
ATOM   4305  CA  LEU A 295     -27.813  37.454  -1.430  1.00 68.94           C  
ANISOU 4305  CA  LEU A 295     8033   8960   9201  -1104   1461  -1810
ATOM   4306  C   LEU A 295     -28.778  38.628  -1.205  1.00 69.61           C  
ANISOU 4306  C   LEU A 295     7987   8969   9493   -935   1537  -1955
ATOM   4307  O   LEU A 295     -29.803  38.444  -0.551  1.00 70.70           O  
ANISOU 4307  O   LEU A 295     7973   9204   9687   -937   1700  -2116
ATOM   4308  CB  LEU A 295     -26.510  37.684  -0.632  1.00 65.29           C  
ANISOU 4308  CB  LEU A 295     7810   8404   8592  -1203   1470  -1789
ATOM   4309  CG  LEU A 295     -25.697  36.408  -0.349  1.00 65.20           C  
ANISOU 4309  CG  LEU A 295     7925   8473   8376  -1372   1471  -1716
ATOM   4310  CD1 LEU A 295     -24.259  36.761   0.079  1.00 65.79           C  
ANISOU 4310  CD1 LEU A 295     8178   8469   8349  -1431   1393  -1636
ATOM   4311  CD2 LEU A 295     -26.394  35.484   0.675  1.00 65.34           C  
ANISOU 4311  CD2 LEU A 295     7965   8578   8284  -1508   1645  -1850
ATOM   4312  H   LEU A 295     -26.563  37.417  -3.147  1.00  0.00           H  
ATOM   4313  HA  LEU A 295     -28.310  36.559  -1.053  1.00  0.00           H  
ATOM   4314  HB3 LEU A 295     -26.730  38.162   0.323  1.00  0.00           H  
ATOM   4315  HB2 LEU A 295     -25.888  38.398  -1.175  1.00  0.00           H  
ATOM   4316  HG  LEU A 295     -25.625  35.860  -1.285  1.00  0.00           H  
ATOM   4317 HD11 LEU A 295     -23.843  36.046   0.790  1.00  0.00           H  
ATOM   4318 HD12 LEU A 295     -23.594  36.777  -0.784  1.00  0.00           H  
ATOM   4319 HD13 LEU A 295     -24.207  37.747   0.541  1.00  0.00           H  
ATOM   4320 HD21 LEU A 295     -26.562  34.497   0.246  1.00  0.00           H  
ATOM   4321 HD22 LEU A 295     -25.803  35.342   1.580  1.00  0.00           H  
ATOM   4322 HD23 LEU A 295     -27.362  35.873   0.992  1.00  0.00           H  
ATOM   4323  N   SER A 296     -28.430  39.799  -1.760  1.00 75.56           N  
ANISOU 4323  N   SER A 296     8803   9543  10364   -792   1428  -1902
ATOM   4324  CA  SER A 296     -29.186  41.041  -1.611  1.00 76.72           C  
ANISOU 4324  CA  SER A 296     8866   9548  10735   -586   1477  -2023
ATOM   4325  C   SER A 296     -30.562  41.008  -2.294  1.00 77.64           C  
ANISOU 4325  C   SER A 296     8662   9774  11063   -418   1427  -2032
ATOM   4326  O   SER A 296     -31.541  41.397  -1.657  1.00 79.21           O  
ANISOU 4326  O   SER A 296     8669  10028  11400   -332   1597  -2221
ATOM   4327  CB  SER A 296     -28.308  42.220  -2.067  1.00 82.80           C  
ANISOU 4327  CB  SER A 296     9820  10075  11567   -491   1338  -1928
ATOM   4328  OG  SER A 296     -28.063  42.211  -3.460  1.00 81.31           O  
ANISOU 4328  OG  SER A 296     9664   9901  11329   -517   1118  -1702
ATOM   4329  H   SER A 296     -27.580  39.865  -2.305  1.00  0.00           H  
ATOM   4330  HA  SER A 296     -29.362  41.172  -0.541  1.00  0.00           H  
ATOM   4331  HB3 SER A 296     -27.355  42.182  -1.544  1.00  0.00           H  
ATOM   4332  HB2 SER A 296     -28.779  43.169  -1.804  1.00  0.00           H  
ATOM   4333  HG  SER A 296     -27.577  43.005  -3.692  1.00  0.00           H  
ATOM   4334  N   ILE A 297     -30.623  40.507  -3.543  1.00 76.03           N  
ANISOU 4334  N   ILE A 297     8391   9623  10875   -394   1202  -1837
ATOM   4335  CA  ILE A 297     -31.867  40.343  -4.303  1.00 76.46           C  
ANISOU 4335  CA  ILE A 297     8137   9810  11105   -269   1102  -1814
ATOM   4336  C   ILE A 297     -32.784  39.281  -3.672  1.00 77.72           C  
ANISOU 4336  C   ILE A 297     8086  10216  11230   -393   1302  -1977
ATOM   4337  O   ILE A 297     -33.993  39.482  -3.707  1.00 79.52           O  
ANISOU 4337  O   ILE A 297     8001  10551  11660   -264   1336  -2074
ATOM   4338  CB  ILE A 297     -31.627  40.027  -5.816  1.00 72.90           C  
ANISOU 4338  CB  ILE A 297     7705   9409  10585   -317    835  -1576
ATOM   4339  CG1 ILE A 297     -30.885  41.185  -6.523  1.00 73.08           C  
ANISOU 4339  CG1 ILE A 297     7925   9199  10645   -212    641  -1415
ATOM   4340  CG2 ILE A 297     -32.904  39.679  -6.620  1.00 73.40           C  
ANISOU 4340  CG2 ILE A 297     7447   9662  10779   -256    716  -1548
ATOM   4341  CD1 ILE A 297     -30.232  40.794  -7.862  1.00 73.12           C  
ANISOU 4341  CD1 ILE A 297     8047   9254  10482   -351    442  -1200
ATOM   4342  H   ILE A 297     -29.773  40.214  -4.008  1.00  0.00           H  
ATOM   4343  HA  ILE A 297     -32.416  41.283  -4.250  1.00  0.00           H  
ATOM   4344  HB  ILE A 297     -30.975  39.157  -5.862  1.00  0.00           H  
ATOM   4345 HG13 ILE A 297     -30.100  41.577  -5.878  1.00  0.00           H  
ATOM   4346 HG12 ILE A 297     -31.572  42.018  -6.680  1.00  0.00           H  
ATOM   4347 HG21 ILE A 297     -32.682  39.508  -7.673  1.00  0.00           H  
ATOM   4348 HG22 ILE A 297     -33.391  38.772  -6.262  1.00  0.00           H  
ATOM   4349 HG23 ILE A 297     -33.633  40.488  -6.568  1.00  0.00           H  
ATOM   4350 HD11 ILE A 297     -29.160  40.990  -7.843  1.00  0.00           H  
ATOM   4351 HD12 ILE A 297     -30.364  39.739  -8.101  1.00  0.00           H  
ATOM   4352 HD13 ILE A 297     -30.654  41.379  -8.678  1.00  0.00           H  
ATOM   4353  N   TYR A 298     -32.217  38.227  -3.053  1.00 88.90           N  
ANISOU 4353  N   TYR A 298     9665  11716  12395   -642   1431  -2005
ATOM   4354  CA  TYR A 298     -32.976  37.211  -2.319  1.00 89.60           C  
ANISOU 4354  CA  TYR A 298     9617  12017  12409   -809   1625  -2147
ATOM   4355  C   TYR A 298     -33.707  37.785  -1.099  1.00 92.04           C  
ANISOU 4355  C   TYR A 298     9793  12329  12847   -733   1878  -2396
ATOM   4356  O   TYR A 298     -34.898  37.514  -0.943  1.00 94.48           O  
ANISOU 4356  O   TYR A 298     9787  12810  13300   -697   1975  -2521
ATOM   4357  CB  TYR A 298     -32.081  36.022  -1.918  1.00 96.13           C  
ANISOU 4357  CB  TYR A 298    10713  12874  12939  -1075   1692  -2104
ATOM   4358  CG  TYR A 298     -32.794  34.961  -1.106  1.00 95.87           C  
ANISOU 4358  CG  TYR A 298    10615  13021  12790  -1287   1900  -2244
ATOM   4359  CD1 TYR A 298     -33.582  34.012  -1.779  1.00 96.00           C  
ANISOU 4359  CD1 TYR A 298    10457  13229  12790  -1405   1873  -2223
ATOM   4360  CD2 TYR A 298     -32.721  34.948   0.304  1.00 95.56           C  
ANISOU 4360  CD2 TYR A 298    10711  12964  12634  -1406   2125  -2397
ATOM   4361  CE1 TYR A 298     -34.301  33.051  -1.051  1.00 95.73           C  
ANISOU 4361  CE1 TYR A 298    10379  13358  12634  -1638   2073  -2352
ATOM   4362  CE2 TYR A 298     -33.458  33.993   1.032  1.00 95.26           C  
ANISOU 4362  CE2 TYR A 298    10641  13090  12463  -1637   2327  -2522
ATOM   4363  CZ  TYR A 298     -34.251  33.049   0.352  1.00 95.29           C  
ANISOU 4363  CZ  TYR A 298    10466  13278  12462  -1753   2304  -2498
ATOM   4364  OH  TYR A 298     -34.994  32.130   1.026  1.00 95.05           O  
ANISOU 4364  OH  TYR A 298    10417  13409  12290  -2017   2507  -2619
ATOM   4365  H   TYR A 298     -31.210  38.132  -3.044  1.00  0.00           H  
ATOM   4366  HA  TYR A 298     -33.736  36.828  -3.005  1.00  0.00           H  
ATOM   4367  HB3 TYR A 298     -31.214  36.364  -1.353  1.00  0.00           H  
ATOM   4368  HB2 TYR A 298     -31.699  35.533  -2.814  1.00  0.00           H  
ATOM   4369  HD1 TYR A 298     -33.648  34.033  -2.856  1.00  0.00           H  
ATOM   4370  HD2 TYR A 298     -32.126  35.683   0.826  1.00  0.00           H  
ATOM   4371  HE1 TYR A 298     -34.898  32.318  -1.570  1.00  0.00           H  
ATOM   4372  HE2 TYR A 298     -33.429  33.999   2.109  1.00  0.00           H  
ATOM   4373  HH  TYR A 298     -34.675  31.892   1.910  1.00  0.00           H  
ATOM   4374  N   ASP A 299     -32.986  38.564  -0.272  1.00 93.34           N  
ANISOU 4374  N   ASP A 299    10195  12318  12953   -728   1993  -2479
ATOM   4375  CA  ASP A 299     -33.545  39.250   0.896  1.00 95.53           C  
ANISOU 4375  CA  ASP A 299    10416  12566  13314   -681   2266  -2739
ATOM   4376  C   ASP A 299     -34.667  40.214   0.506  1.00 97.48           C  
ANISOU 4376  C   ASP A 299    10332  12791  13915   -371   2262  -2830
ATOM   4377  O   ASP A 299     -35.745  40.113   1.082  1.00100.18           O  
ANISOU 4377  O   ASP A 299    10391  13300  14374   -356   2467  -3025
ATOM   4378  CB  ASP A 299     -32.508  39.990   1.770  1.00 98.15           C  
ANISOU 4378  CB  ASP A 299    11094  12673  13526   -718   2326  -2780
ATOM   4379  CG  ASP A 299     -31.347  39.144   2.293  1.00 96.95           C  
ANISOU 4379  CG  ASP A 299    11249  12545  13042  -1003   2305  -2682
ATOM   4380  OD1 ASP A 299     -31.425  37.897   2.244  1.00 96.48           O  
ANISOU 4380  OD1 ASP A 299    11164  12653  12842  -1168   2270  -2592
ATOM   4381  OD2 ASP A 299     -30.413  39.781   2.827  1.00 96.89           O1-
ANISOU 4381  OD2 ASP A 299    11511  12383  12921  -1062   2312  -2689
ATOM   4382  H   ASP A 299     -32.002  38.713  -0.451  1.00  0.00           H  
ATOM   4383  HA  ASP A 299     -33.996  38.474   1.518  1.00  0.00           H  
ATOM   4384  HB3 ASP A 299     -33.014  40.425   2.633  1.00  0.00           H  
ATOM   4385  HB2 ASP A 299     -32.080  40.806   1.186  1.00  0.00           H  
ATOM   4386  N   GLN A 300     -34.410  41.071  -0.497  1.00 99.20           N  
ANISOU 4386  N   GLN A 300    10569  12819  14306   -131   2016  -2675
ATOM   4387  CA  GLN A 300     -35.349  42.057  -1.037  1.00102.20           C  
ANISOU 4387  CA  GLN A 300    10657  13130  15047    213   1931  -2701
ATOM   4388  C   GLN A 300     -36.614  41.404  -1.633  1.00103.93           C  
ANISOU 4388  C   GLN A 300    10437  13647  15403    237   1888  -2704
ATOM   4389  O   GLN A 300     -37.711  41.926  -1.436  1.00107.47           O  
ANISOU 4389  O   GLN A 300    10535  14170  16127    439   2011  -2877
ATOM   4390  CB  GLN A 300     -34.608  42.896  -2.103  1.00105.87           C  
ANISOU 4390  CB  GLN A 300    11290  13355  15579    376   1607  -2452
ATOM   4391  CG  GLN A 300     -35.171  44.316  -2.312  1.00106.14           C  
ANISOU 4391  CG  GLN A 300    11225  13146  15957    751   1551  -2497
ATOM   4392  CD  GLN A 300     -34.895  45.261  -1.134  1.00105.58           C  
ANISOU 4392  CD  GLN A 300    11390  12815  15911    812   1796  -2711
ATOM   4393  OE1 GLN A 300     -33.977  45.046  -0.345  1.00104.53           O  
ANISOU 4393  OE1 GLN A 300    11558  12656  15501    551   1945  -2774
ATOM   4394  NE2 GLN A 300     -35.675  46.338  -1.027  1.00106.86           N  
ANISOU 4394  NE2 GLN A 300    11425  12767  16408   1162   1832  -2826
ATOM   4395  H   GLN A 300     -33.490  41.066  -0.919  1.00  0.00           H  
ATOM   4396  HA  GLN A 300     -35.654  42.696  -0.206  1.00  0.00           H  
ATOM   4397  HB3 GLN A 300     -34.606  42.367  -3.058  1.00  0.00           H  
ATOM   4398  HB2 GLN A 300     -33.555  42.983  -1.839  1.00  0.00           H  
ATOM   4399  HG3 GLN A 300     -36.242  44.272  -2.511  1.00  0.00           H  
ATOM   4400  HG2 GLN A 300     -34.709  44.756  -3.196  1.00  0.00           H  
ATOM   4401 HE22 GLN A 300     -35.524  46.991  -0.272  1.00  0.00           H  
ATOM   4402 HE21 GLN A 300     -36.418  46.504  -1.690  1.00  0.00           H  
ATOM   4403  N   LEU A 301     -36.433  40.254  -2.307  1.00 98.92           N  
ANISOU 4403  N   LEU A 301     9823  13189  14574     17   1724  -2524
ATOM   4404  CA  LEU A 301     -37.496  39.416  -2.861  1.00100.25           C  
ANISOU 4404  CA  LEU A 301     9631  13657  14802    -48   1657  -2504
ATOM   4405  C   LEU A 301     -38.337  38.727  -1.771  1.00101.93           C  
ANISOU 4405  C   LEU A 301     9620  14105  15002   -202   2000  -2772
ATOM   4406  O   LEU A 301     -39.525  38.520  -1.996  1.00105.00           O  
ANISOU 4406  O   LEU A 301     9580  14719  15595   -132   2024  -2859
ATOM   4407  CB  LEU A 301     -36.872  38.413  -3.858  1.00 95.77           C  
ANISOU 4407  CB  LEU A 301     9241  13180  13966   -304   1459  -2283
ATOM   4408  CG  LEU A 301     -37.854  37.592  -4.719  1.00 97.44           C  
ANISOU 4408  CG  LEU A 301     9154  13648  14220   -374   1281  -2191
ATOM   4409  CD1 LEU A 301     -38.727  38.481  -5.626  1.00 99.60           C  
ANISOU 4409  CD1 LEU A 301     9163  13882  14798    -59   1004  -2077
ATOM   4410  CD2 LEU A 301     -37.086  36.551  -5.549  1.00 95.16           C  
ANISOU 4410  CD2 LEU A 301     9131  13393  13631   -645   1146  -2012
ATOM   4411  H   LEU A 301     -35.492  39.906  -2.438  1.00  0.00           H  
ATOM   4412  HA  LEU A 301     -38.160  40.077  -3.416  1.00  0.00           H  
ATOM   4413  HB3 LEU A 301     -36.212  37.736  -3.314  1.00  0.00           H  
ATOM   4414  HB2 LEU A 301     -36.239  38.962  -4.554  1.00  0.00           H  
ATOM   4415  HG  LEU A 301     -38.512  37.034  -4.053  1.00  0.00           H  
ATOM   4416 HD11 LEU A 301     -38.782  38.097  -6.645  1.00  0.00           H  
ATOM   4417 HD12 LEU A 301     -39.748  38.533  -5.246  1.00  0.00           H  
ATOM   4418 HD13 LEU A 301     -38.350  39.502  -5.691  1.00  0.00           H  
ATOM   4419 HD21 LEU A 301     -37.762  35.784  -5.926  1.00  0.00           H  
ATOM   4420 HD22 LEU A 301     -36.593  37.008  -6.408  1.00  0.00           H  
ATOM   4421 HD23 LEU A 301     -36.318  36.056  -4.955  1.00  0.00           H  
ATOM   4422  N   LYS A 302     -37.737  38.431  -0.604  1.00102.58           N  
ANISOU 4422  N   LYS A 302     9986  14145  14845   -421   2257  -2900
ATOM   4423  CA  LYS A 302     -38.438  37.927   0.576  1.00102.99           C  
ANISOU 4423  CA  LYS A 302     9898  14399  14836   -611   2606  -3157
ATOM   4424  C   LYS A 302     -39.216  39.040   1.308  1.00105.23           C  
ANISOU 4424  C   LYS A 302     9936  14630  15415   -343   2836  -3416
ATOM   4425  O   LYS A 302     -40.297  38.748   1.817  1.00105.98           O  
ANISOU 4425  O   LYS A 302     9674  14963  15630   -377   3065  -3625
ATOM   4426  CB  LYS A 302     -37.445  37.186   1.502  1.00105.17           C  
ANISOU 4426  CB  LYS A 302    10602  14617  14742   -930   2769  -3183
ATOM   4427  CG  LYS A 302     -38.109  36.457   2.688  1.00106.53           C  
ANISOU 4427  CG  LYS A 302    10706  15018  14754  -1232   3092  -3392
ATOM   4428  CD  LYS A 302     -37.128  35.862   3.710  1.00104.65           C  
ANISOU 4428  CD  LYS A 302    10921  14668  14173  -1498   3251  -3430
ATOM   4429  CE  LYS A 302     -36.224  34.758   3.145  1.00104.66           C  
ANISOU 4429  CE  LYS A 302    11258  14611  13896  -1694   3030  -3172
ATOM   4430  NZ  LYS A 302     -35.392  34.150   4.198  1.00103.39           N1+
ANISOU 4430  NZ  LYS A 302    11526  14328  13430  -1909   3123  -3174
ATOM   4431  H   LYS A 302     -36.747  38.609  -0.494  1.00  0.00           H  
ATOM   4432  HA  LYS A 302     -39.174  37.193   0.240  1.00  0.00           H  
ATOM   4433  HB3 LYS A 302     -36.700  37.885   1.881  1.00  0.00           H  
ATOM   4434  HB2 LYS A 302     -36.896  36.455   0.907  1.00  0.00           H  
ATOM   4435  HG3 LYS A 302     -38.754  35.669   2.301  1.00  0.00           H  
ATOM   4436  HG2 LYS A 302     -38.762  37.140   3.231  1.00  0.00           H  
ATOM   4437  HD3 LYS A 302     -37.701  35.465   4.549  1.00  0.00           H  
ATOM   4438  HD2 LYS A 302     -36.511  36.663   4.121  1.00  0.00           H  
ATOM   4439  HE3 LYS A 302     -35.576  35.162   2.368  1.00  0.00           H  
ATOM   4440  HE2 LYS A 302     -36.826  33.972   2.688  1.00  0.00           H  
ATOM   4441  HZ1 LYS A 302     -34.841  33.398   3.806  1.00  0.00           H  
ATOM   4442  HZ2 LYS A 302     -34.784  34.847   4.602  1.00  0.00           H  
ATOM   4443  HZ3 LYS A 302     -35.992  33.768   4.916  1.00  0.00           H  
ATOM   4444  N   ILE A 303     -38.687  40.283   1.332  1.00104.46           N  
ANISOU 4444  N   ILE A 303    10025  14221  15444    -84   2789  -3414
ATOM   4445  CA  ILE A 303     -39.345  41.447   1.947  1.00105.45           C  
ANISOU 4445  CA  ILE A 303     9983  14221  15862    207   3014  -3668
ATOM   4446  C   ILE A 303     -40.684  41.784   1.259  1.00106.99           C  
ANISOU 4446  C   ILE A 303     9615  14580  16455    502   2940  -3705
ATOM   4447  O   ILE A 303     -41.673  41.990   1.963  1.00107.71           O  
ANISOU 4447  O   ILE A 303     9369  14824  16730    572   3244  -3985
ATOM   4448  CB  ILE A 303     -38.454  42.740   1.983  1.00105.84           C  
ANISOU 4448  CB  ILE A 303    10388  13862  15964    422   2912  -3611
ATOM   4449  CG1 ILE A 303     -37.135  42.585   2.780  1.00103.39           C  
ANISOU 4449  CG1 ILE A 303    10600  13421  15264    113   2987  -3590
ATOM   4450  CG2 ILE A 303     -39.188  43.999   2.507  1.00110.11           C  
ANISOU 4450  CG2 ILE A 303    10767  14215  16854    780   3112  -3861
ATOM   4451  CD1 ILE A 303     -37.230  41.799   4.096  1.00104.99           C  
ANISOU 4451  CD1 ILE A 303    10914  13781  15199   -220   3351  -3824
ATOM   4452  H   ILE A 303     -37.783  40.448   0.911  1.00  0.00           H  
ATOM   4453  HA  ILE A 303     -39.590  41.168   2.973  1.00  0.00           H  
ATOM   4454  HB  ILE A 303     -38.161  42.966   0.958  1.00  0.00           H  
ATOM   4455 HG13 ILE A 303     -36.699  43.564   2.983  1.00  0.00           H  
ATOM   4456 HG12 ILE A 303     -36.395  42.113   2.148  1.00  0.00           H  
ATOM   4457 HG21 ILE A 303     -38.519  44.858   2.553  1.00  0.00           H  
ATOM   4458 HG22 ILE A 303     -40.016  44.302   1.866  1.00  0.00           H  
ATOM   4459 HG23 ILE A 303     -39.584  43.836   3.510  1.00  0.00           H  
ATOM   4460 HD11 ILE A 303     -36.352  41.979   4.716  1.00  0.00           H  
ATOM   4461 HD12 ILE A 303     -38.107  42.091   4.675  1.00  0.00           H  
ATOM   4462 HD13 ILE A 303     -37.286  40.726   3.912  1.00  0.00           H  
ATOM   4463  N   LEU A 304     -40.701  41.797  -0.088  1.00112.58           N  
ANISOU 4463  N   LEU A 304    10212  15283  17282    651   2534  -3421
ATOM   4464  CA  LEU A 304     -41.914  42.039  -0.876  1.00115.67           C  
ANISOU 4464  CA  LEU A 304    10061  15843  18045    929   2377  -3400
ATOM   4465  C   LEU A 304     -42.905  40.859  -0.851  1.00117.55           C  
ANISOU 4465  C   LEU A 304     9911  16526  18225    661   2492  -3487
ATOM   4466  O   LEU A 304     -44.102  41.100  -1.003  1.00121.61           O  
ANISOU 4466  O   LEU A 304     9891  17253  19064    854   2518  -3597
ATOM   4467  CB  LEU A 304     -41.539  42.512  -2.305  1.00114.48           C  
ANISOU 4467  CB  LEU A 304     9950  15560  17987   1117   1886  -3052
ATOM   4468  CG  LEU A 304     -40.972  41.447  -3.277  1.00111.46           C  
ANISOU 4468  CG  LEU A 304     9707  15338  17307    804   1610  -2781
ATOM   4469  CD1 LEU A 304     -42.064  40.598  -3.967  1.00114.60           C  
ANISOU 4469  CD1 LEU A 304     9610  16079  17853    799   1416  -2707
ATOM   4470  CD2 LEU A 304     -40.042  42.097  -4.317  1.00108.45           C  
ANISOU 4470  CD2 LEU A 304     9714  14657  16834    882   1281  -2496
ATOM   4471  H   LEU A 304     -39.850  41.622  -0.605  1.00  0.00           H  
ATOM   4472  HA  LEU A 304     -42.430  42.879  -0.407  1.00  0.00           H  
ATOM   4473  HB3 LEU A 304     -40.804  43.311  -2.191  1.00  0.00           H  
ATOM   4474  HB2 LEU A 304     -42.401  42.994  -2.768  1.00  0.00           H  
ATOM   4475  HG  LEU A 304     -40.348  40.777  -2.692  1.00  0.00           H  
ATOM   4476 HD11 LEU A 304     -41.998  40.635  -5.055  1.00  0.00           H  
ATOM   4477 HD12 LEU A 304     -41.978  39.551  -3.675  1.00  0.00           H  
ATOM   4478 HD13 LEU A 304     -43.071  40.927  -3.708  1.00  0.00           H  
ATOM   4479 HD21 LEU A 304     -39.910  41.473  -5.201  1.00  0.00           H  
ATOM   4480 HD22 LEU A 304     -40.427  43.062  -4.649  1.00  0.00           H  
ATOM   4481 HD23 LEU A 304     -39.050  42.268  -3.897  1.00  0.00           H  
ATOM   4482  N   LEU A 305     -42.408  39.622  -0.659  1.00114.13           N  
ANISOU 4482  N   LEU A 305     9741  16229  17393    223   2549  -3433
ATOM   4483  CA  LEU A 305     -43.236  38.415  -0.608  1.00115.56           C  
ANISOU 4483  CA  LEU A 305     9631  16803  17472    -90   2653  -3502
ATOM   4484  C   LEU A 305     -43.946  38.250   0.747  1.00118.72           C  
ANISOU 4484  C   LEU A 305     9853  17381  17876   -229   3132  -3856
ATOM   4485  O   LEU A 305     -45.109  37.848   0.768  1.00122.65           O  
ANISOU 4485  O   LEU A 305     9858  18214  18530   -282   3243  -3991
ATOM   4486  CB  LEU A 305     -42.371  37.178  -0.942  1.00111.43           C  
ANISOU 4486  CB  LEU A 305     9494  16315  16528   -494   2537  -3311
ATOM   4487  CG  LEU A 305     -43.174  35.953  -1.424  1.00112.39           C  
ANISOU 4487  CG  LEU A 305     9345  16782  16574   -764   2436  -3247
ATOM   4488  CD1 LEU A 305     -43.797  36.185  -2.818  1.00114.63           C  
ANISOU 4488  CD1 LEU A 305     9342  17122  17092   -534   2026  -3031
ATOM   4489  CD2 LEU A 305     -42.324  34.673  -1.390  1.00108.22           C  
ANISOU 4489  CD2 LEU A 305     9260  16235  15625  -1160   2397  -3107
ATOM   4490  H   LEU A 305     -41.412  39.492  -0.549  1.00  0.00           H  
ATOM   4491  HA  LEU A 305     -44.005  38.513  -1.376  1.00  0.00           H  
ATOM   4492  HB3 LEU A 305     -41.757  36.924  -0.075  1.00  0.00           H  
ATOM   4493  HB2 LEU A 305     -41.672  37.423  -1.737  1.00  0.00           H  
ATOM   4494  HG  LEU A 305     -43.987  35.790  -0.716  1.00  0.00           H  
ATOM   4495 HD11 LEU A 305     -43.566  35.379  -3.515  1.00  0.00           H  
ATOM   4496 HD12 LEU A 305     -44.883  36.244  -2.746  1.00  0.00           H  
ATOM   4497 HD13 LEU A 305     -43.452  37.113  -3.276  1.00  0.00           H  
ATOM   4498 HD21 LEU A 305     -42.957  33.810  -1.184  1.00  0.00           H  
ATOM   4499 HD22 LEU A 305     -41.810  34.491  -2.334  1.00  0.00           H  
ATOM   4500 HD23 LEU A 305     -41.567  34.707  -0.606  1.00  0.00           H  
ATOM   4501  N   PHE A 306     -43.232  38.562   1.844  1.00116.51           N  
ANISOU 4501  N   PHE A 306     9964  16900  17404   -323   3415  -4010
ATOM   4502  CA  PHE A 306     -43.668  38.378   3.232  1.00119.58           C  
ANISOU 4502  CA  PHE A 306    10261  17446  17728   -514   3895  -4352
ATOM   4503  C   PHE A 306     -43.593  39.767   3.834  1.00122.01           C  
ANISOU 4503  C   PHE A 306    10540  17530  18290   -176   4147  -4607
ATOM   4504  O   PHE A 306     -43.278  39.982   5.004  1.00121.15           O  
ANISOU 4504  O   PHE A 306    10878  17176  17979   -253   4310  -4689
ATOM   4505  CB  PHE A 306     -42.765  37.350   3.969  1.00117.41           C  
ANISOU 4505  CB  PHE A 306    10485  17172  16955   -999   4048  -4340
ATOM   4506  CG  PHE A 306     -42.570  35.986   3.316  1.00114.58           C  
ANISOU 4506  CG  PHE A 306    10238  16964  16334  -1322   3814  -4096
ATOM   4507  CD1 PHE A 306     -41.361  35.289   3.527  1.00110.28           C  
ANISOU 4507  CD1 PHE A 306    10235  16259  15405  -1585   3725  -3924
ATOM   4508  CD2 PHE A 306     -43.625  35.326   2.646  1.00116.52           C  
ANISOU 4508  CD2 PHE A 306    10044  17508  16721  -1363   3685  -4044
ATOM   4509  CE1 PHE A 306     -41.190  34.012   3.014  1.00107.97           C  
ANISOU 4509  CE1 PHE A 306    10067  16068  14887  -1858   3529  -3715
ATOM   4510  CE2 PHE A 306     -43.433  34.049   2.134  1.00114.19           C  
ANISOU 4510  CE2 PHE A 306     9896  17321  16171  -1676   3482  -3834
ATOM   4511  CZ  PHE A 306     -42.221  33.396   2.321  1.00109.92           C  
ANISOU 4511  CZ  PHE A 306     9918  16587  15261  -1913   3421  -3680
ATOM   4512  H   PHE A 306     -42.263  38.831   1.729  1.00  0.00           H  
ATOM   4513  HA  PHE A 306     -44.703  38.035   3.283  1.00  0.00           H  
ATOM   4514  HXT PHE A 306     -43.848  40.588   3.161  1.00  0.00           H  
ATOM   4515  HB3 PHE A 306     -43.151  37.176   4.974  1.00  0.00           H  
ATOM   4516  HB2 PHE A 306     -41.770  37.780   4.103  1.00  0.00           H  
ATOM   4517  HD1 PHE A 306     -40.562  35.749   4.089  1.00  0.00           H  
ATOM   4518  HD2 PHE A 306     -44.584  35.806   2.518  1.00  0.00           H  
ATOM   4519  HE1 PHE A 306     -40.257  33.489   3.167  1.00  0.00           H  
ATOM   4520  HE2 PHE A 306     -44.235  33.553   1.607  1.00  0.00           H  
ATOM   4521  HZ  PHE A 306     -42.082  32.393   1.951  1.00  0.00           H  
CONECT 3719 3725
CONECT 3725 3719
CONECT 4503 4514
CONECT 4514 4503
END   


A second structure was input as follows:


CRYST1   85.437   83.463   49.922  90.00  90.00  90.00 P 21 21 2     1
ATOM      1  N   ASP A   2      35.966  22.437  50.076  1.00 62.41           N  
ATOM      2  CA  ASP A   2      36.247  23.663  49.275  1.00 62.22           C  
ATOM      3  C   ASP A   2      37.418  23.421  48.325  1.00 62.21           C  
ATOM      4  O   ASP A   2      37.717  24.251  47.463  1.00 62.54           O  
ATOM      5  CB  ASP A   2      36.576  24.833  50.207  1.00 61.13           C  
ATOM      6  N   GLN A   3      38.068  22.272  48.488  1.00 61.37           N  
ATOM      7  CA  GLN A   3      39.219  21.903  47.674  1.00 59.74           C  
ATOM      8  C   GLN A   3      38.999  22.135  46.188  1.00 57.93           C  
ATOM      9  O   GLN A   3      38.033  21.643  45.602  1.00 57.41           O  
ATOM     10  CB  GLN A   3      39.581  20.434  47.906  1.00 61.07           C  
ATOM     11  CG  GLN A   3      39.681  20.044  49.373  1.00 64.84           C  
ATOM     12  CD  GLN A   3      40.526  21.012  50.186  1.00 66.77           C  
ATOM     13  OE1 GLN A   3      40.178  22.185  50.337  1.00 67.89           O  
ATOM     14  NE2 GLN A   3      41.642  20.523  50.714  1.00 68.50           N  
ATOM     15  N   ALA A   4      39.904  22.898  45.585  1.00 55.40           N  
ATOM     16  CA  ALA A   4      39.827  23.180  44.163  1.00 52.01           C  
ATOM     17  C   ALA A   4      39.940  21.833  43.469  1.00 49.78           C  
ATOM     18  O   ALA A   4      39.311  21.591  42.441  1.00 48.84           O  
ATOM     19  CB  ALA A   4      40.976  24.087  43.748  1.00 52.31           C  
ATOM     20  N   LEU A   5      40.741  20.955  44.066  1.00 48.05           N  
ATOM     21  CA  LEU A   5      40.973  19.616  43.540  1.00 47.15           C  
ATOM     22  C   LEU A   5      39.687  18.796  43.463  1.00 46.31           C  
ATOM     23  O   LEU A   5      39.421  18.137  42.454  1.00 44.55           O  
ATOM     24  CB  LEU A   5      41.995  18.882  44.411  1.00 45.58           C  
ATOM     25  CG  LEU A   5      42.366  17.458  43.987  1.00 46.57           C  
ATOM     26  CD1 LEU A   5      42.955  17.465  42.584  1.00 46.06           C  
ATOM     27  CD2 LEU A   5      43.366  16.883  44.981  1.00 48.68           C  
ATOM     28  N   SER A   6      38.900  18.831  44.537  1.00 45.65           N  
ATOM     29  CA  SER A   6      37.644  18.095  44.581  1.00 45.03           C  
ATOM     30  C   SER A   6      36.720  18.611  43.479  1.00 43.39           C  
ATOM     31  O   SER A   6      36.094  17.831  42.764  1.00 42.53           O  
ATOM     32  CB  SER A   6      36.982  18.268  45.949  1.00 46.59           C  
ATOM     33  OG  SER A   6      36.714  19.635  46.208  1.00 49.56           O  
ATOM     34  N   PHE A   7      36.648  19.932  43.345  1.00 42.64           N  
ATOM     35  CA  PHE A   7      35.819  20.557  42.326  1.00 42.95           C  
ATOM     36  C   PHE A   7      36.242  20.101  40.925  1.00 42.15           C  
ATOM     37  O   PHE A   7      35.401  19.834  40.062  1.00 40.20           O  
ATOM     38  CB  PHE A   7      35.940  22.076  42.414  1.00 46.71           C  
ATOM     39  CG  PHE A   7      35.223  22.800  41.313  1.00 49.84           C  
ATOM     40  CD1 PHE A   7      33.852  23.028  41.389  1.00 52.48           C  
ATOM     41  CD2 PHE A   7      35.911  23.215  40.176  1.00 51.98           C  
ATOM     42  CE1 PHE A   7      33.172  23.659  40.344  1.00 53.93           C  
ATOM     43  CE2 PHE A   7      35.244  23.845  39.123  1.00 54.10           C  
ATOM     44  CZ  PHE A   7      33.870  24.067  39.208  1.00 54.84           C  
ATOM     45  N   LEU A   8      37.552  20.022  40.703  1.00 39.92           N  
ATOM     46  CA  LEU A   8      38.080  19.610  39.411  1.00 38.53           C  
ATOM     47  C   LEU A   8      37.711  18.158  39.136  1.00 37.21           C  
ATOM     48  O   LEU A   8      37.334  17.803  38.019  1.00 34.12           O  
ATOM     49  CB  LEU A   8      39.599  19.777  39.383  1.00 39.95           C  
ATOM     50  CG  LEU A   8      40.194  20.284  38.067  1.00 43.04           C  
ATOM     51  CD1 LEU A   8      39.806  19.354  36.931  1.00 42.92           C  
ATOM     52  CD2 LEU A   8      39.695  21.702  37.793  1.00 43.94           C  
ATOM     53  N   LYS A   9      37.820  17.327  40.168  1.00 37.35           N  
ATOM     54  CA  LYS A   9      37.490  15.913  40.063  1.00 37.97           C  
ATOM     55  C   LYS A   9      36.023  15.750  39.689  1.00 36.74           C  
ATOM     56  O   LYS A   9      35.679  14.930  38.840  1.00 36.61           O  
ATOM     57  CB  LYS A   9      37.747  15.195  41.393  1.00 40.11           C  
ATOM     58  CG  LYS A   9      39.212  15.111  41.808  1.00 46.09           C  
ATOM     59  CD  LYS A   9      39.355  14.397  43.151  1.00 47.65           C  
ATOM     60  CE  LYS A   9      40.802  14.353  43.614  1.00 50.95           C  
ATOM     61  NZ  LYS A   9      40.945  13.695  44.944  1.00 52.80           N1+
ATOM     62  N   ASP A  10      35.158  16.521  40.340  1.00 36.51           N  
ATOM     63  CA  ASP A  10      33.729  16.446  40.056  1.00 36.68           C  
ATOM     64  C   ASP A  10      33.502  16.905  38.623  1.00 34.51           C  
ATOM     65  O   ASP A  10      32.812  16.248  37.845  1.00 33.24           O  
ATOM     66  CB  ASP A  10      32.929  17.344  41.014  1.00 39.79           C  
ATOM     67  CG  ASP A  10      33.058  16.919  42.468  1.00 44.07           C  
ATOM     68  OD1 ASP A  10      32.884  15.718  42.759  1.00 48.18           O  
ATOM     69  OD2 ASP A  10      33.326  17.785  43.326  1.00 47.45           O1-
ATOM     70  N   PHE A  11      34.105  18.037  38.284  1.00 33.18           N  
ATOM     71  CA  PHE A  11      33.979  18.613  36.954  1.00 34.22           C  
ATOM     72  C   PHE A  11      34.334  17.612  35.858  1.00 33.11           C  
ATOM     73  O   PHE A  11      33.573  17.426  34.907  1.00 33.41           O  
ATOM     74  CB  PHE A  11      34.875  19.845  36.834  1.00 33.95           C  
ATOM     75  CG  PHE A  11      34.753  20.551  35.521  1.00 36.44           C  
ATOM     76  CD1 PHE A  11      33.602  21.262  35.206  1.00 38.04           C  
ATOM     77  CD2 PHE A  11      35.779  20.494  34.592  1.00 36.89           C  
ATOM     78  CE1 PHE A  11      33.479  21.909  33.979  1.00 38.86           C  
ATOM     79  CE2 PHE A  11      35.664  21.138  33.363  1.00 39.42           C  
ATOM     80  CZ  PHE A  11      34.511  21.847  33.056  1.00 37.56           C  
ATOM     81  N   LEU A  12      35.484  16.959  36.002  1.00 31.59           N  
ATOM     82  CA  LEU A  12      35.936  15.986  35.012  1.00 31.44           C  
ATOM     83  C   LEU A  12      35.046  14.749  34.975  1.00 30.85           C  
ATOM     84  O   LEU A  12      34.747  14.223  33.900  1.00 30.75           O  
ATOM     85  CB  LEU A  12      37.378  15.568  35.297  1.00 31.65           C  
ATOM     86  CG  LEU A  12      38.397  16.708  35.422  1.00 34.32           C  
ATOM     87  CD1 LEU A  12      39.801  16.114  35.517  1.00 35.21           C  
ATOM     88  CD2 LEU A  12      38.297  17.649  34.228  1.00 33.81           C  
ATOM     89  N   ALA A  13      34.629  14.285  36.149  1.00 28.98           N  
ATOM     90  CA  ALA A  13      33.766  13.113  36.241  1.00 29.19           C  
ATOM     91  C   ALA A  13      32.447  13.369  35.504  1.00 29.05           C  
ATOM     92  O   ALA A  13      31.918  12.487  34.831  1.00 28.70           O  
ATOM     93  CB  ALA A  13      33.493  12.778  37.704  1.00 29.65           C  
ATOM     94  N   GLY A  14      31.917  14.579  35.650  1.00 29.91           N  
ATOM     95  CA  GLY A  14      30.681  14.923  34.978  1.00 30.34           C  
ATOM     96  C   GLY A  14      30.893  14.900  33.475  1.00 31.66           C  
ATOM     97  O   GLY A  14      30.034  14.432  32.725  1.00 30.34           O  
ATOM     98  N   GLY A  15      32.046  15.406  33.041  1.00 29.83           N  
ATOM     99  CA  GLY A  15      32.366  15.427  31.626  1.00 28.96           C  
ATOM    100  C   GLY A  15      32.551  14.025  31.084  1.00 29.65           C  
ATOM    101  O   GLY A  15      32.260  13.756  29.920  1.00 27.80           O  
ATOM    102  N   VAL A  16      33.036  13.120  31.928  1.00 30.35           N  
ATOM    103  CA  VAL A  16      33.236  11.741  31.506  1.00 30.10           C  
ATOM    104  C   VAL A  16      31.887  11.050  31.344  1.00 28.67           C  
ATOM    105  O   VAL A  16      31.654  10.352  30.355  1.00 27.33           O  
ATOM    106  CB  VAL A  16      34.079  10.952  32.525  1.00 32.50           C  
ATOM    107  CG1 VAL A  16      34.177   9.491  32.100  1.00 31.70           C  
ATOM    108  CG2 VAL A  16      35.474  11.565  32.629  1.00 33.55           C  
ATOM    109  N   ALA A  17      31.003  11.253  32.319  1.00 26.87           N  
ATOM    110  CA  ALA A  17      29.671  10.655  32.289  1.00 26.32           C  
ATOM    111  C   ALA A  17      28.901  11.135  31.057  1.00 25.67           C  
ATOM    112  O   ALA A  17      28.340  10.328  30.314  1.00 25.61           O  
ATOM    113  CB  ALA A  17      28.893  11.013  33.568  1.00 23.71           C  
ATOM    114  N   ALA A  18      28.884  12.447  30.839  1.00 23.72           N  
ATOM    115  CA  ALA A  18      28.178  13.009  29.689  1.00 24.70           C  
ATOM    116  C   ALA A  18      28.746  12.476  28.368  1.00 24.76           C  
ATOM    117  O   ALA A  18      27.995  12.211  27.423  1.00 24.22           O  
ATOM    118  CB  ALA A  18      28.255  14.536  29.717  1.00 22.39           C  
ATOM    119  N   ALA A  19      30.067  12.313  28.318  1.00 23.19           N  
ATOM    120  CA  ALA A  19      30.741  11.823  27.121  1.00 24.97           C  
ATOM    121  C   ALA A  19      30.390  10.370  26.820  1.00 25.49           C  
ATOM    122  O   ALA A  19      30.293   9.966  25.659  1.00 24.85           O  
ATOM    123  CB  ALA A  19      32.253  11.972  27.275  1.00 23.29           C  
ATOM    124  N   ILE A  20      30.207   9.582  27.870  1.00 26.91           N  
ATOM    125  CA  ILE A  20      29.870   8.177  27.700  1.00 28.39           C  
ATOM    126  C   ILE A  20      28.436   7.964  27.229  1.00 26.57           C  
ATOM    127  O   ILE A  20      28.195   7.230  26.276  1.00 28.52           O  
ATOM    128  CB  ILE A  20      30.129   7.388  29.011  1.00 29.82           C  
ATOM    129  CG1 ILE A  20      31.639   7.148  29.152  1.00 31.26           C  
ATOM    130  CG2 ILE A  20      29.356   6.065  29.006  1.00 28.32           C  
ATOM    131  CD1 ILE A  20      32.063   6.551  30.479  1.00 34.15           C  
ATOM    132  N   SER A  21      27.480   8.607  27.882  1.00 27.96           N  
ATOM    133  CA  SER A  21      26.092   8.439  27.484  1.00 29.15           C  
ATOM    134  C   SER A  21      25.818   8.973  26.076  1.00 28.90           C  
ATOM    135  O   SER A  21      25.131   8.322  25.289  1.00 28.68           O  
ATOM    136  CB  SER A  21      25.170   9.115  28.498  1.00 30.24           C  
ATOM    137  OG  SER A  21      25.673  10.382  28.857  1.00 36.52           O  
ATOM    138  N   LYS A  22      26.363  10.144  25.748  1.00 28.47           N  
ATOM    139  CA  LYS A  22      26.138  10.717  24.421  1.00 29.05           C  
ATOM    140  C   LYS A  22      26.814   9.894  23.336  1.00 26.60           C  
ATOM    141  O   LYS A  22      26.261   9.720  22.244  1.00 26.23           O  
ATOM    142  CB  LYS A  22      26.623  12.170  24.361  1.00 29.80           C  
ATOM    143  CG  LYS A  22      25.797  13.119  25.224  1.00 33.55           C  
ATOM    144  CD  LYS A  22      26.193  14.566  24.987  1.00 37.61           C  
ATOM    145  CE  LYS A  22      25.275  15.519  25.737  1.00 43.56           C  
ATOM    146  NZ  LYS A  22      25.583  16.960  25.442  1.00 47.16           N1+
ATOM    147  N   THR A  23      28.004   9.381  23.628  1.00 24.28           N  
ATOM    148  CA  THR A  23      28.703   8.561  22.649  1.00 24.36           C  
ATOM    149  C   THR A  23      27.910   7.266  22.468  1.00 25.75           C  
ATOM    150  O   THR A  23      27.785   6.740  21.358  1.00 23.74           O  
ATOM    151  CB  THR A  23      30.142   8.225  23.114  1.00 26.72           C  
ATOM    152  OG1 THR A  23      30.940   9.418  23.110  1.00 27.57           O  
ATOM    153  CG2 THR A  23      30.782   7.186  22.189  1.00 23.80           C  
ATOM    154  N   ALA A  24      27.362   6.767  23.572  1.00 25.96           N  
ATOM    155  CA  ALA A  24      26.585   5.539  23.548  1.00 27.05           C  
ATOM    156  C   ALA A  24      25.361   5.626  22.632  1.00 26.98           C  
ATOM    157  O   ALA A  24      25.082   4.691  21.886  1.00 26.65           O  
ATOM    158  CB  ALA A  24      26.154   5.170  24.959  1.00 26.97           C  
ATOM    159  N   VAL A  25      24.634   6.742  22.686  1.00 25.44           N  
ATOM    160  CA  VAL A  25      23.441   6.903  21.859  1.00 25.27           C  
ATOM    161  C   VAL A  25      23.662   7.703  20.570  1.00 25.42           C  
ATOM    162  O   VAL A  25      22.703   8.066  19.892  1.00 24.75           O  
ATOM    163  CB  VAL A  25      22.282   7.562  22.667  1.00 27.60           C  
ATOM    164  CG1 VAL A  25      21.894   6.667  23.843  1.00 25.70           C  
ATOM    165  CG2 VAL A  25      22.698   8.946  23.165  1.00 23.96           C  
ATOM    166  N   ALA A  26      24.921   7.963  20.230  1.00 24.98           N  
ATOM    167  CA  ALA A  26      25.248   8.716  19.022  1.00 26.31           C  
ATOM    168  C   ALA A  26      24.682   8.068  17.753  1.00 25.95           C  
ATOM    169  O   ALA A  26      24.241   8.764  16.843  1.00 25.52           O  
ATOM    170  CB  ALA A  26      26.772   8.882  18.900  1.00 25.62           C  
ATOM    171  N   PRO A  27      24.703   6.727  17.669  1.00 26.04           N  
ATOM    172  CA  PRO A  27      24.167   6.068  16.471  1.00 25.19           C  
ATOM    173  C   PRO A  27      22.699   6.415  16.238  1.00 25.20           C  
ATOM    174  O   PRO A  27      22.313   6.809  15.136  1.00 25.07           O  
ATOM    175  CB  PRO A  27      24.366   4.581  16.775  1.00 25.51           C  
ATOM    176  CG  PRO A  27      25.617   4.579  17.614  1.00 23.86           C  
ATOM    177  CD  PRO A  27      25.360   5.746  18.556  1.00 25.57           C  
ATOM    178  N   ILE A  28      21.883   6.273  17.277  1.00 23.64           N  
ATOM    179  CA  ILE A  28      20.466   6.580  17.149  1.00 22.61           C  
ATOM    180  C   ILE A  28      20.268   8.087  16.971  1.00 24.09           C  
ATOM    181  O   ILE A  28      19.306   8.519  16.335  1.00 22.07           O  
ATOM    182  CB  ILE A  28      19.654   6.067  18.375  1.00 22.91           C  
ATOM    183  CG1 ILE A  28      18.155   6.302  18.155  1.00 23.59           C  
ATOM    184  CG2 ILE A  28      20.100   6.768  19.637  1.00 23.54           C  
ATOM    185  CD1 ILE A  28      17.618   5.682  16.871  1.00 26.48           C  
ATOM    186  N   GLU A  29      21.178   8.890  17.522  1.00 23.16           N  
ATOM    187  CA  GLU A  29      21.051  10.328  17.360  1.00 24.26           C  
ATOM    188  C   GLU A  29      21.348  10.698  15.909  1.00 24.73           C  
ATOM    189  O   GLU A  29      20.755  11.633  15.369  1.00 24.59           O  
ATOM    190  CB  GLU A  29      22.001  11.111  18.270  1.00 23.38           C  
ATOM    191  CG  GLU A  29      21.868  12.599  17.981  1.00 25.23           C  
ATOM    192  CD  GLU A  29      22.867  13.475  18.686  1.00 25.79           C  
ATOM    193  OE1 GLU A  29      23.973  13.002  19.020  1.00 28.02           O  
ATOM    194  OE2 GLU A  29      22.542  14.666  18.880  1.00 31.19           O1-
ATOM    195  N   ARG A  30      22.268   9.972  15.279  1.00 22.13           N  
ATOM    196  CA  ARG A  30      22.585  10.255  13.893  1.00 22.30           C  
ATOM    197  C   ARG A  30      21.400   9.916  12.995  1.00 22.63           C  
ATOM    198  O   ARG A  30      21.120  10.629  12.029  1.00 22.30           O  
ATOM    199  CB  ARG A  30      23.817   9.486  13.414  1.00 23.15           C  
ATOM    200  CG  ARG A  30      24.304  10.076  12.106  1.00 23.61           C  
ATOM    201  CD  ARG A  30      25.478   9.371  11.456  1.00 24.37           C  
ATOM    202  NE  ARG A  30      25.728  10.011  10.169  1.00 27.24           N  
ATOM    203  CZ  ARG A  30      26.347   9.443   9.142  1.00 27.85           C  
ATOM    204  NH1 ARG A  30      26.803   8.199   9.243  1.00 26.06           N1+
ATOM    205  NH2 ARG A  30      26.480  10.116   8.004  1.00 23.94           N  
ATOM    206  N   VAL A  31      20.702   8.830  13.314  1.00 22.31           N  
ATOM    207  CA  VAL A  31      19.542   8.438  12.530  1.00 21.86           C  
ATOM    208  C   VAL A  31      18.508   9.555  12.654  1.00 23.28           C  
ATOM    209  O   VAL A  31      17.932   9.998  11.660  1.00 24.31           O  
ATOM    210  CB  VAL A  31      18.960   7.089  13.037  1.00 22.00           C  
ATOM    211  CG1 VAL A  31      17.699   6.731  12.267  1.00 20.34           C  
ATOM    212  CG2 VAL A  31      19.997   5.988  12.856  1.00 19.98           C  
ATOM    213  N   LYS A  32      18.295  10.018  13.882  1.00 22.38           N  
ATOM    214  CA  LYS A  32      17.352  11.091  14.151  1.00 21.63           C  
ATOM    215  C   LYS A  32      17.691  12.309  13.281  1.00 21.66           C  
ATOM    216  O   LYS A  32      16.831  12.837  12.575  1.00 20.97           O  
ATOM    217  CB  LYS A  32      17.404  11.441  15.648  1.00 22.56           C  
ATOM    218  CG  LYS A  32      16.603  12.667  16.083  1.00 21.36           C  
ATOM    219  CD  LYS A  32      17.448  13.923  15.988  1.00 20.47           C  
ATOM    220  CE  LYS A  32      16.756  15.120  16.614  1.00 20.58           C  
ATOM    221  NZ  LYS A  32      17.581  16.345  16.445  1.00 17.33           N1+
ATOM    222  N   LEU A  33      18.949  12.733  13.322  1.00 21.83           N  
ATOM    223  CA  LEU A  33      19.408  13.884  12.543  1.00 22.55           C  
ATOM    224  C   LEU A  33      19.266  13.685  11.027  1.00 19.95           C  
ATOM    225  O   LEU A  33      18.822  14.589  10.319  1.00 21.01           O  
ATOM    226  CB  LEU A  33      20.867  14.215  12.908  1.00 19.37           C  
ATOM    227  CG  LEU A  33      21.035  14.761  14.339  1.00 23.71           C  
ATOM    228  CD1 LEU A  33      22.500  14.715  14.768  1.00 20.09           C  
ATOM    229  CD2 LEU A  33      20.483  16.187  14.408  1.00 19.45           C  
ATOM    230  N   LEU A  34      19.636  12.512  10.530  1.00 20.73           N  
ATOM    231  CA  LEU A  34      19.520  12.241   9.104  1.00 21.82           C  
ATOM    232  C   LEU A  34      18.064  12.342   8.636  1.00 22.49           C  
ATOM    233  O   LEU A  34      17.764  13.016   7.646  1.00 21.45           O  
ATOM    234  CB  LEU A  34      20.106  10.859   8.778  1.00 23.51           C  
ATOM    235  CG  LEU A  34      21.635  10.788   8.630  1.00 23.60           C  
ATOM    236  CD1 LEU A  34      22.059  11.368   7.289  1.00 20.02           C  
ATOM    237  CD2 LEU A  34      22.304  11.570   9.756  1.00 29.94           C  
ATOM    238  N   LEU A  35      17.158  11.687   9.351  1.00 21.98           N  
ATOM    239  CA  LEU A  35      15.746  11.735   8.983  1.00 22.66           C  
ATOM    240  C   LEU A  35      15.215  13.172   9.081  1.00 22.85           C  
ATOM    241  O   LEU A  35      14.444  13.629   8.234  1.00 21.98           O  
ATOM    242  CB  LEU A  35      14.929  10.809   9.898  1.00 19.40           C  
ATOM    243  CG  LEU A  35      15.173   9.303   9.716  1.00 23.24           C  
ATOM    244  CD1 LEU A  35      14.522   8.530  10.855  1.00 23.96           C  
ATOM    245  CD2 LEU A  35      14.614   8.846   8.362  1.00 22.47           C  
ATOM    246  N   GLN A  36      15.654  13.884  10.110  1.00 21.74           N  
ATOM    247  CA  GLN A  36      15.212  15.250  10.341  1.00 21.53           C  
ATOM    248  C   GLN A  36      15.699  16.269   9.299  1.00 23.27           C  
ATOM    249  O   GLN A  36      14.963  17.190   8.947  1.00 23.30           O  
ATOM    250  CB  GLN A  36      15.654  15.690  11.748  1.00 19.74           C  
ATOM    251  CG  GLN A  36      15.121  17.033  12.208  1.00 20.13           C  
ATOM    252  CD  GLN A  36      15.588  17.398  13.620  1.00 23.13           C  
ATOM    253  OE1 GLN A  36      14.810  17.912  14.434  1.00 22.05           O  
ATOM    254  NE2 GLN A  36      16.859  17.145  13.909  1.00 17.27           N  
ATOM    255  N   VAL A  37      16.917  16.096   8.784  1.00 23.30           N  
ATOM    256  CA  VAL A  37      17.460  17.062   7.838  1.00 23.09           C  
ATOM    257  C   VAL A  37      17.796  16.596   6.425  1.00 24.79           C  
ATOM    258  O   VAL A  37      18.196  17.412   5.596  1.00 25.90           O  
ATOM    259  CB  VAL A  37      18.744  17.742   8.416  1.00 24.05           C  
ATOM    260  CG1 VAL A  37      18.499  18.199   9.857  1.00 24.99           C  
ATOM    261  CG2 VAL A  37      19.926  16.791   8.346  1.00 17.86           C  
ATOM    262  N   GLN A  38      17.644  15.310   6.130  1.00 25.09           N  
ATOM    263  CA  GLN A  38      17.998  14.835   4.792  1.00 25.74           C  
ATOM    264  C   GLN A  38      17.274  15.577   3.669  1.00 25.62           C  
ATOM    265  O   GLN A  38      17.753  15.607   2.538  1.00 26.13           O  
ATOM    266  CB  GLN A  38      17.757  13.325   4.664  1.00 23.35           C  
ATOM    267  CG  GLN A  38      16.302  12.894   4.675  1.00 23.67           C  
ATOM    268  CD  GLN A  38      16.154  11.378   4.615  1.00 25.90           C  
ATOM    269  OE1 GLN A  38      16.994  10.680   4.032  1.00 24.97           O  
ATOM    270  NE2 GLN A  38      15.081  10.863   5.208  1.00 24.23           N  
ATOM    271  N   HIS A  39      16.131  16.182   3.977  1.00 27.71           N  
ATOM    272  CA  HIS A  39      15.380  16.926   2.968  1.00 27.55           C  
ATOM    273  C   HIS A  39      16.206  18.119   2.488  1.00 28.39           C  
ATOM    274  O   HIS A  39      16.069  18.556   1.344  1.00 25.98           O  
ATOM    275  CB  HIS A  39      14.051  17.435   3.537  1.00 30.21           C  
ATOM    276  CG  HIS A  39      13.304  18.340   2.602  1.00 33.57           C  
ATOM    277  ND1 HIS A  39      12.660  17.880   1.472  1.00 36.07           N  
ATOM    278  CD2 HIS A  39      13.135  19.685   2.609  1.00 33.34           C  
ATOM    279  CE1 HIS A  39      12.126  18.901   0.824  1.00 33.77           C  
ATOM    280  NE2 HIS A  39      12.400  20.008   1.493  1.00 33.91           N  
ATOM    281  N   ALA A  40      17.062  18.643   3.365  1.00 27.39           N  
ATOM    282  CA  ALA A  40      17.898  19.791   3.022  1.00 27.58           C  
ATOM    283  C   ALA A  40      19.343  19.405   2.732  1.00 28.21           C  
ATOM    284  O   ALA A  40      20.246  20.235   2.826  1.00 28.78           O  
ATOM    285  CB  ALA A  40      17.855  20.820   4.143  1.00 28.00           C  
ATOM    286  N   SER A  41      19.560  18.145   2.377  1.00 28.81           N  
ATOM    287  CA  SER A  41      20.903  17.669   2.079  1.00 30.87           C  
ATOM    288  C   SER A  41      21.228  17.784   0.595  1.00 32.71           C  
ATOM    289  O   SER A  41      20.374  17.545  -0.259  1.00 32.79           O  
ATOM    290  CB  SER A  41      21.059  16.211   2.519  1.00 31.55           C  
ATOM    291  OG  SER A  41      22.270  15.657   2.032  1.00 30.87           O  
ATOM    292  N   LYS A  42      22.472  18.149   0.302  1.00 33.42           N  
ATOM    293  CA  LYS A  42      22.940  18.280  -1.069  1.00 34.67           C  
ATOM    294  C   LYS A  42      23.388  16.942  -1.650  1.00 34.45           C  
ATOM    295  O   LYS A  42      23.431  16.778  -2.866  1.00 35.14           O  
ATOM    296  CB  LYS A  42      24.113  19.255  -1.135  1.00 35.19           C  
ATOM    297  CG  LYS A  42      23.717  20.673  -1.424  1.00 39.26           C  
ATOM    298  CD  LYS A  42      24.943  21.540  -1.592  1.00 42.81           C  
ATOM    299  CE  LYS A  42      24.600  22.792  -2.369  1.00 43.80           C  
ATOM    300  NZ  LYS A  42      23.956  22.415  -3.659  1.00 43.03           N1+
ATOM    301  N   GLN A  43      23.729  15.994  -0.785  1.00 34.23           N  
ATOM    302  CA  GLN A  43      24.201  14.680  -1.234  1.00 35.12           C  
ATOM    303  C   GLN A  43      23.096  13.643  -1.374  1.00 35.24           C  
ATOM    304  O   GLN A  43      23.238  12.672  -2.113  1.00 37.55           O  
ATOM    305  CB  GLN A  43      25.238  14.128  -0.254  1.00 35.60           C  
ATOM    306  CG  GLN A  43      26.456  15.001  -0.016  1.00 36.28           C  
ATOM    307  CD  GLN A  43      27.285  14.498   1.163  1.00 38.99           C  
ATOM    308  OE1 GLN A  43      26.783  14.400   2.285  1.00 40.10           O  
ATOM    309  NE2 GLN A  43      28.554  14.172   0.914  1.00 35.55           N  
ATOM    310  N   ILE A  44      21.997  13.839  -0.657  1.00 35.95           N  
ATOM    311  CA  ILE A  44      20.902  12.881  -0.695  1.00 34.77           C  
ATOM    312  C   ILE A  44      19.793  13.243  -1.671  1.00 35.20           C  
ATOM    313  O   ILE A  44      19.063  14.218  -1.463  1.00 34.73           O  
ATOM    314  CB  ILE A  44      20.276  12.706   0.709  1.00 34.34           C  
ATOM    315  CG1 ILE A  44      21.374  12.369   1.726  1.00 32.77           C  
ATOM    316  CG2 ILE A  44      19.218  11.609   0.673  1.00 33.64           C  
ATOM    317  CD1 ILE A  44      20.889  12.236   3.165  1.00 28.41           C  
ATOM    318  N   SER A  45      19.674  12.457  -2.740  1.00 34.55           N  
ATOM    319  CA  SER A  45      18.625  12.675  -3.728  1.00 34.38           C  
ATOM    320  C   SER A  45      17.358  12.140  -3.077  1.00 34.56           C  
ATOM    321  O   SER A  45      17.430  11.277  -2.200  1.00 32.89           O  
ATOM    322  CB  SER A  45      18.924  11.902  -5.022  1.00 37.07           C  
ATOM    323  OG  SER A  45      18.989  10.500  -4.801  1.00 36.72           O  
ATOM    324  N   ALA A  46      16.203  12.648  -3.494  1.00 35.22           N  
ATOM    325  CA  ALA A  46      14.936  12.214  -2.916  1.00 37.65           C  
ATOM    326  C   ALA A  46      14.777  10.707  -3.008  1.00 39.62           C  
ATOM    327  O   ALA A  46      14.167  10.082  -2.140  1.00 39.34           O  
ATOM    328  CB  ALA A  46      13.770  12.903  -3.621  1.00 39.26           C  
ATOM    329  N   GLU A  47      15.333  10.129  -4.064  1.00 41.33           N  
ATOM    330  CA  GLU A  47      15.251   8.694  -4.284  1.00 44.31           C  
ATOM    331  C   GLU A  47      16.141   7.918  -3.314  1.00 44.37           C  
ATOM    332  O   GLU A  47      15.836   6.782  -2.954  1.00 43.90           O  
ATOM    333  CB  GLU A  47      15.652   8.355  -5.723  1.00 46.94           C  
ATOM    334  CG  GLU A  47      14.835   9.053  -6.803  1.00 52.42           C  
ATOM    335  CD  GLU A  47      15.114  10.542  -6.888  1.00 56.33           C  
ATOM    336  OE1 GLU A  47      14.656  11.293  -6.002  1.00 59.33           O  
ATOM    337  OE2 GLU A  47      15.804  10.965  -7.840  1.00 58.27           O1-
ATOM    338  N   LYS A  48      17.239   8.530  -2.886  1.00 43.64           N  
ATOM    339  CA  LYS A  48      18.149   7.849  -1.972  1.00 42.08           C  
ATOM    340  C   LYS A  48      17.900   8.180  -0.506  1.00 38.94           C  
ATOM    341  O   LYS A  48      18.676   7.788   0.359  1.00 37.33           O  
ATOM    342  CB  LYS A  48      19.597   8.176  -2.337  1.00 44.50           C  
ATOM    343  CG  LYS A  48      19.927   7.919  -3.797  1.00 48.45           C  
ATOM    344  CD  LYS A  48      21.408   8.100  -4.069  1.00 51.68           C  
ATOM    345  CE  LYS A  48      22.198   6.872  -3.652  1.00 53.41           C  
ATOM    346  NZ  LYS A  48      21.852   5.692  -4.499  1.00 55.72           N1+
ATOM    347  N   GLN A  49      16.816   8.895  -0.226  1.00 37.28           N  
ATOM    348  CA  GLN A  49      16.498   9.252   1.151  1.00 36.39           C  
ATOM    349  C   GLN A  49      16.213   8.008   1.992  1.00 36.21           C  
ATOM    350  O   GLN A  49      15.703   7.005   1.485  1.00 36.25           O  
ATOM    351  CB  GLN A  49      15.297  10.210   1.196  1.00 36.66           C  
ATOM    352  CG  GLN A  49      15.694  11.688   1.212  1.00 39.90           C  
ATOM    353  CD  GLN A  49      14.504  12.636   1.289  1.00 42.59           C  
ATOM    354  OE1 GLN A  49      13.535  12.390   2.010  1.00 43.42           O  
ATOM    355  NE2 GLN A  49      14.586  13.740   0.557  1.00 43.59           N  
ATOM    356  N   TYR A  50      16.563   8.073   3.274  1.00 33.73           N  
ATOM    357  CA  TYR A  50      16.328   6.961   4.186  1.00 32.66           C  
ATOM    358  C   TYR A  50      14.828   6.860   4.435  1.00 33.86           C  
ATOM    359  O   TYR A  50      14.170   7.860   4.740  1.00 30.67           O  
ATOM    360  CB  TYR A  50      17.093   7.190   5.494  1.00 30.94           C  
ATOM    361  CG  TYR A  50      18.588   7.249   5.264  1.00 30.42           C  
ATOM    362  CD1 TYR A  50      19.293   6.110   4.880  1.00 29.07           C  
ATOM    363  CD2 TYR A  50      19.281   8.457   5.342  1.00 28.43           C  
ATOM    364  CE1 TYR A  50      20.651   6.173   4.568  1.00 29.17           C  
ATOM    365  CE2 TYR A  50      20.638   8.531   5.034  1.00 30.13           C  
ATOM    366  CZ  TYR A  50      21.314   7.386   4.644  1.00 29.15           C  
ATOM    367  OH  TYR A  50      22.642   7.452   4.306  1.00 30.28           O  
ATOM    368  N   LYS A  51      14.288   5.652   4.288  1.00 34.20           N  
ATOM    369  CA  LYS A  51      12.855   5.438   4.464  1.00 36.23           C  
ATOM    370  C   LYS A  51      12.420   5.395   5.922  1.00 35.25           C  
ATOM    371  O   LYS A  51      11.230   5.489   6.218  1.00 36.60           O  
ATOM    372  CB  LYS A  51      12.417   4.156   3.739  1.00 39.69           C  
ATOM    373  CG  LYS A  51      12.861   4.107   2.275  1.00 44.42           C  
ATOM    374  CD  LYS A  51      12.016   3.168   1.403  1.00 48.13           C  
ATOM    375  CE  LYS A  51      12.036   1.710   1.877  1.00 50.43           C  
ATOM    376  NZ  LYS A  51      11.138   1.465   3.047  1.00 52.59           N1+
ATOM    377  N   GLY A  52      13.381   5.269   6.832  1.00 33.33           N  
ATOM    378  CA  GLY A  52      13.047   5.227   8.245  1.00 30.20           C  
ATOM    379  C   GLY A  52      14.226   4.841   9.120  1.00 29.89           C  
ATOM    380  O   GLY A  52      15.373   4.839   8.672  1.00 28.85           O  
ATOM    381  N   ILE A  53      13.938   4.497  10.369  1.00 28.76           N  
ATOM    382  CA  ILE A  53      14.970   4.119  11.326  1.00 29.11           C  
ATOM    383  C   ILE A  53      15.710   2.858  10.889  1.00 29.69           C  
ATOM    384  O   ILE A  53      16.938   2.846  10.766  1.00 27.32           O  
ATOM    385  CB  ILE A  53      14.349   3.882  12.718  1.00 29.88           C  
ATOM    386  CG1 ILE A  53      13.662   5.167  13.195  1.00 29.54           C  
ATOM    387  CG2 ILE A  53      15.430   3.408  13.705  1.00 30.48           C  
ATOM    388  CD1 ILE A  53      12.902   5.027  14.498  1.00 29.73           C  
ATOM    389  N   ILE A  54      14.943   1.800  10.654  1.00 29.65           N  
ATOM    390  CA  ILE A  54      15.497   0.526  10.242  1.00 30.39           C  
ATOM    391  C   ILE A  54      16.244   0.639   8.926  1.00 29.62           C  
ATOM    392  O   ILE A  54      17.380   0.178   8.812  1.00 31.65           O  
ATOM    393  CB  ILE A  54      14.383  -0.536  10.138  1.00 31.45           C  
ATOM    394  CG1 ILE A  54      13.842  -0.828  11.543  1.00 31.61           C  
ATOM    395  CG2 ILE A  54      14.920  -1.803   9.482  1.00 31.90           C  
ATOM    396  CD1 ILE A  54      12.615  -1.705  11.564  1.00 38.13           C  
ATOM    397  N   ASP A  55      15.613   1.251   7.933  1.00 28.85           N  
ATOM    398  CA  ASP A  55      16.250   1.428   6.640  1.00 29.40           C  
ATOM    399  C   ASP A  55      17.540   2.213   6.829  1.00 29.40           C  
ATOM    400  O   ASP A  55      18.542   1.973   6.157  1.00 30.11           O  
ATOM    401  CB  ASP A  55      15.329   2.198   5.693  1.00 31.49           C  
ATOM    402  CG  ASP A  55      15.969   2.451   4.342  1.00 33.63           C  
ATOM    403  OD1 ASP A  55      16.274   1.466   3.632  1.00 35.52           O  
ATOM    404  OD2 ASP A  55      16.176   3.633   3.990  1.00 34.18           O1-
ATOM    405  N   CYS A  56      17.510   3.157   7.757  1.00 30.31           N  
ATOM    406  CA  CYS A  56      18.672   3.982   8.014  1.00 31.19           C  
ATOM    407  C   CYS A  56      19.799   3.215   8.720  1.00 30.68           C  
ATOM    408  O   CYS A  56      20.942   3.242   8.260  1.00 27.01           O  
ATOM    409  CB  CYS A  56      18.260   5.217   8.828  1.00 31.49           C  
ATOM    410  SG  CYS A  56      19.466   6.559   8.814  1.00 33.18           S  
ATOM    411  N   VAL A  57      19.485   2.517   9.813  1.00 30.58           N  
ATOM    412  CA  VAL A  57      20.521   1.781  10.545  1.00 32.76           C  
ATOM    413  C   VAL A  57      21.174   0.662   9.742  1.00 34.17           C  
ATOM    414  O   VAL A  57      22.355   0.366   9.927  1.00 33.28           O  
ATOM    415  CB  VAL A  57      19.992   1.176  11.870  1.00 33.85           C  
ATOM    416  CG1 VAL A  57      19.389   2.272  12.736  1.00 34.55           C  
ATOM    417  CG2 VAL A  57      18.988   0.076  11.590  1.00 35.06           C  
ATOM    418  N   VAL A  58      20.412   0.040   8.850  1.00 34.82           N  
ATOM    419  CA  VAL A  58      20.949  -1.037   8.027  1.00 35.16           C  
ATOM    420  C   VAL A  58      21.795  -0.504   6.871  1.00 34.93           C  
ATOM    421  O   VAL A  58      22.750  -1.147   6.451  1.00 36.42           O  
ATOM    422  CB  VAL A  58      19.809  -1.925   7.451  1.00 36.72           C  
ATOM    423  CG1 VAL A  58      20.371  -2.905   6.448  1.00 39.93           C  
ATOM    424  CG2 VAL A  58      19.118  -2.680   8.570  1.00 34.62           C  
ATOM    425  N   ARG A  59      21.462   0.680   6.367  1.00 34.74           N  
ATOM    426  CA  ARG A  59      22.203   1.248   5.243  1.00 34.48           C  
ATOM    427  C   ARG A  59      23.527   1.968   5.522  1.00 35.22           C  
ATOM    428  O   ARG A  59      24.486   1.797   4.766  1.00 35.77           O  
ATOM    429  CB  ARG A  59      21.297   2.190   4.446  1.00 34.01           C  
ATOM    430  CG  ARG A  59      20.298   1.494   3.525  1.00 33.60           C  
ATOM    431  CD  ARG A  59      19.297   2.498   2.932  1.00 31.10           C  
ATOM    432  NE  ARG A  59      19.948   3.536   2.136  1.00 30.24           N  
ATOM    433  CZ  ARG A  59      19.327   4.601   1.632  1.00 30.46           C  
ATOM    434  NH1 ARG A  59      18.030   4.779   1.841  1.00 30.89           N1+
ATOM    435  NH2 ARG A  59      20.002   5.488   0.911  1.00 31.22           N  
ATOM    436  N   ILE A  60      23.608   2.763   6.587  1.00 35.04           N  
ATOM    437  CA  ILE A  60      24.849   3.502   6.825  1.00 35.52           C  
ATOM    438  C   ILE A  60      26.108   2.653   7.022  1.00 33.43           C  
ATOM    439  O   ILE A  60      27.182   3.043   6.576  1.00 32.66           O  
ATOM    440  CB  ILE A  60      24.722   4.525   8.002  1.00 37.66           C  
ATOM    441  CG1 ILE A  60      24.966   3.846   9.344  1.00 39.92           C  
ATOM    442  CG2 ILE A  60      23.363   5.207   7.970  1.00 39.28           C  
ATOM    443  CD1 ILE A  60      26.418   3.894   9.787  1.00 43.03           C  
ATOM    444  N   PRO A  61      26.002   1.486   7.688  1.00 33.18           N  
ATOM    445  CA  PRO A  61      27.217   0.682   7.867  1.00 32.91           C  
ATOM    446  C   PRO A  61      27.843   0.256   6.536  1.00 32.97           C  
ATOM    447  O   PRO A  61      29.033   0.451   6.316  1.00 31.68           O  
ATOM    448  CB  PRO A  61      26.732  -0.520   8.681  1.00 33.02           C  
ATOM    449  CG  PRO A  61      25.549   0.027   9.432  1.00 34.63           C  
ATOM    450  CD  PRO A  61      24.860   0.866   8.382  1.00 32.84           C  
ATOM    451  N   LYS A  62      27.042  -0.325   5.648  1.00 35.16           N  
ATOM    452  CA  LYS A  62      27.561  -0.769   4.357  1.00 38.10           C  
ATOM    453  C   LYS A  62      27.779   0.391   3.393  1.00 38.31           C  
ATOM    454  O   LYS A  62      28.582   0.298   2.466  1.00 40.04           O  
ATOM    455  CB  LYS A  62      26.615  -1.792   3.721  1.00 41.57           C  
ATOM    456  CG  LYS A  62      25.251  -1.254   3.335  1.00 45.14           C  
ATOM    457  CD  LYS A  62      24.383  -2.357   2.734  1.00 49.15           C  
ATOM    458  CE  LYS A  62      25.038  -2.992   1.510  1.00 52.27           C  
ATOM    459  NZ  LYS A  62      24.189  -4.074   0.909  1.00 53.23           N1+
ATOM    460  N   GLU A  63      27.065   1.486   3.616  1.00 37.52           N  
ATOM    461  CA  GLU A  63      27.193   2.658   2.760  1.00 37.13           C  
ATOM    462  C   GLU A  63      28.397   3.522   3.119  1.00 35.25           C  
ATOM    463  O   GLU A  63      29.171   3.921   2.255  1.00 34.85           O  
ATOM    464  CB  GLU A  63      25.934   3.519   2.868  1.00 39.20           C  
ATOM    465  CG  GLU A  63      24.967   3.407   1.713  1.00 40.50           C  
ATOM    466  CD  GLU A  63      23.655   4.099   2.016  1.00 44.57           C  
ATOM    467  OE1 GLU A  63      23.685   5.226   2.562  1.00 46.36           O  
ATOM    468  OE2 GLU A  63      22.594   3.517   1.708  1.00 46.68           O1-
ATOM    469  N   GLN A  64      28.558   3.788   4.410  1.00 33.28           N  
ATOM    470  CA  GLN A  64      29.618   4.669   4.867  1.00 31.43           C  
ATOM    471  C   GLN A  64      30.563   4.088   5.919  1.00 30.48           C  
ATOM    472  O   GLN A  64      31.509   4.756   6.341  1.00 31.57           O  
ATOM    473  CB  GLN A  64      28.962   5.947   5.399  1.00 29.94           C  
ATOM    474  CG  GLN A  64      27.820   6.436   4.506  1.00 29.23           C  
ATOM    475  CD  GLN A  64      26.881   7.390   5.218  1.00 30.66           C  
ATOM    476  OE1 GLN A  64      25.701   7.485   4.877  1.00 29.26           O  
ATOM    477  NE2 GLN A  64      27.400   8.107   6.208  1.00 26.54           N  
ATOM    478  N   GLY A  65      30.319   2.850   6.338  1.00 29.64           N  
ATOM    479  CA  GLY A  65      31.170   2.245   7.350  1.00 28.13           C  
ATOM    480  C   GLY A  65      30.519   2.320   8.724  1.00 28.97           C  
ATOM    481  O   GLY A  65      29.920   3.337   9.083  1.00 28.95           O  
ATOM    482  N   PHE A  66      30.644   1.239   9.490  1.00 27.93           N  
ATOM    483  CA  PHE A  66      30.069   1.140  10.828  1.00 27.06           C  
ATOM    484  C   PHE A  66      30.453   2.318  11.711  1.00 27.47           C  
ATOM    485  O   PHE A  66      29.633   2.846  12.457  1.00 28.19           O  
ATOM    486  CB  PHE A  66      30.532  -0.159  11.497  1.00 26.32           C  
ATOM    487  CG  PHE A  66      29.977  -0.361  12.885  1.00 27.13           C  
ATOM    488  CD1 PHE A  66      28.667  -0.786  13.070  1.00 26.68           C  
ATOM    489  CD2 PHE A  66      30.767  -0.113  14.006  1.00 26.32           C  
ATOM    490  CE1 PHE A  66      28.142  -0.964  14.357  1.00 29.94           C  
ATOM    491  CE2 PHE A  66      30.255  -0.287  15.294  1.00 30.96           C  
ATOM    492  CZ  PHE A  66      28.938  -0.714  15.472  1.00 27.92           C  
ATOM    493  N   LEU A  67      31.716   2.709  11.633  1.00 27.97           N  
ATOM    494  CA  LEU A  67      32.228   3.813  12.429  1.00 28.85           C  
ATOM    495  C   LEU A  67      31.466   5.116  12.169  1.00 27.38           C  
ATOM    496  O   LEU A  67      31.357   5.953  13.059  1.00 26.47           O  
ATOM    497  CB  LEU A  67      33.716   4.002  12.128  1.00 31.43           C  
ATOM    498  CG  LEU A  67      34.656   4.221  13.313  1.00 37.68           C  
ATOM    499  CD1 LEU A  67      34.343   3.218  14.416  1.00 36.63           C  
ATOM    500  CD2 LEU A  67      36.100   4.079  12.849  1.00 37.47           C  
ATOM    501  N   SER A  68      30.931   5.277  10.959  1.00 26.34           N  
ATOM    502  CA  SER A  68      30.198   6.494  10.611  1.00 25.96           C  
ATOM    503  C   SER A  68      28.980   6.734  11.507  1.00 25.71           C  
ATOM    504  O   SER A  68      28.396   7.811  11.479  1.00 25.69           O  
ATOM    505  CB  SER A  68      29.770   6.472   9.134  1.00 26.08           C  
ATOM    506  OG  SER A  68      28.659   5.615   8.914  1.00 27.09           O  
ATOM    507  N   PHE A  69      28.586   5.733  12.292  1.00 26.33           N  
ATOM    508  CA  PHE A  69      27.461   5.910  13.210  1.00 26.19           C  
ATOM    509  C   PHE A  69      27.795   7.018  14.210  1.00 25.10           C  
ATOM    510  O   PHE A  69      26.898   7.649  14.768  1.00 25.00           O  
ATOM    511  CB  PHE A  69      27.167   4.624  13.993  1.00 26.73           C  
ATOM    512  CG  PHE A  69      26.165   3.721  13.331  1.00 29.35           C  
ATOM    513  CD1 PHE A  69      24.916   4.209  12.940  1.00 28.90           C  
ATOM    514  CD2 PHE A  69      26.457   2.376  13.120  1.00 28.86           C  
ATOM    515  CE1 PHE A  69      23.974   3.370  12.349  1.00 30.69           C  
ATOM    516  CE2 PHE A  69      25.521   1.526  12.529  1.00 29.94           C  
ATOM    517  CZ  PHE A  69      24.277   2.022  12.143  1.00 30.08           C  
ATOM    518  N   TRP A  70      29.088   7.237  14.439  1.00 21.65           N  
ATOM    519  CA  TRP A  70      29.543   8.267  15.371  1.00 22.69           C  
ATOM    520  C   TRP A  70      30.044   9.515  14.655  1.00 21.47           C  
ATOM    521  O   TRP A  70      30.773  10.322  15.235  1.00 25.35           O  
ATOM    522  CB  TRP A  70      30.655   7.709  16.273  1.00 20.06           C  
ATOM    523  CG  TRP A  70      30.146   6.699  17.252  1.00 22.68           C  
ATOM    524  CD1 TRP A  70      29.699   6.937  18.521  1.00 21.34           C  
ATOM    525  CD2 TRP A  70      29.924   5.306  17.002  1.00 22.25           C  
ATOM    526  NE1 TRP A  70      29.203   5.778  19.076  1.00 22.56           N  
ATOM    527  CE2 TRP A  70      29.328   4.762  18.165  1.00 22.29           C  
ATOM    528  CE3 TRP A  70      30.166   4.464  15.904  1.00 21.84           C  
ATOM    529  CZ2 TRP A  70      28.968   3.411  18.263  1.00 22.74           C  
ATOM    530  CZ3 TRP A  70      29.809   3.125  15.998  1.00 21.99           C  
ATOM    531  CH2 TRP A  70      29.213   2.610  17.174  1.00 23.62           C  
ATOM    532  N   ARG A  71      29.665   9.678  13.393  1.00 22.24           N  
ATOM    533  CA  ARG A  71      30.104  10.849  12.639  1.00 23.22           C  
ATOM    534  C   ARG A  71      29.587  12.134  13.310  1.00 23.53           C  
ATOM    535  O   ARG A  71      28.389  12.289  13.539  1.00 21.17           O  
ATOM    536  CB  ARG A  71      29.619  10.755  11.188  1.00 22.45           C  
ATOM    537  CG  ARG A  71      30.224  11.798  10.252  1.00 24.12           C  
ATOM    538  CD  ARG A  71      29.946  11.455   8.775  1.00 26.19           C  
ATOM    539  NE  ARG A  71      30.708  10.289   8.316  1.00 27.44           N  
ATOM    540  CZ  ARG A  71      30.709   9.825   7.066  1.00 26.54           C  
ATOM    541  NH1 ARG A  71      29.983  10.416   6.123  1.00 24.44           N1+
ATOM    542  NH2 ARG A  71      31.451   8.769   6.753  1.00 27.05           N  
ATOM    543  N   GLY A  72      30.512  13.032  13.641  1.00 23.83           N  
ATOM    544  CA  GLY A  72      30.165  14.290  14.284  1.00 23.98           C  
ATOM    545  C   GLY A  72      30.052  14.204  15.798  1.00 24.51           C  
ATOM    546  O   GLY A  72      29.709  15.189  16.453  1.00 25.09           O  
ATOM    547  N   ASN A  73      30.349  13.035  16.363  1.00 24.88           N  
ATOM    548  CA  ASN A  73      30.237  12.843  17.808  1.00 24.00           C  
ATOM    549  C   ASN A  73      31.296  13.525  18.677  1.00 24.47           C  
ATOM    550  O   ASN A  73      31.092  13.683  19.886  1.00 22.94           O  
ATOM    551  CB  ASN A  73      30.189  11.344  18.148  1.00 23.55           C  
ATOM    552  CG  ASN A  73      30.052  11.092  19.649  1.00 24.52           C  
ATOM    553  OD1 ASN A  73      31.007  10.676  20.316  1.00 25.28           O  
ATOM    554  ND2 ASN A  73      28.867  11.364  20.189  1.00 19.97           N  
ATOM    555  N   LEU A  74      32.417  13.933  18.085  1.00 23.16           N  
ATOM    556  CA  LEU A  74      33.459  14.605  18.866  1.00 24.61           C  
ATOM    557  C   LEU A  74      32.870  15.826  19.568  1.00 23.67           C  
ATOM    558  O   LEU A  74      33.164  16.090  20.734  1.00 24.39           O  
ATOM    559  CB  LEU A  74      34.616  15.064  17.973  1.00 25.60           C  
ATOM    560  CG  LEU A  74      36.033  15.052  18.574  1.00 29.33           C  
ATOM    561  CD1 LEU A  74      36.904  16.072  17.833  1.00 25.62           C  
ATOM    562  CD2 LEU A  74      36.003  15.365  20.048  1.00 25.79           C  
ATOM    563  N   ALA A  75      32.041  16.578  18.850  1.00 24.86           N  
ATOM    564  CA  ALA A  75      31.418  17.761  19.424  1.00 24.58           C  
ATOM    565  C   ALA A  75      30.653  17.374  20.682  1.00 24.96           C  
ATOM    566  O   ALA A  75      30.659  18.113  21.668  1.00 25.42           O  
ATOM    567  CB  ALA A  75      30.479  18.415  18.412  1.00 23.11           C  
ATOM    568  N   ASN A  76      30.001  16.216  20.651  1.00 27.48           N  
ATOM    569  CA  ASN A  76      29.244  15.742  21.811  1.00 28.56           C  
ATOM    570  C   ASN A  76      30.090  15.578  23.078  1.00 28.76           C  
ATOM    571  O   ASN A  76      29.675  16.002  24.153  1.00 30.47           O  
ATOM    572  CB  ASN A  76      28.556  14.398  21.517  1.00 27.94           C  
ATOM    573  CG  ASN A  76      27.250  14.555  20.743  1.00 29.75           C  
ATOM    574  OD1 ASN A  76      26.576  15.585  20.836  1.00 29.30           O  
ATOM    575  ND2 ASN A  76      26.875  13.516  19.993  1.00 26.25           N  
ATOM    576  N   VAL A  77      31.267  14.972  22.964  1.00 26.10           N  
ATOM    577  CA  VAL A  77      32.093  14.755  24.146  1.00 29.74           C  
ATOM    578  C   VAL A  77      32.803  16.003  24.659  1.00 30.91           C  
ATOM    579  O   VAL A  77      33.200  16.052  25.823  1.00 31.26           O  
ATOM    580  CB  VAL A  77      33.160  13.663  23.907  1.00 30.11           C  
ATOM    581  CG1 VAL A  77      32.521  12.450  23.260  1.00 29.26           C  
ATOM    582  CG2 VAL A  77      34.290  14.210  23.051  1.00 35.18           C  
ATOM    583  N   ILE A  78      32.950  17.004  23.794  1.00 30.32           N  
ATOM    584  CA  ILE A  78      33.629  18.254  24.136  1.00 29.99           C  
ATOM    585  C   ILE A  78      32.744  19.337  24.762  1.00 29.35           C  
ATOM    586  O   ILE A  78      33.142  19.988  25.731  1.00 29.29           O  
ATOM    587  CB  ILE A  78      34.292  18.872  22.877  1.00 31.67           C  
ATOM    588  CG1 ILE A  78      35.533  18.071  22.491  1.00 33.41           C  
ATOM    589  CG2 ILE A  78      34.659  20.332  23.123  1.00 31.79           C  
ATOM    590  CD1 ILE A  78      36.081  18.468  21.143  1.00 35.40           C  
ATOM    591  N   ARG A  79      31.559  19.529  24.190  1.00 26.26           N  
ATOM    592  CA  ARG A  79      30.619  20.557  24.626  1.00 25.38           C  
ATOM    593  C   ARG A  79      30.454  20.743  26.125  1.00 23.89           C  
ATOM    594  O   ARG A  79      30.420  21.870  26.605  1.00 23.78           O  
ATOM    595  CB  ARG A  79      29.239  20.316  24.003  1.00 22.62           C  
ATOM    596  CG  ARG A  79      28.503  21.608  23.721  1.00 24.37           C  
ATOM    597  CD  ARG A  79      27.069  21.351  23.313  1.00 24.63           C  
ATOM    598  NE  ARG A  79      26.295  20.860  24.444  1.00 24.22           N  
ATOM    599  CZ  ARG A  79      24.990  20.612  24.406  1.00 26.76           C  
ATOM    600  NH1 ARG A  79      24.307  20.810  23.287  1.00 22.47           N1+
ATOM    601  NH2 ARG A  79      24.370  20.162  25.492  1.00 25.15           N  
ATOM    602  N   TYR A  80      30.336  19.642  26.855  1.00 26.15           N  
ATOM    603  CA  TYR A  80      30.168  19.683  28.304  1.00 28.52           C  
ATOM    604  C   TYR A  80      31.110  20.643  29.037  1.00 28.78           C  
ATOM    605  O   TYR A  80      30.684  21.415  29.891  1.00 27.79           O  
ATOM    606  CB  TYR A  80      30.351  18.277  28.888  1.00 28.84           C  
ATOM    607  CG  TYR A  80      30.478  18.251  30.395  1.00 31.42           C  
ATOM    608  CD1 TYR A  80      31.667  18.624  31.025  1.00 32.35           C  
ATOM    609  CD2 TYR A  80      29.393  17.901  31.198  1.00 34.63           C  
ATOM    610  CE1 TYR A  80      31.769  18.657  32.415  1.00 34.20           C  
ATOM    611  CE2 TYR A  80      29.486  17.928  32.589  1.00 35.40           C  
ATOM    612  CZ  TYR A  80      30.675  18.309  33.188  1.00 34.77           C  
ATOM    613  OH  TYR A  80      30.764  18.356  34.561  1.00 37.33           O  
ATOM    614  N   PHE A  81      32.394  20.574  28.709  1.00 29.57           N  
ATOM    615  CA  PHE A  81      33.398  21.394  29.377  1.00 30.17           C  
ATOM    616  C   PHE A  81      33.170  22.890  29.266  1.00 30.15           C  
ATOM    617  O   PHE A  81      33.048  23.568  30.287  1.00 29.92           O  
ATOM    618  CB  PHE A  81      34.781  20.975  28.888  1.00 28.69           C  
ATOM    619  CG  PHE A  81      35.086  19.530  29.179  1.00 30.10           C  
ATOM    620  CD1 PHE A  81      35.383  19.119  30.478  1.00 29.74           C  
ATOM    621  CD2 PHE A  81      34.982  18.567  28.180  1.00 28.42           C  
ATOM    622  CE1 PHE A  81      35.563  17.770  30.781  1.00 28.72           C  
ATOM    623  CE2 PHE A  81      35.160  17.214  28.469  1.00 28.60           C  
ATOM    624  CZ  PHE A  81      35.450  16.814  29.774  1.00 29.99           C  
ATOM    625  N   PRO A  82      33.111  23.438  28.041  1.00 28.84           N  
ATOM    626  CA  PRO A  82      32.875  24.884  28.028  1.00 29.04           C  
ATOM    627  C   PRO A  82      31.480  25.213  28.592  1.00 29.64           C  
ATOM    628  O   PRO A  82      31.307  26.188  29.330  1.00 28.55           O  
ATOM    629  CB  PRO A  82      33.031  25.255  26.550  1.00 28.82           C  
ATOM    630  CG  PRO A  82      32.686  23.967  25.821  1.00 30.76           C  
ATOM    631  CD  PRO A  82      33.343  22.915  26.683  1.00 29.20           C  
ATOM    632  N   THR A  83      30.495  24.379  28.271  1.00 28.07           N  
ATOM    633  CA  THR A  83      29.131  24.606  28.750  1.00 29.43           C  
ATOM    634  C   THR A  83      29.054  24.739  30.279  1.00 29.90           C  
ATOM    635  O   THR A  83      28.506  25.714  30.800  1.00 28.90           O  
ATOM    636  CB  THR A  83      28.182  23.475  28.282  1.00 29.15           C  
ATOM    637  OG1 THR A  83      28.119  23.469  26.847  1.00 27.29           O  
ATOM    638  CG2 THR A  83      26.791  23.682  28.838  1.00 27.10           C  
ATOM    639  N   GLN A  84      29.608  23.767  30.994  1.00 29.81           N  
ATOM    640  CA  GLN A  84      29.593  23.801  32.453  1.00 32.36           C  
ATOM    641  C   GLN A  84      30.474  24.921  33.014  1.00 32.33           C  
ATOM    642  O   GLN A  84      30.185  25.479  34.075  1.00 32.32           O  
ATOM    643  CB  GLN A  84      30.046  22.453  33.017  1.00 34.44           C  
ATOM    644  CG  GLN A  84      29.106  21.323  32.679  1.00 39.75           C  
ATOM    645  CD  GLN A  84      27.697  21.590  33.163  1.00 43.84           C  
ATOM    646  OE1 GLN A  84      27.460  21.751  34.364  1.00 47.17           O  
ATOM    647  NE2 GLN A  84      26.750  21.645  32.231  1.00 42.95           N  
ATOM    648  N   ALA A  85      31.551  25.246  32.310  1.00 31.84           N  
ATOM    649  CA  ALA A  85      32.427  26.315  32.764  1.00 33.83           C  
ATOM    650  C   ALA A  85      31.607  27.597  32.730  1.00 35.19           C  
ATOM    651  O   ALA A  85      31.629  28.392  33.666  1.00 37.37           O  
ATOM    652  CB  ALA A  85      33.639  26.430  31.848  1.00 34.24           C  
ATOM    653  N   LEU A  86      30.865  27.780  31.644  1.00 36.42           N  
ATOM    654  CA  LEU A  86      30.025  28.953  31.479  1.00 37.40           C  
ATOM    655  C   LEU A  86      28.898  28.999  32.514  1.00 38.28           C  
ATOM    656  O   LEU A  86      28.592  30.065  33.047  1.00 39.89           O  
ATOM    657  CB  LEU A  86      29.461  28.990  30.057  1.00 37.56           C  
ATOM    658  CG  LEU A  86      30.526  29.314  29.003  1.00 40.34           C  
ATOM    659  CD1 LEU A  86      30.016  28.991  27.604  1.00 39.07           C  
ATOM    660  CD2 LEU A  86      30.909  30.783  29.119  1.00 38.52           C  
ATOM    661  N   ASN A  87      28.285  27.855  32.805  1.00 37.70           N  
ATOM    662  CA  ASN A  87      27.217  27.827  33.799  1.00 37.16           C  
ATOM    663  C   ASN A  87      27.761  28.237  35.164  1.00 37.33           C  
ATOM    664  O   ASN A  87      27.085  28.915  35.934  1.00 38.23           O  
ATOM    665  CB  ASN A  87      26.598  26.430  33.912  1.00 35.78           C  
ATOM    666  CG  ASN A  87      25.611  26.133  32.805  1.00 35.82           C  
ATOM    667  OD1 ASN A  87      25.136  27.037  32.117  1.00 37.51           O  
ATOM    668  ND2 ASN A  87      25.282  24.862  32.638  1.00 32.97           N  
ATOM    669  N   PHE A  88      28.988  27.824  35.456  1.00 37.31           N  
ATOM    670  CA  PHE A  88      29.624  28.137  36.733  1.00 38.92           C  
ATOM    671  C   PHE A  88      29.679  29.644  36.987  1.00 37.72           C  
ATOM    672  O   PHE A  88      29.598  30.094  38.123  1.00 36.51           O  
ATOM    673  CB  PHE A  88      31.045  27.564  36.764  1.00 41.72           C  
ATOM    674  CG  PHE A  88      31.749  27.756  38.077  1.00 46.81           C  
ATOM    675  CD1 PHE A  88      31.368  27.024  39.203  1.00 48.90           C  
ATOM    676  CD2 PHE A  88      32.795  28.671  38.194  1.00 48.36           C  
ATOM    677  CE1 PHE A  88      32.020  27.200  40.431  1.00 50.31           C  
ATOM    678  CE2 PHE A  88      33.454  28.856  39.416  1.00 51.31           C  
ATOM    679  CZ  PHE A  88      33.064  28.117  40.537  1.00 50.96           C  
ATOM    680  N   ALA A  89      29.809  30.424  35.921  1.00 37.51           N  
ATOM    681  CA  ALA A  89      29.881  31.868  36.064  1.00 36.20           C  
ATOM    682  C   ALA A  89      28.547  32.582  35.863  1.00 35.37           C  
ATOM    683  O   ALA A  89      28.360  33.691  36.365  1.00 35.32           O  
ATOM    684  CB  ALA A  89      30.915  32.430  35.097  1.00 36.69           C  
ATOM    685  N   PHE A  90      27.615  31.955  35.150  1.00 33.25           N  
ATOM    686  CA  PHE A  90      26.335  32.606  34.887  1.00 32.21           C  
ATOM    687  C   PHE A  90      25.076  32.023  35.502  1.00 31.22           C  
ATOM    688  O   PHE A  90      24.245  32.762  36.027  1.00 33.44           O  
ATOM    689  CB  PHE A  90      26.094  32.708  33.379  1.00 33.44           C  
ATOM    690  CG  PHE A  90      27.073  33.585  32.669  1.00 35.82           C  
ATOM    691  CD1 PHE A  90      28.259  33.066  32.176  1.00 34.57           C  
ATOM    692  CD2 PHE A  90      26.816  34.945  32.511  1.00 37.95           C  
ATOM    693  CE1 PHE A  90      29.182  33.890  31.533  1.00 36.72           C  
ATOM    694  CE2 PHE A  90      27.732  35.776  31.871  1.00 37.84           C  
ATOM    695  CZ  PHE A  90      28.917  35.245  31.382  1.00 38.00           C  
ATOM    696  N   LYS A  91      24.931  30.705  35.420  1.00 29.49           N  
ATOM    697  CA  LYS A  91      23.735  30.035  35.896  1.00 28.82           C  
ATOM    698  C   LYS A  91      23.104  30.535  37.189  1.00 27.53           C  
ATOM    699  O   LYS A  91      21.942  30.935  37.181  1.00 26.77           O  
ATOM    700  CB  LYS A  91      23.963  28.521  35.977  1.00 28.99           C  
ATOM    701  CG  LYS A  91      22.659  27.748  36.001  1.00 28.22           C  
ATOM    702  CD  LYS A  91      22.879  26.248  35.860  1.00 29.56           C  
ATOM    703  CE  LYS A  91      21.563  25.497  36.021  1.00 30.18           C  
ATOM    704  NZ  LYS A  91      21.746  24.022  35.950  1.00 34.12           N1+
ATOM    705  N   ASP A  92      23.833  30.525  38.298  1.00 27.77           N  
ATOM    706  CA  ASP A  92      23.227  30.997  39.541  1.00 29.16           C  
ATOM    707  C   ASP A  92      22.905  32.497  39.537  1.00 27.34           C  
ATOM    708  O   ASP A  92      21.917  32.923  40.136  1.00 24.35           O  
ATOM    709  CB  ASP A  92      24.104  30.685  40.751  1.00 32.33           C  
ATOM    710  CG  ASP A  92      23.479  31.174  42.046  1.00 37.03           C  
ATOM    711  OD1 ASP A  92      22.452  30.598  42.478  1.00 37.96           O  
ATOM    712  OD2 ASP A  92      24.000  32.154  42.619  1.00 39.71           O1-
ATOM    713  N   LYS A  93      23.734  33.296  38.874  1.00 27.16           N  
ATOM    714  CA  LYS A  93      23.483  34.737  38.815  1.00 28.00           C  
ATOM    715  C   LYS A  93      22.150  35.020  38.134  1.00 25.80           C  
ATOM    716  O   LYS A  93      21.389  35.874  38.582  1.00 26.65           O  
ATOM    717  CB  LYS A  93      24.596  35.463  38.055  1.00 29.74           C  
ATOM    718  CG  LYS A  93      25.962  35.385  38.714  1.00 32.86           C  
ATOM    719  CD  LYS A  93      25.933  35.933  40.118  1.00 32.98           C  
ATOM    720  CE  LYS A  93      27.325  35.943  40.729  1.00 37.20           C  
ATOM    721  NZ  LYS A  93      27.273  36.376  42.154  1.00 39.31           N1+
ATOM    722  N   TYR A  94      21.868  34.310  37.046  1.00 24.54           N  
ATOM    723  CA  TYR A  94      20.609  34.515  36.348  1.00 24.59           C  
ATOM    724  C   TYR A  94      19.450  34.118  37.250  1.00 25.60           C  
ATOM    725  O   TYR A  94      18.413  34.783  37.265  1.00 27.62           O  
ATOM    726  CB  TYR A  94      20.560  33.712  35.040  1.00 25.32           C  
ATOM    727  CG  TYR A  94      21.389  34.307  33.916  1.00 24.58           C  
ATOM    728  CD1 TYR A  94      21.361  35.678  33.650  1.00 26.09           C  
ATOM    729  CD2 TYR A  94      22.183  33.496  33.100  1.00 24.41           C  
ATOM    730  CE1 TYR A  94      22.106  36.231  32.596  1.00 25.41           C  
ATOM    731  CE2 TYR A  94      22.928  34.031  32.046  1.00 21.46           C  
ATOM    732  CZ  TYR A  94      22.885  35.400  31.799  1.00 26.97           C  
ATOM    733  OH  TYR A  94      23.619  35.932  30.757  1.00 25.50           O  
ATOM    734  N   LYS A  95      19.626  33.043  38.012  1.00 23.92           N  
ATOM    735  CA  LYS A  95      18.573  32.602  38.918  1.00 26.68           C  
ATOM    736  C   LYS A  95      18.301  33.674  39.962  1.00 24.85           C  
ATOM    737  O   LYS A  95      17.149  33.983  40.249  1.00 25.09           O  
ATOM    738  CB  LYS A  95      18.964  31.287  39.604  1.00 28.19           C  
ATOM    739  CG  LYS A  95      18.856  30.062  38.704  1.00 32.41           C  
ATOM    740  CD  LYS A  95      19.306  28.803  39.438  1.00 34.34           C  
ATOM    741  CE  LYS A  95      19.272  27.586  38.528  1.00 36.40           C  
ATOM    742  NZ  LYS A  95      19.904  26.404  39.190  1.00 36.51           N1+
ATOM    743  N   GLN A  96      19.361  34.242  40.528  1.00 25.09           N  
ATOM    744  CA  GLN A  96      19.207  35.299  41.526  1.00 27.77           C  
ATOM    745  C   GLN A  96      18.538  36.515  40.890  1.00 28.31           C  
ATOM    746  O   GLN A  96      17.662  37.143  41.485  1.00 28.63           O  
ATOM    747  CB  GLN A  96      20.567  35.719  42.085  1.00 29.16           C  
ATOM    748  CG  GLN A  96      21.278  34.649  42.894  1.00 32.08           C  
ATOM    749  CD  GLN A  96      22.526  35.179  43.562  1.00 33.17           C  
ATOM    750  OE1 GLN A  96      22.454  36.010  44.466  1.00 37.85           O  
ATOM    751  NE2 GLN A  96      23.679  34.712  43.112  1.00 33.06           N  
ATOM    752  N   ILE A  97      18.960  36.841  39.671  1.00 27.51           N  
ATOM    753  CA  ILE A  97      18.411  37.984  38.951  1.00 25.77           C  
ATOM    754  C   ILE A  97      16.926  37.830  38.638  1.00 25.57           C  
ATOM    755  O   ILE A  97      16.143  38.736  38.912  1.00 26.31           O  
ATOM    756  CB  ILE A  97      19.183  38.230  37.626  1.00 25.00           C  
ATOM    757  CG1 ILE A  97      20.607  38.689  37.937  1.00 24.33           C  
ATOM    758  CG2 ILE A  97      18.454  39.265  36.768  1.00 26.85           C  
ATOM    759  CD1 ILE A  97      21.513  38.772  36.724  1.00 24.71           C  
ATOM    760  N   PHE A  98      16.535  36.682  38.081  1.00 25.20           N  
ATOM    761  CA  PHE A  98      15.133  36.450  37.714  1.00 25.42           C  
ATOM    762  C   PHE A  98      14.247  35.843  38.800  1.00 27.53           C  
ATOM    763  O   PHE A  98      13.020  35.846  38.670  1.00 26.76           O  
ATOM    764  CB  PHE A  98      15.053  35.563  36.468  1.00 24.72           C  
ATOM    765  CG  PHE A  98      15.644  36.186  35.240  1.00 24.47           C  
ATOM    766  CD1 PHE A  98      14.999  37.246  34.604  1.00 23.86           C  
ATOM    767  CD2 PHE A  98      16.850  35.714  34.720  1.00 22.24           C  
ATOM    768  CE1 PHE A  98      15.544  37.830  33.463  1.00 24.69           C  
ATOM    769  CE2 PHE A  98      17.408  36.285  33.584  1.00 24.22           C  
ATOM    770  CZ  PHE A  98      16.752  37.353  32.948  1.00 26.01           C  
ATOM    771  N   LEU A  99      14.842  35.322  39.868  1.00 27.13           N  
ATOM    772  CA  LEU A  99      14.024  34.728  40.917  1.00 27.68           C  
ATOM    773  C   LEU A  99      14.244  35.309  42.311  1.00 27.30           C  
ATOM    774  O   LEU A  99      13.501  35.008  43.235  1.00 27.56           O  
ATOM    775  CB  LEU A  99      14.220  33.205  40.934  1.00 25.86           C  
ATOM    776  CG  LEU A  99      13.659  32.467  39.708  1.00 28.46           C  
ATOM    777  CD1 LEU A  99      14.002  30.984  39.780  1.00 27.72           C  
ATOM    778  CD2 LEU A  99      12.144  32.658  39.642  1.00 28.19           C  
ATOM    779  N   GLY A 100      15.257  36.147  42.467  1.00 28.77           N  
ATOM    780  CA  GLY A 100      15.509  36.734  43.770  1.00 29.83           C  
ATOM    781  C   GLY A 100      14.298  37.500  44.274  1.00 32.15           C  
ATOM    782  O   GLY A 100      13.703  38.295  43.539  1.00 30.14           O  
ATOM    783  N   GLY A 101      13.921  37.245  45.525  1.00 33.73           N  
ATOM    784  CA  GLY A 101      12.780  37.925  46.109  1.00 36.38           C  
ATOM    785  C   GLY A 101      11.405  37.359  45.773  1.00 36.13           C  
ATOM    786  O   GLY A 101      10.403  37.842  46.300  1.00 37.70           O  
ATOM    787  N   VAL A 102      11.329  36.349  44.912  1.00 34.44           N  
ATOM    788  CA  VAL A 102      10.022  35.790  44.572  1.00 33.45           C  
ATOM    789  C   VAL A 102       9.636  34.631  45.484  1.00 34.07           C  
ATOM    790  O   VAL A 102      10.439  33.733  45.741  1.00 30.04           O  
ATOM    791  CB  VAL A 102       9.960  35.305  43.099  1.00 34.68           C  
ATOM    792  CG1 VAL A 102      10.997  34.234  42.853  1.00 37.33           C  
ATOM    793  CG2 VAL A 102       8.566  34.752  42.786  1.00 31.24           C  
ATOM    794  N   ASP A 103       8.408  34.673  45.994  1.00 35.45           N  
ATOM    795  CA  ASP A 103       7.908  33.610  46.860  1.00 36.59           C  
ATOM    796  C   ASP A 103       7.281  32.546  45.966  1.00 36.04           C  
ATOM    797  O   ASP A 103       6.209  32.746  45.389  1.00 35.45           O  
ATOM    798  CB  ASP A 103       6.859  34.141  47.838  1.00 38.98           C  
ATOM    799  CG  ASP A 103       6.428  33.093  48.855  1.00 42.92           C  
ATOM    800  OD1 ASP A 103       5.886  32.040  48.445  1.00 41.23           O  
ATOM    801  OD2 ASP A 103       6.639  33.325  50.067  1.00 44.39           O1-
ATOM    802  N   ARG A 104       7.972  31.421  45.854  1.00 34.27           N  
ATOM    803  CA  ARG A 104       7.530  30.305  45.036  1.00 35.54           C  
ATOM    804  C   ARG A 104       6.088  29.876  45.320  1.00 35.73           C  
ATOM    805  O   ARG A 104       5.320  29.602  44.397  1.00 34.85           O  
ATOM    806  CB  ARG A 104       8.486  29.132  45.258  1.00 36.54           C  
ATOM    807  CG  ARG A 104       8.166  27.872  44.493  1.00 37.22           C  
ATOM    808  CD  ARG A 104       9.389  26.975  44.459  1.00 37.59           C  
ATOM    809  NE  ARG A 104       9.982  26.801  45.783  1.00 41.38           N  
ATOM    810  CZ  ARG A 104       9.466  26.042  46.748  1.00 42.66           C  
ATOM    811  NH1 ARG A 104       8.337  25.376  46.539  1.00 38.81           N1+
ATOM    812  NH2 ARG A 104      10.077  25.952  47.924  1.00 39.95           N  
ATOM    813  N   HIS A 105       5.720  29.834  46.596  1.00 34.92           N  
ATOM    814  CA  HIS A 105       4.380  29.413  46.991  1.00 36.20           C  
ATOM    815  C   HIS A 105       3.269  30.413  46.723  1.00 37.60           C  
ATOM    816  O   HIS A 105       2.221  30.046  46.192  1.00 38.59           O  
ATOM    817  CB  HIS A 105       4.376  29.038  48.473  1.00 33.77           C  
ATOM    818  CG  HIS A 105       5.285  27.899  48.792  1.00 34.82           C  
ATOM    819  ND1 HIS A 105       5.042  26.615  48.353  1.00 34.15           N  
ATOM    820  CD2 HIS A 105       6.482  27.862  49.425  1.00 35.55           C  
ATOM    821  CE1 HIS A 105       6.052  25.836  48.699  1.00 36.70           C  
ATOM    822  NE2 HIS A 105       6.939  26.568  49.350  1.00 37.77           N  
ATOM    823  N   LYS A 106       3.495  31.672  47.088  1.00 37.17           N  
ATOM    824  CA  LYS A 106       2.489  32.709  46.905  1.00 37.64           C  
ATOM    825  C   LYS A 106       2.484  33.357  45.525  1.00 36.62           C  
ATOM    826  O   LYS A 106       1.542  34.070  45.186  1.00 39.33           O  
ATOM    827  CB  LYS A 106       2.665  33.795  47.969  1.00 39.35           C  
ATOM    828  CG  LYS A 106       2.530  33.288  49.394  1.00 42.94           C  
ATOM    829  CD  LYS A 106       1.099  32.877  49.703  1.00 46.99           C  
ATOM    830  CE  LYS A 106       1.050  31.846  50.821  1.00 47.77           C  
ATOM    831  NZ  LYS A 106       1.691  30.572  50.377  1.00 49.10           N1+
ATOM    832  N   GLN A 107       3.521  33.114  44.729  1.00 33.62           N  
ATOM    833  CA  GLN A 107       3.601  33.719  43.398  1.00 31.77           C  
ATOM    834  C   GLN A 107       3.968  32.710  42.315  1.00 31.51           C  
ATOM    835  O   GLN A 107       4.984  32.865  41.635  1.00 29.44           O  
ATOM    836  CB  GLN A 107       4.646  34.835  43.403  1.00 31.28           C  
ATOM    837  CG  GLN A 107       4.396  35.938  44.420  1.00 31.93           C  
ATOM    838  CD  GLN A 107       5.578  36.884  44.535  1.00 34.12           C  
ATOM    839  OE1 GLN A 107       6.522  36.636  45.290  1.00 35.06           O  
ATOM    840  NE2 GLN A 107       5.539  37.970  43.771  1.00 33.16           N  
ATOM    841  N   PHE A 108       3.136  31.690  42.143  1.00 30.60           N  
ATOM    842  CA  PHE A 108       3.401  30.656  41.154  1.00 30.88           C  
ATOM    843  C   PHE A 108       3.853  31.125  39.770  1.00 31.37           C  
ATOM    844  O   PHE A 108       4.900  30.694  39.278  1.00 29.41           O  
ATOM    845  CB  PHE A 108       2.176  29.770  40.948  1.00 31.91           C  
ATOM    846  CG  PHE A 108       2.390  28.711  39.910  1.00 32.45           C  
ATOM    847  CD1 PHE A 108       3.082  27.548  40.224  1.00 33.13           C  
ATOM    848  CD2 PHE A 108       1.970  28.909  38.599  1.00 33.21           C  
ATOM    849  CE1 PHE A 108       3.360  26.598  39.249  1.00 34.11           C  
ATOM    850  CE2 PHE A 108       2.239  27.967  37.611  1.00 32.77           C  
ATOM    851  CZ  PHE A 108       2.938  26.808  37.938  1.00 33.56           C  
ATOM    852  N   TRP A 109       3.056  31.982  39.135  1.00 30.30           N  
ATOM    853  CA  TRP A 109       3.376  32.435  37.786  1.00 31.13           C  
ATOM    854  C   TRP A 109       4.626  33.295  37.688  1.00 31.42           C  
ATOM    855  O   TRP A 109       5.429  33.110  36.776  1.00 29.62           O  
ATOM    856  CB  TRP A 109       2.172  33.146  37.157  1.00 32.53           C  
ATOM    857  CG  TRP A 109       1.014  32.210  36.919  1.00 35.27           C  
ATOM    858  CD1 TRP A 109      -0.183  32.200  37.581  1.00 38.03           C  
ATOM    859  CD2 TRP A 109       0.970  31.105  36.000  1.00 36.39           C  
ATOM    860  NE1 TRP A 109      -0.967  31.158  37.136  1.00 36.70           N  
ATOM    861  CE2 TRP A 109      -0.286  30.470  36.167  1.00 38.50           C  
ATOM    862  CE3 TRP A 109       1.867  30.588  35.054  1.00 37.06           C  
ATOM    863  CZ2 TRP A 109      -0.666  29.340  35.422  1.00 38.64           C  
ATOM    864  CZ3 TRP A 109       1.488  29.463  34.313  1.00 38.79           C  
ATOM    865  CH2 TRP A 109       0.231  28.854  34.505  1.00 37.39           C  
ATOM    866  N   ARG A 110       4.796  34.225  38.622  1.00 30.51           N  
ATOM    867  CA  ARG A 110       5.979  35.069  38.620  1.00 30.63           C  
ATOM    868  C   ARG A 110       7.194  34.146  38.755  1.00 30.00           C  
ATOM    869  O   ARG A 110       8.236  34.386  38.148  1.00 28.77           O  
ATOM    870  CB  ARG A 110       5.919  36.069  39.782  1.00 29.55           C  
ATOM    871  CG  ARG A 110       7.209  36.830  40.033  1.00 29.75           C  
ATOM    872  CD  ARG A 110       7.678  37.603  38.806  1.00 31.27           C  
ATOM    873  NE  ARG A 110       8.934  38.304  39.082  1.00 30.24           N  
ATOM    874  CZ  ARG A 110      10.138  37.751  38.984  1.00 28.21           C  
ATOM    875  NH1 ARG A 110      10.259  36.485  38.597  1.00 24.63           N1+
ATOM    876  NH2 ARG A 110      11.218  38.452  39.312  1.00 27.89           N  
ATOM    877  N   TYR A 111       7.049  33.080  39.538  1.00 29.35           N  
ATOM    878  CA  TYR A 111       8.140  32.124  39.712  1.00 28.24           C  
ATOM    879  C   TYR A 111       8.338  31.329  38.413  1.00 27.08           C  
ATOM    880  O   TYR A 111       9.464  31.117  37.960  1.00 24.51           O  
ATOM    881  CB  TYR A 111       7.838  31.148  40.852  1.00 29.45           C  
ATOM    882  CG  TYR A 111       9.065  30.378  41.303  1.00 31.52           C  
ATOM    883  CD1 TYR A 111       9.924  30.907  42.262  1.00 33.26           C  
ATOM    884  CD2 TYR A 111       9.394  29.145  40.737  1.00 32.76           C  
ATOM    885  CE1 TYR A 111      11.079  30.235  42.647  1.00 34.76           C  
ATOM    886  CE2 TYR A 111      10.552  28.464  41.117  1.00 31.84           C  
ATOM    887  CZ  TYR A 111      11.387  29.019  42.071  1.00 34.22           C  
ATOM    888  OH  TYR A 111      12.548  28.377  42.447  1.00 37.90           O  
ATOM    889  N   PHE A 112       7.234  30.882  37.824  1.00 26.54           N  
ATOM    890  CA  PHE A 112       7.296  30.124  36.582  1.00 27.39           C  
ATOM    891  C   PHE A 112       8.052  30.925  35.519  1.00 27.48           C  
ATOM    892  O   PHE A 112       9.003  30.431  34.914  1.00 24.79           O  
ATOM    893  CB  PHE A 112       5.891  29.823  36.068  1.00 30.28           C  
ATOM    894  CG  PHE A 112       5.864  28.862  34.910  1.00 33.15           C  
ATOM    895  CD1 PHE A 112       5.992  27.494  35.123  1.00 35.03           C  
ATOM    896  CD2 PHE A 112       5.729  29.327  33.603  1.00 35.67           C  
ATOM    897  CE1 PHE A 112       5.985  26.593  34.048  1.00 36.08           C  
ATOM    898  CE2 PHE A 112       5.722  28.432  32.520  1.00 34.57           C  
ATOM    899  CZ  PHE A 112       5.851  27.067  32.747  1.00 34.20           C  
ATOM    900  N   ALA A 113       7.617  32.163  35.295  1.00 26.90           N  
ATOM    901  CA  ALA A 113       8.247  33.027  34.305  1.00 27.67           C  
ATOM    902  C   ALA A 113       9.716  33.269  34.646  1.00 27.85           C  
ATOM    903  O   ALA A 113      10.568  33.302  33.759  1.00 28.82           O  
ATOM    904  CB  ALA A 113       7.500  34.359  34.222  1.00 28.43           C  
ATOM    905  N   GLY A 114      10.006  33.453  35.930  1.00 27.32           N  
ATOM    906  CA  GLY A 114      11.377  33.674  36.341  1.00 28.18           C  
ATOM    907  C   GLY A 114      12.232  32.469  35.997  1.00 30.02           C  
ATOM    908  O   GLY A 114      13.382  32.603  35.556  1.00 28.50           O  
ATOM    909  N   ASN A 115      11.657  31.286  36.184  1.00 28.62           N  
ATOM    910  CA  ASN A 115      12.353  30.037  35.911  1.00 29.44           C  
ATOM    911  C   ASN A 115      12.669  29.903  34.420  1.00 28.93           C  
ATOM    912  O   ASN A 115      13.772  29.494  34.033  1.00 26.11           O  
ATOM    913  CB  ASN A 115      11.492  28.857  36.373  1.00 32.26           C  
ATOM    914  CG  ASN A 115      12.247  27.552  36.352  1.00 37.09           C  
ATOM    915  OD1 ASN A 115      13.296  27.424  36.985  1.00 39.65           O  
ATOM    916  ND2 ASN A 115      11.726  26.573  35.619  1.00 39.36           N  
ATOM    917  N   LEU A 116      11.696  30.246  33.585  1.00 27.72           N  
ATOM    918  CA  LEU A 116      11.884  30.176  32.143  1.00 28.61           C  
ATOM    919  C   LEU A 116      12.947  31.166  31.653  1.00 27.36           C  
ATOM    920  O   LEU A 116      13.785  30.829  30.812  1.00 25.61           O  
ATOM    921  CB  LEU A 116      10.570  30.463  31.417  1.00 29.70           C  
ATOM    922  CG  LEU A 116       9.446  29.432  31.488  1.00 31.62           C  
ATOM    923  CD1 LEU A 116       8.357  29.858  30.509  1.00 29.21           C  
ATOM    924  CD2 LEU A 116       9.963  28.039  31.130  1.00 29.82           C  
ATOM    925  N   ALA A 117      12.894  32.389  32.174  1.00 26.36           N  
ATOM    926  CA  ALA A 117      13.838  33.439  31.784  1.00 26.13           C  
ATOM    927  C   ALA A 117      15.250  33.059  32.214  1.00 26.18           C  
ATOM    928  O   ALA A 117      16.215  33.289  31.485  1.00 26.18           O  
ATOM    929  CB  ALA A 117      13.432  34.782  32.429  1.00 25.56           C  
ATOM    930  N   SER A 118      15.359  32.482  33.406  1.00 25.93           N  
ATOM    931  CA  SER A 118      16.646  32.055  33.929  1.00 28.13           C  
ATOM    932  C   SER A 118      17.238  30.947  33.058  1.00 26.87           C  
ATOM    933  O   SER A 118      18.401  31.011  32.662  1.00 25.01           O  
ATOM    934  CB  SER A 118      16.494  31.551  35.364  1.00 28.34           C  
ATOM    935  OG  SER A 118      17.741  31.080  35.844  1.00 33.93           O  
ATOM    936  N   GLY A 119      16.437  29.925  32.774  1.00 26.74           N  
ATOM    937  CA  GLY A 119      16.905  28.834  31.931  1.00 27.57           C  
ATOM    938  C   GLY A 119      17.243  29.346  30.537  1.00 27.66           C  
ATOM    939  O   GLY A 119      18.285  29.004  29.967  1.00 28.16           O  
ATOM    940  N   GLY A 120      16.364  30.184  29.996  1.00 27.02           N  
ATOM    941  CA  GLY A 120      16.585  30.745  28.675  1.00 28.44           C  
ATOM    942  C   GLY A 120      17.831  31.613  28.597  1.00 29.06           C  
ATOM    943  O   GLY A 120      18.567  31.557  27.611  1.00 27.71           O  
ATOM    944  N   ALA A 121      18.072  32.410  29.637  1.00 27.26           N  
ATOM    945  CA  ALA A 121      19.241  33.280  29.673  1.00 27.18           C  
ATOM    946  C   ALA A 121      20.531  32.466  29.780  1.00 27.12           C  
ATOM    947  O   ALA A 121      21.516  32.767  29.101  1.00 27.41           O  
ATOM    948  CB  ALA A 121      19.138  34.256  30.844  1.00 26.40           C  
ATOM    949  N   ALA A 122      20.530  31.440  30.632  1.00 25.52           N  
ATOM    950  CA  ALA A 122      21.719  30.604  30.803  1.00 24.70           C  
ATOM    951  C   ALA A 122      21.992  29.812  29.526  1.00 26.31           C  
ATOM    952  O   ALA A 122      23.148  29.650  29.128  1.00 26.93           O  
ATOM    953  CB  ALA A 122      21.544  29.652  31.982  1.00 20.67           C  
ATOM    954  N   GLY A 123      20.926  29.326  28.890  1.00 25.02           N  
ATOM    955  CA  GLY A 123      21.078  28.567  27.658  1.00 25.80           C  
ATOM    956  C   GLY A 123      21.619  29.401  26.499  1.00 25.78           C  
ATOM    957  O   GLY A 123      22.555  28.990  25.816  1.00 25.12           O  
ATOM    958  N   ALA A 124      21.031  30.572  26.270  1.00 26.71           N  
ATOM    959  CA  ALA A 124      21.482  31.451  25.190  1.00 27.08           C  
ATOM    960  C   ALA A 124      22.921  31.896  25.427  1.00 28.61           C  
ATOM    961  O   ALA A 124      23.706  31.999  24.483  1.00 29.82           O  
ATOM    962  CB  ALA A 124      20.569  32.674  25.087  1.00 27.21           C  
ATOM    963  N   THR A 125      23.262  32.159  26.688  1.00 27.74           N  
ATOM    964  CA  THR A 125      24.614  32.588  27.040  1.00 26.95           C  
ATOM    965  C   THR A 125      25.622  31.491  26.703  1.00 27.51           C  
ATOM    966  O   THR A 125      26.651  31.756  26.065  1.00 26.88           O  
ATOM    967  CB  THR A 125      24.706  32.951  28.539  1.00 25.94           C  
ATOM    968  OG1 THR A 125      23.843  34.062  28.806  1.00 24.93           O  
ATOM    969  CG2 THR A 125      26.123  33.329  28.922  1.00 26.72           C  
ATOM    970  N   SER A 126      25.332  30.261  27.121  1.00 25.45           N  
ATOM    971  CA  SER A 126      26.223  29.142  26.818  1.00 27.20           C  
ATOM    972  C   SER A 126      26.343  28.953  25.302  1.00 25.46           C  
ATOM    973  O   SER A 126      27.442  28.791  24.771  1.00 24.98           O  
ATOM    974  CB  SER A 126      25.692  27.849  27.445  1.00 28.80           C  
ATOM    975  OG  SER A 126      25.654  27.964  28.854  1.00 37.98           O  
ATOM    976  N   LEU A 127      25.202  28.971  24.617  1.00 24.74           N  
ATOM    977  CA  LEU A 127      25.175  28.804  23.167  1.00 25.38           C  
ATOM    978  C   LEU A 127      25.971  29.886  22.434  1.00 25.57           C  
ATOM    979  O   LEU A 127      26.434  29.661  21.318  1.00 23.73           O  
ATOM    980  CB  LEU A 127      23.730  28.784  22.656  1.00 23.28           C  
ATOM    981  CG  LEU A 127      22.927  27.502  22.929  1.00 24.70           C  
ATOM    982  CD1 LEU A 127      21.500  27.673  22.439  1.00 23.69           C  
ATOM    983  CD2 LEU A 127      23.577  26.322  22.226  1.00 21.31           C  
ATOM    984  N   CYS A 128      26.124  31.061  23.043  1.00 25.50           N  
ATOM    985  CA  CYS A 128      26.908  32.112  22.397  1.00 28.32           C  
ATOM    986  C   CYS A 128      28.317  31.580  22.166  1.00 27.94           C  
ATOM    987  O   CYS A 128      29.018  32.031  21.265  1.00 29.87           O  
ATOM    988  CB  CYS A 128      26.983  33.371  23.269  1.00 28.52           C  
ATOM    989  SG  CYS A 128      25.569  34.489  23.115  1.00 36.94           S  
ATOM    990  N   PHE A 129      28.727  30.614  22.984  1.00 27.66           N  
ATOM    991  CA  PHE A 129      30.057  30.031  22.859  1.00 28.09           C  
ATOM    992  C   PHE A 129      30.108  28.628  22.249  1.00 27.35           C  
ATOM    993  O   PHE A 129      31.002  28.334  21.456  1.00 26.83           O  
ATOM    994  CB  PHE A 129      30.749  29.982  24.225  1.00 30.74           C  
ATOM    995  CG  PHE A 129      30.965  31.334  24.852  1.00 33.62           C  
ATOM    996  CD1 PHE A 129      29.913  32.017  25.447  1.00 33.06           C  
ATOM    997  CD2 PHE A 129      32.225  31.926  24.838  1.00 36.54           C  
ATOM    998  CE1 PHE A 129      30.107  33.271  26.020  1.00 35.13           C  
ATOM    999  CE2 PHE A 129      32.431  33.179  25.408  1.00 37.24           C  
ATOM   1000  CZ  PHE A 129      31.368  33.855  26.001  1.00 36.20           C  
ATOM   1001  N   VAL A 130      29.161  27.761  22.610  1.00 25.36           N  
ATOM   1002  CA  VAL A 130      29.191  26.389  22.106  1.00 23.11           C  
ATOM   1003  C   VAL A 130      28.323  26.050  20.898  1.00 21.80           C  
ATOM   1004  O   VAL A 130      28.426  24.951  20.372  1.00 21.24           O  
ATOM   1005  CB  VAL A 130      28.866  25.368  23.237  1.00 23.53           C  
ATOM   1006  CG1 VAL A 130      29.807  25.584  24.421  1.00 23.83           C  
ATOM   1007  CG2 VAL A 130      27.414  25.501  23.676  1.00 21.77           C  
ATOM   1008  N   TYR A 131      27.485  26.980  20.447  1.00 22.09           N  
ATOM   1009  CA  TYR A 131      26.622  26.718  19.294  1.00 21.63           C  
ATOM   1010  C   TYR A 131      27.372  26.167  18.068  1.00 22.11           C  
ATOM   1011  O   TYR A 131      26.871  25.276  17.379  1.00 20.69           O  
ATOM   1012  CB  TYR A 131      25.842  27.984  18.905  1.00 22.34           C  
ATOM   1013  CG  TYR A 131      24.662  27.721  17.977  1.00 22.60           C  
ATOM   1014  CD1 TYR A 131      24.857  27.415  16.628  1.00 22.39           C  
ATOM   1015  CD2 TYR A 131      23.357  27.731  18.462  1.00 22.96           C  
ATOM   1016  CE1 TYR A 131      23.784  27.120  15.790  1.00 23.22           C  
ATOM   1017  CE2 TYR A 131      22.272  27.438  17.634  1.00 22.70           C  
ATOM   1018  CZ  TYR A 131      22.493  27.132  16.301  1.00 24.60           C  
ATOM   1019  OH  TYR A 131      21.425  26.827  15.486  1.00 26.04           O  
ATOM   1020  N   PRO A 132      28.585  26.681  17.781  1.00 22.47           N  
ATOM   1021  CA  PRO A 132      29.311  26.158  16.612  1.00 21.51           C  
ATOM   1022  C   PRO A 132      29.529  24.648  16.721  1.00 21.74           C  
ATOM   1023  O   PRO A 132      29.564  23.934  15.717  1.00 22.41           O  
ATOM   1024  CB  PRO A 132      30.630  26.933  16.642  1.00 19.84           C  
ATOM   1025  CG  PRO A 132      30.228  28.253  17.263  1.00 23.24           C  
ATOM   1026  CD  PRO A 132      29.321  27.797  18.404  1.00 19.41           C  
ATOM   1027  N   LEU A 133      29.690  24.174  17.951  1.00 22.67           N  
ATOM   1028  CA  LEU A 133      29.887  22.755  18.194  1.00 24.04           C  
ATOM   1029  C   LEU A 133      28.593  22.015  17.834  1.00 22.28           C  
ATOM   1030  O   LEU A 133      28.641  20.961  17.206  1.00 20.59           O  
ATOM   1031  CB  LEU A 133      30.276  22.516  19.659  1.00 23.33           C  
ATOM   1032  CG  LEU A 133      31.634  23.105  20.080  1.00 27.31           C  
ATOM   1033  CD1 LEU A 133      31.831  22.956  21.588  1.00 26.33           C  
ATOM   1034  CD2 LEU A 133      32.754  22.408  19.325  1.00 25.26           C  
ATOM   1035  N   ASP A 134      27.441  22.567  18.217  1.00 22.73           N  
ATOM   1036  CA  ASP A 134      26.165  21.923  17.869  1.00 23.32           C  
ATOM   1037  C   ASP A 134      26.015  21.960  16.355  1.00 22.26           C  
ATOM   1038  O   ASP A 134      25.549  21.008  15.734  1.00 24.14           O  
ATOM   1039  CB  ASP A 134      24.967  22.649  18.500  1.00 24.11           C  
ATOM   1040  CG  ASP A 134      24.786  22.334  19.976  1.00 24.67           C  
ATOM   1041  OD1 ASP A 134      25.294  21.295  20.454  1.00 26.72           O  
ATOM   1042  OD2 ASP A 134      24.103  23.120  20.658  1.00 25.18           O1-
ATOM   1043  N   PHE A 135      26.416  23.076  15.760  1.00 22.34           N  
ATOM   1044  CA  PHE A 135      26.326  23.230  14.320  1.00 20.52           C  
ATOM   1045  C   PHE A 135      27.128  22.151  13.597  1.00 20.46           C  
ATOM   1046  O   PHE A 135      26.621  21.474  12.705  1.00 20.66           O  
ATOM   1047  CB  PHE A 135      26.859  24.599  13.904  1.00 20.01           C  
ATOM   1048  CG  PHE A 135      27.090  24.728  12.424  1.00 19.66           C  
ATOM   1049  CD1 PHE A 135      26.027  24.986  11.560  1.00 19.81           C  
ATOM   1050  CD2 PHE A 135      28.373  24.597  11.896  1.00 17.31           C  
ATOM   1051  CE1 PHE A 135      26.239  25.118  10.182  1.00 21.51           C  
ATOM   1052  CE2 PHE A 135      28.597  24.726  10.519  1.00 21.10           C  
ATOM   1053  CZ  PHE A 135      27.527  24.988   9.661  1.00 18.97           C  
ATOM   1054  N   ALA A 136      28.391  22.003  13.980  1.00 20.39           N  
ATOM   1055  CA  ALA A 136      29.259  21.018  13.344  1.00 21.08           C  
ATOM   1056  C   ALA A 136      28.780  19.594  13.602  1.00 21.92           C  
ATOM   1057  O   ALA A 136      28.867  18.728  12.722  1.00 22.58           O  
ATOM   1058  CB  ALA A 136      30.697  21.193  13.836  1.00 19.71           C  
ATOM   1059  N   ARG A 137      28.273  19.346  14.808  1.00 22.10           N  
ATOM   1060  CA  ARG A 137      27.784  18.009  15.143  1.00 20.85           C  
ATOM   1061  C   ARG A 137      26.689  17.649  14.145  1.00 19.55           C  
ATOM   1062  O   ARG A 137      26.640  16.533  13.632  1.00 19.07           O  
ATOM   1063  CB  ARG A 137      27.241  17.990  16.580  1.00 22.14           C  
ATOM   1064  CG  ARG A 137      26.898  16.606  17.132  1.00 21.00           C  
ATOM   1065  CD  ARG A 137      25.513  16.118  16.694  1.00 20.88           C  
ATOM   1066  NE  ARG A 137      25.324  14.718  17.066  1.00 20.11           N  
ATOM   1067  CZ  ARG A 137      25.880  13.701  16.417  1.00 21.74           C  
ATOM   1068  NH1 ARG A 137      26.647  13.929  15.356  1.00 18.33           N1+
ATOM   1069  NH2 ARG A 137      25.690  12.457  16.842  1.00 21.07           N  
ATOM   1070  N   THR A 138      25.826  18.616  13.850  1.00 19.33           N  
ATOM   1071  CA  THR A 138      24.735  18.401  12.908  1.00 20.73           C  
ATOM   1072  C   THR A 138      25.208  18.260  11.459  1.00 22.43           C  
ATOM   1073  O   THR A 138      24.809  17.323  10.763  1.00 22.81           O  
ATOM   1074  CB  THR A 138      23.703  19.544  12.976  1.00 20.01           C  
ATOM   1075  OG1 THR A 138      23.137  19.592  14.294  1.00 22.62           O  
ATOM   1076  CG2 THR A 138      22.587  19.324  11.953  1.00 18.17           C  
ATOM   1077  N   ARG A 139      26.046  19.186  11.003  1.00 21.46           N  
ATOM   1078  CA  ARG A 139      26.527  19.126   9.627  1.00 23.20           C  
ATOM   1079  C   ARG A 139      27.334  17.854   9.356  1.00 22.58           C  
ATOM   1080  O   ARG A 139      27.238  17.279   8.275  1.00 22.46           O  
ATOM   1081  CB  ARG A 139      27.350  20.380   9.284  1.00 21.78           C  
ATOM   1082  CG  ARG A 139      26.529  21.673   9.274  1.00 21.17           C  
ATOM   1083  CD  ARG A 139      25.281  21.548   8.386  1.00 19.46           C  
ATOM   1084  NE  ARG A 139      25.626  21.258   6.998  1.00 23.02           N  
ATOM   1085  CZ  ARG A 139      25.821  22.176   6.053  1.00 25.07           C  
ATOM   1086  NH1 ARG A 139      25.696  23.472   6.330  1.00 20.01           N1+
ATOM   1087  NH2 ARG A 139      26.169  21.794   4.828  1.00 25.59           N  
ATOM   1088  N   LEU A 140      28.122  17.412  10.332  1.00 22.36           N  
ATOM   1089  CA  LEU A 140      28.897  16.181  10.157  1.00 24.84           C  
ATOM   1090  C   LEU A 140      27.959  14.976  10.159  1.00 25.29           C  
ATOM   1091  O   LEU A 140      28.143  14.034   9.390  1.00 25.07           O  
ATOM   1092  CB  LEU A 140      29.928  16.016  11.275  1.00 25.47           C  
ATOM   1093  CG  LEU A 140      31.199  16.862  11.197  1.00 27.12           C  
ATOM   1094  CD1 LEU A 140      31.953  16.774  12.521  1.00 27.06           C  
ATOM   1095  CD2 LEU A 140      32.066  16.372  10.051  1.00 28.56           C  
ATOM   1096  N   ALA A 141      26.949  15.007  11.025  1.00 23.38           N  
ATOM   1097  CA  ALA A 141      26.001  13.906  11.077  1.00 23.42           C  
ATOM   1098  C   ALA A 141      25.283  13.771   9.732  1.00 24.22           C  
ATOM   1099  O   ALA A 141      25.048  12.663   9.255  1.00 22.37           O  
ATOM   1100  CB  ALA A 141      24.977  14.132  12.194  1.00 23.12           C  
ATOM   1101  N   ALA A 142      24.943  14.905   9.125  1.00 24.06           N  
ATOM   1102  CA  ALA A 142      24.225  14.909   7.847  1.00 25.52           C  
ATOM   1103  C   ALA A 142      25.080  14.480   6.651  1.00 26.99           C  
ATOM   1104  O   ALA A 142      24.552  14.059   5.625  1.00 29.10           O  
ATOM   1105  CB  ALA A 142      23.630  16.305   7.589  1.00 24.29           C  
ATOM   1106  N   ASP A 143      26.395  14.592   6.784  1.00 26.05           N  
ATOM   1107  CA  ASP A 143      27.309  14.218   5.713  1.00 28.16           C  
ATOM   1108  C   ASP A 143      27.276  12.700   5.485  1.00 27.64           C  
ATOM   1109  O   ASP A 143      27.625  11.921   6.372  1.00 26.79           O  
ATOM   1110  CB  ASP A 143      28.723  14.693   6.079  1.00 29.16           C  
ATOM   1111  CG  ASP A 143      29.752  14.394   5.003  1.00 31.24           C  
ATOM   1112  OD1 ASP A 143      29.374  13.906   3.916  1.00 29.62           O  
ATOM   1113  OD2 ASP A 143      30.953  14.656   5.255  1.00 30.97           O1-
ATOM   1114  N   VAL A 144      26.847  12.286   4.294  1.00 27.66           N  
ATOM   1115  CA  VAL A 144      26.768  10.863   3.967  1.00 28.04           C  
ATOM   1116  C   VAL A 144      27.885  10.359   3.038  1.00 31.02           C  
ATOM   1117  O   VAL A 144      27.771   9.279   2.447  1.00 29.98           O  
ATOM   1118  CB  VAL A 144      25.399  10.515   3.340  1.00 27.75           C  
ATOM   1119  CG1 VAL A 144      24.295  10.723   4.368  1.00 26.90           C  
ATOM   1120  CG2 VAL A 144      25.141  11.382   2.112  1.00 25.43           C  
ATOM   1121  N   GLY A 145      28.958  11.141   2.921  1.00 32.71           N  
ATOM   1122  CA  GLY A 145      30.085  10.759   2.082  1.00 35.37           C  
ATOM   1123  C   GLY A 145      30.613   9.395   2.484  1.00 37.71           C  
ATOM   1124  O   GLY A 145      30.765   9.103   3.668  1.00 36.70           O  
ATOM   1125  N   LYS A 146      30.908   8.563   1.493  1.00 40.90           N  
ATOM   1126  CA  LYS A 146      31.372   7.206   1.750  1.00 45.32           C  
ATOM   1127  C   LYS A 146      32.877   7.041   1.889  1.00 46.43           C  
ATOM   1128  O   LYS A 146      33.366   5.934   2.097  1.00 48.50           O  
ATOM   1129  CB  LYS A 146      30.847   6.275   0.652  1.00 46.54           C  
ATOM   1130  CG  LYS A 146      29.324   6.270   0.543  1.00 50.01           C  
ATOM   1131  CD  LYS A 146      28.824   5.199  -0.416  1.00 52.08           C  
ATOM   1132  CE  LYS A 146      27.307   5.072  -0.358  1.00 53.43           C  
ATOM   1133  NZ  LYS A 146      26.811   3.937  -1.190  1.00 54.11           N1+
ATOM   1134  N   GLY A 147      33.607   8.142   1.776  1.00 47.72           N  
ATOM   1135  CA  GLY A 147      35.049   8.096   1.896  1.00 47.43           C  
ATOM   1136  C   GLY A 147      35.573   9.510   1.988  1.00 48.48           C  
ATOM   1137  O   GLY A 147      34.842  10.460   1.709  1.00 47.55           O  
ATOM   1138  N   ALA A 148      36.835   9.654   2.377  1.00 48.45           N  
ATOM   1139  CA  ALA A 148      37.453  10.967   2.515  1.00 50.71           C  
ATOM   1140  C   ALA A 148      37.187  11.880   1.321  1.00 52.00           C  
ATOM   1141  O   ALA A 148      36.900  13.069   1.486  1.00 53.16           O  
ATOM   1142  CB  ALA A 148      38.955  10.814   2.722  1.00 50.29           C  
ATOM   1143  N   ALA A 149      37.274  11.319   0.121  1.00 52.15           N  
ATOM   1144  CA  ALA A 149      37.064  12.093  -1.095  1.00 52.17           C  
ATOM   1145  C   ALA A 149      35.624  12.552  -1.300  1.00 51.86           C  
ATOM   1146  O   ALA A 149      35.385  13.587  -1.927  1.00 52.28           O  
ATOM   1147  CB  ALA A 149      37.530  11.289  -2.305  1.00 52.48           C  
ATOM   1148  N   GLN A 150      34.664  11.792  -0.782  1.00 50.25           N  
ATOM   1149  CA  GLN A 150      33.259  12.160  -0.943  1.00 47.66           C  
ATOM   1150  C   GLN A 150      32.711  12.903   0.269  1.00 44.36           C  
ATOM   1151  O   GLN A 150      31.570  13.354   0.259  1.00 43.88           O  
ATOM   1152  CB  GLN A 150      32.402  10.917  -1.199  1.00 49.95           C  
ATOM   1153  CG  GLN A 150      33.004   9.924  -2.178  1.00 53.09           C  
ATOM   1154  CD  GLN A 150      33.833   8.865  -1.477  1.00 56.03           C  
ATOM   1155  OE1 GLN A 150      33.306   8.054  -0.711  1.00 58.19           O  
ATOM   1156  NE2 GLN A 150      35.136   8.870  -1.727  1.00 56.85           N  
ATOM   1157  N   ARG A 151      33.525  13.029   1.312  1.00 41.76           N  
ATOM   1158  CA  ARG A 151      33.101  13.721   2.524  1.00 38.59           C  
ATOM   1159  C   ARG A 151      32.912  15.215   2.272  1.00 38.28           C  
ATOM   1160  O   ARG A 151      33.737  15.859   1.619  1.00 38.59           O  
ATOM   1161  CB  ARG A 151      34.127  13.505   3.646  1.00 36.17           C  
ATOM   1162  CG  ARG A 151      34.151  12.082   4.212  1.00 34.38           C  
ATOM   1163  CD  ARG A 151      32.892  11.797   5.024  1.00 33.81           C  
ATOM   1164  NE  ARG A 151      32.861  12.574   6.262  1.00 28.99           N  
ATOM   1165  CZ  ARG A 151      33.553  12.261   7.353  1.00 31.03           C  
ATOM   1166  NH1 ARG A 151      34.327  11.180   7.365  1.00 27.60           N1+
ATOM   1167  NH2 ARG A 151      33.485  13.037   8.430  1.00 29.16           N  
ATOM   1168  N   GLU A 152      31.806  15.744   2.786  1.00 36.65           N  
ATOM   1169  CA  GLU A 152      31.451  17.156   2.669  1.00 35.31           C  
ATOM   1170  C   GLU A 152      32.317  17.895   3.691  1.00 35.18           C  
ATOM   1171  O   GLU A 152      32.700  19.053   3.508  1.00 34.49           O  
ATOM   1172  CB  GLU A 152      29.969  17.319   3.010  1.00 36.90           C  
ATOM   1173  CG  GLU A 152      29.333  18.635   2.631  1.00 39.51           C  
ATOM   1174  CD  GLU A 152      27.937  18.774   3.226  1.00 44.04           C  
ATOM   1175  OE1 GLU A 152      27.217  17.754   3.320  1.00 45.86           O  
ATOM   1176  OE2 GLU A 152      27.555  19.901   3.595  1.00 45.35           O1-
ATOM   1177  N   PHE A 153      32.601  17.196   4.782  1.00 34.14           N  
ATOM   1178  CA  PHE A 153      33.437  17.697   5.864  1.00 34.81           C  
ATOM   1179  C   PHE A 153      34.175  16.450   6.338  1.00 36.33           C  
ATOM   1180  O   PHE A 153      33.591  15.361   6.388  1.00 38.38           O  
ATOM   1181  CB  PHE A 153      32.585  18.265   7.006  1.00 32.97           C  
ATOM   1182  CG  PHE A 153      31.673  19.388   6.592  1.00 32.44           C  
ATOM   1183  CD1 PHE A 153      32.185  20.644   6.276  1.00 29.92           C  
ATOM   1184  CD2 PHE A 153      30.295  19.182   6.507  1.00 32.39           C  
ATOM   1185  CE1 PHE A 153      31.341  21.683   5.880  1.00 31.35           C  
ATOM   1186  CE2 PHE A 153      29.439  20.209   6.113  1.00 31.80           C  
ATOM   1187  CZ  PHE A 153      29.964  21.466   5.797  1.00 32.62           C  
ATOM   1188  N   THR A 154      35.449  16.603   6.676  1.00 35.07           N  
ATOM   1189  CA  THR A 154      36.264  15.479   7.129  1.00 34.26           C  
ATOM   1190  C   THR A 154      36.375  15.412   8.645  1.00 32.78           C  
ATOM   1191  O   THR A 154      36.849  14.423   9.193  1.00 33.53           O  
ATOM   1192  CB  THR A 154      37.687  15.579   6.577  1.00 34.61           C  
ATOM   1193  OG1 THR A 154      38.226  16.859   6.923  1.00 35.72           O  
ATOM   1194  CG2 THR A 154      37.694  15.413   5.070  1.00 34.11           C  
ATOM   1195  N   GLY A 155      35.952  16.470   9.325  1.00 31.08           N  
ATOM   1196  CA  GLY A 155      36.036  16.468  10.771  1.00 28.74           C  
ATOM   1197  C   GLY A 155      35.524  17.748  11.390  1.00 28.39           C  
ATOM   1198  O   GLY A 155      35.127  18.671  10.686  1.00 28.17           O  
ATOM   1199  N   LEU A 156      35.547  17.795  12.716  1.00 27.41           N  
ATOM   1200  CA  LEU A 156      35.082  18.948  13.473  1.00 26.87           C  
ATOM   1201  C   LEU A 156      35.774  20.246  13.062  1.00 28.09           C  
ATOM   1202  O   LEU A 156      35.116  21.231  12.711  1.00 25.20           O  
ATOM   1203  CB  LEU A 156      35.287  18.688  14.971  1.00 26.75           C  
ATOM   1204  CG  LEU A 156      34.869  19.756  15.988  1.00 28.28           C  
ATOM   1205  CD1 LEU A 156      33.462  20.244  15.682  1.00 26.17           C  
ATOM   1206  CD2 LEU A 156      34.936  19.168  17.395  1.00 25.23           C  
ATOM   1207  N   GLY A 157      37.103  20.245  13.115  1.00 28.16           N  
ATOM   1208  CA  GLY A 157      37.854  21.431  12.751  1.00 28.78           C  
ATOM   1209  C   GLY A 157      37.592  21.857  11.319  1.00 30.35           C  
ATOM   1210  O   GLY A 157      37.374  23.039  11.051  1.00 29.73           O  
ATOM   1211  N   ASN A 158      37.613  20.889  10.405  1.00 31.57           N  
ATOM   1212  CA  ASN A 158      37.382  21.140   8.986  1.00 32.85           C  
ATOM   1213  C   ASN A 158      36.011  21.771   8.738  1.00 32.94           C  
ATOM   1214  O   ASN A 158      35.896  22.750   7.993  1.00 32.47           O  
ATOM   1215  CB  ASN A 158      37.496  19.835   8.191  1.00 33.71           C  
ATOM   1216  CG  ASN A 158      37.194  20.026   6.709  1.00 35.93           C  
ATOM   1217  OD1 ASN A 158      37.869  20.791   6.014  1.00 35.78           O  
ATOM   1218  ND2 ASN A 158      36.175  19.329   6.220  1.00 36.21           N  
ATOM   1219  N   CYS A 159      34.976  21.206   9.355  1.00 30.52           N  
ATOM   1220  CA  CYS A 159      33.621  21.737   9.207  1.00 28.52           C  
ATOM   1221  C   CYS A 159      33.578  23.207   9.621  1.00 28.15           C  
ATOM   1222  O   CYS A 159      33.199  24.082   8.836  1.00 27.77           O  
ATOM   1223  CB  CYS A 159      32.639  20.932  10.070  1.00 26.70           C  
ATOM   1224  SG  CYS A 159      30.922  21.525  10.033  1.00 26.26           S  
ATOM   1225  N   ILE A 160      33.977  23.472  10.861  1.00 28.21           N  
ATOM   1226  CA  ILE A 160      33.976  24.828  11.401  1.00 28.38           C  
ATOM   1227  C   ILE A 160      34.776  25.823  10.562  1.00 28.83           C  
ATOM   1228  O   ILE A 160      34.300  26.925  10.285  1.00 26.71           O  
ATOM   1229  CB  ILE A 160      34.493  24.819  12.858  1.00 28.63           C  
ATOM   1230  CG1 ILE A 160      33.371  24.325  13.781  1.00 30.48           C  
ATOM   1231  CG2 ILE A 160      34.983  26.195  13.265  1.00 28.51           C  
ATOM   1232  CD1 ILE A 160      33.777  24.137  15.217  1.00 29.88           C  
ATOM   1233  N   THR A 161      35.976  25.433  10.142  1.00 29.45           N  
ATOM   1234  CA  THR A 161      36.815  26.317   9.340  1.00 31.75           C  
ATOM   1235  C   THR A 161      36.259  26.524   7.933  1.00 31.84           C  
ATOM   1236  O   THR A 161      36.191  27.653   7.439  1.00 32.98           O  
ATOM   1237  CB  THR A 161      38.269  25.786   9.237  1.00 30.97           C  
ATOM   1238  OG1 THR A 161      38.266  24.468   8.676  1.00 34.83           O  
ATOM   1239  CG2 THR A 161      38.909  25.731  10.611  1.00 33.42           C  
ATOM   1240  N   LYS A 162      35.856  25.434   7.290  1.00 30.46           N  
ATOM   1241  CA  LYS A 162      35.317  25.520   5.943  1.00 31.04           C  
ATOM   1242  C   LYS A 162      34.104  26.451   5.911  1.00 31.41           C  
ATOM   1243  O   LYS A 162      34.026  27.351   5.071  1.00 31.87           O  
ATOM   1244  CB  LYS A 162      34.936  24.125   5.447  1.00 32.77           C  
ATOM   1245  CG  LYS A 162      34.549  24.062   3.981  1.00 36.48           C  
ATOM   1246  CD  LYS A 162      34.153  22.648   3.576  1.00 38.92           C  
ATOM   1247  CE  LYS A 162      33.453  22.636   2.222  1.00 43.02           C  
ATOM   1248  NZ  LYS A 162      32.740  21.347   1.967  1.00 46.05           N1+
ATOM   1249  N   ILE A 163      33.164  26.244   6.832  1.00 29.08           N  
ATOM   1250  CA  ILE A 163      31.969  27.080   6.889  1.00 27.74           C  
ATOM   1251  C   ILE A 163      32.340  28.525   7.223  1.00 28.40           C  
ATOM   1252  O   ILE A 163      31.808  29.468   6.634  1.00 27.72           O  
ATOM   1253  CB  ILE A 163      30.947  26.546   7.948  1.00 27.27           C  
ATOM   1254  CG1 ILE A 163      30.361  25.203   7.490  1.00 24.92           C  
ATOM   1255  CG2 ILE A 163      29.840  27.557   8.167  1.00 23.07           C  
ATOM   1256  CD1 ILE A 163      29.615  25.263   6.168  1.00 23.92           C  
ATOM   1257  N   PHE A 164      33.250  28.703   8.170  1.00 28.69           N  
ATOM   1258  CA  PHE A 164      33.670  30.045   8.547  1.00 32.74           C  
ATOM   1259  C   PHE A 164      34.173  30.830   7.334  1.00 34.42           C  
ATOM   1260  O   PHE A 164      33.791  31.982   7.129  1.00 32.65           O  
ATOM   1261  CB  PHE A 164      34.780  29.995   9.593  1.00 34.54           C  
ATOM   1262  CG  PHE A 164      35.243  31.351  10.028  1.00 37.65           C  
ATOM   1263  CD1 PHE A 164      34.369  32.221  10.672  1.00 38.20           C  
ATOM   1264  CD2 PHE A 164      36.537  31.781   9.756  1.00 39.21           C  
ATOM   1265  CE1 PHE A 164      34.774  33.500  11.036  1.00 39.81           C  
ATOM   1266  CE2 PHE A 164      36.953  33.064  10.118  1.00 40.43           C  
ATOM   1267  CZ  PHE A 164      36.067  33.923  10.758  1.00 40.09           C  
ATOM   1268  N   LYS A 165      35.029  30.197   6.534  1.00 34.20           N  
ATOM   1269  CA  LYS A 165      35.587  30.836   5.349  1.00 35.32           C  
ATOM   1270  C   LYS A 165      34.564  31.249   4.298  1.00 36.00           C  
ATOM   1271  O   LYS A 165      34.733  32.272   3.640  1.00 36.03           O  
ATOM   1272  CB  LYS A 165      36.615  29.924   4.684  1.00 36.15           C  
ATOM   1273  CG  LYS A 165      37.927  29.807   5.430  1.00 38.21           C  
ATOM   1274  CD  LYS A 165      38.903  28.960   4.639  1.00 40.90           C  
ATOM   1275  CE  LYS A 165      40.207  28.782   5.385  1.00 42.40           C  
ATOM   1276  NZ  LYS A 165      41.155  27.930   4.614  1.00 43.51           N1+
ATOM   1277  N   SER A 166      33.505  30.461   4.136  1.00 36.15           N  
ATOM   1278  CA  SER A 166      32.500  30.769   3.126  1.00 33.92           C  
ATOM   1279  C   SER A 166      31.352  31.642   3.608  1.00 33.40           C  
ATOM   1280  O   SER A 166      30.774  32.388   2.821  1.00 33.86           O  
ATOM   1281  CB  SER A 166      31.922  29.476   2.553  1.00 34.22           C  
ATOM   1282  OG  SER A 166      31.086  28.835   3.501  1.00 36.33           O  
ATOM   1283  N   ASP A 167      31.020  31.556   4.893  1.00 32.40           N  
ATOM   1284  CA  ASP A 167      29.899  32.318   5.435  1.00 31.94           C  
ATOM   1285  C   ASP A 167      30.274  33.235   6.583  1.00 33.22           C  
ATOM   1286  O   ASP A 167      29.480  34.086   6.977  1.00 33.34           O  
ATOM   1287  CB  ASP A 167      28.812  31.366   5.942  1.00 31.50           C  
ATOM   1288  CG  ASP A 167      28.248  30.476   4.855  1.00 34.51           C  
ATOM   1289  OD1 ASP A 167      28.965  30.189   3.874  1.00 34.28           O  
ATOM   1290  OD2 ASP A 167      27.084  30.041   4.997  1.00 34.35           O1-
ATOM   1291  N   GLY A 168      31.467  33.059   7.135  1.00 33.79           N  
ATOM   1292  CA  GLY A 168      31.860  33.879   8.266  1.00 35.34           C  
ATOM   1293  C   GLY A 168      31.162  33.338   9.500  1.00 36.33           C  
ATOM   1294  O   GLY A 168      30.649  32.219   9.471  1.00 37.34           O  
ATOM   1295  N   LEU A 169      31.126  34.125  10.573  1.00 37.35           N  
ATOM   1296  CA  LEU A 169      30.487  33.721  11.827  1.00 37.88           C  
ATOM   1297  C   LEU A 169      29.018  33.332  11.732  1.00 36.96           C  
ATOM   1298  O   LEU A 169      28.589  32.354  12.344  1.00 37.90           O  
ATOM   1299  CB  LEU A 169      30.599  34.829  12.874  1.00 40.14           C  
ATOM   1300  CG  LEU A 169      31.754  34.781  13.867  1.00 41.24           C  
ATOM   1301  CD1 LEU A 169      31.503  35.832  14.941  1.00 42.81           C  
ATOM   1302  CD2 LEU A 169      31.853  33.398  14.494  1.00 41.99           C  
ATOM   1303  N   ARG A 170      28.246  34.119  10.997  1.00 34.50           N  
ATOM   1304  CA  ARG A 170      26.819  33.865  10.843  1.00 33.23           C  
ATOM   1305  C   ARG A 170      26.533  32.431  10.397  1.00 32.51           C  
ATOM   1306  O   ARG A 170      25.518  31.842  10.777  1.00 31.17           O  
ATOM   1307  CB  ARG A 170      26.218  34.851   9.836  1.00 31.44           C  
ATOM   1308  N   GLY A 171      27.432  31.876   9.590  1.00 30.76           N  
ATOM   1309  CA  GLY A 171      27.250  30.521   9.112  1.00 28.99           C  
ATOM   1310  C   GLY A 171      27.276  29.504  10.240  1.00 28.09           C  
ATOM   1311  O   GLY A 171      26.501  28.546  10.226  1.00 24.82           O  
ATOM   1312  N   LEU A 172      28.158  29.723  11.216  1.00 26.64           N  
ATOM   1313  CA  LEU A 172      28.309  28.818  12.358  1.00 27.68           C  
ATOM   1314  C   LEU A 172      27.216  28.949  13.415  1.00 27.00           C  
ATOM   1315  O   LEU A 172      27.110  28.100  14.306  1.00 28.43           O  
ATOM   1316  CB  LEU A 172      29.663  29.040  13.036  1.00 25.58           C  
ATOM   1317  CG  LEU A 172      30.935  28.841  12.210  1.00 24.42           C  
ATOM   1318  CD1 LEU A 172      32.133  29.161  13.087  1.00 21.75           C  
ATOM   1319  CD2 LEU A 172      31.020  27.413  11.675  1.00 22.06           C  
ATOM   1320  N   TYR A 173      26.413  30.008  13.323  1.00 25.35           N  
ATOM   1321  CA  TYR A 173      25.339  30.242  14.289  1.00 24.01           C  
ATOM   1322  C   TYR A 173      23.930  30.178  13.704  1.00 22.94           C  
ATOM   1323  O   TYR A 173      22.975  30.587  14.360  1.00 20.02           O  
ATOM   1324  CB  TYR A 173      25.511  31.601  14.979  1.00 22.08           C  
ATOM   1325  CG  TYR A 173      26.642  31.650  15.972  1.00 24.01           C  
ATOM   1326  CD1 TYR A 173      27.955  31.819  15.544  1.00 22.22           C  
ATOM   1327  CD2 TYR A 173      26.406  31.484  17.347  1.00 24.96           C  
ATOM   1328  CE1 TYR A 173      29.010  31.817  16.442  1.00 21.59           C  
ATOM   1329  CE2 TYR A 173      27.465  31.481  18.261  1.00 22.39           C  
ATOM   1330  CZ  TYR A 173      28.768  31.645  17.792  1.00 23.46           C  
ATOM   1331  OH  TYR A 173      29.844  31.608  18.652  1.00 22.57           O  
ATOM   1332  N   GLN A 174      23.806  29.672  12.479  1.00 22.96           N  
ATOM   1333  CA  GLN A 174      22.504  29.552  11.818  1.00 25.49           C  
ATOM   1334  C   GLN A 174      21.498  28.785  12.680  1.00 23.59           C  
ATOM   1335  O   GLN A 174      21.749  27.646  13.068  1.00 22.36           O  
ATOM   1336  CB  GLN A 174      22.666  28.825  10.479  1.00 29.58           C  
ATOM   1337  CG  GLN A 174      23.159  29.690   9.341  1.00 36.86           C  
ATOM   1338  CD  GLN A 174      22.016  30.337   8.576  1.00 39.75           C  
ATOM   1339  OE1 GLN A 174      21.173  31.012   9.156  1.00 41.52           O  
ATOM   1340  NE2 GLN A 174      21.986  30.126   7.265  1.00 42.38           N  
ATOM   1341  N   GLY A 175      20.363  29.414  12.976  1.00 24.21           N  
ATOM   1342  CA  GLY A 175      19.339  28.763  13.774  1.00 24.29           C  
ATOM   1343  C   GLY A 175      19.408  29.090  15.254  1.00 26.50           C  
ATOM   1344  O   GLY A 175      18.664  28.525  16.057  1.00 24.95           O  
ATOM   1345  N   PHE A 176      20.296  30.008  15.617  1.00 26.46           N  
ATOM   1346  CA  PHE A 176      20.464  30.404  17.011  1.00 27.21           C  
ATOM   1347  C   PHE A 176      19.161  30.819  17.692  1.00 27.34           C  
ATOM   1348  O   PHE A 176      18.816  30.304  18.759  1.00 25.50           O  
ATOM   1349  CB  PHE A 176      21.456  31.567  17.125  1.00 28.52           C  
ATOM   1350  CG  PHE A 176      21.834  31.901  18.544  1.00 28.80           C  
ATOM   1351  CD1 PHE A 176      22.895  31.252  19.165  1.00 29.88           C  
ATOM   1352  CD2 PHE A 176      21.105  32.838  19.270  1.00 30.61           C  
ATOM   1353  CE1 PHE A 176      23.225  31.530  20.490  1.00 29.86           C  
ATOM   1354  CE2 PHE A 176      21.425  33.122  20.596  1.00 30.25           C  
ATOM   1355  CZ  PHE A 176      22.489  32.464  21.206  1.00 30.25           C  
ATOM   1356  N   ASN A 177      18.441  31.755  17.079  1.00 28.03           N  
ATOM   1357  CA  ASN A 177      17.198  32.248  17.665  1.00 29.21           C  
ATOM   1358  C   ASN A 177      16.095  31.222  17.900  1.00 26.13           C  
ATOM   1359  O   ASN A 177      15.487  31.203  18.970  1.00 23.94           O  
ATOM   1360  CB  ASN A 177      16.640  33.407  16.844  1.00 32.80           C  
ATOM   1361  CG  ASN A 177      17.416  34.686  17.057  1.00 40.16           C  
ATOM   1362  OD1 ASN A 177      18.518  34.851  16.535  1.00 45.31           O  
ATOM   1363  ND2 ASN A 177      16.852  35.597  17.840  1.00 45.49           N  
ATOM   1364  N   VAL A 178      15.815  30.378  16.916  1.00 24.29           N  
ATOM   1365  CA  VAL A 178      14.766  29.400  17.125  1.00 23.54           C  
ATOM   1366  C   VAL A 178      15.213  28.384  18.175  1.00 23.13           C  
ATOM   1367  O   VAL A 178      14.387  27.841  18.901  1.00 24.63           O  
ATOM   1368  CB  VAL A 178      14.359  28.689  15.808  1.00 26.00           C  
ATOM   1369  CG1 VAL A 178      15.449  27.729  15.350  1.00 24.97           C  
ATOM   1370  CG2 VAL A 178      13.029  27.957  16.015  1.00 23.93           C  
ATOM   1371  N   SER A 179      16.522  28.156  18.287  1.00 22.50           N  
ATOM   1372  CA  SER A 179      17.023  27.207  19.273  1.00 21.55           C  
ATOM   1373  C   SER A 179      16.751  27.721  20.688  1.00 22.55           C  
ATOM   1374  O   SER A 179      16.457  26.941  21.594  1.00 21.89           O  
ATOM   1375  CB  SER A 179      18.524  26.954  19.080  1.00 21.41           C  
ATOM   1376  OG  SER A 179      19.309  27.992  19.631  1.00 22.78           O  
ATOM   1377  N   VAL A 180      16.846  29.034  20.871  1.00 23.48           N  
ATOM   1378  CA  VAL A 180      16.590  29.649  22.169  1.00 24.00           C  
ATOM   1379  C   VAL A 180      15.093  29.588  22.479  1.00 26.11           C  
ATOM   1380  O   VAL A 180      14.693  29.357  23.627  1.00 24.89           O  
ATOM   1381  CB  VAL A 180      17.075  31.108  22.190  1.00 24.27           C  
ATOM   1382  CG1 VAL A 180      16.633  31.808  23.489  1.00 23.43           C  
ATOM   1383  CG2 VAL A 180      18.594  31.132  22.061  1.00 24.40           C  
ATOM   1384  N   GLN A 181      14.273  29.804  21.454  1.00 26.03           N  
ATOM   1385  CA  GLN A 181      12.822  29.723  21.610  1.00 26.77           C  
ATOM   1386  C   GLN A 181      12.536  28.285  22.034  1.00 27.33           C  
ATOM   1387  O   GLN A 181      11.716  28.030  22.920  1.00 28.77           O  
ATOM   1388  CB  GLN A 181      12.114  29.999  20.277  1.00 27.03           C  
ATOM   1389  CG  GLN A 181      12.155  31.433  19.795  1.00 31.63           C  
ATOM   1390  CD  GLN A 181      11.529  31.596  18.415  1.00 36.04           C  
ATOM   1391  OE1 GLN A 181      10.580  30.894  18.061  1.00 37.81           O  
ATOM   1392  NE2 GLN A 181      12.051  32.535  17.637  1.00 38.74           N  
ATOM   1393  N   GLY A 182      13.225  27.348  21.386  1.00 24.98           N  
ATOM   1394  CA  GLY A 182      13.048  25.946  21.708  1.00 24.81           C  
ATOM   1395  C   GLY A 182      13.437  25.625  23.140  1.00 24.03           C  
ATOM   1396  O   GLY A 182      12.801  24.797  23.793  1.00 23.34           O  
ATOM   1397  N   ILE A 183      14.489  26.270  23.632  1.00 23.17           N  
ATOM   1398  CA  ILE A 183      14.937  26.038  24.993  1.00 24.35           C  
ATOM   1399  C   ILE A 183      13.841  26.443  25.977  1.00 26.59           C  
ATOM   1400  O   ILE A 183      13.580  25.745  26.952  1.00 28.23           O  
ATOM   1401  CB  ILE A 183      16.224  26.834  25.296  1.00 25.17           C  
ATOM   1402  CG1 ILE A 183      17.425  26.125  24.659  1.00 23.10           C  
ATOM   1403  CG2 ILE A 183      16.409  26.994  26.810  1.00 23.70           C  
ATOM   1404  CD1 ILE A 183      18.717  26.872  24.803  1.00 23.94           C  
ATOM   1405  N   ILE A 184      13.195  27.568  25.700  1.00 27.09           N  
ATOM   1406  CA  ILE A 184      12.132  28.075  26.553  1.00 29.71           C  
ATOM   1407  C   ILE A 184      10.867  27.204  26.513  1.00 29.73           C  
ATOM   1408  O   ILE A 184      10.260  26.928  27.553  1.00 28.31           O  
ATOM   1409  CB  ILE A 184      11.778  29.517  26.153  1.00 29.91           C  
ATOM   1410  CG1 ILE A 184      12.950  30.443  26.496  1.00 30.38           C  
ATOM   1411  CG2 ILE A 184      10.506  29.960  26.859  1.00 30.32           C  
ATOM   1412  CD1 ILE A 184      12.905  31.781  25.780  1.00 31.18           C  
ATOM   1413  N   ILE A 185      10.471  26.788  25.313  1.00 29.84           N  
ATOM   1414  CA  ILE A 185       9.292  25.945  25.150  1.00 28.73           C  
ATOM   1415  C   ILE A 185       9.562  24.631  25.877  1.00 28.74           C  
ATOM   1416  O   ILE A 185       8.713  24.120  26.607  1.00 27.99           O  
ATOM   1417  CB  ILE A 185       9.016  25.639  23.653  1.00 29.02           C  
ATOM   1418  CG1 ILE A 185       8.669  26.930  22.898  1.00 28.66           C  
ATOM   1419  CG2 ILE A 185       7.884  24.626  23.527  1.00 27.11           C  
ATOM   1420  CD1 ILE A 185       7.311  27.533  23.254  1.00 32.40           C  
ATOM   1421  N   TYR A 186      10.757  24.093  25.665  1.00 26.58           N  
ATOM   1422  CA  TYR A 186      11.164  22.841  26.283  1.00 27.28           C  
ATOM   1423  C   TYR A 186      11.101  22.933  27.812  1.00 27.24           C  
ATOM   1424  O   TYR A 186      10.568  22.046  28.487  1.00 24.68           O  
ATOM   1425  CB  TYR A 186      12.592  22.500  25.846  1.00 25.98           C  
ATOM   1426  CG  TYR A 186      13.161  21.257  26.476  1.00 25.10           C  
ATOM   1427  CD1 TYR A 186      12.796  19.992  26.024  1.00 26.64           C  
ATOM   1428  CD2 TYR A 186      14.080  21.343  27.521  1.00 28.79           C  
ATOM   1429  CE1 TYR A 186      13.331  18.840  26.593  1.00 28.93           C  
ATOM   1430  CE2 TYR A 186      14.627  20.192  28.104  1.00 29.61           C  
ATOM   1431  CZ  TYR A 186      14.248  18.949  27.634  1.00 30.15           C  
ATOM   1432  OH  TYR A 186      14.777  17.813  28.203  1.00 34.01           O  
ATOM   1433  N   ARG A 187      11.655  24.010  28.351  1.00 27.24           N  
ATOM   1434  CA  ARG A 187      11.671  24.198  29.790  1.00 28.50           C  
ATOM   1435  C   ARG A 187      10.253  24.389  30.323  1.00 29.12           C  
ATOM   1436  O   ARG A 187       9.923  23.914  31.408  1.00 28.87           O  
ATOM   1437  CB  ARG A 187      12.542  25.404  30.145  1.00 29.95           C  
ATOM   1438  CG  ARG A 187      12.988  25.453  31.590  1.00 34.11           C  
ATOM   1439  CD  ARG A 187      13.878  26.662  31.854  1.00 34.65           C  
ATOM   1440  NE  ARG A 187      14.233  26.755  33.266  1.00 33.65           N  
ATOM   1441  CZ  ARG A 187      15.176  26.027  33.851  1.00 31.61           C  
ATOM   1442  NH1 ARG A 187      15.871  25.152  33.144  1.00 31.78           N1+
ATOM   1443  NH2 ARG A 187      15.412  26.163  35.147  1.00 34.55           N  
ATOM   1444  N   ALA A 188       9.410  25.065  29.548  1.00 29.16           N  
ATOM   1445  CA  ALA A 188       8.036  25.314  29.959  1.00 29.69           C  
ATOM   1446  C   ALA A 188       7.238  24.018  29.986  1.00 31.09           C  
ATOM   1447  O   ALA A 188       6.450  23.782  30.906  1.00 30.84           O  
ATOM   1448  CB  ALA A 188       7.377  26.318  29.018  1.00 30.69           C  
ATOM   1449  N   ALA A 189       7.457  23.172  28.985  1.00 30.88           N  
ATOM   1450  CA  ALA A 189       6.755  21.897  28.900  1.00 30.99           C  
ATOM   1451  C   ALA A 189       7.233  20.940  29.984  1.00 32.04           C  
ATOM   1452  O   ALA A 189       6.428  20.267  30.636  1.00 29.67           O  
ATOM   1453  CB  ALA A 189       6.963  21.271  27.516  1.00 28.26           C  
ATOM   1454  N   TYR A 190       8.548  20.887  30.172  1.00 33.23           N  
ATOM   1455  CA  TYR A 190       9.148  20.011  31.167  1.00 35.50           C  
ATOM   1456  C   TYR A 190       8.603  20.268  32.574  1.00 37.96           C  
ATOM   1457  O   TYR A 190       8.071  19.359  33.214  1.00 37.86           O  
ATOM   1458  CB  TYR A 190      10.674  20.176  31.158  1.00 36.82           C  
ATOM   1459  CG  TYR A 190      11.398  19.188  32.043  1.00 39.90           C  
ATOM   1460  CD1 TYR A 190      11.394  19.329  33.430  1.00 43.15           C  
ATOM   1461  CD2 TYR A 190      12.041  18.076  31.498  1.00 42.68           C  
ATOM   1462  CE1 TYR A 190      12.006  18.384  34.254  1.00 43.91           C  
ATOM   1463  CE2 TYR A 190      12.655  17.125  32.311  1.00 44.09           C  
ATOM   1464  CZ  TYR A 190      12.629  17.287  33.688  1.00 45.44           C  
ATOM   1465  OH  TYR A 190      13.210  16.344  34.502  1.00 47.50           O  
ATOM   1466  N   PHE A 191       8.737  21.505  33.051  1.00 39.12           N  
ATOM   1467  CA  PHE A 191       8.266  21.862  34.381  1.00 40.04           C  
ATOM   1468  C   PHE A 191       6.744  21.831  34.474  1.00 40.77           C  
ATOM   1469  O   PHE A 191       6.184  21.473  35.510  1.00 37.48           O  
ATOM   1470  CB  PHE A 191       8.786  23.250  34.780  1.00 42.01           C  
ATOM   1471  CG  PHE A 191      10.276  23.295  35.025  1.00 45.11           C  
ATOM   1472  CD1 PHE A 191      11.178  23.110  33.977  1.00 46.39           C  
ATOM   1473  CD2 PHE A 191      10.777  23.498  36.309  1.00 44.38           C  
ATOM   1474  CE1 PHE A 191      12.555  23.123  34.203  1.00 46.15           C  
ATOM   1475  CE2 PHE A 191      12.152  23.513  36.546  1.00 47.03           C  
ATOM   1476  CZ  PHE A 191      13.045  23.324  35.489  1.00 46.51           C  
ATOM   1477  N   GLY A 192       6.081  22.207  33.387  1.00 41.46           N  
ATOM   1478  CA  GLY A 192       4.631  22.206  33.374  1.00 43.12           C  
ATOM   1479  C   GLY A 192       4.082  20.804  33.549  1.00 44.52           C  
ATOM   1480  O   GLY A 192       3.152  20.588  34.328  1.00 44.84           O  
ATOM   1481  N   VAL A 193       4.664  19.851  32.825  1.00 46.13           N  
ATOM   1482  CA  VAL A 193       4.238  18.457  32.891  1.00 47.35           C  
ATOM   1483  C   VAL A 193       4.613  17.833  34.224  1.00 51.12           C  
ATOM   1484  O   VAL A 193       3.757  17.292  34.924  1.00 52.50           O  
ATOM   1485  CB  VAL A 193       4.874  17.609  31.759  1.00 44.94           C  
ATOM   1486  CG1 VAL A 193       4.575  16.135  31.979  1.00 44.14           C  
ATOM   1487  CG2 VAL A 193       4.330  18.046  30.412  1.00 42.46           C  
ATOM   1488  N   TYR A 194       5.891  17.909  34.577  1.00 54.34           N  
ATOM   1489  CA  TYR A 194       6.353  17.334  35.833  1.00 58.13           C  
ATOM   1490  C   TYR A 194       5.538  17.872  36.997  1.00 59.04           C  
ATOM   1491  O   TYR A 194       5.160  17.124  37.896  1.00 58.32           O  
ATOM   1492  CB  TYR A 194       7.832  17.645  36.060  1.00 60.56           C  
ATOM   1493  CG  TYR A 194       8.585  16.475  36.646  1.00 65.21           C  
ATOM   1494  CD1 TYR A 194       9.740  15.988  36.032  1.00 67.47           C  
ATOM   1495  CD2 TYR A 194       8.120  15.825  37.789  1.00 66.75           C  
ATOM   1496  CE1 TYR A 194      10.414  14.877  36.540  1.00 69.59           C  
ATOM   1497  CE2 TYR A 194       8.784  14.715  38.306  1.00 69.19           C  
ATOM   1498  CZ  TYR A 194       9.930  14.244  37.677  1.00 70.51           C  
ATOM   1499  OH  TYR A 194      10.588  13.140  38.181  1.00 72.09           O  
ATOM   1500  N   ASP A 195       5.267  19.172  36.969  1.00 60.43           N  
ATOM   1501  CA  ASP A 195       4.490  19.812  38.019  1.00 62.62           C  
ATOM   1502  C   ASP A 195       3.131  19.136  38.136  1.00 64.59           C  
ATOM   1503  O   ASP A 195       2.747  18.665  39.203  1.00 65.00           O  
ATOM   1504  CB  ASP A 195       4.295  21.294  37.703  1.00 62.77           C  
ATOM   1505  CG  ASP A 195       3.502  22.016  38.773  1.00 64.64           C  
ATOM   1506  OD1 ASP A 195       3.976  22.074  39.927  1.00 65.31           O  
ATOM   1507  OD2 ASP A 195       2.402  22.526  38.464  1.00 64.94           O1-
ATOM   1508  N   THR A 196       2.403  19.093  37.027  1.00 67.16           N  
ATOM   1509  CA  THR A 196       1.087  18.471  37.006  1.00 69.35           C  
ATOM   1510  C   THR A 196       1.196  16.991  37.355  1.00 71.41           C  
ATOM   1511  O   THR A 196       0.277  16.408  37.928  1.00 72.28           O  
ATOM   1512  CB  THR A 196       0.438  18.615  35.619  1.00 68.76           C  
ATOM   1513  OG1 THR A 196       0.269  20.005  35.318  1.00 68.24           O  
ATOM   1514  CG2 THR A 196      -0.913  17.923  35.586  1.00 68.39           C  
ATOM   1515  N   ALA A 197       2.331  16.392  37.009  1.00 73.79           N  
ATOM   1516  CA  ALA A 197       2.574  14.978  37.271  1.00 75.96           C  
ATOM   1517  C   ALA A 197       2.743  14.684  38.762  1.00 77.52           C  
ATOM   1518  O   ALA A 197       2.045  13.833  39.312  1.00 77.68           O  
ATOM   1519  CB  ALA A 197       3.814  14.513  36.508  1.00 75.56           C  
ATOM   1520  N   LYS A 198       3.669  15.392  39.407  1.00 79.47           N  
ATOM   1521  CA  LYS A 198       3.945  15.199  40.829  1.00 81.09           C  
ATOM   1522  C   LYS A 198       2.674  15.294  41.667  1.00 82.47           C  
ATOM   1523  O   LYS A 198       2.614  14.802  42.795  1.00 82.20           O  
ATOM   1524  CB  LYS A 198       4.979  16.218  41.319  1.00 80.66           C  
ATOM   1525  CG  LYS A 198       4.499  17.659  41.347  1.00 81.18           C  
ATOM   1526  CD  LYS A 198       5.617  18.586  41.808  1.00 82.07           C  
ATOM   1527  CE  LYS A 198       5.189  20.045  41.770  1.00 82.85           C  
ATOM   1528  NZ  LYS A 198       6.299  20.967  42.148  1.00 83.07           N1+
ATOM   1529  N   GLY A 199       1.657  15.929  41.103  1.00 83.80           N  
ATOM   1530  CA  GLY A 199       0.401  16.053  41.807  1.00 86.12           C  
ATOM   1531  C   GLY A 199      -0.375  14.755  41.716  1.00 88.02           C  
ATOM   1532  O   GLY A 199      -0.798  14.213  42.732  1.00 87.93           O  
ATOM   1533  N   MET A 200      -0.558  14.244  40.502  1.00 90.01           N  
ATOM   1534  CA  MET A 200      -1.307  13.005  40.312  1.00 92.66           C  
ATOM   1535  C   MET A 200      -0.445  11.769  40.158  1.00 94.52           C  
ATOM   1536  O   MET A 200       0.372  11.688  39.238  1.00 94.65           O  
ATOM   1537  CB  MET A 200      -2.216  13.103  39.084  1.00 92.97           C  
ATOM   1538  CG  MET A 200      -3.050  11.839  38.840  1.00 94.18           C  
ATOM   1539  SD  MET A 200      -3.982  11.832  37.289  1.00 95.95           S  
ATOM   1540  CE  MET A 200      -5.548  12.530  37.835  1.00 96.04           C  
ATOM   1541  N   LEU A 201      -0.632  10.819  41.073  1.00 97.10           N  
ATOM   1542  CA  LEU A 201       0.076   9.543  41.055  1.00 99.93           C  
ATOM   1543  C   LEU A 201       1.391   9.459  41.832  1.00101.75           C  
ATOM   1544  O   LEU A 201       1.842   8.361  42.162  1.00102.24           O  
ATOM   1545  CB  LEU A 201       0.313   9.099  39.610  1.00100.29           C  
ATOM   1546  CG  LEU A 201       0.636   7.629  39.300  1.00100.92           C  
ATOM   1547  CD1 LEU A 201      -0.540   6.746  39.717  1.00100.84           C  
ATOM   1548  CD2 LEU A 201       0.922   7.482  37.809  1.00100.86           C  
ATOM   1549  N   PRO A 202       2.027  10.600  42.146  1.00103.31           N  
ATOM   1550  CA  PRO A 202       3.266  10.384  42.885  1.00104.72           C  
ATOM   1551  C   PRO A 202       3.294  11.072  44.247  1.00105.83           C  
ATOM   1552  O   PRO A 202       3.925  12.117  44.388  1.00105.96           O  
ATOM   1553  CB  PRO A 202       4.304  10.961  41.944  1.00104.60           C  
ATOM   1554  CG  PRO A 202       3.578  12.185  41.370  1.00104.40           C  
ATOM   1555  CD  PRO A 202       2.067  11.925  41.507  1.00103.82           C  
ATOM   1556  N   ASP A 203       2.624  10.488  45.239  1.00106.91           N  
ATOM   1557  CA  ASP A 203       2.599  11.050  46.591  1.00107.57           C  
ATOM   1558  C   ASP A 203       4.004  10.883  47.171  1.00107.52           C  
ATOM   1559  O   ASP A 203       4.630   9.848  46.956  1.00107.79           O  
ATOM   1560  CB  ASP A 203       1.595  10.285  47.453  1.00108.28           C  
ATOM   1561  CG  ASP A 203       0.573   9.533  46.623  1.00108.73           C  
ATOM   1562  OD1 ASP A 203       0.961   8.555  45.944  1.00108.72           O  
ATOM   1563  OD2 ASP A 203      -0.614   9.921  46.641  1.00108.75           O1-
ATOM   1564  N   PRO A 204       4.498  11.871  47.946  1.00107.30           N  
ATOM   1565  CA  PRO A 204       5.840  11.791  48.531  1.00107.01           C  
ATOM   1566  C   PRO A 204       6.715  10.635  48.029  1.00106.56           C  
ATOM   1567  O   PRO A 204       7.245   9.842  48.811  1.00106.64           O  
ATOM   1568  CB  PRO A 204       5.533  11.732  50.017  1.00107.16           C  
ATOM   1569  CG  PRO A 204       4.463  12.816  50.118  1.00107.35           C  
ATOM   1570  CD  PRO A 204       3.638  12.703  48.810  1.00107.12           C  
ATOM   1571  N   LYS A 205       6.853  10.573  46.706  1.00105.83           N  
ATOM   1572  CA  LYS A 205       7.634   9.559  45.999  1.00104.98           C  
ATOM   1573  C   LYS A 205       8.134   8.379  46.825  1.00104.76           C  
ATOM   1574  O   LYS A 205       9.302   8.335  47.212  1.00105.25           O  
ATOM   1575  CB  LYS A 205       8.825  10.220  45.303  1.00104.58           C  
ATOM   1576  N   ASN A 206       7.249   7.422  47.084  1.00104.20           N  
ATOM   1577  CA  ASN A 206       7.602   6.224  47.843  1.00103.59           C  
ATOM   1578  C   ASN A 206       7.693   5.043  46.883  1.00103.17           C  
ATOM   1579  O   ASN A 206       8.257   3.997  47.210  1.00103.07           O  
ATOM   1580  CB  ASN A 206       6.541   5.932  48.906  1.00103.51           C  
ATOM   1581  CG  ASN A 206       6.534   6.957  50.019  1.00103.47           C  
ATOM   1582  OD1 ASN A 206       7.533   7.138  50.712  1.00103.35           O  
ATOM   1583  ND2 ASN A 206       5.404   7.631  50.199  1.00103.80           N  
ATOM   1584  N   VAL A 207       7.128   5.230  45.694  1.00102.65           N  
ATOM   1585  CA  VAL A 207       7.111   4.200  44.665  1.00101.75           C  
ATOM   1586  C   VAL A 207       8.502   3.690  44.323  1.00101.06           C  
ATOM   1587  O   VAL A 207       9.505   4.341  44.614  1.00101.02           O  
ATOM   1588  CB  VAL A 207       6.453   4.719  43.375  1.00102.27           C  
ATOM   1589  N   HIS A 208       8.544   2.519  43.696  1.00100.23           N  
ATOM   1590  CA  HIS A 208       9.795   1.883  43.302  1.00 99.70           C  
ATOM   1591  C   HIS A 208      10.639   2.786  42.411  1.00 98.93           C  
ATOM   1592  O   HIS A 208      10.111   3.595  41.648  1.00 99.16           O  
ATOM   1593  CB  HIS A 208       9.505   0.570  42.569  1.00100.48           C  
ATOM   1594  CG  HIS A 208       8.048   0.232  42.490  1.00101.28           C  
ATOM   1595  ND1 HIS A 208       7.260   0.072  43.609  1.00101.58           N  
ATOM   1596  CD2 HIS A 208       7.233   0.038  41.426  1.00101.38           C  
ATOM   1597  CE1 HIS A 208       6.022  -0.205  43.239  1.00101.57           C  
ATOM   1598  NE2 HIS A 208       5.979  -0.232  41.919  1.00101.52           N  
ATOM   1599  N   ILE A 209      11.956   2.636  42.516  1.00 97.60           N  
ATOM   1600  CA  ILE A 209      12.895   3.425  41.727  1.00 95.75           C  
ATOM   1601  C   ILE A 209      12.508   3.382  40.254  1.00 94.25           C  
ATOM   1602  O   ILE A 209      12.569   4.391  39.553  1.00 94.24           O  
ATOM   1603  CB  ILE A 209      14.330   2.876  41.865  1.00 95.88           C  
ATOM   1604  CG1 ILE A 209      14.673   2.679  43.342  1.00 96.10           C  
ATOM   1605  CG2 ILE A 209      15.318   3.837  41.217  1.00 95.69           C  
ATOM   1606  CD1 ILE A 209      16.004   1.993  43.581  1.00 96.09           C  
ATOM   1607  N   ILE A 210      12.107   2.200  39.797  1.00 92.42           N  
ATOM   1608  CA  ILE A 210      11.712   1.994  38.409  1.00 90.03           C  
ATOM   1609  C   ILE A 210      10.682   3.016  37.945  1.00 87.97           C  
ATOM   1610  O   ILE A 210      10.995   3.905  37.153  1.00 88.08           O  
ATOM   1611  CB  ILE A 210      11.133   0.580  38.203  1.00 90.33           C  
ATOM   1612  CG1 ILE A 210      12.160  -0.471  38.630  1.00 90.43           C  
ATOM   1613  CG2 ILE A 210      10.753   0.380  36.743  1.00 90.87           C  
ATOM   1614  CD1 ILE A 210      13.468  -0.409  37.862  1.00 90.42           C  
ATOM   1615  N   VAL A 211       9.454   2.887  38.437  1.00 85.35           N  
ATOM   1616  CA  VAL A 211       8.387   3.804  38.058  1.00 82.62           C  
ATOM   1617  C   VAL A 211       8.813   5.257  38.231  1.00 80.49           C  
ATOM   1618  O   VAL A 211       8.402   6.128  37.465  1.00 80.51           O  
ATOM   1619  CB  VAL A 211       7.114   3.558  38.889  1.00 82.62           C  
ATOM   1620  CG1 VAL A 211       6.589   2.156  38.628  1.00 82.23           C  
ATOM   1621  CG2 VAL A 211       7.411   3.752  40.362  1.00 82.79           C  
ATOM   1622  N   SER A 212       9.643   5.514  39.235  1.00 77.48           N  
ATOM   1623  CA  SER A 212      10.118   6.866  39.491  1.00 74.60           C  
ATOM   1624  C   SER A 212      11.053   7.315  38.367  1.00 72.45           C  
ATOM   1625  O   SER A 212      11.202   8.509  38.103  1.00 71.66           O  
ATOM   1626  CB  SER A 212      10.850   6.920  40.834  1.00 74.71           C  
ATOM   1627  OG  SER A 212      11.222   8.248  41.158  1.00 74.67           O  
ATOM   1628  N   TRP A 213      11.676   6.349  37.703  1.00 69.45           N  
ATOM   1629  CA  TRP A 213      12.589   6.642  36.608  1.00 66.79           C  
ATOM   1630  C   TRP A 213      11.799   6.839  35.323  1.00 65.24           C  
ATOM   1631  O   TRP A 213      12.010   7.802  34.589  1.00 63.55           O  
ATOM   1632  CB  TRP A 213      13.574   5.490  36.416  1.00 66.19           C  
ATOM   1633  CG  TRP A 213      14.649   5.790  35.425  1.00 65.15           C  
ATOM   1634  CD1 TRP A 213      15.724   6.609  35.607  1.00 64.90           C  
ATOM   1635  CD2 TRP A 213      14.749   5.286  34.088  1.00 65.20           C  
ATOM   1636  NE1 TRP A 213      16.491   6.646  34.468  1.00 64.97           N  
ATOM   1637  CE2 TRP A 213      15.917   5.842  33.519  1.00 65.10           C  
ATOM   1638  CE3 TRP A 213      13.967   4.417  33.316  1.00 64.92           C  
ATOM   1639  CZ2 TRP A 213      16.321   5.560  32.209  1.00 64.96           C  
ATOM   1640  CZ3 TRP A 213      14.368   4.135  32.014  1.00 65.22           C  
ATOM   1641  CH2 TRP A 213      15.538   4.706  31.475  1.00 65.48           C  
ATOM   1642  N   MET A 214      10.888   5.909  35.059  1.00 64.32           N  
ATOM   1643  CA  MET A 214      10.059   5.969  33.866  1.00 62.85           C  
ATOM   1644  C   MET A 214       9.310   7.293  33.813  1.00 60.40           C  
ATOM   1645  O   MET A 214       9.177   7.898  32.753  1.00 59.87           O  
ATOM   1646  CB  MET A 214       9.056   4.814  33.860  1.00 65.00           C  
ATOM   1647  CG  MET A 214       9.685   3.444  34.041  1.00 68.10           C  
ATOM   1648  SD  MET A 214       8.503   2.102  33.777  1.00 71.35           S  
ATOM   1649  CE  MET A 214       7.422   2.308  35.208  1.00 70.68           C  
ATOM   1650  N   ILE A 215       8.822   7.739  34.964  1.00 56.78           N  
ATOM   1651  CA  ILE A 215       8.086   8.991  35.033  1.00 54.48           C  
ATOM   1652  C   ILE A 215       8.981  10.160  34.634  1.00 51.78           C  
ATOM   1653  O   ILE A 215       8.546  11.063  33.921  1.00 49.99           O  
ATOM   1654  CB  ILE A 215       7.499   9.210  36.457  1.00 54.98           C  
ATOM   1655  CG1 ILE A 215       6.812  10.575  36.558  1.00 54.10           C  
ATOM   1656  CG2 ILE A 215       8.591   9.077  37.493  1.00 56.34           C  
ATOM   1657  CD1 ILE A 215       7.743  11.734  36.846  1.00 52.69           C  
ATOM   1658  N   ALA A 216      10.231  10.141  35.087  1.00 49.31           N  
ATOM   1659  CA  ALA A 216      11.165  11.208  34.747  1.00 47.58           C  
ATOM   1660  C   ALA A 216      11.465  11.163  33.250  1.00 45.35           C  
ATOM   1661  O   ALA A 216      11.629  12.199  32.612  1.00 44.90           O  
ATOM   1662  CB  ALA A 216      12.459  11.065  35.550  1.00 45.58           C  
ATOM   1663  N   GLN A 217      11.525   9.956  32.695  1.00 44.49           N  
ATOM   1664  CA  GLN A 217      11.801   9.785  31.274  1.00 44.33           C  
ATOM   1665  C   GLN A 217      10.619  10.254  30.444  1.00 43.32           C  
ATOM   1666  O   GLN A 217      10.788  10.860  29.380  1.00 42.37           O  
ATOM   1667  CB  GLN A 217      12.099   8.319  30.955  1.00 46.08           C  
ATOM   1668  CG  GLN A 217      13.378   7.816  31.584  1.00 50.18           C  
ATOM   1669  CD  GLN A 217      14.526   8.779  31.368  1.00 52.43           C  
ATOM   1670  OE1 GLN A 217      14.860   9.122  30.231  1.00 54.80           O  
ATOM   1671  NE2 GLN A 217      15.137   9.225  32.460  1.00 53.05           N  
ATOM   1672  N   THR A 218       9.421   9.969  30.941  1.00 40.11           N  
ATOM   1673  CA  THR A 218       8.201  10.357  30.261  1.00 38.42           C  
ATOM   1674  C   THR A 218       8.101  11.872  30.152  1.00 35.90           C  
ATOM   1675  O   THR A 218       7.719  12.396  29.109  1.00 35.00           O  
ATOM   1676  CB  THR A 218       6.970   9.794  30.989  1.00 39.89           C  
ATOM   1677  OG1 THR A 218       7.019   8.363  30.938  1.00 41.32           O  
ATOM   1678  CG2 THR A 218       5.679  10.273  30.325  1.00 40.02           C  
ATOM   1679  N   VAL A 219       8.450  12.575  31.225  1.00 35.43           N  
ATOM   1680  CA  VAL A 219       8.411  14.033  31.216  1.00 35.38           C  
ATOM   1681  C   VAL A 219       9.404  14.576  30.181  1.00 35.63           C  
ATOM   1682  O   VAL A 219       9.122  15.549  29.482  1.00 34.67           O  
ATOM   1683  CB  VAL A 219       8.766  14.607  32.605  1.00 37.27           C  
ATOM   1684  CG1 VAL A 219       8.954  16.109  32.524  1.00 36.80           C  
ATOM   1685  CG2 VAL A 219       7.659  14.275  33.601  1.00 39.21           C  
ATOM   1686  N   THR A 220      10.563  13.931  30.090  1.00 34.38           N  
ATOM   1687  CA  THR A 220      11.606  14.331  29.153  1.00 33.70           C  
ATOM   1688  C   THR A 220      11.152  14.125  27.709  1.00 34.06           C  
ATOM   1689  O   THR A 220      11.327  15.006  26.862  1.00 32.92           O  
ATOM   1690  CB  THR A 220      12.903  13.519  29.405  1.00 33.54           C  
ATOM   1691  OG1 THR A 220      13.444  13.877  30.682  1.00 33.52           O  
ATOM   1692  CG2 THR A 220      13.941  13.793  28.322  1.00 34.85           C  
ATOM   1693  N   ALA A 221      10.564  12.961  27.441  1.00 32.81           N  
ATOM   1694  CA  ALA A 221      10.081  12.629  26.106  1.00 31.37           C  
ATOM   1695  C   ALA A 221       8.995  13.602  25.662  1.00 30.99           C  
ATOM   1696  O   ALA A 221       9.019  14.101  24.540  1.00 30.44           O  
ATOM   1697  CB  ALA A 221       9.547  11.203  26.083  1.00 30.23           C  
ATOM   1698  N   VAL A 222       8.042  13.877  26.545  1.00 29.77           N  
ATOM   1699  CA  VAL A 222       6.967  14.800  26.210  1.00 28.91           C  
ATOM   1700  C   VAL A 222       7.493  16.210  25.962  1.00 29.25           C  
ATOM   1701  O   VAL A 222       7.074  16.873  25.004  1.00 30.66           O  
ATOM   1702  CB  VAL A 222       5.895  14.854  27.323  1.00 29.23           C  
ATOM   1703  CG1 VAL A 222       4.859  15.919  26.996  1.00 26.59           C  
ATOM   1704  CG2 VAL A 222       5.216  13.493  27.454  1.00 29.56           C  
ATOM   1705  N   ALA A 223       8.399  16.681  26.820  1.00 27.05           N  
ATOM   1706  CA  ALA A 223       8.959  18.023  26.646  1.00 25.85           C  
ATOM   1707  C   ALA A 223       9.725  18.082  25.325  1.00 25.37           C  
ATOM   1708  O   ALA A 223       9.722  19.102  24.641  1.00 23.92           O  
ATOM   1709  CB  ALA A 223       9.892  18.374  27.805  1.00 23.64           C  
ATOM   1710  N   GLY A 224      10.376  16.974  24.980  1.00 23.54           N  
ATOM   1711  CA  GLY A 224      11.137  16.913  23.748  1.00 23.61           C  
ATOM   1712  C   GLY A 224      10.244  16.931  22.521  1.00 25.36           C  
ATOM   1713  O   GLY A 224      10.610  17.504  21.493  1.00 23.35           O  
ATOM   1714  N   LEU A 225       9.075  16.301  22.625  1.00 24.00           N  
ATOM   1715  CA  LEU A 225       8.132  16.250  21.517  1.00 25.61           C  
ATOM   1716  C   LEU A 225       7.490  17.607  21.243  1.00 26.04           C  
ATOM   1717  O   LEU A 225       7.422  18.053  20.097  1.00 27.50           O  
ATOM   1718  CB  LEU A 225       7.044  15.204  21.799  1.00 25.13           C  
ATOM   1719  CG  LEU A 225       7.519  13.758  21.624  1.00 26.74           C  
ATOM   1720  CD1 LEU A 225       6.555  12.782  22.292  1.00 26.22           C  
ATOM   1721  CD2 LEU A 225       7.665  13.463  20.134  1.00 28.00           C  
ATOM   1722  N   VAL A 226       7.029  18.256  22.308  1.00 26.77           N  
ATOM   1723  CA  VAL A 226       6.383  19.558  22.223  1.00 25.27           C  
ATOM   1724  C   VAL A 226       7.289  20.603  21.576  1.00 25.55           C  
ATOM   1725  O   VAL A 226       6.827  21.445  20.804  1.00 23.26           O  
ATOM   1726  CB  VAL A 226       5.981  20.058  23.637  1.00 27.52           C  
ATOM   1727  CG1 VAL A 226       5.463  21.483  23.566  1.00 28.54           C  
ATOM   1728  CG2 VAL A 226       4.921  19.134  24.239  1.00 28.90           C  
ATOM   1729  N   SER A 227       8.579  20.553  21.894  1.00 23.16           N  
ATOM   1730  CA  SER A 227       9.517  21.516  21.342  1.00 22.07           C  
ATOM   1731  C   SER A 227      10.216  21.035  20.068  1.00 23.14           C  
ATOM   1732  O   SER A 227      10.958  21.797  19.449  1.00 21.27           O  
ATOM   1733  CB  SER A 227      10.573  21.881  22.401  1.00 22.96           C  
ATOM   1734  OG  SER A 227      11.399  20.776  22.739  1.00 21.23           O  
ATOM   1735  N   TYR A 228       9.965  19.784  19.671  1.00 21.92           N  
ATOM   1736  CA  TYR A 228      10.624  19.204  18.503  1.00 22.41           C  
ATOM   1737  C   TYR A 228      10.561  20.051  17.230  1.00 23.16           C  
ATOM   1738  O   TYR A 228      11.560  20.194  16.534  1.00 23.23           O  
ATOM   1739  CB  TYR A 228      10.078  17.797  18.211  1.00 20.93           C  
ATOM   1740  CG  TYR A 228      11.010  16.979  17.341  1.00 19.48           C  
ATOM   1741  CD1 TYR A 228      12.124  16.332  17.890  1.00 16.35           C  
ATOM   1742  CD2 TYR A 228      10.816  16.901  15.964  1.00 15.80           C  
ATOM   1743  CE1 TYR A 228      13.021  15.630  17.081  1.00 17.28           C  
ATOM   1744  CE2 TYR A 228      11.701  16.210  15.149  1.00 18.28           C  
ATOM   1745  CZ  TYR A 228      12.803  15.577  15.712  1.00 19.55           C  
ATOM   1746  OH  TYR A 228      13.685  14.909  14.897  1.00 20.68           O  
ATOM   1747  N   PRO A 229       9.385  20.610  16.900  1.00 24.29           N  
ATOM   1748  CA  PRO A 229       9.295  21.433  15.686  1.00 23.93           C  
ATOM   1749  C   PRO A 229      10.361  22.526  15.645  1.00 25.37           C  
ATOM   1750  O   PRO A 229      10.956  22.791  14.594  1.00 23.22           O  
ATOM   1751  CB  PRO A 229       7.881  21.995  15.761  1.00 23.34           C  
ATOM   1752  CG  PRO A 229       7.125  20.834  16.360  1.00 25.65           C  
ATOM   1753  CD  PRO A 229       8.050  20.400  17.492  1.00 23.26           C  
ATOM   1754  N   PHE A 230      10.604  23.156  16.791  1.00 24.45           N  
ATOM   1755  CA  PHE A 230      11.614  24.209  16.859  1.00 25.26           C  
ATOM   1756  C   PHE A 230      13.000  23.635  16.568  1.00 22.72           C  
ATOM   1757  O   PHE A 230      13.841  24.302  15.966  1.00 20.67           O  
ATOM   1758  CB  PHE A 230      11.598  24.889  18.237  1.00 25.48           C  
ATOM   1759  CG  PHE A 230      10.334  25.672  18.513  1.00 28.98           C  
ATOM   1760  CD1 PHE A 230       9.140  25.017  18.802  1.00 28.67           C  
ATOM   1761  CD2 PHE A 230      10.332  27.065  18.437  1.00 28.76           C  
ATOM   1762  CE1 PHE A 230       7.963  25.731  19.009  1.00 30.15           C  
ATOM   1763  CE2 PHE A 230       9.159  27.791  18.641  1.00 29.47           C  
ATOM   1764  CZ  PHE A 230       7.971  27.121  18.927  1.00 30.80           C  
ATOM   1765  N   ASP A 231      13.228  22.390  16.976  1.00 21.20           N  
ATOM   1766  CA  ASP A 231      14.517  21.756  16.756  1.00 18.76           C  
ATOM   1767  C   ASP A 231      14.711  21.462  15.280  1.00 20.47           C  
ATOM   1768  O   ASP A 231      15.820  21.589  14.741  1.00 19.84           O  
ATOM   1769  CB  ASP A 231      14.627  20.461  17.556  1.00 20.12           C  
ATOM   1770  CG  ASP A 231      15.987  19.809  17.406  1.00 22.35           C  
ATOM   1771  OD1 ASP A 231      16.983  20.403  17.876  1.00 20.91           O  
ATOM   1772  OD2 ASP A 231      16.060  18.712  16.811  1.00 22.51           O1-
ATOM   1773  N   THR A 232      13.629  21.050  14.627  1.00 19.00           N  
ATOM   1774  CA  THR A 232      13.696  20.763  13.209  1.00 19.80           C  
ATOM   1775  C   THR A 232      14.021  22.010  12.377  1.00 19.40           C  
ATOM   1776  O   THR A 232      14.921  21.958  11.530  1.00 19.60           O  
ATOM   1777  CB  THR A 232      12.398  20.124  12.709  1.00 19.62           C  
ATOM   1778  OG1 THR A 232      12.265  18.821  13.289  1.00 20.79           O  
ATOM   1779  CG2 THR A 232      12.413  19.999  11.197  1.00 18.87           C  
ATOM   1780  N   VAL A 233      13.343  23.137  12.605  1.00 20.03           N  
ATOM   1781  CA  VAL A 233      13.689  24.296  11.778  1.00 21.51           C  
ATOM   1782  C   VAL A 233      15.105  24.759  12.124  1.00 21.85           C  
ATOM   1783  O   VAL A 233      15.831  25.243  11.252  1.00 24.10           O  
ATOM   1784  CB  VAL A 233      12.645  25.487  11.858  1.00 24.54           C  
ATOM   1785  CG1 VAL A 233      11.321  25.013  12.429  1.00 22.18           C  
ATOM   1786  CG2 VAL A 233      13.221  26.683  12.588  1.00 20.49           C  
ATOM   1787  N   ARG A 234      15.506  24.585  13.382  1.00 19.30           N  
ATOM   1788  CA  ARG A 234      16.865  24.935  13.796  1.00 21.77           C  
ATOM   1789  C   ARG A 234      17.890  24.200  12.916  1.00 22.54           C  
ATOM   1790  O   ARG A 234      18.747  24.831  12.301  1.00 25.38           O  
ATOM   1791  CB  ARG A 234      17.123  24.540  15.258  1.00 20.53           C  
ATOM   1792  CG  ARG A 234      18.530  24.888  15.737  1.00 21.00           C  
ATOM   1793  CD  ARG A 234      18.941  24.148  17.023  1.00 21.91           C  
ATOM   1794  NE  ARG A 234      20.275  24.559  17.460  1.00 20.67           N  
ATOM   1795  CZ  ARG A 234      20.944  24.039  18.488  1.00 21.47           C  
ATOM   1796  NH1 ARG A 234      20.414  23.060  19.217  1.00 19.98           N1+
ATOM   1797  NH2 ARG A 234      22.148  24.510  18.797  1.00 19.49           N  
ATOM   1798  N   ARG A 235      17.794  22.869  12.863  1.00 21.97           N  
ATOM   1799  CA  ARG A 235      18.724  22.047  12.079  1.00 22.14           C  
ATOM   1800  C   ARG A 235      18.611  22.319  10.583  1.00 21.17           C  
ATOM   1801  O   ARG A 235      19.611  22.312   9.866  1.00 21.97           O  
ATOM   1802  CB  ARG A 235      18.469  20.552  12.307  1.00 23.74           C  
ATOM   1803  CG  ARG A 235      18.252  20.127  13.747  1.00 26.76           C  
ATOM   1804  CD  ARG A 235      19.523  20.041  14.551  1.00 26.87           C  
ATOM   1805  NE  ARG A 235      19.217  19.760  15.951  1.00 26.21           N  
ATOM   1806  CZ  ARG A 235      20.126  19.496  16.884  1.00 27.20           C  
ATOM   1807  NH1 ARG A 235      21.413  19.461  16.568  1.00 24.81           N1+
ATOM   1808  NH2 ARG A 235      19.751  19.303  18.140  1.00 25.51           N  
ATOM   1809  N   ARG A 236      17.390  22.524  10.106  1.00 19.92           N  
ATOM   1810  CA  ARG A 236      17.185  22.803   8.690  1.00 21.62           C  
ATOM   1811  C   ARG A 236      17.896  24.110   8.327  1.00 21.93           C  
ATOM   1812  O   ARG A 236      18.430  24.248   7.226  1.00 20.22           O  
ATOM   1813  CB  ARG A 236      15.687  22.901   8.374  1.00 22.56           C  
ATOM   1814  CG  ARG A 236      14.953  21.562   8.406  1.00 19.69           C  
ATOM   1815  CD  ARG A 236      15.487  20.606   7.341  1.00 22.92           C  
ATOM   1816  NE  ARG A 236      14.671  19.398   7.258  1.00 24.15           N  
ATOM   1817  CZ  ARG A 236      13.498  19.323   6.633  1.00 23.12           C  
ATOM   1818  NH1 ARG A 236      12.999  20.381   6.014  1.00 22.22           N1+
ATOM   1819  NH2 ARG A 236      12.803  18.199   6.667  1.00 23.09           N  
ATOM   1820  N   MET A 237      17.911  25.060   9.261  1.00 19.96           N  
ATOM   1821  CA  MET A 237      18.594  26.321   9.023  1.00 23.06           C  
ATOM   1822  C   MET A 237      20.108  26.080   9.001  1.00 23.40           C  
ATOM   1823  O   MET A 237      20.819  26.675   8.189  1.00 21.98           O  
ATOM   1824  CB  MET A 237      18.241  27.344  10.108  1.00 24.05           C  
ATOM   1825  CG  MET A 237      16.817  27.871  10.018  1.00 28.11           C  
ATOM   1826  SD  MET A 237      16.510  28.639   8.421  1.00 33.30           S  
ATOM   1827  CE  MET A 237      17.321  30.223   8.659  1.00 32.32           C  
ATOM   1828  N   MET A 238      20.595  25.202   9.880  1.00 21.78           N  
ATOM   1829  CA  MET A 238      22.029  24.896   9.934  1.00 21.23           C  
ATOM   1830  C   MET A 238      22.485  24.336   8.595  1.00 21.00           C  
ATOM   1831  O   MET A 238      23.624  24.544   8.177  1.00 20.71           O  
ATOM   1832  CB  MET A 238      22.341  23.840  10.999  1.00 21.55           C  
ATOM   1833  CG  MET A 238      22.141  24.240  12.442  1.00 20.66           C  
ATOM   1834  SD  MET A 238      22.521  22.800  13.487  1.00 21.95           S  
ATOM   1835  CE  MET A 238      22.774  23.587  15.075  1.00 19.61           C  
ATOM   1836  N   MET A 239      21.592  23.599   7.944  1.00 20.16           N  
ATOM   1837  CA  MET A 239      21.899  22.993   6.657  1.00 20.88           C  
ATOM   1838  C   MET A 239      22.082  24.041   5.565  1.00 21.08           C  
ATOM   1839  O   MET A 239      22.603  23.737   4.506  1.00 22.21           O  
ATOM   1840  CB  MET A 239      20.783  22.027   6.243  1.00 21.57           C  
ATOM   1841  CG  MET A 239      20.633  20.810   7.138  1.00 23.39           C  
ATOM   1842  SD  MET A 239      22.123  19.793   7.178  1.00 26.07           S  
ATOM   1843  CE  MET A 239      22.024  18.960   5.592  1.00 24.95           C  
ATOM   1844  N   GLN A 240      21.656  25.274   5.817  1.00 22.35           N  
ATOM   1845  CA  GLN A 240      21.795  26.317   4.809  1.00 24.40           C  
ATOM   1846  C   GLN A 240      23.201  26.894   4.718  1.00 25.33           C  
ATOM   1847  O   GLN A 240      23.599  27.387   3.662  1.00 26.05           O  
ATOM   1848  CB  GLN A 240      20.789  27.437   5.063  1.00 23.83           C  
ATOM   1849  CG  GLN A 240      19.354  26.931   5.079  1.00 26.89           C  
ATOM   1850  CD  GLN A 240      19.080  25.956   3.949  1.00 26.90           C  
ATOM   1851  OE1 GLN A 240      19.170  26.306   2.772  1.00 28.78           O  
ATOM   1852  NE2 GLN A 240      18.758  24.721   4.304  1.00 26.28           N  
ATOM   1853  N   SER A 241      23.959  26.826   5.811  1.00 23.21           N  
ATOM   1854  CA  SER A 241      25.315  27.366   5.800  1.00 24.58           C  
ATOM   1855  C   SER A 241      26.128  26.722   4.687  1.00 24.80           C  
ATOM   1856  O   SER A 241      26.029  25.521   4.450  1.00 24.10           O  
ATOM   1857  CB  SER A 241      26.005  27.133   7.143  1.00 22.19           C  
ATOM   1858  OG  SER A 241      25.234  27.676   8.205  1.00 25.51           O  
ATOM   1859  N   GLY A 242      26.916  27.535   3.989  1.00 27.46           N  
ATOM   1860  CA  GLY A 242      27.736  27.017   2.908  1.00 28.83           C  
ATOM   1861  C   GLY A 242      27.067  27.134   1.551  1.00 32.03           C  
ATOM   1862  O   GLY A 242      27.742  27.091   0.523  1.00 34.95           O  
ATOM   1863  N   ARG A 243      25.744  27.267   1.533  1.00 31.24           N  
ATOM   1864  CA  ARG A 243      25.025  27.404   0.272  1.00 32.81           C  
ATOM   1865  C   ARG A 243      25.040  28.859  -0.182  1.00 32.90           C  
ATOM   1866  O   ARG A 243      25.128  29.770   0.635  1.00 34.13           O  
ATOM   1867  CB  ARG A 243      23.578  26.939   0.424  1.00 32.10           C  
ATOM   1868  CG  ARG A 243      23.412  25.446   0.635  1.00 32.18           C  
ATOM   1869  CD  ARG A 243      21.941  25.090   0.570  1.00 33.11           C  
ATOM   1870  NE  ARG A 243      21.698  23.660   0.721  1.00 31.87           N  
ATOM   1871  CZ  ARG A 243      20.840  22.975  -0.029  1.00 31.90           C  
ATOM   1872  NH1 ARG A 243      20.153  23.593  -0.981  1.00 29.52           N1+
ATOM   1873  NH2 ARG A 243      20.663  21.678   0.176  1.00 30.88           N  
ATOM   1874  N   LYS A 244      24.943  29.084  -1.486  1.00 34.86           N  
ATOM   1875  CA  LYS A 244      24.954  30.446  -1.995  1.00 35.48           C  
ATOM   1876  C   LYS A 244      23.839  30.700  -2.981  1.00 35.01           C  
ATOM   1877  O   LYS A 244      23.267  29.769  -3.547  1.00 35.17           O  
ATOM   1878  CB  LYS A 244      26.300  30.753  -2.664  1.00 37.65           C  
ATOM   1879  CG  LYS A 244      27.484  30.704  -1.714  1.00 41.07           C  
ATOM   1880  CD  LYS A 244      27.389  31.792  -0.654  1.00 43.51           C  
ATOM   1881  CE  LYS A 244      28.431  31.591   0.437  1.00 44.33           C  
ATOM   1882  NZ  LYS A 244      28.222  30.293   1.146  1.00 46.34           N1+
ATOM   1883  N   GLY A 245      23.542  31.980  -3.172  1.00 35.64           N  
ATOM   1884  CA  GLY A 245      22.518  32.403  -4.108  1.00 35.84           C  
ATOM   1885  C   GLY A 245      21.223  31.629  -4.094  1.00 35.70           C  
ATOM   1886  O   GLY A 245      20.652  31.375  -3.036  1.00 37.31           O  
ATOM   1887  N   ALA A 246      20.763  31.261  -5.286  1.00 35.77           N  
ATOM   1888  CA  ALA A 246      19.521  30.528  -5.455  1.00 35.22           C  
ATOM   1889  C   ALA A 246      19.570  29.139  -4.834  1.00 35.67           C  
ATOM   1890  O   ALA A 246      18.565  28.433  -4.807  1.00 36.01           O  
ATOM   1891  CB  ALA A 246      19.188  30.418  -6.932  1.00 36.19           C  
ATOM   1892  N   ASP A 247      20.735  28.739  -4.343  1.00 35.01           N  
ATOM   1893  CA  ASP A 247      20.854  27.425  -3.733  1.00 36.52           C  
ATOM   1894  C   ASP A 247      20.259  27.407  -2.331  1.00 34.67           C  
ATOM   1895  O   ASP A 247      19.957  26.346  -1.789  1.00 34.01           O  
ATOM   1896  CB  ASP A 247      22.315  27.003  -3.654  1.00 39.20           C  
ATOM   1897  CG  ASP A 247      22.576  25.717  -4.385  1.00 43.20           C  
ATOM   1898  OD1 ASP A 247      22.701  25.767  -5.630  1.00 44.94           O  
ATOM   1899  OD2 ASP A 247      22.640  24.659  -3.718  1.00 41.38           O1-
ATOM   1900  N   ILE A 248      20.106  28.591  -1.751  1.00 32.06           N  
ATOM   1901  CA  ILE A 248      19.562  28.731  -0.408  1.00 30.04           C  
ATOM   1902  C   ILE A 248      18.079  28.359  -0.368  1.00 30.00           C  
ATOM   1903  O   ILE A 248      17.251  28.959  -1.054  1.00 30.27           O  
ATOM   1904  CB  ILE A 248      19.786  30.173   0.098  1.00 28.89           C  
ATOM   1905  CG1 ILE A 248      21.297  30.415   0.256  1.00 29.37           C  
ATOM   1906  CG2 ILE A 248      19.055  30.399   1.413  1.00 28.87           C  
ATOM   1907  CD1 ILE A 248      21.695  31.875   0.499  1.00 28.29           C  
ATOM   1908  N   MET A 249      17.754  27.355   0.440  1.00 27.59           N  
ATOM   1909  CA  MET A 249      16.381  26.881   0.566  1.00 27.04           C  
ATOM   1910  C   MET A 249      15.515  27.763   1.459  1.00 25.64           C  
ATOM   1911  O   MET A 249      14.320  27.895   1.222  1.00 19.65           O  
ATOM   1912  CB  MET A 249      16.369  25.456   1.129  1.00 29.08           C  
ATOM   1913  CG  MET A 249      17.165  24.446   0.324  1.00 29.19           C  
ATOM   1914  SD  MET A 249      17.283  22.862   1.185  1.00 32.13           S  
ATOM   1915  CE  MET A 249      15.571  22.291   1.087  1.00 27.78           C  
ATOM   1916  N   TYR A 250      16.120  28.350   2.491  1.00 26.04           N  
ATOM   1917  CA  TYR A 250      15.390  29.201   3.429  1.00 27.92           C  
ATOM   1918  C   TYR A 250      16.123  30.519   3.642  1.00 29.99           C  
ATOM   1919  O   TYR A 250      17.309  30.529   3.987  1.00 29.10           O  
ATOM   1920  CB  TYR A 250      15.240  28.500   4.784  1.00 24.49           C  
ATOM   1921  CG  TYR A 250      14.806  27.055   4.698  1.00 23.06           C  
ATOM   1922  CD1 TYR A 250      13.521  26.712   4.292  1.00 19.71           C  
ATOM   1923  CD2 TYR A 250      15.691  26.028   5.029  1.00 24.09           C  
ATOM   1924  CE1 TYR A 250      13.126  25.386   4.218  1.00 23.32           C  
ATOM   1925  CE2 TYR A 250      15.311  24.697   4.959  1.00 21.68           C  
ATOM   1926  CZ  TYR A 250      14.031  24.379   4.555  1.00 24.39           C  
ATOM   1927  OH  TYR A 250      13.662  23.057   4.482  1.00 23.95           O  
ATOM   1928  N   THR A 251      15.404  31.622   3.459  1.00 31.91           N  
ATOM   1929  CA  THR A 251      15.978  32.957   3.610  1.00 36.09           C  
ATOM   1930  C   THR A 251      16.006  33.404   5.067  1.00 36.60           C  
ATOM   1931  O   THR A 251      16.731  34.331   5.431  1.00 37.52           O  
ATOM   1932  CB  THR A 251      15.189  33.999   2.790  1.00 36.00           C  
ATOM   1933  OG1 THR A 251      13.838  34.066   3.268  1.00 39.20           O  
ATOM   1934  CG2 THR A 251      15.181  33.618   1.320  1.00 37.85           C  
ATOM   1935  N   GLY A 252      15.211  32.739   5.897  1.00 36.79           N  
ATOM   1936  CA  GLY A 252      15.164  33.074   7.309  1.00 34.43           C  
ATOM   1937  C   GLY A 252      14.353  32.037   8.061  1.00 33.28           C  
ATOM   1938  O   GLY A 252      13.733  31.176   7.448  1.00 31.96           O  
ATOM   1939  N   THR A 253      14.354  32.124   9.386  1.00 32.80           N  
ATOM   1940  CA  THR A 253      13.617  31.191  10.227  1.00 33.65           C  
ATOM   1941  C   THR A 253      12.138  31.113   9.860  1.00 32.19           C  
ATOM   1942  O   THR A 253      11.576  30.026   9.737  1.00 31.26           O  
ATOM   1943  CB  THR A 253      13.718  31.590  11.711  1.00 34.61           C  
ATOM   1944  OG1 THR A 253      15.096  31.609  12.103  1.00 38.25           O  
ATOM   1945  CG2 THR A 253      12.951  30.600  12.585  1.00 32.45           C  
ATOM   1946  N   VAL A 254      11.513  32.273   9.701  1.00 31.48           N  
ATOM   1947  CA  VAL A 254      10.103  32.339   9.356  1.00 31.94           C  
ATOM   1948  C   VAL A 254       9.861  31.663   8.017  1.00 31.37           C  
ATOM   1949  O   VAL A 254       8.902  30.904   7.854  1.00 31.89           O  
ATOM   1950  CB  VAL A 254       9.618  33.805   9.290  1.00 33.13           C  
ATOM   1951  CG1 VAL A 254       8.195  33.862   8.747  1.00 32.60           C  
ATOM   1952  CG2 VAL A 254       9.669  34.425  10.683  1.00 33.65           C  
ATOM   1953  N   ASP A 255      10.741  31.936   7.061  1.00 29.19           N  
ATOM   1954  CA  ASP A 255      10.629  31.342   5.737  1.00 29.04           C  
ATOM   1955  C   ASP A 255      10.791  29.827   5.854  1.00 27.72           C  
ATOM   1956  O   ASP A 255      10.174  29.062   5.110  1.00 27.50           O  
ATOM   1957  CB  ASP A 255      11.699  31.917   4.804  1.00 29.40           C  
ATOM   1958  CG  ASP A 255      11.608  31.350   3.401  1.00 32.16           C  
ATOM   1959  OD1 ASP A 255      10.513  31.433   2.800  1.00 35.09           O  
ATOM   1960  OD2 ASP A 255      12.625  30.822   2.901  1.00 30.99           O1-
ATOM   1961  N   CYS A 256      11.625  29.397   6.794  1.00 25.59           N  
ATOM   1962  CA  CYS A 256      11.839  27.976   7.007  1.00 23.91           C  
ATOM   1963  C   CYS A 256      10.535  27.327   7.489  1.00 22.31           C  
ATOM   1964  O   CYS A 256      10.076  26.343   6.907  1.00 22.53           O  
ATOM   1965  CB  CYS A 256      12.956  27.755   8.028  1.00 24.46           C  
ATOM   1966  SG  CYS A 256      13.400  26.015   8.224  1.00 24.49           S  
ATOM   1967  N   TRP A 257       9.937  27.883   8.539  1.00 23.04           N  
ATOM   1968  CA  TRP A 257       8.676  27.353   9.063  1.00 25.83           C  
ATOM   1969  C   TRP A 257       7.651  27.194   7.935  1.00 25.61           C  
ATOM   1970  O   TRP A 257       7.003  26.156   7.810  1.00 24.79           O  
ATOM   1971  CB  TRP A 257       8.062  28.283  10.118  1.00 25.02           C  
ATOM   1972  CG  TRP A 257       8.719  28.303  11.474  1.00 27.76           C  
ATOM   1973  CD1 TRP A 257       9.586  29.242  11.948  1.00 27.38           C  
ATOM   1974  CD2 TRP A 257       8.478  27.395  12.564  1.00 27.47           C  
ATOM   1975  NE1 TRP A 257       9.893  28.987  13.265  1.00 29.34           N  
ATOM   1976  CE2 TRP A 257       9.228  27.859  13.668  1.00 28.02           C  
ATOM   1977  CE3 TRP A 257       7.699  26.239  12.714  1.00 29.27           C  
ATOM   1978  CZ2 TRP A 257       9.225  27.208  14.908  1.00 29.62           C  
ATOM   1979  CZ3 TRP A 257       7.695  25.588  13.952  1.00 30.38           C  
ATOM   1980  CH2 TRP A 257       8.454  26.078  15.030  1.00 31.88           C  
ATOM   1981  N   ARG A 258       7.495  28.238   7.125  1.00 26.97           N  
ATOM   1982  CA  ARG A 258       6.540  28.203   6.020  1.00 27.58           C  
ATOM   1983  C   ARG A 258       6.871  27.173   4.956  1.00 26.37           C  
ATOM   1984  O   ARG A 258       5.992  26.435   4.506  1.00 24.84           O  
ATOM   1985  CB  ARG A 258       6.436  29.577   5.359  1.00 32.28           C  
ATOM   1986  CG  ARG A 258       5.738  30.604   6.219  1.00 38.63           C  
ATOM   1987  CD  ARG A 258       5.611  31.928   5.507  1.00 44.23           C  
ATOM   1988  NE  ARG A 258       4.915  32.908   6.337  1.00 52.26           N  
ATOM   1989  CZ  ARG A 258       3.631  32.828   6.682  1.00 55.12           C  
ATOM   1990  NH1 ARG A 258       2.882  31.810   6.269  1.00 56.30           N1+
ATOM   1991  NH2 ARG A 258       3.096  33.770   7.448  1.00 57.80           N  
ATOM   1992  N   LYS A 259       8.137  27.132   4.550  1.00 24.77           N  
ATOM   1993  CA  LYS A 259       8.584  26.198   3.526  1.00 25.76           C  
ATOM   1994  C   LYS A 259       8.334  24.741   3.908  1.00 25.37           C  
ATOM   1995  O   LYS A 259       7.794  23.965   3.114  1.00 26.43           O  
ATOM   1996  CB  LYS A 259      10.074  26.386   3.261  1.00 28.58           C  
ATOM   1997  CG  LYS A 259      10.426  26.691   1.819  1.00 32.91           C  
ATOM   1998  CD  LYS A 259      10.173  28.144   1.502  1.00 31.37           C  
ATOM   1999  CE  LYS A 259      10.854  28.545   0.211  1.00 31.17           C  
ATOM   2000  NZ  LYS A 259      10.807  30.016   0.052  1.00 32.50           N1+
ATOM   2001  N   ILE A 260       8.742  24.369   5.117  1.00 24.08           N  
ATOM   2002  CA  ILE A 260       8.554  22.998   5.582  1.00 24.54           C  
ATOM   2003  C   ILE A 260       7.064  22.660   5.564  1.00 25.28           C  
ATOM   2004  O   ILE A 260       6.654  21.619   5.047  1.00 25.30           O  
ATOM   2005  CB  ILE A 260       9.098  22.812   7.021  1.00 21.52           C  
ATOM   2006  CG1 ILE A 260      10.618  22.990   7.031  1.00 21.61           C  
ATOM   2007  CG2 ILE A 260       8.717  21.424   7.563  1.00 21.14           C  
ATOM   2008  CD1 ILE A 260      11.226  22.967   8.435  1.00 18.64           C  
ATOM   2009  N   ALA A 261       6.259  23.560   6.120  1.00 26.34           N  
ATOM   2010  CA  ALA A 261       4.819  23.365   6.181  1.00 28.28           C  
ATOM   2011  C   ALA A 261       4.201  23.175   4.794  1.00 29.48           C  
ATOM   2012  O   ALA A 261       3.408  22.260   4.587  1.00 31.40           O  
ATOM   2013  CB  ALA A 261       4.159  24.556   6.893  1.00 28.33           C  
ATOM   2014  N   LYS A 262       4.587  24.022   3.844  1.00 29.08           N  
ATOM   2015  CA  LYS A 262       4.032  23.958   2.498  1.00 30.34           C  
ATOM   2016  C   LYS A 262       4.629  22.899   1.579  1.00 30.38           C  
ATOM   2017  O   LYS A 262       3.895  22.253   0.831  1.00 30.80           O  
ATOM   2018  CB  LYS A 262       4.117  25.341   1.836  1.00 32.06           C  
ATOM   2019  CG  LYS A 262       3.176  26.362   2.475  1.00 34.49           C  
ATOM   2020  CD  LYS A 262       3.431  27.786   1.994  1.00 36.17           C  
ATOM   2021  CE  LYS A 262       2.528  28.763   2.741  1.00 39.54           C  
ATOM   2022  NZ  LYS A 262       2.952  30.181   2.589  1.00 39.59           N1+
ATOM   2023  N   ASP A 263       5.944  22.706   1.626  1.00 29.03           N  
ATOM   2024  CA  ASP A 263       6.565  21.704   0.764  1.00 27.75           C  
ATOM   2025  C   ASP A 263       6.503  20.281   1.293  1.00 27.41           C  
ATOM   2026  O   ASP A 263       6.483  19.337   0.512  1.00 27.92           O  
ATOM   2027  CB  ASP A 263       8.038  22.026   0.503  1.00 30.35           C  
ATOM   2028  CG  ASP A 263       8.230  23.202  -0.423  1.00 32.40           C  
ATOM   2029  OD1 ASP A 263       7.421  23.361  -1.362  1.00 34.03           O  
ATOM   2030  OD2 ASP A 263       9.207  23.956  -0.218  1.00 33.52           O1-
ATOM   2031  N   GLU A 264       6.475  20.118   2.610  1.00 27.66           N  
ATOM   2032  CA  GLU A 264       6.485  18.776   3.185  1.00 29.02           C  
ATOM   2033  C   GLU A 264       5.284  18.368   4.031  1.00 27.97           C  
ATOM   2034  O   GLU A 264       5.053  17.180   4.239  1.00 29.72           O  
ATOM   2035  CB  GLU A 264       7.747  18.604   4.032  1.00 28.80           C  
ATOM   2036  CG  GLU A 264       9.043  18.911   3.310  1.00 28.21           C  
ATOM   2037  CD  GLU A 264      10.215  18.976   4.274  1.00 27.00           C  
ATOM   2038  OE1 GLU A 264      10.568  17.930   4.861  1.00 25.25           O  
ATOM   2039  OE2 GLU A 264      10.768  20.076   4.452  1.00 24.44           O1-
ATOM   2040  N   GLY A 265       4.537  19.339   4.540  1.00 28.29           N  
ATOM   2041  CA  GLY A 265       3.394  19.004   5.369  1.00 27.59           C  
ATOM   2042  C   GLY A 265       3.719  19.204   6.842  1.00 29.84           C  
ATOM   2043  O   GLY A 265       4.884  19.113   7.246  1.00 29.17           O  
ATOM   2044  N   PRO A 266       2.706  19.483   7.673  1.00 29.58           N  
ATOM   2045  CA  PRO A 266       2.860  19.705   9.114  1.00 30.11           C  
ATOM   2046  C   PRO A 266       3.510  18.546   9.867  1.00 29.58           C  
ATOM   2047  O   PRO A 266       4.202  18.755  10.861  1.00 31.33           O  
ATOM   2048  CB  PRO A 266       1.428  19.953   9.577  1.00 30.57           C  
ATOM   2049  CG  PRO A 266       0.804  20.593   8.382  1.00 31.99           C  
ATOM   2050  CD  PRO A 266       1.314  19.724   7.258  1.00 31.89           C  
ATOM   2051  N   LYS A 267       3.285  17.326   9.396  1.00 28.50           N  
ATOM   2052  CA  LYS A 267       3.857  16.158  10.050  1.00 27.56           C  
ATOM   2053  C   LYS A 267       5.373  16.135   9.892  1.00 28.25           C  
ATOM   2054  O   LYS A 267       6.081  15.567  10.723  1.00 26.21           O  
ATOM   2055  CB  LYS A 267       3.272  14.877   9.453  1.00 28.06           C  
ATOM   2056  N   ALA A 268       5.860  16.750   8.815  1.00 26.03           N  
ATOM   2057  CA  ALA A 268       7.289  16.783   8.529  1.00 26.83           C  
ATOM   2058  C   ALA A 268       8.130  17.428   9.632  1.00 25.05           C  
ATOM   2059  O   ALA A 268       9.326  17.147   9.744  1.00 26.12           O  
ATOM   2060  CB  ALA A 268       7.537  17.491   7.200  1.00 25.46           C  
ATOM   2061  N   PHE A 269       7.521  18.291  10.441  1.00 23.20           N  
ATOM   2062  CA  PHE A 269       8.262  18.931  11.523  1.00 22.61           C  
ATOM   2063  C   PHE A 269       8.718  17.893  12.540  1.00 23.84           C  
ATOM   2064  O   PHE A 269       9.640  18.147  13.323  1.00 22.08           O  
ATOM   2065  CB  PHE A 269       7.406  19.996  12.212  1.00 22.76           C  
ATOM   2066  CG  PHE A 269       7.274  21.268  11.422  1.00 24.15           C  
ATOM   2067  CD1 PHE A 269       8.322  22.194  11.387  1.00 22.98           C  
ATOM   2068  CD2 PHE A 269       6.119  21.531  10.696  1.00 22.93           C  
ATOM   2069  CE1 PHE A 269       8.219  23.360  10.642  1.00 24.12           C  
ATOM   2070  CE2 PHE A 269       6.000  22.697   9.941  1.00 24.57           C  
ATOM   2071  CZ  PHE A 269       7.049  23.616   9.912  1.00 27.22           C  
ATOM   2072  N   PHE A 270       8.075  16.724  12.521  1.00 22.55           N  
ATOM   2073  CA  PHE A 270       8.419  15.651  13.447  1.00 23.74           C  
ATOM   2074  C   PHE A 270       9.244  14.520  12.840  1.00 23.92           C  
ATOM   2075  O   PHE A 270       9.304  13.419  13.394  1.00 24.71           O  
ATOM   2076  CB  PHE A 270       7.155  15.069  14.086  1.00 24.33           C  
ATOM   2077  CG  PHE A 270       6.403  16.051  14.935  1.00 24.11           C  
ATOM   2078  CD1 PHE A 270       5.449  16.892  14.370  1.00 25.00           C  
ATOM   2079  CD2 PHE A 270       6.683  16.171  16.293  1.00 24.08           C  
ATOM   2080  CE1 PHE A 270       4.781  17.842  15.146  1.00 25.21           C  
ATOM   2081  CE2 PHE A 270       6.023  17.119  17.081  1.00 23.70           C  
ATOM   2082  CZ  PHE A 270       5.070  17.957  16.506  1.00 24.92           C  
ATOM   2083  N   LYS A 271       9.859  14.772  11.692  1.00 22.06           N  
ATOM   2084  CA  LYS A 271      10.706  13.754  11.084  1.00 23.50           C  
ATOM   2085  C   LYS A 271      11.867  13.500  12.051  1.00 23.58           C  
ATOM   2086  O   LYS A 271      12.604  14.419  12.405  1.00 22.65           O  
ATOM   2087  CB  LYS A 271      11.248  14.230   9.731  1.00 24.50           C  
ATOM   2088  CG  LYS A 271      10.216  14.198   8.617  1.00 28.15           C  
ATOM   2089  CD  LYS A 271      10.758  14.743   7.296  1.00 29.04           C  
ATOM   2090  CE  LYS A 271       9.758  14.497   6.168  1.00 29.57           C  
ATOM   2091  NZ  LYS A 271      10.167  15.121   4.884  1.00 32.49           N1+
ATOM   2092  N   GLY A 272      12.011  12.251  12.482  1.00 24.67           N  
ATOM   2093  CA  GLY A 272      13.075  11.897  13.406  1.00 21.60           C  
ATOM   2094  C   GLY A 272      12.645  12.002  14.863  1.00 21.84           C  
ATOM   2095  O   GLY A 272      13.387  11.607  15.760  1.00 22.09           O  
ATOM   2096  N   ALA A 273      11.445  12.525  15.107  1.00 20.43           N  
ATOM   2097  CA  ALA A 273      10.961  12.687  16.475  1.00 23.63           C  
ATOM   2098  C   ALA A 273      10.911  11.386  17.297  1.00 25.36           C  
ATOM   2099  O   ALA A 273      11.234  11.402  18.486  1.00 26.15           O  
ATOM   2100  CB  ALA A 273       9.600  13.374  16.472  1.00 20.14           C  
ATOM   2101  N   TRP A 274      10.521  10.269  16.683  1.00 25.74           N  
ATOM   2102  CA  TRP A 274      10.483   8.998  17.415  1.00 27.79           C  
ATOM   2103  C   TRP A 274      11.916   8.591  17.780  1.00 27.15           C  
ATOM   2104  O   TRP A 274      12.193   8.174  18.913  1.00 25.24           O  
ATOM   2105  CB  TRP A 274       9.842   7.891  16.568  1.00 29.39           C  
ATOM   2106  CG  TRP A 274       9.780   6.555  17.279  1.00 34.43           C  
ATOM   2107  CD1 TRP A 274      10.142   5.336  16.771  1.00 33.42           C  
ATOM   2108  CD2 TRP A 274       9.311   6.307  18.614  1.00 33.64           C  
ATOM   2109  NE1 TRP A 274       9.928   4.350  17.705  1.00 34.71           N  
ATOM   2110  CE2 TRP A 274       9.417   4.917  18.843  1.00 34.72           C  
ATOM   2111  CE3 TRP A 274       8.808   7.125  19.636  1.00 34.93           C  
ATOM   2112  CZ2 TRP A 274       9.037   4.325  20.054  1.00 36.48           C  
ATOM   2113  CZ3 TRP A 274       8.429   6.537  20.842  1.00 36.93           C  
ATOM   2114  CH2 TRP A 274       8.547   5.148  21.039  1.00 36.61           C  
ATOM   2115  N   SER A 275      12.815   8.703  16.802  1.00 24.09           N  
ATOM   2116  CA  SER A 275      14.224   8.393  17.006  1.00 22.97           C  
ATOM   2117  C   SER A 275      14.736   9.232  18.176  1.00 22.45           C  
ATOM   2118  O   SER A 275      15.509   8.755  19.005  1.00 21.06           O  
ATOM   2119  CB  SER A 275      15.037   8.744  15.757  1.00 22.71           C  
ATOM   2120  OG  SER A 275      14.686   7.939  14.649  1.00 21.23           O  
ATOM   2121  N   ASN A 276      14.299  10.487  18.230  1.00 21.28           N  
ATOM   2122  CA  ASN A 276      14.713  11.384  19.300  1.00 24.27           C  
ATOM   2123  C   ASN A 276      14.247  10.884  20.661  1.00 25.38           C  
ATOM   2124  O   ASN A 276      14.971  10.999  21.652  1.00 25.48           O  
ATOM   2125  CB  ASN A 276      14.164  12.796  19.083  1.00 21.85           C  
ATOM   2126  CG  ASN A 276      14.802  13.805  20.016  1.00 23.46           C  
ATOM   2127  OD1 ASN A 276      16.029  13.924  20.057  1.00 22.32           O  
ATOM   2128  ND2 ASN A 276      13.986  14.528  20.770  1.00 18.91           N  
ATOM   2129  N   VAL A 277      13.026  10.357  20.712  1.00 26.40           N  
ATOM   2130  CA  VAL A 277      12.488   9.831  21.960  1.00 26.96           C  
ATOM   2131  C   VAL A 277      13.385   8.685  22.431  1.00 26.78           C  
ATOM   2132  O   VAL A 277      13.757   8.610  23.603  1.00 27.76           O  
ATOM   2133  CB  VAL A 277      11.059   9.278  21.782  1.00 27.61           C  
ATOM   2134  CG1 VAL A 277      10.636   8.534  23.051  1.00 25.81           C  
ATOM   2135  CG2 VAL A 277      10.088  10.412  21.483  1.00 25.12           C  
ATOM   2136  N   LEU A 278      13.728   7.802  21.502  1.00 25.78           N  
ATOM   2137  CA  LEU A 278      14.577   6.661  21.813  1.00 28.68           C  
ATOM   2138  C   LEU A 278      15.951   7.105  22.282  1.00 29.90           C  
ATOM   2139  O   LEU A 278      16.476   6.585  23.268  1.00 29.73           O  
ATOM   2140  CB  LEU A 278      14.712   5.760  20.588  1.00 25.72           C  
ATOM   2141  CG  LEU A 278      13.362   5.248  20.091  1.00 28.37           C  
ATOM   2142  CD1 LEU A 278      13.574   4.235  18.987  1.00 28.88           C  
ATOM   2143  CD2 LEU A 278      12.593   4.630  21.255  1.00 27.22           C  
ATOM   2144  N   ARG A 279      16.526   8.066  21.564  1.00 29.85           N  
ATOM   2145  CA  ARG A 279      17.839   8.600  21.893  1.00 29.96           C  
ATOM   2146  C   ARG A 279      17.839   9.112  23.334  1.00 30.28           C  
ATOM   2147  O   ARG A 279      18.737   8.789  24.116  1.00 30.99           O  
ATOM   2148  CB  ARG A 279      18.197   9.724  20.906  1.00 29.75           C  
ATOM   2149  CG  ARG A 279      19.598  10.306  21.056  1.00 31.93           C  
ATOM   2150  CD  ARG A 279      19.656  11.332  22.168  1.00 31.30           C  
ATOM   2151  NE  ARG A 279      18.671  12.386  21.956  1.00 32.40           N  
ATOM   2152  CZ  ARG A 279      18.299  13.262  22.882  1.00 33.99           C  
ATOM   2153  NH1 ARG A 279      18.834  13.215  24.093  1.00 35.01           N1+
ATOM   2154  NH2 ARG A 279      17.379  14.177  22.606  1.00 32.88           N  
ATOM   2155  N   GLY A 280      16.826   9.899  23.684  1.00 31.06           N  
ATOM   2156  CA  GLY A 280      16.731  10.428  25.035  1.00 31.66           C  
ATOM   2157  C   GLY A 280      16.635   9.341  26.098  1.00 33.91           C  
ATOM   2158  O   GLY A 280      17.272   9.429  27.149  1.00 33.45           O  
ATOM   2159  N   MET A 281      15.840   8.311  25.835  1.00 33.97           N  
ATOM   2160  CA  MET A 281      15.691   7.221  26.794  1.00 37.46           C  
ATOM   2161  C   MET A 281      16.992   6.455  26.978  1.00 36.18           C  
ATOM   2162  O   MET A 281      17.428   6.230  28.106  1.00 35.41           O  
ATOM   2163  CB  MET A 281      14.592   6.256  26.349  1.00 39.24           C  
ATOM   2164  CG  MET A 281      13.200   6.850  26.404  1.00 45.31           C  
ATOM   2165  SD  MET A 281      11.934   5.631  26.004  1.00 54.31           S  
ATOM   2166  CE  MET A 281      11.644   4.919  27.652  1.00 50.78           C  
ATOM   2167  N   GLY A 282      17.600   6.054  25.865  1.00 36.11           N  
ATOM   2168  CA  GLY A 282      18.848   5.318  25.921  1.00 35.57           C  
ATOM   2169  C   GLY A 282      19.941   6.125  26.596  1.00 37.61           C  
ATOM   2170  O   GLY A 282      20.771   5.575  27.316  1.00 36.48           O  
ATOM   2171  N   GLY A 283      19.942   7.435  26.361  1.00 39.13           N  
ATOM   2172  CA  GLY A 283      20.943   8.293  26.963  1.00 39.69           C  
ATOM   2173  C   GLY A 283      20.865   8.224  28.475  1.00 42.00           C  
ATOM   2174  O   GLY A 283      21.882   8.050  29.154  1.00 41.80           O  
ATOM   2175  N   ALA A 284      19.650   8.348  29.002  1.00 42.86           N  
ATOM   2176  CA  ALA A 284      19.427   8.309  30.444  1.00 42.82           C  
ATOM   2177  C   ALA A 284      19.723   6.925  31.021  1.00 42.83           C  
ATOM   2178  O   ALA A 284      20.193   6.804  32.152  1.00 40.85           O  
ATOM   2179  CB  ALA A 284      17.996   8.712  30.759  1.00 43.03           C  
ATOM   2180  N   PHE A 285      19.448   5.889  30.235  1.00 43.35           N  
ATOM   2181  CA  PHE A 285      19.685   4.512  30.656  1.00 44.56           C  
ATOM   2182  C   PHE A 285      21.180   4.199  30.783  1.00 45.17           C  
ATOM   2183  O   PHE A 285      21.586   3.406  31.634  1.00 43.57           O  
ATOM   2184  CB  PHE A 285      19.042   3.543  29.660  1.00 46.40           C  
ATOM   2185  CG  PHE A 285      19.238   2.094  30.007  1.00 49.67           C  
ATOM   2186  CD1 PHE A 285      18.721   1.571  31.190  1.00 51.47           C  
ATOM   2187  CD2 PHE A 285      19.941   1.249  29.152  1.00 50.55           C  
ATOM   2188  CE1 PHE A 285      18.902   0.222  31.518  1.00 51.37           C  
ATOM   2189  CE2 PHE A 285      20.127  -0.101  29.470  1.00 51.70           C  
ATOM   2190  CZ  PHE A 285      19.607  -0.614  30.656  1.00 51.01           C  
ATOM   2191  N   VAL A 286      21.995   4.816  29.932  1.00 44.87           N  
ATOM   2192  CA  VAL A 286      23.436   4.595  29.970  1.00 44.72           C  
ATOM   2193  C   VAL A 286      24.059   5.276  31.187  1.00 46.12           C  
ATOM   2194  O   VAL A 286      25.039   4.783  31.743  1.00 45.57           O  
ATOM   2195  CB  VAL A 286      24.109   5.107  28.677  1.00 43.53           C  
ATOM   2196  CG1 VAL A 286      25.626   5.005  28.790  1.00 41.13           C  
ATOM   2197  CG2 VAL A 286      23.622   4.289  27.497  1.00 41.55           C  
ATOM   2198  N   LEU A 287      23.487   6.406  31.600  1.00 47.73           N  
ATOM   2199  CA  LEU A 287      23.990   7.131  32.764  1.00 49.87           C  
ATOM   2200  C   LEU A 287      23.780   6.301  34.027  1.00 51.17           C  
ATOM   2201  O   LEU A 287      24.681   6.185  34.856  1.00 51.41           O  
ATOM   2202  CB  LEU A 287      23.286   8.486  32.907  1.00 48.95           C  
ATOM   2203  CG  LEU A 287      23.813   9.631  32.035  1.00 50.40           C  
ATOM   2204  CD1 LEU A 287      22.879  10.825  32.119  1.00 49.56           C  
ATOM   2205  CD2 LEU A 287      25.213  10.016  32.491  1.00 50.62           C  
ATOM   2206  N   VAL A 288      22.589   5.729  34.175  1.00 52.37           N  
ATOM   2207  CA  VAL A 288      22.304   4.898  35.337  1.00 54.17           C  
ATOM   2208  C   VAL A 288      23.191   3.661  35.254  1.00 54.38           C  
ATOM   2209  O   VAL A 288      23.754   3.216  36.254  1.00 54.89           O  
ATOM   2210  CB  VAL A 288      20.813   4.467  35.381  1.00 55.39           C  
ATOM   2211  CG1 VAL A 288      19.926   5.679  35.612  1.00 55.59           C  
ATOM   2212  CG2 VAL A 288      20.424   3.781  34.089  1.00 56.16           C  
ATOM   2213  N   LEU A 289      23.317   3.118  34.047  1.00 54.58           N  
ATOM   2214  CA  LEU A 289      24.144   1.945  33.809  1.00 55.23           C  
ATOM   2215  C   LEU A 289      25.586   2.303  34.147  1.00 56.92           C  
ATOM   2216  O   LEU A 289      26.339   1.480  34.668  1.00 56.31           O  
ATOM   2217  CB  LEU A 289      24.052   1.533  32.341  1.00 55.26           C  
ATOM   2218  CG  LEU A 289      24.633   0.169  31.963  1.00 55.99           C  
ATOM   2219  CD1 LEU A 289      23.763  -0.929  32.552  1.00 54.66           C  
ATOM   2220  CD2 LEU A 289      24.691   0.033  30.450  1.00 55.97           C  
ATOM   2221  N   TYR A 290      25.957   3.544  33.846  1.00 57.92           N  
ATOM   2222  CA  TYR A 290      27.302   4.041  34.104  1.00 59.61           C  
ATOM   2223  C   TYR A 290      27.569   4.306  35.588  1.00 61.46           C  
ATOM   2224  O   TYR A 290      28.586   3.873  36.131  1.00 59.65           O  
ATOM   2225  CB  TYR A 290      27.547   5.330  33.318  1.00 57.88           C  
ATOM   2226  CG  TYR A 290      28.875   5.965  33.641  1.00 57.27           C  
ATOM   2227  CD1 TYR A 290      30.068   5.371  33.237  1.00 57.77           C  
ATOM   2228  CD2 TYR A 290      28.944   7.136  34.395  1.00 56.93           C  
ATOM   2229  CE1 TYR A 290      31.297   5.924  33.577  1.00 57.78           C  
ATOM   2230  CE2 TYR A 290      30.172   7.698  34.740  1.00 56.37           C  
ATOM   2231  CZ  TYR A 290      31.342   7.086  34.327  1.00 55.99           C  
ATOM   2232  OH  TYR A 290      32.561   7.627  34.662  1.00 56.38           O  
ATOM   2233  N   ASP A 291      26.661   5.033  36.233  1.00 64.20           N  
ATOM   2234  CA  ASP A 291      26.804   5.357  37.648  1.00 68.04           C  
ATOM   2235  C   ASP A 291      26.854   4.097  38.499  1.00 69.85           C  
ATOM   2236  O   ASP A 291      27.275   4.134  39.655  1.00 70.55           O  
ATOM   2237  CB  ASP A 291      25.645   6.245  38.105  1.00 69.54           C  
ATOM   2238  CG  ASP A 291      25.797   7.680  37.645  1.00 71.95           C  
ATOM   2239  OD1 ASP A 291      25.968   7.909  36.427  1.00 73.45           O  
ATOM   2240  OD2 ASP A 291      25.745   8.583  38.507  1.00 73.21           O1-
ATOM   2241  N   GLU A 292      26.424   2.984  37.916  1.00 71.73           N  
ATOM   2242  CA  GLU A 292      26.420   1.702  38.607  1.00 73.21           C  
ATOM   2243  C   GLU A 292      27.551   0.826  38.068  1.00 73.49           C  
ATOM   2244  O   GLU A 292      27.321  -0.288  37.599  1.00 73.62           O  
ATOM   2245  CB  GLU A 292      25.069   1.010  38.405  1.00 74.26           C  
ATOM   2246  CG  GLU A 292      24.893  -0.284  39.183  1.00 76.63           C  
ATOM   2247  CD  GLU A 292      25.006  -0.089  40.684  1.00 78.10           C  
ATOM   2248  OE1 GLU A 292      24.323   0.807  41.221  1.00 79.37           O  
ATOM   2249  OE2 GLU A 292      25.773  -0.838  41.327  1.00 79.14           O1-
ATOM   2250  N   ILE A 293      28.775   1.345  38.136  1.00 73.63           N  
ATOM   2251  CA  ILE A 293      29.950   0.623  37.659  1.00 73.56           C  
ATOM   2252  C   ILE A 293      31.217   1.450  37.863  1.00 73.78           C  
ATOM   2253  O   ILE A 293      31.364   2.149  38.867  1.00 74.12           O  
ATOM   2254  CB  ILE A 293      29.823   0.276  36.161  1.00 72.88           C  
TER   
CONECT    1    2
CONECT    2    1    3    5
CONECT    3    2    4    4    6
CONECT    4    3    3
CONECT    5    2
CONECT    6    3    7
CONECT    7    6    8   10
CONECT    8    7    9    9   15
CONECT    9    8    8
CONECT   10    7   11
CONECT   11   10   12
CONECT   12   11   13   13   14
CONECT   13   12   12
CONECT   14   12
CONECT   15    8   16
CONECT   16   15   17   19
CONECT   17   16   18   18   20
CONECT   18   17   17
CONECT   19   16
CONECT   20   17   21
CONECT   21   20   22   24
CONECT   22   21   23   23   28
CONECT   23   22   22
CONECT   24   21   25
CONECT   25   24   26   27
CONECT   26   25
CONECT   27   25
CONECT   28   22   29
CONECT   29   28   30   32
CONECT   30   29   31   31   34
CONECT   31   30   30
CONECT   32   29   33
CONECT   33   32
CONECT   34   30   35
CONECT   35   34   36   38
CONECT   36   35   37   37   45
CONECT   37   36   36
CONECT   38   35   39
CONECT   39   38   40   40   41
CONECT   40   39   39   42
CONECT   41   39   43   43
CONECT   42   40   44   44
CONECT   43   41   41   44
CONECT   44   42   42   43
CONECT   45   36   46
CONECT   46   45   47   49
CONECT   47   46   48   48   53
CONECT   48   47   47
CONECT   49   46   50
CONECT   50   49   51   52
CONECT   51   50
CONECT   52   50
CONECT   53   47   54
CONECT   54   53   55   57
CONECT   55   54   56   56   62
CONECT   56   55   55
CONECT   57   54   58
CONECT   58   57   59
CONECT   59   58   60
CONECT   60   59   61
CONECT   61   60
CONECT   62   55   63
CONECT   63   62   64   66
CONECT   64   63   65   65   70
CONECT   65   64   64
CONECT   66   63   67
CONECT   67   66   68   68   69
CONECT   68   67   67
CONECT   69   67
CONECT   70   64   71
CONECT   71   70   72   74
CONECT   72   71   73   73   81
CONECT   73   72   72
CONECT   74   71   75
CONECT   75   74   76   76   77
CONECT   76   75   75   78
CONECT   77   75   79   79
CONECT   78   76   80   80
CONECT   79   77   77   80
CONECT   80   78   78   79
CONECT   81   72   82
CONECT   82   81   83   85
CONECT   83   82   84   84   89
CONECT   84   83   83
CONECT   85   82   86
CONECT   86   85   87   88
CONECT   87   86
CONECT   88   86
CONECT   89   83   90
CONECT   90   89   91   93
CONECT   91   90   92   92   94
CONECT   92   91   91
CONECT   93   90
CONECT   94   91   95
CONECT   95   94   96
CONECT   96   95   97   97   98
CONECT   97   96   96
CONECT   98   96   99
CONECT   99   98  100
CONECT  100   99  101  101  102
CONECT  101  100  100
CONECT  102  100  103
CONECT  103  102  104  106
CONECT  104  103  105  105  109
CONECT  105  104  104
CONECT  106  103  107  108
CONECT  107  106
CONECT  108  106
CONECT  109  104  110
CONECT  110  109  111  113
CONECT  111  110  112  112  114
CONECT  112  111  111
CONECT  113  110
CONECT  114  111  115
CONECT  115  114  116  118
CONECT  116  115  117  117  119
CONECT  117  116  116
CONECT  118  115
CONECT  119  116  120
CONECT  120  119  121  123
CONECT  121  120  122  122  124
CONECT  122  121  121
CONECT  123  120
CONECT  124  121  125
CONECT  125  124  126  128
CONECT  126  125  127  127  132
CONECT  127  126  126
CONECT  128  125  129  130
CONECT  129  128  131
CONECT  130  128
CONECT  131  129
CONECT  132  126  133
CONECT  133  132  134  136
CONECT  134  133  135  135  138
CONECT  135  134  134
CONECT  136  133  137
CONECT  137  136
CONECT  138  134  139
CONECT  139  138  140  142
CONECT  140  139  141  141  147
CONECT  141  140  140
CONECT  142  139  143
CONECT  143  142  144
CONECT  144  143  145
CONECT  145  144  146
CONECT  146  145
CONECT  147  140  148
CONECT  148  147  149  151
CONECT  149  148  150  150  154
CONECT  150  149  149
CONECT  151  148  152  153
CONECT  152  151
CONECT  153  151
CONECT  154  149  155
CONECT  155  154  156  158
CONECT  156  155  157  157  159
CONECT  157  156  156
CONECT  158  155
CONECT  159  156  160
CONECT  160  159  161  163
CONECT  161  160  162  162  166
CONECT  162  161  161
CONECT  163  160  164  165
CONECT  164  163
CONECT  165  163
CONECT  166  161  167
CONECT  167  166  168  170
CONECT  168  167  169  169  171
CONECT  169  168  168
CONECT  170  167
CONECT  171  168  172  177
CONECT  172  171  173  175
CONECT  173  172  174  174  178
CONECT  174  173  173
CONECT  175  172  176
CONECT  176  175  177
CONECT  177  171  176
CONECT  178  173  179
CONECT  179  178  180  182
CONECT  180  179  181  181  186
CONECT  181  180  180
CONECT  182  179  183  184
CONECT  183  182  185
CONECT  184  182
CONECT  185  183
CONECT  186  180  187
CONECT  187  186  188  190
CONECT  188  187  189  189  195
CONECT  189  188  188
CONECT  190  187  191
CONECT  191  190  192
CONECT  192  191  193  193  194
CONECT  193  192  192
CONECT  194  192
CONECT  195  188  196
CONECT  196  195  197  199
CONECT  197  196  198  198  206
CONECT  198  197  197
CONECT  199  196  200
CONECT  200  199  201
CONECT  201  200  202
CONECT  202  201  203
CONECT  203  202  204  204  205
CONECT  204  203  203
CONECT  205  203
CONECT  206  197  207
CONECT  207  206  208  210
CONECT  208  207  209  209  213
CONECT  209  208  208
CONECT  210  207  211  212
CONECT  211  210
CONECT  212  210
CONECT  213  208  214
CONECT  214  213  215  217
CONECT  215  214  216  216  222
CONECT  216  215  215
CONECT  217  214  218
CONECT  218  217  219
CONECT  219  218  220
CONECT  220  219  221
CONECT  221  220
CONECT  222  215  223
CONECT  223  222  224  226
CONECT  224  223  225  225  230
CONECT  225  224  224
CONECT  226  223  227
CONECT  227  226  228  229
CONECT  228  227
CONECT  229  227
CONECT  230  224  231
CONECT  231  230  232  234
CONECT  232  231  233  233  238
CONECT  233  232  232
CONECT  234  231  235
CONECT  235  234  236  237
CONECT  236  235
CONECT  237  235
CONECT  238  232  239
CONECT  239  238  240  242
CONECT  240  239  241  241  246
CONECT  241  240  240
CONECT  242  239  243
CONECT  243  242  244  245
CONECT  244  243
CONECT  245  243
CONECT  246  240  247
CONECT  247  246  248  250
CONECT  248  247  249  249  255
CONECT  249  248  248
CONECT  250  247  251
CONECT  251  250  252
CONECT  252  251  253  253  254
CONECT  253  252  252
CONECT  254  252
CONECT  255  248  256
CONECT  256  255  257  259
CONECT  257  256  258  258  262
CONECT  258  257  257
CONECT  259  256  260  261
CONECT  260  259
CONECT  261  259
CONECT  262  257  263
CONECT  263  262  264  266
CONECT  264  263  265  265  271
CONECT  265  264  264
CONECT  266  263  267
CONECT  267  266  268
CONECT  268  267  269  269  270
CONECT  269  268  268
CONECT  270  268
CONECT  271  264  272
CONECT  272  271  273  275
CONECT  273  272  274  274  281
CONECT  274  273  273
CONECT  275  272  276
CONECT  276  275  277  278  278
CONECT  277  276  279  279
CONECT  278  276  276  280
CONECT  279  277  277  280
CONECT  280  278  279
CONECT  281  273  282
CONECT  282  281  283  285
CONECT  283  282  284  284  286
CONECT  284  283  283
CONECT  285  282
CONECT  286  283  287
CONECT  287  286  288  290
CONECT  288  287  289  289  292
CONECT  289  288  288
CONECT  290  287  291
CONECT  291  290
CONECT  292  288  293
CONECT  293  292  294  296
CONECT  294  293  295  295  301
CONECT  295  294  294
CONECT  296  293  297
CONECT  297  296  298
CONECT  298  297  299
CONECT  299  298  300
CONECT  300  299
CONECT  301  294  302
CONECT  302  301  303  305
CONECT  303  302  304  304  310
CONECT  304  303  303
CONECT  305  302  306
CONECT  306  305  307
CONECT  307  306  308  308  309
CONECT  308  307  307
CONECT  309  307
CONECT  310  303  311
CONECT  311  310  312  314
CONECT  312  311  313  313  318
CONECT  313  312  312
CONECT  314  311  315  316
CONECT  315  314  317
CONECT  316  314
CONECT  317  315
CONECT  318  312  319
CONECT  319  318  320  322
CONECT  320  319  321  321  324
CONECT  321  320  320
CONECT  322  319  323
CONECT  323  322
CONECT  324  320  325
CONECT  325  324  326  328
CONECT  326  325  327  327  329
CONECT  327  326  326
CONECT  328  325
CONECT  329  326  330
CONECT  330  329  331  333
CONECT  331  330  332  332  338
CONECT  332  331  331
CONECT  333  330  334
CONECT  334  333  335
CONECT  335  334  336  336  337
CONECT  336  335  335
CONECT  337  335
CONECT  338  331  339
CONECT  339  338  340  342
CONECT  340  339  341  341  347
CONECT  341  340  340
CONECT  342  339  343
CONECT  343  342  344
CONECT  344  343  345
CONECT  345  344  346
CONECT  346  345
CONECT  347  340  348
CONECT  348  347  349  351
CONECT  349  348  350  350  356
CONECT  350  349  349
CONECT  351  348  352
CONECT  352  351  353
CONECT  353  352  354  354  355
CONECT  354  353  353
CONECT  355  353
CONECT  356  349  357
CONECT  357  356  358  360
CONECT  358  357  359  359  368
CONECT  359  358  358
CONECT  360  357  361
CONECT  361  360  362  362  363
CONECT  362  361  361  364
CONECT  363  361  365  365
CONECT  364  362  366  366
CONECT  365  363  363  366
CONECT  366  364  364  365  367
CONECT  367  366
CONECT  368  358  369
CONECT  369  368  370  372
CONECT  370  369  371  371  377
CONECT  371  370  370
CONECT  372  369  373
CONECT  373  372  374
CONECT  374  373  375
CONECT  375  374  376
CONECT  376  375
CONECT  377  370  378
CONECT  378  377  379
CONECT  379  378  380  380  381
CONECT  380  379  379
CONECT  381  379  382
CONECT  382  381  383  385
CONECT  383  382  384  384  389
CONECT  384  383  383
CONECT  385  382  386  387
CONECT  386  385  388
CONECT  387  385
CONECT  388  386
CONECT  389  383  390
CONECT  390  389  391  393
CONECT  391  390  392  392  397
CONECT  392  391  391
CONECT  393  390  394  395
CONECT  394  393  396
CONECT  395  393
CONECT  396  394
CONECT  397  391  398
CONECT  398  397  399  401
CONECT  399  398  400  400  405
CONECT  400  399  399
CONECT  401  398  402
CONECT  402  401  403  403  404
CONECT  403  402  402
CONECT  404  402
CONECT  405  399  406
CONECT  406  405  407  409
CONECT  407  406  408  408  411
CONECT  408  407  407
CONECT  409  406  410
CONECT  410  409
CONECT  411  407  412
CONECT  412  411  413  415
CONECT  413  412  414  414  418
CONECT  414  413  413
CONECT  415  412  416  417
CONECT  416  415
CONECT  417  415
CONECT  418  413  419
CONECT  419  418  420  422
CONECT  420  419  421  421  425
CONECT  421  420  420
CONECT  422  419  423  424
CONECT  423  422
CONECT  424  422
CONECT  425  420  426
CONECT  426  425  427  429
CONECT  427  426  428  428  436
CONECT  428  427  427
CONECT  429  426  430
CONECT  430  429  431
CONECT  431  430  432
CONECT  432  431  433
CONECT  433  432  434  434  435
CONECT  434  433  433
CONECT  435  433
CONECT  436  427  437
CONECT  437  436  438  440
CONECT  438  437  439  439  444
CONECT  439  438  438
CONECT  440  437  441  442
CONECT  441  440  443
CONECT  442  440
CONECT  443  441
CONECT  444  438  445  450
CONECT  445  444  446  448
CONECT  446  445  447  447  451
CONECT  447  446  446
CONECT  448  445  449
CONECT  449  448  450
CONECT  450  444  449
CONECT  451  446  452
CONECT  452  451  453  455
CONECT  453  452  454  454  460
CONECT  454  453  453
CONECT  455  452  456
CONECT  456  455  457
CONECT  457  456  458
CONECT  458  457  459
CONECT  459  458
CONECT  460  453  461
CONECT  461  460  462  464
CONECT  462  461  463  463  469
CONECT  463  462  462
CONECT  464  461  465
CONECT  465  464  466
CONECT  466  465  467  467  468
CONECT  467  466  466
CONECT  468  466
CONECT  469  462  470
CONECT  470  469  471  473
CONECT  471  470  472  472  478
CONECT  472  471  471
CONECT  473  470  474
CONECT  474  473  475
CONECT  475  474  476  476  477
CONECT  476  475  475
CONECT  477  475
CONECT  478  471  479
CONECT  479  478  480
CONECT  480  479  481  481  482
CONECT  481  480  480
CONECT  482  480  483
CONECT  483  482  484  486
CONECT  484  483  485  485  493
CONECT  485  484  484
CONECT  486  483  487
CONECT  487  486  488  488  489
CONECT  488  487  487  490
CONECT  489  487  491  491
CONECT  490  488  492  492
CONECT  491  489  489  492
CONECT  492  490  490  491
CONECT  493  484  494
CONECT  494  493  495  497
CONECT  495  494  496  496  501
CONECT  496  495  495
CONECT  497  494  498
CONECT  498  497  499  500
CONECT  499  498
CONECT  500  498
CONECT  501  495  502
CONECT  502  501  503  505
CONECT  503  502  504  504  507
CONECT  504  503  503
CONECT  505  502  506
CONECT  506  505
CONECT  507  503  508
CONECT  508  507  509  511
CONECT  509  508  510  510  518
CONECT  510  509  509
CONECT  511  508  512
CONECT  512  511  513  513  514
CONECT  513  512  512  515
CONECT  514  512  516  516
CONECT  515  513  517  517
CONECT  516  514  514  517
CONECT  517  515  515  516
CONECT  518  509  519
CONECT  519  518  520  522
CONECT  520  519  521  521  532
CONECT  521  520  520
CONECT  522  519  523
CONECT  523  522  524  524  525
CONECT  524  523  523  526
CONECT  525  523  527  527  528
CONECT  526  524  527
CONECT  527  525  525  526  529
CONECT  528  525  530  530
CONECT  529  527  531  531
CONECT  530  528  528  531
CONECT  531  529  529  530
CONECT  532  520  533
CONECT  533  532  534  536
CONECT  534  533  535  535  543
CONECT  535  534  534
CONECT  536  533  537
CONECT  537  536  538
CONECT  538  537  539
CONECT  539  538  540
CONECT  540  539  541  541  542
CONECT  541  540  540
CONECT  542  540
CONECT  543  534  544
CONECT  544  543  545
CONECT  545  544  546  546  547
CONECT  546  545  545
CONECT  547  545  548
CONECT  548  547  549  551
CONECT  549  548  550  550  555
CONECT  550  549  549
CONECT  551  548  552
CONECT  552  551  553  553  554
CONECT  553  552  552
CONECT  554  552
CONECT  555  549  556
CONECT  556  555  557  559
CONECT  557  556  558  558  563
CONECT  558  557  557
CONECT  559  556  560
CONECT  560  559  561  562
CONECT  561  560
CONECT  562  560
CONECT  563  557  564
CONECT  564  563  565  567
CONECT  565  564  566  566  568
CONECT  566  565  565
CONECT  567  564
CONECT  568  565  569
CONECT  569  568  570  572
CONECT  570  569  571  571  576
CONECT  571  570  570
CONECT  572  569  573
CONECT  573  572  574  574  575
CONECT  574  573  573
CONECT  575  573
CONECT  576  570  577
CONECT  577  576  578  580
CONECT  578  577  579  579  583
CONECT  579  578  578
CONECT  580  577  581  582
CONECT  581  580
CONECT  582  580
CONECT  583  578  584
CONECT  584  583  585  587
CONECT  585  584  586  586  591
CONECT  586  585  585
CONECT  587  584  588  589
CONECT  588  587  590
CONECT  589  587
CONECT  590  588
CONECT  591  585  592
CONECT  592  591  593  595
CONECT  593  592  594  594  602
CONECT  594  593  593
CONECT  595  592  596
CONECT  596  595  597
CONECT  597  596  598
CONECT  598  597  599
CONECT  599  598  600  600  601
CONECT  600  599  599
CONECT  601  599
CONECT  602  593  603
CONECT  603  602  604  606
CONECT  604  603  605  605  614
CONECT  605  604  604
CONECT  606  603  607
CONECT  607  606  608  608  609
CONECT  608  607  607  610
CONECT  609  607  611  611
CONECT  610  608  612  612
CONECT  611  609  609  612
CONECT  612  610  610  611  613
CONECT  613  612
CONECT  614  604  615
CONECT  615  614  616  618
CONECT  616  615  617  617  625
CONECT  617  616  616
CONECT  618  615  619
CONECT  619  618  620  620  621
CONECT  620  619  619  622
CONECT  621  619  623  623
CONECT  622  620  624  624
CONECT  623  621  621  624
CONECT  624  622  622  623
CONECT  625  616  626  631
CONECT  626  625  627  629
CONECT  627  626  628  628  632
CONECT  628  627  627
CONECT  629  626  630
CONECT  630  629  631
CONECT  631  625  630
CONECT  632  627  633
CONECT  633  632  634  636
CONECT  634  633  635  635  639
CONECT  635  634  634
CONECT  636  633  637  638
CONECT  637  636
CONECT  638  636
CONECT  639  634  640
CONECT  640  639  641  643
CONECT  641  640  642  642  648
CONECT  642  641  641
CONECT  643  640  644
CONECT  644  643  645
CONECT  645  644  646  646  647
CONECT  646  645  645
CONECT  647  645
CONECT  648  641  649
CONECT  649  648  650  652
CONECT  650  649  651  651  653
CONECT  651  650  650
CONECT  652  649
CONECT  653  650  654
CONECT  654  653  655  657
CONECT  655  654  656  656  661
CONECT  656  655  655
CONECT  657  654  658
CONECT  658  657  659  660
CONECT  659  658
CONECT  660  658
CONECT  661  655  662
CONECT  662  661  663  665
CONECT  663  662  664  664  669
CONECT  664  663  663
CONECT  665  662  666
CONECT  666  665  667  667  668
CONECT  667  666  666
CONECT  668  666
CONECT  669  663  670
CONECT  670  669  671  673
CONECT  671  670  672  672  680
CONECT  672  671  671
CONECT  673  670  674
CONECT  674  673  675  675  676
CONECT  675  674  674  677
CONECT  676  674  678  678
CONECT  677  675  679  679
CONECT  678  676  676  679
CONECT  679  677  677  678
CONECT  680  671  681
CONECT  681  680  682  684
CONECT  682  681  683  683  685
CONECT  683  682  682
CONECT  684  681
CONECT  685  682  686
CONECT  686  685  687  689
CONECT  687  686  688  688  696
CONECT  688  687  687
CONECT  689  686  690
CONECT  690  689  691  691  692
CONECT  691  690  690  693
CONECT  692  690  694  694
CONECT  693  691  695  695
CONECT  694  692  692  695
CONECT  695  693  693  694
CONECT  696  687  697
CONECT  697  696  698  700
CONECT  698  697  699  699  705
CONECT  699  698  698
CONECT  700  697  701
CONECT  701  700  702
CONECT  702  701  703
CONECT  703  702  704
CONECT  704  703
CONECT  705  698  706
CONECT  706  705  707  709
CONECT  707  706  708  708  713
CONECT  708  707  707
CONECT  709  706  710
CONECT  710  709  711  711  712
CONECT  711  710  710
CONECT  712  710
CONECT  713  707  714
CONECT  714  713  715  717
CONECT  715  714  716  716  722
CONECT  716  715  715
CONECT  717  714  718
CONECT  718  717  719
CONECT  719  718  720
CONECT  720  719  721
CONECT  721  720
CONECT  722  715  723
CONECT  723  722  724  726
CONECT  724  723  725  725  734
CONECT  725  724  724
CONECT  726  723  727
CONECT  727  726  728  728  729
CONECT  728  727  727  730
CONECT  729  727  731  731
CONECT  730  728  732  732
CONECT  731  729  729  732
CONECT  732  730  730  731  733
CONECT  733  732
CONECT  734  724  735
CONECT  735  734  736  738
CONECT  736  735  737  737  743
CONECT  737  736  736
CONECT  738  735  739
CONECT  739  738  740
CONECT  740  739  741
CONECT  741  740  742
CONECT  742  741
CONECT  743  736  744
CONECT  744  743  745  747
CONECT  745  744  746  746  752
CONECT  746  745  745
CONECT  747  744  748
CONECT  748  747  749
CONECT  749  748  750  750  751
CONECT  750  749  749
CONECT  751  749
CONECT  752  745  753
CONECT  753  752  754  756
CONECT  754  753  755  755  760
CONECT  755  754  754
CONECT  756  753  757  758
CONECT  757  756  759
CONECT  758  756
CONECT  759  757
CONECT  760  754  761
CONECT  761  760  762  764
CONECT  762  761  763  763  771
CONECT  763  762  762
CONECT  764  761  765
CONECT  765  764  766  766  767
CONECT  766  765  765  768
CONECT  767  765  769  769
CONECT  768  766  770  770
CONECT  769  767  767  770
CONECT  770  768  768  769
CONECT  771  762  772
CONECT  772  771  773  775
CONECT  773  772  774  774  779
CONECT  774  773  773
CONECT  775  772  776
CONECT  776  775  777  778
CONECT  777  776
CONECT  778  776
CONECT  779  773  780
CONECT  780  779  781
CONECT  781  780  782  782  783
CONECT  782  781  781
CONECT  783  781  784
CONECT  784  783  785
CONECT  785  784  786  786  787
CONECT  786  785  785
CONECT  787  785  788
CONECT  788  787  789  791
CONECT  789  788  790  790  794
CONECT  790  789  789
CONECT  791  788  792  793
CONECT  792  791
CONECT  793  791
CONECT  794  789  795
CONECT  795  794  796  798
CONECT  796  795  797  797  802
CONECT  797  796  796
CONECT  798  795  799
CONECT  799  798  800  800  801
CONECT  800  799  799
CONECT  801  799
CONECT  802  796  803
CONECT  803  802  804  806
CONECT  804  803  805  805  813
CONECT  805  804  804
CONECT  806  803  807
CONECT  807  806  808
CONECT  808  807  809
CONECT  809  808  810
CONECT  810  809  811  811  812
CONECT  811  810  810
CONECT  812  810
CONECT  813  804  814
CONECT  814  813  815  817
CONECT  815  814  816  816  823
CONECT  816  815  815
CONECT  817  814  818
CONECT  818  817  819  820  820
CONECT  819  818  821  821
CONECT  820  818  818  822
CONECT  821  819  819  822
CONECT  822  820  821
CONECT  823  815  824
CONECT  824  823  825  827
CONECT  825  824  826  826  832
CONECT  826  825  825
CONECT  827  824  828
CONECT  828  827  829
CONECT  829  828  830
CONECT  830  829  831
CONECT  831  830
CONECT  832  825  833
CONECT  833  832  834  836
CONECT  834  833  835  835  841
CONECT  835  834  834
CONECT  836  833  837
CONECT  837  836  838
CONECT  838  837  839  839  840
CONECT  839  838  838
CONECT  840  838
CONECT  841  834  842
CONECT  842  841  843  845
CONECT  843  842  844  844  852
CONECT  844  843  843
CONECT  845  842  846
CONECT  846  845  847  847  848
CONECT  847  846  846  849
CONECT  848  846  850  850
CONECT  849  847  851  851
CONECT  850  848  848  851
CONECT  851  849  849  850
CONECT  852  843  853
CONECT  853  852  854  856
CONECT  854  853  855  855  866
CONECT  855  854  854
CONECT  856  853  857
CONECT  857  856  858  858  859
CONECT  858  857  857  860
CONECT  859  857  861  861  862
CONECT  860  858  861
CONECT  861  859  859  860  863
CONECT  862  859  864  864
CONECT  863  861  865  865
CONECT  864  862  862  865
CONECT  865  863  863  864
CONECT  866  854  867
CONECT  867  866  868  870
CONECT  868  867  869  869  877
CONECT  869  868  868
CONECT  870  867  871
CONECT  871  870  872
CONECT  872  871  873
CONECT  873  872  874
CONECT  874  873  875  875  876
CONECT  875  874  874
CONECT  876  874
CONECT  877  868  878
CONECT  878  877  879  881
CONECT  879  878  880  880  889
CONECT  880  879  879
CONECT  881  878  882
CONECT  882  881  883  883  884
CONECT  883  882  882  885
CONECT  884  882  886  886
CONECT  885  883  887  887
CONECT  886  884  884  887
CONECT  887  885  885  886  888
CONECT  888  887
CONECT  889  879  890
CONECT  890  889  891  893
CONECT  891  890  892  892  900
CONECT  892  891  891
CONECT  893  890  894
CONECT  894  893  895  895  896
CONECT  895  894  894  897
CONECT  896  894  898  898
CONECT  897  895  899  899
CONECT  898  896  896  899
CONECT  899  897  897  898
CONECT  900  891  901
CONECT  901  900  902  904
CONECT  902  901  903  903  905
CONECT  903  902  902
CONECT  904  901
CONECT  905  902  906
CONECT  906  905  907
CONECT  907  906  908  908  909
CONECT  908  907  907
CONECT  909  907  910
CONECT  910  909  911  913
CONECT  911  910  912  912  917
CONECT  912  911  911
CONECT  913  910  914
CONECT  914  913  915  915  916
CONECT  915  914  914
CONECT  916  914
CONECT  917  911  918
CONECT  918  917  919  921
CONECT  919  918  920  920  925
CONECT  920  919  919
CONECT  921  918  922
CONECT  922  921  923  924
CONECT  923  922
CONECT  924  922
CONECT  925  919  926
CONECT  926  925  927  929
CONECT  927  926  928  928  930
CONECT  928  927  927
CONECT  929  926
CONECT  930  927  931
CONECT  931  930  932  934
CONECT  932  931  933  933  936
CONECT  933  932  932
CONECT  934  931  935
CONECT  935  934
CONECT  936  932  937
CONECT  937  936  938
CONECT  938  937  939  939  940
CONECT  939  938  938
CONECT  940  938  941
CONECT  941  940  942
CONECT  942  941  943  943  944
CONECT  943  942  942
CONECT  944  942  945
CONECT  945  944  946  948
CONECT  946  945  947  947  949
CONECT  947  946  946
CONECT  948  945
CONECT  949  946  950
CONECT  950  949  951  953
CONECT  951  950  952  952  954
CONECT  952  951  951
CONECT  953  950
CONECT  954  951  955
CONECT  955  954  956
CONECT  956  955  957  957  958
CONECT  957  956  956
CONECT  958  956  959
CONECT  959  958  960  962
CONECT  960  959  961  961  963
CONECT  961  960  960
CONECT  962  959
CONECT  963  960  964
CONECT  964  963  965  967
CONECT  965  964  966  966  970
CONECT  966  965  965
CONECT  967  964  968  969
CONECT  968  967
CONECT  969  967
CONECT  970  965  971
CONECT  971  970  972  974
CONECT  972  971  973  973  976
CONECT  973  972  972
CONECT  974  971  975
CONECT  975  974
CONECT  976  972  977
CONECT  977  976  978  980
CONECT  978  977  979  979  984
CONECT  979  978  978
CONECT  980  977  981
CONECT  981  980  982  983
CONECT  982  981
CONECT  983  981
CONECT  984  978  985
CONECT  985  984  986  988
CONECT  986  985  987  987  990
CONECT  987  986  986
CONECT  988  985  989
CONECT  989  988
CONECT  990  986  991
CONECT  991  990  992  994
CONECT  992  991  993  993 1001
CONECT  993  992  992
CONECT  994  991  995
CONECT  995  994  996  996  997
CONECT  996  995  995  998
CONECT  997  995  999  999
CONECT  998  996 1000 1000
CONECT  999  997  997 1000
CONECT 1000  998  998  999
CONECT 1001  992 1002
CONECT 1002 1001 1003 1005
CONECT 1003 1002 1004 1004 1008
CONECT 1004 1003 1003
CONECT 1005 1002 1006 1007
CONECT 1006 1005
CONECT 1007 1005
CONECT 1008 1003 1009
CONECT 1009 1008 1010 1012
CONECT 1010 1009 1011 1011 1020
CONECT 1011 1010 1010
CONECT 1012 1009 1013
CONECT 1013 1012 1014 1014 1015
CONECT 1014 1013 1013 1016
CONECT 1015 1013 1017 1017
CONECT 1016 1014 1018 1018
CONECT 1017 1015 1015 1018
CONECT 1018 1016 1016 1017 1019
CONECT 1019 1018
CONECT 1020 1010 1021 1026
CONECT 1021 1020 1022 1024
CONECT 1022 1021 1023 1023 1027
CONECT 1023 1022 1022
CONECT 1024 1021 1025
CONECT 1025 1024 1026
CONECT 1026 1020 1025
CONECT 1027 1022 1028
CONECT 1028 1027 1029 1031
CONECT 1029 1028 1030 1030 1035
CONECT 1030 1029 1029
CONECT 1031 1028 1032
CONECT 1032 1031 1033 1034
CONECT 1033 1032
CONECT 1034 1032
CONECT 1035 1029 1036
CONECT 1036 1035 1037 1039
CONECT 1037 1036 1038 1038 1043
CONECT 1038 1037 1037
CONECT 1039 1036 1040
CONECT 1040 1039 1041 1041 1042
CONECT 1041 1040 1040
CONECT 1042 1040
CONECT 1043 1037 1044
CONECT 1044 1043 1045 1047
CONECT 1045 1044 1046 1046 1054
CONECT 1046 1045 1045
CONECT 1047 1044 1048
CONECT 1048 1047 1049 1049 1050
CONECT 1049 1048 1048 1051
CONECT 1050 1048 1052 1052
CONECT 1051 1049 1053 1053
CONECT 1052 1050 1050 1053
CONECT 1053 1051 1051 1052
CONECT 1054 1045 1055
CONECT 1055 1054 1056 1058
CONECT 1056 1055 1057 1057 1059
CONECT 1057 1056 1056
CONECT 1058 1055
CONECT 1059 1056 1060
CONECT 1060 1059 1061 1063
CONECT 1061 1060 1062 1062 1070
CONECT 1062 1061 1061
CONECT 1063 1060 1064
CONECT 1064 1063 1065
CONECT 1065 1064 1066
CONECT 1066 1065 1067
CONECT 1067 1066 1068 1068 1069
CONECT 1068 1067 1067
CONECT 1069 1067
CONECT 1070 1061 1071
CONECT 1071 1070 1072 1074
CONECT 1072 1071 1073 1073 1077
CONECT 1073 1072 1072
CONECT 1074 1071 1075 1076
CONECT 1075 1074
CONECT 1076 1074
CONECT 1077 1072 1078
CONECT 1078 1077 1079 1081
CONECT 1079 1078 1080 1080 1088
CONECT 1080 1079 1079
CONECT 1081 1078 1082
CONECT 1082 1081 1083
CONECT 1083 1082 1084
CONECT 1084 1083 1085
CONECT 1085 1084 1086 1086 1087
CONECT 1086 1085 1085
CONECT 1087 1085
CONECT 1088 1079 1089
CONECT 1089 1088 1090 1092
CONECT 1090 1089 1091 1091 1096
CONECT 1091 1090 1090
CONECT 1092 1089 1093
CONECT 1093 1092 1094 1095
CONECT 1094 1093
CONECT 1095 1093
CONECT 1096 1090 1097
CONECT 1097 1096 1098 1100
CONECT 1098 1097 1099 1099 1101
CONECT 1099 1098 1098
CONECT 1100 1097
CONECT 1101 1098 1102
CONECT 1102 1101 1103 1105
CONECT 1103 1102 1104 1104 1106
CONECT 1104 1103 1103
CONECT 1105 1102
CONECT 1106 1103 1107
CONECT 1107 1106 1108 1110
CONECT 1108 1107 1109 1109 1114
CONECT 1109 1108 1108
CONECT 1110 1107 1111
CONECT 1111 1110 1112 1112 1113
CONECT 1112 1111 1111
CONECT 1113 1111
CONECT 1114 1108 1115
CONECT 1115 1114 1116 1118
CONECT 1116 1115 1117 1117 1121
CONECT 1117 1116 1116
CONECT 1118 1115 1119 1120
CONECT 1119 1118
CONECT 1120 1118
CONECT 1121 1116 1122
CONECT 1122 1121 1123
CONECT 1123 1122 1124 1124 1125
CONECT 1124 1123 1123
CONECT 1125 1123 1126
CONECT 1126 1125 1127 1129
CONECT 1127 1126 1128 1128 1134
CONECT 1128 1127 1127
CONECT 1129 1126 1130
CONECT 1130 1129 1131
CONECT 1131 1130 1132
CONECT 1132 1131 1133
CONECT 1133 1132
CONECT 1134 1127 1135
CONECT 1135 1134 1136
CONECT 1136 1135 1137 1137 1138
CONECT 1137 1136 1136
CONECT 1138 1136 1139
CONECT 1139 1138 1140 1142
CONECT 1140 1139 1141 1141 1143
CONECT 1141 1140 1140
CONECT 1142 1139
CONECT 1143 1140 1144
CONECT 1144 1143 1145 1147
CONECT 1145 1144 1146 1146 1148
CONECT 1146 1145 1145
CONECT 1147 1144
CONECT 1148 1145 1149
CONECT 1149 1148 1150 1152
CONECT 1150 1149 1151 1151 1157
CONECT 1151 1150 1150
CONECT 1152 1149 1153
CONECT 1153 1152 1154
CONECT 1154 1153 1155 1155 1156
CONECT 1155 1154 1154
CONECT 1156 1154
CONECT 1157 1150 1158
CONECT 1158 1157 1159 1161
CONECT 1159 1158 1160 1160 1168
CONECT 1160 1159 1159
CONECT 1161 1158 1162
CONECT 1162 1161 1163
CONECT 1163 1162 1164
CONECT 1164 1163 1165
CONECT 1165 1164 1166 1166 1167
CONECT 1166 1165 1165
CONECT 1167 1165
CONECT 1168 1159 1169
CONECT 1169 1168 1170 1172
CONECT 1170 1169 1171 1171 1177
CONECT 1171 1170 1170
CONECT 1172 1169 1173
CONECT 1173 1172 1174
CONECT 1174 1173 1175 1175 1176
CONECT 1175 1174 1174
CONECT 1176 1174
CONECT 1177 1170 1178
CONECT 1178 1177 1179 1181
CONECT 1179 1178 1180 1180 1188
CONECT 1180 1179 1179
CONECT 1181 1178 1182
CONECT 1182 1181 1183 1183 1184
CONECT 1183 1182 1182 1185
CONECT 1184 1182 1186 1186
CONECT 1185 1183 1187 1187
CONECT 1186 1184 1184 1187
CONECT 1187 1185 1185 1186
CONECT 1188 1179 1189
CONECT 1189 1188 1190 1192
CONECT 1190 1189 1191 1191 1195
CONECT 1191 1190 1190
CONECT 1192 1189 1193 1194
CONECT 1193 1192
CONECT 1194 1192
CONECT 1195 1190 1196
CONECT 1196 1195 1197
CONECT 1197 1196 1198 1198 1199
CONECT 1198 1197 1197
CONECT 1199 1197 1200
CONECT 1200 1199 1201 1203
CONECT 1201 1200 1202 1202 1207
CONECT 1202 1201 1201
CONECT 1203 1200 1204
CONECT 1204 1203 1205 1206
CONECT 1205 1204
CONECT 1206 1204
CONECT 1207 1201 1208
CONECT 1208 1207 1209
CONECT 1209 1208 1210 1210 1211
CONECT 1210 1209 1209
CONECT 1211 1209 1212
CONECT 1212 1211 1213 1215
CONECT 1213 1212 1214 1214 1219
CONECT 1214 1213 1213
CONECT 1215 1212 1216
CONECT 1216 1215 1217 1217 1218
CONECT 1217 1216 1216
CONECT 1218 1216
CONECT 1219 1213 1220
CONECT 1220 1219 1221 1223
CONECT 1221 1220 1222 1222 1225
CONECT 1222 1221 1221
CONECT 1223 1220 1224
CONECT 1224 1223
CONECT 1225 1221 1226
CONECT 1226 1225 1227 1229
CONECT 1227 1226 1228 1228 1233
CONECT 1228 1227 1227
CONECT 1229 1226 1230 1231
CONECT 1230 1229 1232
CONECT 1231 1229
CONECT 1232 1230
CONECT 1233 1227 1234
CONECT 1234 1233 1235 1237
CONECT 1235 1234 1236 1236 1240
CONECT 1236 1235 1235
CONECT 1237 1234 1238 1239
CONECT 1238 1237
CONECT 1239 1237
CONECT 1240 1235 1241
CONECT 1241 1240 1242 1244
CONECT 1242 1241 1243 1243 1249
CONECT 1243 1242 1242
CONECT 1244 1241 1245
CONECT 1245 1244 1246
CONECT 1246 1245 1247
CONECT 1247 1246 1248
CONECT 1248 1247
CONECT 1249 1242 1250
CONECT 1250 1249 1251 1253
CONECT 1251 1250 1252 1252 1257
CONECT 1252 1251 1251
CONECT 1253 1250 1254 1255
CONECT 1254 1253 1256
CONECT 1255 1253
CONECT 1256 1254
CONECT 1257 1251 1258
CONECT 1258 1257 1259 1261
CONECT 1259 1258 1260 1260 1268
CONECT 1260 1259 1259
CONECT 1261 1258 1262
CONECT 1262 1261 1263 1263 1264
CONECT 1263 1262 1262 1265
CONECT 1264 1262 1266 1266
CONECT 1265 1263 1267 1267
CONECT 1266 1264 1264 1267
CONECT 1267 1265 1265 1266
CONECT 1268 1259 1269
CONECT 1269 1268 1270 1272
CONECT 1270 1269 1271 1271 1277
CONECT 1271 1270 1270
CONECT 1272 1269 1273
CONECT 1273 1272 1274
CONECT 1274 1273 1275
CONECT 1275 1274 1276
CONECT 1276 1275
CONECT 1277 1270 1278
CONECT 1278 1277 1279 1281
CONECT 1279 1278 1280 1280 1283
CONECT 1280 1279 1279
CONECT 1281 1278 1282
CONECT 1282 1281
CONECT 1283 1279 1284
CONECT 1284 1283 1285 1287
CONECT 1285 1284 1286 1286 1291
CONECT 1286 1285 1285
CONECT 1287 1284 1288
CONECT 1288 1287 1289 1289 1290
CONECT 1289 1288 1288
CONECT 1290 1288
CONECT 1291 1285 1292
CONECT 1292 1291 1293
CONECT 1293 1292 1294 1294 1295
CONECT 1294 1293 1293
CONECT 1295 1293 1296
CONECT 1296 1295 1297 1299
CONECT 1297 1296 1298 1298 1303
CONECT 1298 1297 1297
CONECT 1299 1296 1300
CONECT 1300 1299 1301 1302
CONECT 1301 1300
CONECT 1302 1300
CONECT 1303 1297 1304
CONECT 1304 1303 1305 1307
CONECT 1305 1304 1306 1306 1308
CONECT 1306 1305 1305
CONECT 1307 1304
CONECT 1308 1305 1309
CONECT 1309 1308 1310
CONECT 1310 1309 1311 1311 1312
CONECT 1311 1310 1310
CONECT 1312 1310 1313
CONECT 1313 1312 1314 1316
CONECT 1314 1313 1315 1315 1320
CONECT 1315 1314 1314
CONECT 1316 1313 1317
CONECT 1317 1316 1318 1319
CONECT 1318 1317
CONECT 1319 1317
CONECT 1320 1314 1321
CONECT 1321 1320 1322 1324
CONECT 1322 1321 1323 1323 1332
CONECT 1323 1322 1322
CONECT 1324 1321 1325
CONECT 1325 1324 1326 1326 1327
CONECT 1326 1325 1325 1328
CONECT 1327 1325 1329 1329
CONECT 1328 1326 1330 1330
CONECT 1329 1327 1327 1330
CONECT 1330 1328 1328 1329 1331
CONECT 1331 1330
CONECT 1332 1322 1333
CONECT 1333 1332 1334 1336
CONECT 1334 1333 1335 1335 1341
CONECT 1335 1334 1334
CONECT 1336 1333 1337
CONECT 1337 1336 1338
CONECT 1338 1337 1339 1339 1340
CONECT 1339 1338 1338
CONECT 1340 1338
CONECT 1341 1334 1342
CONECT 1342 1341 1343
CONECT 1343 1342 1344 1344 1345
CONECT 1344 1343 1343
CONECT 1345 1343 1346
CONECT 1346 1345 1347 1349
CONECT 1347 1346 1348 1348 1356
CONECT 1348 1347 1347
CONECT 1349 1346 1350
CONECT 1350 1349 1351 1351 1352
CONECT 1351 1350 1350 1353
CONECT 1352 1350 1354 1354
CONECT 1353 1351 1355 1355
CONECT 1354 1352 1352 1355
CONECT 1355 1353 1353 1354
CONECT 1356 1347 1357
CONECT 1357 1356 1358 1360
CONECT 1358 1357 1359 1359 1364
CONECT 1359 1358 1358
CONECT 1360 1357 1361
CONECT 1361 1360 1362 1362 1363
CONECT 1362 1361 1361
CONECT 1363 1361
CONECT 1364 1358 1365
CONECT 1365 1364 1366 1368
CONECT 1366 1365 1367 1367 1371
CONECT 1367 1366 1366
CONECT 1368 1365 1369 1370
CONECT 1369 1368
CONECT 1370 1368
CONECT 1371 1366 1372
CONECT 1372 1371 1373 1375
CONECT 1373 1372 1374 1374 1377
CONECT 1374 1373 1373
CONECT 1375 1372 1376
CONECT 1376 1375
CONECT 1377 1373 1378
CONECT 1378 1377 1379 1381
CONECT 1379 1378 1380 1380 1384
CONECT 1380 1379 1379
CONECT 1381 1378 1382 1383
CONECT 1382 1381
CONECT 1383 1381
CONECT 1384 1379 1385
CONECT 1385 1384 1386 1388
CONECT 1386 1385 1387 1387 1393
CONECT 1387 1386 1386
CONECT 1388 1385 1389
CONECT 1389 1388 1390
CONECT 1390 1389 1391 1391 1392
CONECT 1391 1390 1390
CONECT 1392 1390
CONECT 1393 1386 1394
CONECT 1394 1393 1395
CONECT 1395 1394 1396 1396 1397
CONECT 1396 1395 1395
CONECT 1397 1395 1398
CONECT 1398 1397 1399 1401
CONECT 1399 1398 1400 1400 1405
CONECT 1400 1399 1399
CONECT 1401 1398 1402 1403
CONECT 1402 1401 1404
CONECT 1403 1401
CONECT 1404 1402
CONECT 1405 1399 1406
CONECT 1406 1405 1407 1409
CONECT 1407 1406 1408 1408 1413
CONECT 1408 1407 1407
CONECT 1409 1406 1410 1411
CONECT 1410 1409 1412
CONECT 1411 1409
CONECT 1412 1410
CONECT 1413 1407 1414
CONECT 1414 1413 1415 1417
CONECT 1415 1414 1416 1416 1421
CONECT 1416 1415 1415
CONECT 1417 1414 1418 1419
CONECT 1418 1417 1420
CONECT 1419 1417
CONECT 1420 1418
CONECT 1421 1415 1422
CONECT 1422 1421 1423 1425
CONECT 1423 1422 1424 1424 1433
CONECT 1424 1423 1423
CONECT 1425 1422 1426
CONECT 1426 1425 1427 1427 1428
CONECT 1427 1426 1426 1429
CONECT 1428 1426 1430 1430
CONECT 1429 1427 1431 1431
CONECT 1430 1428 1428 1431
CONECT 1431 1429 1429 1430 1432
CONECT 1432 1431
CONECT 1433 1423 1434
CONECT 1434 1433 1435 1437
CONECT 1435 1434 1436 1436 1444
CONECT 1436 1435 1435
CONECT 1437 1434 1438
CONECT 1438 1437 1439
CONECT 1439 1438 1440
CONECT 1440 1439 1441
CONECT 1441 1440 1442 1442 1443
CONECT 1442 1441 1441
CONECT 1443 1441
CONECT 1444 1435 1445
CONECT 1445 1444 1446 1448
CONECT 1446 1445 1447 1447 1449
CONECT 1447 1446 1446
CONECT 1448 1445
CONECT 1449 1446 1450
CONECT 1450 1449 1451 1453
CONECT 1451 1450 1452 1452 1454
CONECT 1452 1451 1451
CONECT 1453 1450
CONECT 1454 1451 1455
CONECT 1455 1454 1456 1458
CONECT 1456 1455 1457 1457 1466
CONECT 1457 1456 1456
CONECT 1458 1455 1459
CONECT 1459 1458 1460 1460 1461
CONECT 1460 1459 1459 1462
CONECT 1461 1459 1463 1463
CONECT 1462 1460 1464 1464
CONECT 1463 1461 1461 1464
CONECT 1464 1462 1462 1463 1465
CONECT 1465 1464
CONECT 1466 1456 1467
CONECT 1467 1466 1468 1470
CONECT 1468 1467 1469 1469 1477
CONECT 1469 1468 1468
CONECT 1470 1467 1471
CONECT 1471 1470 1472 1472 1473
CONECT 1472 1471 1471 1474
CONECT 1473 1471 1475 1475
CONECT 1474 1472 1476 1476
CONECT 1475 1473 1473 1476
CONECT 1476 1474 1474 1475
CONECT 1477 1468 1478
CONECT 1478 1477 1479
CONECT 1479 1478 1480 1480 1481
CONECT 1480 1479 1479
CONECT 1481 1479 1482
CONECT 1482 1481 1483 1485
CONECT 1483 1482 1484 1484 1488
CONECT 1484 1483 1483
CONECT 1485 1482 1486 1487
CONECT 1486 1485
CONECT 1487 1485
CONECT 1488 1483 1489
CONECT 1489 1488 1490 1492
CONECT 1490 1489 1491 1491 1500
CONECT 1491 1490 1490
CONECT 1492 1489 1493
CONECT 1493 1492 1494 1494 1495
CONECT 1494 1493 1493 1496
CONECT 1495 1493 1497 1497
CONECT 1496 1494 1498 1498
CONECT 1497 1495 1495 1498
CONECT 1498 1496 1496 1497 1499
CONECT 1499 1498
CONECT 1500 1490 1501
CONECT 1501 1500 1502 1504
CONECT 1502 1501 1503 1503 1508
CONECT 1503 1502 1502
CONECT 1504 1501 1505
CONECT 1505 1504 1506 1506 1507
CONECT 1506 1505 1505
CONECT 1507 1505
CONECT 1508 1502 1509
CONECT 1509 1508 1510 1512
CONECT 1510 1509 1511 1511 1515
CONECT 1511 1510 1510
CONECT 1512 1509 1513 1514
CONECT 1513 1512
CONECT 1514 1512
CONECT 1515 1510 1516
CONECT 1516 1515 1517 1519
CONECT 1517 1516 1518 1518 1520
CONECT 1518 1517 1517
CONECT 1519 1516
CONECT 1520 1517 1521
CONECT 1521 1520 1522 1524
CONECT 1522 1521 1523 1523 1529
CONECT 1523 1522 1522
CONECT 1524 1521 1525
CONECT 1525 1524 1526
CONECT 1526 1525 1527
CONECT 1527 1526 1528
CONECT 1528 1527
CONECT 1529 1522 1530
CONECT 1530 1529 1531
CONECT 1531 1530 1532 1532 1533
CONECT 1532 1531 1531
CONECT 1533 1531 1534
CONECT 1534 1533 1535 1537
CONECT 1535 1534 1536 1536 1541
CONECT 1536 1535 1535
CONECT 1537 1534 1538
CONECT 1538 1537 1539
CONECT 1539 1538 1540
CONECT 1540 1539
CONECT 1541 1535 1542
CONECT 1542 1541 1543 1545
CONECT 1543 1542 1544 1544 1549
CONECT 1544 1543 1543
CONECT 1545 1542 1546
CONECT 1546 1545 1547 1548
CONECT 1547 1546
CONECT 1548 1546
CONECT 1549 1543 1550 1555
CONECT 1550 1549 1551 1553
CONECT 1551 1550 1552 1552 1556
CONECT 1552 1551 1551
CONECT 1553 1550 1554
CONECT 1554 1553 1555
CONECT 1555 1549 1554
CONECT 1556 1551 1557
CONECT 1557 1556 1558 1560
CONECT 1558 1557 1559 1559 1564
CONECT 1559 1558 1558
CONECT 1560 1557 1561
CONECT 1561 1560 1562 1562 1563
CONECT 1562 1561 1561
CONECT 1563 1561
CONECT 1564 1558 1565 1570
CONECT 1565 1564 1566 1568
CONECT 1566 1565 1567 1567 1571
CONECT 1567 1566 1566
CONECT 1568 1565 1569
CONECT 1569 1568 1570
CONECT 1570 1564 1569
CONECT 1571 1566 1572
CONECT 1572 1571 1573 1575
CONECT 1573 1572 1574 1574 1576
CONECT 1574 1573 1573
CONECT 1575 1572
CONECT 1576 1573 1577
CONECT 1577 1576 1578 1580
CONECT 1578 1577 1579 1579 1584
CONECT 1579 1578 1578
CONECT 1580 1577 1581
CONECT 1581 1580 1582 1582 1583
CONECT 1582 1581 1581
CONECT 1583 1581
CONECT 1584 1578 1585
CONECT 1585 1584 1586 1588
CONECT 1586 1585 1587 1587 1589
CONECT 1587 1586 1586
CONECT 1588 1585
CONECT 1589 1586 1590
CONECT 1590 1589 1591 1593
CONECT 1591 1590 1592 1592 1599
CONECT 1592 1591 1591
CONECT 1593 1590 1594
CONECT 1594 1593 1595 1596 1596
CONECT 1595 1594 1597 1597
CONECT 1596 1594 1594 1598
CONECT 1597 1595 1595 1598
CONECT 1598 1596 1597
CONECT 1599 1591 1600
CONECT 1600 1599 1601 1603
CONECT 1601 1600 1602 1602 1607
CONECT 1602 1601 1601
CONECT 1603 1600 1604 1605
CONECT 1604 1603 1606
CONECT 1605 1603
CONECT 1606 1604
CONECT 1607 1601 1608
CONECT 1608 1607 1609 1611
CONECT 1609 1608 1610 1610 1615
CONECT 1610 1609 1609
CONECT 1611 1608 1612 1613
CONECT 1612 1611 1614
CONECT 1613 1611
CONECT 1614 1612
CONECT 1615 1609 1616
CONECT 1616 1615 1617 1619
CONECT 1617 1616 1618 1618 1622
CONECT 1618 1617 1617
CONECT 1619 1616 1620 1621
CONECT 1620 1619
CONECT 1621 1619
CONECT 1622 1617 1623
CONECT 1623 1622 1624 1626
CONECT 1624 1623 1625 1625 1628
CONECT 1625 1624 1624
CONECT 1626 1623 1627
CONECT 1627 1626
CONECT 1628 1624 1629
CONECT 1629 1628 1630 1632
CONECT 1630 1629 1631 1631 1642
CONECT 1631 1630 1630
CONECT 1632 1629 1633
CONECT 1633 1632 1634 1634 1635
CONECT 1634 1633 1633 1636
CONECT 1635 1633 1637 1637 1638
CONECT 1636 1634 1637
CONECT 1637 1635 1635 1636 1639
CONECT 1638 1635 1640 1640
CONECT 1639 1637 1641 1641
CONECT 1640 1638 1638 1641
CONECT 1641 1639 1639 1640
CONECT 1642 1630 1643
CONECT 1643 1642 1644 1646
CONECT 1644 1643 1645 1645 1650
CONECT 1645 1644 1644
CONECT 1646 1643 1647
CONECT 1647 1646 1648
CONECT 1648 1647 1649
CONECT 1649 1648
CONECT 1650 1644 1651
CONECT 1651 1650 1652 1654
CONECT 1652 1651 1653 1653 1658
CONECT 1653 1652 1652
CONECT 1654 1651 1655 1656
CONECT 1655 1654 1657
CONECT 1656 1654
CONECT 1657 1655
CONECT 1658 1652 1659
CONECT 1659 1658 1660 1662
CONECT 1660 1659 1661 1661 1663
CONECT 1661 1660 1660
CONECT 1662 1659
CONECT 1663 1660 1664
CONECT 1664 1663 1665 1667
CONECT 1665 1664 1666 1666 1672
CONECT 1666 1665 1665
CONECT 1667 1664 1668
CONECT 1668 1667 1669
CONECT 1669 1668 1670 1670 1671
CONECT 1670 1669 1669
CONECT 1671 1669
CONECT 1672 1665 1673
CONECT 1673 1672 1674 1676
CONECT 1674 1673 1675 1675 1679
CONECT 1675 1674 1674
CONECT 1676 1673 1677 1678
CONECT 1677 1676
CONECT 1678 1676
CONECT 1679 1674 1680
CONECT 1680 1679 1681 1683
CONECT 1681 1680 1682 1682 1686
CONECT 1682 1681 1681
CONECT 1683 1680 1684 1685
CONECT 1684 1683
CONECT 1685 1683
CONECT 1686 1681 1687
CONECT 1687 1686 1688 1690
CONECT 1688 1687 1689 1689 1693
CONECT 1689 1688 1688
CONECT 1690 1687 1691 1692
CONECT 1691 1690
CONECT 1692 1690
CONECT 1693 1688 1694
CONECT 1694 1693 1695 1697
CONECT 1695 1694 1696 1696 1698
CONECT 1696 1695 1695
CONECT 1697 1694
CONECT 1698 1695 1699
CONECT 1699 1698 1700 1702
CONECT 1700 1699 1701 1701 1705
CONECT 1701 1700 1700
CONECT 1702 1699 1703 1704
CONECT 1703 1702
CONECT 1704 1702
CONECT 1705 1700 1706
CONECT 1706 1705 1707 1709
CONECT 1707 1706 1708 1708 1710
CONECT 1708 1707 1707
CONECT 1709 1706
CONECT 1710 1707 1711
CONECT 1711 1710 1712
CONECT 1712 1711 1713 1713 1714
CONECT 1713 1712 1712
CONECT 1714 1712 1715
CONECT 1715 1714 1716 1718
CONECT 1716 1715 1717 1717 1722
CONECT 1717 1716 1716
CONECT 1718 1715 1719
CONECT 1719 1718 1720 1721
CONECT 1720 1719
CONECT 1721 1719
CONECT 1722 1716 1723
CONECT 1723 1722 1724 1726
CONECT 1724 1723 1725 1725 1729
CONECT 1725 1724 1724
CONECT 1726 1723 1727 1728
CONECT 1727 1726
CONECT 1728 1726
CONECT 1729 1724 1730
CONECT 1730 1729 1731 1733
CONECT 1731 1730 1732 1732 1735
CONECT 1732 1731 1731
CONECT 1733 1730 1734
CONECT 1734 1733
CONECT 1735 1731 1736
CONECT 1736 1735 1737 1739
CONECT 1737 1736 1738 1738 1747
CONECT 1738 1737 1737
CONECT 1739 1736 1740
CONECT 1740 1739 1741 1741 1742
CONECT 1741 1740 1740 1743
CONECT 1742 1740 1744 1744
CONECT 1743 1741 1745 1745
CONECT 1744 1742 1742 1745
CONECT 1745 1743 1743 1744 1746
CONECT 1746 1745
CONECT 1747 1737 1748 1753
CONECT 1748 1747 1749 1751
CONECT 1749 1748 1750 1750 1754
CONECT 1750 1749 1749
CONECT 1751 1748 1752
CONECT 1752 1751 1753
CONECT 1753 1747 1752
CONECT 1754 1749 1755
CONECT 1755 1754 1756 1758
CONECT 1756 1755 1757 1757 1765
CONECT 1757 1756 1756
CONECT 1758 1755 1759
CONECT 1759 1758 1760 1760 1761
CONECT 1760 1759 1759 1762
CONECT 1761 1759 1763 1763
CONECT 1762 1760 1764 1764
CONECT 1763 1761 1761 1764
CONECT 1764 1762 1762 1763
CONECT 1765 1756 1766
CONECT 1766 1765 1767 1769
CONECT 1767 1766 1768 1768 1773
CONECT 1768 1767 1767
CONECT 1769 1766 1770
CONECT 1770 1769 1771 1771 1772
CONECT 1771 1770 1770
CONECT 1772 1770
CONECT 1773 1767 1774
CONECT 1774 1773 1775 1777
CONECT 1775 1774 1776 1776 1780
CONECT 1776 1775 1775
CONECT 1777 1774 1778 1779
CONECT 1778 1777
CONECT 1779 1777
CONECT 1780 1775 1781
CONECT 1781 1780 1782 1784
CONECT 1782 1781 1783 1783 1787
CONECT 1783 1782 1782
CONECT 1784 1781 1785 1786
CONECT 1785 1784
CONECT 1786 1784
CONECT 1787 1782 1788
CONECT 1788 1787 1789 1791
CONECT 1789 1788 1790 1790 1798
CONECT 1790 1789 1789
CONECT 1791 1788 1792
CONECT 1792 1791 1793
CONECT 1793 1792 1794
CONECT 1794 1793 1795
CONECT 1795 1794 1796 1796 1797
CONECT 1796 1795 1795
CONECT 1797 1795
CONECT 1798 1789 1799
CONECT 1799 1798 1800 1802
CONECT 1800 1799 1801 1801 1809
CONECT 1801 1800 1800
CONECT 1802 1799 1803
CONECT 1803 1802 1804
CONECT 1804 1803 1805
CONECT 1805 1804 1806
CONECT 1806 1805 1807 1807 1808
CONECT 1807 1806 1806
CONECT 1808 1806
CONECT 1809 1800 1810
CONECT 1810 1809 1811 1813
CONECT 1811 1810 1812 1812 1820
CONECT 1812 1811 1811
CONECT 1813 1810 1814
CONECT 1814 1813 1815
CONECT 1815 1814 1816
CONECT 1816 1815 1817
CONECT 1817 1816 1818 1818 1819
CONECT 1818 1817 1817
CONECT 1819 1817
CONECT 1820 1811 1821
CONECT 1821 1820 1822 1824
CONECT 1822 1821 1823 1823 1828
CONECT 1823 1822 1822
CONECT 1824 1821 1825
CONECT 1825 1824 1826
CONECT 1826 1825 1827
CONECT 1827 1826
CONECT 1828 1822 1829
CONECT 1829 1828 1830 1832
CONECT 1830 1829 1831 1831 1836
CONECT 1831 1830 1830
CONECT 1832 1829 1833
CONECT 1833 1832 1834
CONECT 1834 1833 1835
CONECT 1835 1834
CONECT 1836 1830 1837
CONECT 1837 1836 1838 1840
CONECT 1838 1837 1839 1839 1844
CONECT 1839 1838 1838
CONECT 1840 1837 1841
CONECT 1841 1840 1842
CONECT 1842 1841 1843
CONECT 1843 1842
CONECT 1844 1838 1845
CONECT 1845 1844 1846 1848
CONECT 1846 1845 1847 1847 1853
CONECT 1847 1846 1846
CONECT 1848 1845 1849
CONECT 1849 1848 1850
CONECT 1850 1849 1851 1851 1852
CONECT 1851 1850 1850
CONECT 1852 1850
CONECT 1853 1846 1854
CONECT 1854 1853 1855 1857
CONECT 1855 1854 1856 1856 1859
CONECT 1856 1855 1855
CONECT 1857 1854 1858
CONECT 1858 1857
CONECT 1859 1855 1860
CONECT 1860 1859 1861
CONECT 1861 1860 1862 1862 1863
CONECT 1862 1861 1861
CONECT 1863 1861 1864
CONECT 1864 1863 1865 1867
CONECT 1865 1864 1866 1866 1874
CONECT 1866 1865 1865
CONECT 1867 1864 1868
CONECT 1868 1867 1869
CONECT 1869 1868 1870
CONECT 1870 1869 1871
CONECT 1871 1870 1872 1872 1873
CONECT 1872 1871 1871
CONECT 1873 1871
CONECT 1874 1865 1875
CONECT 1875 1874 1876 1878
CONECT 1876 1875 1877 1877 1883
CONECT 1877 1876 1876
CONECT 1878 1875 1879
CONECT 1879 1878 1880
CONECT 1880 1879 1881
CONECT 1881 1880 1882
CONECT 1882 1881
CONECT 1883 1876 1884
CONECT 1884 1883 1885
CONECT 1885 1884 1886 1886 1887
CONECT 1886 1885 1885
CONECT 1887 1885 1888
CONECT 1888 1887 1889 1891
CONECT 1889 1888 1890 1890 1892
CONECT 1890 1889 1889
CONECT 1891 1888
CONECT 1892 1889 1893
CONECT 1893 1892 1894 1896
CONECT 1894 1893 1895 1895 1900
CONECT 1895 1894 1894
CONECT 1896 1893 1897
CONECT 1897 1896 1898 1898 1899
CONECT 1898 1897 1897
CONECT 1899 1897
CONECT 1900 1894 1901
CONECT 1901 1900 1902 1904
CONECT 1902 1901 1903 1903 1908
CONECT 1903 1902 1902
CONECT 1904 1901 1905 1906
CONECT 1905 1904 1907
CONECT 1906 1904
CONECT 1907 1905
CONECT 1908 1902 1909
CONECT 1909 1908 1910 1912
CONECT 1910 1909 1911 1911 1916
CONECT 1911 1910 1910
CONECT 1912 1909 1913
CONECT 1913 1912 1914
CONECT 1914 1913 1915
CONECT 1915 1914
CONECT 1916 1910 1917
CONECT 1917 1916 1918 1920
CONECT 1918 1917 1919 1919 1928
CONECT 1919 1918 1918
CONECT 1920 1917 1921
CONECT 1921 1920 1922 1922 1923
CONECT 1922 1921 1921 1924
CONECT 1923 1921 1925 1925
CONECT 1924 1922 1926 1926
CONECT 1925 1923 1923 1926
CONECT 1926 1924 1924 1925 1927
CONECT 1927 1926
CONECT 1928 1918 1929
CONECT 1929 1928 1930 1932
CONECT 1930 1929 1931 1931 1935
CONECT 1931 1930 1930
CONECT 1932 1929 1933 1934
CONECT 1933 1932
CONECT 1934 1932
CONECT 1935 1930 1936
CONECT 1936 1935 1937
CONECT 1937 1936 1938 1938 1939
CONECT 1938 1937 1937
CONECT 1939 1937 1940
CONECT 1940 1939 1941 1943
CONECT 1941 1940 1942 1942 1946
CONECT 1942 1941 1941
CONECT 1943 1940 1944 1945
CONECT 1944 1943
CONECT 1945 1943
CONECT 1946 1941 1947
CONECT 1947 1946 1948 1950
CONECT 1948 1947 1949 1949 1953
CONECT 1949 1948 1948
CONECT 1950 1947 1951 1952
CONECT 1951 1950
CONECT 1952 1950
CONECT 1953 1948 1954
CONECT 1954 1953 1955 1957
CONECT 1955 1954 1956 1956 1961
CONECT 1956 1955 1955
CONECT 1957 1954 1958
CONECT 1958 1957 1959 1959 1960
CONECT 1959 1958 1958
CONECT 1960 1958
CONECT 1961 1955 1962
CONECT 1962 1961 1963 1965
CONECT 1963 1962 1964 1964 1967
CONECT 1964 1963 1963
CONECT 1965 1962 1966
CONECT 1966 1965
CONECT 1967 1963 1968
CONECT 1968 1967 1969 1971
CONECT 1969 1968 1970 1970 1981
CONECT 1970 1969 1969
CONECT 1971 1968 1972
CONECT 1972 1971 1973 1973 1974
CONECT 1973 1972 1972 1975
CONECT 1974 1972 1976 1976 1977
CONECT 1975 1973 1976
CONECT 1976 1974 1974 1975 1978
CONECT 1977 1974 1979 1979
CONECT 1978 1976 1980 1980
CONECT 1979 1977 1977 1980
CONECT 1980 1978 1978 1979
CONECT 1981 1969 1982
CONECT 1982 1981 1983 1985
CONECT 1983 1982 1984 1984 1992
CONECT 1984 1983 1983
CONECT 1985 1982 1986
CONECT 1986 1985 1987
CONECT 1987 1986 1988
CONECT 1988 1987 1989
CONECT 1989 1988 1990 1990 1991
CONECT 1990 1989 1989
CONECT 1991 1989
CONECT 1992 1983 1993
CONECT 1993 1992 1994 1996
CONECT 1994 1993 1995 1995 2001
CONECT 1995 1994 1994
CONECT 1996 1993 1997
CONECT 1997 1996 1998
CONECT 1998 1997 1999
CONECT 1999 1998 2000
CONECT 2000 1999
CONECT 2001 1994 2002
CONECT 2002 2001 2003 2005
CONECT 2003 2002 2004 2004 2009
CONECT 2004 2003 2003
CONECT 2005 2002 2006 2007
CONECT 2006 2005 2008
CONECT 2007 2005
CONECT 2008 2006
CONECT 2009 2003 2010
CONECT 2010 2009 2011 2013
CONECT 2011 2010 2012 2012 2014
CONECT 2012 2011 2011
CONECT 2013 2010
CONECT 2014 2011 2015
CONECT 2015 2014 2016 2018
CONECT 2016 2015 2017 2017 2023
CONECT 2017 2016 2016
CONECT 2018 2015 2019
CONECT 2019 2018 2020
CONECT 2020 2019 2021
CONECT 2021 2020 2022
CONECT 2022 2021
CONECT 2023 2016 2024
CONECT 2024 2023 2025 2027
CONECT 2025 2024 2026 2026 2031
CONECT 2026 2025 2025
CONECT 2027 2024 2028
CONECT 2028 2027 2029 2029 2030
CONECT 2029 2028 2028
CONECT 2030 2028
CONECT 2031 2025 2032
CONECT 2032 2031 2033 2035
CONECT 2033 2032 2034 2034 2040
CONECT 2034 2033 2033
CONECT 2035 2032 2036
CONECT 2036 2035 2037
CONECT 2037 2036 2038 2038 2039
CONECT 2038 2037 2037
CONECT 2039 2037
CONECT 2040 2033 2041
CONECT 2041 2040 2042
CONECT 2042 2041 2043 2043 2044
CONECT 2043 2042 2042
CONECT 2044 2042 2045 2050
CONECT 2045 2044 2046 2048
CONECT 2046 2045 2047 2047 2051
CONECT 2047 2046 2046
CONECT 2048 2045 2049
CONECT 2049 2048 2050
CONECT 2050 2044 2049
CONECT 2051 2046 2052
CONECT 2052 2051 2053 2055
CONECT 2053 2052 2054 2054 2056
CONECT 2054 2053 2053
CONECT 2055 2052
CONECT 2056 2053 2057
CONECT 2057 2056 2058 2060
CONECT 2058 2057 2059 2059 2061
CONECT 2059 2058 2058
CONECT 2060 2057
CONECT 2061 2058 2062
CONECT 2062 2061 2063 2065
CONECT 2063 2062 2064 2064 2072
CONECT 2064 2063 2063
CONECT 2065 2062 2066
CONECT 2066 2065 2067 2067 2068
CONECT 2067 2066 2066 2069
CONECT 2068 2066 2070 2070
CONECT 2069 2067 2071 2071
CONECT 2070 2068 2068 2071
CONECT 2071 2069 2069 2070
CONECT 2072 2063 2073
CONECT 2073 2072 2074 2076
CONECT 2074 2073 2075 2075 2083
CONECT 2075 2074 2074
CONECT 2076 2073 2077
CONECT 2077 2076 2078 2078 2079
CONECT 2078 2077 2077 2080
CONECT 2079 2077 2081 2081
CONECT 2080 2078 2082 2082
CONECT 2081 2079 2079 2082
CONECT 2082 2080 2080 2081
CONECT 2083 2074 2084
CONECT 2084 2083 2085 2087
CONECT 2085 2084 2086 2086 2092
CONECT 2086 2085 2085
CONECT 2087 2084 2088
CONECT 2088 2087 2089
CONECT 2089 2088 2090
CONECT 2090 2089 2091
CONECT 2091 2090
CONECT 2092 2085 2093
CONECT 2093 2092 2094
CONECT 2094 2093 2095 2095 2096
CONECT 2095 2094 2094
CONECT 2096 2094 2097
CONECT 2097 2096 2098 2100
CONECT 2098 2097 2099 2099 2101
CONECT 2099 2098 2098
CONECT 2100 2097
CONECT 2101 2098 2102
CONECT 2102 2101 2103 2105
CONECT 2103 2102 2104 2104 2115
CONECT 2104 2103 2103
CONECT 2105 2102 2106
CONECT 2106 2105 2107 2107 2108
CONECT 2107 2106 2106 2109
CONECT 2108 2106 2110 2110 2111
CONECT 2109 2107 2110
CONECT 2110 2108 2108 2109 2112
CONECT 2111 2108 2113 2113
CONECT 2112 2110 2114 2114
CONECT 2113 2111 2111 2114
CONECT 2114 2112 2112 2113
CONECT 2115 2103 2116
CONECT 2116 2115 2117 2119
CONECT 2117 2116 2118 2118 2121
CONECT 2118 2117 2117
CONECT 2119 2116 2120
CONECT 2120 2119
CONECT 2121 2117 2122
CONECT 2122 2121 2123 2125
CONECT 2123 2122 2124 2124 2129
CONECT 2124 2123 2123
CONECT 2125 2122 2126
CONECT 2126 2125 2127 2127 2128
CONECT 2127 2126 2126
CONECT 2128 2126
CONECT 2129 2123 2130
CONECT 2130 2129 2131 2133
CONECT 2131 2130 2132 2132 2136
CONECT 2132 2131 2131
CONECT 2133 2130 2134 2135
CONECT 2134 2133
CONECT 2135 2133
CONECT 2136 2131 2137
CONECT 2137 2136 2138 2140
CONECT 2138 2137 2139 2139 2144
CONECT 2139 2138 2138
CONECT 2140 2137 2141
CONECT 2141 2140 2142 2143
CONECT 2142 2141
CONECT 2143 2141
CONECT 2144 2138 2145
CONECT 2145 2144 2146 2148
CONECT 2146 2145 2147 2147 2155
CONECT 2147 2146 2146
CONECT 2148 2145 2149
CONECT 2149 2148 2150
CONECT 2150 2149 2151
CONECT 2151 2150 2152
CONECT 2152 2151 2153 2153 2154
CONECT 2153 2152 2152
CONECT 2154 2152
CONECT 2155 2146 2156
CONECT 2156 2155 2157
CONECT 2157 2156 2158 2158 2159
CONECT 2158 2157 2157
CONECT 2159 2157 2160
CONECT 2160 2159 2161 2163
CONECT 2161 2160 2162 2162 2167
CONECT 2162 2161 2161
CONECT 2163 2160 2164
CONECT 2164 2163 2165
CONECT 2165 2164 2166
CONECT 2166 2165
CONECT 2167 2161 2168
CONECT 2168 2167 2169
CONECT 2169 2168 2170 2170 2171
CONECT 2170 2169 2169
CONECT 2171 2169 2172
CONECT 2172 2171 2173
CONECT 2173 2172 2174 2174 2175
CONECT 2174 2173 2173
CONECT 2175 2173 2176
CONECT 2176 2175 2177 2179
CONECT 2177 2176 2178 2178 2180
CONECT 2178 2177 2177
CONECT 2179 2176
CONECT 2180 2177 2181
CONECT 2181 2180 2182 2184
CONECT 2182 2181 2183 2183 2191
CONECT 2183 2182 2182
CONECT 2184 2181 2185
CONECT 2185 2184 2186 2186 2187
CONECT 2186 2185 2185 2188
CONECT 2187 2185 2189 2189
CONECT 2188 2186 2190 2190
CONECT 2189 2187 2187 2190
CONECT 2190 2188 2188 2189
CONECT 2191 2182 2192
CONECT 2192 2191 2193 2195
CONECT 2193 2192 2194 2194 2198
CONECT 2194 2193 2193
CONECT 2195 2192 2196 2197
CONECT 2196 2195
CONECT 2197 2195
CONECT 2198 2193 2199
CONECT 2199 2198 2200 2202
CONECT 2200 2199 2201 2201 2206
CONECT 2201 2200 2200
CONECT 2202 2199 2203
CONECT 2203 2202 2204 2205
CONECT 2204 2203
CONECT 2205 2203
CONECT 2206 2200 2207
CONECT 2207 2206 2208 2210
CONECT 2208 2207 2209 2209 2213
CONECT 2209 2208 2208
CONECT 2210 2207 2211 2212
CONECT 2211 2210
CONECT 2212 2210
CONECT 2213 2208 2214
CONECT 2214 2213 2215 2217
CONECT 2215 2214 2216 2216 2221
CONECT 2216 2215 2215
CONECT 2217 2214 2218
CONECT 2218 2217 2219 2220
CONECT 2219 2218
CONECT 2220 2218
CONECT 2221 2215 2222
CONECT 2222 2221 2223 2225
CONECT 2223 2222 2224 2224 2233
CONECT 2224 2223 2223
CONECT 2225 2222 2226
CONECT 2226 2225 2227 2227 2228
CONECT 2227 2226 2226 2229
CONECT 2228 2226 2230 2230
CONECT 2229 2227 2231 2231
CONECT 2230 2228 2228 2231
CONECT 2231 2229 2229 2230 2232
CONECT 2232 2231
CONECT 2233 2223 2234
CONECT 2234 2233 2235 2237
CONECT 2235 2234 2236 2236 2241
CONECT 2236 2235 2235
CONECT 2237 2234 2238
CONECT 2238 2237 2239 2239 2240
CONECT 2239 2238 2238
CONECT 2240 2238
CONECT 2241 2235 2242
CONECT 2242 2241 2243 2245
CONECT 2243 2242 2244 2244 2250
CONECT 2244 2243 2243
CONECT 2245 2242 2246
CONECT 2246 2245 2247
CONECT 2247 2246 2248 2248 2249
CONECT 2248 2247 2247
CONECT 2249 2247
CONECT 2250 2243 2251
CONECT 2251 2250 2252 2254
CONECT 2252 2251 2253 2253
CONECT 2253 2252 2252
CONECT 2254 2251
END



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.