CNRS Nantes University US2B US2B
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***  CDK2  ***

elNémo ID: 23050916240439595

Job options:

ID        	=	 23050916240439595
JOBID     	=	 CDK2
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER CDK2

CRYST1   53.340   71.434   72.406  90.00  90.00  90.00 P 21 21 21    1
HETATM    1  C   ACE A   0      40.807  33.635  39.882  1.00 27.76           C  
HETATM    2  O   ACE A   0      39.803  34.163  40.365  1.00 27.43           O  
HETATM    3  CH3 ACE A   0      42.068  34.466  39.623  1.00 28.59           C  
ATOM      4  N   MET A   1      40.897  32.336  39.600  1.00 28.70           N  
ANISOU    4  N   MET A   1     3196   4258   3449    289   -618    126       N  
ATOM      5  CA  MET A   1      39.768  31.403  39.770  1.00 28.96           C  
ANISOU    5  CA  MET A   1     3249   4277   3477    290   -606    107       C  
ATOM      6  C   MET A   1      39.220  31.283  41.191  1.00 29.04           C  
ANISOU    6  C   MET A   1     3275   4270   3488    288   -609    103       C  
ATOM      7  O   MET A   1      38.068  30.894  41.365  1.00 27.74           O  
ANISOU    7  O   MET A   1     3119   4098   3320    284   -604     97       O  
ATOM      8  CB  MET A   1      40.078  30.012  39.197  1.00 32.84           C  
ANISOU    8  CB  MET A   1     3746   4770   3962    306   -599     99       C  
ATOM      9  CG  MET A   1      39.930  29.911  37.699  1.00 38.78           C  
ANISOU    9  CG  MET A   1     4492   5536   4709    317   -594     97       C  
ATOM     10  SD  MET A   1      38.276  30.329  37.081  1.00 45.92           S  
ANISOU   10  SD  MET A   1     5407   6419   5621    302   -590     88       S  
ATOM     11  CE  MET A   1      38.626  31.924  36.430  1.00 42.63           C  
ANISOU   11  CE  MET A   1     4966   6023   5207    286   -591     94       C  
ATOM     12  N   GLU A   2      40.020  31.620  42.206  1.00 25.36           N  
ANISOU   12  N   GLU A   2     2812   3796   3028    293   -620    111       N  
ATOM     13  CA  GLU A   2      39.543  31.561  43.600  1.00 25.61           C  
ANISOU   13  CA  GLU A   2     2859   3813   3058    299   -624    109       C  
ATOM     14  C   GLU A   2      38.415  32.575  43.860  1.00 28.69           C  
ANISOU   14  C   GLU A   2     3252   4210   3439    300   -633    108       C  
ATOM     15  O   GLU A   2      37.722  32.465  44.872  1.00 28.32           O  
ANISOU   15  O   GLU A   2     3215   4161   3384    311   -632    108       O  
ATOM     16  CB  GLU A   2      40.703  31.746  44.610  1.00 27.08           C  
ANISOU   16  CB  GLU A   2     3055   3979   3256    310   -637    117       C  
ATOM     17  CG  GLU A   2      41.277  33.155  44.696  1.00 35.68           C  
ANISOU   17  CG  GLU A   2     4140   5062   4353    317   -666    134       C  
ATOM     18  CD  GLU A   2      42.275  33.581  43.634  1.00 57.09           C  
ANISOU   18  CD  GLU A   2     6831   7786   7075    310   -675    153       C  
ATOM     19  OE1 GLU A   2      42.644  32.746  42.776  1.00 42.77           O  
ANISOU   19  OE1 GLU A   2     5006   5988   5258    304   -653    149       O  
ATOM     20  OE2 GLU A   2      42.702  34.758  43.672  1.00 54.71           O1-
ANISOU   20  OE2 GLU A   2     6522   7481   6784    313   -710    175       O1-
ATOM     21  N   ASN A   3      38.217  33.549  42.925  1.00 25.59           N  
ANISOU   21  N   ASN A   3     2848   3828   3046    290   -643    108       N  
ATOM     22  CA  ASN A   3      37.173  34.567  43.027  1.00 25.52           C  
ANISOU   22  CA  ASN A   3     2842   3826   3027    288   -659    101       C  
ATOM     23  C   ASN A   3      35.836  34.041  42.511  1.00 27.25           C  
ANISOU   23  C   ASN A   3     3064   4050   3241    276   -636     91       C  
ATOM     24  O   ASN A   3      34.853  34.790  42.525  1.00 27.65           O  
ANISOU   24  O   ASN A   3     3118   4107   3282    272   -644     83       O  
ATOM     25  CB  ASN A   3      37.547  35.794  42.194  1.00 27.15           C  
ANISOU   25  CB  ASN A   3     3035   4042   3239    275   -688    103       C  
ATOM     26  CG  ASN A   3      38.759  36.521  42.701  1.00 36.93           C  
ANISOU   26  CG  ASN A   3     4270   5274   4488    287   -725    123       C  
ATOM     27  ND2 ASN A   3      39.829  36.458  41.937  1.00 29.13           N  
ANISOU   27  ND2 ASN A   3     3263   4291   3513    279   -725    140       N  
ATOM     28  OD1 ASN A   3      38.733  37.175  43.750  1.00 34.99           O  
ANISOU   28  OD1 ASN A   3     4038   5018   4237    308   -758    127       O  
ATOM     29  N   PHE A   4      35.803  32.795  42.023  1.00 23.51           N  
ANISOU   29  N   PHE A   4     2590   3568   2774    272   -613     93       N  
ATOM     30  CA  PHE A   4      34.591  32.164  41.485  1.00 22.61           C  
ANISOU   30  CA  PHE A   4     2481   3446   2662    264   -599     92       C  
ATOM     31  C   PHE A   4      34.271  30.894  42.229  1.00 28.22           C  
ANISOU   31  C   PHE A   4     3196   4153   3373    271   -593    106       C  
ATOM     32  O   PHE A   4      35.151  30.065  42.469  1.00 30.94           O  
ANISOU   32  O   PHE A   4     3540   4494   3721    277   -596    108       O  
ATOM     33  CB  PHE A   4      34.717  31.867  39.977  1.00 22.66           C  
ANISOU   33  CB  PHE A   4     2487   3443   2680    256   -594     86       C  
ATOM     34  CG  PHE A   4      34.877  33.109  39.148  1.00 21.85           C  
ANISOU   34  CG  PHE A   4     2376   3347   2578    242   -601     74       C  
ATOM     35  CD1 PHE A   4      33.763  33.796  38.674  1.00 21.22           C  
ANISOU   35  CD1 PHE A   4     2303   3259   2502    224   -602     62       C  
ATOM     36  CD2 PHE A   4      36.135  33.648  38.910  1.00 23.80           C  
ANISOU   36  CD2 PHE A   4     2608   3610   2826    244   -612     79       C  
ATOM     37  CE1 PHE A   4      33.910  34.982  37.954  1.00 23.53           C  
ANISOU   37  CE1 PHE A   4     2586   3559   2796    206   -617     49       C  
ATOM     38  CE2 PHE A   4      36.276  34.834  38.196  1.00 26.42           C  
ANISOU   38  CE2 PHE A   4     2926   3952   3161    228   -628     74       C  
ATOM     39  CZ  PHE A   4      35.166  35.482  37.703  1.00 23.96           C  
ANISOU   39  CZ  PHE A   4     2621   3632   2851    207   -632     57       C  
ATOM     40  N   GLN A   5      33.021  30.762  42.643  1.00 26.06           N  
ANISOU   40  N   GLN A   5     2925   3882   3096    270   -589    118       N  
ATOM     41  CA  GLN A   5      32.532  29.571  43.308  1.00 26.89           C  
ANISOU   41  CA  GLN A   5     3027   3987   3203    274   -590    141       C  
ATOM     42  C   GLN A   5      31.680  28.826  42.298  1.00 28.66           C  
ANISOU   42  C   GLN A   5     3255   4189   3444    264   -595    154       C  
ATOM     43  O   GLN A   5      30.680  29.369  41.829  1.00 25.98           O  
ANISOU   43  O   GLN A   5     2920   3843   3108    256   -589    157       O  
ATOM     44  CB  GLN A   5      31.685  29.956  44.535  1.00 28.91           C  
ANISOU   44  CB  GLN A   5     3277   4266   3442    284   -586    157       C  
ATOM     45  CG  GLN A   5      31.034  28.762  45.244  1.00 51.34           C  
ANISOU   45  CG  GLN A   5     6107   7114   6286    285   -589    191       C  
ATOM     46  CD  GLN A   5      29.981  29.170  46.247  0.50 73.59           C  
ANISOU   46  CD  GLN A   5     8915   9964   9084    300   -581    215       C  
ATOM     47  NE2 GLN A   5      30.057  28.601  47.439  0.50 67.50           N  
ANISOU   47  NE2 GLN A   5     8132   9212   8303    312   -583    236       N  
ATOM     48  OE1 GLN A   5      29.065  29.952  45.957  0.50 68.88           O  
ANISOU   48  OE1 GLN A   5     8319   9376   8478    301   -574    217       O  
ATOM     49  N   LYS A   6      32.073  27.591  41.961  1.00 26.67           N  
ANISOU   49  N   LYS A   6     3007   3923   3204    267   -612    161       N  
ATOM     50  CA ALYS A   6      31.342  26.728  41.036  0.50 26.84           C  
ANISOU   50  CA ALYS A   6     3037   3915   3245    267   -632    178       C  
ATOM     51  CA BLYS A   6      31.317  26.766  41.026  0.50 27.06           C  
ANISOU   51  CA BLYS A   6     3066   3944   3273    267   -631    178       C  
ATOM     52  C   LYS A   6      29.972  26.377  41.643  1.00 30.73           C  
ANISOU   52  C   LYS A   6     3523   4408   3745    260   -639    218       C  
ATOM     53  O   LYS A   6      29.908  25.959  42.804  1.00 32.50           O  
ANISOU   53  O   LYS A   6     3732   4656   3962    260   -643    239       O  
ATOM     54  CB ALYS A   6      32.163  25.451  40.767  0.50 29.50           C  
ANISOU   54  CB ALYS A   6     3379   4243   3586    279   -663    176       C  
ATOM     55  CB BLYS A   6      32.120  25.525  40.604  0.50 30.21           C  
ANISOU   55  CB BLYS A   6     3471   4331   3678    279   -662    175       C  
ATOM     56  CG ALYS A   6      31.465  24.409  39.897  0.50 37.74           C  
ANISOU   56  CG ALYS A   6     4436   5251   4650    288   -702    198       C  
ATOM     57  CG BLYS A   6      33.259  25.842  39.642  0.50 43.83           C  
ANISOU   57  CG BLYS A   6     5202   6055   5395    292   -655    143       C  
ATOM     58  CD ALYS A   6      32.068  23.028  40.116  0.50 49.75           C  
ANISOU   58  CD ALYS A   6     5958   6771   6172    299   -750    203       C  
ATOM     59  CD BLYS A   6      34.078  24.607  39.299  0.50 54.58           C  
ANISOU   59  CD BLYS A   6     6571   7413   6754    312   -690    137       C  
ATOM     60  CE ALYS A   6      31.148  21.923  39.660  0.50 62.54           C  
ANISOU   60  CE ALYS A   6     7590   8358   7816    308   -806    240       C  
ATOM     61  CE BLYS A   6      35.383  24.979  38.640  0.50 65.58           C  
ANISOU   61  CE BLYS A   6     7963   8823   8132    327   -677    110       C  
ATOM     62  NZ ALYS A   6      31.684  20.583  40.016  0.50 72.51           N1+
ANISOU   62  NZ ALYS A   6     8851   9623   9078    314   -866    245       N1+
ATOM     63  NZ BLYS A   6      36.170  23.777  38.260  0.50 74.08           N1+
ANISOU   63  NZ BLYS A   6     9048   9900   9199    353   -713    101       N1+
ATOM     64  N   VAL A   7      28.891  26.558  40.879  1.00 23.21           N  
ANISOU   64  N   VAL A   7     3261   2605   2952    302    541    134       N  
ATOM     65  CA  VAL A   7      27.536  26.237  41.318  1.00 22.68           C  
ANISOU   65  CA  VAL A   7     3179   2580   2857    246    568    171       C  
ATOM     66  C   VAL A   7      27.231  24.844  40.786  1.00 27.18           C  
ANISOU   66  C   VAL A   7     3832   3078   3419    151    637    194       C  
ATOM     67  O   VAL A   7      26.942  23.938  41.574  1.00 27.54           O  
ANISOU   67  O   VAL A   7     3937   3096   3433    149    695    236       O  
ATOM     68  CB  VAL A   7      26.487  27.293  40.865  1.00 24.93           C  
ANISOU   68  CB  VAL A   7     3376   2946   3150    195    507    145       C  
ATOM     69  CG1 VAL A   7      25.061  26.830  41.194  1.00 25.42           C  
ANISOU   69  CG1 VAL A   7     3421   3062   3176    120    542    147       C  
ATOM     70  CG2 VAL A   7      26.765  28.664  41.475  1.00 24.70           C  
ANISOU   70  CG2 VAL A   7     3260   2987   3139    296    419    123       C  
ATOM     71  N   GLU A   8      27.307  24.668  39.452  1.00 24.11           N  
ANISOU   71  N   GLU A   8     3446   2657   3058     77    629    167       N  
ATOM     72  CA  GLU A   8      27.070  23.396  38.781  1.00 25.41           C  
ANISOU   72  CA  GLU A   8     3663   2757   3235     -3    676    172       C  
ATOM     73  C   GLU A   8      27.619  23.369  37.362  1.00 27.81           C  
ANISOU   73  C   GLU A   8     3952   3042   3571    -35    644    132       C  
ATOM     74  O   GLU A   8      27.826  24.419  36.742  1.00 23.04           O  
ANISOU   74  O   GLU A   8     3299   2480   2974    -27    599    106       O  
ATOM     75  CB  GLU A   8      25.569  23.032  38.781  1.00 27.71           C  
ANISOU   75  CB  GLU A   8     3926   3073   3528    -94    727    175       C  
ATOM     76  CG  GLU A   8      24.668  24.039  38.082  1.00 34.54           C  
ANISOU   76  CG  GLU A   8     4705   4018   4400   -127    687    118       C  
ATOM     77  CD  GLU A   8      23.180  23.829  38.283  1.00 53.79           C  
ANISOU   77  CD  GLU A   8     7105   6507   6826   -200    731     81       C  
ATOM     78  OE1 GLU A   8      22.768  23.431  39.399  1.00 55.10           O  
ANISOU   78  OE1 GLU A   8     7287   6689   6961   -215    780    115       O  
ATOM     79  OE2 GLU A   8      22.418  24.099  37.327  1.00 39.05           O1-
ANISOU   79  OE2 GLU A   8     5191   4673   4974   -238    716      4       O1-
ATOM     80  N   LYS A   9      27.830  22.168  36.837  1.00 26.69           N  
ANISOU   80  N   LYS A   9     3852   2843   3448    -72    662    127       N  
ATOM     81  CA  LYS A   9      28.250  21.983  35.456  1.00 24.77           C  
ANISOU   81  CA  LYS A   9     3576   2602   3234   -102    628     84       C  
ATOM     82  C   LYS A   9      27.004  22.230  34.614  1.00 29.33           C  
ANISOU   82  C   LYS A   9     4084   3218   3841   -161    645     65       C  
ATOM     83  O   LYS A   9      25.925  21.710  34.936  1.00 30.66           O  
ANISOU   83  O   LYS A   9     4248   3377   4023   -205    696     68       O  
ATOM     84  CB  LYS A   9      28.759  20.545  35.230  1.00 27.14           C  
ANISOU   84  CB  LYS A   9     3927   2836   3549   -112    622     72       C  
ATOM     85  CG  LYS A   9      29.223  20.300  33.794  1.00 29.47           C  
ANISOU   85  CG  LYS A   9     4164   3158   3874   -134    571     19       C  
ATOM     86  CD  LYS A   9      29.791  18.914  33.599  1.00 32.91           C  
ANISOU   86  CD  LYS A   9     4639   3542   4325   -132    533     -9       C  
ATOM     87  CE  LYS A   9      29.630  18.497  32.160  1.00 40.01           C  
ANISOU   87  CE  LYS A   9     5442   4482   5278   -164    496    -55       C  
ATOM     88  NZ  LYS A   9      30.266  17.179  31.893  1.00 49.08           N1+
ANISOU   88  NZ  LYS A   9     6609   5594   6445   -153    427    -98       N1+
ATOM     89  N   ILE A  10      27.117  23.084  33.594  1.00 24.62           N  
ANISOU   89  N   ILE A  10     3441   2669   3247   -159    606     34       N  
ATOM     90  CA  ILE A  10      25.958  23.381  32.755  1.00 25.93           C  
ANISOU   90  CA  ILE A  10     3551   2872   3427   -186    613     -8       C  
ATOM     91  C   ILE A  10      26.073  22.812  31.352  1.00 31.74           C  
ANISOU   91  C   ILE A  10     4243   3616   4201   -195    602    -49       C  
ATOM     92  O   ILE A  10      25.067  22.703  30.656  1.00 34.16           O  
ANISOU   92  O   ILE A  10     4501   3946   4533   -201    619   -103       O  
ATOM     93  CB  ILE A  10      25.418  24.836  32.872  1.00 29.03           C  
ANISOU   93  CB  ILE A  10     3931   3318   3782   -166    577    -21       C  
ATOM     94  CG1 ILE A  10      26.517  25.860  32.540  1.00 28.60           C  
ANISOU   94  CG1 ILE A  10     3892   3270   3706   -136    525      1       C  
ATOM     95  CG2 ILE A  10      24.840  25.047  34.284  1.00 30.26           C  
ANISOU   95  CG2 ILE A  10     4093   3489   3914   -161    591     -2       C  
ATOM     96  CD1 ILE A  10      26.112  27.370  32.470  1.00 27.90           C  
ANISOU   96  CD1 ILE A  10     3801   3215   3582   -114    468     -9       C  
ATOM     97  N   GLY A  11      27.274  22.384  30.970  1.00 26.44           N  
ANISOU   97  N   GLY A  11     3579   2935   3532   -186    570    -41       N  
ATOM     98  CA  GLY A  11      27.462  21.757  29.670  1.00 26.87           C  
ANISOU   98  CA  GLY A  11     3571   3015   3621   -185    545    -84       C  
ATOM     99  C   GLY A  11      28.891  21.470  29.288  1.00 28.15           C  
ANISOU   99  C   GLY A  11     3734   3195   3766   -177    490    -94       C  
ATOM    100  O   GLY A  11      29.829  21.740  30.044  1.00 23.77           O  
ANISOU  100  O   GLY A  11     3236   2624   3171   -168    477    -81       O  
ATOM    101  N   GLU A  12      29.036  20.876  28.105  1.00 26.63           N  
ANISOU  101  N   GLU A  12     3466   3048   3605   -171    455   -138       N  
ATOM    102  CA  GLU A  12      30.304  20.534  27.480  1.00 25.67           C  
ANISOU  102  CA  GLU A  12     3313   2979   3463   -168    387   -177       C  
ATOM    103  C   GLU A  12      30.306  21.308  26.186  1.00 27.96           C  
ANISOU  103  C   GLU A  12     3538   3353   3732   -162    377   -190       C  
ATOM    104  O   GLU A  12      29.473  21.065  25.306  1.00 27.37           O  
ANISOU  104  O   GLU A  12     3390   3310   3700   -134    383   -213       O  
ATOM    105  CB  GLU A  12      30.414  19.021  27.219  1.00 27.56           C  
ANISOU  105  CB  GLU A  12     3504   3209   3759   -157    335   -224       C  
ATOM    106  CG  GLU A  12      30.437  18.187  28.492  1.00 36.88           C  
ANISOU  106  CG  GLU A  12     4777   4288   4948   -161    343   -204       C  
ATOM    107  CD  GLU A  12      29.830  16.804  28.380  1.00 59.05           C  
ANISOU  107  CD  GLU A  12     7553   7044   7839   -163    329   -221       C  
ATOM    108  OE1 GLU A  12      29.615  16.327  27.241  1.00 43.19           O  
ANISOU  108  OE1 GLU A  12     5426   5093   5891   -147    287   -272       O  
ATOM    109  OE2 GLU A  12      29.578  16.191  29.442  1.00 52.49           O1-
ANISOU  109  OE2 GLU A  12     6815   6113   7014   -178    359   -185       O1-
ATOM    110  N   GLY A  13      31.181  22.304  26.109  1.00 21.44           N  
ANISOU  110  N   GLY A  13     2746   2559   2841   -184    372   -177       N  
ATOM    111  CA  GLY A  13      31.292  23.140  24.931  1.00 21.89           C  
ANISOU  111  CA  GLY A  13     2770   2688   2859   -189    371   -173       C  
ATOM    112  C   GLY A  13      32.207  22.527  23.900  1.00 24.38           C  
ANISOU  112  C   GLY A  13     2997   3105   3161   -194    312   -230       C  
ATOM    113  O   GLY A  13      32.657  21.384  24.045  1.00 24.33           O  
ANISOU  113  O   GLY A  13     2946   3113   3184   -185    256   -285       O  
ATOM    114  N   THR A  14      32.479  23.280  22.853  1.00 22.94           N  
ANISOU  114  N   THR A  14     2791   2997   2929   -207    315   -221       N  
ATOM    115  CA  THR A  14      33.366  22.830  21.803  1.00 22.15           C  
ANISOU  115  CA  THR A  14     2593   3023   2801   -217    258   -279       C  
ATOM    116  C   THR A  14      34.796  22.712  22.350  1.00 21.75           C  
ANISOU  116  C   THR A  14     2559   3000   2703   -276    224   -338       C  
ATOM    117  O   THR A  14      35.519  21.763  22.029  1.00 20.97           O  
ANISOU  117  O   THR A  14     2378   2987   2601   -272    143   -427       O  
ATOM    118  CB  THR A  14      33.340  23.836  20.637  1.00 34.96           C  
ANISOU  118  CB  THR A  14     4211   4712   4359   -225    288   -241       C  
ATOM    119  CG2 THR A  14      34.036  23.313  19.401  1.00 33.55           C  
ANISOU  119  CG2 THR A  14     3906   4690   4151   -221    229   -299       C  
ATOM    120  OG1 THR A  14      31.990  24.191  20.327  1.00 38.98           O  
ANISOU  120  OG1 THR A  14     4743   5174   4893   -156    324   -202       O  
ATOM    121  N   TYR A  15      35.194  23.662  23.207  1.00 19.28           N  
ANISOU  121  N   TYR A  15     2348   2620   2357   -318    277   -309       N  
ATOM    122  CA  TYR A  15      36.575  23.766  23.678  1.00 18.81           C  
ANISOU  122  CA  TYR A  15     2305   2592   2248   -365    261   -390       C  
ATOM    123  C   TYR A  15      36.851  23.304  25.075  1.00 19.75           C  
ANISOU  123  C   TYR A  15     2487   2628   2389   -330    249   -432       C  
ATOM    124  O   TYR A  15      38.020  23.204  25.461  1.00 20.60           O  
ANISOU  124  O   TYR A  15     2602   2770   2455   -343    222   -538       O  
ATOM    125  CB  TYR A  15      37.088  25.208  23.528  1.00 20.88           C  
ANISOU  125  CB  TYR A  15     2620   2855   2458   -435    328   -356       C  
ATOM    126  CG  TYR A  15      36.803  25.805  22.172  1.00 23.11           C  
ANISOU  126  CG  TYR A  15     2876   3205   2701   -468    350   -298       C  
ATOM    127  CD1 TYR A  15      37.497  25.383  21.043  1.00 25.56           C  
ANISOU  127  CD1 TYR A  15     3087   3662   2961   -501    310   -361       C  
ATOM    128  CD2 TYR A  15      35.805  26.759  22.008  1.00 25.68           C  
ANISOU  128  CD2 TYR A  15     3272   3454   3030   -453    401   -188       C  
ATOM    129  CE1 TYR A  15      37.207  25.897  19.783  1.00 28.27           C  
ANISOU  129  CE1 TYR A  15     3408   4072   3259   -514    333   -301       C  
ATOM    130  CE2 TYR A  15      35.520  27.297  20.754  1.00 27.94           C  
ANISOU  130  CE2 TYR A  15     3556   3793   3267   -462    418   -137       C  
ATOM    131  CZ  TYR A  15      36.217  26.855  19.645  1.00 34.26           C  
ANISOU  131  CZ  TYR A  15     4261   4737   4019   -490    391   -187       C  
ATOM    132  OH  TYR A  15      35.945  27.394  18.413  1.00 36.34           O  
ANISOU  132  OH  TYR A  15     4527   5057   4223   -487    413   -131       O  
ATOM    133  N   GLY A  16      35.812  23.187  25.884  1.00 17.85           N  
ANISOU  133  N   GLY A  16     2299   2281   2201   -285    280   -358       N  
ATOM    134  CA  GLY A  16      35.996  22.797  27.271  1.00 18.09           C  
ANISOU  134  CA  GLY A  16     2401   2228   2243   -241    279   -381       C  
ATOM    135  C   GLY A  16      34.705  22.819  28.042  1.00 20.59           C  
ANISOU  135  C   GLY A  16     2766   2447   2610   -209    326   -284       C  
ATOM    136  O   GLY A  16      33.640  23.086  27.483  1.00 19.73           O  
ANISOU  136  O   GLY A  16     2633   2336   2530   -217    352   -220       O  
ATOM    137  N   VAL A  17      34.788  22.477  29.314  1.00 20.06           N  
ANISOU  137  N   VAL A  17     2767   2309   2548   -164    332   -290       N  
ATOM    138  CA  VAL A  17      33.616  22.412  30.184  1.00 19.81           C  
ANISOU  138  CA  VAL A  17     2778   2196   2552   -140    378   -208       C  
ATOM    139  C   VAL A  17      33.049  23.814  30.455  1.00 20.23           C  
ANISOU  139  C   VAL A  17     2841   2239   2605   -147    427   -143       C  
ATOM    140  O   VAL A  17      33.784  24.806  30.431  1.00 18.81           O  
ANISOU  140  O   VAL A  17     2664   2082   2402   -155    431   -160       O  
ATOM    141  CB  VAL A  17      33.972  21.624  31.473  1.00 24.70           C  
ANISOU  141  CB  VAL A  17     3477   2749   3161    -83    369   -231       C  
ATOM    142  CG1 VAL A  17      34.974  22.384  32.354  1.00 25.60           C  
ANISOU  142  CG1 VAL A  17     3631   2860   3235    -32    377   -280       C  
ATOM    143  CG2 VAL A  17      32.728  21.230  32.265  1.00 25.23           C  
ANISOU  143  CG2 VAL A  17     3582   2743   3260    -75    417   -148       C  
ATOM    144  N   VAL A  18      31.733  23.875  30.692  1.00 17.26           N  
ANISOU  144  N   VAL A  18     2467   1832   2257   -146    457    -83       N  
ATOM    145  CA  VAL A  18      31.029  25.123  31.011  1.00 16.28           C  
ANISOU  145  CA  VAL A  18     2352   1705   2130   -143    476    -37       C  
ATOM    146  C   VAL A  18      30.378  24.959  32.384  1.00 17.07           C  
ANISOU  146  C   VAL A  18     2482   1764   2239   -108    500     -6       C  
ATOM    147  O   VAL A  18      29.659  23.975  32.634  1.00 17.26           O  
ANISOU  147  O   VAL A  18     2513   1764   2282   -117    523      3       O  
ATOM    148  CB  VAL A  18      29.962  25.500  29.961  1.00 19.84           C  
ANISOU  148  CB  VAL A  18     2772   2182   2584   -165    477    -24       C  
ATOM    149  CG1 VAL A  18      29.338  26.852  30.298  1.00 19.82           C  
ANISOU  149  CG1 VAL A  18     2791   2176   2563   -154    468      4       C  
ATOM    150  CG2 VAL A  18      30.527  25.512  28.543  1.00 20.16           C  
ANISOU  150  CG2 VAL A  18     2777   2272   2609   -190    458    -47       C  
ATOM    151  N   TYR A  19      30.636  25.897  33.285  1.00 16.09           N  
ANISOU  151  N   TYR A  19     1894   1692   2528    206    208      6       N  
ATOM    152  CA  TYR A  19      30.035  25.870  34.616  1.00 16.09           C  
ANISOU  152  CA  TYR A  19     2004   1656   2453    244    197    122       C  
ATOM    153  C   TYR A  19      29.222  27.110  34.846  1.00 17.16           C  
ANISOU  153  C   TYR A  19     2185   1908   2427    231    155    107       C  
ATOM    154  O   TYR A  19      29.541  28.181  34.340  1.00 16.00           O  
ANISOU  154  O   TYR A  19     2011   1836   2232    232     91     75       O  
ATOM    155  CB  TYR A  19      31.117  25.893  35.712  1.00 20.32           C  
ANISOU  155  CB  TYR A  19     2587   2151   2981    326     95    256       C  
ATOM    156  CG  TYR A  19      32.032  24.695  35.737  1.00 28.12           C  
ANISOU  156  CG  TYR A  19     3531   3000   4154    372    106    310       C  
ATOM    157  CD1 TYR A  19      31.570  23.452  36.150  1.00 31.80           C  
ANISOU  157  CD1 TYR A  19     4017   3327   4740    376    199    393       C  
ATOM    158  CD2 TYR A  19      33.373  24.812  35.387  1.00 30.34           C  
ANISOU  158  CD2 TYR A  19     3745   3273   4512    414     29    275       C  
ATOM    159  CE1 TYR A  19      32.416  22.338  36.179  1.00 33.70           C  
ANISOU  159  CE1 TYR A  19     4201   3401   5202    432    212    456       C  
ATOM    160  CE2 TYR A  19      34.234  23.716  35.444  1.00 33.08           C  
ANISOU  160  CE2 TYR A  19     4031   3476   5061    471     29    315       C  
ATOM    161  CZ  TYR A  19      33.747  22.479  35.829  1.00 42.65           C  
ANISOU  161  CZ  TYR A  19     5254   4530   6419    486    118    414       C  
ATOM    162  OH  TYR A  19      34.591  21.397  35.873  1.00 48.46           O  
ANISOU  162  OH  TYR A  19     5916   5091   7405    553    120    466       O  
ATOM    163  N   LYS A  20      28.198  26.977  35.674  1.00 15.55           N  
ANISOU  163  N   LYS A  20     2045   1708   2156    214    196    132       N  
ATOM    164  CA  LYS A  20      27.501  28.111  36.253  1.00 15.03           C  
ANISOU  164  CA  LYS A  20     2014   1734   1964    207    148    114       C  
ATOM    165  C   LYS A  20      28.355  28.406  37.516  1.00 16.56           C  
ANISOU  165  C   LYS A  20     2252   1941   2098    248     62    216       C  
ATOM    166  O   LYS A  20      28.739  27.473  38.255  1.00 17.39           O  
ANISOU  166  O   LYS A  20     2396   1997   2216    267     71    327       O  
ATOM    167  CB  LYS A  20      26.062  27.744  36.641  1.00 16.98           C  
ANISOU  167  CB  LYS A  20     2293   1996   2163    152    238     60       C  
ATOM    168  CG  LYS A  20      25.318  28.966  37.186  1.00 15.89           C  
ANISOU  168  CG  LYS A  20     2160   1950   1926    138    188      1       C  
ATOM    169  CD  LYS A  20      23.875  28.624  37.466  1.00 17.80           C  
ANISOU  169  CD  LYS A  20     2418   2220   2124     74    279    -93       C  
ATOM    170  CE  LYS A  20      23.068  29.846  37.781  1.00 17.91           C  
ANISOU  170  CE  LYS A  20     2402   2316   2088     61    233   -195       C  
ATOM    171  NZ  LYS A  20      21.678  29.489  38.174  1.00 21.71           N1+
ANISOU  171  NZ  LYS A  20     2894   2835   2520    -11    321   -316       N1+
ATOM    172  N   ALA A  21      28.697  29.682  37.733  1.00 15.79           N  
ANISOU  172  N   ALA A  21     2134   1918   1949    262    -15    182       N  
ATOM    173  CA  ALA A  21      29.517  30.063  38.877  1.00 16.23           C  
ANISOU  173  CA  ALA A  21     2194   2038   1934    290    -88    233       C  
ATOM    174  C   ALA A  21      29.101  31.371  39.459  1.00 17.99           C  
ANISOU  174  C   ALA A  21     2385   2355   2094    259   -112    142       C  
ATOM    175  O   ALA A  21      28.371  32.116  38.821  1.00 16.66           O  
ANISOU  175  O   ALA A  21     2190   2169   1970    240    -93     58       O  
ATOM    176  CB  ALA A  21      30.983  30.154  38.460  1.00 17.70           C  
ANISOU  176  CB  ALA A  21     2342   2203   2182    346   -149    250       C  
ATOM    177  N   ARG A  22      29.552  31.654  40.697  1.00 17.62           N  
ANISOU  177  N   ARG A  22     2321   2423   1951    253   -154    153       N  
ATOM    178  CA AARG A  22      29.268  32.924  41.353  0.50 18.29           C  
ANISOU  178  CA AARG A  22     2337   2610   2002    209   -163     22       C  
ATOM    179  CA BARG A  22      29.263  32.921  41.354  0.50 18.34           C  
ANISOU  179  CA BARG A  22     2344   2617   2009    208   -162     23       C  
ATOM    180  C   ARG A  22      30.566  33.686  41.522  1.00 21.67           C  
ANISOU  180  C   ARG A  22     2694   3092   2446    243   -213    -21       C  
ATOM    181  O   ARG A  22      31.539  33.129  42.051  1.00 23.46           O  
ANISOU  181  O   ARG A  22     2920   3393   2602    282   -260     56       O  
ATOM    182  CB AARG A  22      28.600  32.727  42.727  0.50 20.00           C  
ANISOU  182  CB AARG A  22     2550   2976   2071    133   -146      9       C  
ATOM    183  CB BARG A  22      28.553  32.711  42.713  0.50 20.28           C  
ANISOU  183  CB BARG A  22     2589   3010   2108    131   -144      9       C  
ATOM    184  CG AARG A  22      28.273  34.064  43.403  0.50 24.49           C  
ANISOU  184  CG AARG A  22     3008   3662   2636     66   -139   -180       C  
ATOM    185  CG BARG A  22      27.142  32.166  42.552  0.50 24.69           C  
ANISOU  185  CG BARG A  22     3205   3516   2660     75    -74     -5       C  
ATOM    186  CD AARG A  22      27.474  33.925  44.676  0.50 25.35           C  
ANISOU  186  CD AARG A  22     3093   3948   2593    -44   -110   -237       C  
ATOM    187  CD BARG A  22      26.262  32.269  43.786  0.50 29.97           C  
ANISOU  187  CD BARG A  22     3853   4339   3195    -35    -41    -82       C  
ATOM    188  NE AARG A  22      26.286  33.099  44.480  0.50 26.44           N  
ANISOU  188  NE AARG A  22     3321   4016   2709    -85    -55   -197       N  
ATOM    189  NE BARG A  22      25.050  31.458  43.621  0.50 30.52           N  
ANISOU  189  NE BARG A  22     3995   4350   3250    -89     38    -79       N  
ATOM    190  CZ AARG A  22      25.162  33.509  43.902  0.50 34.32           C  
ANISOU  190  CZ AARG A  22     4307   4927   3808   -110    -10   -325       C  
ATOM    191  CZ BARG A  22      24.894  30.237  44.122  0.50 42.91           C  
ANISOU  191  CZ BARG A  22     5652   5925   4726   -123     81     63       C  
ATOM    192  NH1AARG A  22      25.054  34.754  43.449  0.50 21.92           N1+
ANISOU  192  NH1AARG A  22     2640   3303   2385    -89    -22   -468       N1+
ATOM    193  NH1BARG A  22      25.852  29.688  44.860  0.50 36.23           N1+
ANISOU  193  NH1BARG A  22     4830   5152   3785    -98     33    242       N1+
ATOM    194  NH2AARG A  22      24.139  32.679  43.771  0.50 23.54           N  
ANISOU  194  NH2AARG A  22     3015   3522   2408   -152     50   -309       N  
ATOM    195  NH2BARG A  22      23.776  29.558  43.899  0.50 22.76           N  
ANISOU  195  NH2BARG A  22     3158   3309   2183   -181    176     30       N  
ATOM    196  N   ASN A  23      30.576  34.953  41.081  1.00 19.46           N  
ANISOU  196  N   ASN A  23     2349   2774   2273    233   -199   -144       N  
ATOM    197  CA  ASN A  23      31.705  35.869  41.210  1.00 21.11           C  
ANISOU  197  CA  ASN A  23     2475   3021   2525    246   -214   -233       C  
ATOM    198  C   ASN A  23      31.606  36.368  42.650  1.00 27.46           C  
ANISOU  198  C   ASN A  23     3183   4018   3234    185   -205   -353       C  
ATOM    199  O   ASN A  23      30.633  37.034  43.010  1.00 27.39           O  
ANISOU  199  O   ASN A  23     3118   4024   3264    121   -161   -468       O  
ATOM    200  CB  ASN A  23      31.546  37.023  40.207  1.00 24.55           C  
ANISOU  200  CB  ASN A  23     2877   3316   3134    244   -178   -299       C  
ATOM    201  CG  ASN A  23      32.676  38.016  40.234  1.00 33.19           C  
ANISOU  201  CG  ASN A  23     3890   4415   4308    243   -163   -403       C  
ATOM    202  ND2 ASN A  23      33.080  38.475  39.063  1.00 27.05           N  
ANISOU  202  ND2 ASN A  23     3130   3502   3646    259   -148   -371       N  
ATOM    203  OD1 ASN A  23      33.182  38.397  41.291  1.00 28.32           O  
ANISOU  203  OD1 ASN A  23     3181   3938   3640    217   -155   -524       O  
ATOM    204  N   LYS A  24      32.557  35.991  43.491  1.00 25.46           N  
ANISOU  204  N   LYS A  24     2892   3933   2848    200   -248   -334       N  
ATOM    205  CA  LYS A  24      32.562  36.387  44.905  1.00 27.66           C  
ANISOU  205  CA  LYS A  24     3052   4469   2989    128   -243   -453       C  
ATOM    206  C   LYS A  24      32.696  37.896  45.155  1.00 33.85           C  
ANISOU  206  C   LYS A  24     3674   5297   3891     65   -176   -712       C  
ATOM    207  O   LYS A  24      32.217  38.388  46.179  1.00 35.89           O  
ANISOU  207  O   LYS A  24     3811   5739   4086    -33   -138   -869       O  
ATOM    208  CB  LYS A  24      33.646  35.620  45.668  1.00 30.22           C  
ANISOU  208  CB  LYS A  24     3358   4992   3132    175   -319   -349       C  
ATOM    209  CG  LYS A  24      33.371  34.124  45.747  1.00 39.78           C  
ANISOU  209  CG  LYS A  24     4703   6172   4241    220   -369    -89       C  
ATOM    210  CD  LYS A  24      34.567  33.371  46.297  1.00 46.31           C  
ANISOU  210  CD  LYS A  24     5508   7142   4944    304   -462     49       C  
ATOM    211  CE  LYS A  24      34.291  31.898  46.440  1.00 55.80           C  
ANISOU  211  CE  LYS A  24     6830   8282   6088    352   -500    327       C  
ATOM    212  NZ  LYS A  24      35.515  31.145  46.816  1.00 65.69           N1+
ANISOU  212  NZ  LYS A  24     8056   9625   7278    465   -603    487       N1+
ATOM    213  N   LEU A  25      33.314  38.627  44.212  1.00 30.43           N  
ANISOU  213  N   LEU A  25     3228   4690   3642    106   -148   -767       N  
ATOM    214  CA  LEU A  25      33.545  40.067  44.355  1.00 30.63           C  
ANISOU  214  CA  LEU A  25     3099   4706   3835     52    -62  -1005       C  
ATOM    215  C   LEU A  25      32.319  40.909  44.022  1.00 34.77           C  
ANISOU  215  C   LEU A  25     3591   5059   4561      8      3  -1083       C  
ATOM    216  O   LEU A  25      32.009  41.847  44.758  1.00 36.19           O  
ANISOU  216  O   LEU A  25     3605   5312   4834    -75     77  -1310       O  
ATOM    217  CB  LEU A  25      34.764  40.530  43.535  0.50 29.95           C  
ANISOU  217  CB  LEU A  25     3010   4503   3867    101    -44  -1029       C  
ATOM    218  CG  LEU A  25      36.129  39.942  43.919  0.50 34.59           C  
ANISOU  218  CG  LEU A  25     3576   5271   4294    146   -102  -1025       C  
ATOM    219  CD1 LEU A  25      37.141  40.188  42.826  0.50 33.78           C  
ANISOU  219  CD1 LEU A  25     3514   5006   4314    190    -88  -1022       C  
ATOM    220  CD2 LEU A  25      36.638  40.521  45.228  0.50 38.07           C  
ANISOU  220  CD2 LEU A  25     3817   6005   4641     82    -64  -1257       C  
ATOM    221  N   THR A  26      31.638  40.588  42.916  1.00 29.42           N  
ANISOU  221  N   THR A  26     3047   4168   3962     63    -22   -915       N  
ATOM    222  CA  THR A  26      30.468  41.346  42.457  1.00 27.97           C  
ANISOU  222  CA  THR A  26     2835   3813   3978     50     19   -956       C  
ATOM    223  C   THR A  26      29.135  40.706  42.883  1.00 30.12           C  
ANISOU  223  C   THR A  26     3143   4150   4151     15     -2   -943       C  
ATOM    224  O   THR A  26      28.102  41.377  42.849  1.00 29.86           O  
ANISOU  224  O   THR A  26     3041   4032   4274    -11     31  -1043       O  
ATOM    225  CB  THR A  26      30.495  41.480  40.932  1.00 33.44           C  
ANISOU  225  CB  THR A  26     3628   4274   4803    126      3   -785       C  
ATOM    226  CG2 THR A  26      31.773  42.161  40.409  1.00 34.13           C  
ANISOU  226  CG2 THR A  26     3689   4280   4999    141     39   -799       C  
ATOM    227  OG1 THR A  26      30.343  40.179  40.365  1.00 29.65           O  
ANISOU  227  OG1 THR A  26     3296   3810   4159    170    -63   -597       O  
ATOM    228  N   GLY A  27      29.160  39.404  43.183  1.00 24.38           N  
ANISOU  228  N   GLY A  27     2525   3546   3192     20    -52   -812       N  
ATOM    229  CA  GLY A  27      27.979  38.627  43.548  1.00 22.56           C  
ANISOU  229  CA  GLY A  27     2352   3373   2847    -23    -57   -784       C  
ATOM    230  C   GLY A  27      27.232  38.115  42.331  1.00 24.41           C  
ANISOU  230  C   GLY A  27     2704   3432   3139     40    -71   -646       C  
ATOM    231  O   GLY A  27      26.228  37.409  42.470  1.00 23.29           O  
ANISOU  231  O   GLY A  27     2616   3316   2915      8    -61   -630       O  
ATOM    232  N   GLU A  28      27.706  38.452  41.128  1.00 21.68           N  
ANISOU  232  N   GLU A  28     2388   2929   2920    117    -86   -557       N  
ATOM    233  CA AGLU A  28      27.000  38.026  39.929  0.50 20.31           C  
ANISOU  233  CA AGLU A  28     2293   2642   2782    166    -98   -443       C  
ATOM    234  CA BGLU A  28      27.028  38.034  39.905  0.50 19.86           C  
ANISOU  234  CA BGLU A  28     2236   2583   2726    167    -99   -440       C  
ATOM    235  C   GLU A  28      27.184  36.538  39.605  1.00 20.56           C  
ANISOU  235  C   GLU A  28     2442   2704   2666    183   -111   -305       C  
ATOM    236  O   GLU A  28      28.213  35.947  39.930  1.00 20.43           O  
ANISOU  236  O   GLU A  28     2458   2737   2567    194   -131   -243       O  
ATOM    237  CB AGLU A  28      27.320  38.947  38.729  0.50 22.08           C  
ANISOU  237  CB AGLU A  28     2492   2719   3177    222   -107   -384       C  
ATOM    238  CB BGLU A  28      27.507  38.891  38.704  0.50 21.17           C  
ANISOU  238  CB BGLU A  28     2384   2607   3052    224   -108   -373       C  
ATOM    239  CG AGLU A  28      28.646  38.671  38.051  0.50 26.50           C  
ANISOU  239  CG AGLU A  28     3105   3258   3708    251   -124   -278       C  
ATOM    240  CG BGLU A  28      26.663  38.819  37.426  0.50 21.51           C  
ANISOU  240  CG BGLU A  28     2457   2573   3143    269   -125   -271       C  
ATOM    241  CD AGLU A  28      29.191  39.742  37.129  0.50 40.66           C  
ANISOU  241  CD AGLU A  28     4863   4929   5656    275   -115   -235       C  
ATOM    242  CD BGLU A  28      25.157  38.992  37.527  0.50 22.36           C  
ANISOU  242  CD BGLU A  28     2522   2679   3295    268   -122   -344       C  
ATOM    243  OE1AGLU A  28      28.479  40.158  36.187  0.50 35.60           O  
ANISOU  243  OE1AGLU A  28     4217   4207   5101    303   -124   -152       O  
ATOM    244  OE1BGLU A  28      24.638  40.043  37.086  0.50 20.67           O  
ANISOU  244  OE1BGLU A  28     2231   2368   3255    306   -133   -349       O  
ATOM    245  OE2AGLU A  28      30.373  40.107  37.307  0.50 24.19           O1-
ANISOU  245  OE2AGLU A  28     2756   2842   3594    263    -99   -274       O1-
ATOM    246  OE2BGLU A  28      24.488  38.011  37.906  0.50 12.98           O1-
ANISOU  246  OE2BGLU A  28     1379   1576   1977    235   -107   -379       O1-
ATOM    247  N   VAL A  29      26.165  35.953  38.997  1.00 17.47           N  
ANISOU  247  N   VAL A  29     2092   2283   2261    186    -94   -275       N  
ATOM    248  CA AVAL A  29      26.134  34.581  38.526  0.50 15.92           C  
ANISOU  248  CA AVAL A  29     1981   2087   1983    194    -76   -178       C  
ATOM    249  CA BVAL A  29      26.202  34.568  38.514  0.50 16.55           C  
ANISOU  249  CA BVAL A  29     2061   2164   2061    195    -77   -174       C  
ATOM    250  C   VAL A  29      26.599  34.648  37.058  1.00 16.85           C  
ANISOU  250  C   VAL A  29     2095   2138   2168    241    -92   -102       C  
ATOM    251  O   VAL A  29      26.091  35.508  36.309  1.00 17.21           O  
ANISOU  251  O   VAL A  29     2093   2154   2293    261   -105   -113       O  
ATOM    252  CB AVAL A  29      24.676  34.096  38.689  0.50 19.22           C  
ANISOU  252  CB AVAL A  29     2411   2532   2359    150    -26   -247       C  
ATOM    253  CB BVAL A  29      24.949  33.674  38.766  0.50 21.24           C  
ANISOU  253  CB BVAL A  29     2694   2791   2587    149    -20   -210       C  
ATOM    254  CG1AVAL A  29      24.386  32.909  37.797  0.50 18.25           C  
ANISOU  254  CG1AVAL A  29     2337   2384   2214    157     21   -191       C  
ATOM    255  CG1BVAL A  29      24.719  33.444  40.253  0.50 21.84           C  
ANISOU  255  CG1BVAL A  29     2783   2960   2556     79     -2   -254       C  
ATOM    256  CG2AVAL A  29      24.362  33.772  40.151  0.50 19.80           C  
ANISOU  256  CG2AVAL A  29     2500   2697   2324     75      0   -301       C  
ATOM    257  CG2BVAL A  29      23.687  34.209  38.099  0.50 20.89           C  
ANISOU  257  CG2BVAL A  29     2599   2734   2605    153     -7   -299       C  
ATOM    258  N   VAL A  30      27.538  33.799  36.665  1.00 15.50           N  
ANISOU  258  N   VAL A  30     1960   1956   1974    253    -93    -28       N  
ATOM    259  CA  VAL A  30      28.119  33.809  35.328  1.00 14.60           C  
ANISOU  259  CA  VAL A  30     1827   1817   1904    267   -102     19       C  
ATOM    260  C   VAL A  30      28.194  32.414  34.741  1.00 15.53           C  
ANISOU  260  C   VAL A  30     1960   1938   2004    252    -58     39       C  
ATOM    261  O   VAL A  30      28.018  31.419  35.453  1.00 15.14           O  
ANISOU  261  O   VAL A  30     1949   1872   1930    244    -23     46       O  
ATOM    262  CB  VAL A  30      29.571  34.387  35.417  1.00 16.55           C  
ANISOU  262  CB  VAL A  30     2062   2042   2185    283   -142     33       C  
ATOM    263  CG1 VAL A  30      29.569  35.803  35.997  1.00 17.35           C  
ANISOU  263  CG1 VAL A  30     2122   2126   2343    287   -157    -18       C  
ATOM    264  CG2 VAL A  30      30.499  33.470  36.247  1.00 17.02           C  
ANISOU  264  CG2 VAL A  30     2149   2116   2201    297   -156     49       C  
ATOM    265  N   ALA A  31      28.504  32.348  33.445  1.00 13.98           N  
ANISOU  265  N   ALA A  31     1719   1763   1831    236    -52     47       N  
ATOM    266  CA  ALA A  31      28.857  31.101  32.771  1.00 14.60           C  
ANISOU  266  CA  ALA A  31     1769   1847   1933    205     -1     25       C  
ATOM    267  C   ALA A  31      30.390  31.133  32.630  1.00 17.05           C  
ANISOU  267  C   ALA A  31     2068   2125   2287    211    -41     38       C  
ATOM    268  O   ALA A  31      30.960  32.082  32.074  1.00 18.99           O  
ANISOU  268  O   ALA A  31     2291   2395   2528    200    -79     48       O  
ATOM    269  CB  ALA A  31      28.188  31.032  31.409  1.00 16.24           C  
ANISOU  269  CB  ALA A  31     1898   2158   2116    159     38    -15       C  
ATOM    270  N   LEU A  32      31.064  30.137  33.164  1.00 14.54           N  
ANISOU  270  N   LEU A  32     1761   1743   2020    231    -33     42       N  
ATOM    271  CA ALEU A  32      32.507  30.106  33.104  0.50 14.28           C  
ANISOU  271  CA ALEU A  32     1704   1685   2039    246    -78     30       C  
ATOM    272  CA BLEU A  32      32.534  30.038  33.127  0.50 15.29           C  
ANISOU  272  CA BLEU A  32     1830   1808   2170    248    -77     30       C  
ATOM    273  C   LEU A  32      32.924  28.983  32.132  1.00 16.24           C  
ANISOU  273  C   LEU A  32     1869   1915   2387    201    -23    -42       C  
ATOM    274  O   LEU A  32      32.531  27.835  32.304  1.00 15.96           O  
ANISOU  274  O   LEU A  32     1821   1815   2428    204     38    -46       O  
ATOM    275  CB ALEU A  32      33.000  29.898  34.554  0.50 15.90           C  
ANISOU  275  CB ALEU A  32     1959   1850   2231    318   -128     93       C  
ATOM    276  CB BLEU A  32      33.085  29.573  34.495  0.50 17.48           C  
ANISOU  276  CB BLEU A  32     2153   2034   2455    319   -121     94       C  
ATOM    277  CG ALEU A  32      34.490  29.785  34.806  0.50 18.96           C  
ANISOU  277  CG ALEU A  32     2315   2223   2665    361   -190     79       C  
ATOM    278  CG BLEU A  32      33.318  30.586  35.596  0.50 21.48           C  
ANISOU  278  CG BLEU A  32     2695   2593   2875    356   -184    119       C  
ATOM    279  CD1ALEU A  32      35.207  31.095  34.494  0.50 18.60           C  
ANISOU  279  CD1ALEU A  32     2248   2232   2586    340   -225     12       C  
ATOM    280  CD1BLEU A  32      34.158  29.968  36.676  0.50 21.33           C  
ANISOU  280  CD1BLEU A  32     2681   2574   2849    423   -238    180       C  
ATOM    281  CD2ALEU A  32      34.751  29.378  36.242  0.50 21.51           C  
ANISOU  281  CD2ALEU A  32     2674   2550   2949    436   -240    172       C  
ATOM    282  CD2BLEU A  32      34.032  31.827  35.093  0.50 20.85           C  
ANISOU  282  CD2BLEU A  32     2581   2546   2795    337   -212     52       C  
ATOM    283  N   LYS A  33      33.707  29.326  31.113  1.00 14.37           N  
ANISOU  283  N   LYS A  33     1562   1733   2163    144    -32   -114       N  
ATOM    284  CA  LYS A  33      34.121  28.371  30.109  1.00 15.54           C  
ANISOU  284  CA  LYS A  33     1597   1898   2409     72     28   -230       C  
ATOM    285  C   LYS A  33      35.610  28.113  30.173  1.00 19.76           C  
ANISOU  285  C   LYS A  33     2086   2378   3044     85    -15   -294       C  
ATOM    286  O   LYS A  33      36.408  29.059  30.076  1.00 20.55           O  
ANISOU  286  O   LYS A  33     2200   2522   3088     75    -71   -307       O  
ATOM    287  CB  LYS A  33      33.715  28.844  28.697  1.00 16.82           C  
ANISOU  287  CB  LYS A  33     1678   2226   2485    -41     67   -290       C  
ATOM    288  CG  LYS A  33      32.230  29.157  28.566  1.00 18.83           C  
ANISOU  288  CG  LYS A  33     1958   2559   2639    -41     95   -234       C  
ATOM    289  CD  LYS A  33      31.714  29.061  27.128  1.00 19.20           C  
ANISOU  289  CD  LYS A  33     1876   2806   2614   -153    154   -313       C  
ATOM    290  CE  LYS A  33      30.213  29.230  27.117  1.00 19.94           C  
ANISOU  290  CE  LYS A  33     1980   2977   2620   -131    178   -275       C  
ATOM    291  NZ  LYS A  33      29.684  28.873  25.755  1.00 24.30           N1+
ANISOU  291  NZ  LYS A  33     2372   3766   3095   -242    248   -381       N1+
ATOM    292  N   LYS A  34      36.004  26.853  30.377  1.00 19.70           N  
ANISOU  292  N   LYS A  34     2018   2261   3204    113     14   -339       N  
ATOM    293  CA  LYS A  34      37.421  26.471  30.356  1.00 22.96           C  
ANISOU  293  CA  LYS A  34     2356   2619   3750    132    -30   -428       C  
ATOM    294  C   LYS A  34      37.801  26.240  28.876  1.00 28.18           C  
ANISOU  294  C   LYS A  34     2863   3374   4469    -17     38   -629       C  
ATOM    295  O   LYS A  34      37.037  25.604  28.131  1.00 27.52           O  
ANISOU  295  O   LYS A  34     2693   3334   4428   -101    139   -707       O  
ATOM    296  CB  LYS A  34      37.639  25.165  31.130  1.00 28.93           C  
ANISOU  296  CB  LYS A  34     3089   3199   4703    229    -25   -378       C  
ATOM    297  CG  LYS A  34      37.584  25.315  32.641  0.50 44.37           C  
ANISOU  297  CG  LYS A  34     5171   5101   6587    366   -109   -178       C  
ATOM    298  CD  LYS A  34      38.242  24.121  33.322  0.50 56.38           C  
ANISOU  298  CD  LYS A  34     6649   6462   8312    473   -138   -106       C  
ATOM    299  CE  LYS A  34      37.995  24.106  34.809  0.50 67.69           C  
ANISOU  299  CE  LYS A  34     8198   7878   9645    590   -209    125       C  
ATOM    300  NZ  LYS A  34      38.662  22.951  35.465  0.50 77.96           N1+
ANISOU  300  NZ  LYS A  34     9453   9025  11143    709   -251    245       N1+
ATOM    301  N   ILE A  35      38.956  26.761  28.432  1.00 25.54           N  
ANISOU  301  N   ILE A  35     2479   3099   4125    -67     -6   -738       N  
ATOM    302  CA  ILE A  35      39.383  26.585  27.031  1.00 26.84           C  
ANISOU  302  CA  ILE A  35     2486   3393   4320   -237     59   -945       C  
ATOM    303  C   ILE A  35      40.549  25.627  26.983  1.00 35.21           C  
ANISOU  303  C   ILE A  35     3407   4353   5619   -235     57  -1126       C  
ATOM    304  O   ILE A  35      41.559  25.877  27.634  1.00 36.99           O  
ANISOU  304  O   ILE A  35     3665   4511   5880   -148    -32  -1125       O  
ATOM    305  CB  ILE A  35      39.713  27.924  26.300  1.00 29.75           C  
ANISOU  305  CB  ILE A  35     2883   3932   4488   -346     37   -952       C  
ATOM    306  CG1 ILE A  35      38.552  28.953  26.402  1.00 29.40           C  
ANISOU  306  CG1 ILE A  35     2969   3954   4247   -324     27   -750       C  
ATOM    307  CG2 ILE A  35      40.176  27.685  24.831  1.00 32.11           C  
ANISOU  307  CG2 ILE A  35     3003   4409   4787   -553    108  -1169       C  
ATOM    308  CD1 ILE A  35      37.234  28.549  25.666  1.00 28.89           C  
ANISOU  308  CD1 ILE A  35     2846   4010   4122   -391    104   -736       C  
ATOM    309  N   ARG A  36      40.312  24.428  26.444  1.00 33.93           N  
ANISOU  309  N   ARG A  36     3088   4150   5654   -296    155  -1268       N  
ATOM    310  N   PRO A  45      48.308  30.281  23.488  1.00 49.77           N  
ANISOU  310  N   PRO A  45     4967   6855   7087  -1035     16  -2272       N  
ATOM    311  CA  PRO A  45      48.901  31.050  22.383  1.00 49.55           C  
ANISOU  311  CA  PRO A  45     4903   7009   6916  -1288     93  -2410       C  
ATOM    312  C   PRO A  45      48.539  32.528  22.460  1.00 49.21           C  
ANISOU  312  C   PRO A  45     5047   6980   6670  -1303    118  -2168       C  
ATOM    313  O   PRO A  45      47.382  32.879  22.712  1.00 47.75           O  
ANISOU  313  O   PRO A  45     4979   6759   6403  -1213    107  -1881       O  
ATOM    314  CB  PRO A  45      48.337  30.375  21.131  1.00 52.19           C  
ANISOU  314  CB  PRO A  45     5087   7526   7215  -1487    165  -2484       C  
ATOM    315  CG  PRO A  45      48.007  28.993  21.564  1.00 57.19           C  
ANISOU  315  CG  PRO A  45     5610   8034   8085  -1352    136  -2549       C  
ATOM    316  CD  PRO A  45      47.574  29.099  23.000  1.00 51.69           C  
ANISOU  316  CD  PRO A  45     5085   7116   7438  -1064     47  -2298       C  
ATOM    317  N   SER A  46      49.544  33.388  22.246  1.00 43.68           N  
ANISOU  317  N   SER A  46     4365   6320   5913  -1421    161  -2302       N  
ATOM    318  CA  SER A  46      49.446  34.846  22.307  1.00 41.57           C  
ANISOU  318  CA  SER A  46     4254   6030   5511  -1453    212  -2119       C  
ATOM    319  C   SER A  46      48.466  35.453  21.309  1.00 42.02           C  
ANISOU  319  C   SER A  46     4368   6209   5387  -1593    267  -1856       C  
ATOM    320  O   SER A  46      47.768  36.408  21.662  1.00 39.85           O  
ANISOU  320  O   SER A  46     4236   5844   5061  -1509    273  -1582       O  
ATOM    321  CB  SER A  46      50.825  35.474  22.158  1.00 46.40           C  
ANISOU  321  CB  SER A  46     4839   6667   6123  -1585    273  -2375       C  
ATOM    322  OG  SER A  46      51.674  35.040  23.208  1.00 58.24           O  
ANISOU  322  OG  SER A  46     6288   8064   7776  -1419    206  -2590       O  
ATOM    323  N   THR A  47      48.380  34.877  20.078  1.00 36.86           N  
ANISOU  323  N   THR A  47     3583   5776   4647  -1803    305  -1944       N  
ATOM    324  CA  THR A  47      47.465  35.357  19.042  1.00 37.48           C  
ANISOU  324  CA  THR A  47     3682   6038   4521  -1945    345  -1694       C  
ATOM    325  C   THR A  47      46.020  35.227  19.513  1.00 37.49           C  
ANISOU  325  C   THR A  47     3758   5966   4519  -1748    286  -1405       C  
ATOM    326  O   THR A  47      45.231  36.144  19.296  1.00 37.26           O  
ANISOU  326  O   THR A  47     3836   5949   4372  -1738    292  -1101       O  
ATOM    327  CB  THR A  47      47.731  34.667  17.699  1.00 50.08           C  
ANISOU  327  CB  THR A  47     5079   7936   6012  -2221    399  -1901       C  
ATOM    328  CG2 THR A  47      49.014  35.157  17.032  1.00 49.31           C  
ANISOU  328  CG2 THR A  47     4934   7954   5848  -2471    478  -2124       C  
ATOM    329  OG1 THR A  47      47.783  33.252  17.894  1.00 56.67           O  
ANISOU  329  OG1 THR A  47     5750   8762   7021  -2166    371  -2156       O  
ATOM    330  N   ALA A  48      45.687  34.114  20.202  1.00 33.49           N  
ANISOU  330  N   ALA A  48     3198   5365   4160  -1587    232  -1495       N  
ATOM    331  CA  ALA A  48      44.347  33.897  20.751  1.00 32.12           C  
ANISOU  331  CA  ALA A  48     3093   5114   3997  -1404    185  -1263       C  
ATOM    332  C   ALA A  48      44.036  34.898  21.859  1.00 30.48           C  
ANISOU  332  C   ALA A  48     3070   4690   3819  -1213    146  -1047       C  
ATOM    333  O   ALA A  48      42.931  35.426  21.886  1.00 28.03           O  
ANISOU  333  O   ALA A  48     2840   4370   3438  -1146    132   -790       O  
ATOM    334  CB  ALA A  48      44.196  32.479  21.271  1.00 32.82           C  
ANISOU  334  CB  ALA A  48     3084   5128   4258  -1293    156  -1419       C  
ATOM    335  N   ILE A  49      45.000  35.187  22.753  1.00 27.64           N  
ANISOU  335  N   ILE A  49     2755   4179   3568  -1132    133  -1170       N  
ATOM    336  CA  ILE A  49      44.774  36.158  23.839  1.00 26.57           C  
ANISOU  336  CA  ILE A  49     2758   3867   3472   -973    115  -1019       C  
ATOM    337  C   ILE A  49      44.378  37.528  23.291  1.00 27.81           C  
ANISOU  337  C   ILE A  49     3003   4027   3538  -1055    172   -797       C  
ATOM    338  O   ILE A  49      43.404  38.112  23.783  1.00 25.11           O  
ANISOU  338  O   ILE A  49     2745   3584   3210   -934    153   -577       O  
ATOM    339  CB  ILE A  49      45.996  36.249  24.802  1.00 29.38           C  
ANISOU  339  CB  ILE A  49     3107   4120   3936   -900    104  -1235       C  
ATOM    340  CG1 ILE A  49      46.425  34.860  25.352  1.00 31.58           C  
ANISOU  340  CG1 ILE A  49     3289   4384   4328   -799     31  -1418       C  
ATOM    341  CG2 ILE A  49      45.804  37.308  25.915  1.00 30.14           C  
ANISOU  341  CG2 ILE A  49     3308   4073   4070   -765    108  -1127       C  
ATOM    342  CD1 ILE A  49      45.436  34.127  26.332  1.00 41.75           C  
ANISOU  342  CD1 ILE A  49     4613   5580   5670   -596    -42  -1268       C  
ATOM    343  N   ARG A  50      45.105  38.017  22.265  1.00 28.45           N  
ANISOU  343  N   ARG A  50     3055   4218   3536  -1263    243   -850       N  
ATOM    344  CA AARG A  50      44.833  39.314  21.649  0.50 29.89           C  
ANISOU  344  CA AARG A  50     3318   4394   3645  -1356    306   -610       C  
ATOM    345  CA BARG A  50      44.836  39.315  21.635  0.50 30.17           C  
ANISOU  345  CA BARG A  50     3353   4431   3678  -1358    306   -610       C  
ATOM    346  C   ARG A  50      43.444  39.329  20.996  1.00 33.87           C  
ANISOU  346  C   ARG A  50     3829   5004   4036  -1343    268   -313       C  
ATOM    347  O   ARG A  50      42.669  40.261  21.242  1.00 33.67           O  
ANISOU  347  O   ARG A  50     3892   4855   4045  -1249    265    -52       O  
ATOM    348  CB AARG A  50      45.942  39.696  20.653  0.50 30.80           C  
ANISOU  348  CB AARG A  50     3394   4633   3674  -1607    395   -735       C  
ATOM    349  CB BARG A  50      45.930  39.667  20.605  0.50 32.38           C  
ANISOU  349  CB BARG A  50     3591   4844   3868  -1613    395   -734       C  
ATOM    350  CG AARG A  50      47.335  39.689  21.287  0.50 30.90           C  
ANISOU  350  CG AARG A  50     3384   4557   3799  -1618    435  -1066       C  
ATOM    351  CG BARG A  50      45.655  40.912  19.746  0.50 41.25           C  
ANISOU  351  CG BARG A  50     4789   5991   4894  -1744    466   -440       C  
ATOM    352  CD AARG A  50      48.428  40.245  20.400  0.50 31.21           C  
ANISOU  352  CD AARG A  50     3402   4692   3766  -1873    543  -1201       C  
ATOM    353  CD BARG A  50      46.055  42.222  20.406  0.50 41.53           C  
ANISOU  353  CD BARG A  50     4933   5770   5076  -1694    549   -379       C  
ATOM    354  NE AARG A  50      49.748  40.084  21.018  0.50 32.77           N  
ANISOU  354  NE AARG A  50     3549   4830   4070  -1873    571  -1569       N  
ATOM    355  NE BARG A  50      45.735  43.368  19.551  0.50 39.93           N  
ANISOU  355  NE BARG A  50     4799   5560   4815  -1810    619    -55       N  
ATOM    356  CZ AARG A  50      50.690  39.253  20.577  0.50 45.86           C  
ANISOU  356  CZ AARG A  50     5078   6633   5713  -2005    570  -1896       C  
ATOM    357  CZ BARG A  50      45.171  44.495  19.975  0.50 50.37           C  
ANISOU  357  CZ BARG A  50     6212   6648   6280  -1699    655    200       C  
ATOM    358  NH1AARG A  50      50.467  38.488  19.514  0.50 40.03           N1+
ANISOU  358  NH1AARG A  50     4235   6111   4862  -2164    555  -1921       N1+
ATOM    359  NH1BARG A  50      44.855  44.648  21.256  0.50 34.32           N1+
ANISOU  359  NH1BARG A  50     4204   4397   4441  -1485    633    136       N1+
ATOM    360  NH2AARG A  50      51.865  39.184  21.192  0.50 30.37           N  
ANISOU  360  NH2AARG A  50     3066   4615   3857  -1983    586  -2224       N  
ATOM    361  NH2BARG A  50      44.916  45.477  19.123  0.50 35.79           N  
ANISOU  361  NH2BARG A  50     4418   4788   4394  -1805    716    521       N  
ATOM    362  N   GLU A  51      43.119  38.271  20.209  1.00 28.75           N  
ANISOU  362  N   GLU A  51     2572   3409   4944   -252   -190    790       N  
ATOM    363  CA AGLU A  51      41.831  38.147  19.517  0.50 27.42           C  
ANISOU  363  CA AGLU A  51     2552   3279   4586   -185   -104    707       C  
ATOM    364  CA BGLU A  51      41.832  38.118  19.520  0.50 27.43           C  
ANISOU  364  CA BGLU A  51     2554   3282   4587   -183   -104    706       C  
ATOM    365  C   GLU A  51      40.664  38.093  20.511  1.00 27.95           C  
ANISOU  365  C   GLU A  51     2754   3349   4517   -228   -221    551       C  
ATOM    366  O   GLU A  51      39.648  38.779  20.313  1.00 26.63           O  
ANISOU  366  O   GLU A  51     2678   3169   4270   -232   -215    488       O  
ATOM    367  CB AGLU A  51      41.820  36.918  18.584  0.50 28.97           C  
ANISOU  367  CB AGLU A  51     2782   3542   4683    -61     36    736       C  
ATOM    368  CB BGLU A  51      41.830  36.821  18.697  0.50 28.97           C  
ANISOU  368  CB BGLU A  51     2782   3544   4680    -64     25    729       C  
ATOM    369  CG AGLU A  51      42.691  37.056  17.341  0.50 41.57           C  
ANISOU  369  CG AGLU A  51     4290   5139   6366     22    199    890       C  
ATOM    370  CG BGLU A  51      42.563  36.910  17.372  0.50 42.32           C  
ANISOU  370  CG BGLU A  51     4403   5240   6435     28    195    872       C  
ATOM    371  CD AGLU A  51      42.084  37.712  16.113  0.50 56.99           C  
ANISOU  371  CD AGLU A  51     6317   7090   8248     91    320    911       C  
ATOM    372  CD BGLU A  51      42.358  35.689  16.502  0.50 61.84           C  
ANISOU  372  CD BGLU A  51     6962   7768   8767    162    316    870       C  
ATOM    373  OE1AGLU A  51      41.156  38.540  16.260  0.50 38.39           O  
ANISOU  373  OE1AGLU A  51     4036   4712   5840     41    262    831       O  
ATOM    374  OE1BGLU A  51      41.196  35.424  16.121  0.50 59.08           O  
ANISOU  374  OE1BGLU A  51     6759   7439   8248    204    323    768       O  
ATOM    375  OE2AGLU A  51      42.570  37.423  14.996  0.50 56.27           O1-
ANISOU  375  OE2AGLU A  51     6211   7017   8153    205    478   1017       O1-
ATOM    376  OE2BGLU A  51      43.354  34.988  16.211  0.50 55.84           O1-
ANISOU  376  OE2BGLU A  51     6123   7024   8069    229    397    972       O1-
ATOM    377  N   ILE A  52      40.809  37.293  21.589  1.00 25.24           N  
ANISOU  377  N   ILE A  52     2422   3020   4150   -253   -320    498       N  
ATOM    378  CA  ILE A  52      39.768  37.156  22.613  1.00 25.77           C  
ANISOU  378  CA  ILE A  52     2614   3088   4090   -280   -415    367       C  
ATOM    379  C   ILE A  52      39.584  38.458  23.366  1.00 28.69           C  
ANISOU  379  C   ILE A  52     3013   3386   4501   -360   -530    326       C  
ATOM    380  O   ILE A  52      38.458  38.857  23.645  1.00 27.14           O  
ANISOU  380  O   ILE A  52     2931   3183   4197   -360   -545    239       O  
ATOM    381  CB  ILE A  52      40.036  35.933  23.551  1.00 30.59           C  
ANISOU  381  CB  ILE A  52     3234   3728   4661   -272   -479    335       C  
ATOM    382  CG1 ILE A  52      40.117  34.610  22.768  1.00 32.43           C  
ANISOU  382  CG1 ILE A  52     3460   4022   4840   -184   -363    367       C  
ATOM    383  CG2 ILE A  52      39.006  35.828  24.662  1.00 32.47           C  
ANISOU  383  CG2 ILE A  52     3600   3962   4774   -290   -564    218       C  
ATOM    384  CD1 ILE A  52      38.897  34.264  21.954  1.00 41.08           C  
ANISOU  384  CD1 ILE A  52     4662   5150   5798   -124   -271    311       C  
ATOM    385  N   SER A  53      40.695  39.150  23.662  1.00 29.26           N  
ANISOU  385  N   SER A  53     2980   3397   4740   -427   -612    394       N  
ATOM    386  CA  SER A  53      40.661  40.448  24.332  1.00 30.24           C  
ANISOU  386  CA  SER A  53     3134   3433   4923   -507   -738    359       C  
ATOM    387  C   SER A  53      39.860  41.476  23.539  1.00 34.29           C  
ANISOU  387  C   SER A  53     3698   3923   5406   -498   -658    351       C  
ATOM    388  O   SER A  53      39.066  42.208  24.136  1.00 36.46           O  
ANISOU  388  O   SER A  53     4087   4155   5610   -521   -726    265       O  
ATOM    389  CB  SER A  53      42.071  40.930  24.627  1.00 36.78           C  
ANISOU  389  CB  SER A  53     3818   4192   5965   -583   -843    451       C  
ATOM    390  OG  SER A  53      42.675  40.027  25.538  1.00 43.23           O  
ANISOU  390  OG  SER A  53     4610   5025   6789   -590   -945    439       O  
ATOM    391  N   LEU A  54      39.985  41.470  22.191  1.00 30.82           N  
ANISOU  391  N   LEU A  54     3194   3516   4999   -446   -504    440       N  
ATOM    392  CA  LEU A  54      39.227  42.344  21.293  1.00 30.71           C  
ANISOU  392  CA  LEU A  54     3230   3491   4947   -420   -412    443       C  
ATOM    393  C   LEU A  54      37.702  42.084  21.421  1.00 28.75           C  
ANISOU  393  C   LEU A  54     3134   3287   4502   -373   -394    324       C  
ATOM    394  O   LEU A  54      36.893  42.993  21.257  1.00 26.59           O  
ANISOU  394  O   LEU A  54     2932   2984   4186   -375   -385    287       O  
ATOM    395  CB  LEU A  54      39.668  42.149  19.828  1.00 32.40           C  
ANISOU  395  CB  LEU A  54     3365   3742   5204   -347   -243    562       C  
ATOM    396  CG  LEU A  54      41.041  42.707  19.445  1.00 40.94           C  
ANISOU  396  CG  LEU A  54     4283   4770   6504   -383   -219    712       C  
ATOM    397  CD1 LEU A  54      41.710  41.836  18.401  1.00 42.79           C  
ANISOU  397  CD1 LEU A  54     4438   5064   6758   -288    -61    826       C  
ATOM    398  CD2 LEU A  54      40.935  44.131  18.936  1.00 45.64           C  
ANISOU  398  CD2 LEU A  54     4868   5292   7180   -415   -192    759       C  
ATOM    399  N   LEU A  55      37.308  40.841  21.733  1.00 23.60           N  
ANISOU  399  N   LEU A  55     2526   2700   3741   -332   -388    270       N  
ATOM    400  CA  LEU A  55      35.894  40.502  21.889  1.00 21.22           C  
ANISOU  400  CA  LEU A  55     2345   2437   3282   -292   -372    174       C  
ATOM    401  C   LEU A  55      35.233  41.144  23.118  1.00 23.08           C  
ANISOU  401  C   LEU A  55     2674   2625   3469   -333   -475     87       C  
ATOM    402  O   LEU A  55      34.017  41.316  23.116  1.00 20.85           O  
ANISOU  402  O   LEU A  55     2478   2356   3086   -302   -447     30       O  
ATOM    403  CB  LEU A  55      35.681  38.968  21.862  1.00 20.70           C  
ANISOU  403  CB  LEU A  55     2293   2440   3132   -240   -337    152       C  
ATOM    404  CG  LEU A  55      36.141  38.266  20.585  1.00 25.27           C  
ANISOU  404  CG  LEU A  55     2820   3061   3719   -174   -225    224       C  
ATOM    405  CD1 LEU A  55      36.225  36.769  20.808  1.00 25.24           C  
ANISOU  405  CD1 LEU A  55     2826   3105   3661   -137   -220    205       C  
ATOM    406  CD2 LEU A  55      35.237  38.592  19.394  1.00 27.56           C  
ANISOU  406  CD2 LEU A  55     3167   3368   3936   -115   -137    220       C  
ATOM    407  N   LYS A  56      36.010  41.539  24.141  1.00 20.90           N  
ANISOU  407  N   LYS A  56     2386   2290   3266   -395   -597     81       N  
ATOM    408  CA ALYS A  56      35.460  42.184  25.340  0.50 21.36           C  
ANISOU  408  CA ALYS A  56     2559   2292   3264   -418   -701     -3       C  
ATOM    409  CA BLYS A  56      35.488  42.197  25.352  0.50 21.08           C  
ANISOU  409  CA BLYS A  56     2523   2255   3231   -420   -704     -2       C  
ATOM    410  C   LYS A  56      34.826  43.539  25.024  1.00 23.53           C  
ANISOU  410  C   LYS A  56     2891   2511   3539   -425   -686    -18       C  
ATOM    411  O   LYS A  56      34.014  44.030  25.805  1.00 25.15           O  
ANISOU  411  O   LYS A  56     3217   2683   3657   -412   -727    -91       O  
ATOM    412  CB ALYS A  56      36.524  42.339  26.430  0.50 25.14           C  
ANISOU  412  CB ALYS A  56     3024   2706   3821   -479   -857     -7       C  
ATOM    413  CB BLYS A  56      36.598  42.438  26.391  0.50 24.24           C  
ANISOU  413  CB BLYS A  56     2903   2586   3721   -485   -861     -2       C  
ATOM    414  CG ALYS A  56      36.307  41.411  27.627  0.50 34.63           C  
ANISOU  414  CG ALYS A  56     4308   3933   4916   -453   -922    -72       C  
ATOM    415  CG BLYS A  56      37.234  41.169  26.971  0.50 25.30           C  
ANISOU  415  CG BLYS A  56     2998   2765   3849   -477   -903      5       C  
ATOM    416  CD ALYS A  56      37.446  41.509  28.662  0.50 44.83           C  
ANISOU  416  CD ALYS A  56     5586   5161   6285   -508  -1096    -73       C  
ATOM    417  CD BLYS A  56      38.201  41.491  28.120  0.50 27.62           C  
ANISOU  417  CD BLYS A  56     3295   2982   4216   -537  -1087     -8       C  
ATOM    418  CE ALYS A  56      37.456  42.778  29.491  0.50 53.27           C  
ANISOU  418  CE ALYS A  56     6761   6118   7363   -549  -1238   -129       C  
ATOM    419  CE BLYS A  56      39.572  41.920  27.660  0.50 26.36           C  
ANISOU  419  CE BLYS A  56     2975   2776   4266   -606  -1140     91       C  
ATOM    420  NZ ALYS A  56      36.345  42.823  30.475  0.50 60.84           N1+
ANISOU  420  NZ ALYS A  56     7909   7068   8138   -487  -1252   -228       N1+
ATOM    421  NZ BLYS A  56      40.435  42.311  28.809  0.50 29.92           N1+
ANISOU  421  NZ BLYS A  56     3435   3137   4796   -672  -1351     71       N1+
ATOM    422  N   GLU A  57      35.211  44.143  23.896  1.00 18.80           N  
ANISOU  422  N   GLU A  57     2210   1898   3034   -435   -618     58       N  
ATOM    423  CA AGLU A  57      34.666  45.432  23.497  0.70 19.34           C  
ANISOU  423  CA AGLU A  57     2325   1912   3111   -439   -595     55       C  
ATOM    424  CA BGLU A  57      34.720  45.440  23.428  0.30 18.52           C  
ANISOU  424  CA BGLU A  57     2214   1808   3015   -439   -591     61       C  
ATOM    425  C   GLU A  57      33.551  45.305  22.464  1.00 19.99           C  
ANISOU  425  C   GLU A  57     2436   2059   3099   -365   -463     55       C  
ATOM    426  O   GLU A  57      32.904  46.307  22.160  1.00 21.33           O  
ANISOU  426  O   GLU A  57     2658   2193   3253   -353   -437     46       O  
ATOM    427  CB AGLU A  57      35.784  46.355  22.994  0.70 22.24           C  
ANISOU  427  CB AGLU A  57     2591   2203   3656   -500   -616    145       C  
ATOM    428  CB BGLU A  57      35.843  46.190  22.696  0.30 20.75           C  
ANISOU  428  CB BGLU A  57     2379   2033   3473   -489   -583    166       C  
ATOM    429  CG AGLU A  57      36.776  46.776  24.072  0.70 33.79           C  
ANISOU  429  CG AGLU A  57     4036   3572   5232   -586   -784    138       C  
ATOM    430  CG BGLU A  57      37.037  46.549  23.564  0.30 28.51           C  
ANISOU  430  CG BGLU A  57     3307   2929   4598   -578   -733    185       C  
ATOM    431  CD AGLU A  57      36.170  47.386  25.323  0.70 62.45           C  
ANISOU  431  CD AGLU A  57     7824   7130   8774   -599   -910     26       C  
ATOM    432  CD BGLU A  57      38.011  47.535  22.949  0.30 49.54           C  
ANISOU  432  CD BGLU A  57     5855   5509   7459   -639   -736    292       C  
ATOM    433  OE1AGLU A  57      35.727  48.556  25.261  0.70 65.88           O  
ANISOU  433  OE1AGLU A  57     8329   7489   9214   -608   -921      6       O  
ATOM    434  OE1BGLU A  57      38.473  47.298  21.809  0.30 38.85           O  
ANISOU  434  OE1BGLU A  57     4388   4198   6177   -610   -606    401       O  
ATOM    435  OE2AGLU A  57      36.110  46.682  26.358  0.70 59.39           O1-
ANISOU  435  OE2AGLU A  57     7501   6760   8304   -588   -990    -39       O1-
ATOM    436  OE2BGLU A  57      38.336  48.536  23.626  0.30 47.84           O1-
ANISOU  436  OE2BGLU A  57     5667   5180   7332   -713   -870    272       O1-
ATOM    437  N   LEU A  58      33.299  44.081  21.942  1.00 16.73           N  
ANISOU  437  N   LEU A  58     1997   1736   2622   -313   -390     62       N  
ATOM    438  CA  LEU A  58      32.276  43.812  20.929  1.00 17.45           C  
ANISOU  438  CA  LEU A  58     2117   1887   2627   -242   -289     59       C  
ATOM    439  C   LEU A  58      30.920  43.579  21.632  1.00 15.49           C  
ANISOU  439  C   LEU A  58     1962   1660   2263   -215   -305    -24       C  
ATOM    440  O   LEU A  58      30.411  42.481  21.720  1.00 16.05           O  
ANISOU  440  O   LEU A  58     2042   1788   2270   -184   -289    -51       O  
ATOM    441  CB  LEU A  58      32.744  42.603  20.076  1.00 18.80           C  
ANISOU  441  CB  LEU A  58     2226   2124   2793   -200   -222    106       C  
ATOM    442  CG  LEU A  58      31.961  42.288  18.800  1.00 22.06           C  
ANISOU  442  CG  LEU A  58     2667   2587   3129   -123   -131    115       C  
ATOM    443  CD1 LEU A  58      32.190  43.341  17.725  1.00 22.63           C  
ANISOU  443  CD1 LEU A  58     2722   2630   3246   -100    -63    185       C  
ATOM    444  CD2 LEU A  58      32.349  40.925  18.308  1.00 23.87           C  
ANISOU  444  CD2 LEU A  58     2870   2870   3329    -79    -94    134       C  
ATOM    445  N   ASN A  59      30.379  44.671  22.174  1.00 14.27           N  
ANISOU  445  N   ASN A  59     1877   1450   2096   -224   -336    -58       N  
ATOM    446  CA  ASN A  59      29.197  44.640  23.016  1.00 12.49           C  
ANISOU  446  CA  ASN A  59     1741   1229   1776   -193   -345   -123       C  
ATOM    447  C   ASN A  59      27.953  45.028  22.302  1.00 11.76           C  
ANISOU  447  C   ASN A  59     1674   1159   1634   -139   -275   -124       C  
ATOM    448  O   ASN A  59      27.888  46.066  21.643  1.00 13.25           O  
ANISOU  448  O   ASN A  59     1868   1314   1853   -134   -249    -98       O  
ATOM    449  CB  ASN A  59      29.418  45.542  24.240  1.00 13.01           C  
ANISOU  449  CB  ASN A  59     1889   1209   1844   -222   -431   -164       C  
ATOM    450  CG  ASN A  59      30.534  45.098  25.126  1.00 14.64           C  
ANISOU  450  CG  ASN A  59     2082   1390   2089   -272   -528   -174       C  
ATOM    451  ND2 ASN A  59      31.326  46.045  25.589  1.00 16.35           N  
ANISOU  451  ND2 ASN A  59     2321   1516   2376   -324   -621   -177       N  
ATOM    452  OD1 ASN A  59      30.724  43.901  25.363  1.00 15.61           O  
ANISOU  452  OD1 ASN A  59     2173   1569   2189   -264   -527   -175       O  
ATOM    453  N   HIS A  60      26.921  44.209  22.450  1.00 10.92           N  
ANISOU  453  N   HIS A  60     1581   1106   1461    -97   -246   -148       N  
ATOM    454  CA  HIS A  60      25.615  44.498  21.830  1.00 11.49           C  
ANISOU  454  CA  HIS A  60     1667   1202   1497    -44   -192   -145       C  
ATOM    455  C   HIS A  60      24.559  43.738  22.599  1.00 11.10           C  
ANISOU  455  C   HIS A  60     1637   1184   1398    -13   -180   -171       C  
ATOM    456  O   HIS A  60      24.843  42.662  23.119  1.00 11.42           O  
ANISOU  456  O   HIS A  60     1660   1249   1430    -27   -199   -181       O  
ATOM    457  CB  HIS A  60      25.656  44.039  20.350  1.00 11.38           C  
ANISOU  457  CB  HIS A  60     1596   1235   1494    -24   -156   -109       C  
ATOM    458  CG  HIS A  60      24.404  44.333  19.581  1.00 11.50           C  
ANISOU  458  CG  HIS A  60     1620   1271   1480     30   -122   -103       C  
ATOM    459  CD2 HIS A  60      24.087  45.407  18.825  1.00 12.78           C  
ANISOU  459  CD2 HIS A  60     1799   1412   1644     58    -94    -80       C  
ATOM    460  ND1 HIS A  60      23.324  43.469  19.609  1.00 11.22           N  
ANISOU  460  ND1 HIS A  60     1569   1277   1417     57   -123   -118       N  
ATOM    461  CE1 HIS A  60      22.386  44.039  18.879  1.00 12.08           C  
ANISOU  461  CE1 HIS A  60     1682   1390   1516    100   -105   -104       C  
ATOM    462  NE2 HIS A  60      22.797  45.201  18.370  1.00 12.75           N  
ANISOU  462  NE2 HIS A  60     1791   1442   1610    107    -84    -82       N  
ATOM    463  N   PRO A  61      23.296  44.221  22.653  1.00 11.97           N  
ANISOU  463  N   PRO A  61     1773   1293   1482     35   -142   -170       N  
ATOM    464  CA  PRO A  61      22.273  43.507  23.438  1.00 11.69           C  
ANISOU  464  CA  PRO A  61     1742   1283   1419     69   -116   -174       C  
ATOM    465  C   PRO A  61      21.943  42.104  22.948  1.00 12.27           C  
ANISOU  465  C   PRO A  61     1739   1412   1510     63   -117   -162       C  
ATOM    466  O   PRO A  61      21.411  41.312  23.736  1.00 13.43           O  
ANISOU  466  O   PRO A  61     1880   1572   1650     76   -102   -158       O  
ATOM    467  CB  PRO A  61      21.021  44.384  23.325  1.00 15.00           C  
ANISOU  467  CB  PRO A  61     2180   1691   1829    126    -67   -157       C  
ATOM    468  CG  PRO A  61      21.512  45.698  22.883  1.00 19.34           C  
ANISOU  468  CG  PRO A  61     2771   2193   2383    119    -75   -161       C  
ATOM    469  CD  PRO A  61      22.824  45.549  22.208  1.00 12.85           C  
ANISOU  469  CD  PRO A  61     1917   1370   1596     63   -116   -159       C  
ATOM    470  N   ASN A  62      22.274  41.771  21.700  1.00 10.43           N  
ANISOU  470  N   ASN A  62     1462   1204   1299     51   -134   -152       N  
ATOM    471  CA  ASN A  62      21.994  40.438  21.164  1.00 10.18           C  
ANISOU  471  CA  ASN A  62     1378   1211   1280     48   -152   -149       C  
ATOM    472  C   ASN A  62      23.248  39.589  21.085  1.00 11.00           C  
ANISOU  472  C   ASN A  62     1473   1324   1384     16   -177   -158       C  
ATOM    473  O   ASN A  62      23.240  38.586  20.373  1.00 11.49           O  
ANISOU  473  O   ASN A  62     1509   1408   1449     20   -196   -158       O  
ATOM    474  CB  ASN A  62      21.239  40.517  19.846  1.00 11.33           C  
ANISOU  474  CB  ASN A  62     1498   1373   1435     78   -162   -136       C  
ATOM    475  CG  ASN A  62      19.914  41.173  20.030  1.00 11.93           C  
ANISOU  475  CG  ASN A  62     1564   1443   1525    112   -140   -118       C  
ATOM    476  ND2 ASN A  62      19.011  40.513  20.754  1.00 10.83           N  
ANISOU  476  ND2 ASN A  62     1388   1310   1416    117   -130   -104       N  
ATOM    477  OD1 ASN A  62      19.694  42.288  19.553  1.00 13.00           O  
ANISOU  477  OD1 ASN A  62     1720   1565   1652    138   -123   -108       O  
ATOM    478  N   ILE A  63      24.325  39.979  21.799  1.00  9.66           N  
ANISOU  478  N   ILE A  63     1327   1130   1213    -12   -186   -164       N  
ATOM    479  CA AILE A  63      25.563  39.218  21.873  0.70  9.84           C  
ANISOU  479  CA AILE A  63     1330   1160   1248    -41   -209   -161       C  
ATOM    480  CA BILE A  63      25.567  39.208  21.875  0.30  8.91           C  
ANISOU  480  CA BILE A  63     1213   1044   1131    -41   -209   -162       C  
ATOM    481  C   ILE A  63      25.764  38.892  23.337  1.00 10.67           C  
ANISOU  481  C   ILE A  63     1463   1253   1339    -58   -230   -179       C  
ATOM    482  O   ILE A  63      25.773  39.809  24.162  1.00 10.55           O  
ANISOU  482  O   ILE A  63     1498   1201   1310    -60   -241   -193       O  
ATOM    483  CB AILE A  63      26.743  40.016  21.280  0.70 10.88           C  
ANISOU  483  CB AILE A  63     1450   1271   1412    -58   -210   -137       C  
ATOM    484  CB BILE A  63      26.802  39.951  21.299  0.30 10.89           C  
ANISOU  484  CB BILE A  63     1449   1273   1414    -60   -211   -137       C  
ATOM    485  CG1AILE A  63      26.460  40.422  19.799  0.70 11.29           C  
ANISOU  485  CG1AILE A  63     1494   1334   1461    -22   -174   -112       C  
ATOM    486  CG1BILE A  63      26.668  40.157  19.782  0.30 11.05           C  
ANISOU  486  CG1BILE A  63     1457   1309   1433    -24   -176   -110       C  
ATOM    487  CG2AILE A  63      28.088  39.291  21.436  0.70 13.27           C  
ANISOU  487  CG2AILE A  63     1718   1580   1746    -85   -230   -120       C  
ATOM    488  CG2BILE A  63      28.121  39.218  21.648  0.30 12.53           C  
ANISOU  488  CG2BILE A  63     1626   1485   1651    -89   -236   -124       C  
ATOM    489  CD1AILE A  63      26.294  39.231  18.825  0.70 12.57           C  
ANISOU  489  CD1AILE A  63     1644   1534   1598     13   -169   -110       C  
ATOM    490  CD1BILE A  63      27.744  41.012  19.196  0.30 13.40           C  
ANISOU  490  CD1BILE A  63     1736   1581   1773    -32   -155    -66       C  
ATOM    491  N   VAL A  64      25.947  37.625  23.680  1.00 10.05           N  
ANISOU  491  N   VAL A  64     1366   1196   1257    -63   -240   -181       N  
ATOM    492  CA  VAL A  64      26.211  37.275  25.075  1.00 10.26           C  
ANISOU  492  CA  VAL A  64     1429   1211   1260    -69   -260   -194       C  
ATOM    493  C   VAL A  64      27.456  38.023  25.548  1.00 11.19           C  
ANISOU  493  C   VAL A  64     1569   1294   1389    -99   -312   -200       C  
ATOM    494  O   VAL A  64      28.509  37.941  24.907  1.00 12.83           O  
ANISOU  494  O   VAL A  64     1727   1506   1643   -125   -331   -180       O  
ATOM    495  CB  VAL A  64      26.383  35.734  25.206  1.00 11.30           C  
ANISOU  495  CB  VAL A  64     1530   1369   1394    -70   -262   -187       C  
ATOM    496  CG1 VAL A  64      26.718  35.349  26.652  1.00 12.67           C  
ANISOU  496  CG1 VAL A  64     1749   1530   1535    -67   -282   -194       C  
ATOM    497  CG2 VAL A  64      25.121  34.980  24.765  1.00 11.51           C  
ANISOU  497  CG2 VAL A  64     1530   1413   1431    -50   -229   -178       C  
ATOM    498  N   LYS A  65      27.351  38.734  26.672  1.00 11.86           N  
ANISOU  498  N   LYS A  65     1730   1339   1438    -92   -339   -224       N  
ATOM    499  CA  LYS A  65      28.457  39.558  27.070  1.00 13.57           C  
ANISOU  499  CA  LYS A  65     1970   1506   1679   -128   -414   -234       C  
ATOM    500  C   LYS A  65      29.655  38.803  27.586  1.00 13.40           C  
ANISOU  500  C   LYS A  65     1924   1487   1681   -157   -479   -229       C  
ATOM    501  O   LYS A  65      29.514  37.933  28.465  1.00 14.73           O  
ANISOU  501  O   LYS A  65     2128   1670   1799   -134   -486   -240       O  
ATOM    502  CB  LYS A  65      28.005  40.584  28.109  1.00 15.93           C  
ANISOU  502  CB  LYS A  65     2385   1748   1921   -103   -440   -269       C  
ATOM    503  CG  LYS A  65      29.035  41.699  28.398  1.00 17.77           C  
ANISOU  503  CG  LYS A  65     2652   1906   2194   -148   -538   -286       C  
ATOM    504  CD  LYS A  65      28.487  42.681  29.388  1.00 20.10           C  
ANISOU  504  CD  LYS A  65     3088   2135   2415   -109   -565   -330       C  
ATOM    505  CE  LYS A  65      29.555  43.591  29.920  1.00 19.11           C  
ANISOU  505  CE  LYS A  65     3015   1919   2326   -156   -696   -357       C  
ATOM    506  NZ  LYS A  65      30.105  44.485  28.876  1.00 17.81           N1+
ANISOU  506  NZ  LYS A  65     2771   1722   2273   -216   -709   -326       N1+
ATOM    507  N   LEU A  66      30.812  39.101  27.014  1.00 14.31           N  
ANISOU  507  N   LEU A  66     1971   1588   1879   -202   -519   -200       N  
ATOM    508  CA  LEU A  66      32.076  38.554  27.501  1.00 14.43           C  
ANISOU  508  CA  LEU A  66     1947   1598   1939   -233   -593   -185       C  
ATOM    509  C   LEU A  66      32.547  39.466  28.641  1.00 18.67           C  
ANISOU  509  C   LEU A  66     2561   2060   2474   -259   -710   -219       C  
ATOM    510  O   LEU A  66      32.950  40.611  28.411  1.00 17.83           O  
ANISOU  510  O   LEU A  66     2448   1896   2431   -297   -755   -213       O  
ATOM    511  CB  LEU A  66      33.109  38.493  26.388  1.00 16.54           C  
ANISOU  511  CB  LEU A  66     2096   1878   2311   -262   -575   -123       C  
ATOM    512  CG  LEU A  66      34.493  38.001  26.795  1.00 19.71           C  
ANISOU  512  CG  LEU A  66     2431   2272   2786   -294   -649    -88       C  
ATOM    513  CD1 LEU A  66      34.440  36.600  27.472  1.00 20.60           C  
ANISOU  513  CD1 LEU A  66     2563   2427   2836   -263   -652   -104       C  
ATOM    514  CD2 LEU A  66      35.481  38.063  25.601  1.00 22.47           C  
ANISOU  514  CD2 LEU A  66     2655   2631   3252   -309   -603     -6       C  
ATOM    515  N   LEU A  67      32.417  38.976  29.873  1.00 17.06           N  
ANISOU  515  N   LEU A  67     2444   1849   2190   -231   -758   -255       N  
ATOM    516  CA  LEU A  67      32.753  39.781  31.047  1.00 18.44           C  
ANISOU  516  CA  LEU A  67     2731   1945   2332   -236   -882   -300       C  
ATOM    517  C   LEU A  67      34.236  39.866  31.293  1.00 21.40           C  
ANISOU  517  C   LEU A  67     3045   2279   2806   -299  -1018   -282       C  
ATOM    518  O   LEU A  67      34.710  40.949  31.660  1.00 21.78           O  
ANISOU  518  O   LEU A  67     3138   2243   2897   -338  -1132   -304       O  
ATOM    519  CB  LEU A  67      32.014  39.258  32.291  1.00 19.45           C  
ANISOU  519  CB  LEU A  67     2995   2076   2319   -163   -875   -340       C  
ATOM    520  CG  LEU A  67      30.484  39.188  32.187  1.00 23.23           C  
ANISOU  520  CG  LEU A  67     3524   2588   2715    -95   -737   -344       C  
ATOM    521  CD1 LEU A  67      29.896  38.391  33.335  1.00 24.03           C  
ANISOU  521  CD1 LEU A  67     3726   2703   2700    -19   -706   -354       C  
ATOM    522  CD2 LEU A  67      29.871  40.591  32.222  1.00 28.51           C  
ANISOU  522  CD2 LEU A  67     4281   3196   3355    -78   -735   -374       C  
ATOM    523  N   ASP A  68      34.966  38.756  31.145  1.00 20.07           N  
ANISOU  523  N   ASP A  68     2781   2162   2684   -309  -1017   -240       N  
ATOM    524  CA  ASP A  68      36.408  38.715  31.360  1.00 22.01           C  
ANISOU  524  CA  ASP A  68     2943   2376   3043   -364  -1143   -206       C  
ATOM    525  C   ASP A  68      37.082  37.545  30.729  1.00 23.95           C  
ANISOU  525  C   ASP A  68     3053   2692   3357   -364  -1085   -139       C  
ATOM    526  O   ASP A  68      36.441  36.534  30.446  1.00 20.03           O  
ANISOU  526  O   ASP A  68     2559   2262   2788   -315   -974   -137       O  
ATOM    527  CB  ASP A  68      36.756  38.746  32.857  1.00 25.05           C  
ANISOU  527  CB  ASP A  68     3451   2706   3363   -354  -1302   -259       C  
ATOM    528  CG  ASP A  68      37.370  40.072  33.261  1.00 37.72           C  
ANISOU  528  CG  ASP A  68     5095   4200   5038   -413  -1465   -285       C  
ATOM    529  OD1 ASP A  68      38.207  40.600  32.489  1.00 35.04           O  
ANISOU  529  OD1 ASP A  68     4616   3833   4866   -487  -1495   -227       O  
ATOM    530  OD2 ASP A  68      36.978  40.608  34.320  1.00 49.47           O1-
ANISOU  530  OD2 ASP A  68     6758   5623   6415   -379  -1557   -359       O1-
ATOM    531  N   VAL A  69      38.388  37.670  30.511  1.00 24.52           N  
ANISOU  531  N   VAL A  69     3003   2740   3575   -418  -1162    -79       N  
ATOM    532  CA  VAL A  69      39.282  36.664  29.987  1.00 25.56           C  
ANISOU  532  CA  VAL A  69     2997   2923   3791   -414  -1122     -1       C  
ATOM    533  C   VAL A  69      40.330  36.473  31.097  1.00 27.41           C  
ANISOU  533  C   VAL A  69     3220   3119   4075   -442  -1296      2       C  
ATOM    534  O   VAL A  69      40.969  37.454  31.525  1.00 28.31           O  
ANISOU  534  O   VAL A  69     3324   3151   4280   -504  -1443      1       O  
ATOM    535  CB  VAL A  69      39.928  37.150  28.661  1.00 31.60           C  
ANISOU  535  CB  VAL A  69     3611   3687   4707   -445  -1049     89       C  
ATOM    536  CG1 VAL A  69      40.871  36.094  28.090  1.00 31.95           C  
ANISOU  536  CG1 VAL A  69     3521   3785   4835   -422   -988    180       C  
ATOM    537  CG2 VAL A  69      38.867  37.545  27.638  1.00 30.66           C  
ANISOU  537  CG2 VAL A  69     3529   3593   4529   -416   -907     76       C  
ATOM    538  N   ILE A  70      40.485  35.250  31.609  1.00 24.09           N  
ANISOU  538  N   ILE A  70     2811   2746   3595   -397  -1294      4       N  
ATOM    539  CA  ILE A  70      41.482  34.968  32.644  1.00 26.03           C  
ANISOU  539  CA  ILE A  70     3046   2961   3883   -413  -1462     12       C  
ATOM    540  C   ILE A  70      42.433  33.898  32.105  1.00 28.72           C  
ANISOU  540  C   ILE A  70     3230   3358   4325   -400  -1410    106       C  
ATOM    541  O   ILE A  70      41.996  32.789  31.834  1.00 26.34           O  
ANISOU  541  O   ILE A  70     2943   3124   3942   -338  -1286    110       O  
ATOM    542  CB  ILE A  70      40.809  34.604  34.019  1.00 30.08           C  
ANISOU  542  CB  ILE A  70     3751   3464   4213   -358  -1531    -76       C  
ATOM    543  CG1 ILE A  70      39.882  35.767  34.492  1.00 32.21           C  
ANISOU  543  CG1 ILE A  70     4183   3672   4385   -358  -1568   -161       C  
ATOM    544  CG2 ILE A  70      41.869  34.254  35.100  1.00 32.94           C  
ANISOU  544  CG2 ILE A  70     4116   3795   4606   -364  -1719    -69       C  
ATOM    545  CD1 ILE A  70      38.750  35.413  35.439  1.00 42.33           C  
ANISOU  545  CD1 ILE A  70     5658   4963   5463   -274  -1530   -232       C  
ATOM    546  N   HIS A  71      43.747  34.242  31.938  1.00 31.85           N  
ANISOU  546  N   HIS A  71     3471   3720   4911   -455  -1504    189       N  
ATOM    547  CA  HIS A  71      44.754  33.292  31.462  1.00 33.68           C  
ANISOU  547  CA  HIS A  71     3542   3999   5255   -433  -1454    293       C  
ATOM    548  C   HIS A  71      45.665  32.995  32.634  1.00 39.90           C  
ANISOU  548  C   HIS A  71     4316   4757   6089   -449  -1649    300       C  
ATOM    549  O   HIS A  71      46.369  33.896  33.100  1.00 41.89           O  
ANISOU  549  O   HIS A  71     4522   4931   6463   -522  -1827    311       O  
ATOM    550  CB  HIS A  71      45.555  33.844  30.262  1.00 35.54           C  
ANISOU  550  CB  HIS A  71     3589   4225   5689   -469  -1380    411       C  
ATOM    551  CG  HIS A  71      46.577  32.879  29.726  1.00 39.07           C  
ANISOU  551  CG  HIS A  71     3875   4720   6249   -428  -1304    531       C  
ATOM    552  CD2 HIS A  71      46.500  31.533  29.566  1.00 39.94           C  
ANISOU  552  CD2 HIS A  71     3999   4901   6274   -344  -1198    542       C  
ATOM    553  ND1 HIS A  71      47.821  33.306  29.306  1.00 42.39           N  
ANISOU  553  ND1 HIS A  71     4095   5109   6900   -469  -1334    661       N  
ATOM    554  CE1 HIS A  71      48.455  32.218  28.896  1.00 41.94           C  
ANISOU  554  CE1 HIS A  71     3940   5110   6884   -401  -1235    749       C  
ATOM    555  NE2 HIS A  71      47.704  31.125  29.045  1.00 40.70           N  
ANISOU  555  NE2 HIS A  71     3915   5014   6537   -325  -1156    677       N  
ATOM    556  N   THR A  72      45.608  31.755  33.148  1.00 36.42           N  
ANISOU  556  N   THR A  72     3924   4367   5546   -382  -1628    288       N  
ATOM    557  CA  THR A  72      46.375  31.349  34.319  1.00 38.60           C  
ANISOU  557  CA  THR A  72     4211   4621   5834   -379  -1811    289       C  
ATOM    558  C   THR A  72      46.813  29.878  34.307  1.00 46.83           C  
ANISOU  558  C   THR A  72     5196   5732   6864   -308  -1738    347       C  
ATOM    559  O   THR A  72      46.010  28.998  33.991  1.00 46.93           O  
ANISOU  559  O   THR A  72     5282   5802   6748   -242  -1576    323       O  
ATOM    560  CB  THR A  72      45.714  31.889  35.609  1.00 45.44           C  
ANISOU  560  CB  THR A  72     5290   5430   6544   -379  -1964    168       C  
ATOM    561  CG2 THR A  72      44.425  31.154  35.995  1.00 40.13           C  
ANISOU  561  CG2 THR A  72     4802   4805   5641   -295  -1841     91       C  
ATOM    562  OG1 THR A  72      46.659  31.901  36.674  1.00 42.16           O  
ANISOU  562  OG1 THR A  72     4874   4966   6180   -396  -2195    172       O  
ATOM    563  N   GLU A  73      48.114  29.641  34.615  1.00 46.96           N  
ANISOU  563  N   GLU A  73     5072   5736   7034   -325  -1863    431       N  
ATOM    564  CA  GLU A  73      48.802  28.348  34.701  1.00 48.35           C  
ANISOU  564  CA  GLU A  73     5170   5964   7235   -260  -1829    504       C  
ATOM    565  C   GLU A  73      48.523  27.348  33.561  1.00 53.89           C  
ANISOU  565  C   GLU A  73     5826   6740   7909   -188  -1577    555       C  
ATOM    566  O   GLU A  73      48.344  26.154  33.819  1.00 53.60           O  
ANISOU  566  O   GLU A  73     5848   6746   7771   -114  -1515    549       O  
ATOM    567  CB  GLU A  73      48.618  27.724  36.098  1.00 50.03           C  
ANISOU  567  CB  GLU A  73     5541   6173   7296   -215  -1961    433       C  
ATOM    568  N   ASN A  74      48.524  27.846  32.297  1.00 51.69           N  
ANISOU  568  N   ASN A  74     5449   6468   7721   -204  -1439    609       N  
ATOM    569  CA  ASN A  74      48.269  27.113  31.037  1.00 50.67           C  
ANISOU  569  CA  ASN A  74     5288   6394   7569   -133  -1206    656       C  
ATOM    570  C   ASN A  74      46.785  26.876  30.715  1.00 52.66           C  
ANISOU  570  C   ASN A  74     5715   6668   7626   -102  -1082    550       C  
ATOM    571  O   ASN A  74      46.457  26.225  29.715  1.00 52.30           O  
ANISOU  571  O   ASN A  74     5674   6658   7539    -41   -911    570       O  
ATOM    572  CB  ASN A  74      49.118  25.835  30.893  1.00 52.42           C  
ANISOU  572  CB  ASN A  74     5420   6657   7839    -53  -1143    749       C  
ATOM    573  N   LYS A  75      45.890  27.430  31.548  1.00 46.93           N  
ANISOU  573  N   LYS A  75     5132   5914   6784   -140  -1173    442       N  
ATOM    574  CA  LYS A  75      44.452  27.341  31.347  1.00 44.09           C  
ANISOU  574  CA  LYS A  75     4922   5567   6263   -120  -1072    351       C  
ATOM    575  C   LYS A  75      43.888  28.716  30.990  1.00 42.21           C  
ANISOU  575  C   LYS A  75     4707   5295   6036   -180  -1081    311       C  
ATOM    576  O   LYS A  75      44.388  29.745  31.457  1.00 41.11           O  
ANISOU  576  O   LYS A  75     4536   5106   5979   -243  -1218    313       O  
ATOM    577  CB  LYS A  75      43.751  26.765  32.588  1.00 46.22           C  
ANISOU  577  CB  LYS A  75     5347   5836   6380    -93  -1133    272       C  
ATOM    578  N   LEU A  76      42.878  28.732  30.131  1.00 34.32           N  
ANISOU  578  N   LEU A  76     3763   4315   4962   -159   -944    278       N  
ATOM    579  CA  LEU A  76      42.218  29.953  29.720  1.00 31.30           C  
ANISOU  579  CA  LEU A  76     3412   3905   4575   -203   -933    240       C  
ATOM    580  C   LEU A  76      40.764  29.837  30.156  1.00 27.49           C  
ANISOU  580  C   LEU A  76     3088   3428   3931   -184   -901    143       C  
ATOM    581  O   LEU A  76      40.135  28.806  29.913  1.00 28.40           O  
ANISOU  581  O   LEU A  76     3248   3577   3966   -134   -806    129       O  
ATOM    582  CB  LEU A  76      42.352  30.168  28.192  1.00 31.47           C  
ANISOU  582  CB  LEU A  76     3344   3945   4668   -188   -794    303       C  
ATOM    583  CG  LEU A  76      41.748  31.443  27.585  1.00 36.87           C  
ANISOU  583  CG  LEU A  76     4047   4602   5361   -226   -767    280       C  
ATOM    584  CD1 LEU A  76      42.472  32.693  28.067  1.00 38.21           C  
ANISOU  584  CD1 LEU A  76     4155   4709   5653   -305   -900    303       C  
ATOM    585  CD2 LEU A  76      41.816  31.399  26.076  1.00 39.63           C  
ANISOU  585  CD2 LEU A  76     4336   4977   5746   -183   -614    344       C  
ATOM    586  N   TYR A  77      40.242  30.870  30.824  1.00 21.20           N  
ANISOU  586  N   TYR A  77     2375   2588   3091   -220   -982     83       N  
ATOM    587  CA  TYR A  77      38.843  30.896  31.299  1.00 19.99           C  
ANISOU  587  CA  TYR A  77     2367   2435   2794   -195   -945      5       C  
ATOM    588  C   TYR A  77      38.131  32.097  30.742  1.00 20.55           C  
ANISOU  588  C   TYR A  77     2462   2482   2865   -223   -913    -24       C  
ATOM    589  O   TYR A  77      38.644  33.221  30.803  1.00 21.47           O  
ANISOU  589  O   TYR A  77     2554   2551   3054   -273   -998    -20       O  
ATOM    590  CB  TYR A  77      38.789  30.987  32.833  1.00 23.00           C  
ANISOU  590  CB  TYR A  77     2865   2782   3091   -183  -1067    -44       C  
ATOM    591  CG  TYR A  77      39.536  29.883  33.545  1.00 26.97           C  
ANISOU  591  CG  TYR A  77     3357   3303   3588   -151  -1121    -16       C  
ATOM    592  CD1 TYR A  77      38.897  28.700  33.898  1.00 29.42           C  
ANISOU  592  CD1 TYR A  77     3732   3646   3799    -92  -1042    -23       C  
ATOM    593  CD2 TYR A  77      40.884  30.020  33.868  1.00 29.22           C  
ANISOU  593  CD2 TYR A  77     3558   3566   3977   -182  -1254     26       C  
ATOM    594  CE1 TYR A  77      39.575  27.688  34.583  1.00 32.73           C  
ANISOU  594  CE1 TYR A  77     4150   4079   4209    -56  -1089      5       C  
ATOM    595  CE2 TYR A  77      41.573  29.011  34.538  1.00 31.25           C  
ANISOU  595  CE2 TYR A  77     3805   3841   4230   -147  -1309     55       C  
ATOM    596  CZ  TYR A  77      40.919  27.837  34.873  1.00 37.57           C  
ANISOU  596  CZ  TYR A  77     4682   4676   4916    -81  -1221     43       C  
ATOM    597  OH  TYR A  77      41.590  26.837  35.540  1.00 38.59           O  
ANISOU  597  OH  TYR A  77     4807   4820   5037    -40  -1271     75       O  
ATOM    598  N   LEU A  78      36.964  31.880  30.153  1.00 16.36           N  
ANISOU  598  N   LEU A  78     1973   1978   2265   -195   -797    -48       N  
ATOM    599  CA  LEU A  78      36.156  32.956  29.632  1.00 15.88           C  
ANISOU  599  CA  LEU A  78     1942   1899   2193   -211   -759    -75       C  
ATOM    600  C   LEU A  78      34.951  33.088  30.530  1.00 17.00           C  
ANISOU  600  C   LEU A  78     2215   2028   2216   -182   -754   -135       C  
ATOM    601  O   LEU A  78      34.279  32.080  30.814  1.00 16.73           O  
ANISOU  601  O   LEU A  78     2219   2023   2116   -140   -696   -142       O  
ATOM    602  CB  LEU A  78      35.725  32.671  28.193  1.00 14.60           C  
ANISOU  602  CB  LEU A  78     1725   1773   2049   -194   -636    -50       C  
ATOM    603  CG  LEU A  78      36.849  32.442  27.199  1.00 18.32           C  
ANISOU  603  CG  LEU A  78     2080   2260   2622   -195   -605     22       C  
ATOM    604  CD1 LEU A  78      36.292  32.187  25.803  1.00 18.93           C  
ANISOU  604  CD1 LEU A  78     2145   2366   2683   -158   -488     36       C  
ATOM    605  CD2 LEU A  78      37.833  33.599  27.167  1.00 22.45           C  
ANISOU  605  CD2 LEU A  78     2531   2741   3258   -247   -674     62       C  
ATOM    606  N   VAL A  79      34.671  34.293  30.987  1.00 15.95           N  
ANISOU  606  N   VAL A  79     2151   1847   2062   -197   -808   -172       N  
ATOM    607  CA  VAL A  79      33.555  34.535  31.894  1.00 15.28           C  
ANISOU  607  CA  VAL A  79     2201   1744   1860   -153   -793   -220       C  
ATOM    608  C   VAL A  79      32.501  35.276  31.112  1.00 15.94           C  
ANISOU  608  C   VAL A  79     2290   1830   1938   -150   -707   -230       C  
ATOM    609  O   VAL A  79      32.763  36.381  30.622  1.00 16.20           O  
ANISOU  609  O   VAL A  79     2302   1828   2025   -186   -737   -232       O  
ATOM    610  CB  VAL A  79      34.036  35.389  33.101  1.00 18.78           C  
ANISOU  610  CB  VAL A  79     2751   2119   2266   -155   -932   -260       C  
ATOM    611  CG1 VAL A  79      32.934  35.514  34.159  1.00 19.43           C  
ANISOU  611  CG1 VAL A  79     2996   2183   2205    -82   -902   -302       C  
ATOM    612  CG2 VAL A  79      35.358  34.867  33.718  1.00 19.72           C  
ANISOU  612  CG2 VAL A  79     2838   2227   2425   -175  -1056   -244       C  
ATOM    613  N   PHE A  80      31.333  34.681  30.986  1.00 13.75           N  
ANISOU  613  N   PHE A  80     2031   1585   1608   -108   -605   -228       N  
ATOM    614  CA  PHE A  80      30.230  35.228  30.201  1.00 13.26           C  
ANISOU  614  CA  PHE A  80     1961   1530   1546    -99   -523   -230       C  
ATOM    615  C   PHE A  80      29.043  35.507  31.062  1.00 14.30           C  
ANISOU  615  C   PHE A  80     2196   1646   1593    -44   -479   -248       C  
ATOM    616  O   PHE A  80      28.834  34.859  32.107  1.00 15.39           O  
ANISOU  616  O   PHE A  80     2398   1783   1665      0   -471   -247       O  
ATOM    617  CB  PHE A  80      29.802  34.216  29.121  1.00 14.36           C  
ANISOU  617  CB  PHE A  80     2016   1719   1721    -98   -445   -202       C  
ATOM    618  CG  PHE A  80      30.738  34.143  27.942  1.00 13.19           C  
ANISOU  618  CG  PHE A  80     1777   1587   1649   -131   -452   -177       C  
ATOM    619  CD1 PHE A  80      30.689  35.107  26.937  1.00 14.75           C  
ANISOU  619  CD1 PHE A  80     1943   1776   1884   -146   -434   -171       C  
ATOM    620  CD2 PHE A  80      31.644  33.092  27.814  1.00 14.65           C  
ANISOU  620  CD2 PHE A  80     1910   1793   1863   -133   -465   -152       C  
ATOM    621  CE1 PHE A  80      31.528  35.032  25.841  1.00 15.28           C  
ANISOU  621  CE1 PHE A  80     1934   1857   2014   -159   -420   -134       C  
ATOM    622  CE2 PHE A  80      32.488  33.022  26.707  1.00 16.78           C  
ANISOU  622  CE2 PHE A  80     2101   2076   2198   -144   -450   -117       C  
ATOM    623  CZ  PHE A  80      32.425  33.992  25.741  1.00 15.19           C  
ANISOU  623  CZ  PHE A  80     1875   1867   2030   -154   -424   -106       C  
ATOM    624  N   GLU A  81      28.210  36.415  30.598  1.00 15.12           N  
ANISOU  624  N   GLU A  81     2310   1738   1696    -35   -434   -254       N  
ATOM    625  CA  GLU A  81      26.913  36.635  31.184  1.00 16.60           C  
ANISOU  625  CA  GLU A  81     2569   1918   1819     28   -359   -252       C  
ATOM    626  C   GLU A  81      26.152  35.280  31.142  1.00 15.81           C  
ANISOU  626  C   GLU A  81     2416   1861   1729     50   -280   -213       C  
ATOM    627  O   GLU A  81      26.319  34.493  30.199  1.00 16.34           O  
ANISOU  627  O   GLU A  81     2387   1962   1861     13   -274   -197       O  
ATOM    628  CB  GLU A  81      26.245  37.713  30.303  1.00 20.24           C  
ANISOU  628  CB  GLU A  81     3009   2370   2311     23   -323   -254       C  
ATOM    629  CG  GLU A  81      24.784  37.546  30.007  1.00 25.76           C  
ANISOU  629  CG  GLU A  81     3682   3094   3013     65   -222   -223       C  
ATOM    630  CD  GLU A  81      24.138  38.501  29.025  1.00 19.34           C  
ANISOU  630  CD  GLU A  81     2835   2279   2235     62   -192   -219       C  
ATOM    631  OE1 GLU A  81      24.763  38.891  28.011  1.00 16.34           O  
ANISOU  631  OE1 GLU A  81     2404   1901   1903     15   -230   -227       O  
ATOM    632  OE2 GLU A  81      22.936  38.763  29.229  1.00 25.20           O1-
ANISOU  632  OE2 GLU A  81     3593   3019   2963    114   -119   -196       O1-
ATOM    633  N   PHE A  82      25.341  35.014  32.141  1.00 15.14           N  
ANISOU  633  N   PHE A  82     2400   1769   1585    115   -218   -193       N  
ATOM    634  CA  PHE A  82      24.592  33.787  32.255  1.00 14.39           C  
ANISOU  634  CA  PHE A  82     2255   1699   1513    137   -142   -145       C  
ATOM    635  C   PHE A  82      23.195  33.967  31.723  1.00 16.08           C  
ANISOU  635  C   PHE A  82     2413   1921   1775    155    -55   -107       C  
ATOM    636  O   PHE A  82      22.528  34.953  32.071  1.00 15.95           O  
ANISOU  636  O   PHE A  82     2455   1885   1722    204    -12   -103       O  
ATOM    637  CB  PHE A  82      24.538  33.366  33.750  1.00 16.53           C  
ANISOU  637  CB  PHE A  82     2634   1952   1694    209   -113   -126       C  
ATOM    638  CG  PHE A  82      23.740  32.112  33.980  1.00 14.99           C  
ANISOU  638  CG  PHE A  82     2389   1774   1533    235    -22    -61       C  
ATOM    639  CD1 PHE A  82      24.298  30.863  33.737  1.00 16.78           C  
ANISOU  639  CD1 PHE A  82     2552   2018   1804    195    -49    -50       C  
ATOM    640  CD2 PHE A  82      22.396  32.176  34.340  1.00 17.26           C  
ANISOU  640  CD2 PHE A  82     2677   2054   1827    297     95     -1       C  
ATOM    641  CE1 PHE A  82      23.533  29.693  33.870  1.00 17.25           C  
ANISOU  641  CE1 PHE A  82     2558   2081   1916    208     29     13       C  
ATOM    642  CE2 PHE A  82      21.649  31.005  34.499  1.00 19.77           C  
ANISOU  642  CE2 PHE A  82     2926   2377   2206    310    177     73       C  
ATOM    643  CZ  PHE A  82      22.233  29.765  34.291  1.00 17.25           C  
ANISOU  643  CZ  PHE A  82     2554   2068   1931    263    139     77       C  
ATOM    644  N   LEU A  83      22.766  33.010  30.866  1.00 14.24           N  
ANISOU  644  N   LEU A  83     2069   1711   1628    118    -38    -78       N  
ATOM    645  CA ALEU A  83      21.392  32.951  30.407  0.80 14.83           C  
ANISOU  645  CA ALEU A  83     2072   1789   1772    130     29    -31       C  
ATOM    646  CA BLEU A  83      21.411  32.937  30.357  0.20 14.43           C  
ANISOU  646  CA BLEU A  83     2019   1740   1725    127     26    -33       C  
ATOM    647  C   LEU A  83      20.949  31.542  30.673  1.00 19.62           C  
ANISOU  647  C   LEU A  83     2624   2396   2435    128     66     21       C  
ATOM    648  O   LEU A  83      21.746  30.607  30.611  1.00 20.06           O  
ANISOU  648  O   LEU A  83     2671   2456   2493     96     22      6       O  
ATOM    649  CB ALEU A  83      21.231  33.310  28.920  0.80 14.47           C  
ANISOU  649  CB ALEU A  83     1951   1757   1792     82    -15    -53       C  
ATOM    650  CB BLEU A  83      21.333  33.247  28.860  0.20 13.69           C  
ANISOU  650  CB BLEU A  83     1850   1660   1694     77    -22    -56       C  
ATOM    651  CG ALEU A  83      21.420  34.784  28.602  0.80 17.95           C  
ANISOU  651  CG ALEU A  83     2435   2191   2195     89    -32    -87       C  
ATOM    652  CG BLEU A  83      21.122  34.729  28.550  0.20 17.48           C  
ANISOU  652  CG BLEU A  83     2361   2132   2148     94    -20    -76       C  
ATOM    653  CD1ALEU A  83      22.826  35.013  28.100  0.80 19.39           C  
ANISOU  653  CD1ALEU A  83     2633   2376   2357     44   -111   -136       C  
ATOM    654  CD1BLEU A  83      22.442  35.435  28.395  0.20 17.69           C  
ANISOU  654  CD1BLEU A  83     2442   2153   2128     66    -88   -130       C  
ATOM    655  CD2ALEU A  83      20.445  35.244  27.487  0.80 19.50           C  
ANISOU  655  CD2ALEU A  83     2560   2395   2454     84    -23    -72       C  
ATOM    656  CD2BLEU A  83      20.308  34.917  27.278  0.20 17.69           C  
ANISOU  656  CD2BLEU A  83     2305   2170   2248     75    -27    -65       C  
ATOM    657  N   HIS A  84      19.692  31.405  31.042  0.79 21.69           N  
ANISOU  657  N   HIS A  84     3079   3488   1676   -148     14    -70       N  
ATOM    658  CA  HIS A  84      19.122  30.143  31.497  0.65 21.21           C  
ANISOU  658  CA  HIS A  84     3085   3441   1533   -226     39     60       C  
ATOM    659  C   HIS A  84      18.809  29.030  30.476  1.00 21.98           C  
ANISOU  659  C   HIS A  84     3207   3426   1718   -293     35    149       C  
ATOM    660  O   HIS A  84      18.720  27.878  30.891  0.88 23.38           O  
ANISOU  660  O   HIS A  84     3464   3577   1843   -347     23    263       O  
ATOM    661  CB  HIS A  84      17.928  30.393  32.458  0.68 23.60           C  
ANISOU  661  CB  HIS A  84     3355   3900   1711   -272    134     68       C  
ATOM    662  CG  HIS A  84      18.235  31.148  33.740  0.48 27.95           C  
ANISOU  662  CG  HIS A  84     3908   4579   2133   -211    131      1       C  
ATOM    663  CD2 HIS A  84      18.279  30.699  35.021  0.63 31.29           C  
ANISOU  663  CD2 HIS A  84     4400   5100   2388   -223    137     63       C  
ATOM    664  ND1 HIS A  84      18.407  32.537  33.758  0.81 29.39           N  
ANISOU  664  ND1 HIS A  84     4012   4803   2351   -133    126   -148       N  
ATOM    665  CE1 HIS A  84      18.627  32.865  35.021  0.87 30.14           C  
ANISOU  665  CE1 HIS A  84     4128   5016   2307    -93    120   -185       C  
ATOM    666  NE2 HIS A  84      18.545  31.803  35.829  0.93 31.59           N  
ANISOU  666  NE2 HIS A  84     4400   5248   2355   -142    130    -61       N  
ATOM    667  N  AGLN A  85      18.697  29.304  29.180  0.50 18.45           N  
ANISOU  667  N  AGLN A  85     2705   2906   1401   -288     36    102       N  
ATOM    668  N  BGLN A  85      18.670  29.371  29.176  0.50 19.40           N  
ANISOU  668  N  BGLN A  85     2820   3030   1522   -286     38     97       N  
ATOM    669  CA AGLN A  85      18.444  28.183  28.276  0.50 17.27           C  
ANISOU  669  CA AGLN A  85     2582   2653   1325   -344     21    176       C  
ATOM    670  CA BGLN A  85      18.238  28.396  28.193  0.50 18.67           C  
ANISOU  670  CA BGLN A  85     2739   2846   1508   -346     37    161       C  
ATOM    671  C  AGLN A  85      18.972  28.540  26.919  0.50 16.42           C  
ANISOU  671  C  AGLN A  85     2437   2459   1344   -299    -14    109       C  
ATOM    672  C  BGLN A  85      18.792  28.609  26.774  0.50 18.93           C  
ANISOU  672  C  BGLN A  85     2742   2780   1672   -305     -4    104       C  
ATOM    673  O  AGLN A  85      19.280  29.712  26.676  0.50 14.78           O  
ANISOU  673  O  AGLN A  85     2174   2277   1166   -243     -9     18       O  
ATOM    674  O  BGLN A  85      18.871  29.742  26.310  0.50 18.22           O  
ANISOU  674  O  BGLN A  85     2589   2710   1625   -260      9     17       O  
ATOM    675  CB AGLN A  85      16.930  27.869  28.203  0.50 19.74           C  
ANISOU  675  CB AGLN A  85     2854   3019   1628   -439    105    221       C  
ATOM    676  CB BGLN A  85      16.686  28.458  28.185  0.50 20.37           C  
ANISOU  676  CB BGLN A  85     2891   3140   1707   -425    130    177       C  
ATOM    677  CG AGLN A  85      16.571  26.515  27.603  0.50 24.51           C  
ANISOU  677  CG AGLN A  85     3500   3524   2288   -517     88    314       C  
ATOM    678  CG BGLN A  85      15.951  27.526  27.237  0.50 18.89           C  
ANISOU  678  CG BGLN A  85     2697   2880   1601   -500    139    231       C  
ATOM    679  CD AGLN A  85      15.115  26.224  27.797  0.50 33.16           C  
ANISOU  679  CD AGLN A  85     4550   4689   3361   -620    174    359       C  
ATOM    680  CD BGLN A  85      16.040  26.069  27.586  0.50 37.50           C  
ANISOU  680  CD BGLN A  85     5147   5167   3936   -569    109    354       C  
ATOM    681  NE2AGLN A  85      14.804  25.488  28.848  0.50 33.36           N  
ANISOU  681  NE2AGLN A  85     4632   4754   3287   -694    204    463       N  
ATOM    682  NE2BGLN A  85      14.896  25.411  27.635  0.50 31.07           N  
ANISOU  682  NE2BGLN A  85     4314   4371   3118   -674    166    420       N  
ATOM    683  OE1AGLN A  85      14.261  26.664  27.031  0.50 20.30           O  
ANISOU  683  OE1AGLN A  85     2832   3084   1797   -635    215    301       O  
ATOM    684  OE1BGLN A  85      17.125  25.506  27.755  0.50 28.45           O  
ANISOU  684  OE1BGLN A  85     4084   3939   2785   -531     30    389       O  
ATOM    685  N   ASP A  86      19.111  27.525  26.054  1.00 15.98           N  
ANISOU  685  N   ASP A  86     2413   2300   1359   -324    -52    153       N  
ATOM    686  CA  ASP A  86      19.529  27.647  24.654  1.00 15.13           C  
ANISOU  686  CA  ASP A  86     2274   2117   1360   -290    -81     99       C  
ATOM    687  C   ASP A  86      18.353  27.327  23.732  1.00 15.21           C  
ANISOU  687  C   ASP A  86     2243   2112   1423   -350    -43    112       C  
ATOM    688  O   ASP A  86      17.330  26.768  24.157  1.00 16.58           O  
ANISOU  688  O   ASP A  86     2420   2313   1566   -425     -5    172       O  
ATOM    689  CB  ASP A  86      20.798  26.818  24.333  1.00 16.67           C  
ANISOU  689  CB  ASP A  86     2526   2214   1596   -247   -167    106       C  
ATOM    690  CG  ASP A  86      20.676  25.310  24.327  1.00 22.91           C  
ANISOU  690  CG  ASP A  86     3389   2918   2399   -291   -213    189       C  
ATOM    691  OD1 ASP A  86      19.731  24.809  23.744  1.00 23.96           O  
ANISOU  691  OD1 ASP A  86     3507   3025   2569   -352   -187    218       O  
ATOM    692  OD2 ASP A  86      21.628  24.638  24.766  1.00 30.09           O1-
ANISOU  692  OD2 ASP A  86     4363   3771   3297   -253   -288    213       O1-
ATOM    693  N   LEU A  87      18.478  27.710  22.477  1.00 14.27           N  
ANISOU  693  N   LEU A  87     2083   1958   1380   -319    -52     56       N  
ATOM    694  CA  LEU A  87      17.418  27.500  21.509  1.00 13.38           C  
ANISOU  694  CA  LEU A  87     1929   1836   1319   -361    -29     52       C  
ATOM    695  C   LEU A  87      17.207  26.043  21.183  1.00 15.56           C  
ANISOU  695  C   LEU A  87     2249   2031   1631   -413    -66    108       C  
ATOM    696  O   LEU A  87      16.071  25.657  20.860  1.00 16.25           O  
ANISOU  696  O   LEU A  87     2305   2126   1745   -476    -40    125       O  
ATOM    697  CB  LEU A  87      17.709  28.314  20.222  1.00 12.44           C  
ANISOU  697  CB  LEU A  87     1766   1702   1258   -307    -37    -18       C  
ATOM    698  CG  LEU A  87      16.601  28.338  19.185  1.00 13.87           C  
ANISOU  698  CG  LEU A  87     1899   1889   1483   -331    -21    -36       C  
ATOM    699  CD1 LEU A  87      15.339  29.048  19.736  1.00 16.07           C  
ANISOU  699  CD1 LEU A  87     2116   2254   1736   -359     37    -46       C  
ATOM    700  CD2 LEU A  87      17.089  29.031  17.895  1.00 13.99           C  
ANISOU  700  CD2 LEU A  87     1894   1884   1538   -274    -38    -89       C  
ATOM    701  N   LYS A  88      18.258  25.216  21.297  1.00 15.51           N  
ANISOU  701  N   LYS A  88     2311   1947   1634   -388   -132    132       N  
ATOM    702  CA  LYS A  88      18.095  23.787  21.015  1.00 16.24           C  
ANISOU  702  CA  LYS A  88     2454   1943   1773   -433   -181    181       C  
ATOM    703  C   LYS A  88      17.132  23.193  22.046  1.00 18.65           C  
ANISOU  703  C   LYS A  88     2786   2266   2033   -530   -145    276       C  
ATOM    704  O   LYS A  88      16.161  22.507  21.692  1.00 18.45           O  
ANISOU  704  O   LYS A  88     2746   2211   2052   -607   -134    306       O  
ATOM    705  CB  LYS A  88      19.449  23.060  21.042  1.00 18.72           C  
ANISOU  705  CB  LYS A  88     2836   2169   2107   -373   -268    181       C  
ATOM    706  CG  LYS A  88      19.345  21.541  20.781  1.00 25.89           C  
ANISOU  706  CG  LYS A  88     3805   2955   3076   -411   -337    227       C  
ATOM    707  CD  LYS A  88      20.204  20.711  21.720  0.50 40.45           C  
ANISOU  707  CD  LYS A  88     5745   4726   4897   -391   -412    290       C  
ATOM    708  CE  LYS A  88      20.242  19.256  21.310  0.50 46.09           C  
ANISOU  708  CE  LYS A  88     6522   5298   5693   -410   -498    319       C  
ATOM    709  NZ  LYS A  88      19.042  18.513  21.780  0.50 53.03           N1+
ANISOU  709  NZ  LYS A  88     7434   6141   6573   -533   -473    424       N1+
ATOM    710  N   LYS A  89      17.356  23.481  23.340  1.00 17.52           N  
ANISOU  710  N   LYS A  89     2677   2182   1797   -532   -123    322       N  
ATOM    711  CA  LYS A  89      16.468  22.970  24.367  1.00 19.55           C  
ANISOU  711  CA  LYS A  89     2960   2477   1990   -629    -75    420       C  
ATOM    712  C   LYS A  89      15.052  23.542  24.229  1.00 20.43           C  
ANISOU  712  C   LYS A  89     2974   2688   2100   -693     19    397       C  
ATOM    713  O   LYS A  89      14.078  22.799  24.382  1.00 21.64           O  
ANISOU  713  O   LYS A  89     3122   2836   2264   -797     52    461       O  
ATOM    714  CB  LYS A  89      17.079  23.252  25.740  1.00 22.01           C  
ANISOU  714  CB  LYS A  89     3328   2850   2185   -602    -74    461       C  
ATOM    715  CG  LYS A  89      18.347  22.438  25.995  1.00 29.31           C  
ANISOU  715  CG  LYS A  89     4356   3668   3113   -549   -179    500       C  
ATOM    716  CD  LYS A  89      18.897  22.675  27.399  1.00 36.27           C  
ANISOU  716  CD  LYS A  89     5297   4615   3868   -521   -187    544       C  
ATOM    717  CE  LYS A  89      20.275  22.081  27.574  1.00 44.45           C  
ANISOU  717  CE  LYS A  89     6418   5555   4915   -440   -304    553       C  
ATOM    718  NZ  LYS A  89      20.746  22.214  28.980  1.00 57.40           N1+
ANISOU  718  NZ  LYS A  89     8126   7260   6423   -414   -323    603       N1+
ATOM    719  N   PHE A  90      14.931  24.830  23.856  1.00 18.27           N  
ANISOU  719  N   PHE A  90     2620   2496   1827   -633     54    301       N  
ATOM    720  CA  PHE A  90      13.629  25.480  23.652  1.00 17.82           C  
ANISOU  720  CA  PHE A  90     2460   2532   1777   -671    130    258       C  
ATOM    721  C   PHE A  90      12.882  24.839  22.460  1.00 19.49           C  
ANISOU  721  C   PHE A  90     2633   2680   2091   -717    112    245       C  
ATOM    722  O   PHE A  90      11.677  24.570  22.565  1.00 21.48           O  
ANISOU  722  O   PHE A  90     2828   2980   2354   -802    164    262       O  
ATOM    723  CB  PHE A  90      13.788  27.007  23.501  1.00 18.04           C  
ANISOU  723  CB  PHE A  90     2425   2636   1793   -582    150    159       C  
ATOM    724  CG  PHE A  90      12.494  27.786  23.444  1.00 18.71           C  
ANISOU  724  CG  PHE A  90     2404   2824   1880   -601    218    104       C  
ATOM    725  CD1 PHE A  90      11.648  27.846  24.543  1.00 23.11           C  
ANISOU  725  CD1 PHE A  90     2925   3495   2360   -659    293    126       C  
ATOM    726  CD2 PHE A  90      12.152  28.512  22.314  1.00 19.48           C  
ANISOU  726  CD2 PHE A  90     2438   2913   2049   -552    203     25       C  
ATOM    727  CE1 PHE A  90      10.450  28.570  24.482  1.00 24.53           C  
ANISOU  727  CE1 PHE A  90     2994   3778   2550   -668    353     58       C  
ATOM    728  CE2 PHE A  90      10.942  29.204  22.245  1.00 22.45           C  
ANISOU  728  CE2 PHE A  90     2714   3379   2436   -559    251    -32       C  
ATOM    729  CZ  PHE A  90      10.094  29.220  23.322  1.00 22.96           C  
ANISOU  729  CZ  PHE A  90     2731   3555   2436   -615    325    -22       C  
ATOM    730  N   MET A  91      13.598  24.568  21.346  1.00 16.63           N  
ANISOU  730  N   MET A  91     2297   2220   1801   -662     39    209       N  
ATOM    731  CA AMET A  91      12.920  23.919  20.227  0.50 15.21           C  
ANISOU  731  CA AMET A  91     2085   1984   1711   -699     13    188       C  
ATOM    732  CA BMET A  91      13.035  23.896  20.161  0.50 16.66           C  
ANISOU  732  CA BMET A  91     2274   2158   1898   -692      5    185       C  
ATOM    733  C   MET A  91      12.492  22.515  20.562  1.00 20.37           C  
ANISOU  733  C   MET A  91     2781   2563   2396   -803     -2    271       C  
ATOM    734  O   MET A  91      11.393  22.125  20.158  1.00 21.80           O  
ANISOU  734  O   MET A  91     2903   2747   2631   -878     16    265       O  
ATOM    735  CB AMET A  91      13.796  23.892  19.008  0.50 15.22           C  
ANISOU  735  CB AMET A  91     2107   1910   1767   -617    -58    128       C  
ATOM    736  CB BMET A  91      14.132  23.702  19.091  0.50 18.01           C  
ANISOU  736  CB BMET A  91     2485   2240   2118   -609    -73    138       C  
ATOM    737  CG AMET A  91      13.906  25.231  18.354  0.50 15.15           C  
ANISOU  737  CG AMET A  91     2043   1964   1749   -537    -41     50       C  
ATOM    738  CG BMET A  91      14.407  24.944  18.263  0.50 20.34           C  
ANISOU  738  CG BMET A  91     2731   2585   2413   -522    -66     55       C  
ATOM    739  SD AMET A  91      14.586  25.052  16.729  0.50 14.95           S  
ANISOU  739  SD AMET A  91     2028   1871   1782   -468   -108    -15       S  
ATOM    740  SD BMET A  91      16.052  24.947  17.488  0.50 24.14           S  
ANISOU  740  SD BMET A  91     3263   3000   2910   -425   -131     13       S  
ATOM    741  CE AMET A  91      16.167  24.388  17.145  0.50 10.16           C  
ANISOU  741  CE AMET A  91     1508   1186   1165   -428   -160     11       C  
ATOM    742  CE BMET A  91      15.682  25.706  15.986  0.50 20.38           C  
ANISOU  742  CE BMET A  91     2727   2554   2463   -380   -130    -63       C  
ATOM    743  N   ASP A  92      13.300  21.753  21.326  1.00 19.58           N  
ANISOU  743  N   ASP A  92     2781   2394   2265   -814    -39    351       N  
ATOM    744  CA  ASP A  92      12.931  20.403  21.751  1.00 21.76           C  
ANISOU  744  CA  ASP A  92     3116   2582   2570   -921    -59    451       C  
ATOM    745  C   ASP A  92      11.698  20.458  22.639  1.00 26.26           C  
ANISOU  745  C   ASP A  92     3636   3251   3089  -1038     40    513       C  
ATOM    746  O   ASP A  92      10.780  19.651  22.445  1.00 27.78           O  
ANISOU  746  O   ASP A  92     3804   3405   3346  -1147     51    549       O  
ATOM    747  CB  ASP A  92      14.090  19.723  22.494  1.00 23.63           C  
ANISOU  747  CB  ASP A  92     3476   2731   2770   -893   -125    528       C  
ATOM    748  CG  ASP A  92      15.239  19.272  21.625  1.00 28.46           C  
ANISOU  748  CG  ASP A  92     4137   3224   3454   -798   -233    472       C  
ATOM    749  OD1 ASP A  92      15.067  19.218  20.388  1.00 29.96           O  
ANISOU  749  OD1 ASP A  92     4278   3380   3727   -773   -260    388       O  
ATOM    750  OD2 ASP A  92      16.324  19.015  22.173  1.00 32.39           O1-
ANISOU  750  OD2 ASP A  92     4716   3672   3917   -741   -290    504       O1-
ATOM    751  N   ALA A  93      11.642  21.422  23.583  1.00 24.00           N  
ANISOU  751  N   ALA A  93     3325   3101   2693  -1018    114    515       N  
ATOM    752  CA  ALA A  93      10.498  21.580  24.489  1.00 27.16           C  
ANISOU  752  CA  ALA A  93     3666   3627   3026  -1121    221    560       C  
ATOM    753  C   ALA A  93       9.232  22.061  23.788  1.00 30.69           C  
ANISOU  753  C   ALA A  93     3973   4152   3536  -1154    275    474       C  
ATOM    754  O   ALA A  93       8.133  21.773  24.267  1.00 33.07           O  
ANISOU  754  O   ALA A  93     4214   4526   3826  -1269    353    513       O  
ATOM    755  CB  ALA A  93      10.853  22.517  25.631  1.00 28.03           C  
ANISOU  755  CB  ALA A  93     3784   3866   2999  -1070    275    560       C  
ATOM    756  N   SER A  94       9.386  22.768  22.651  1.00 27.22           N  
ANISOU  756  N   SER A  94     3482   3701   3160  -1055    233    361       N  
ATOM    757  CA  SER A  94       8.286  23.298  21.841  1.00 27.28           C  
ANISOU  757  CA  SER A  94     3364   3773   3231  -1058    259    268       C  
ATOM    758  C   SER A  94       7.944  22.363  20.661  1.00 34.21           C  
ANISOU  758  C   SER A  94     4231   4537   4230  -1097    192    250       C  
ATOM    759  O   SER A  94       7.203  22.782  19.780  1.00 33.75           O  
ANISOU  759  O   SER A  94     4080   4515   4230  -1075    186    162       O  
ATOM    760  CB  SER A  94       8.653  24.684  21.303  1.00 27.36           C  
ANISOU  760  CB  SER A  94     3333   3833   3227   -923    244    163       C  
ATOM    761  OG  SER A  94       8.990  25.622  22.316  1.00 30.20           O  
ANISOU  761  OG  SER A  94     3696   4288   3488   -876    293    158       O  
ATOM    762  N   ALA A  95       8.488  21.123  20.620  1.00 32.72           N  
ANISOU  762  N   ALA A  95     4139   4211   4083  -1144    131    324       N  
ATOM    763  CA  ALA A  95       8.297  20.173  19.512  1.00 33.34           C  
ANISOU  763  CA  ALA A  95     4218   4168   4281  -1170     53    296       C  
ATOM    764  C   ALA A  95       6.842  19.813  19.180  1.00 37.71           C  
ANISOU  764  C   ALA A  95     4661   4753   4912  -1279     85    270       C  
ATOM    765  O   ALA A  95       6.501  19.681  18.002  1.00 37.63           O  
ANISOU  765  O   ALA A  95     4601   4706   4989  -1253     26    183       O  
ATOM    766  CB  ALA A  95       9.090  18.901  19.763  1.00 35.01           C  
ANISOU  766  CB  ALA A  95     4555   4225   4523  -1207    -17    385       C  
ATOM    767  N   LEU A  96       6.006  19.624  20.202  1.00 34.40           N  
ANISOU  767  N   LEU A  96     4202   4409   4462  -1403    176    341       N  
ATOM    768  CA  LEU A  96       4.610  19.216  20.011  1.00 34.41           C  
ANISOU  768  CA  LEU A  96     4086   4447   4542  -1526    216    321       C  
ATOM    769  C   LEU A  96       3.755  20.291  19.356  1.00 33.29           C  
ANISOU  769  C   LEU A  96     3798   4434   4416  -1464    240    187       C  
ATOM    770  O   LEU A  96       2.945  19.991  18.483  1.00 32.14           O  
ANISOU  770  O   LEU A  96     3567   4273   4373  -1495    205    114       O  
ATOM    771  CB  LEU A  96       3.988  18.776  21.352  1.00 37.02           C  
ANISOU  771  CB  LEU A  96     4407   4842   4817  -1682    323    440       C  
ATOM    772  CG  LEU A  96       3.913  17.270  21.624  1.00 45.24           C  
ANISOU  772  CG  LEU A  96     5526   5737   5928  -1832    297    563       C  
ATOM    773  CD1 LEU A  96       5.303  16.656  21.793  1.00 45.99           C  
ANISOU  773  CD1 LEU A  96     5797   5675   6000  -1774    207    645       C  
ATOM    774  CD2 LEU A  96       3.090  16.997  22.861  1.00 50.01           C  
ANISOU  774  CD2 LEU A  96     6094   6438   6469  -1997    424    674       C  
ATOM    775  N   THR A  97       3.979  21.545  19.742  1.00 28.92           N  
ANISOU  775  N   THR A  97     3222   3998   3768  -1365    286    148       N  
ATOM    776  CA  THR A  97       3.201  22.688  19.292  1.00 28.78           C  
ANISOU  776  CA  THR A  97     3076   4105   3756  -1294    307     28       C  
ATOM    777  C   THR A  97       3.889  23.574  18.278  1.00 30.25           C  
ANISOU  777  C   THR A  97     3288   4262   3941  -1132    229    -56       C  
ATOM    778  O   THR A  97       3.210  24.260  17.520  1.00 32.73           O  
ANISOU  778  O   THR A  97     3509   4633   4294  -1073    207   -156       O  
ATOM    779  CB  THR A  97       2.821  23.552  20.517  1.00 40.12           C  
ANISOU  779  CB  THR A  97     4453   5702   5089  -1302    419     33       C  
ATOM    780  CG2 THR A  97       1.846  22.854  21.459  1.00 44.44           C  
ANISOU  780  CG2 THR A  97     4934   6325   5627  -1470    519     99       C  
ATOM    781  OG1 THR A  97       4.021  23.905  21.222  1.00 43.10           O  
ANISOU  781  OG1 THR A  97     4948   6062   5365  -1236    421     92       O  
ATOM    782  N   GLY A  98       5.218  23.609  18.311  1.00 21.60           N  
ANISOU  782  N   GLY A  98     2318   3089   2800  -1060    188    -13       N  
ATOM    783  CA  GLY A  98       6.008  24.526  17.512  1.00 19.83           C  
ANISOU  783  CA  GLY A  98     2127   2849   2560   -917    133    -74       C  
ATOM    784  C   GLY A  98       6.181  25.867  18.215  1.00 21.65           C  
ANISOU  784  C   GLY A  98     2337   3181   2708   -844    186    -97       C  
ATOM    785  O   GLY A  98       5.360  26.259  19.062  1.00 23.25           O  
ANISOU  785  O   GLY A  98     2460   3495   2878   -886    262   -107       O  
ATOM    786  N   ILE A  99       7.266  26.562  17.913  1.00 18.89           N  
ANISOU  786  N   ILE A  99     2054   2796   2326   -739    148   -110       N  
ATOM    787  CA  ILE A  99       7.471  27.901  18.449  1.00 17.67           C  
ANISOU  787  CA  ILE A  99     1881   2719   2113   -661    182   -145       C  
ATOM    788  C   ILE A  99       6.491  28.808  17.669  1.00 19.61           C  
ANISOU  788  C   ILE A  99     2027   3024   2402   -605    167   -240       C  
ATOM    789  O   ILE A  99       6.428  28.715  16.436  1.00 18.59           O  
ANISOU  789  O   ILE A  99     1898   2842   2324   -568    102   -272       O  
ATOM    790  CB  ILE A  99       8.933  28.373  18.248  1.00 18.18           C  
ANISOU  790  CB  ILE A  99     2041   2717   2147   -573    141   -134       C  
ATOM    791  CG1 ILE A  99       9.943  27.477  18.980  1.00 19.49           C  
ANISOU  791  CG1 ILE A  99     2306   2824   2277   -613    138    -51       C  
ATOM    792  CG2 ILE A  99       9.084  29.848  18.653  1.00 19.08           C  
ANISOU  792  CG2 ILE A  99     2129   2896   2223   -491    163   -184       C  
ATOM    793  CD1 ILE A  99      11.449  27.855  18.709  1.00 25.31           C  
ANISOU  793  CD1 ILE A  99     3122   3496   2996   -527     93    -52       C  
ATOM    794  N   PRO A 100       5.688  29.661  18.342  1.00 18.45           N  
ANISOU  794  N   PRO A 100     1790   2987   2233   -592    220   -290       N  
ATOM    795  CA  PRO A 100       4.759  30.530  17.602  1.00 17.80           C  
ANISOU  795  CA  PRO A 100     1612   2952   2198   -525    191   -386       C  
ATOM    796  C   PRO A 100       5.477  31.422  16.592  1.00 18.73           C  
ANISOU  796  C   PRO A 100     1789   3002   2327   -408    116   -410       C  
ATOM    797  O   PRO A 100       6.551  31.919  16.883  1.00 16.38           O  
ANISOU  797  O   PRO A 100     1568   2666   1989   -364    115   -382       O  
ATOM    798  CB  PRO A 100       4.110  31.360  18.723  1.00 20.06           C  
ANISOU  798  CB  PRO A 100     1813   3363   2445   -515    262   -436       C  
ATOM    799  CG  PRO A 100       4.186  30.471  19.918  1.00 25.50           C  
ANISOU  799  CG  PRO A 100     2520   4093   3076   -627    342   -361       C  
ATOM    800  CD  PRO A 100       5.555  29.858  19.802  1.00 20.41           C  
ANISOU  800  CD  PRO A 100     2017   3329   2408   -631    305   -272       C  
ATOM    801  N   LEU A 101       4.898  31.629  15.406  1.00 17.45           N  
ANISOU  801  N   LEU A 101     1590   2826   2216   -361     52   -461       N  
ATOM    802  CA  LEU A 101       5.525  32.447  14.353  1.00 17.20           C  
ANISOU  802  CA  LEU A 101     1619   2732   2185   -259    -18   -470       C  
ATOM    803  C   LEU A 101       5.937  33.821  14.861  1.00 17.01           C  
ANISOU  803  C   LEU A 101     1609   2717   2136   -180     -9   -488       C  
ATOM    804  O   LEU A 101       7.046  34.241  14.535  1.00 14.74           O  
ANISOU  804  O   LEU A 101     1410   2362   1828   -138    -31   -451       O  
ATOM    805  CB  LEU A 101       4.630  32.563  13.099  1.00 19.39           C  
ANISOU  805  CB  LEU A 101     1845   3014   2510   -213    -92   -528       C  
ATOM    806  CG  LEU A 101       5.088  33.571  12.042  1.00 25.14           C  
ANISOU  806  CG  LEU A 101     2632   3694   3227   -104   -162   -532       C  
ATOM    807  CD1 LEU A 101       6.310  33.079  11.307  1.00 25.30           C  
ANISOU  807  CD1 LEU A 101     2763   3636   3214   -106   -184   -470       C  
ATOM    808  CD2 LEU A 101       3.980  33.851  11.060  1.00 31.48           C  
ANISOU  808  CD2 LEU A 101     3369   4525   4068    -49   -236   -599       C  
ATOM    809  N   PRO A 102       5.140  34.551  15.662  1.00 14.82           N  
ANISOU  809  N   PRO A 102     1246   2522   1864   -159     23   -550       N  
ATOM    810  CA  PRO A 102       5.625  35.875  16.076  1.00 14.10           C  
ANISOU  810  CA  PRO A 102     1178   2420   1760    -76     16   -575       C  
ATOM    811  C   PRO A 102       6.909  35.804  16.887  1.00 15.32           C  
ANISOU  811  C   PRO A 102     1416   2541   1863   -101     56   -518       C  
ATOM    812  O   PRO A 102       7.741  36.715  16.819  1.00 13.19           O  
ANISOU  812  O   PRO A 102     1203   2215   1592    -40     30   -515       O  
ATOM    813  CB  PRO A 102       4.465  36.422  16.911  1.00 16.71           C  
ANISOU  813  CB  PRO A 102     1387   2861   2102    -59     51   -666       C  
ATOM    814  CG  PRO A 102       3.254  35.708  16.358  1.00 21.43           C  
ANISOU  814  CG  PRO A 102     1892   3510   2742    -99     41   -700       C  
ATOM    815  CD  PRO A 102       3.727  34.337  16.075  1.00 17.18           C  
ANISOU  815  CD  PRO A 102     1413   2925   2189   -195     56   -616       C  
ATOM    816  N   LEU A 103       7.109  34.693  17.636  1.00 13.91           N  
ANISOU  816  N   LEU A 103     1252   2390   1646   -192    112   -469       N  
ATOM    817  CA  LEU A 103       8.317  34.505  18.425  1.00 13.07           C  
ANISOU  817  CA  LEU A 103     1225   2254   1487   -212    138   -415       C  
ATOM    818  C   LEU A 103       9.478  34.110  17.525  1.00 13.11           C  
ANISOU  818  C   LEU A 103     1327   2154   1502   -205     93   -358       C  
ATOM    819  O   LEU A 103      10.588  34.617  17.697  1.00 12.36           O  
ANISOU  819  O   LEU A 103     1291   2015   1391   -170     83   -343       O  
ATOM    820  CB  LEU A 103       8.074  33.524  19.588  1.00 14.08           C  
ANISOU  820  CB  LEU A 103     1340   2450   1562   -305    207   -378       C  
ATOM    821  CG  LEU A 103       9.265  33.362  20.561  1.00 14.24           C  
ANISOU  821  CG  LEU A 103     1440   2452   1516   -315    227   -328       C  
ATOM    822  CD1 LEU A 103       9.642  34.703  21.200  1.00 16.30           C  
ANISOU  822  CD1 LEU A 103     1693   2744   1756   -236    227   -390       C  
ATOM    823  CD2 LEU A 103       8.934  32.348  21.658  1.00 17.60           C  
ANISOU  823  CD2 LEU A 103     1863   2944   1880   -411    290   -274       C  
ATOM    824  N   ILE A 104       9.224  33.243  16.533  1.00 12.62           N  
ANISOU  824  N   ILE A 104     1270   2056   1467   -234     63   -336       N  
ATOM    825  CA  ILE A 104      10.267  32.916  15.570  1.00 11.08           C  
ANISOU  825  CA  ILE A 104     1155   1777   1277   -217     20   -299       C  
ATOM    826  C   ILE A 104      10.730  34.200  14.899  1.00 11.84           C  
ANISOU  826  C   ILE A 104     1275   1841   1383   -135    -13   -318       C  
ATOM    827  O   ILE A 104      11.929  34.428  14.738  1.00 10.70           O  
ANISOU  827  O   ILE A 104     1194   1647   1226   -116    -19   -289       O  
ATOM    828  CB  ILE A 104       9.714  31.948  14.490  1.00 12.66           C  
ANISOU  828  CB  ILE A 104     1345   1957   1510   -244    -17   -300       C  
ATOM    829  CG1 ILE A 104       9.337  30.602  15.100  1.00 13.55           C  
ANISOU  829  CG1 ILE A 104     1445   2076   1629   -338      9   -271       C  
ATOM    830  CG2 ILE A 104      10.762  31.801  13.346  1.00 12.31           C  
ANISOU  830  CG2 ILE A 104     1375   1844   1461   -207    -62   -280       C  
ATOM    831  CD1 ILE A 104       8.781  29.529  14.155  1.00 15.16           C  
ANISOU  831  CD1 ILE A 104     1633   2249   1877   -377    -33   -280       C  
ATOM    832  N   LYS A 105       9.770  35.053  14.511  1.00 11.24           N  
ANISOU  832  N   LYS A 105     1145   1793   1335    -86    -37   -365       N  
ATOM    833  CA  LYS A 105      10.126  36.282  13.800  1.00 10.81           C  
ANISOU  833  CA  LYS A 105     1122   1692   1293    -11    -78   -370       C  
ATOM    834  C   LYS A 105      10.934  37.232  14.702  1.00 11.88           C  
ANISOU  834  C   LYS A 105     1281   1808   1425     12    -56   -374       C  
ATOM    835  O   LYS A 105      11.920  37.813  14.258  1.00 11.39           O  
ANISOU  835  O   LYS A 105     1278   1684   1366     35    -72   -344       O  
ATOM    836  CB  LYS A 105       8.834  36.941  13.296  1.00 13.29           C  
ANISOU  836  CB  LYS A 105     1372   2035   1642     43   -121   -424       C  
ATOM    837  CG  LYS A 105       9.045  38.196  12.461  1.00 14.81           C  
ANISOU  837  CG  LYS A 105     1607   2170   1852    122   -178   -418       C  
ATOM    838  CD  LYS A 105       7.743  38.766  11.907  1.00 15.30           C  
ANISOU  838  CD  LYS A 105     1609   2255   1949    187   -238   -473       C  
ATOM    839  CE  LYS A 105       7.158  37.812  10.900  1.00 14.40           C  
ANISOU  839  CE  LYS A 105     1481   2165   1826    170   -271   -471       C  
ATOM    840  NZ  LYS A 105       6.103  38.468  10.090  1.00 20.11           N1+
ANISOU  840  NZ  LYS A 105     2168   2897   2578    249   -352   -515       N1+
ATOM    841  N   SER A 106      10.515  37.381  15.963  1.00 11.02           N  
ANISOU  841  N   SER A 106     1121   1759   1307      2    -18   -415       N  
ATOM    842  CA  SER A 106      11.250  38.205  16.922  1.00 10.58           C  
ANISOU  842  CA  SER A 106     1081   1693   1244     25     -3   -434       C  
ATOM    843  C   SER A 106      12.669  37.675  17.096  1.00 11.37           C  
ANISOU  843  C   SER A 106     1252   1750   1317    -11     11   -380       C  
ATOM    844  O   SER A 106      13.640  38.448  17.070  1.00 11.07           O  
ANISOU  844  O   SER A 106     1253   1658   1296     15     -3   -377       O  
ATOM    845  CB  SER A 106      10.538  38.154  18.260  1.00 12.45           C  
ANISOU  845  CB  SER A 106     1251   2026   1452     11     44   -487       C  
ATOM    846  OG  SER A 106      11.287  38.877  19.236  1.00 12.13           O  
ANISOU  846  OG  SER A 106     1228   1984   1397     36     53   -516       O  
ATOM    847  N   TYR A 107      12.812  36.367  17.266  1.00 10.45           N  
ANISOU  847  N   TYR A 107     1151   1652   1167    -70     34   -339       N  
ATOM    848  CA  TYR A 107      14.140  35.804  17.431  1.00 10.27           C  
ANISOU  848  CA  TYR A 107     1191   1589   1124    -93     37   -297       C  
ATOM    849  C   TYR A 107      14.995  36.025  16.202  1.00 10.31           C  
ANISOU  849  C   TYR A 107     1240   1525   1154    -72      7   -273       C  
ATOM    850  O   TYR A 107      16.160  36.423  16.311  1.00 10.70           O  
ANISOU  850  O   TYR A 107     1322   1538   1207    -62      5   -267       O  
ATOM    851  CB  TYR A 107      14.084  34.317  17.786  1.00 11.61           C  
ANISOU  851  CB  TYR A 107     1375   1775   1261   -155     53   -257       C  
ATOM    852  CG  TYR A 107      13.662  33.970  19.195  1.00 10.48           C  
ANISOU  852  CG  TYR A 107     1212   1700   1071   -191     94   -256       C  
ATOM    853  CD1 TYR A 107      13.565  34.947  20.182  1.00 12.16           C  
ANISOU  853  CD1 TYR A 107     1395   1965   1259   -160    114   -303       C  
ATOM    854  CD2 TYR A 107      13.369  32.657  19.547  1.00 11.79           C  
ANISOU  854  CD2 TYR A 107     1391   1878   1211   -259    110   -207       C  
ATOM    855  CE1 TYR A 107      13.245  34.607  21.493  1.00 12.57           C  
ANISOU  855  CE1 TYR A 107     1434   2096   1246   -192    156   -301       C  
ATOM    856  CE2 TYR A 107      13.018  32.316  20.851  1.00 13.00           C  
ANISOU  856  CE2 TYR A 107     1535   2099   1304   -301    153   -190       C  
ATOM    857  CZ  TYR A 107      12.962  33.292  21.818  1.00 13.12           C  
ANISOU  857  CZ  TYR A 107     1522   2183   1280   -267    180   -237       C  
ATOM    858  OH  TYR A 107      12.649  32.920  23.108  1.00 14.69           O  
ANISOU  858  OH  TYR A 107     1716   2465   1400   -308    227   -218       O  
ATOM    859  N   LEU A 108      14.438  35.786  15.000  1.00  9.56           N  
ANISOU  859  N   LEU A 108     1143   1418   1071    -67    -16   -262       N  
ATOM    860  CA  LEU A 108      15.238  35.991  13.802  1.00  9.64           C  
ANISOU  860  CA  LEU A 108     1196   1380   1086    -49    -36   -235       C  
ATOM    861  C   LEU A 108      15.687  37.452  13.654  1.00 10.42           C  
ANISOU  861  C   LEU A 108     1308   1440   1209    -12    -44   -237       C  
ATOM    862  O   LEU A 108      16.848  37.736  13.320  1.00 10.49           O  
ANISOU  862  O   LEU A 108     1353   1413   1222    -16    -38   -213       O  
ATOM    863  CB  LEU A 108      14.468  35.530  12.577  1.00  9.87           C  
ANISOU  863  CB  LEU A 108     1222   1417   1112    -42    -65   -230       C  
ATOM    864  CG  LEU A 108      15.185  35.664  11.220  1.00 10.84           C  
ANISOU  864  CG  LEU A 108     1391   1511   1217    -23    -83   -202       C  
ATOM    865  CD1 LEU A 108      16.395  34.734  11.148  1.00 12.94           C  
ANISOU  865  CD1 LEU A 108     1687   1766   1465    -50    -66   -190       C  
ATOM    866  CD2 LEU A 108      14.224  35.302  10.103  1.00 11.28           C  
ANISOU  866  CD2 LEU A 108     1438   1587   1262     -6   -121   -210       C  
ATOM    867  N   PHE A 109      14.748  38.379  13.948  1.00  9.96           N  
ANISOU  867  N   PHE A 109     1216   1390   1177     23    -60   -270       N  
ATOM    868  CA  PHE A 109      15.029  39.805  13.871  1.00  9.89           C  
ANISOU  868  CA  PHE A 109     1222   1328   1208     61    -80   -275       C  
ATOM    869  C   PHE A 109      16.180  40.186  14.808  1.00 10.53           C  
ANISOU  869  C   PHE A 109     1314   1385   1301     46    -59   -287       C  
ATOM    870  O   PHE A 109      17.133  40.891  14.420  1.00 10.66           O  
ANISOU  870  O   PHE A 109     1364   1342   1345     43    -63   -263       O  
ATOM    871  CB  PHE A 109      13.731  40.539  14.222  1.00 12.34           C  
ANISOU  871  CB  PHE A 109     1483   1659   1548    110   -107   -329       C  
ATOM    872  CG  PHE A 109      13.793  42.032  14.106  1.00 14.12           C  
ANISOU  872  CG  PHE A 109     1724   1814   1828    160   -147   -342       C  
ATOM    873  CD1 PHE A 109      13.973  42.637  12.863  1.00 15.69           C  
ANISOU  873  CD1 PHE A 109     1975   1944   2041    179   -185   -285       C  
ATOM    874  CD2 PHE A 109      13.520  42.836  15.205  1.00 16.81           C  
ANISOU  874  CD2 PHE A 109     2024   2158   2204    194   -153   -414       C  
ATOM    875  CE1 PHE A 109      13.965  44.037  12.736  1.00 19.45           C  
ANISOU  875  CE1 PHE A 109     2475   2337   2578    223   -231   -287       C  
ATOM    876  CE2 PHE A 109      13.541  44.238  15.078  1.00 20.26           C  
ANISOU  876  CE2 PHE A 109     2478   2512   2708    245   -203   -433       C  
ATOM    877  CZ  PHE A 109      13.760  44.803  13.844  1.00 19.45           C  
ANISOU  877  CZ  PHE A 109     2437   2325   2629    256   -243   -363       C  
ATOM    878  N   GLN A 110      16.118  39.699  16.051  1.00 10.12           N  
ANISOU  878  N   GLN A 110     1234   1386   1228     33    -35   -324       N  
ATOM    879  CA  GLN A 110      17.149  39.991  17.043  1.00  9.65           C  
ANISOU  879  CA  GLN A 110     1180   1316   1172     26    -25   -348       C  
ATOM    880  C   GLN A 110      18.473  39.350  16.670  1.00 11.06           C  
ANISOU  880  C   GLN A 110     1393   1469   1339     -8    -14   -308       C  
ATOM    881  O   GLN A 110      19.517  40.009  16.819  1.00 11.02           O  
ANISOU  881  O   GLN A 110     1397   1423   1367     -9    -18   -317       O  
ATOM    882  CB  GLN A 110      16.689  39.450  18.380  1.00 10.52           C  
ANISOU  882  CB  GLN A 110     1259   1503   1236     20     -3   -385       C  
ATOM    883  CG  GLN A 110      15.553  40.270  19.019  1.00 11.55           C  
ANISOU  883  CG  GLN A 110     1336   1675   1377     60     -6   -453       C  
ATOM    884  CD  GLN A 110      15.214  39.649  20.337  1.00 11.05           C  
ANISOU  884  CD  GLN A 110     1245   1705   1247     43     29   -480       C  
ATOM    885  NE2 GLN A 110      14.057  39.004  20.461  1.00 12.05           N  
ANISOU  885  NE2 GLN A 110     1332   1904   1342     22     57   -479       N  
ATOM    886  OE1 GLN A 110      16.047  39.709  21.281  1.00 12.50           O  
ANISOU  886  OE1 GLN A 110     1444   1901   1404     43     32   -500       O  
ATOM    887  N   LEU A 111      18.467  38.131  16.136  1.00 10.10           N  
ANISOU  887  N   LEU A 111     1286   1368   1183    -33     -5   -272       N  
ATOM    888  CA  LEU A 111      19.715  37.504  15.734  1.00 10.26           C  
ANISOU  888  CA  LEU A 111     1332   1370   1197    -53      0   -249       C  
ATOM    889  C   LEU A 111      20.351  38.257  14.565  1.00 10.96           C  
ANISOU  889  C   LEU A 111     1436   1414   1313    -54      2   -224       C  
ATOM    890  O   LEU A 111      21.576  38.408  14.524  1.00 11.12           O  
ANISOU  890  O   LEU A 111     1459   1416   1350    -68     13   -225       O  
ATOM    891  CB  LEU A 111      19.461  36.043  15.389  1.00 11.13           C  
ANISOU  891  CB  LEU A 111     1453   1503   1272    -72     -1   -227       C  
ATOM    892  CG  LEU A 111      19.059  35.207  16.612  1.00 13.12           C  
ANISOU  892  CG  LEU A 111     1701   1790   1493    -89      1   -233       C  
ATOM    893  CD1 LEU A 111      18.579  33.870  16.191  1.00 16.10           C  
ANISOU  893  CD1 LEU A 111     2090   2171   1854   -114     -7   -208       C  
ATOM    894  CD2 LEU A 111      20.195  35.044  17.573  1.00 17.65           C  
ANISOU  894  CD2 LEU A 111     2288   2361   2058    -87     -5   -246       C  
ATOM    895  N   LEU A 112      19.528  38.720  13.610  1.00  9.98           N  
ANISOU  895  N   LEU A 112     1322   1279   1191    -39     -8   -199       N  
ATOM    896  CA  LEU A 112      20.053  39.512  12.515  1.00 10.34           C  
ANISOU  896  CA  LEU A 112     1394   1284   1250    -44     -5   -159       C  
ATOM    897  C   LEU A 112      20.671  40.818  13.031  1.00 10.99           C  
ANISOU  897  C   LEU A 112     1473   1310   1392    -48     -6   -168       C  
ATOM    898  O   LEU A 112      21.650  41.297  12.478  1.00 11.68           O  
ANISOU  898  O   LEU A 112     1575   1365   1498    -77     13   -138       O  
ATOM    899  CB  LEU A 112      18.984  39.794  11.447  1.00 10.38           C  
ANISOU  899  CB  LEU A 112     1419   1287   1239    -19    -30   -127       C  
ATOM    900  CG  LEU A 112      18.590  38.569  10.645  1.00 10.36           C  
ANISOU  900  CG  LEU A 112     1421   1332   1183    -19    -32   -119       C  
ATOM    901  CD1 LEU A 112      17.296  38.845   9.906  1.00 12.66           C  
ANISOU  901  CD1 LEU A 112     1718   1630   1464     16    -72   -109       C  
ATOM    902  CD2 LEU A 112      19.703  38.256   9.625  1.00 11.29           C  
ANISOU  902  CD2 LEU A 112     1565   1459   1266    -41     -6    -87       C  
ATOM    903  N   GLN A 113      20.087  41.434  14.076  1.00 10.52           N  
ANISOU  903  N   GLN A 113     1392   1240   1365    -22    -27   -216       N  
ATOM    904  CA  GLN A 113      20.679  42.635  14.656  1.00 11.29           C  
ANISOU  904  CA  GLN A 113     1483   1276   1528    -23    -39   -242       C  
ATOM    905  C   GLN A 113      22.057  42.310  15.243  1.00 11.93           C  
ANISOU  905  C   GLN A 113     1547   1366   1618    -56    -18   -266       C  
ATOM    906  O   GLN A 113      22.982  43.100  15.051  1.00 12.07           O  
ANISOU  906  O   GLN A 113     1566   1330   1690    -84    -13   -259       O  
ATOM    907  CB  GLN A 113      19.780  43.198  15.763  1.00 12.46           C  
ANISOU  907  CB  GLN A 113     1602   1431   1700     22    -68   -312       C  
ATOM    908  CG  GLN A 113      18.544  43.896  15.209  1.00 13.14           C  
ANISOU  908  CG  GLN A 113     1696   1490   1808     66   -104   -305       C  
ATOM    909  CD  GLN A 113      17.709  44.345  16.354  1.00 15.12           C  
ANISOU  909  CD  GLN A 113     1902   1767   2076    114   -125   -392       C  
ATOM    910  NE2 GLN A 113      16.513  43.833  16.417  1.00 17.57           N  
ANISOU  910  NE2 GLN A 113     2183   2144   2349    140   -125   -411       N  
ATOM    911  OE1 GLN A 113      18.178  45.082  17.228  1.00 16.69           O  
ANISOU  911  OE1 GLN A 113     2087   1937   2319    125   -139   -450       O  
ATOM    912  N   GLY A 114      22.201  41.188  15.933  1.00 11.47           N  
ANISOU  912  N   GLY A 114     1475   1371   1513    -55     -9   -292       N  
ATOM    913  CA  GLY A 114      23.505  40.817  16.497  1.00 11.88           C  
ANISOU  913  CA  GLY A 114     1509   1433   1571    -73     -2   -321       C  
ATOM    914  C   GLY A 114      24.510  40.567  15.383  1.00 13.06           C  
ANISOU  914  C   GLY A 114     1663   1573   1727   -109     26   -282       C  
ATOM    915  O   GLY A 114      25.673  40.988  15.490  1.00 13.08           O  
ANISOU  915  O   GLY A 114     1641   1555   1774   -135     34   -302       O  
ATOM    916  N   LEU A 115      24.105  39.870  14.308  1.00 11.05           N  
ANISOU  916  N   LEU A 115     1431   1342   1427   -112     41   -235       N  
ATOM    917  CA  LEU A 115      25.011  39.644  13.201  1.00 11.93           C  
ANISOU  917  CA  LEU A 115     1541   1463   1529   -142     74   -206       C  
ATOM    918  C   LEU A 115      25.373  40.951  12.517  1.00 12.25           C  
ANISOU  918  C   LEU A 115     1589   1452   1614   -176     95   -165       C  
ATOM    919  O   LEU A 115      26.554  41.153  12.187  1.00 13.16           O  
ANISOU  919  O   LEU A 115     1680   1568   1753   -217    128   -164       O  
ATOM    920  CB  LEU A 115      24.406  38.703  12.153  1.00 11.45           C  
ANISOU  920  CB  LEU A 115     1505   1441   1405   -130     80   -173       C  
ATOM    921  CG  LEU A 115      24.310  37.225  12.510  1.00 14.29           C  
ANISOU  921  CG  LEU A 115     1861   1841   1729   -110     63   -204       C  
ATOM    922  CD1 LEU A 115      23.870  36.436  11.290  1.00 14.45           C  
ANISOU  922  CD1 LEU A 115     1900   1892   1700   -103     66   -183       C  
ATOM    923  CD2 LEU A 115      25.601  36.665  13.060  1.00 17.65           C  
ANISOU  923  CD2 LEU A 115     2256   2279   2170   -113     64   -248       C  
ATOM    924  N   ALA A 116      24.391  41.842  12.278  1.00 11.72           N  
ANISOU  924  N   ALA A 116     1554   1337   1561   -163     74   -130       N  
ATOM    925  CA  ALA A 116      24.714  43.086  11.583  1.00 12.12           C  
ANISOU  925  CA  ALA A 116     1628   1322   1656   -199     85    -75       C  
ATOM    926  C   ALA A 116      25.749  43.866  12.371  1.00 14.17           C  
ANISOU  926  C   ALA A 116     1851   1532   2000   -236     88   -114       C  
ATOM    927  O   ALA A 116      26.670  44.445  11.777  1.00 14.02           O  
ANISOU  927  O   ALA A 116     1827   1485   2016   -296    124    -76       O  
ATOM    928  CB  ALA A 116      23.475  43.935  11.383  1.00 14.47           C  
ANISOU  928  CB  ALA A 116     1967   1563   1969   -164     41    -44       C  
ATOM    929  N   PHE A 117      25.624  43.866  13.725  1.00 12.86           N  
ANISOU  929  N   PHE A 117     1656   1365   1866   -203     52   -194       N  
ATOM    930  CA  PHE A 117      26.589  44.579  14.558  1.00 13.06           C  
ANISOU  930  CA  PHE A 117     1641   1348   1973   -229     42   -250       C  
ATOM    931  C   PHE A 117      27.971  43.938  14.421  1.00 13.15           C  
ANISOU  931  C   PHE A 117     1606   1407   1982   -270     81   -268       C  
ATOM    932  O   PHE A 117      28.962  44.640  14.160  1.00 13.50           O  
ANISOU  932  O   PHE A 117     1622   1413   2093   -330    105   -263       O  
ATOM    933  CB  PHE A 117      26.116  44.522  16.028  1.00 14.14           C  
ANISOU  933  CB  PHE A 117     1758   1500   2114   -173     -5   -339       C  
ATOM    934  CG  PHE A 117      27.163  45.003  17.006  1.00 14.82           C  
ANISOU  934  CG  PHE A 117     1797   1565   2268   -188    -25   -417       C  
ATOM    935  CD1 PHE A 117      27.386  46.356  17.199  1.00 17.14           C  
ANISOU  935  CD1 PHE A 117     2083   1765   2664   -209    -51   -441       C  
ATOM    936  CD2 PHE A 117      27.961  44.097  17.688  1.00 16.98           C  
ANISOU  936  CD2 PHE A 117     2034   1905   2511   -180    -27   -470       C  
ATOM    937  CE1 PHE A 117      28.399  46.797  18.074  1.00 18.57           C  
ANISOU  937  CE1 PHE A 117     2213   1926   2916   -226    -76   -525       C  
ATOM    938  CE2 PHE A 117      28.973  44.530  18.535  1.00 19.38           C  
ANISOU  938  CE2 PHE A 117     2289   2195   2878   -190    -53   -549       C  
ATOM    939  CZ  PHE A 117      29.217  45.871  18.687  1.00 18.32           C  
ANISOU  939  CZ  PHE A 117     2140   1973   2847   -217    -74   -578       C  
ATOM    940  N   CYS A 118      28.087  42.631  14.661  1.00 12.31           N  
ANISOU  940  N   CYS A 118     1487   1381   1811   -240     84   -297       N  
ATOM    941  CA ACYS A 118      29.401  42.004  14.578  0.60 11.50           C  
ANISOU  941  CA ACYS A 118     1332   1324   1713   -264    109   -331       C  
ATOM    942  CA BCYS A 118      29.448  42.084  14.592  0.40 15.68           C  
ANISOU  942  CA BCYS A 118     1859   1849   2248   -267    109   -332       C  
ATOM    943  C   CYS A 118      30.028  42.124  13.194  1.00 14.63           C  
ANISOU  943  C   CYS A 118     1720   1735   2103   -322    173   -274       C  
ATOM    944  O   CYS A 118      31.220  42.407  13.050  1.00 14.27           O  
ANISOU  944  O   CYS A 118     1618   1697   2107   -372    205   -296       O  
ATOM    945  CB ACYS A 118      29.346  40.554  15.052  0.60 10.76           C  
ANISOU  945  CB ACYS A 118     1237   1297   1554   -213     86   -368       C  
ATOM    946  CB BCYS A 118      29.489  40.677  15.141  0.40 19.02           C  
ANISOU  946  CB BCYS A 118     2276   2339   2612   -217     85   -375       C  
ATOM    947  SG ACYS A 118      29.001  40.372  16.841  0.60 13.78           S  
ANISOU  947  SG ACYS A 118     1620   1683   1932   -158     20   -437       S  
ATOM    948  SG BCYS A 118      28.500  39.541  14.175  0.40 24.80           S  
ANISOU  948  SG BCYS A 118     3059   3114   3252   -191     99   -318       S  
ATOM    949  N   HIS A 119      29.210  41.871  12.176  1.00 12.20           N  
ANISOU  949  N   HIS A 119     1464   1442   1729   -314    192   -204       N  
ATOM    950  CA  HIS A 119      29.699  41.949  10.800  1.00 11.98           C  
ANISOU  950  CA  HIS A 119     1439   1446   1669   -364    256   -143       C  
ATOM    951  C   HIS A 119      30.191  43.351  10.438  1.00 15.76           C  
ANISOU  951  C   HIS A 119     1916   1856   2215   -441    288    -89       C  
ATOM    952  O   HIS A 119      31.172  43.489   9.698  1.00 16.37           O  
ANISOU  952  O   HIS A 119     1958   1968   2294   -506    353    -66       O  
ATOM    953  CB  HIS A 119      28.609  41.474   9.834  1.00 11.92           C  
ANISOU  953  CB  HIS A 119     1493   1465   1570   -331    255    -83       C  
ATOM    954  CG  HIS A 119      28.317  40.015   9.952  1.00 11.35           C  
ANISOU  954  CG  HIS A 119     1416   1459   1439   -275    234   -132       C  
ATOM    955  CD2 HIS A 119      28.955  39.057  10.668  1.00 12.32           C  
ANISOU  955  CD2 HIS A 119     1494   1617   1570   -250    218   -208       C  
ATOM    956  ND1 HIS A 119      27.279  39.445   9.261  1.00 12.66           N  
ANISOU  956  ND1 HIS A 119     1627   1648   1534   -240    219   -101       N  
ATOM    957  CE1 HIS A 119      27.302  38.153   9.568  1.00 11.64           C  
ANISOU  957  CE1 HIS A 119     1482   1562   1379   -202    197   -157       C  
ATOM    958  NE2 HIS A 119      28.291  37.868  10.421  1.00 11.38           N  
ANISOU  958  NE2 HIS A 119     1399   1534   1390   -203    193   -218       N  
ATOM    959  N   SER A 120      29.559  44.409  11.035  1.00 14.76           N  
ANISOU  959  N   SER A 120     1822   1631   2154   -436    241    -77       N  
ATOM    960  CA  SER A 120      29.992  45.800  10.790  1.00 14.62           C  
ANISOU  960  CA  SER A 120     1811   1520   2223   -511    256    -26       C  
ATOM    961  C   SER A 120      31.396  46.047  11.350  1.00 18.23           C  
ANISOU  961  C   SER A 120     2182   1977   2768   -572    279    -92       C  
ATOM    962  O   SER A 120      32.069  46.970  10.886  1.00 19.96           O  
ANISOU  962  O   SER A 120     2390   2143   3052   -661    318    -43       O  
ATOM    963  CB  SER A 120      28.990  46.797  11.356  1.00 18.18           C  
ANISOU  963  CB  SER A 120     2312   1861   2734   -476    185    -20       C  
ATOM    964  OG  SER A 120      29.082  46.950  12.762  1.00 19.00           O  
ANISOU  964  OG  SER A 120     2373   1939   2905   -442    132   -126       O  
ATOM    965  N   HIS A 121      31.843  45.216  12.311  1.00 15.88           N  
ANISOU  965  N   HIS A 121     1824   1738   2472   -527    254   -198       N  
ATOM    966  CA  HIS A 121      33.171  45.290  12.924  1.00 18.23           C  
ANISOU  966  CA  HIS A 121     2029   2050   2848   -566    262   -282       C  
ATOM    967  C   HIS A 121      34.093  44.225  12.339  1.00 20.92           C  
ANISOU  967  C   HIS A 121     2308   2505   3135   -576    318   -307       C  
ATOM    968  O   HIS A 121      35.164  43.954  12.872  1.00 21.83           O  
ANISOU  968  O   HIS A 121     2336   2659   3299   -584    316   -396       O  
ATOM    969  CB  HIS A 121      33.046  45.162  14.448  1.00 18.47           C  
ANISOU  969  CB  HIS A 121     2038   2066   2913   -497    180   -389       C  
ATOM    970  CG  HIS A 121      32.394  46.351  15.081  1.00 21.98           C  
ANISOU  970  CG  HIS A 121     2519   2403   3430   -493    126   -394       C  
ATOM    971  CD2 HIS A 121      31.142  46.504  15.565  1.00 22.75           C  
ANISOU  971  CD2 HIS A 121     2676   2469   3499   -425     75   -393       C  
ATOM    972  ND1 HIS A 121      33.065  47.560  15.192  1.00 26.25           N  
ANISOU  972  ND1 HIS A 121     3026   2855   4094   -566    124   -406       N  
ATOM    973  CE1 HIS A 121      32.204  48.398  15.738  1.00 25.74           C  
ANISOU  973  CE1 HIS A 121     3008   2701   4072   -532     63   -416       C  
ATOM    974  NE2 HIS A 121      31.036  47.817  15.982  1.00 24.74           N  
ANISOU  974  NE2 HIS A 121     2934   2612   3855   -445     35   -412       N  
ATOM    975  N   ARG A 122      33.628  43.571  11.255  1.00 18.31           N  
ANISOU  975  N   ARG A 122     2021   2234   2702   -563    360   -241       N  
ATOM    976  CA  ARG A 122      34.384  42.545  10.519  1.00 18.44           C  
ANISOU  976  CA  ARG A 122     1985   2366   2657   -563    416   -267       C  
ATOM    977  C   ARG A 122      34.668  41.302  11.388  1.00 21.64           C  
ANISOU  977  C   ARG A 122     2349   2825   3050   -479    360   -376       C  
ATOM    978  O   ARG A 122      35.685  40.619  11.205  1.00 24.11           O  
ANISOU  978  O   ARG A 122     2583   3215   3361   -476    385   -443       O  
ATOM    979  CB  ARG A 122      35.655  43.150   9.857  1.00 22.57           C  
ANISOU  979  CB  ARG A 122     2428   2919   3227   -668    503   -258       C  
ATOM    980  CG  ARG A 122      35.333  44.375   9.000  1.00 27.15           C  
ANISOU  980  CG  ARG A 122     3068   3433   3816   -758    553   -128       C  
ATOM    981  CD  ARG A 122      36.538  45.309   8.816  1.00 40.58           C  
ANISOU  981  CD  ARG A 122     4690   5118   5611   -882    620   -119       C  
ATOM    982  NE  ARG A 122      37.137  45.740  10.089  1.00 48.95           N  
ANISOU  982  NE  ARG A 122     5679   6116   6804   -888    563   -220       N  
ATOM    983  CZ  ARG A 122      36.693  46.743  10.846  1.00 61.01           C  
ANISOU  983  CZ  ARG A 122     7245   7512   8423   -896    499   -213       C  
ATOM    984  NH1 ARG A 122      35.626  47.443  10.478  1.00 45.09           N1+
ANISOU  984  NH1 ARG A 122     5339   5403   6389   -896    479   -108       N1+
ATOM    985  NH2 ARG A 122      37.310  47.048  11.980  1.00 50.72           N  
ANISOU  985  NH2 ARG A 122     5870   6170   7230   -896    445   -320       N  
ATOM    986  N   VAL A 123      33.763  40.990  12.315  1.00 17.64           N  
ANISOU  986  N   VAL A 123     1895   2279   2529   -408    284   -393       N  
ATOM    987  CA  VAL A 123      33.867  39.806  13.180  1.00 16.93           C  
ANISOU  987  CA  VAL A 123     1791   2225   2416   -329    223   -472       C  
ATOM    988  C   VAL A 123      32.793  38.815  12.746  1.00 17.37           C  
ANISOU  988  C   VAL A 123     1918   2302   2381   -275    208   -432       C  
ATOM    989  O   VAL A 123      31.607  39.154  12.702  1.00 16.82           O  
ANISOU  989  O   VAL A 123     1916   2191   2283   -268    196   -372       O  
ATOM    990  CB  VAL A 123      33.772  40.152  14.690  1.00 19.52           C  
ANISOU  990  CB  VAL A 123     2119   2505   2794   -297    149   -526       C  
ATOM    991  CG1 VAL A 123      33.802  38.889  15.567  1.00 19.78           C  
ANISOU  991  CG1 VAL A 123     2157   2573   2786   -216     82   -585       C  
ATOM    992  CG2 VAL A 123      34.910  41.107  15.100  1.00 20.35           C  
ANISOU  992  CG2 VAL A 123     2142   2587   3002   -351    154   -583       C  
ATOM    993  N   LEU A 124      33.224  37.608  12.418  1.00 16.45           N  
ANISOU  993  N   LEU A 124     1778   2247   2226   -236    204   -474       N  
ATOM    994  CA  LEU A 124      32.341  36.529  11.989  1.00 16.53           C  
ANISOU  994  CA  LEU A 124     1845   2274   2161   -188    184   -453       C  
ATOM    995  C   LEU A 124      32.159  35.572  13.170  1.00 15.93           C  
ANISOU  995  C   LEU A 124     1788   2180   2086   -124    103   -497       C  
ATOM    996  O   LEU A 124      33.021  35.465  14.039  1.00 16.98           O  
ANISOU  996  O   LEU A 124     1876   2314   2261   -105     67   -560       O  
ATOM    997  CB  LEU A 124      33.027  35.747  10.823  1.00 19.47           C  
ANISOU  997  CB  LEU A 124     2177   2724   2496   -181    225   -484       C  
ATOM    998  CG  LEU A 124      33.096  36.338   9.417  1.00 25.04           C  
ANISOU  998  CG  LEU A 124     2879   3476   3160   -236    311   -430       C  
ATOM    999  CD1 LEU A 124      34.024  37.541   9.336  1.00 28.12           C  
ANISOU  999  CD1 LEU A 124     3211   3867   3607   -316    373   -418       C  
ATOM   1000  CD2 LEU A 124      33.626  35.310   8.461  1.00 25.63           C  
ANISOU 1000  CD2 LEU A 124     2916   3639   3181   -206    336   -484       C  
ATOM   1001  N   HIS A 125      31.051  34.808  13.189  1.00 13.64           N  
ANISOU 1001  N   HIS A 125     1562   1874   1746    -92     71   -464       N  
ATOM   1002  CA  HIS A 125      30.885  33.774  14.209  1.00 13.26           C  
ANISOU 1002  CA  HIS A 125     1541   1808   1689    -41     -1   -489       C  
ATOM   1003  C   HIS A 125      31.514  32.477  13.682  1.00 16.06           C  
ANISOU 1003  C   HIS A 125     1878   2188   2035      1    -25   -540       C  
ATOM   1004  O   HIS A 125      32.420  31.904  14.325  1.00 16.44           O  
ANISOU 1004  O   HIS A 125     1897   2238   2112     42    -75   -601       O  
ATOM   1005  CB  HIS A 125      29.414  33.572  14.587  1.00 13.59           C  
ANISOU 1005  CB  HIS A 125     1652   1818   1691    -38    -21   -431       C  
ATOM   1006  CG  HIS A 125      29.259  32.591  15.723  1.00 13.46           C  
ANISOU 1006  CG  HIS A 125     1670   1783   1662     -2    -88   -440       C  
ATOM   1007  CD2 HIS A 125      28.831  32.824  16.996  1.00 15.56           C  
ANISOU 1007  CD2 HIS A 125     1961   2036   1914      2   -116   -427       C  
ATOM   1008  ND1 HIS A 125      29.657  31.292  15.622  1.00 13.55           N  
ANISOU 1008  ND1 HIS A 125     1691   1788   1669     36   -133   -466       N  
ATOM   1009  CE1 HIS A 125      29.441  30.742  16.819  1.00 13.85           C  
ANISOU 1009  CE1 HIS A 125     1770   1800   1691     56   -189   -453       C  
ATOM   1010  NE2 HIS A 125      28.918  31.630  17.659  1.00 14.58           N  
ANISOU 1010  NE2 HIS A 125     1872   1898   1769     35   -175   -428       N  
ATOM   1011  N   ARG A 126      31.024  32.009  12.515  1.00 13.08           N  
ANISOU 1011  N   ARG A 126     1519   1831   1621      1      0   -522       N  
ATOM   1012  CA AARG A 126      31.556  30.821  11.817  0.50 13.67           C  
ANISOU 1012  CA AARG A 126     1573   1934   1687     46    -21   -583       C  
ATOM   1013  CA BARG A 126      31.428  30.832  11.748  0.50 14.88           C  
ANISOU 1013  CA BARG A 126     1733   2086   1836     43    -18   -576       C  
ATOM   1014  C   ARG A 126      30.948  29.482  12.261  1.00 14.42           C  
ANISOU 1014  C   ARG A 126     1726   1976   1777     91   -101   -584       C  
ATOM   1015  O   ARG A 126      31.053  28.479  11.525  1.00 15.39           O  
ANISOU 1015  O   ARG A 126     1848   2107   1893    128   -125   -629       O  
ATOM   1016  CB AARG A 126      33.107  30.753  11.873  0.50 13.88           C  
ANISOU 1016  CB AARG A 126     1515   2003   1756     68    -19   -671       C  
ATOM   1017  CB BARG A 126      32.897  30.881  11.280  0.50 20.42           C  
ANISOU 1017  CB BARG A 126     2345   2850   2563     54     12   -657       C  
ATOM   1018  CG AARG A 126      33.851  31.982  11.306  0.50 23.98           C  
ANISOU 1018  CG AARG A 126     2724   3339   3049      9     69   -673       C  
ATOM   1019  CG BARG A 126      33.838  29.823  11.821  0.50 27.83           C  
ANISOU 1019  CG BARG A 126     3249   3784   3541    122    -61   -747       C  
ATOM   1020  CD AARG A 126      35.269  32.129  11.862  0.50 33.75           C  
ANISOU 1020  CD AARG A 126     3870   4604   4349     20     59   -758       C  
ATOM   1021  CD BARG A 126      34.374  28.936  10.716  0.50 25.19           C  
ANISOU 1021  CD BARG A 126     2873   3505   3194    166    -55   -825       C  
ATOM   1022  NE AARG A 126      36.084  33.037  11.050  0.50 39.45           N  
ANISOU 1022  NE AARG A 126     4511   5393   5085    -43    154   -770       N  
ATOM   1023  NE BARG A 126      33.608  27.701  10.573  0.50 21.96           N  
ANISOU 1023  NE BARG A 126     2530   3044   2769    213   -124   -826       N  
ATOM   1024  CZ AARG A 126      36.330  34.310  11.345  0.50 47.54           C  
ANISOU 1024  CZ AARG A 126     5510   6404   6151   -113    196   -738       C  
ATOM   1025  CZ BARG A 126      34.126  26.550  10.148  0.50 32.07           C  
ANISOU 1025  CZ BARG A 126     3787   4332   4065    283   -176   -918       C  
ATOM   1026  NH1AARG A 126      35.847  34.847  12.457  0.50 39.79           N1+
ANISOU 1026  NH1AARG A 126     4571   5349   5199   -117    149   -707       N1+
ATOM   1027  NH1BARG A 126      35.411  26.469   9.824  0.50 24.16           N1+
ANISOU 1027  NH1BARG A 126     2689   3400   3088    319   -161  -1021       N1+
ATOM   1028  NH2AARG A 126      37.071  35.054  10.532  0.50 24.91           N  
ANISOU 1028  NH2AARG A 126     2572   3595   3297   -181    287   -739       N  
ATOM   1029  NH2BARG A 126      33.370  25.468  10.067  0.50 22.54           N  
ANISOU 1029  NH2BARG A 126     2647   3060   2857    318   -246   -914       N  
ATOM   1030  N   ASP A 127      30.364  29.440  13.458  1.00 13.96           N  
ANISOU 1030  N   ASP A 127     1716   1866   1722     87   -144   -541       N  
ATOM   1031  CA  ASP A 127      29.818  28.169  13.933  1.00 13.49           C  
ANISOU 1031  CA  ASP A 127     1716   1750   1660    116   -217   -528       C  
ATOM   1032  C   ASP A 127      28.503  28.376  14.639  1.00 14.07           C  
ANISOU 1032  C   ASP A 127     1846   1792   1707     76   -216   -447       C  
ATOM   1033  O   ASP A 127      28.268  27.818  15.734  1.00 14.78           O  
ANISOU 1033  O   ASP A 127     1981   1842   1792     83   -267   -418       O  
ATOM   1034  CB  ASP A 127      30.818  27.398  14.810  1.00 15.23           C  
ANISOU 1034  CB  ASP A 127     1933   1941   1912    171   -296   -576       C  
ATOM   1035  CG  ASP A 127      30.445  25.948  15.082  1.00 18.36           C  
ANISOU 1035  CG  ASP A 127     2395   2266   2316    204   -380   -564       C  
ATOM   1036  OD1 ASP A 127      29.672  25.367  14.287  1.00 17.98           O  
ANISOU 1036  OD1 ASP A 127     2372   2198   2263    192   -378   -552       O  
ATOM   1037  OD2 ASP A 127      30.889  25.401  16.129  1.00 21.63           O1-
ANISOU 1037  OD2 ASP A 127     2840   2637   2742    240   -455   -564       O1-
ATOM   1038  N   LEU A 128      27.589  29.115  14.007  1.00 12.63           N  
ANISOU 1038  N   LEU A 128     1665   1631   1502     37   -160   -408       N  
ATOM   1039  CA  LEU A 128      26.284  29.306  14.609  1.00 12.55           C  
ANISOU 1039  CA  LEU A 128     1693   1603   1471      3   -156   -346       C  
ATOM   1040  C   LEU A 128      25.511  28.031  14.583  1.00 12.31           C  
ANISOU 1040  C   LEU A 128     1706   1532   1439      0   -199   -325       C  
ATOM   1041  O   LEU A 128      25.510  27.301  13.590  1.00 13.20           O  
ANISOU 1041  O   LEU A 128     1818   1635   1561     15   -216   -354       O  
ATOM   1042  CB  LEU A 128      25.481  30.328  13.828  1.00 14.26           C  
ANISOU 1042  CB  LEU A 128     1897   1849   1672    -26   -100   -320       C  
ATOM   1043  CG  LEU A 128      25.951  31.739  14.052  1.00 19.77           C  
ANISOU 1043  CG  LEU A 128     2564   2566   2381    -37    -60   -321       C  
ATOM   1044  CD1 LEU A 128      25.179  32.681  13.148  1.00 21.46           C  
ANISOU 1044  CD1 LEU A 128     2777   2794   2583    -59    -18   -289       C  
ATOM   1045  CD2 LEU A 128      25.843  32.122  15.537  1.00 20.12           C  
ANISOU 1045  CD2 LEU A 128     2616   2600   2427    -40    -76   -314       C  
ATOM   1046  N   LYS A 129      24.769  27.768  15.661  1.00 12.45           N  
ANISOU 1046  N   LYS A 129     1761   1527   1442    -26   -216   -274       N  
ATOM   1047  CA ALYS A 129      23.957  26.571  15.820  0.60 12.02           C  
ANISOU 1047  CA ALYS A 129     1751   1424   1393    -49   -254   -239       C  
ATOM   1048  CA BLYS A 129      23.922  26.593  15.785  0.40 11.37           C  
ANISOU 1048  CA BLYS A 129     1667   1342   1309    -50   -252   -239       C  
ATOM   1049  C   LYS A 129      22.966  26.838  16.940  1.00 11.71           C  
ANISOU 1049  C   LYS A 129     1732   1398   1320    -96   -232   -176       C  
ATOM   1050  O   LYS A 129      23.251  27.712  17.792  1.00 11.37           O  
ANISOU 1050  O   LYS A 129     1678   1391   1249    -90   -210   -173       O  
ATOM   1051  CB ALYS A 129      24.846  25.335  16.123  0.60 13.69           C  
ANISOU 1051  CB ALYS A 129     1999   1573   1631    -11   -331   -257       C  
ATOM   1052  CB BLYS A 129      24.758  25.313  15.980  0.40 12.34           C  
ANISOU 1052  CB BLYS A 129     1825   1402   1461    -13   -329   -258       C  
ATOM   1053  CG ALYS A 129      25.588  25.394  17.468  0.60 17.77           C  
ANISOU 1053  CG ALYS A 129     2539   2084   2128     10   -363   -240       C  
ATOM   1054  CG BLYS A 129      25.690  25.389  17.157  0.40 10.49           C  
ANISOU 1054  CG BLYS A 129     1608   1164   1215     16   -361   -255       C  
ATOM   1055  CD ALYS A 129      26.643  24.292  17.627  0.60 15.68           C  
ANISOU 1055  CD ALYS A 129     2303   1758   1897     67   -452   -272       C  
ATOM   1056  CD BLYS A 129      26.890  24.499  16.952  0.40 13.54           C  
ANISOU 1056  CD BLYS A 129     1998   1506   1640     81   -435   -313       C  
ATOM   1057  CE ALYS A 129      27.925  24.639  16.933  0.60 20.21           C  
ANISOU 1057  CE ALYS A 129     2814   2366   2501    127   -453   -367       C  
ATOM   1058  CE BLYS A 129      27.791  24.585  18.156  0.40 12.99           C  
ANISOU 1058  CE BLYS A 129     1944   1434   1557    117   -479   -313       C  
ATOM   1059  NZ ALYS A 129      29.019  23.688  17.296  0.60 17.56           N1+
ANISOU 1059  NZ ALYS A 129     2494   1978   2199    196   -547   -410       N1+
ATOM   1060  NZ BLYS A 129      28.998  23.723  18.007  0.40 15.84           N1+
ANISOU 1060  NZ BLYS A 129     2302   1753   1964    192   -563   -380       N1+
ATOM   1061  N   PRO A 130      21.846  26.105  17.026  1.00 11.14           N  
ANISOU 1061  N   PRO A 130     1683   1302   1249   -144   -237   -132       N  
ATOM   1062  CA  PRO A 130      20.893  26.391  18.107  1.00 11.78           C  
ANISOU 1062  CA  PRO A 130     1771   1417   1290   -194   -201    -76       C  
ATOM   1063  C   PRO A 130      21.492  26.348  19.499  1.00 13.01           C  
ANISOU 1063  C   PRO A 130     1965   1578   1401   -185   -218    -45       C  
ATOM   1064  O   PRO A 130      21.062  27.147  20.351  1.00 13.30           O  
ANISOU 1064  O   PRO A 130     1987   1677   1389   -200   -175    -32       O  
ATOM   1065  CB  PRO A 130      19.805  25.349  17.887  1.00 13.27           C  
ANISOU 1065  CB  PRO A 130     1975   1565   1500   -253   -212    -37       C  
ATOM   1066  CG  PRO A 130      19.829  25.084  16.390  1.00 14.95           C  
ANISOU 1066  CG  PRO A 130     2165   1753   1762   -230   -234    -91       C  
ATOM   1067  CD  PRO A 130      21.291  25.119  16.075  1.00 12.61           C  
ANISOU 1067  CD  PRO A 130     1877   1441   1474   -161   -266   -139       C  
ATOM   1068  N   GLN A 131      22.497  25.511  19.727  1.00 12.81           N  
ANISOU 1068  N   GLN A 131     1984   1495   1388   -150   -285    -45       N  
ATOM   1069  CA AGLN A 131      23.099  25.421  21.071  0.50 13.12           C  
ANISOU 1069  CA AGLN A 131     2068   1541   1377   -133   -316    -14       C  
ATOM   1070  CA BGLN A 131      23.215  25.338  20.982  0.50 15.01           C  
ANISOU 1070  CA BGLN A 131     2309   1772   1624   -127   -323    -19       C  
ATOM   1071  C   GLN A 131      23.881  26.654  21.472  1.00 14.71           C  
ANISOU 1071  C   GLN A 131     2229   1804   1556    -87   -297    -70       C  
ATOM   1072  O   GLN A 131      24.104  26.840  22.690  1.00 16.93           O  
ANISOU 1072  O   GLN A 131     2538   2118   1779    -77   -310    -49       O  
ATOM   1073  CB AGLN A 131      23.992  24.187  21.204  0.50 14.41           C  
ANISOU 1073  CB AGLN A 131     2292   1617   1567    -96   -409     -4       C  
ATOM   1074  CB BGLN A 131      24.250  24.211  20.760  0.50 17.33           C  
ANISOU 1074  CB BGLN A 131     2644   1979   1960    -78   -414    -34       C  
ATOM   1075  CG AGLN A 131      23.277  22.861  21.383  0.50 20.08           C  
ANISOU 1075  CG AGLN A 131     3079   2255   2295   -149   -445     77       C  
ATOM   1076  CG BGLN A 131      23.635  22.807  20.536  0.50 31.80           C  
ANISOU 1076  CG BGLN A 131     4535   3720   3828   -119   -459     22       C  
ATOM   1077  CD AGLN A 131      24.267  21.747  21.675  0.50 40.27           C  
ANISOU 1077  CD AGLN A 131     5705   4717   4880    -97   -553     86       C  
ATOM   1078  CD BGLN A 131      23.001  22.443  19.185  0.50 33.78           C  
ANISOU 1078  CD BGLN A 131     4753   3940   4140   -141   -448    -11       C  
ATOM   1079  NE2AGLN A 131      23.901  20.870  22.600  0.50 40.80           N  
ANISOU 1079  NE2AGLN A 131     5859   4729   4914   -140   -592    188       N  
ATOM   1080  NE2BGLN A 131      22.413  21.250  19.151  0.50 34.42           N  
ANISOU 1080  NE2BGLN A 131     4885   3936   4258   -186   -491     38       N  
ATOM   1081  OE1AGLN A 131      25.361  21.651  21.081  0.50 31.10           O  
ANISOU 1081  OE1AGLN A 131     4519   3531   3768    -20   -605      4       O  
ATOM   1082  OE1BGLN A 131      23.057  23.147  18.156  0.50 15.50           O  
ANISOU 1082  OE1BGLN A 131     2375   1672   1845   -119   -409    -79       O  
ATOM   1083  N  AASN A 132      24.227  27.534  20.486  0.50 12.87           N  
ANISOU 1083  N  AASN A 132     1933   1591   1366    -64   -266   -136       N  
ATOM   1084  N  BASN A 132      24.283  27.529  20.565  0.50 11.20           N  
ANISOU 1084  N  BASN A 132     1723   1380   1152    -62   -269   -136       N  
ATOM   1085  CA AASN A 132      24.950  28.820  20.621  0.50 12.52           C  
ANISOU 1085  CA AASN A 132     1839   1593   1326    -33   -244   -194       C  
ATOM   1086  CA BASN A 132      24.915  28.770  21.024  0.50 10.22           C  
ANISOU 1086  CA BASN A 132     1559   1307   1018    -33   -250   -184       C  
ATOM   1087  C  AASN A 132      24.007  30.020  20.618  0.50 11.98           C  
ANISOU 1087  C  AASN A 132     1734   1575   1244    -61   -178   -195       C  
ATOM   1088  C  BASN A 132      24.011  30.005  20.907  0.50 11.33           C  
ANISOU 1088  C  BASN A 132     1657   1497   1149    -60   -182   -192       C  
ATOM   1089  O  AASN A 132      24.461  31.148  20.439  0.50 11.08           O  
ANISOU 1089  O  AASN A 132     1576   1480   1152    -44   -157   -242       O  
ATOM   1090  O  BASN A 132      24.493  31.128  21.029  0.50 11.14           O  
ANISOU 1090  O  BASN A 132     1595   1499   1139    -40   -166   -239       O  
ATOM   1091  CB AASN A 132      25.938  29.004  19.460  0.50 16.58           C  
ANISOU 1091  CB AASN A 132     2308   2091   1899     -1   -248   -255       C  
ATOM   1092  CB BASN A 132      26.311  28.975  20.449  0.50  9.73           C  
ANISOU 1092  CB BASN A 132     1460   1231   1007     16   -277   -253       C  
ATOM   1093  CG AASN A 132      27.275  28.419  19.719  0.50 35.78           C  
ANISOU 1093  CG AASN A 132     4744   4500   4352     51   -312   -296       C  
ATOM   1094  CG BASN A 132      26.430  28.880  18.958  0.50  8.83           C  
ANISOU 1094  CG BASN A 132     1312   1101    942     15   -256   -281       C  
ATOM   1095  ND2AASN A 132      27.996  28.142  18.651  0.50 27.65           N  
ANISOU 1095  ND2AASN A 132     3679   3458   3368     75   -319   -346       N  
ATOM   1096  ND2BASN A 132      27.515  28.326  18.464  0.50 11.09           N  
ANISOU 1096  ND2BASN A 132     1582   1366   1264     56   -295   -329       N  
ATOM   1097  OD1AASN A 132      27.696  28.253  20.870  0.50 28.86           O  
ANISOU 1097  OD1AASN A 132     3895   3624   3445     74   -358   -290       O  
ATOM   1098  OD1BASN A 132      25.524  29.214  18.209  0.50  9.00           O  
ANISOU 1098  OD1BASN A 132     1322   1133    965    -17   -210   -263       O  
ATOM   1099  N   LEU A 133      22.693  29.791  20.739  1.00 10.51           N  
ANISOU 1099  N   LEU A 133     1558   1405   1031   -105   -147   -149       N  
ATOM   1100  CA  LEU A 133      21.719  30.895  20.741  1.00 10.48           C  
ANISOU 1100  CA  LEU A 133     1512   1451   1018   -121    -93   -162       C  
ATOM   1101  C   LEU A 133      20.987  30.806  22.058  1.00 12.06           C  
ANISOU 1101  C   LEU A 133     1728   1705   1149   -146    -75   -132       C  
ATOM   1102  O   LEU A 133      20.357  29.772  22.338  1.00 13.94           O  
ANISOU 1102  O   LEU A 133     1999   1938   1360   -189    -75    -73       O  
ATOM   1103  CB  LEU A 133      20.763  30.785  19.559  1.00 10.78           C  
ANISOU 1103  CB  LEU A 133     1529   1477   1088   -147    -69   -152       C  
ATOM   1104  CG  LEU A 133      21.462  30.759  18.196  1.00 12.17           C  
ANISOU 1104  CG  LEU A 133     1696   1614   1313   -124    -84   -177       C  
ATOM   1105  CD1 LEU A 133      20.455  30.685  17.099  1.00 12.78           C  
ANISOU 1105  CD1 LEU A 133     1757   1692   1408   -142    -69   -170       C  
ATOM   1106  CD2 LEU A 133      22.399  31.950  17.978  1.00 15.24           C  
ANISOU 1106  CD2 LEU A 133     2057   2009   1725    -92    -73   -219       C  
ATOM   1107  N   LEU A 134      21.184  31.793  22.930  1.00 10.53           N  
ANISOU 1107  N   LEU A 134     1516   1562    925   -120    -64   -172       N  
ATOM   1108  CA  LEU A 134      20.663  31.754  24.302  1.00 11.53           C  
ANISOU 1108  CA  LEU A 134     1657   1760    964   -133    -47   -154       C  
ATOM   1109  C   LEU A 134      19.506  32.667  24.499  1.00 11.95           C  
ANISOU 1109  C   LEU A 134     1656   1883   1003   -143      9   -187       C  
ATOM   1110  O   LEU A 134      19.494  33.767  23.965  1.00 12.13           O  
ANISOU 1110  O   LEU A 134     1633   1897   1079   -113     16   -246       O  
ATOM   1111  CB  LEU A 134      21.762  32.049  25.306  1.00 12.92           C  
ANISOU 1111  CB  LEU A 134     1854   1954   1100    -86    -88   -188       C  
ATOM   1112  CG  LEU A 134      23.043  31.211  25.156  1.00 16.56           C  
ANISOU 1112  CG  LEU A 134     2359   2349   1584    -60   -156   -174       C  
ATOM   1113  CD1 LEU A 134      24.015  31.518  26.223  1.00 17.71           C  
ANISOU 1113  CD1 LEU A 134     2519   2524   1687    -11   -204   -213       C  
ATOM   1114  CD2 LEU A 134      22.770  29.689  25.076  1.00 20.22           C  
ANISOU 1114  CD2 LEU A 134     2886   2768   2030    -97   -179    -85       C  
ATOM   1115  N   ILE A 135      18.512  32.213  25.257  1.00 12.74           N  
ANISOU 1115  N   ILE A 135     1757   2050   1032   -186     49   -148       N  
ATOM   1116  CA  ILE A 135      17.291  33.002  25.447  1.00 13.02           C  
ANISOU 1116  CA  ILE A 135     1726   2166   1054   -194    106   -190       C  
ATOM   1117  C   ILE A 135      17.067  33.320  26.902  1.00 16.31           C  
ANISOU 1117  C   ILE A 135     2139   2692   1367   -186    134   -212       C  
ATOM   1118  O   ILE A 135      17.520  32.588  27.787  1.00 15.82           O  
ANISOU 1118  O   ILE A 135     2137   2652   1223   -202    121   -159       O  
ATOM   1119  CB  ILE A 135      16.065  32.261  24.858  1.00 14.50           C  
ANISOU 1119  CB  ILE A 135     1890   2360   1260   -260    144   -143       C  
ATOM   1120  CG1 ILE A 135      15.817  30.905  25.544  1.00 17.01           C  
ANISOU 1120  CG1 ILE A 135     2260   2692   1511   -333    158    -47       C  
ATOM   1121  CG2 ILE A 135      16.204  32.070  23.338  1.00 14.21           C  
ANISOU 1121  CG2 ILE A 135     1850   2228   1320   -256    112   -139       C  
ATOM   1122  CD1 ILE A 135      14.398  30.322  25.251  1.00 25.69           C  
ANISOU 1122  CD1 ILE A 135     3313   3825   2623   -413    211    -13       C  
ATOM   1123  N   ASN A 136      16.305  34.388  27.154  1.00 15.42           N  
ANISOU 1123  N   ASN A 136     1956   2654   1251   -160    170   -292       N  
ATOM   1124  CA  ASN A 136      15.922  34.724  28.526  1.00 17.25           C  
ANISOU 1124  CA  ASN A 136     2170   3013   1372   -150    207   -329       C  
ATOM   1125  C   ASN A 136      14.383  34.739  28.627  1.00 18.93           C  
ANISOU 1125  C   ASN A 136     2308   3325   1560   -192    284   -341       C  
ATOM   1126  O   ASN A 136      13.665  34.612  27.631  1.00 19.18           O  
ANISOU 1126  O   ASN A 136     2300   3318   1670   -218    296   -331       O  
ATOM   1127  CB  ASN A 136      16.599  36.013  29.002  1.00 16.55           C  
ANISOU 1127  CB  ASN A 136     2060   2936   1292    -66    171   -440       C  
ATOM   1128  CG  ASN A 136      16.148  37.261  28.314  1.00 17.51           C  
ANISOU 1128  CG  ASN A 136     2111   3031   1513    -19    166   -534       C  
ATOM   1129  ND2 ASN A 136      16.942  38.321  28.425  1.00 20.89           N  
ANISOU 1129  ND2 ASN A 136     2532   3418   1989     45    117   -617       N  
ATOM   1130  OD1 ASN A 136      15.075  37.297  27.709  1.00 17.15           O  
ANISOU 1130  OD1 ASN A 136     2015   2998   1504    -40    201   -534       O  
ATOM   1131  N   THR A 137      13.850  34.879  29.833  1.00 19.24           N  
ANISOU 1131  N   THR A 137     2322   3503   1485   -198    337   -367       N  
ATOM   1132  CA  THR A 137      12.385  34.813  29.969  1.00 19.50           C  
ANISOU 1132  CA  THR A 137     2271   3647   1491   -246    419   -381       C  
ATOM   1133  C   THR A 137      11.676  36.094  29.513  1.00 22.70           C  
ANISOU 1133  C   THR A 137     2573   4075   1977   -178    421   -513       C  
ATOM   1134  O   THR A 137      10.439  36.109  29.477  1.00 24.77           O  
ANISOU 1134  O   THR A 137     2748   4425   2238   -206    480   -543       O  
ATOM   1135  CB  THR A 137      11.958  34.369  31.385  1.00 28.60           C  
ANISOU 1135  CB  THR A 137     3427   4958   2480   -293    492   -350       C  
ATOM   1136  CG2 THR A 137      12.456  32.970  31.776  1.00 29.45           C  
ANISOU 1136  CG2 THR A 137     3645   5034   2512   -374    490   -196       C  
ATOM   1137  OG1 THR A 137      12.534  35.303  32.255  1.00 24.98           O  
ANISOU 1137  OG1 THR A 137     2970   4563   1958   -207    468   -446       O  
ATOM   1138  N   GLU A 138      12.429  37.139  29.127  1.00 18.04           N  
ANISOU 1138  N   GLU A 138     2201   3052   1603    186    -14   -446       N  
ATOM   1139  CA  GLU A 138      11.887  38.421  28.664  1.00 19.92           C  
ANISOU 1139  CA  GLU A 138     2460   3277   1833    266     23   -470       C  
ATOM   1140  C   GLU A 138      11.625  38.485  27.160  1.00 22.89           C  
ANISOU 1140  C   GLU A 138     2832   3629   2235    291     52   -439       C  
ATOM   1141  O   GLU A 138      11.064  39.466  26.675  1.00 26.77           O  
ANISOU 1141  O   GLU A 138     3340   4121   2711    370     90   -446       O  
ATOM   1142  CB  GLU A 138      12.805  39.574  29.050  1.00 21.49           C  
ANISOU 1142  CB  GLU A 138     2712   3376   2076    288     30   -527       C  
ATOM   1143  CG  GLU A 138      12.766  39.880  30.542  1.00 33.51           C  
ANISOU 1143  CG  GLU A 138     4238   4943   3552    292     12   -572       C  
ATOM   1144  CD  GLU A 138      13.482  41.143  30.969  1.00 56.84           C  
ANISOU 1144  CD  GLU A 138     7248   7810   6538    312     26   -643       C  
ATOM   1145  OE1 GLU A 138      14.630  41.375  30.519  1.00 39.86           O  
ANISOU 1145  OE1 GLU A 138     5124   5559   4463    273     25   -662       O  
ATOM   1146  OE2 GLU A 138      12.894  41.897  31.777  1.00 54.11           O1-
ANISOU 1146  OE2 GLU A 138     6920   7500   6139    363     40   -683       O1-
ATOM   1147  N   GLY A 139      12.071  37.491  26.413  1.00 16.85           N  
ANISOU 1147  N   GLY A 139     2052   2841   1509    232     38   -406       N  
ATOM   1148  CA  GLY A 139      11.888  37.537  24.965  1.00 15.92           C  
ANISOU 1148  CA  GLY A 139     1929   2706   1415    255     63   -380       C  
ATOM   1149  C   GLY A 139      13.146  37.850  24.194  1.00 14.88           C  
ANISOU 1149  C   GLY A 139     1835   2446   1373    246     66   -383       C  
ATOM   1150  O   GLY A 139      13.084  37.886  22.969  1.00 14.26           O  
ANISOU 1150  O   GLY A 139     1752   2350   1316    267     87   -359       O  
ATOM   1151  N   ALA A 140      14.296  38.024  24.875  1.00 13.37           N  
ANISOU 1151  N   ALA A 140     1674   2178   1229    212     46   -411       N  
ATOM   1152  CA  ALA A 140      15.535  38.277  24.141  1.00 12.67           C  
ANISOU 1152  CA  ALA A 140     1612   1978   1222    194     49   -414       C  
ATOM   1153  C   ALA A 140      16.191  36.980  23.729  1.00 12.87           C  
ANISOU 1153  C   ALA A 140     1618   1996   1278    131     20   -380       C  
ATOM   1154  O   ALA A 140      15.997  35.925  24.357  1.00 13.05           O  
ANISOU 1154  O   ALA A 140     1618   2074   1266     89     -7   -363       O  
ATOM   1155  CB  ALA A 140      16.508  39.082  25.012  1.00 14.73           C  
ANISOU 1155  CB  ALA A 140     1907   2173   1516    180     42   -466       C  
ATOM   1156  N   ILE A 141      16.986  37.059  22.661  1.00 11.46           N  
ANISOU 1156  N   ILE A 141     1452   1742   1162    129     30   -366       N  
ATOM   1157  CA  ILE A 141      17.858  35.979  22.234  1.00 10.18           C  
ANISOU 1157  CA  ILE A 141     1281   1552   1036     78      5   -338       C  
ATOM   1158  C   ILE A 141      19.209  36.568  21.905  1.00 12.06           C  
ANISOU 1158  C   ILE A 141     1539   1698   1344     71      8   -354       C  
ATOM   1159  O   ILE A 141      19.281  37.708  21.442  1.00 11.76           O  
ANISOU 1159  O   ILE A 141     1524   1609   1335    106     41   -371       O  
ATOM   1160  CB  ILE A 141      17.246  35.177  21.091  1.00 10.95           C  
ANISOU 1160  CB  ILE A 141     1359   1679   1122     78     16   -299       C  
ATOM   1161  CG1 ILE A 141      18.056  33.915  20.788  1.00 11.05           C  
ANISOU 1161  CG1 ILE A 141     1371   1664   1163     27     -8   -272       C  
ATOM   1162  CG2 ILE A 141      17.076  36.038  19.838  1.00 12.01           C  
ANISOU 1162  CG2 ILE A 141     1499   1782   1281    133     53   -292       C  
ATOM   1163  CD1 ILE A 141      17.260  32.866  19.938  1.00 10.97           C  
ANISOU 1163  CD1 ILE A 141     1345   1699   1124      6      0   -243       C  
ATOM   1164  N   LYS A 142      20.272  35.827  22.235  1.00 11.12           N  
ANISOU 1164  N   LYS A 142     1412   1564   1248     26    -25   -348       N  
ATOM   1165  CA  LYS A 142      21.622  36.363  22.091  1.00 10.98           C  
ANISOU 1165  CA  LYS A 142     1402   1481   1289      9    -27   -368       C  
ATOM   1166  C   LYS A 142      22.525  35.309  21.513  1.00 10.58           C  
ANISOU 1166  C   LYS A 142     1338   1416   1265    -14    -47   -331       C  
ATOM   1167  O   LYS A 142      22.373  34.084  21.754  1.00 11.92           O  
ANISOU 1167  O   LYS A 142     1500   1624   1405    -27    -68   -300       O  
ATOM   1168  CB  LYS A 142      22.183  36.797  23.462  1.00 11.48           C  
ANISOU 1168  CB  LYS A 142     1462   1561   1339    -16    -49   -418       C  
ATOM   1169  CG  LYS A 142      21.254  37.737  24.226  1.00 11.84           C  
ANISOU 1169  CG  LYS A 142     1526   1628   1347      9    -32   -459       C  
ATOM   1170  CD  LYS A 142      21.992  38.353  25.390  1.00 13.05           C  
ANISOU 1170  CD  LYS A 142     1678   1783   1497    -20    -49   -521       C  
ATOM   1171  CE  LYS A 142      21.046  39.217  26.194  1.00 15.56           C  
ANISOU 1171  CE  LYS A 142     2018   2123   1771      9    -32   -563       C  
ATOM   1172  NZ  LYS A 142      21.823  40.140  27.098  1.00 17.50           N1+
ANISOU 1172  NZ  LYS A 142     2275   2348   2025    -23    -35   -640       N1+
ATOM   1173  N   LEU A 143      23.512  35.777  20.762  1.00 10.35           N  
ANISOU 1173  N   LEU A 143     1311   1327   1293    -17    -35   -333       N  
ATOM   1174  CA ALEU A 143      24.541  34.968  20.110  0.50 10.79           C  
ANISOU 1174  CA ALEU A 143     1354   1366   1380    -30    -50   -301       C  
ATOM   1175  CA BLEU A 143      24.493  34.875  20.166  0.50 10.70           C  
ANISOU 1175  CA BLEU A 143     1342   1359   1364    -30    -52   -299       C  
ATOM   1176  C   LEU A 143      25.672  34.691  21.095  1.00 10.84           C  
ANISOU 1176  C   LEU A 143     1339   1398   1381    -60    -84   -318       C  
ATOM   1177  O   LEU A 143      26.298  35.653  21.576  1.00 11.22           O  
ANISOU 1177  O   LEU A 143     1379   1436   1447    -82    -83   -365       O  
ATOM   1178  CB ALEU A 143      25.116  35.779  18.927  0.50 11.51           C  
ANISOU 1178  CB ALEU A 143     1451   1391   1531    -19    -18   -298       C  
ATOM   1179  CB BLEU A 143      24.966  35.374  18.805  0.50 11.38           C  
ANISOU 1179  CB BLEU A 143     1432   1385   1505    -15    -22   -284       C  
ATOM   1180  CG ALEU A 143      24.141  36.035  17.762  0.50 15.64           C  
ANISOU 1180  CG ALEU A 143     1990   1897   2057     24     20   -272       C  
ATOM   1181  CG BLEU A 143      23.858  35.483  17.773  0.50 12.98           C  
ANISOU 1181  CG BLEU A 143     1648   1583   1701     24     10   -260       C  
ATOM   1182  CD1ALEU A 143      24.473  37.288  17.035  0.50 18.10           C  
ANISOU 1182  CD1ALEU A 143     2319   2143   2416     42     63   -282       C  
ATOM   1183  CD1BLEU A 143      23.531  36.926  17.437  0.50 12.51           C  
ANISOU 1183  CD1BLEU A 143     1609   1481   1662     54     54   -281       C  
ATOM   1184  CD2ALEU A 143      24.108  34.869  16.785  0.50 18.49           C  
ANISOU 1184  CD2ALEU A 143     2340   2269   2415     33     12   -227       C  
ATOM   1185  CD2BLEU A 143      24.278  34.835  16.501  0.50 16.24           C  
ANISOU 1185  CD2BLEU A 143     2054   1976   2140     36     15   -220       C  
ATOM   1186  N   ALA A 144      25.985  33.414  21.368  1.00 10.67           N  
ANISOU 1186  N   ALA A 144     1309   1412   1332    -60   -111   -283       N  
ATOM   1187  CA  ALA A 144      27.084  33.005  22.230  1.00 11.50           C  
ANISOU 1187  CA  ALA A 144     1389   1559   1421    -71   -143   -288       C  
ATOM   1188  C   ALA A 144      28.263  32.569  21.400  1.00 11.54           C  
ANISOU 1188  C   ALA A 144     1380   1546   1460    -65   -147   -259       C  
ATOM   1189  O   ALA A 144      28.100  32.065  20.281  1.00 11.88           O  
ANISOU 1189  O   ALA A 144     1441   1550   1525    -47   -131   -221       O  
ATOM   1190  CB  ALA A 144      26.674  31.866  23.155  1.00 13.18           C  
ANISOU 1190  CB  ALA A 144     1609   1826   1574    -62   -164   -259       C  
ATOM   1191  N   ASP A 145      29.445  32.742  21.974  1.00 13.42           N  
ANISOU 1191  N   ASP A 145     1580   1823   1695    -78   -169   -280       N  
ATOM   1192  CA  ASP A 145      30.722  32.269  21.421  1.00 13.89           C  
ANISOU 1192  CA  ASP A 145     1614   1894   1771    -66   -178   -253       C  
ATOM   1193  C   ASP A 145      31.166  32.945  20.166  1.00 15.11           C  
ANISOU 1193  C   ASP A 145     1763   1991   1988    -76   -153   -255       C  
ATOM   1194  O   ASP A 145      31.956  32.390  19.399  1.00 15.56           O  
ANISOU 1194  O   ASP A 145     1807   2045   2059    -56   -153   -218       O  
ATOM   1195  CB  ASP A 145      30.716  30.732  21.262  1.00 14.21           C  
ANISOU 1195  CB  ASP A 145     1677   1944   1779    -22   -186   -187       C  
ATOM   1196  CG  ASP A 145      30.563  29.946  22.563  1.00 17.39           C  
ANISOU 1196  CG  ASP A 145     2082   2409   2115     -4   -208   -174       C  
ATOM   1197  OD1 ASP A 145      30.620  30.561  23.668  1.00 16.91           O  
ANISOU 1197  OD1 ASP A 145     1992   2404   2026    -24   -226   -218       O  
ATOM   1198  OD2 ASP A 145      30.391  28.711  22.485  1.00 21.73           O1-
ANISOU 1198  OD2 ASP A 145     2668   2951   2637     30   -204   -119       O1-
ATOM   1199  N   PHE A 146      30.662  34.159  19.910  1.00 16.02           N  
ANISOU 1199  N   PHE A 146     1892   2056   2137   -102   -124   -293       N  
ATOM   1200  CA  PHE A 146      31.060  34.907  18.753  1.00 16.21           C  
ANISOU 1200  CA  PHE A 146     1917   2022   2220   -111    -92   -292       C  
ATOM   1201  C   PHE A 146      32.563  35.114  18.769  1.00 19.37           C  
ANISOU 1201  C   PHE A 146     2267   2455   2638   -141   -103   -307       C  
ATOM   1202  O   PHE A 146      33.137  35.478  19.797  1.00 18.67           O  
ANISOU 1202  O   PHE A 146     2145   2420   2528   -180   -123   -354       O  
ATOM   1203  CB  PHE A 146      30.387  36.296  18.800  1.00 19.63           C  
ANISOU 1203  CB  PHE A 146     2378   2400   2679   -133    -55   -338       C  
ATOM   1204  CG  PHE A 146      29.755  36.600  17.475  1.00 19.87           C  
ANISOU 1204  CG  PHE A 146     2441   2364   2744    -99    -13   -304       C  
ATOM   1205  CD1 PHE A 146      30.530  36.990  16.397  1.00 20.43           C  
ANISOU 1205  CD1 PHE A 146     2504   2394   2865   -102     14   -286       C  
ATOM   1206  CD2 PHE A 146      28.390  36.437  17.286  1.00 21.10           C  
ANISOU 1206  CD2 PHE A 146     2628   2513   2875    -60     -1   -287       C  
ATOM   1207  CE1 PHE A 146      29.950  37.217  15.163  1.00 20.72           C  
ANISOU 1207  CE1 PHE A 146     2567   2381   2926    -60     52   -251       C  
ATOM   1208  CE2 PHE A 146      27.813  36.652  16.038  1.00 25.03           C  
ANISOU 1208  CE2 PHE A 146     3146   2970   3394    -21     36   -254       C  
ATOM   1209  CZ  PHE A 146      28.603  37.039  14.985  1.00 22.31           C  
ANISOU 1209  CZ  PHE A 146     2796   2583   3098    -18     62   -235       C  
ATOM   1210  N   GLY A 147      33.221  34.882  17.634  1.00 18.98           N  
ANISOU 1210  N   GLY A 147     2206   2385   2621   -125    -90   -269       N  
ATOM   1211  CA  GLY A 147      34.642  35.125  17.528  1.00 19.63           C  
ANISOU 1211  CA  GLY A 147     2234   2507   2719   -155    -96   -280       C  
ATOM   1212  C   GLY A 147      35.563  34.042  18.043  1.00 21.88           C  
ANISOU 1212  C   GLY A 147     2472   2887   2954   -129   -138   -257       C  
ATOM   1213  O   GLY A 147      36.760  34.094  17.771  1.00 21.80           O  
ANISOU 1213  O   GLY A 147     2409   2924   2951   -142   -143   -256       O  
ATOM   1214  N   LEU A 148      35.024  33.023  18.731  1.00 17.78           N  
ANISOU 1214  N   LEU A 148     1973   2400   2383    -87   -164   -233       N  
ATOM   1215  CA  LEU A 148      35.869  31.957  19.285  1.00 17.36           C  
ANISOU 1215  CA  LEU A 148     1885   2436   2274    -46   -197   -202       C  
ATOM   1216  C   LEU A 148      36.436  31.014  18.209  1.00 22.71           C  
ANISOU 1216  C   LEU A 148     2567   3103   2956     12   -191   -138       C  
ATOM   1217  O   LEU A 148      37.544  30.502  18.351  1.00 22.16           O  
ANISOU 1217  O   LEU A 148     2452   3112   2855     43   -210   -117       O  
ATOM   1218  CB  LEU A 148      35.155  31.155  20.383  1.00 18.06           C  
ANISOU 1218  CB  LEU A 148     2002   2556   2302    -16   -218   -190       C  
ATOM   1219  CG  LEU A 148      34.630  31.961  21.608  1.00 21.33           C  
ANISOU 1219  CG  LEU A 148     2409   3000   2697    -63   -229   -253       C  
ATOM   1220  CD1 LEU A 148      34.231  31.032  22.714  1.00 22.56           C  
ANISOU 1220  CD1 LEU A 148     2577   3210   2783    -24   -252   -230       C  
ATOM   1221  CD2 LEU A 148      35.657  32.978  22.156  1.00 23.72           C  
ANISOU 1221  CD2 LEU A 148     2642   3371   3001   -121   -242   -321       C  
ATOM   1222  N   ALA A 149      35.690  30.793  17.118  1.00 19.80           N  
ANISOU 1222  N   ALA A 149     2251   2649   2623     32   -165   -107       N  
ATOM   1223  CA  ALA A 149      36.171  29.938  16.023  1.00 19.77           C  
ANISOU 1223  CA  ALA A 149     2257   2628   2625     87   -156    -52       C  
ATOM   1224  C   ALA A 149      37.433  30.510  15.349  1.00 25.61           C  
ANISOU 1224  C   ALA A 149     2936   3401   3394     75   -151    -54       C  
ATOM   1225  O   ALA A 149      38.306  29.735  14.971  1.00 27.24           O  
ANISOU 1225  O   ALA A 149     3122   3648   3578    128   -158    -14       O  
ATOM   1226  CB  ALA A 149      35.076  29.773  14.997  1.00 20.35           C  
ANISOU 1226  CB  ALA A 149     2390   2614   2729     98   -129    -34       C  
ATOM   1227  N   ARG A 150      37.563  31.836  15.215  1.00 22.06           N  
ANISOU 1227  N   ARG A 150     2458   2934   2989     10   -133    -99       N  
ATOM   1228  CA  ARG A 150      38.761  32.429  14.611  1.00 23.15           C  
ANISOU 1228  CA  ARG A 150     2536   3105   3155    -16   -122   -103       C  
ATOM   1229  C   ARG A 150      39.909  32.339  15.588  1.00 30.15           C  
ANISOU 1229  C   ARG A 150     3347   4113   3995    -31   -155   -126       C  
ATOM   1230  O   ARG A 150      41.047  32.091  15.179  1.00 33.15           O  
ANISOU 1230  O   ARG A 150     3671   4561   4363    -12   -160   -104       O  
ATOM   1231  CB  ARG A 150      38.523  33.892  14.247  1.00 24.83           C  
ANISOU 1231  CB  ARG A 150     2752   3252   3429    -88    -84   -146       C  
ATOM   1232  CG  ARG A 150      39.662  34.544  13.466  1.00 33.27           C  
ANISOU 1232  CG  ARG A 150     3768   4338   4535   -123    -61   -145       C  
ATOM   1233  CD  ARG A 150      39.336  35.974  13.078  1.00 47.00           C  
ANISOU 1233  CD  ARG A 150     5531   5991   6336   -190    -11   -180       C  
ATOM   1234  NE  ARG A 150      40.503  36.690  12.559  1.00 59.14           N  
ANISOU 1234  NE  ARG A 150     7013   7551   7906   -246     16   -190       N  
ATOM   1235  CZ  ARG A 150      40.936  36.626  11.302  1.00 77.38           C  
ANISOU 1235  CZ  ARG A 150     9313   9842  10244   -217     43   -140       C  
ATOM   1236  NH1 ARG A 150      40.316  35.854  10.415  1.00 66.70           N1+
ANISOU 1236  NH1 ARG A 150     8002   8451   8890   -130     45    -81       N1+
ATOM   1237  NH2 ARG A 150      42.002  37.318  10.926  1.00 64.67           N  
ANISOU 1237  NH2 ARG A 150     7651   8259   8662   -278     69   -151       N  
ATOM   1238  N   ALA A 151      39.624  32.567  16.877  1.00 24.82           N  
ANISOU 1238  N   ALA A 151     2665   3477   3287    -64   -177   -172       N  
ATOM   1239  CA  ALA A 151      40.671  32.519  17.894  1.00 26.09           C  
ANISOU 1239  CA  ALA A 151     2746   3773   3392    -78   -210   -200       C  
ATOM   1240  C   ALA A 151      41.229  31.116  18.127  1.00 30.97           C  
ANISOU 1240  C   ALA A 151     3350   4478   3941     20   -238   -139       C  
ATOM   1241  O   ALA A 151      42.449  30.972  18.319  1.00 33.37           O  
ANISOU 1241  O   ALA A 151     3572   4902   4203     33   -256   -137       O  
ATOM   1242  CB  ALA A 151      40.149  33.106  19.180  1.00 27.07           C  
ANISOU 1242  CB  ALA A 151     2871   3919   3496   -132   -225   -265       C  
ATOM   1243  N   PHE A 152      40.365  30.081  18.047  1.00 26.36           N  
ANISOU 1243  N   PHE A 152     2844   3832   3341     90   -236    -87       N  
ATOM   1244  CA  PHE A 152      40.744  28.698  18.340  1.00 26.37           C  
ANISOU 1244  CA  PHE A 152     2855   3889   3273    190   -252    -25       C  
ATOM   1245  C   PHE A 152      40.535  27.640  17.233  1.00 30.41           C  
ANISOU 1245  C   PHE A 152     3436   4323   3796    267   -230     44       C  
ATOM   1246  O   PHE A 152      40.937  26.489  17.430  1.00 32.81           O  
ANISOU 1246  O   PHE A 152     3758   4665   4042    356   -235     97       O  
ATOM   1247  CB  PHE A 152      40.070  28.244  19.667  1.00 28.81           C  
ANISOU 1247  CB  PHE A 152     3195   4223   3527    207   -270    -29       C  
ATOM   1248  CG  PHE A 152      40.057  29.222  20.830  1.00 31.33           C  
ANISOU 1248  CG  PHE A 152     3461   4612   3831    134   -291   -103       C  
ATOM   1249  CD1 PHE A 152      41.244  29.725  21.354  1.00 36.73           C  
ANISOU 1249  CD1 PHE A 152     4044   5432   4481    108   -314   -143       C  
ATOM   1250  CD2 PHE A 152      38.864  29.575  21.449  1.00 34.04           C  
ANISOU 1250  CD2 PHE A 152     3853   4897   4185     95   -288   -135       C  
ATOM   1251  CE1 PHE A 152      41.229  30.615  22.432  1.00 38.90           C  
ANISOU 1251  CE1 PHE A 152     4271   5771   4737     35   -333   -220       C  
ATOM   1252  CE2 PHE A 152      38.849  30.453  22.535  1.00 38.11           C  
ANISOU 1252  CE2 PHE A 152     4324   5475   4682     33   -307   -206       C  
ATOM   1253  CZ  PHE A 152      40.031  30.968  23.019  1.00 37.65           C  
ANISOU 1253  CZ  PHE A 152     4170   5542   4593      1   -329   -251       C  
ATOM   1254  N   GLY A 153      39.896  28.001  16.113  1.00 25.46           N  
ANISOU 1254  N   GLY A 153     2851   3590   3235    239   -203     43       N  
ATOM   1255  CA  GLY A 153      39.590  27.068  15.030  1.00 24.36           C  
ANISOU 1255  CA  GLY A 153     2776   3373   3105    301   -181     95       C  
ATOM   1256  C   GLY A 153      38.315  26.277  15.290  1.00 27.14           C  
ANISOU 1256  C   GLY A 153     3220   3647   3444    315   -172    110       C  
ATOM   1257  O   GLY A 153      37.820  26.266  16.422  1.00 28.23           O  
ANISOU 1257  O   GLY A 153     3367   3805   3552    296   -185     93       O  
ATOM   1258  N   VAL A 154      37.734  25.662  14.239  1.00 23.71           N  
ANISOU 1258  N   VAL A 154     2850   3127   3030    340   -147    136       N  
ATOM   1259  CA  VAL A 154      36.547  24.805  14.398  1.00 22.39           C  
ANISOU 1259  CA  VAL A 154     2770   2889   2847    344   -133    148       C  
ATOM   1260  C   VAL A 154      37.070  23.382  14.224  1.00 24.31           C  
ANISOU 1260  C   VAL A 154     3066   3124   3047    430   -122    204       C  
ATOM   1261  O   VAL A 154      37.501  23.018  13.132  1.00 24.38           O  
ANISOU 1261  O   VAL A 154     3087   3107   3068    470   -108    226       O  
ATOM   1262  CB  VAL A 154      35.356  25.109  13.458  1.00 25.02           C  
ANISOU 1262  CB  VAL A 154     3141   3139   3225    301   -111    128       C  
ATOM   1263  CG1 VAL A 154      34.227  24.092  13.683  1.00 24.66           C  
ANISOU 1263  CG1 VAL A 154     3180   3038   3153    298    -95    138       C  
ATOM   1264  CG2 VAL A 154      34.850  26.531  13.675  1.00 25.17           C  
ANISOU 1264  CG2 VAL A 154     3118   3164   3282    232   -114     79       C  
ATOM   1265  N   PRO A 155      37.109  22.583  15.307  1.00 21.80           N  
ANISOU 1265  N   PRO A 155     2781   2830   2672    467   -126    230       N  
ATOM   1266  CA  PRO A 155      37.656  21.229  15.185  1.00 21.09           C  
ANISOU 1266  CA  PRO A 155     2753   2726   2535    561   -107    288       C  
ATOM   1267  C   PRO A 155      36.636  20.236  14.663  1.00 22.01           C  
ANISOU 1267  C   PRO A 155     2982   2726   2656    557    -70    301       C  
ATOM   1268  O   PRO A 155      35.454  20.558  14.587  1.00 21.20           O  
ANISOU 1268  O   PRO A 155     2900   2572   2582    480    -64    266       O  
ATOM   1269  CB  PRO A 155      38.064  20.899  16.622  1.00 22.65           C  
ANISOU 1269  CB  PRO A 155     2937   3001   2667    603   -121    311       C  
ATOM   1270  CG  PRO A 155      37.009  21.595  17.460  1.00 25.99           C  
ANISOU 1270  CG  PRO A 155     3351   3419   3103    516   -134    266       C  
ATOM   1271  CD  PRO A 155      36.649  22.865  16.683  1.00 22.18           C  
ANISOU 1271  CD  PRO A 155     2818   2918   2692    433   -143    210       C  
ATOM   1272  N   VAL A 156      37.093  19.062  14.272  1.00 20.69           N  
ANISOU 1272  N   VAL A 156     2884   2519   2457    637    -43    347       N  
ATOM   1273  CA  VAL A 156      36.203  17.997  13.812  1.00 19.37           C  
ANISOU 1273  CA  VAL A 156     2835   2237   2289    629     -1    356       C  
ATOM   1274  C   VAL A 156      35.439  17.454  15.014  1.00 21.19           C  
ANISOU 1274  C   VAL A 156     3126   2442   2483    607     13    368       C  
ATOM   1275  O   VAL A 156      34.225  17.211  14.943  1.00 18.68           O  
ANISOU 1275  O   VAL A 156     2865   2053   2180    533     34    344       O  
ATOM   1276  CB  VAL A 156      36.976  16.891  13.047  1.00 22.83           C  
ANISOU 1276  CB  VAL A 156     3341   2631   2701    727     30    400       C  
ATOM   1277  CG1 VAL A 156      36.065  15.728  12.674  1.00 23.24           C  
ANISOU 1277  CG1 VAL A 156     3527   2556   2747    709     80    402       C  
ATOM   1278  CG2 VAL A 156      37.650  17.466  11.804  1.00 23.03           C  
ANISOU 1278  CG2 VAL A 156     3302   2686   2762    744     16    387       C  
ATOM   1279  N   ARG A 157      36.157  17.300  16.141  1.00 17.74           N  
ANISOU 1279  N   ARG A 157     2517   2003   2220    100   -448    -53       N  
ATOM   1280  CA  ARG A 157      35.575  16.769  17.373  1.00 16.92           C  
ANISOU 1280  CA  ARG A 157     2456   1892   2079     73   -472     -6       C  
ATOM   1281  C   ARG A 157      35.853  17.725  18.489  1.00 18.30           C  
ANISOU 1281  C   ARG A 157     2627   2103   2224     66   -456    -12       C  
ATOM   1282  O   ARG A 157      36.870  18.443  18.491  1.00 19.35           O  
ANISOU 1282  O   ARG A 157     2730   2250   2371     91   -451    -56       O  
ATOM   1283  CB  ARG A 157      36.237  15.444  17.744  1.00 18.35           C  
ANISOU 1283  CB  ARG A 157     2668   2032   2272     90   -548      4       C  
ATOM   1284  CG  ARG A 157      36.234  14.428  16.655  1.00 19.32           C  
ANISOU 1284  CG  ARG A 157     2787   2118   2437    107   -578     -4       C  
ATOM   1285  CD  ARG A 157      34.828  14.029  16.290  1.00 18.68           C  
ANISOU 1285  CD  ARG A 157     2719   2028   2351     76   -554     35       C  
ATOM   1286  NE  ARG A 157      34.872  12.867  15.403  1.00 19.66           N  
ANISOU 1286  NE  ARG A 157     2839   2111   2520     95   -595     26       N  
ATOM   1287  CZ  ARG A 157      35.000  11.622  15.839  1.00 19.32           C  
ANISOU 1287  CZ  ARG A 157     2828   2022   2492     96   -661     51       C  
ATOM   1288  NH1 ARG A 157      34.970  11.361  17.141  1.00 21.82           N1+
ANISOU 1288  NH1 ARG A 157     3188   2328   2774     75   -687     95       N1+
ATOM   1289  NH2 ARG A 157      35.080  10.622  14.978  1.00 19.99           N  
ANISOU 1289  NH2 ARG A 157     2901   2071   2625    116   -701     35       N  
ATOM   1290  N   THR A 158      34.973  17.747  19.484  1.00 16.25           N  
ANISOU 1290  N   THR A 158     2392   1862   1921     32   -448     28       N  
ATOM   1291  CA  THR A 158      35.168  18.604  20.656  1.00 16.88           C  
ANISOU 1291  CA  THR A 158     2464   1983   1967     25   -437     21       C  
ATOM   1292  C   THR A 158      36.185  17.970  21.577  1.00 18.48           C  
ANISOU 1292  C   THR A 158     2690   2175   2159     48   -496     22       C  
ATOM   1293  O   THR A 158      36.676  16.865  21.330  1.00 18.04           O  
ANISOU 1293  O   THR A 158     2659   2076   2122     66   -548     30       O  
ATOM   1294  CB  THR A 158      33.853  18.796  21.414  1.00 18.41           C  
ANISOU 1294  CB  THR A 158     2672   2208   2113    -21   -411     60       C  
ATOM   1295  CG2 THR A 158      32.703  19.194  20.505  1.00 19.55           C  
ANISOU 1295  CG2 THR A 158     2804   2358   2268    -44   -361     62       C  
ATOM   1296  OG1 THR A 158      33.562  17.581  22.159  1.00 19.08           O  
ANISOU 1296  OG1 THR A 158     2806   2274   2168    -39   -455    112       O  
ATOM   1297  N   TYR A 159      36.474  18.647  22.704  1.00 18.07           N  
ANISOU 1297  N   TYR A 159     2628   2162   2075     49   -493     11       N  
ATOM   1298  CA  TYR A 159      37.411  18.161  23.686  1.00 18.62           C  
ANISOU 1298  CA  TYR A 159     2718   2230   2128     74   -547      9       C  
ATOM   1299  C   TYR A 159      36.957  16.831  24.318  1.00 21.38           C  
ANISOU 1299  C   TYR A 159     3127   2554   2444     55   -597     74       C  
ATOM   1300  O   TYR A 159      37.796  16.134  24.885  1.00 22.80           O  
ANISOU 1300  O   TYR A 159     3333   2713   2618     81   -656     77       O  
ATOM   1301  CB  TYR A 159      37.645  19.253  24.760  1.00 21.27           C  
ANISOU 1301  CB  TYR A 159     3025   2624   2434     78   -527    -18       C  
ATOM   1302  CG  TYR A 159      36.548  19.345  25.804  1.00 21.47           C  
ANISOU 1302  CG  TYR A 159     3066   2694   2399     37   -513     28       C  
ATOM   1303  CD1 TYR A 159      35.295  19.854  25.483  1.00 22.79           C  
ANISOU 1303  CD1 TYR A 159     3220   2883   2556     -4   -462     44       C  
ATOM   1304  CD2 TYR A 159      36.766  18.919  27.113  1.00 23.03           C  
ANISOU 1304  CD2 TYR A 159     3290   2916   2545     38   -552     53       C  
ATOM   1305  CE1 TYR A 159      34.269  19.894  26.425  1.00 24.05           C  
ANISOU 1305  CE1 TYR A 159     3391   3088   2658    -46   -449     81       C  
ATOM   1306  CE2 TYR A 159      35.751  18.974  28.069  1.00 24.06           C  
ANISOU 1306  CE2 TYR A 159     3432   3095   2614     -4   -538     96       C  
ATOM   1307  CZ  TYR A 159      34.511  19.479  27.724  1.00 30.17           C  
ANISOU 1307  CZ  TYR A 159     4190   3892   3381    -47   -486    106       C  
ATOM   1308  OH  TYR A 159      33.495  19.506  28.650  1.00 28.81           O  
ANISOU 1308  OH  TYR A 159     4026   3773   3146    -92   -472    142       O  
ATOM   1309  N   THR A 160      35.646  16.486  24.222  1.00 19.21           N  
ANISOU 1309  N   THR A 160     2873   2279   2149      9   -575    126       N  
ATOM   1310  CA  THR A 160      35.058  15.244  24.770  1.00 19.66           C  
ANISOU 1310  CA  THR A 160     2986   2309   2177    -20   -614    195       C  
ATOM   1311  C   THR A 160      34.914  14.201  23.651  1.00 21.51           C  
ANISOU 1311  C   THR A 160     3236   2477   2460    -16   -638    207       C  
ATOM   1312  O   THR A 160      34.308  13.140  23.868  1.00 21.95           O  
ANISOU 1312  O   THR A 160     3333   2500   2506    -43   -665    263       O  
ATOM   1313  CB  THR A 160      33.622  15.489  25.322  1.00 27.48           C  
ANISOU 1313  CB  THR A 160     3985   3341   3117    -78   -570    239       C  
ATOM   1314  CG2 THR A 160      33.575  16.390  26.527  1.00 32.82           C  
ANISOU 1314  CG2 THR A 160     4643   4089   3737    -88   -550    232       C  
ATOM   1315  OG1 THR A 160      32.733  15.902  24.283  1.00 28.23           O  
ANISOU 1315  OG1 THR A 160     4054   3435   3237    -97   -518    224       O  
ATOM   1316  N   HIS A 161      35.450  14.501  22.450  1.00 18.68           N  
ANISOU 1316  N   HIS A 161     2840   2101   2155     16   -626    153       N  
ATOM   1317  CA  HIS A 161      35.380  13.644  21.247  1.00 17.97           C  
ANISOU 1317  CA  HIS A 161     2751   1961   2117     27   -645    149       C  
ATOM   1318  C   HIS A 161      34.025  13.692  20.535  1.00 19.39           C  
ANISOU 1318  C   HIS A 161     2924   2143   2300     -8   -596    169       C  
ATOM   1319  O   HIS A 161      33.853  13.013  19.514  1.00 20.07           O  
ANISOU 1319  O   HIS A 161     3005   2192   2429      1   -607    163       O  
ATOM   1320  CB  HIS A 161      35.907  12.198  21.514  1.00 20.23           C  
ANISOU 1320  CB  HIS A 161     3078   2187   2420     42   -729    176       C  
ATOM   1321  CG  HIS A 161      37.192  12.190  22.275  1.00 23.49           C  
ANISOU 1321  CG  HIS A 161     3499   2600   2825     78   -779    152       C  
ATOM   1322  CD2 HIS A 161      37.416  11.923  23.583  1.00 26.39           C  
ANISOU 1322  CD2 HIS A 161     3904   2974   3147     74   -815    188       C  
ATOM   1323  ND1 HIS A 161      38.380  12.602  21.691  1.00 25.67           N  
ANISOU 1323  ND1 HIS A 161     3738   2878   3137    125   -789     80       N  
ATOM   1324  CE1 HIS A 161      39.291  12.551  22.656  1.00 25.56           C  
ANISOU 1324  CE1 HIS A 161     3741   2868   3103    150   -832     69       C  
ATOM   1325  NE2 HIS A 161      38.753  12.163  23.814  1.00 26.89           N  
ANISOU 1325  NE2 HIS A 161     3955   3041   3222    122   -850    134       N  
ATOM   1326  N   GLU A 162      33.083  14.535  21.019  1.00 16.12           N  
ANISOU 1326  N   GLU A 162     2504   1776   1844    -45   -541    184       N  
ATOM   1327  CA  GLU A 162      31.769  14.690  20.382  1.00 16.72           C  
ANISOU 1327  CA  GLU A 162     2572   1860   1921    -76   -492    194       C  
ATOM   1328  C   GLU A 162      31.934  15.298  18.998  1.00 16.14           C  
ANISOU 1328  C   GLU A 162     2456   1787   1891    -48   -459    144       C  
ATOM   1329  O   GLU A 162      32.802  16.139  18.782  1.00 16.06           O  
ANISOU 1329  O   GLU A 162     2415   1795   1893    -19   -447    103       O  
ATOM   1330  CB  GLU A 162      30.866  15.592  21.255  1.00 17.58           C  
ANISOU 1330  CB  GLU A 162     2678   2027   1976   -117   -444    207       C  
ATOM   1331  CG  GLU A 162      29.498  15.903  20.663  1.00 27.86           C  
ANISOU 1331  CG  GLU A 162     3968   3343   3274   -149   -392    207       C  
ATOM   1332  CD  GLU A 162      28.530  16.669  21.545  1.00 52.87           C  
ANISOU 1332  CD  GLU A 162     7131   6568   6389   -192   -352    215       C  
ATOM   1333  OE1 GLU A 162      28.267  16.215  22.683  1.00 38.67           O  
ANISOU 1333  OE1 GLU A 162     5362   4786   4545   -225   -370    256       O  
ATOM   1334  OE2 GLU A 162      27.988  17.694  21.071  1.00 51.39           O1-
ANISOU 1334  OE2 GLU A 162     6910   6410   6204   -195   -305    180       O1-
ATOM   1335  N   VAL A 163      31.145  14.842  18.053  1.00 15.29           N  
ANISOU 1335  N   VAL A 163     2344   1658   1806    -54   -444    147       N  
ATOM   1336  CA  VAL A 163      31.227  15.361  16.701  1.00 14.37           C  
ANISOU 1336  CA  VAL A 163     2188   1547   1725    -27   -413    105       C  
ATOM   1337  C   VAL A 163      30.682  16.787  16.635  1.00 15.57           C  
ANISOU 1337  C   VAL A 163     2315   1746   1856    -40   -350     86       C  
ATOM   1338  O   VAL A 163      29.557  17.045  17.076  1.00 16.81           O  
ANISOU 1338  O   VAL A 163     2481   1923   1981    -76   -320    105       O  
ATOM   1339  CB  VAL A 163      30.429  14.417  15.766  1.00 17.70           C  
ANISOU 1339  CB  VAL A 163     2613   1937   2176    -29   -418    112       C  
ATOM   1340  CG1 VAL A 163      30.390  14.952  14.339  1.00 18.84           C  
ANISOU 1340  CG1 VAL A 163     2715   2093   2349      0   -383     70       C  
ATOM   1341  CG2 VAL A 163      31.035  13.012  15.764  1.00 17.72           C  
ANISOU 1341  CG2 VAL A 163     2634   1886   2211    -12   -487    125       C  
ATOM   1342  N   VAL A 164      31.453  17.718  16.092  1.00 14.10           N  
ANISOU 1342  N   VAL A 164     2094   1576   1687    -12   -330     48       N  
ATOM   1343  CA  VAL A 164      30.969  19.096  15.882  1.00 14.13           C  
ANISOU 1343  CA  VAL A 164     2071   1617   1681    -21   -273     29       C  
ATOM   1344  C   VAL A 164      29.972  19.040  14.699  1.00 15.63           C  
ANISOU 1344  C   VAL A 164     2252   1803   1884    -21   -242     25       C  
ATOM   1345  O   VAL A 164      30.272  18.498  13.636  1.00 14.53           O  
ANISOU 1345  O   VAL A 164     2102   1644   1776      6   -253     13       O  
ATOM   1346  CB  VAL A 164      32.145  20.061  15.649  1.00 16.50           C  
ANISOU 1346  CB  VAL A 164     2338   1931   2002      7   -262     -7       C  
ATOM   1347  CG1 VAL A 164      31.638  21.452  15.247  1.00 18.21           C  
ANISOU 1347  CG1 VAL A 164     2525   2176   2219      0   -207    -24       C  
ATOM   1348  CG2 VAL A 164      33.029  20.147  16.890  1.00 16.65           C  
ANISOU 1348  CG2 VAL A 164     2363   1957   2005     10   -291    -10       C  
ATOM   1349  N   THR A 165      28.784  19.587  14.890  1.00 13.47           N  
ANISOU 1349  N   THR A 165     1980   1551   1586    -50   -206     31       N  
ATOM   1350  CA  THR A 165      27.778  19.467  13.860  1.00 11.52           C  
ANISOU 1350  CA  THR A 165     1727   1300   1349    -49   -180     25       C  
ATOM   1351  C   THR A 165      28.118  20.199  12.576  1.00 11.67           C  
ANISOU 1351  C   THR A 165     1714   1326   1394    -15   -153     -3       C  
ATOM   1352  O   THR A 165      28.671  21.289  12.579  1.00 11.42           O  
ANISOU 1352  O   THR A 165     1662   1312   1366     -7   -134    -18       O  
ATOM   1353  CB  THR A 165      26.432  19.953  14.422  1.00 13.58           C  
ANISOU 1353  CB  THR A 165     1996   1587   1576    -87   -149     29       C  
ATOM   1354  CG2 THR A 165      26.356  21.474  14.657  1.00 14.82           C  
ANISOU 1354  CG2 THR A 165     2130   1780   1723    -92   -115      7       C  
ATOM   1355  OG1 THR A 165      25.417  19.600  13.471  1.00 15.52           O  
ANISOU 1355  OG1 THR A 165     2241   1825   1832    -84   -131     21       O  
ATOM   1356  N   LEU A 166      27.749  19.581  11.479  1.00 10.43           N  
ANISOU 1356  N   LEU A 166     1551   1156   1256      4   -152    -10       N  
ATOM   1357  CA  LEU A 166      27.908  20.143  10.135  1.00 10.38           C  
ANISOU 1357  CA  LEU A 166     1514   1161   1268     36   -126    -33       C  
ATOM   1358  C   LEU A 166      26.620  20.766   9.625  1.00  9.98           C  
ANISOU 1358  C   LEU A 166     1461   1127   1205     30    -85    -41       C  
ATOM   1359  O   LEU A 166      26.635  21.364   8.531  1.00 10.69           O  
ANISOU 1359  O   LEU A 166     1528   1230   1304     55    -60    -56       O  
ATOM   1360  CB  LEU A 166      28.303  19.019   9.146  1.00 11.49           C  
ANISOU 1360  CB  LEU A 166     1643   1284   1438     68   -153    -44       C  
ATOM   1361  CG  LEU A 166      29.596  18.276   9.495  1.00 13.11           C  
ANISOU 1361  CG  LEU A 166     1849   1470   1662     81   -202    -45       C  
ATOM   1362  CD1 LEU A 166      29.830  17.183   8.521  1.00 15.10           C  
ANISOU 1362  CD1 LEU A 166     2084   1707   1946    112   -232    -62       C  
ATOM   1363  CD2 LEU A 166      30.778  19.214   9.517  1.00 15.99           C  
ANISOU 1363  CD2 LEU A 166     2194   1851   2030     93   -192    -60       C  
ATOM   1364  N   TRP A 167      25.525  20.642  10.378  1.00  9.27           N  
ANISOU 1364  N   TRP A 167     1391   1039   1092     -4    -79    -32       N  
ATOM   1365  CA  TRP A 167      24.217  20.929   9.816  1.00  9.36           C  
ANISOU 1365  CA  TRP A 167     1400   1062   1093     -7    -49    -48       C  
ATOM   1366  C   TRP A 167      24.015  22.336   9.349  1.00  8.94           C  
ANISOU 1366  C   TRP A 167     1330   1031   1036      3    -14    -65       C  
ATOM   1367  O   TRP A 167      23.144  22.619   8.490  1.00  9.52           O  
ANISOU 1367  O   TRP A 167     1396   1112   1108     18     10    -82       O  
ATOM   1368  CB  TRP A 167      23.111  20.588  10.811  1.00  9.84           C  
ANISOU 1368  CB  TRP A 167     1484   1126   1128    -50    -48    -41       C  
ATOM   1369  CG  TRP A 167      23.064  19.147  11.246  1.00  9.65           C  
ANISOU 1369  CG  TRP A 167     1482   1076   1109    -65    -80    -19       C  
ATOM   1370  CD1 TRP A 167      23.840  18.109  10.808  1.00 11.69           C  
ANISOU 1370  CD1 TRP A 167     1739   1304   1397    -41   -115    -10       C  
ATOM   1371  CD2 TRP A 167      22.148  18.599  12.193  1.00 10.32           C  
ANISOU 1371  CD2 TRP A 167     1592   1161   1171   -110    -83     -4       C  
ATOM   1372  CE2 TRP A 167      22.426  17.218  12.300  1.00 12.09           C  
ANISOU 1372  CE2 TRP A 167     1832   1349   1414   -112   -119     21       C  
ATOM   1373  CE3 TRP A 167      21.155  19.162  13.013  1.00 11.28           C  
ANISOU 1373  CE3 TRP A 167     1720   1311   1255   -152    -60    -10       C  
ATOM   1374  NE1 TRP A 167      23.437  16.931  11.418  1.00 11.28           N  
ANISOU 1374  NE1 TRP A 167     1712   1227   1346    -67   -140     13       N  
ATOM   1375  CZ2 TRP A 167      21.683  16.372  13.128  1.00 13.64           C  
ANISOU 1375  CZ2 TRP A 167     2055   1533   1594   -156   -129     45       C  
ATOM   1376  CZ3 TRP A 167      20.394  18.323  13.826  1.00 13.61           C  
ANISOU 1376  CZ3 TRP A 167     2039   1603   1531   -196    -66      9       C  
ATOM   1377  CH2 TRP A 167      20.674  16.949  13.893  1.00 14.06           C  
ANISOU 1377  CH2 TRP A 167     2116   1621   1607   -199    -99     41       C  
ATOM   1378  N   TYR A 168      24.750  23.269   9.940  1.00  8.73           N  
ANISOU 1378  N   TYR A 168     1295   1013   1008     -4    -10    -61       N  
ATOM   1379  CA  TYR A 168      24.568  24.698   9.672  1.00  8.77           C  
ANISOU 1379  CA  TYR A 168     1282   1034   1014     -1     19    -75       C  
ATOM   1380  C   TYR A 168      25.717  25.276   8.872  1.00  8.76           C  
ANISOU 1380  C   TYR A 168     1261   1031   1038     29     27    -72       C  
ATOM   1381  O   TYR A 168      25.796  26.506   8.704  1.00  9.53           O  
ANISOU 1381  O   TYR A 168     1343   1134   1143     30     49    -77       O  
ATOM   1382  CB  TYR A 168      24.399  25.456  11.022  1.00  9.28           C  
ANISOU 1382  CB  TYR A 168     1347   1114   1063    -35     19    -79       C  
ATOM   1383  CG  TYR A 168      23.350  24.765  11.880  1.00  8.78           C  
ANISOU 1383  CG  TYR A 168     1305   1060    971    -70     10    -79       C  
ATOM   1384  CD1 TYR A 168      21.993  24.991  11.668  1.00  9.69           C  
ANISOU 1384  CD1 TYR A 168     1422   1187   1071    -82     29   -100       C  
ATOM   1385  CD2 TYR A 168      23.718  23.823  12.852  1.00  9.63           C  
ANISOU 1385  CD2 TYR A 168     1431   1163   1065    -91    -17    -57       C  
ATOM   1386  CE1 TYR A 168      21.027  24.270  12.365  1.00 10.56           C  
ANISOU 1386  CE1 TYR A 168     1550   1307   1155   -116     24   -102       C  
ATOM   1387  CE2 TYR A 168      22.768  23.107  13.557  1.00 10.13           C  
ANISOU 1387  CE2 TYR A 168     1514   1234   1100   -126    -23    -51       C  
ATOM   1388  CZ  TYR A 168      21.422  23.321  13.295  1.00 10.01           C  
ANISOU 1388  CZ  TYR A 168     1499   1233   1072   -140      0    -74       C  
ATOM   1389  OH  TYR A 168      20.496  22.593  13.987  1.00 10.80           O  
ANISOU 1389  OH  TYR A 168     1617   1341   1144   -178     -3    -69       O  
ATOM   1390  N   ARG A 169      26.586  24.415   8.343  1.00  8.86           N  
ANISOU 1390  N   ARG A 169     1269   1033   1064     51      9    -67       N  
ATOM   1391  CA  ARG A 169      27.773  24.866   7.641  1.00  9.46           C  
ANISOU 1391  CA  ARG A 169     1322   1111   1160     74     16    -68       C  
ATOM   1392  C   ARG A 169      27.468  25.314   6.209  1.00  9.67           C  
ANISOU 1392  C   ARG A 169     1333   1150   1190    101     44    -71       C  
ATOM   1393  O   ARG A 169      26.869  24.555   5.437  1.00 10.28           O  
ANISOU 1393  O   ARG A 169     1412   1230   1262    120     42    -76       O  
ATOM   1394  CB  ARG A 169      28.818  23.723   7.658  1.00 11.23           C  
ANISOU 1394  CB  ARG A 169     1544   1325   1397     87    -19    -69       C  
ATOM   1395  CG  ARG A 169      30.158  24.128   7.061  1.00 11.66           C  
ANISOU 1395  CG  ARG A 169     1572   1386   1471    107    -14    -77       C  
ATOM   1396  CD  ARG A 169      31.231  23.082   7.279  1.00 12.62           C  
ANISOU 1396  CD  ARG A 169     1690   1498   1606    118    -55    -87       C  
ATOM   1397  NE  ARG A 169      31.587  23.038   8.699  1.00 13.93           N  
ANISOU 1397  NE  ARG A 169     1874   1652   1768     97    -78    -83       N  
ATOM   1398  CZ  ARG A 169      32.477  22.218   9.238  1.00 15.69           C  
ANISOU 1398  CZ  ARG A 169     2102   1861   1999    102   -120    -91       C  
ATOM   1399  NH1 ARG A 169      33.174  21.382   8.468  1.00 16.18           N1+
ANISOU 1399  NH1 ARG A 169     2149   1919   2079    128   -145   -108       N1+
ATOM   1400  NH2 ARG A 169      32.682  22.231  10.551  1.00 17.02           N  
ANISOU 1400  NH2 ARG A 169     2287   2022   2157     84   -139    -85       N  
ATOM   1401  N   ALA A 170      27.985  26.502   5.828  1.00  8.62           N  
ANISOU 1401  N   ALA A 170     1184   1023   1067    105     70    -66       N  
ATOM   1402  CA  ALA A 170      27.783  27.048   4.500  1.00  8.65           C  
ANISOU 1402  CA  ALA A 170     1176   1041   1071    130     97    -62       C  
ATOM   1403  C   ALA A 170      28.481  26.205   3.424  1.00  9.83           C  
ANISOU 1403  C   ALA A 170     1306   1205   1223    160     90    -66       C  
ATOM   1404  O   ALA A 170      29.547  25.600   3.639  1.00  9.87           O  
ANISOU 1404  O   ALA A 170     1301   1209   1241    161     69    -73       O  
ATOM   1405  CB  ALA A 170      28.296  28.469   4.479  1.00 10.00           C  
ANISOU 1405  CB  ALA A 170     1333   1209   1256    122    122    -51       C  
ATOM   1406  N   PRO A 171      27.900  26.206   2.205  1.00  9.24           N  
ANISOU 1406  N   PRO A 171     1224   1148   1137    187    108    -66       N  
ATOM   1407  CA  PRO A 171      28.470  25.358   1.146  1.00  9.65           C  
ANISOU 1407  CA  PRO A 171     1252   1224   1190    218     99    -76       C  
ATOM   1408  C   PRO A 171      29.874  25.753   0.756  1.00 10.82           C  
ANISOU 1408  C   PRO A 171     1375   1387   1349    220    108    -72       C  
ATOM   1409  O   PRO A 171      30.669  24.879   0.392  1.00 11.04           O  
ANISOU 1409  O   PRO A 171     1380   1429   1384    236     87    -91       O  
ATOM   1410  CB  PRO A 171      27.430  25.461   0.017  1.00 10.98           C  
ANISOU 1410  CB  PRO A 171     1418   1413   1340    247    119    -79       C  
ATOM   1411  CG  PRO A 171      26.762  26.822   0.267  1.00 12.42           C  
ANISOU 1411  CG  PRO A 171     1620   1585   1516    231    146    -61       C  
ATOM   1412  CD  PRO A 171      26.674  26.891   1.771  1.00 10.69           C  
ANISOU 1412  CD  PRO A 171     1420   1337   1307    193    130    -63       C  
ATOM   1413  N   GLU A 172      30.203  27.045   0.836  1.00 10.12           N  
ANISOU 1413  N   GLU A 172     1286   1295   1265    204    136    -53       N  
ATOM   1414  CA  GLU A 172      31.560  27.430   0.474  1.00 10.65           C  
ANISOU 1414  CA  GLU A 172     1326   1377   1343    202    148    -51       C  
ATOM   1415  C   GLU A 172      32.582  26.863   1.433  1.00 11.66           C  
ANISOU 1415  C   GLU A 172     1449   1490   1490    189    118    -72       C  
ATOM   1416  O   GLU A 172      33.704  26.571   0.994  1.00 12.85           O  
ANISOU 1416  O   GLU A 172     1574   1661   1649    197    113    -88       O  
ATOM   1417  CB  GLU A 172      31.698  28.960   0.350  1.00 11.32           C  
ANISOU 1417  CB  GLU A 172     1410   1455   1435    186    185    -24       C  
ATOM   1418  CG  GLU A 172      31.376  29.805   1.582  1.00 11.34           C  
ANISOU 1418  CG  GLU A 172     1431   1423   1456    157    186    -19       C  
ATOM   1419  CD  GLU A 172      29.921  30.218   1.748  1.00 11.46           C  
ANISOU 1419  CD  GLU A 172     1470   1424   1458    156    189    -11       C  
ATOM   1420  OE1 GLU A 172      29.030  29.465   1.282  1.00 10.64           O  
ANISOU 1420  OE1 GLU A 172     1378   1332   1333    176    181    -18       O  
ATOM   1421  OE2 GLU A 172      29.679  31.311   2.321  1.00 11.70           O1-
ANISOU 1421  OE2 GLU A 172     1506   1434   1505    137    199     -3       O1-
ATOM   1422  N   ILE A 173      32.233  26.661   2.716  1.00 10.33           N  
ANISOU 1422  N   ILE A 173     1305   1293   1328    170     96    -76       N  
ATOM   1423  CA  ILE A 173      33.189  26.057   3.629  1.00 10.76           C  
ANISOU 1423  CA  ILE A 173     1357   1334   1396    163     63    -95       C  
ATOM   1424  C   ILE A 173      33.352  24.576   3.249  1.00 13.00           C  
ANISOU 1424  C   ILE A 173     1635   1625   1679    185     24   -116       C  
ATOM   1425  O   ILE A 173      34.483  24.078   3.153  1.00 13.34           O  
ANISOU 1425  O   ILE A 173     1658   1675   1736    194      3   -140       O  
ATOM   1426  CB  ILE A 173      32.710  26.202   5.081  1.00 11.31           C  
ANISOU 1426  CB  ILE A 173     1453   1378   1466    138     48    -90       C  
ATOM   1427  CG1 ILE A 173      32.614  27.686   5.480  1.00 12.28           C  
ANISOU 1427  CG1 ILE A 173     1573   1494   1597    118     80    -79       C  
ATOM   1428  CG2 ILE A 173      33.700  25.467   6.025  1.00 12.97           C  
ANISOU 1428  CG2 ILE A 173     1665   1577   1687    135      9   -110       C  
ATOM   1429  CD1 ILE A 173      32.011  27.897   6.898  1.00 14.22           C  
ANISOU 1429  CD1 ILE A 173     1838   1725   1839     94     67    -79       C  
ATOM   1430  N   LEU A 174      32.242  23.887   2.984  1.00 11.79           N  
ANISOU 1430  N   LEU A 174     1496   1470   1514    195     15   -111       N  
ATOM   1431  CA  LEU A 174      32.258  22.479   2.585  1.00 12.79           C  
ANISOU 1431  CA  LEU A 174     1613   1599   1647    217    -22   -132       C  
ATOM   1432  C   LEU A 174      33.012  22.265   1.287  1.00 14.17           C  
ANISOU 1432  C   LEU A 174     1747   1811   1826    246    -19   -154       C  
ATOM   1433  O   LEU A 174      33.603  21.204   1.093  1.00 15.56           O  
ANISOU 1433  O   LEU A 174     1903   1991   2017    264    -58   -182       O  
ATOM   1434  CB  LEU A 174      30.827  21.970   2.442  1.00 12.72           C  
ANISOU 1434  CB  LEU A 174     1622   1582   1628    222    -23   -125       C  
ATOM   1435  CG  LEU A 174      30.046  21.859   3.764  1.00 13.02           C  
ANISOU 1435  CG  LEU A 174     1699   1588   1660    191    -34   -110       C  
ATOM   1436  CD1 LEU A 174      28.562  21.848   3.525  1.00 13.83           C  
ANISOU 1436  CD1 LEU A 174     1815   1690   1748    191    -17   -105       C  
ATOM   1437  CD2 LEU A 174      30.456  20.598   4.560  1.00 15.75           C  
ANISOU 1437  CD2 LEU A 174     2056   1907   2021    186    -86   -116       C  
ATOM   1438  N   LEU A 175      33.002  23.242   0.398  1.00 12.75           N  
ANISOU 1438  N   LEU A 175     1283   1749   1814    -28    137   -735       N  
ATOM   1439  CA  LEU A 175      33.681  23.164  -0.893  1.00 12.74           C  
ANISOU 1439  CA  LEU A 175     1236   1760   1843    -64    213   -675       C  
ATOM   1440  C   LEU A 175      35.129  23.623  -0.826  1.00 16.47           C  
ANISOU 1440  C   LEU A 175     1632   2189   2438    -58    186   -666       C  
ATOM   1441  O   LEU A 175      35.802  23.647  -1.851  1.00 16.23           O  
ANISOU 1441  O   LEU A 175     1561   2161   2445   -106    240   -641       O  
ATOM   1442  CB  LEU A 175      32.886  23.868  -1.982  1.00 13.36           C  
ANISOU 1442  CB  LEU A 175     1312   1864   1901   -128    238   -621       C  
ATOM   1443  CG  LEU A 175      31.609  23.155  -2.339  1.00 14.98           C  
ANISOU 1443  CG  LEU A 175     1594   2130   1968   -147    301   -616       C  
ATOM   1444  CD1 LEU A 175      30.715  24.022  -3.239  1.00 18.72           C  
ANISOU 1444  CD1 LEU A 175     2057   2616   2439   -214    296   -550       C  
ATOM   1445  CD2 LEU A 175      31.894  21.798  -3.030  1.00 16.39           C  
ANISOU 1445  CD2 LEU A 175     1802   2361   2065   -179    430   -603       C  
ATOM   1446  N   GLY A 176      35.617  23.962   0.365  1.00 15.92           N  
ANISOU 1446  N   GLY A 176     1544   2081   2422    -16    108   -692       N  
ATOM   1447  CA  GLY A 176      37.042  24.242   0.564  1.00 17.24           C  
ANISOU 1447  CA  GLY A 176     1647   2215   2687     -3     88   -685       C  
ATOM   1448  C   GLY A 176      37.512  25.671   0.482  1.00 21.07           C  
ANISOU 1448  C   GLY A 176     2085   2688   3232    -18     50   -666       C  
ATOM   1449  O   GLY A 176      38.728  25.912   0.397  1.00 21.06           O  
ANISOU 1449  O   GLY A 176     2038   2674   3291    -13     49   -664       O  
ATOM   1450  N   CYS A 177      36.608  26.627   0.544  1.00 18.19           N  
ANISOU 1450  N   CYS A 177     1729   2326   2855    -34     19   -658       N  
ATOM   1451  CA  CYS A 177      36.973  28.041   0.621  1.00 19.35           C  
ANISOU 1451  CA  CYS A 177     1835   2462   3057    -45    -17   -641       C  
ATOM   1452  C   CYS A 177      37.478  28.237   2.083  1.00 22.21           C  
ANISOU 1452  C   CYS A 177     2181   2806   3452    -25    -53   -658       C  
ATOM   1453  O   CYS A 177      36.723  27.966   3.030  1.00 25.19           O  
ANISOU 1453  O   CYS A 177     2585   3171   3814    -34    -77   -688       O  
ATOM   1454  CB  CYS A 177      35.740  28.899   0.337  1.00 20.23           C  
ANISOU 1454  CB  CYS A 177     1951   2568   3167    -71    -40   -627       C  
ATOM   1455  SG  CYS A 177      35.995  30.693   0.362  1.00 25.71           S  
ANISOU 1455  SG  CYS A 177     2593   3243   3933    -89    -81   -605       S  
ATOM   1456  N   LYS A 178      38.712  28.656   2.257  1.00 24.43           N  
ANISOU 1456  N   LYS A 178     2425   3088   3769    -17    -55   -645       N  
ATOM   1457  CA  LYS A 178      39.247  28.935   3.582  1.00 24.12           C  
ANISOU 1457  CA  LYS A 178     2368   3041   3756    -24    -78   -641       C  
ATOM   1458  C   LYS A 178      39.195  30.455   3.849  1.00 26.03           C  
ANISOU 1458  C   LYS A 178     2581   3291   4016    -51    -76   -628       C  
ATOM   1459  O   LYS A 178      39.457  30.859   4.972  1.00 26.34           O  
ANISOU 1459  O   LYS A 178     2604   3331   4074    -86    -78   -620       O  
ATOM   1460  CB  LYS A 178      40.686  28.399   3.739  1.00 28.41           C  
ANISOU 1460  CB  LYS A 178     2885   3584   4325     -1    -75   -626       C  
ATOM   1461  CG  LYS A 178      40.742  26.873   3.716  1.00 42.12           C  
ANISOU 1461  CG  LYS A 178     4637   5298   6068     22    -79   -638       C  
ATOM   1462  CD  LYS A 178      42.123  26.331   4.035  1.00 55.02           C  
ANISOU 1462  CD  LYS A 178     6231   6914   7761     43    -88   -622       C  
ATOM   1463  CE  LYS A 178      42.172  24.822   3.953  1.00 68.69           C  
ANISOU 1463  CE  LYS A 178     7968   8612   9519     66    -90   -633       C  
ATOM   1464  NZ  LYS A 178      41.410  24.169   5.056  1.00 79.46           N1+
ANISOU 1464  NZ  LYS A 178     9376   9962  10853     41   -147   -632       N1+
ATOM   1465  N   TYR A 179      38.818  31.283   2.835  1.00 23.18           N  
ANISOU 1465  N   TYR A 179     2216   2938   3655    -52    -72   -621       N  
ATOM   1466  CA  TYR A 179      38.762  32.762   2.944  1.00 23.56           C  
ANISOU 1466  CA  TYR A 179     2235   2989   3726    -74    -70   -607       C  
ATOM   1467  C   TYR A 179      37.351  33.234   2.724  1.00 26.50           C  
ANISOU 1467  C   TYR A 179     2604   3331   4136    -94    -89   -613       C  
ATOM   1468  O   TYR A 179      37.053  34.054   1.855  1.00 28.04           O  
ANISOU 1468  O   TYR A 179     2786   3520   4348   -103   -107   -592       O  
ATOM   1469  CB  TYR A 179      39.744  33.403   1.954  1.00 26.38           C  
ANISOU 1469  CB  TYR A 179     2591   3379   4054    -67    -67   -596       C  
ATOM   1470  CG  TYR A 179      41.129  32.822   2.109  1.00 27.91           C  
ANISOU 1470  CG  TYR A 179     2786   3598   4220    -45    -48   -605       C  
ATOM   1471  CD1 TYR A 179      41.990  33.281   3.102  1.00 28.50           C  
ANISOU 1471  CD1 TYR A 179     2845   3699   4285    -44    -25   -590       C  
ATOM   1472  CD2 TYR A 179      41.536  31.726   1.349  1.00 29.45           C  
ANISOU 1472  CD2 TYR A 179     2992   3787   4411    -35    -44   -626       C  
ATOM   1473  CE1 TYR A 179      43.244  32.702   3.295  1.00 28.97           C  
ANISOU 1473  CE1 TYR A 179     2898   3775   4332    -23    -15   -592       C  
ATOM   1474  CE2 TYR A 179      42.783  31.135   1.539  1.00 30.44           C  
ANISOU 1474  CE2 TYR A 179     3104   3920   4543    -13    -29   -641       C  
ATOM   1475  CZ  TYR A 179      43.638  31.629   2.510  1.00 34.73           C  
ANISOU 1475  CZ  TYR A 179     3631   4485   5078     -1    -22   -622       C  
ATOM   1476  OH  TYR A 179      44.876  31.045   2.682  1.00 34.69           O  
ANISOU 1476  OH  TYR A 179     3608   4483   5091     21    -14   -632       O  
ATOM   1477  N   TYR A 180      36.470  32.662   3.502  1.00 22.57           N  
ANISOU 1477  N   TYR A 180     2117   2808   3650   -110    -93   -647       N  
ATOM   1478  CA  TYR A 180      35.047  32.935   3.454  1.00 22.19           C  
ANISOU 1478  CA  TYR A 180     2065   2723   3643   -130   -110   -672       C  
ATOM   1479  C   TYR A 180      34.703  34.270   4.165  1.00 23.89           C  
ANISOU 1479  C   TYR A 180     2223   2906   3949   -175    -98   -686       C  
ATOM   1480  O   TYR A 180      35.546  34.942   4.792  1.00 25.67           O  
ANISOU 1480  O   TYR A 180     2418   3147   4187   -197    -65   -673       O  
ATOM   1481  CB  TYR A 180      34.238  31.715   3.947  1.00 23.13           C  
ANISOU 1481  CB  TYR A 180     2234   2836   3718   -137   -118   -726       C  
ATOM   1482  CG  TYR A 180      34.724  31.259   5.303  1.00 26.67           C  
ANISOU 1482  CG  TYR A 180     2691   3285   4157   -178   -116   -763       C  
ATOM   1483  CD1 TYR A 180      34.443  32.000   6.449  1.00 29.66           C  
ANISOU 1483  CD1 TYR A 180     3035   3636   4598   -259   -107   -804       C  
ATOM   1484  CD2 TYR A 180      35.566  30.161   5.426  1.00 26.81           C  
ANISOU 1484  CD2 TYR A 180     2741   3325   4119   -154   -122   -749       C  
ATOM   1485  CE1 TYR A 180      34.975  31.649   7.683  1.00 33.84           C  
ANISOU 1485  CE1 TYR A 180     3569   4169   5119   -335   -108   -823       C  
ATOM   1486  CE2 TYR A 180      36.070  29.774   6.663  1.00 29.06           C  
ANISOU 1486  CE2 TYR A 180     3030   3606   4405   -209   -138   -764       C  
ATOM   1487  CZ  TYR A 180      35.789  30.535   7.785  1.00 41.55           C  
ANISOU 1487  CZ  TYR A 180     4584   5169   6035   -308   -133   -796       C  
ATOM   1488  OH  TYR A 180      36.319  30.186   8.998  1.00 49.95           O  
ANISOU 1488  OH  TYR A 180     5651   6231   7098   -398   -150   -799       O  
ATOM   1489  N   SER A 181      33.444  34.650   4.017  1.00 16.89           N  
ANISOU 1489  N   SER A 181     1994   2143   2282   -139    313    -99       N  
ATOM   1490  CA  SER A 181      32.904  35.950   4.388  1.00 14.98           C  
ANISOU 1490  CA  SER A 181     1754   1842   2096   -172    341   -110       C  
ATOM   1491  C   SER A 181      31.840  35.858   5.467  1.00 13.93           C  
ANISOU 1491  C   SER A 181     1630   1705   1958   -170    307   -141       C  
ATOM   1492  O   SER A 181      31.432  34.769   5.900  1.00 13.23           O  
ANISOU 1492  O   SER A 181     1551   1655   1822   -146    264   -146       O  
ATOM   1493  CB  SER A 181      32.306  36.581   3.130  1.00 17.02           C  
ANISOU 1493  CB  SER A 181     2051   2047   2369   -151    375    -48       C  
ATOM   1494  OG  SER A 181      31.043  36.002   2.827  1.00 15.28           O  
ANISOU 1494  OG  SER A 181     1870   1824   2111   -107    343    -22       O  
ATOM   1495  N   THR A 182      31.342  37.020   5.872  1.00 12.54           N  
ANISOU 1495  N   THR A 182     1451   1478   1834   -196    330   -161       N  
ATOM   1496  CA  THR A 182      30.239  37.119   6.828  1.00 12.03           C  
ANISOU 1496  CA  THR A 182     1394   1407   1769   -196    306   -192       C  
ATOM   1497  C   THR A 182      29.020  36.357   6.321  1.00 12.13           C  
ANISOU 1497  C   THR A 182     1449   1420   1740   -150    278   -151       C  
ATOM   1498  O   THR A 182      28.152  35.989   7.121  1.00 12.09           O  
ANISOU 1498  O   THR A 182     1448   1431   1715   -145    250   -174       O  
ATOM   1499  CB  THR A 182      29.939  38.589   7.079  1.00 15.47           C  
ANISOU 1499  CB  THR A 182     1823   1779   2277   -225    341   -216       C  
ATOM   1500  CG2 THR A 182      31.082  39.326   7.805  1.00 15.94           C  
ANISOU 1500  CG2 THR A 182     1831   1841   2384   -278    365   -277       C  
ATOM   1501  OG1 THR A 182      29.632  39.214   5.836  1.00 15.73           O  
ANISOU 1501  OG1 THR A 182     1890   1751   2337   -207    375   -156       O  
ATOM   1502  N   ALA A 183      28.924  36.091   5.024  1.00 11.45           N  
ANISOU 1502  N   ALA A 183     1392   1323   1637   -117    286    -96       N  
ATOM   1503  CA  ALA A 183      27.816  35.329   4.497  1.00 10.70           C  
ANISOU 1503  CA  ALA A 183     1330   1234   1503    -75    258    -67       C  
ATOM   1504  C   ALA A 183      27.681  33.944   5.128  1.00 10.92           C  
ANISOU 1504  C   ALA A 183     1355   1312   1482    -66    214    -85       C  
ATOM   1505  O   ALA A 183      26.584  33.369   5.107  1.00 10.39           O  
ANISOU 1505  O   ALA A 183     1307   1247   1393    -44    190    -79       O  
ATOM   1506  CB  ALA A 183      27.910  35.198   2.972  1.00 11.63           C  
ANISOU 1506  CB  ALA A 183     1472   1346   1602    -38    272    -11       C  
ATOM   1507  N   VAL A 184      28.785  33.374   5.645  1.00 10.57           N  
ANISOU 1507  N   VAL A 184     1286   1307   1421    -80    205   -104       N  
ATOM   1508  CA  VAL A 184      28.648  32.034   6.242  1.00  9.55           C  
ANISOU 1508  CA  VAL A 184     1160   1220   1249    -66    165   -112       C  
ATOM   1509  C   VAL A 184      27.665  32.056   7.422  1.00  9.71           C  
ANISOU 1509  C   VAL A 184     1180   1243   1267    -80    149   -139       C  
ATOM   1510  O   VAL A 184      26.962  31.072   7.678  1.00  9.83           O  
ANISOU 1510  O   VAL A 184     1212   1272   1252    -66    123   -131       O  
ATOM   1511  CB  VAL A 184      29.992  31.428   6.663  1.00 11.62           C  
ANISOU 1511  CB  VAL A 184     1395   1527   1492    -71    155   -127       C  
ATOM   1512  CG1 VAL A 184      30.941  31.357   5.496  1.00 12.19           C  
ANISOU 1512  CG1 VAL A 184     1464   1604   1564    -56    172   -104       C  
ATOM   1513  CG2 VAL A 184      30.646  32.142   7.858  1.00 12.39           C  
ANISOU 1513  CG2 VAL A 184     1454   1646   1609   -108    162   -175       C  
ATOM   1514  N   ASP A 185      27.586  33.184   8.158  1.00  9.32           N  
ANISOU 1514  N   ASP A 185     1111   1180   1251   -111    167   -173       N  
ATOM   1515  CA  ASP A 185      26.690  33.270   9.305  1.00  9.41           C  
ANISOU 1515  CA  ASP A 185     1116   1203   1257   -124    155   -204       C  
ATOM   1516  C   ASP A 185      25.255  33.427   8.876  1.00 10.28           C  
ANISOU 1516  C   ASP A 185     1251   1281   1375   -107    155   -189       C  
ATOM   1517  O   ASP A 185      24.351  32.939   9.561  1.00  9.40           O  
ANISOU 1517  O   ASP A 185     1143   1187   1242   -108    138   -200       O  
ATOM   1518  CB  ASP A 185      27.104  34.423  10.181  1.00 10.94           C  
ANISOU 1518  CB  ASP A 185     1275   1396   1485   -158    174   -255       C  
ATOM   1519  CG  ASP A 185      28.415  34.240  10.910  1.00 10.94           C  
ANISOU 1519  CG  ASP A 185     1240   1446   1472   -176    167   -287       C  
ATOM   1520  OD1 ASP A 185      28.813  33.065  11.160  1.00 11.80           O  
ANISOU 1520  OD1 ASP A 185     1351   1600   1531   -158    141   -272       O  
ATOM   1521  OD2 ASP A 185      29.011  35.260  11.298  1.00 12.01           O1-
ANISOU 1521  OD2 ASP A 185     1343   1575   1647   -205    188   -331       O1-
ATOM   1522  N   ILE A 186      25.018  34.113   7.747  1.00 10.06           N  
ANISOU 1522  N   ILE A 186     1240   1208   1375    -91    175   -164       N  
ATOM   1523  CA  ILE A 186      23.670  34.244   7.198  1.00  9.28           C  
ANISOU 1523  CA  ILE A 186     1162   1084   1280    -66    170   -150       C  
ATOM   1524  C   ILE A 186      23.159  32.891   6.768  1.00  9.46           C  
ANISOU 1524  C   ILE A 186     1202   1131   1260    -42    142   -128       C  
ATOM   1525  O   ILE A 186      21.997  32.574   7.033  1.00  9.30           O  
ANISOU 1525  O   ILE A 186     1186   1115   1231    -36    128   -138       O  
ATOM   1526  CB  ILE A 186      23.657  35.271   6.040  1.00 10.62           C  
ANISOU 1526  CB  ILE A 186     1347   1205   1484    -46    198   -119       C  
ATOM   1527  CG1 ILE A 186      23.925  36.692   6.596  1.00 12.30           C  
ANISOU 1527  CG1 ILE A 186     1542   1377   1752    -75    228   -148       C  
ATOM   1528  CG2 ILE A 186      22.337  35.222   5.254  1.00 11.40           C  
ANISOU 1528  CG2 ILE A 186     1468   1290   1574     -6    186    -99       C  
ATOM   1529  CD1 ILE A 186      22.704  37.241   7.455  1.00 15.78           C  
ANISOU 1529  CD1 ILE A 186     1975   1807   2212    -78    222   -189       C  
ATOM   1530  N   TRP A 187      24.004  32.063   6.143  1.00  8.61           N  
ANISOU 1530  N   TRP A 187     1102   1040   1130    -29    134   -104       N  
ATOM   1531  CA  TRP A 187      23.578  30.708   5.781  1.00  8.58           C  
ANISOU 1531  CA  TRP A 187     1114   1055   1094     -8    107    -91       C  
ATOM   1532  C   TRP A 187      23.152  29.950   7.045  1.00  8.97           C  
ANISOU 1532  C   TRP A 187     1156   1126   1126    -29     90   -111       C  
ATOM   1533  O   TRP A 187      22.092  29.327   7.079  1.00  8.90           O  
ANISOU 1533  O   TRP A 187     1155   1117   1108    -25     77   -113       O  
ATOM   1534  CB  TRP A 187      24.758  29.983   5.108  1.00  9.30           C  
ANISOU 1534  CB  TRP A 187     1207   1161   1165      8    103    -71       C  
ATOM   1535  CG  TRP A 187      24.410  28.565   4.780  1.00  8.72           C  
ANISOU 1535  CG  TRP A 187     1148   1100   1066     29     75    -65       C  
ATOM   1536  CD1 TRP A 187      24.439  27.473   5.616  1.00 10.52           C  
ANISOU 1536  CD1 TRP A 187     1377   1341   1278     19     55    -71       C  
ATOM   1537  CD2 TRP A 187      23.954  28.095   3.516  1.00  9.00           C  
ANISOU 1537  CD2 TRP A 187     1198   1132   1091     64     65    -52       C  
ATOM   1538  CE2 TRP A 187      23.668  26.716   3.659  1.00  9.97           C  
ANISOU 1538  CE2 TRP A 187     1329   1261   1200     69     39    -59       C  
ATOM   1539  CE3 TRP A 187      23.685  28.721   2.289  1.00 10.22           C  
ANISOU 1539  CE3 TRP A 187     1360   1280   1245     93     76    -37       C  
ATOM   1540  NE1 TRP A 187      24.033  26.351   4.930  1.00  9.73           N  
ANISOU 1540  NE1 TRP A 187     1293   1238   1168     42     35    -65       N  
ATOM   1541  CZ2 TRP A 187      23.190  25.950   2.590  1.00 10.10           C  
ANISOU 1541  CZ2 TRP A 187     1354   1277   1206    100     23    -61       C  
ATOM   1542  CZ3 TRP A 187      23.249  27.946   1.237  1.00 10.90           C  
ANISOU 1542  CZ3 TRP A 187     1454   1377   1310    128     57    -35       C  
ATOM   1543  CH2 TRP A 187      22.992  26.582   1.413  1.00 11.23           C  
ANISOU 1543  CH2 TRP A 187     1498   1424   1342    130     30    -53       C  
ATOM   1544  N   SER A 188      24.009  29.931   8.060  1.00  8.59           N  
ANISOU 1544  N   SER A 188     1092   1101   1070    -51     91   -124       N  
ATOM   1545  CA  SER A 188      23.691  29.179   9.274  1.00  8.52           C  
ANISOU 1545  CA  SER A 188     1079   1120   1036    -67     77   -134       C  
ATOM   1546  C   SER A 188      22.383  29.647   9.866  1.00  8.38           C  
ANISOU 1546  C   SER A 188     1057   1099   1027    -82     83   -155       C  
ATOM   1547  O   SER A 188      21.541  28.845  10.267  1.00  8.88           O  
ANISOU 1547  O   SER A 188     1128   1172   1075    -87     74   -151       O  
ATOM   1548  CB  SER A 188      24.784  29.362  10.306  1.00  9.94           C  
ANISOU 1548  CB  SER A 188     1237   1336   1204    -84     77   -152       C  
ATOM   1549  OG  SER A 188      26.052  28.943   9.808  1.00  9.51           O  
ANISOU 1549  OG  SER A 188     1182   1291   1142    -69     71   -137       O  
ATOM   1550  N   LEU A 189      22.192  30.966   9.927  1.00  8.73           N  
ANISOU 1550  N   LEU A 189     1087   1128   1101    -91    101   -180       N  
ATOM   1551  CA  LEU A 189      20.948  31.481  10.497  1.00  8.85           C  
ANISOU 1551  CA  LEU A 189     1093   1143   1127   -101    106   -207       C  
ATOM   1552  C   LEU A 189      19.738  31.125   9.631  1.00  9.14           C  
ANISOU 1552  C   LEU A 189     1145   1161   1167    -80     99   -194       C  
ATOM   1553  O   LEU A 189      18.664  30.843  10.202  1.00  9.46           O  
ANISOU 1553  O   LEU A 189     1178   1216   1200    -90     96   -210       O  
ATOM   1554  CB  LEU A 189      21.060  32.996  10.721  1.00  9.46           C  
ANISOU 1554  CB  LEU A 189     1152   1200   1242   -111    127   -240       C  
ATOM   1555  CG  LEU A 189      19.909  33.652  11.429  1.00 11.05           C  
ANISOU 1555  CG  LEU A 189     1338   1405   1456   -119    133   -278       C  
ATOM   1556  CD1 LEU A 189      19.677  33.024  12.823  1.00 12.91           C  
ANISOU 1556  CD1 LEU A 189     1557   1696   1652   -143    126   -300       C  
ATOM   1557  CD2 LEU A 189      20.228  35.132  11.621  1.00 12.87           C  
ANISOU 1557  CD2 LEU A 189     1551   1606   1733   -128    153   -313       C  
ATOM   1558  N   GLY A 190      19.913  31.057   8.307  1.00  8.80           N  
ANISOU 1558  N   GLY A 190     1118   1093   1132    -51     96   -168       N  
ATOM   1559  CA  GLY A 190      18.795  30.636   7.473  1.00  8.78           C  
ANISOU 1559  CA  GLY A 190     1124   1083   1127    -27     84   -163       C  
ATOM   1560  C   GLY A 190      18.413  29.195   7.785  1.00  8.33           C  
ANISOU 1560  C   GLY A 190     1072   1046   1048    -39     68   -160       C  
ATOM   1561  O   GLY A 190      17.224  28.851   7.877  1.00  9.90           O  
ANISOU 1561  O   GLY A 190     1264   1250   1249    -43     63   -176       O  
ATOM   1562  N   CYS A 191      19.417  28.351   7.998  1.00  8.53           N  
ANISOU 1562  N   CYS A 191     1106   1079   1055    -45     61   -141       N  
ATOM   1563  CA  CYS A 191      19.128  26.958   8.354  1.00  8.92           C  
ANISOU 1563  CA  CYS A 191     1164   1135   1089    -55     49   -132       C  
ATOM   1564  C   CYS A 191      18.369  26.869   9.677  1.00  9.73           C  
ANISOU 1564  C   CYS A 191     1254   1258   1184    -89     59   -146       C  
ATOM   1565  O   CYS A 191      17.495  25.999   9.846  1.00  9.61           O  
ANISOU 1565  O   CYS A 191     1241   1241   1168   -102     57   -146       O  
ATOM   1566  CB  CYS A 191      20.425  26.160   8.445  1.00  9.05           C  
ANISOU 1566  CB  CYS A 191     1193   1156   1089    -50     41   -108       C  
ATOM   1567  SG  CYS A 191      21.274  25.888   6.873  1.00 10.00           S  
ANISOU 1567  SG  CYS A 191     1326   1262   1212    -11     30    -93       S  
ATOM   1568  N   ILE A 192      18.764  27.713  10.652  1.00  9.07           N  
ANISOU 1568  N   ILE A 192     1156   1196   1094   -104     70   -159       N  
ATOM   1569  CA  ILE A 192      18.099  27.721  11.945  1.00  9.24           C  
ANISOU 1569  CA  ILE A 192     1163   1248   1100   -133     81   -175       C  
ATOM   1570  C   ILE A 192      16.678  28.236  11.830  1.00 10.30           C  
ANISOU 1570  C   ILE A 192     1282   1379   1253   -138     89   -205       C  
ATOM   1571  O   ILE A 192      15.768  27.687  12.473  1.00 10.29           O  
ANISOU 1571  O   ILE A 192     1272   1397   1241   -160     96   -210       O  
ATOM   1572  CB  ILE A 192      18.964  28.522  12.955  1.00  9.97           C  
ANISOU 1572  CB  ILE A 192     1240   1371   1178   -144     88   -192       C  
ATOM   1573  CG1 ILE A 192      20.273  27.774  13.190  1.00 10.58           C  
ANISOU 1573  CG1 ILE A 192     1328   1462   1229   -137     77   -164       C  
ATOM   1574  CG2 ILE A 192      18.204  28.758  14.291  1.00 11.95           C  
ANISOU 1574  CG2 ILE A 192     1468   1663   1408   -170    101   -218       C  
ATOM   1575  CD1 ILE A 192      21.362  28.579  13.961  1.00 13.12           C  
ANISOU 1575  CD1 ILE A 192     1627   1817   1539   -142     79   -187       C  
ATOM   1576  N   PHE A 193      16.448  29.281  11.029  1.00  9.67           N  
ANISOU 1576  N   PHE A 193     1195   1277   1200   -116     89   -223       N  
ATOM   1577  CA  PHE A 193      15.116  29.805  10.759  1.00  9.68           C  
ANISOU 1577  CA  PHE A 193     1180   1276   1221   -109     92   -252       C  
ATOM   1578  C   PHE A 193      14.208  28.684  10.219  1.00 10.77           C  
ANISOU 1578  C   PHE A 193     1321   1414   1358   -109     82   -247       C  
ATOM   1579  O   PHE A 193      13.109  28.454  10.766  1.00 10.38           O  
ANISOU 1579  O   PHE A 193     1252   1385   1308   -130     90   -270       O  
ATOM   1580  CB  PHE A 193      15.273  30.974   9.798  1.00 11.06           C  
ANISOU 1580  CB  PHE A 193     1359   1420   1424    -75     92   -256       C  
ATOM   1581  CG  PHE A 193      14.034  31.620   9.238  1.00 11.09           C  
ANISOU 1581  CG  PHE A 193     1350   1417   1448    -49     89   -280       C  
ATOM   1582  CD1 PHE A 193      12.849  31.668   9.971  1.00 12.79           C  
ANISOU 1582  CD1 PHE A 193     1538   1657   1664    -65     94   -317       C  
ATOM   1583  CD2 PHE A 193      14.080  32.271   8.021  1.00 11.96           C  
ANISOU 1583  CD2 PHE A 193     1472   1498   1575     -7     84   -265       C  
ATOM   1584  CE1 PHE A 193      11.720  32.345   9.467  1.00 13.64           C  
ANISOU 1584  CE1 PHE A 193     1629   1762   1792    -35     89   -344       C  
ATOM   1585  CE2 PHE A 193      12.966  32.969   7.532  1.00 12.84           C  
ANISOU 1585  CE2 PHE A 193     1572   1605   1704     26     79   -286       C  
ATOM   1586  CZ  PHE A 193      11.790  32.981   8.248  1.00 12.23           C  
ANISOU 1586  CZ  PHE A 193     1465   1553   1629     13     80   -328       C  
ATOM   1587  N   ALA A 194      14.685  27.938   9.217  1.00  9.89           N  
ANISOU 1587  N   ALA A 194     1229   1281   1245    -90     67   -222       N  
ATOM   1588  CA  ALA A 194      13.879  26.867   8.651  1.00  9.46           C  
ANISOU 1588  CA  ALA A 194     1174   1224   1197    -91     57   -227       C  
ATOM   1589  C   ALA A 194      13.560  25.811   9.718  1.00 10.23           C  
ANISOU 1589  C   ALA A 194     1270   1332   1285   -134     68   -220       C  
ATOM   1590  O   ALA A 194      12.435  25.263   9.743  1.00 10.71           O  
ANISOU 1590  O   ALA A 194     1314   1397   1358   -153     73   -240       O  
ATOM   1591  CB  ALA A 194      14.650  26.224   7.517  1.00  9.97           C  
ANISOU 1591  CB  ALA A 194     1261   1268   1260    -63     39   -205       C  
ATOM   1592  N   GLU A 195      14.506  25.504  10.586  1.00  9.58           N  
ANISOU 1592  N   GLU A 195     1202   1255   1181   -150     75   -191       N  
ATOM   1593  CA  GLU A 195      14.326  24.501  11.627  1.00 10.85           C  
ANISOU 1593  CA  GLU A 195     1368   1426   1327   -185     89   -171       C  
ATOM   1594  C   GLU A 195      13.311  24.959  12.655  1.00 11.35           C  
ANISOU 1594  C   GLU A 195     1405   1525   1383   -215    112   -195       C  
ATOM   1595  O   GLU A 195      12.515  24.156  13.144  1.00 11.59           O  
ANISOU 1595  O   GLU A 195     1429   1560   1413   -247    128   -190       O  
ATOM   1596  CB  GLU A 195      15.688  24.211  12.252  1.00 11.56           C  
ANISOU 1596  CB  GLU A 195     1481   1522   1391   -181     87   -133       C  
ATOM   1597  CG  GLU A 195      15.663  23.130  13.331  1.00 12.09           C  
ANISOU 1597  CG  GLU A 195     1560   1598   1435   -209    101    -98       C  
ATOM   1598  CD  GLU A 195      17.042  22.715  13.799  1.00 13.05           C  
ANISOU 1598  CD  GLU A 195     1704   1727   1528   -193     92    -59       C  
ATOM   1599  OE1 GLU A 195      18.047  23.041  13.127  1.00 11.75           O  
ANISOU 1599  OE1 GLU A 195     1545   1552   1367   -163     73    -61       O  
ATOM   1600  OE2 GLU A 195      17.126  22.036  14.851  1.00 15.64           O1-
ANISOU 1600  OE2 GLU A 195     2042   2072   1827   -208    104    -25       O1-
ATOM   1601  N   MET A 196      13.302  26.243  13.027  1.00 10.17           N  
ANISOU 1601  N   MET A 196     1236   1399   1228   -208    116   -223       N  
ATOM   1602  CA  MET A 196      12.292  26.709  13.976  1.00 10.43           C  
ANISOU 1602  CA  MET A 196     1238   1471   1253   -233    137   -254       C  
ATOM   1603  C   MET A 196      10.910  26.564  13.348  1.00 11.87           C  
ANISOU 1603  C   MET A 196     1398   1648   1464   -236    138   -285       C  
ATOM   1604  O   MET A 196       9.962  26.191  14.048  1.00 12.27           O  
ANISOU 1604  O   MET A 196     1427   1726   1509   -269    159   -298       O  
ATOM   1605  CB  MET A 196      12.520  28.194  14.290  1.00 11.21           C  
ANISOU 1605  CB  MET A 196     1320   1588   1354   -217    138   -290       C  
ATOM   1606  CG  MET A 196      13.714  28.454  15.202  1.00 11.28           C  
ANISOU 1606  CG  MET A 196     1335   1619   1332   -221    140   -278       C  
ATOM   1607  SD  MET A 196      13.699  30.167  15.910  1.00 14.25           S  
ANISOU 1607  SD  MET A 196     1678   2022   1715   -217    149   -338       S  
ATOM   1608  CE  MET A 196      14.417  31.087  14.566  1.00 15.18           C  
ANISOU 1608  CE  MET A 196     1811   2080   1879   -180    134   -339       C  
ATOM   1609  N   VAL A 197      10.760  26.873  12.061  1.00 10.59           N  
ANISOU 1609  N   VAL A 197     1237   1459   1328   -202    117   -300       N  
ATOM   1610  CA  VAL A 197       9.477  26.828  11.388  1.00 11.14           C  
ANISOU 1610  CA  VAL A 197     1280   1532   1421   -196    112   -337       C  
ATOM   1611  C   VAL A 197       8.958  25.412  11.218  1.00 12.22           C  
ANISOU 1611  C   VAL A 197     1415   1658   1568   -226    116   -330       C  
ATOM   1612  O   VAL A 197       7.770  25.156  11.465  1.00 13.14           O  
ANISOU 1612  O   VAL A 197     1499   1795   1697   -253    129   -362       O  
ATOM   1613  CB  VAL A 197       9.571  27.527  10.003  1.00 12.81           C  
ANISOU 1613  CB  VAL A 197     1496   1722   1650   -142     85   -348       C  
ATOM   1614  CG1 VAL A 197       8.309  27.297   9.152  1.00 14.92           C  
ANISOU 1614  CG1 VAL A 197     1735   1999   1937   -128     72   -388       C  
ATOM   1615  CG2 VAL A 197       9.827  29.026  10.167  1.00 14.08           C  
ANISOU 1615  CG2 VAL A 197     1653   1884   1813   -115     87   -360       C  
ATOM   1616  N   THR A 198       9.818  24.506  10.803  1.00 11.18           N  
ANISOU 1616  N   THR A 198     1317   1494   1437   -224    106   -294       N  
ATOM   1617  CA  THR A 198       9.355  23.158  10.455  1.00 11.20           C  
ANISOU 1617  CA  THR A 198     1320   1474   1462   -249    107   -293       C  
ATOM   1618  C   THR A 198       9.474  22.167  11.564  1.00 13.49           C  
ANISOU 1618  C   THR A 198     1624   1756   1744   -297    135   -255       C  
ATOM   1619  O   THR A 198       8.861  21.096  11.472  1.00 13.77           O  
ANISOU 1619  O   THR A 198     1655   1770   1806   -329    147   -258       O  
ATOM   1620  CB  THR A 198      10.110  22.639   9.243  1.00 13.04           C  
ANISOU 1620  CB  THR A 198     1579   1672   1706   -215     79   -282       C  
ATOM   1621  CG2 THR A 198       9.939  23.515   8.010  1.00 12.42           C  
ANISOU 1621  CG2 THR A 198     1487   1602   1630   -163     53   -314       C  
ATOM   1622  OG1 THR A 198      11.489  22.480   9.585  1.00 12.77           O  
ANISOU 1622  OG1 THR A 198     1581   1621   1651   -206     78   -233       O  
ATOM   1623  N   ARG A 199      10.258  22.485  12.589  1.00 13.06           N  
ANISOU 1623  N   ARG A 199     1587   1720   1654   -301    147   -219       N  
ATOM   1624  CA  ARG A 199      10.511  21.610  13.751  1.00 14.10           C  
ANISOU 1624  CA  ARG A 199     1738   1854   1764   -337    174   -170       C  
ATOM   1625  C   ARG A 199      11.372  20.421  13.383  1.00 16.30           C  
ANISOU 1625  C   ARG A 199     2057   2082   2054   -330    164   -125       C  
ATOM   1626  O   ARG A 199      11.334  19.375  14.056  1.00 17.48           O  
ANISOU 1626  O   ARG A 199     2225   2213   2204   -360    186    -83       O  
ATOM   1627  CB  ARG A 199       9.230  21.149  14.466  1.00 16.45           C  
ANISOU 1627  CB  ARG A 199     2009   2171   2071   -389    210   -180       C  
ATOM   1628  CG  ARG A 199       8.210  22.258  14.736  1.00 20.88           C  
ANISOU 1628  CG  ARG A 199     2522   2783   2627   -394    219   -236       C  
ATOM   1629  CD  ARG A 199       6.909  21.679  15.313  1.00 19.28           C  
ANISOU 1629  CD  ARG A 199     2288   2600   2438   -448    258   -250       C  
ATOM   1630  NE  ARG A 199       5.728  22.351  14.802  1.00 27.24           N  
ANISOU 1630  NE  ARG A 199     3246   3635   3471   -445    253   -321       N  
ATOM   1631  CZ  ARG A 199       4.504  21.912  15.019  1.00 33.73           C  
ANISOU 1631  CZ  ARG A 199     4028   4473   4313   -489    281   -350       C  
ATOM   1632  NH1 ARG A 199       4.304  20.836  15.764  1.00 27.26           N1+
ANISOU 1632  NH1 ARG A 199     3218   3644   3496   -544    321   -309       N1+
ATOM   1633  NH2 ARG A 199       3.463  22.566  14.527  1.00 35.91           N  
ANISOU 1633  NH2 ARG A 199     4255   4780   4610   -478    272   -419       N  
ATOM   1634  N   ARG A 200      12.172  20.555  12.326  1.00 14.02           N  
ANISOU 1634  N   ARG A 200     1782   1768   1775   -288    132   -131       N  
ATOM   1635  CA AARG A 200      13.084  19.524  11.910  0.60 14.24           C  
ANISOU 1635  CA AARG A 200     1846   1751   1813   -272    118    -96       C  
ATOM   1636  CA BARG A 200      13.113  19.531  11.878  0.40 14.11           C  
ANISOU 1636  CA BARG A 200     1830   1734   1797   -271    117    -96       C  
ATOM   1637  C   ARG A 200      14.316  20.232  11.318  1.00 14.66           C  
ANISOU 1637  C   ARG A 200     1912   1812   1849   -224     90    -93       C  
ATOM   1638  O   ARG A 200      14.165  21.261  10.655  1.00 12.87           O  
ANISOU 1638  O   ARG A 200     1666   1602   1623   -202     78   -128       O  
ATOM   1639  CB AARG A 200      12.383  18.650  10.877  0.60 17.28           C  
ANISOU 1639  CB AARG A 200     2225   2094   2248   -280    110   -125       C  
ATOM   1640  CB BARG A 200      12.534  18.659  10.756  0.40 16.87           C  
ANISOU 1640  CB BARG A 200     2176   2040   2195   -273    106   -124       C  
ATOM   1641  CG AARG A 200      13.140  17.417  10.499  0.60 18.72           C  
ANISOU 1641  CG AARG A 200     2440   2221   2450   -269    100    -96       C  
ATOM   1642  CG BARG A 200      11.497  17.670  11.184  0.40 21.66           C  
ANISOU 1642  CG BARG A 200     2774   2622   2834   -325    134   -125       C  
ATOM   1643  CD AARG A 200      12.277  16.571   9.587  0.60 22.26           C  
ANISOU 1643  CD AARG A 200     2874   2631   2953   -285     96   -138       C  
ATOM   1644  CD BARG A 200      12.007  16.571  12.097  0.40 26.46           C  
ANISOU 1644  CD BARG A 200     3419   3196   3440   -346    156    -59       C  
ATOM   1645  NE AARG A 200      11.941  15.294  10.202  0.60 34.97           N  
ANISOU 1645  NE AARG A 200     4500   4191   4595   -329    124   -109       N  
ATOM   1646  NE BARG A 200      10.883  15.791  12.607  0.40 25.88           N  
ANISOU 1646  NE BARG A 200     3334   3102   3399   -404    194    -57       N  
ATOM   1647  CZ AARG A 200      11.411  14.265   9.548  0.60 46.42           C  
ANISOU 1647  CZ AARG A 200     5944   5589   6102   -348    124   -139       C  
ATOM   1648  CZ BARG A 200      10.308  14.803  11.935  0.40 32.10           C  
ANISOU 1648  CZ BARG A 200     4116   3835   4245   -428    197    -82       C  
ATOM   1649  NH1AARG A 200      11.159  14.353   8.246  0.60 20.78           N1+
ANISOU 1649  NH1AARG A 200     2673   2343   2878   -323     94   -203       N1+
ATOM   1650  NH1BARG A 200      10.765  14.451  10.739  0.40 16.37           N1+
ANISOU 1650  NH1BARG A 200     2131   1807   2282   -393    163   -111       N1+
ATOM   1651  NH2AARG A 200      11.143  13.137  10.186  0.60 44.06           N  
ANISOU 1651  NH2AARG A 200     5664   5237   5839   -391    156   -104       N  
ATOM   1652  NH2BARG A 200       9.269  14.163  12.449  0.40 22.98           N  
ANISOU 1652  NH2BARG A 200     2945   2663   3123   -487    237    -81       N  
ATOM   1653  N   ALA A 201      15.513  19.682  11.519  1.00 13.13           N  
ANISOU 1653  N   ALA A 201     1747   1603   1639   -205     81    -53       N  
ATOM   1654  CA  ALA A 201      16.686  20.308  10.915  1.00 12.44           C  
ANISOU 1654  CA  ALA A 201     1664   1523   1537   -164     59    -54       C  
ATOM   1655  C   ALA A 201      16.558  20.291   9.386  1.00 12.36           C  
ANISOU 1655  C   ALA A 201     1650   1490   1554   -137     38    -86       C  
ATOM   1656  O   ALA A 201      15.986  19.347   8.826  1.00 14.09           O  
ANISOU 1656  O   ALA A 201     1872   1677   1804   -143     34    -98       O  
ATOM   1657  CB  ALA A 201      17.932  19.569  11.343  1.00 14.59           C  
ANISOU 1657  CB  ALA A 201     1965   1787   1791   -146     51    -10       C  
ATOM   1658  N   LEU A 202      17.028  21.332   8.741  1.00 10.96           N  
ANISOU 1658  N   LEU A 202     1465   1332   1369   -108     28   -101       N  
ATOM   1659  CA  LEU A 202      16.921  21.461   7.300  1.00 11.42           C  
ANISOU 1659  CA  LEU A 202     1518   1381   1441    -76     10   -127       C  
ATOM   1660  C   LEU A 202      17.864  20.489   6.593  1.00 11.97           C  
ANISOU 1660  C   LEU A 202     1607   1427   1514    -49     -7   -114       C  
ATOM   1661  O   LEU A 202      17.436  19.757   5.676  1.00 11.94           O  
ANISOU 1661  O   LEU A 202     1602   1403   1531    -38    -20   -138       O  
ATOM   1662  CB  LEU A 202      17.215  22.930   6.928  1.00 11.13           C  
ANISOU 1662  CB  LEU A 202     1470   1368   1391    -54     11   -135       C  
ATOM   1663  CG  LEU A 202      17.086  23.260   5.432  1.00 12.43           C  
ANISOU 1663  CG  LEU A 202     1630   1533   1561    -14     -4   -153       C  
ATOM   1664  CD1 LEU A 202      15.652  22.981   4.916  1.00 14.26           C  
ANISOU 1664  CD1 LEU A 202     1843   1766   1810    -16    -11   -191       C  
ATOM   1665  CD2 LEU A 202      17.417  24.697   5.191  1.00 12.34           C  
ANISOU 1665  CD2 LEU A 202     1612   1535   1540      5      4   -149       C  
ATOM   1666  N   PHE A 203      19.132  20.465   6.995  1.00 10.28           N  
ANISOU 1666  N   PHE A 203     1408   1218   1281    -37     -9    -84       N  
ATOM   1667  CA  PHE A 203      20.175  19.676   6.336  1.00  9.99           C  
ANISOU 1667  CA  PHE A 203     1385   1165   1244     -5    -26    -75       C  
ATOM   1668  C   PHE A 203      20.969  18.899   7.384  1.00 10.70           C  
ANISOU 1668  C   PHE A 203     1495   1247   1325    -10    -25    -38       C  
ATOM   1669  O   PHE A 203      22.071  19.284   7.746  1.00  9.97           O  
ANISOU 1669  O   PHE A 203     1402   1178   1207      5    -28    -21       O  
ATOM   1670  CB  PHE A 203      21.136  20.578   5.539  1.00 10.02           C  
ANISOU 1670  CB  PHE A 203     1382   1195   1230     28    -31    -78       C  
ATOM   1671  CG  PHE A 203      20.479  21.451   4.515  1.00 10.44           C  
ANISOU 1671  CG  PHE A 203     1420   1260   1284     42    -31   -103       C  
ATOM   1672  CD1 PHE A 203      19.664  20.905   3.534  1.00 11.86           C  
ANISOU 1672  CD1 PHE A 203     1596   1431   1479     56    -44   -131       C  
ATOM   1673  CD2 PHE A 203      20.720  22.812   4.495  1.00 11.37           C  
ANISOU 1673  CD2 PHE A 203     1528   1399   1391     45    -18    -98       C  
ATOM   1674  CE1 PHE A 203      19.103  21.720   2.545  1.00 13.04           C  
ANISOU 1674  CE1 PHE A 203     1733   1602   1622     79    -46   -151       C  
ATOM   1675  CE2 PHE A 203      20.175  23.618   3.490  1.00 13.13           C  
ANISOU 1675  CE2 PHE A 203     1743   1632   1614     67    -17   -111       C  
ATOM   1676  CZ  PHE A 203      19.352  23.067   2.548  1.00 12.14           C  
ANISOU 1676  CZ  PHE A 203     1614   1505   1493     86    -32   -136       C  
ATOM   1677  N   PRO A 204      20.415  17.788   7.925  1.00 10.95           N  
ANISOU 1677  N   PRO A 204     1542   1243   1374    -30    -20    -23       N  
ATOM   1678  CA  PRO A 204      21.101  17.074   9.005  1.00 11.54           C  
ANISOU 1678  CA  PRO A 204     1639   1311   1435    -30    -18     22       C  
ATOM   1679  C   PRO A 204      22.163  16.089   8.504  1.00 12.87           C  
ANISOU 1679  C   PRO A 204     1827   1451   1612     10    -38     34       C  
ATOM   1680  O   PRO A 204      22.053  14.846   8.737  1.00 13.00           O  
ANISOU 1680  O   PRO A 204     1867   1418   1653     10    -38     56       O  
ATOM   1681  CB  PRO A 204      19.946  16.407   9.748  1.00 12.64           C  
ANISOU 1681  CB  PRO A 204     1787   1422   1593    -72      4     37       C  
ATOM   1682  CG  PRO A 204      18.957  16.101   8.658  1.00 15.08           C  
ANISOU 1682  CG  PRO A 204     2085   1700   1946    -82      1     -7       C  
ATOM   1683  CD  PRO A 204      19.048  17.280   7.708  1.00 12.38           C  
ANISOU 1683  CD  PRO A 204     1718   1395   1590    -60    -12    -45       C  
ATOM   1684  N   GLY A 205      23.208  16.626   7.904  1.00 10.73           N  
ANISOU 1684  N   GLY A 205     1545   1210   1323     44    -53     22       N  
ATOM   1685  CA  GLY A 205      24.285  15.769   7.380  1.00 10.65           C  
ANISOU 1685  CA  GLY A 205     1546   1181   1318     88    -73     26       C  
ATOM   1686  C   GLY A 205      25.097  15.100   8.458  1.00 11.28           C  
ANISOU 1686  C   GLY A 205     1646   1260   1381    104    -78     71       C  
ATOM   1687  O   GLY A 205      25.276  15.639   9.556  1.00 12.16           O  
ANISOU 1687  O   GLY A 205     1752   1408   1458     91    -70     95       O  
ATOM   1688  N   ASP A 206      25.656  13.924   8.125  1.00 11.07           N  
ANISOU 1688  N   ASP A 206     1638   1192   1375    139    -95     79       N  
ATOM   1689  CA  ASP A 206      26.467  13.187   9.077  1.00 11.70           C  
ANISOU 1689  CA  ASP A 206     1740   1266   1439    166   -103    126       C  
ATOM   1690  C   ASP A 206      27.874  12.947   8.591  1.00 14.28           C  
ANISOU 1690  C   ASP A 206     2060   1613   1755    222   -129    116       C  
ATOM   1691  O   ASP A 206      28.588  12.099   9.151  1.00 14.14           O  
ANISOU 1691  O   ASP A 206     2062   1579   1731    259   -142    150       O  
ATOM   1692  CB  ASP A 206      25.778  11.889   9.511  1.00 13.36           C  
ANISOU 1692  CB  ASP A 206     1988   1402   1687    155    -94    161       C  
ATOM   1693  CG  ASP A 206      25.579  10.894   8.401  1.00 13.72           C  
ANISOU 1693  CG  ASP A 206     2044   1379   1789    170   -105    129       C  
ATOM   1694  OD1 ASP A 206      25.817  11.260   7.218  1.00 14.74           O  
ANISOU 1694  OD1 ASP A 206     2149   1527   1923    187   -119     76       O  
ATOM   1695  OD2 ASP A 206      25.234   9.724   8.712  1.00 16.08           O1-
ANISOU 1695  OD2 ASP A 206     2375   1606   2128    166    -99    157       O1-
ATOM   1696  N   SER A 207      28.275  13.663   7.546  1.00 12.02           N  
ANISOU 1696  N   SER A 207     1744   1359   1463    233   -134     72       N  
ATOM   1697  CA  SER A 207      29.619  13.683   6.982  1.00 12.34           C  
ANISOU 1697  CA  SER A 207     1766   1433   1489    280   -153     54       C  
ATOM   1698  C   SER A 207      29.659  14.873   6.072  1.00 13.25           C  
ANISOU 1698  C   SER A 207     1849   1592   1593    267   -142     17       C  
ATOM   1699  O   SER A 207      28.610  15.452   5.741  1.00 11.57           O  
ANISOU 1699  O   SER A 207     1634   1371   1390    232   -126      4       O  
ATOM   1700  CB  SER A 207      29.958  12.413   6.215  1.00 13.31           C  
ANISOU 1700  CB  SER A 207     1905   1508   1646    324   -172     40       C  
ATOM   1701  OG  SER A 207      29.167  12.368   5.037  1.00 14.85           O  
ANISOU 1701  OG  SER A 207     2096   1678   1870    312   -168     -2       O  
ATOM   1702  N   GLU A 208      30.836  15.297   5.647  1.00 12.88           N  
ANISOU 1702  N   GLU A 208     1776   1593   1526    295   -148      0       N  
ATOM   1703  CA  GLU A 208      30.883  16.457   4.772  1.00 12.49           C  
ANISOU 1703  CA  GLU A 208     1698   1580   1467    281   -131    -27       C  
ATOM   1704  C   GLU A 208      30.158  16.218   3.469  1.00 12.40           C  
ANISOU 1704  C   GLU A 208     1693   1544   1476    287   -131    -53       C  
ATOM   1705  O   GLU A 208      29.453  17.112   2.993  1.00 11.90           O  
ANISOU 1705  O   GLU A 208     1621   1490   1409    262   -114    -62       O  
ATOM   1706  CB  GLU A 208      32.314  16.936   4.521  1.00 14.65           C  
ANISOU 1706  CB  GLU A 208     1938   1909   1717    306   -132    -40       C  
ATOM   1707  CG  GLU A 208      32.960  17.490   5.792  1.00 16.35           C  
ANISOU 1707  CG  GLU A 208     2137   2165   1910    293   -131    -25       C  
ATOM   1708  CD  GLU A 208      34.248  18.251   5.548  1.00 19.95           C  
ANISOU 1708  CD  GLU A 208     2550   2681   2349    302   -124    -47       C  
ATOM   1709  OE1 GLU A 208      34.304  19.030   4.577  1.00 21.97           O  
ANISOU 1709  OE1 GLU A 208     2789   2951   2609    289   -102    -64       O  
ATOM   1710  OE2 GLU A 208      35.152  18.164   6.407  1.00 32.64           O1-
ANISOU 1710  OE2 GLU A 208     4138   4325   3937    317   -137    -46       O1-
ATOM   1711  N   ILE A 209      30.331  15.029   2.850  1.00 12.14           N  
ANISOU 1711  N   ILE A 209     1671   1481   1461    323   -150    -70       N  
ATOM   1712  CA  ILE A 209      29.650  14.803   1.581  1.00 11.31           C  
ANISOU 1712  CA  ILE A 209     1565   1363   1371    332   -152   -106       C  
ATOM   1713  C   ILE A 209      28.149  14.633   1.759  1.00 11.77           C  
ANISOU 1713  C   ILE A 209     1640   1376   1455    295   -148   -108       C  
ATOM   1714  O   ILE A 209      27.384  15.059   0.887  1.00 11.07           O  
ANISOU 1714  O   ILE A 209     1542   1299   1367    288   -143   -134       O  
ATOM   1715  CB  ILE A 209      30.303  13.635   0.812  1.00 13.30           C  
ANISOU 1715  CB  ILE A 209     1817   1600   1637    383   -175   -137       C  
ATOM   1716  CG1 ILE A 209      29.976  13.739  -0.697  1.00 14.54           C  
ANISOU 1716  CG1 ILE A 209     1957   1779   1788    401   -175   -183       C  
ATOM   1717  CG2 ILE A 209      29.877  12.267   1.386  1.00 16.30           C  
ANISOU 1717  CG2 ILE A 209     2228   1905   2060    387   -190   -130       C  
ATOM   1718  CD1 ILE A 209      30.568  14.941  -1.383  1.00 17.47           C  
ANISOU 1718  CD1 ILE A 209     2301   2220   2116    407   -156   -182       C  
ATOM   1719  N   ASP A 210      27.709  14.042   2.891  1.00 11.50           N  
ANISOU 1719  N   ASP A 210     1630   1299   1442    272   -147    -79       N  
ATOM   1720  CA  ASP A 210      26.280  13.926   3.118  1.00 10.98           C  
ANISOU 1720  CA  ASP A 210     1575   1195   1402    231   -138    -82       C  
ATOM   1721  C   ASP A 210      25.695  15.310   3.333  1.00 10.32           C  
ANISOU 1721  C   ASP A 210     1476   1152   1295    197   -118    -76       C  
ATOM   1722  O   ASP A 210      24.604  15.583   2.850  1.00 11.14           O  
ANISOU 1722  O   ASP A 210     1573   1251   1410    177   -113    -99       O  
ATOM   1723  CB  ASP A 210      26.005  13.027   4.324  1.00 12.06           C  
ANISOU 1723  CB  ASP A 210     1740   1280   1561    213   -135    -44       C  
ATOM   1724  CG  ASP A 210      24.554  12.747   4.557  1.00 12.68           C  
ANISOU 1724  CG  ASP A 210     1827   1317   1673    167   -121    -49       C  
ATOM   1725  OD1 ASP A 210      23.949  12.023   3.724  1.00 17.35           O  
ANISOU 1725  OD1 ASP A 210     2418   1870   2304    168   -128    -89       O  
ATOM   1726  OD2 ASP A 210      24.030  13.186   5.573  1.00 12.64           O1-
ANISOU 1726  OD2 ASP A 210     1827   1319   1657    130   -103    -17       O1-
ATOM   1727  N   GLN A 211      26.416  16.187   4.037  1.00 10.03           N  
ANISOU 1727  N   GLN A 211     1430   1154   1227    191   -109    -50       N  
ATOM   1728  CA  GLN A 211      25.950  17.546   4.228  1.00 10.30           C  
ANISOU 1728  CA  GLN A 211     1448   1219   1244    162    -90    -49       C  
ATOM   1729  C   GLN A 211      25.794  18.242   2.883  1.00 10.60           C  
ANISOU 1729  C   GLN A 211     1471   1280   1277    177    -87    -76       C  
ATOM   1730  O   GLN A 211      24.746  18.839   2.589  1.00 10.96           O  
ANISOU 1730  O   GLN A 211     1511   1326   1327    160    -78    -87       O  
ATOM   1731  CB  GLN A 211      26.960  18.289   5.108  1.00 11.00           C  
ANISOU 1731  CB  GLN A 211     1526   1347   1307    158    -83    -28       C  
ATOM   1732  CG  GLN A 211      26.446  19.673   5.533  1.00 10.77           C  
ANISOU 1732  CG  GLN A 211     1483   1342   1269    123    -62    -28       C  
ATOM   1733  CD  GLN A 211      25.236  19.573   6.411  1.00  9.84           C  
ANISOU 1733  CD  GLN A 211     1374   1203   1160     88    -54    -20       C  
ATOM   1734  NE2 GLN A 211      24.287  20.513   6.264  1.00 10.75           N  
ANISOU 1734  NE2 GLN A 211     1480   1323   1281     65    -40    -35       N  
ATOM   1735  OE1 GLN A 211      25.127  18.679   7.259  1.00 10.97           O  
ANISOU 1735  OE1 GLN A 211     1535   1329   1304     82    -59      1       O  
ATOM   1736  N   LEU A 212      26.839  18.171   2.038  1.00 10.45           N  
ANISOU 1736  N   LEU A 212     1442   1285   1244    214    -93    -85       N  
ATOM   1737  CA ALEU A 212      26.790  18.788   0.703  0.60 10.73           C  
ANISOU 1737  CA ALEU A 212     1463   1349   1264    235    -87   -104       C  
ATOM   1738  CA BLEU A 212      26.793  18.826   0.747  0.40 10.04           C  
ANISOU 1738  CA BLEU A 212     1376   1262   1177    234    -87   -103       C  
ATOM   1739  C   LEU A 212      25.678  18.255  -0.129  1.00 12.16           C  
ANISOU 1739  C   LEU A 212     1648   1514   1458    244   -100   -135       C  
ATOM   1740  O   LEU A 212      24.922  19.023  -0.759  1.00 11.70           O  
ANISOU 1740  O   LEU A 212     1582   1473   1390    244    -92   -143       O  
ATOM   1741  CB ALEU A 212      28.088  18.539  -0.077  0.60 12.00           C  
ANISOU 1741  CB ALEU A 212     1611   1540   1406    275    -92   -112       C  
ATOM   1742  CB BLEU A 212      28.167  18.665   0.093  0.40 10.56           C  
ANISOU 1742  CB BLEU A 212     1429   1360   1224    271    -89   -107       C  
ATOM   1743  CG ALEU A 212      29.174  19.546   0.185  0.60 14.31           C  
ANISOU 1743  CG ALEU A 212     1887   1871   1680    269    -71    -92       C  
ATOM   1744  CG BLEU A 212      28.502  19.551  -1.069  0.40 11.29           C  
ANISOU 1744  CG BLEU A 212     1505   1495   1290    289    -72   -110       C  
ATOM   1745  CD1ALEU A 212      30.481  19.080  -0.416  0.60 15.54           C  
ANISOU 1745  CD1ALEU A 212     2027   2057   1821    307    -76   -103       C  
ATOM   1746  CD1BLEU A 212      28.610  21.016  -0.651  0.40 11.28           C  
ANISOU 1746  CD1BLEU A 212     1495   1509   1283    259    -43    -83       C  
ATOM   1747  CD2ALEU A 212      28.797  20.945  -0.376  0.60 16.36           C  
ANISOU 1747  CD2ALEU A 212     2137   2150   1928    255    -44    -81       C  
ATOM   1748  CD2BLEU A 212      29.817  19.079  -1.677  0.40 12.14           C  
ANISOU 1748  CD2BLEU A 212     1598   1634   1382    327    -77   -121       C  
ATOM   1749  N   PHE A 213      25.539  16.943  -0.185  1.00 11.16           N  
ANISOU 1749  N   PHE A 213     1531   1353   1356    255   -119   -156       N  
ATOM   1750  CA  PHE A 213      24.518  16.382  -1.046  1.00 11.41           C  
ANISOU 1750  CA  PHE A 213     1559   1372   1404    263   -133   -198       C  
ATOM   1751  C   PHE A 213      23.111  16.644  -0.539  1.00 11.72           C  
ANISOU 1751  C   PHE A 213     1598   1391   1463    222   -126   -201       C  
ATOM   1752  O   PHE A 213      22.193  16.789  -1.344  1.00 12.19           O  
ANISOU 1752  O   PHE A 213     1645   1465   1522    229   -133   -236       O  
ATOM   1753  CB  PHE A 213      24.803  14.904  -1.321  1.00 13.40           C  
ANISOU 1753  CB  PHE A 213     1819   1587   1686    285   -154   -228       C  
ATOM   1754  CG  PHE A 213      26.005  14.604  -2.220  1.00 13.95           C  
ANISOU 1754  CG  PHE A 213     1878   1688   1734    337   -165   -246       C  
ATOM   1755  CD1 PHE A 213      26.744  15.633  -2.804  1.00 13.79           C  
ANISOU 1755  CD1 PHE A 213     1842   1729   1668    357   -152   -233       C  
ATOM   1756  CD2 PHE A 213      26.346  13.292  -2.522  1.00 16.83           C  
ANISOU 1756  CD2 PHE A 213     2248   2019   2127    364   -186   -279       C  
ATOM   1757  CE1 PHE A 213      27.807  15.342  -3.681  1.00 16.94           C  
ANISOU 1757  CE1 PHE A 213     2228   2165   2045    403   -158   -252       C  
ATOM   1758  CE2 PHE A 213      27.406  13.005  -3.399  1.00 18.22           C  
ANISOU 1758  CE2 PHE A 213     2410   2230   2282    414   -196   -304       C  
ATOM   1759  CZ  PHE A 213      28.132  14.025  -3.946  1.00 17.33           C  
ANISOU 1759  CZ  PHE A 213     2279   2186   2119    432   -181   -290       C  
ATOM   1760  N   ARG A 214      22.919  16.794   0.775  1.00 10.85           N  
ANISOU 1760  N   ARG A 214     1500   1258   1364    183   -113   -168       N  
ATOM   1761  CA  ARG A 214      21.600  17.190   1.290  1.00 10.82           C  
ANISOU 1761  CA  ARG A 214     1492   1246   1374    144   -102   -171       C  
ATOM   1762  C   ARG A 214      21.289  18.601   0.828  1.00 11.58           C  
ANISOU 1762  C   ARG A 214     1572   1384   1442    150    -92   -171       C  
ATOM   1763  O   ARG A 214      20.158  18.884   0.417  1.00 11.43           O  
ANISOU 1763  O   ARG A 214     1540   1374   1429    146    -95   -198       O  
ATOM   1764  CB  ARG A 214      21.559  17.114   2.815  1.00 11.02           C  
ANISOU 1764  CB  ARG A 214     1531   1249   1408    104    -87   -133       C  
ATOM   1765  CG  ARG A 214      21.397  15.681   3.285  1.00 11.25           C  
ANISOU 1765  CG  ARG A 214     1579   1223   1472     92    -91   -130       C  
ATOM   1766  CD  ARG A 214      21.506  15.622   4.803  1.00 11.99           C  
ANISOU 1766  CD  ARG A 214     1689   1306   1562     61    -75    -82       C  
ATOM   1767  NE  ARG A 214      21.224  14.286   5.320  1.00 13.44           N  
ANISOU 1767  NE  ARG A 214     1895   1431   1782     45    -72    -68       N  
ATOM   1768  CZ  ARG A 214      20.008  13.823   5.596  1.00 17.30           C  
ANISOU 1768  CZ  ARG A 214     2383   1887   2305      4    -58    -78       C  
ATOM   1769  NH1 ARG A 214      18.929  14.561   5.331  1.00 17.70           N1+
ANISOU 1769  NH1 ARG A 214     2408   1962   2356    -20    -50   -110       N1+
ATOM   1770  NH2 ARG A 214      19.853  12.600   6.094  1.00 21.77           N  
ANISOU 1770  NH2 ARG A 214     2972   2391   2908    -12    -51    -57       N  
ATOM   1771  N   ILE A 215      22.294  19.489   0.847  1.00  9.59           N  
ANISOU 1771  N   ILE A 215     1320   1160   1163    163    -81   -143       N  
ATOM   1772  CA  ILE A 215      22.084  20.855   0.361  1.00  9.55           C  
ANISOU 1772  CA  ILE A 215     1304   1186   1138    172    -68   -137       C  
ATOM   1773  C   ILE A 215      21.711  20.792  -1.119  1.00 11.08           C  
ANISOU 1773  C   ILE A 215     1489   1405   1317    213    -81   -164       C  
ATOM   1774  O   ILE A 215      20.743  21.438  -1.539  1.00 10.90           O  
ANISOU 1774  O   ILE A 215     1457   1396   1288    219    -81   -175       O  
ATOM   1775  CB  ILE A 215      23.312  21.731   0.610  1.00  9.79           C  
ANISOU 1775  CB  ILE A 215     1334   1235   1151    174    -50   -105       C  
ATOM   1776  CG1 ILE A 215      23.560  21.908   2.129  1.00 10.69           C  
ANISOU 1776  CG1 ILE A 215     1451   1336   1274    135    -40    -86       C  
ATOM   1777  CG2 ILE A 215      23.140  23.098  -0.067  1.00 10.56           C  
ANISOU 1777  CG2 ILE A 215     1425   1354   1234    186    -32    -94       C  
ATOM   1778  CD1 ILE A 215      24.940  22.461   2.457  1.00 11.07           C  
ANISOU 1778  CD1 ILE A 215     1493   1404   1310    136    -27    -67       C  
ATOM   1779  N   PHE A 216      22.446  20.019  -1.907  1.00 10.37           N  
ANISOU 1779  N   PHE A 216     1399   1325   1217    245    -94   -179       N  
ATOM   1780  CA  PHE A 216      22.204  19.945  -3.349  1.00 10.46           C  
ANISOU 1780  CA  PHE A 216     1399   1372   1204    290   -107   -208       C  
ATOM   1781  C   PHE A 216      20.846  19.370  -3.689  1.00 12.63           C  
ANISOU 1781  C   PHE A 216     1661   1640   1495    289   -128   -257       C  
ATOM   1782  O   PHE A 216      20.203  19.826  -4.639  1.00 12.43           O  
ANISOU 1782  O   PHE A 216     1623   1654   1446    320   -136   -276       O  
ATOM   1783  CB  PHE A 216      23.290  19.114  -4.005  1.00 11.57           C  
ANISOU 1783  CB  PHE A 216     1538   1525   1332    323   -118   -222       C  
ATOM   1784  CG  PHE A 216      24.725  19.594  -3.984  1.00 11.19           C  
ANISOU 1784  CG  PHE A 216     1491   1498   1262    334    -99   -186       C  
ATOM   1785  CD1 PHE A 216      25.066  20.821  -3.417  1.00 12.73           C  
ANISOU 1785  CD1 PHE A 216     1689   1698   1451    311    -72   -143       C  
ATOM   1786  CD2 PHE A 216      25.730  18.819  -4.548  1.00 12.73           C  
ANISOU 1786  CD2 PHE A 216     1681   1709   1446    366   -109   -203       C  
ATOM   1787  CE1 PHE A 216      26.398  21.265  -3.449  1.00 14.12           C  
ANISOU 1787  CE1 PHE A 216     1859   1895   1610    316    -52   -117       C  
ATOM   1788  CE2 PHE A 216      27.053  19.243  -4.549  1.00 15.44           C  
ANISOU 1788  CE2 PHE A 216     2019   2079   1771    374    -90   -176       C  
ATOM   1789  CZ  PHE A 216      27.378  20.468  -4.027  1.00 14.63           C  
ANISOU 1789  CZ  PHE A 216     1915   1981   1661    348    -61   -134       C  
ATOM   1790  N   ARG A 217      20.375  18.376  -2.917  1.00 12.27           N  
ANISOU 1790  N   ARG A 217     1620   1550   1493    255   -136   -276       N  
ATOM   1791  CA  ARG A 217      19.090  17.755  -3.221  1.00 12.57           C  
ANISOU 1791  CA  ARG A 217     1641   1579   1556    246   -152   -330       C  
ATOM   1792  C   ARG A 217      17.933  18.676  -2.964  1.00 15.21           C  
ANISOU 1792  C   ARG A 217     1963   1929   1889    229   -145   -330       C  
ATOM   1793  O   ARG A 217      16.861  18.504  -3.577  1.00 16.67           O  
ANISOU 1793  O   ARG A 217     2124   2133   2078    239   -162   -380       O  
ATOM   1794  CB  ARG A 217      18.929  16.464  -2.417  1.00 16.33           C  
ANISOU 1794  CB  ARG A 217     2126   1993   2085    208   -155   -344       C  
ATOM   1795  CG  ARG A 217      19.767  15.349  -2.993  1.00 20.23           C  
ANISOU 1795  CG  ARG A 217     2625   2470   2590    236   -171   -369       C  
ATOM   1796  CD  ARG A 217      19.382  13.991  -2.440  1.00 29.69           C  
ANISOU 1796  CD  ARG A 217     3831   3599   3849    204   -175   -392       C  
ATOM   1797  NE  ARG A 217      19.910  13.824  -1.086  1.00 36.68           N  
ANISOU 1797  NE  ARG A 217     4745   4441   4750    172   -156   -332       N  
ATOM   1798  CZ  ARG A 217      21.061  13.233  -0.791  1.00 49.29           C  
ANISOU 1798  CZ  ARG A 217     6364   6013   6351    190   -159   -306       C  
ATOM   1799  NH1 ARG A 217      21.814  12.709  -1.753  1.00 37.35           N1+
ANISOU 1799  NH1 ARG A 217     4847   4512   4833    236   -178   -338       N1+
ATOM   1800  NH2 ARG A 217      21.465  13.149   0.468  1.00 40.30           N  
ANISOU 1800  NH2 ARG A 217     5249   4845   5218    165   -144   -250       N  
ATOM   1801  N   THR A 218      18.102  19.680  -2.120  1.00 12.16           N  
ANISOU 1801  N   THR A 218     1587   1539   1494    208   -123   -282       N  
ATOM   1802  CA  THR A 218      17.039  20.645  -1.860  1.00 12.79           C  
ANISOU 1802  CA  THR A 218     1654   1634   1573    197   -115   -283       C  
ATOM   1803  C   THR A 218      17.202  21.867  -2.759  1.00 13.79           C  
ANISOU 1803  C   THR A 218     1778   1802   1658    244   -113   -264       C  
ATOM   1804  O   THR A 218      16.203  22.337  -3.355  1.00 14.38           O  
ANISOU 1804  O   THR A 218     1836   1907   1722    269   -123   -287       O  
ATOM   1805  CB  THR A 218      17.042  21.081  -0.387  1.00 14.40           C  
ANISOU 1805  CB  THR A 218     1868   1810   1794    149    -92   -249       C  
ATOM   1806  CG2 THR A 218      16.000  22.154  -0.094  1.00 14.48           C  
ANISOU 1806  CG2 THR A 218     1863   1836   1804    141    -83   -253       C  
ATOM   1807  OG1 THR A 218      16.749  19.923   0.407  1.00 17.16           O  
ANISOU 1807  OG1 THR A 218     2221   2123   2179    107    -92   -261       O  
ATOM   1808  N   LEU A 219      18.406  22.434  -2.863  1.00 11.21           N  
ANISOU 1808  N   LEU A 219     1468   1480   1310    258    -97   -219       N  
ATOM   1809  CA  LEU A 219      18.601  23.706  -3.558  1.00 11.85           C  
ANISOU 1809  CA  LEU A 219     1552   1590   1359    295    -84   -187       C  
ATOM   1810  C   LEU A 219      19.062  23.558  -4.993  1.00 13.24           C  
ANISOU 1810  C   LEU A 219     1727   1811   1494    351    -93   -191       C  
ATOM   1811  O   LEU A 219      19.188  24.571  -5.686  1.00 13.39           O  
ANISOU 1811  O   LEU A 219     1750   1855   1482    386    -80   -158       O  
ATOM   1812  CB  LEU A 219      19.570  24.573  -2.730  1.00 12.27           C  
ANISOU 1812  CB  LEU A 219     1621   1621   1420    268    -53   -138       C  
ATOM   1813  CG  LEU A 219      19.116  24.852  -1.286  1.00 14.21           C  
ANISOU 1813  CG  LEU A 219     1866   1834   1698    217    -42   -137       C  
ATOM   1814  CD1 LEU A 219      20.167  25.640  -0.566  1.00 13.84           C  
ANISOU 1814  CD1 LEU A 219     1828   1773   1656    195    -16   -101       C  
ATOM   1815  CD2 LEU A 219      17.779  25.641  -1.240  1.00 17.45           C  
ANISOU 1815  CD2 LEU A 219     2265   2249   2115    221    -43   -151       C  
ATOM   1816  N   GLY A 220      19.323  22.320  -5.401  1.00 11.85           N  
ANISOU 1816  N   GLY A 220     1545   1641   1319    359   -114   -228       N  
ATOM   1817  CA  GLY A 220      19.843  21.994  -6.710  1.00 13.22           C  
ANISOU 1817  CA  GLY A 220     1711   1861   1450    412   -125   -242       C  
ATOM   1818  C   GLY A 220      21.355  21.931  -6.662  1.00 13.35           C  
ANISOU 1818  C   GLY A 220     1741   1875   1458    411   -106   -208       C  
ATOM   1819  O   GLY A 220      21.972  22.685  -5.908  1.00 13.27           O  
ANISOU 1819  O   GLY A 220     1743   1842   1458    383    -79   -162       O  
ATOM   1820  N   THR A 221      21.981  21.076  -7.475  1.00 12.37           N  
ANISOU 1820  N   THR A 221     1609   1778   1314    443   -120   -237       N  
ATOM   1821  CA  THR A 221      23.438  21.070  -7.507  1.00 12.88           C  
ANISOU 1821  CA  THR A 221     1678   1849   1365    447   -101   -208       C  
ATOM   1822  C   THR A 221      23.883  22.396  -8.104  1.00 15.09           C  
ANISOU 1822  C   THR A 221     1962   2166   1604    469    -69   -153       C  
ATOM   1823  O   THR A 221      23.401  22.786  -9.164  1.00 15.17           O  
ANISOU 1823  O   THR A 221     1968   2223   1572    513    -72   -153       O  
ATOM   1824  CB  THR A 221      23.940  19.895  -8.332  1.00 15.15           C  
ANISOU 1824  CB  THR A 221     1953   2163   1638    484   -123   -256       C  
ATOM   1825  CG2 THR A 221      25.494  19.819  -8.359  1.00 15.37           C  
ANISOU 1825  CG2 THR A 221     1981   2204   1653    491   -105   -233       C  
ATOM   1826  OG1 THR A 221      23.405  18.700  -7.748  1.00 15.14           O  
ANISOU 1826  OG1 THR A 221     1952   2115   1686    460   -150   -305       O  
ATOM   1827  N   PRO A 222      24.798  23.129  -7.443  1.00 13.08           N  
ANISOU 1827  N   PRO A 222     1717   1892   1362    439    -36   -106       N  
ATOM   1828  CA  PRO A 222      25.188  24.436  -7.968  1.00 13.05           C  
ANISOU 1828  CA  PRO A 222     1718   1911   1330    452      1    -51       C  
ATOM   1829  C   PRO A 222      26.039  24.287  -9.211  1.00 14.47           C  
ANISOU 1829  C   PRO A 222     1888   2151   1458    497     12    -45       C  
ATOM   1830  O   PRO A 222      26.754  23.287  -9.392  1.00 16.09           O  
ANISOU 1830  O   PRO A 222     2081   2374   1658    508     -2    -79       O  
ATOM   1831  CB  PRO A 222      26.028  25.036  -6.829  1.00 14.04           C  
ANISOU 1831  CB  PRO A 222     1847   1996   1492    400     30    -19       C  
ATOM   1832  CG  PRO A 222      26.569  23.884  -6.114  1.00 16.14           C  
ANISOU 1832  CG  PRO A 222     2106   2245   1780    381      8    -53       C  
ATOM   1833  CD  PRO A 222      25.459  22.840  -6.160  1.00 13.77           C  
ANISOU 1833  CD  PRO A 222     1807   1936   1490    392    -32   -101       C  
ATOM   1834  N   ASP A 223      25.936  25.273 -10.069  1.00 14.06           N  
ANISOU 1834  N   ASP A 223     1842   2131   1367    527     38     -1       N  
ATOM   1835  CA  ASP A 223      26.679  25.337 -11.308  1.00 15.27           C  
ANISOU 1835  CA  ASP A 223     1988   2351   1462    573     57     17       C  
ATOM   1836  C   ASP A 223      27.152  26.749 -11.532  1.00 15.93           C  
ANISOU 1836  C   ASP A 223     2084   2432   1535    566    112     95       C  
ATOM   1837  O   ASP A 223      26.894  27.629 -10.719  1.00 14.05           O  
ANISOU 1837  O   ASP A 223     1860   2137   1340    528    130    127       O  
ATOM   1838  CB  ASP A 223      25.844  24.777 -12.470  1.00 18.21           C  
ANISOU 1838  CB  ASP A 223     2353   2786   1781    636     23    -20       C  
ATOM   1839  CG  ASP A 223      24.591  25.565 -12.832  1.00 24.74           C  
ANISOU 1839  CG  ASP A 223     3191   3620   2589    665     17      2       C  
ATOM   1840  OD1 ASP A 223      24.414  26.678 -12.319  1.00 21.16           O  
ANISOU 1840  OD1 ASP A 223     2756   3123   2160    641     45     56       O  
ATOM   1841  OD2 ASP A 223      23.782  25.053 -13.628  1.00 31.59           O1-
ANISOU 1841  OD2 ASP A 223     4047   4538   3417    714    -18    -42       O1-
ATOM   1842  N   GLU A 224      27.847  26.973 -12.637  1.00 15.57           N  
ANISOU 1842  N   GLU A 224     2034   2447   1435    603    140    126       N  
ATOM   1843  CA  GLU A 224      28.402  28.271 -12.963  1.00 15.72           C  
ANISOU 1843  CA  GLU A 224     2065   2463   1445    596    200    206       C  
ATOM   1844  C   GLU A 224      27.349  29.326 -13.197  1.00 18.73           C  
ANISOU 1844  C   GLU A 224     2473   2823   1819    619    210    256       C  
ATOM   1845  O   GLU A 224      27.630  30.508 -13.034  1.00 20.04           O  
ANISOU 1845  O   GLU A 224     2655   2949   2009    595    258    321       O  
ATOM   1846  CB  GLU A 224      29.315  28.158 -14.171  1.00 17.08           C  
ANISOU 1846  CB  GLU A 224     2224   2714   1550    635    230    227       C  
ATOM   1847  CG  GLU A 224      30.625  27.442 -13.853  1.00 18.73           C  
ANISOU 1847  CG  GLU A 224     2405   2936   1775    606    237    192       C  
ATOM   1848  CD  GLU A 224      31.581  28.206 -12.955  1.00 18.69           C  
ANISOU 1848  CD  GLU A 224     2396   2879   1828    539    283    226       C  
ATOM   1849  OE1 GLU A 224      31.503  29.455 -12.951  1.00 17.98           O  
ANISOU 1849  OE1 GLU A 224     2323   2755   1753    520    329    291       O  
ATOM   1850  OE2 GLU A 224      32.360  27.576 -12.204  1.00 18.10           O1-
ANISOU 1850  OE2 GLU A 224     2299   2792   1787    506    272    183       O1-
ATOM   1851  N   VAL A 225      26.114  28.928 -13.534  1.00 16.32           N  
ANISOU 1851  N   VAL A 225     2171   2541   1490    662    163    222       N  
ATOM   1852  CA  VAL A 225      25.054  29.911 -13.729  1.00 15.65           C  
ANISOU 1852  CA  VAL A 225     2107   2439   1398    691    166    265       C  
ATOM   1853  C   VAL A 225      24.658  30.555 -12.400  1.00 18.15           C  
ANISOU 1853  C   VAL A 225     2436   2665   1796    633    172    270       C  
ATOM   1854  O   VAL A 225      24.575  31.780 -12.305  1.00 18.46           O  
ANISOU 1854  O   VAL A 225     2496   2662   1855    627    209    332       O  
ATOM   1855  CB  VAL A 225      23.821  29.263 -14.410  1.00 18.88           C  
ANISOU 1855  CB  VAL A 225     2507   2906   1760    754    110    215       C  
ATOM   1856  CG1 VAL A 225      22.616  30.231 -14.456  1.00 18.60           C  
ANISOU 1856  CG1 VAL A 225     2491   2852   1725    786    105    250       C  
ATOM   1857  CG2 VAL A 225      24.174  28.771 -15.808  1.00 20.59           C  
ANISOU 1857  CG2 VAL A 225     2712   3223   1889    820    107    211       C  
ATOM   1858  N   VAL A 226      24.383  29.728 -11.385  1.00 16.14           N  
ANISOU 1858  N   VAL A 226     2167   2380   1586    592    135    204       N  
ATOM   1859  CA  VAL A 226      23.949  30.289 -10.116  1.00 16.01           C  
ANISOU 1859  CA  VAL A 226     2158   2289   1637    540    138    202       C  
ATOM   1860  C   VAL A 226      25.101  30.730  -9.230  1.00 15.89           C  
ANISOU 1860  C   VAL A 226     2141   2225   1671    476    177    221       C  
ATOM   1861  O   VAL A 226      24.908  31.598  -8.385  1.00 16.76           O  
ANISOU 1861  O   VAL A 226     2259   2276   1831    439    196    237       O  
ATOM   1862  CB  VAL A 226      22.945  29.381  -9.367  1.00 20.48           C  
ANISOU 1862  CB  VAL A 226     2712   2842   2228    525     86    131       C  
ATOM   1863  CG1 VAL A 226      21.680  29.149 -10.191  1.00 21.85           C  
ANISOU 1863  CG1 VAL A 226     2880   3060   2361    585     49    107       C  
ATOM   1864  CG2 VAL A 226      23.587  28.065  -8.965  1.00 19.85           C  
ANISOU 1864  CG2 VAL A 226     2614   2770   2157    497     65     79       C  
ATOM   1865  N   TRP A 227      26.290  30.161  -9.431  1.00 14.67           N  
ANISOU 1865  N   TRP A 227     1972   2099   1502    465    189    215       N  
ATOM   1866  CA  TRP A 227      27.431  30.451  -8.586  1.00 14.18           C  
ANISOU 1866  CA  TRP A 227     1899   2003   1484    406    221    221       C  
ATOM   1867  C   TRP A 227      28.710  30.484  -9.410  1.00 15.50           C  
ANISOU 1867  C   TRP A 227     2055   2214   1620    414    259    249       C  
ATOM   1868  O   TRP A 227      29.462  29.501  -9.489  1.00 14.30           O  
ANISOU 1868  O   TRP A 227     1883   2100   1451    416    244    214       O  
ATOM   1869  CB  TRP A 227      27.516  29.413  -7.474  1.00 13.23           C  
ANISOU 1869  CB  TRP A 227     1763   1868   1394    371    183    160       C  
ATOM   1870  CG  TRP A 227      28.536  29.701  -6.408  1.00 12.27           C  
ANISOU 1870  CG  TRP A 227     1628   1717   1318    312    206    156       C  
ATOM   1871  CD1 TRP A 227      29.407  30.751  -6.329  1.00 14.44           C  
ANISOU 1871  CD1 TRP A 227     1897   1974   1617    281    257    192       C  
ATOM   1872  CD2 TRP A 227      28.751  28.907  -5.234  1.00 12.58           C  
ANISOU 1872  CD2 TRP A 227     1654   1742   1384    279    177    110       C  
ATOM   1873  CE2 TRP A 227      29.793  29.511  -4.500  1.00 13.80           C  
ANISOU 1873  CE2 TRP A 227     1791   1880   1572    233    208    116       C  
ATOM   1874  CE3 TRP A 227      28.163  27.737  -4.739  1.00 12.90           C  
ANISOU 1874  CE3 TRP A 227     1695   1781   1425    284    130     67       C  
ATOM   1875  NE1 TRP A 227      30.208  30.606  -5.201  1.00 14.30           N  
ANISOU 1875  NE1 TRP A 227     1856   1940   1636    232    257    162       N  
ATOM   1876  CZ2 TRP A 227      30.257  28.976  -3.277  1.00 14.26           C  
ANISOU 1876  CZ2 TRP A 227     1833   1931   1654    199    188     79       C  
ATOM   1877  CZ3 TRP A 227      28.612  27.214  -3.531  1.00 13.80           C  
ANISOU 1877  CZ3 TRP A 227     1798   1879   1565    248    115     40       C  
ATOM   1878  CH2 TRP A 227      29.650  27.834  -2.821  1.00 14.21           C  
ANISOU 1878  CH2 TRP A 227     1834   1925   1641    210    142     47       C  
ATOM   1879  N   PRO A 228      28.979  31.614 -10.055  1.00 15.63           N  
ANISOU 1879  N   PRO A 228     2085   2226   1629    422    311    316       N  
ATOM   1880  CA  PRO A 228      30.202  31.727 -10.861  1.00 15.81           C  
ANISOU 1880  CA  PRO A 228     2094   2293   1621    425    356    349       C  
ATOM   1881  C   PRO A 228      31.437  31.426 -10.029  1.00 17.50           C  
ANISOU 1881  C   PRO A 228     2277   2498   1874    368    369    315       C  
ATOM   1882  O   PRO A 228      31.595  31.911  -8.901  1.00 18.24           O  
ANISOU 1882  O   PRO A 228     2365   2535   2031    313    377    304       O  
ATOM   1883  CB  PRO A 228      30.187  33.190 -11.306  1.00 18.51           C  
ANISOU 1883  CB  PRO A 228     2459   2600   1973    424    417    431       C  
ATOM   1884  CG  PRO A 228      28.721  33.542 -11.338  1.00 22.45           C  
ANISOU 1884  CG  PRO A 228     2988   3073   2469    461    388    442       C  
ATOM   1885  CD  PRO A 228      28.157  32.846 -10.132  1.00 17.71           C  
ANISOU 1885  CD  PRO A 228     2376   2442   1910    431    334    368       C  
ATOM   1886  N   GLY A 229      32.263  30.546 -10.574  1.00 17.07           N  
ANISOU 1886  N   GLY A 229     2199   2507   1780    388    363    291       N  
ATOM   1887  CA  GLY A 229      33.485  30.086  -9.942  1.00 18.12           C  
ANISOU 1887  CA  GLY A 229     2296   2650   1937    349    368    254       C  
ATOM   1888  C   GLY A 229      33.324  28.805  -9.145  1.00 17.83           C  
ANISOU 1888  C   GLY A 229     2250   2613   1912    351    305    184       C  
ATOM   1889  O   GLY A 229      34.342  28.263  -8.710  1.00 18.82           O  
ANISOU 1889  O   GLY A 229     2346   2757   2048    333    302    151       O  
ATOM   1890  N   VAL A 230      32.084  28.308  -8.898  1.00 14.04           N  
ANISOU 1890  N   VAL A 230     1792   2111   1432    371    256    161       N  
ATOM   1891  CA  VAL A 230      31.891  27.122  -8.053  1.00 12.88           C  
ANISOU 1891  CA  VAL A 230     1640   1952   1304    367    203    102       C  
ATOM   1892  C   VAL A 230      32.656  25.915  -8.571  1.00 15.01           C  
ANISOU 1892  C   VAL A 230     1888   2274   1542    400    182     62       C  
ATOM   1893  O   VAL A 230      33.179  25.153  -7.744  1.00 14.20           O  
ANISOU 1893  O   VAL A 230     1771   2160   1463    385    158     26       O  
ATOM   1894  CB  VAL A 230      30.387  26.769  -7.827  1.00 14.60           C  
ANISOU 1894  CB  VAL A 230     1881   2140   1526    381    160     83       C  
ATOM   1895  CG1 VAL A 230      29.702  26.257  -9.109  1.00 15.34           C  
ANISOU 1895  CG1 VAL A 230     1981   2280   1566    442    140     73       C  
ATOM   1896  CG2 VAL A 230      30.216  25.757  -6.701  1.00 14.62           C  
ANISOU 1896  CG2 VAL A 230     1881   2113   1561    360    118     36       C  
ATOM   1897  N   THR A 231      32.734  25.731  -9.892  1.00 16.01           N  
ANISOU 1897  N   THR A 231     2011   2458   1613    449    190     69       N  
ATOM   1898  CA  THR A 231      33.372  24.523 -10.398  1.00 17.20           C  
ANISOU 1898  CA  THR A 231     2140   2659   1737    486    166     21       C  
ATOM   1899  C   THR A 231      34.871  24.535 -10.252  1.00 19.84           C  
ANISOU 1899  C   THR A 231     2442   3022   2075    469    194     18       C  
ATOM   1900  O   THR A 231      35.497  23.505 -10.545  1.00 22.22           O  
ANISOU 1900  O   THR A 231     2721   3361   2359    500    173    -26       O  
ATOM   1901  CB  THR A 231      32.951  24.218 -11.835  1.00 21.18           C  
ANISOU 1901  CB  THR A 231     2646   3226   2176    548    159     14       C  
ATOM   1902  CG2 THR A 231      31.456  24.070 -11.984  1.00 19.77           C  
ANISOU 1902  CG2 THR A 231     2491   3028   1993    569    123      2       C  
ATOM   1903  OG1 THR A 231      33.477  25.215 -12.709  1.00 20.29           O  
ANISOU 1903  OG1 THR A 231     2528   3157   2023    556    216     72       O  
ATOM   1904  N   SER A 232      35.458  25.642  -9.814  1.00 19.97           N  
ANISOU 1904  N   SER A 232     2864   2496   2227    290    586    -89       N  
ATOM   1905  CA ASER A 232      36.898  25.752  -9.630  0.50 21.31           C  
ANISOU 1905  CA ASER A 232     2991   2641   2464    259    655    -89       C  
ATOM   1906  CA BSER A 232      36.902  25.720  -9.635  0.50 21.25           C  
ANISOU 1906  CA BSER A 232     2983   2634   2456    260    654    -90       C  
ATOM   1907  C   SER A 232      37.261  25.701  -8.150  1.00 24.82           C  
ANISOU 1907  C   SER A 232     3368   3058   3005    192    618   -104       C  
ATOM   1908  O   SER A 232      38.448  25.832  -7.797  1.00 26.39           O  
ANISOU 1908  O   SER A 232     3521   3232   3275    161    664   -111       O  
ATOM   1909  CB ASER A 232      37.433  27.015 -10.303  0.50 25.31           C  
ANISOU 1909  CB ASER A 232     3529   3131   2958    273    766    -35       C  
ATOM   1910  CB BSER A 232      37.467  26.957 -10.329  0.50 25.13           C  
ANISOU 1910  CB BSER A 232     3506   3110   2935    274    766    -37       C  
ATOM   1911  OG ASER A 232      37.273  26.942 -11.710  0.50 28.00           O  
ANISOU 1911  OG ASER A 232     3934   3503   3203    343    807    -22       O  
ATOM   1912  OG BSER A 232      37.102  28.127  -9.620  0.50 27.83           O  
ANISOU 1912  OG BSER A 232     3844   3420   3308    240    777     -1       O  
ATOM   1913  N   MET A 233      36.250  25.499  -7.265  1.00 18.31           N  
ANISOU 1913  N   MET A 233     2536   2238   2184    173    535   -111       N  
ATOM   1914  CA AMET A 233      36.556  25.453  -5.856  0.50 14.72           C  
ANISOU 1914  CA AMET A 233     2025   1763   1807    118    500   -123       C  
ATOM   1915  CA BMET A 233      36.460  25.437  -5.811  0.50 18.33           C  
ANISOU 1915  CA BMET A 233     2483   2221   2262    118    494   -123       C  
ATOM   1916  C   MET A 233      37.322  24.206  -5.439  1.00 18.70           C  
ANISOU 1916  C   MET A 233     2481   2265   2360    104    462   -165       C  
ATOM   1917  O   MET A 233      37.221  23.194  -6.098  1.00 17.19           O  
ANISOU 1917  O   MET A 233     2301   2091   2139    133    437   -190       O  
ATOM   1918  CB AMET A 233      35.301  25.664  -5.060  0.50 14.13           C  
ANISOU 1918  CB AMET A 233     1956   1695   1717    105    436   -112       C  
ATOM   1919  CB BMET A 233      35.118  25.406  -5.042  0.50 20.44           C  
ANISOU 1919  CB BMET A 233     2756   2500   2511    108    418   -118       C  
ATOM   1920  CG AMET A 233      34.700  26.992  -5.382  0.50 12.89           C  
ANISOU 1920  CG AMET A 233     1840   1534   1525    118    475    -73       C  
ATOM   1921  CG BMET A 233      34.345  26.735  -5.073  0.50 24.25           C  
ANISOU 1921  CG BMET A 233     3272   2978   2962    113    443    -80       C  
ATOM   1922  SD AMET A 233      33.279  27.294  -4.364  0.50 13.17           S  
ANISOU 1922  SD AMET A 233     1875   1578   1550    101    404    -65       S  
ATOM   1923  SD BMET A 233      34.719  27.986  -3.797  0.50 28.50           S  
ANISOU 1923  SD BMET A 233     3773   3484   3570     64    464    -64       S  
ATOM   1924  CE AMET A 233      34.129  27.527  -2.865  0.50 11.04           C  
ANISOU 1924  CE AMET A 233     1542   1285   1368     46    399    -77       C  
ATOM   1925  CE BMET A 233      33.959  27.266  -2.415  0.50 25.28           C  
ANISOU 1925  CE BMET A 233     3333   3094   3179     37    371    -84       C  
ATOM   1926  N   PRO A 234      38.144  24.285  -4.354  1.00 18.19           N  
ANISOU 1926  N   PRO A 234     2361   2177   2372     63    457   -178       N  
ATOM   1927  CA  PRO A 234      39.039  23.151  -4.037  1.00 17.96           C  
ANISOU 1927  CA  PRO A 234     2288   2143   2392     55    429   -218       C  
ATOM   1928  C   PRO A 234      38.448  21.758  -3.964  1.00 18.23           C  
ANISOU 1928  C   PRO A 234     2324   2193   2409     68    350   -241       C  
ATOM   1929  O   PRO A 234      39.055  20.809  -4.443  1.00 19.20           O  
ANISOU 1929  O   PRO A 234     2434   2317   2545     84    344   -272       O  
ATOM   1930  CB  PRO A 234      39.711  23.593  -2.731  1.00 19.07           C  
ANISOU 1930  CB  PRO A 234     2376   2261   2608     13    419   -226       C  
ATOM   1931  CG  PRO A 234      39.725  25.070  -2.812  1.00 24.29           C  
ANISOU 1931  CG  PRO A 234     3048   2907   3275      3    482   -197       C  
ATOM   1932  CD  PRO A 234      38.413  25.438  -3.461  1.00 20.23           C  
ANISOU 1932  CD  PRO A 234     2595   2412   2679     28    480   -162       C  
ATOM   1933  N   ASP A 235      37.263  21.618  -3.381  1.00 14.46           N  
ANISOU 1933  N   ASP A 235     1861   1725   1910     60    290   -227       N  
ATOM   1934  CA  ASP A 235      36.656  20.318  -3.165  1.00 14.00           C  
ANISOU 1934  CA  ASP A 235     1797   1671   1852     66    216   -244       C  
ATOM   1935  C   ASP A 235      35.504  20.057  -4.097  1.00 17.08           C  
ANISOU 1935  C   ASP A 235     2228   2080   2181     99    195   -245       C  
ATOM   1936  O   ASP A 235      34.807  19.048  -3.963  1.00 18.69           O  
ANISOU 1936  O   ASP A 235     2427   2284   2391    103    132   -260       O  
ATOM   1937  CB  ASP A 235      36.276  20.152  -1.688  1.00 16.44           C  
ANISOU 1937  CB  ASP A 235     2079   1973   2195     32    162   -231       C  
ATOM   1938  CG  ASP A 235      37.443  20.235  -0.751  1.00 23.92           C  
ANISOU 1938  CG  ASP A 235     2983   2905   3201      8    167   -241       C  
ATOM   1939  OD1 ASP A 235      38.506  19.673  -1.076  1.00 24.97           O  
ANISOU 1939  OD1 ASP A 235     3093   3026   3368     15    179   -271       O  
ATOM   1940  OD2 ASP A 235      37.338  20.947   0.249  1.00 25.63           O1-
ANISOU 1940  OD2 ASP A 235     3188   3120   3429    -13    162   -225       O1-
ATOM   1941  N   TYR A 236      35.318  20.926  -5.101  1.00 13.36           N  
ANISOU 1941  N   TYR A 236     1799   1623   1655    128    247   -231       N  
ATOM   1942  CA  TYR A 236      34.289  20.672  -6.091  1.00 13.17           C  
ANISOU 1942  CA  TYR A 236     1816   1620   1567    171    223   -240       C  
ATOM   1943  C   TYR A 236      34.745  19.504  -6.975  1.00 14.65           C  
ANISOU 1943  C   TYR A 236     2003   1814   1751    206    208   -286       C  
ATOM   1944  O   TYR A 236      35.903  19.483  -7.415  1.00 15.55           O  
ANISOU 1944  O   TYR A 236     2109   1926   1874    215    260   -297       O  
ATOM   1945  CB  TYR A 236      34.056  21.914  -6.957  1.00 14.51           C  
ANISOU 1945  CB  TYR A 236     2037   1804   1673    202    285   -211       C  
ATOM   1946  CG  TYR A 236      33.046  21.643  -8.043  1.00 16.60           C  
ANISOU 1946  CG  TYR A 236     2347   2095   1866    257    255   -226       C  
ATOM   1947  CD1 TYR A 236      31.686  21.835  -7.819  1.00 17.72           C  
ANISOU 1947  CD1 TYR A 236     2503   2244   1986    260    203   -220       C  
ATOM   1948  CD2 TYR A 236      33.447  21.165  -9.288  1.00 17.55           C  
ANISOU 1948  CD2 TYR A 236     2495   2234   1941    310    274   -254       C  
ATOM   1949  CE1 TYR A 236      30.745  21.528  -8.803  1.00 17.44           C  
ANISOU 1949  CE1 TYR A 236     2503   2232   1891    315    165   -245       C  
ATOM   1950  CE2 TYR A 236      32.517  20.823 -10.261  1.00 18.02           C  
ANISOU 1950  CE2 TYR A 236     2593   2319   1934    368    234   -280       C  
ATOM   1951  CZ  TYR A 236      31.170  21.011 -10.013  1.00 18.45           C  
ANISOU 1951  CZ  TYR A 236     2658   2379   1974    370    177   -276       C  
ATOM   1952  OH  TYR A 236      30.253  20.697 -10.983  1.00 22.02           O  
ANISOU 1952  OH  TYR A 236     3145   2857   2365    431    131   -309       O  
ATOM   1953  N   LYS A 237      33.824  18.596  -7.317  1.00 13.44           N  
ANISOU 1953  N   LYS A 237     1855   1668   1583    229    141   -315       N  
ATOM   1954  CA  LYS A 237      34.128  17.509  -8.233  1.00 13.82           C  
ANISOU 1954  CA  LYS A 237     1905   1723   1624    270    119   -366       C  
ATOM   1955  C   LYS A 237      33.092  17.528  -9.324  1.00 15.84           C  
ANISOU 1955  C   LYS A 237     2206   2006   1808    326     94   -387       C  
ATOM   1956  O   LYS A 237      31.892  17.488  -9.036  1.00 15.22           O  
ANISOU 1956  O   LYS A 237     2128   1926   1729    321     40   -385       O  
ATOM   1957  CB  LYS A 237      34.136  16.142  -7.511  1.00 16.64           C  
ANISOU 1957  CB  LYS A 237     2214   2053   2056    244     48   -396       C  
ATOM   1958  CG  LYS A 237      35.192  15.963  -6.364  1.00 19.07           C  
ANISOU 1958  CG  LYS A 237     2476   2334   2435    196     59   -382       C  
ATOM   1959  CD  LYS A 237      36.671  16.226  -6.761  1.00 20.47           C  
ANISOU 1959  CD  LYS A 237     2645   2513   2619    204    126   -392       C  
ATOM   1960  CE  LYS A 237      37.650  15.994  -5.603  1.00 24.54           C  
ANISOU 1960  CE  LYS A 237     3111   3003   3211    162    123   -388       C  
ATOM   1961  NZ  LYS A 237      39.053  16.403  -5.948  1.00 25.53           N1+
ANISOU 1961  NZ  LYS A 237     3221   3128   3352    166    193   -399       N1+
ATOM   1962  N   PRO A 238      33.529  17.504 -10.594  1.00 15.56           N  
ANISOU 1962  N   PRO A 238     2204   1995   1711    385    128   -411       N  
ATOM   1963  CA  PRO A 238      32.572  17.417 -11.715  1.00 15.30           C  
ANISOU 1963  CA  PRO A 238     2218   1993   1602    453     94   -442       C  
ATOM   1964  C   PRO A 238      31.648  16.190 -11.666  1.00 17.14           C  
ANISOU 1964  C   PRO A 238     2423   2215   1872    461     -9   -498       C  
ATOM   1965  O   PRO A 238      30.573  16.177 -12.301  1.00 18.29           O  
ANISOU 1965  O   PRO A 238     2596   2380   1974    505    -56   -525       O  
ATOM   1966  CB  PRO A 238      33.487  17.337 -12.953  1.00 18.02           C  
ANISOU 1966  CB  PRO A 238     2595   2367   1886    514    150   -465       C  
ATOM   1967  CG  PRO A 238      34.723  18.005 -12.538  1.00 20.52           C  
ANISOU 1967  CG  PRO A 238     2896   2670   2231    476    240   -421       C  
ATOM   1968  CD  PRO A 238      34.909  17.672 -11.085  1.00 16.95           C  
ANISOU 1968  CD  PRO A 238     2383   2178   1880    398    206   -411       C  
ATOM   1969  N   SER A 239      32.054  15.148 -10.895  1.00 14.74           N  
ANISOU 1969  N   SER A 239     2064   1878   1658    418    -46   -518       N  
ATOM   1970  CA  SER A 239      31.267  13.913 -10.759  1.00 13.81           C  
ANISOU 1970  CA  SER A 239     1913   1738   1597    417   -139   -568       C  
ATOM   1971  C   SER A 239      30.140  14.066  -9.708  1.00 15.19           C  
ANISOU 1971  C   SER A 239     2063   1889   1818    367   -179   -535       C  
ATOM   1972  O   SER A 239      29.403  13.101  -9.491  1.00 15.82           O  
ANISOU 1972  O   SER A 239     2110   1944   1958    359   -251   -568       O  
ATOM   1973  CB  SER A 239      32.175  12.741 -10.394  1.00 13.18           C  
ANISOU 1973  CB  SER A 239     1788   1626   1595    397   -159   -598       C  
ATOM   1974  OG  SER A 239      32.925  13.105  -9.247  1.00 14.02           O  
ANISOU 1974  OG  SER A 239     1869   1712   1746    336   -118   -544       O  
ATOM   1975  N   PHE A 240      29.980  15.246  -9.061  1.00 14.35           N  
ANISOU 1975  N   PHE A 240     1971   1791   1690    335   -134   -473       N  
ATOM   1976  CA  PHE A 240      28.839  15.400  -8.165  1.00 13.67           C  
ANISOU 1976  CA  PHE A 240     1864   1691   1640    297   -171   -447       C  
ATOM   1977  C   PHE A 240      27.574  15.129  -8.980  1.00 16.55           C  
ANISOU 1977  C   PHE A 240     2239   2066   1981    342   -232   -493       C  
ATOM   1978  O   PHE A 240      27.401  15.684 -10.075  1.00 17.87           O  
ANISOU 1978  O   PHE A 240     2455   2268   2068    402   -220   -511       O  
ATOM   1979  CB  PHE A 240      28.721  16.833  -7.647  1.00 14.98           C  
ANISOU 1979  CB  PHE A 240     2052   1871   1767    275   -117   -387       C  
ATOM   1980  CG  PHE A 240      29.749  17.281  -6.651  1.00 14.70           C  
ANISOU 1980  CG  PHE A 240     2001   1824   1762    226    -65   -342       C  
ATOM   1981  CD1 PHE A 240      30.468  16.360  -5.892  1.00 16.94           C  
ANISOU 1981  CD1 PHE A 240     2242   2079   2114    192    -81   -346       C  
ATOM   1982  CD2 PHE A 240      29.957  18.633  -6.414  1.00 15.71           C  
ANISOU 1982  CD2 PHE A 240     2152   1963   1855    216     -6   -298       C  
ATOM   1983  CE1 PHE A 240      31.379  16.804  -4.907  1.00 17.26           C  
ANISOU 1983  CE1 PHE A 240     2265   2111   2183    152    -42   -311       C  
ATOM   1984  CE2 PHE A 240      30.874  19.068  -5.466  1.00 16.68           C  
ANISOU 1984  CE2 PHE A 240     2253   2072   2011    173     34   -266       C  
ATOM   1985  CZ  PHE A 240      31.552  18.159  -4.704  1.00 14.44           C  
ANISOU 1985  CZ  PHE A 240     1929   1768   1792    143     13   -274       C  
ATOM   1986  N   PRO A 241      26.612  14.401  -8.412  1.00 15.32           N  
ANISOU 1986  N   PRO A 241     2042   1884   1897    315   -294   -507       N  
ATOM   1987  CA  PRO A 241      25.334  14.227  -9.113  1.00 16.30           C  
ANISOU 1987  CA  PRO A 241     2168   2016   2010    355   -355   -555       C  
ATOM   1988  C   PRO A 241      24.618  15.572  -9.297  1.00 19.09           C  
ANISOU 1988  C   PRO A 241     2561   2402   2290    375   -332   -525       C  
ATOM   1989  O   PRO A 241      24.782  16.490  -8.476  1.00 16.35           O  
ANISOU 1989  O   PRO A 241     2220   2058   1934    335   -281   -462       O  
ATOM   1990  CB  PRO A 241      24.558  13.302  -8.178  1.00 18.49           C  
ANISOU 1990  CB  PRO A 241     2382   2248   2396    304   -407   -557       C  
ATOM   1991  CG  PRO A 241      25.640  12.569  -7.368  1.00 21.16           C  
ANISOU 1991  CG  PRO A 241     2691   2554   2795    259   -388   -532       C  
ATOM   1992  CD  PRO A 241      26.656  13.638  -7.147  1.00 17.54           C  
ANISOU 1992  CD  PRO A 241     2269   2123   2273    251   -311   -481       C  
ATOM   1993  N   LYS A 242      23.825  15.688 -10.370  1.00 17.92           N  
ANISOU 1993  N   LYS A 242     2440   2279   2091    440   -373   -574       N  
ATOM   1994  CA  LYS A 242      23.073  16.884 -10.701  1.00 19.34           C  
ANISOU 1994  CA  LYS A 242     2661   2489   2199    472   -362   -554       C  
ATOM   1995  C   LYS A 242      21.617  16.712 -10.294  1.00 22.04           C  
ANISOU 1995  C   LYS A 242     2961   2817   2596    457   -426   -575       C  
ATOM   1996  O   LYS A 242      20.861  16.007 -10.964  1.00 23.44           O  
ANISOU 1996  O   LYS A 242     3121   2992   2792    497   -498   -645       O  
ATOM   1997  CB  LYS A 242      23.217  17.210 -12.199  1.00 23.21           C  
ANISOU 1997  CB  LYS A 242     3216   3021   2584    565   -361   -591       C  
ATOM   1998  CG  LYS A 242      24.643  17.628 -12.574  1.00 33.34           C  
ANISOU 1998  CG  LYS A 242     4542   4320   3807    577   -278   -556       C  
ATOM   1999  CD  LYS A 242      24.745  18.050 -14.037  1.00 45.08           C  
ANISOU 1999  CD  LYS A 242     6099   5851   5177    674   -266   -580       C  
ATOM   2000  CE  LYS A 242      26.163  18.371 -14.444  1.00 55.32           C  
ANISOU 2000  CE  LYS A 242     7434   7163   6425    686   -176   -547       C  
ATOM   2001  NZ  LYS A 242      26.920  17.149 -14.817  1.00 62.93           N1+
ANISOU 2001  NZ  LYS A 242     8372   8122   7415    700   -195   -603       N1+
ATOM   2002  N   TRP A 243      21.234  17.328  -9.178  1.00 17.95           N  
ANISOU 2002  N   TRP A 243     2422   2288   2108    400   -399   -518       N  
ATOM   2003  CA  TRP A 243      19.880  17.325  -8.651  1.00 18.66           C  
ANISOU 2003  CA  TRP A 243     2471   2368   2252    379   -443   -526       C  
ATOM   2004  C   TRP A 243      19.216  18.628  -8.953  1.00 19.78           C  
ANISOU 2004  C   TRP A 243     2654   2542   2321    414   -431   -509       C  
ATOM   2005  O   TRP A 243      19.860  19.681  -8.989  1.00 17.16           O  
ANISOU 2005  O   TRP A 243     2372   2229   1920    421   -369   -460       O  
ATOM   2006  CB  TRP A 243      19.892  17.126  -7.138  1.00 19.08           C  
ANISOU 2006  CB  TRP A 243     2474   2392   2385    296   -417   -472       C  
ATOM   2007  CG  TRP A 243      20.248  15.729  -6.734  1.00 20.27           C  
ANISOU 2007  CG  TRP A 243     2575   2503   2626    260   -441   -488       C  
ATOM   2008  CD1 TRP A 243      19.442  14.630  -6.790  1.00 23.90           C  
ANISOU 2008  CD1 TRP A 243     2979   2929   3172    255   -504   -536       C  
ATOM   2009  CD2 TRP A 243      21.458  15.306  -6.101  1.00 18.83           C  
ANISOU 2009  CD2 TRP A 243     2387   2303   2466    222   -402   -453       C  
ATOM   2010  CE2 TRP A 243      21.342  13.919  -5.853  1.00 23.45           C  
ANISOU 2010  CE2 TRP A 243     2920   2844   3147    199   -445   -479       C  
ATOM   2011  CE3 TRP A 243      22.638  15.964  -5.729  1.00 17.15           C  
ANISOU 2011  CE3 TRP A 243     2206   2103   2208    207   -338   -404       C  
ATOM   2012  NE1 TRP A 243      20.088  13.541  -6.256  1.00 23.84           N  
ANISOU 2012  NE1 TRP A 243     2937   2882   3238    216   -505   -528       N  
ATOM   2013  CZ2 TRP A 243      22.347  13.188  -5.202  1.00 22.63           C  
ANISOU 2013  CZ2 TRP A 243     2799   2712   3088    163   -427   -453       C  
ATOM   2014  CZ3 TRP A 243      23.637  15.232  -5.107  1.00 18.33           C  
ANISOU 2014  CZ3 TRP A 243     2334   2228   2403    172   -322   -386       C  
ATOM   2015  CH2 TRP A 243      23.474  13.870  -4.823  1.00 19.39           C  
ANISOU 2015  CH2 TRP A 243     2421   2321   2626    151   -367   -408       C  
ATOM   2016  N   ALA A 244      17.884  18.556  -9.195  1.00 21.02           N  
ANISOU 2016  N   ALA A 244     2787   2700   2501    437   -494   -553       N  
ATOM   2017  CA  ALA A 244      17.070  19.733  -9.457  1.00 20.99           C  
ANISOU 2017  CA  ALA A 244     2814   2723   2437    474   -496   -544       C  
ATOM   2018  C   ALA A 244      16.696  20.434  -8.168  1.00 22.92           C  
ANISOU 2018  C   ALA A 244     3032   2959   2717    410   -458   -485       C  
ATOM   2019  O   ALA A 244      16.608  19.813  -7.118  1.00 23.94           O  
ANISOU 2019  O   ALA A 244     3104   3063   2931    345   -453   -467       O  
ATOM   2020  CB  ALA A 244      15.797  19.336 -10.195  1.00 22.35           C  
ANISOU 2020  CB  ALA A 244     2965   2900   2628    526   -585   -624       C  
ATOM   2021  N   ARG A 245      16.491  21.737  -8.242  1.00 19.60           N  
ANISOU 2021  N   ARG A 245     2655   2561   2230    433   -428   -452       N  
ATOM   2022  CA  ARG A 245      16.107  22.562  -7.119  1.00 19.05           C  
ANISOU 2022  CA  ARG A 245     2567   2491   2183    385   -394   -402       C  
ATOM   2023  C   ARG A 245      14.621  22.381  -6.738  1.00 21.42           C  
ANISOU 2023  C   ARG A 245     2808   2785   2544    377   -447   -434       C  
ATOM   2024  O   ARG A 245      13.757  22.337  -7.632  1.00 21.69           O  
ANISOU 2024  O   ARG A 245     2846   2830   2564    434   -508   -491       O  
ATOM   2025  CB  ARG A 245      16.363  24.024  -7.469  1.00 17.61           C  
ANISOU 2025  CB  ARG A 245     2451   2329   1912    420   -350   -363       C  
ATOM   2026  CG  ARG A 245      15.940  24.991  -6.398  1.00 18.64           C  
ANISOU 2026  CG  ARG A 245     2565   2458   2058    381   -319   -319       C  
ATOM   2027  CD  ARG A 245      16.354  26.390  -6.768  1.00 19.32           C  
ANISOU 2027  CD  ARG A 245     2717   2555   2067    414   -272   -280       C  
ATOM   2028  NE  ARG A 245      16.053  27.369  -5.738  1.00 20.37           N  
ANISOU 2028  NE  ARG A 245     2837   2686   2217    378   -241   -242       N  
ATOM   2029  CZ  ARG A 245      16.921  27.759  -4.807  1.00 18.57           C  
ANISOU 2029  CZ  ARG A 245     2603   2448   2006    327   -184   -197       C  
ATOM   2030  NH1 ARG A 245      18.129  27.200  -4.733  1.00 18.79           N1+
ANISOU 2030  NH1 ARG A 245     2632   2464   2042    302   -152   -183       N1+
ATOM   2031  NH2 ARG A 245      16.604  28.733  -3.963  1.00 21.80           N  
ANISOU 2031  NH2 ARG A 245     3002   2857   2422    306   -162   -171       N  
ATOM   2032  N   GLN A 246      14.323  22.324  -5.436  1.00 18.72           N  
ANISOU 2032  N   GLN A 246     2414   2431   2267    310   -423   -400       N  
ATOM   2033  CA AGLN A 246      12.942  22.196  -4.950  0.70 19.12           C  
ANISOU 2033  CA AGLN A 246     2404   2478   2384    295   -459   -423       C  
ATOM   2034  CA BGLN A 246      12.954  22.192  -4.920  0.30 18.91           C  
ANISOU 2034  CA BGLN A 246     2377   2451   2358    293   -458   -421       C  
ATOM   2035  C   GLN A 246      12.356  23.569  -4.621  1.00 22.14           C  
ANISOU 2035  C   GLN A 246     2805   2883   2725    307   -439   -398       C  
ATOM   2036  O   GLN A 246      13.084  24.502  -4.271  1.00 21.86           O  
ANISOU 2036  O   GLN A 246     2812   2858   2636    298   -384   -347       O  
ATOM   2037  CB AGLN A 246      12.898  21.309  -3.687  0.70 19.79           C  
ANISOU 2037  CB AGLN A 246     2421   2537   2563    220   -439   -395       C  
ATOM   2038  CB BGLN A 246      12.948  21.366  -3.621  0.30 19.91           C  
ANISOU 2038  CB BGLN A 246     2437   2552   2575    217   -434   -390       C  
ATOM   2039  CG AGLN A 246      13.525  19.927  -3.838  0.70 21.63           C  
ANISOU 2039  CG AGLN A 246     2630   2738   2849    201   -455   -411       C  
ATOM   2040  CG BGLN A 246      13.194  19.873  -3.800  0.30 29.53           C  
ANISOU 2040  CG BGLN A 246     3618   3737   3865    200   -464   -419       C  
ATOM   2041  CD AGLN A 246      12.834  19.069  -4.873  0.70 41.64           C  
ANISOU 2041  CD AGLN A 246     5138   5257   5425    240   -531   -492       C  
ATOM   2042  CD BGLN A 246      13.231  19.123  -2.485  0.30 41.84           C  
ANISOU 2042  CD BGLN A 246     5120   5270   5507    128   -433   -374       C  
ATOM   2043  NE2AGLN A 246      13.583  18.621  -5.877  0.70 34.17           N  
ANISOU 2043  NE2AGLN A 246     4229   4311   4442    281   -554   -527       N  
ATOM   2044  NE2BGLN A 246      14.027  18.067  -2.440  0.30 33.21           N  
ANISOU 2044  NE2BGLN A 246     4018   4148   4451    107   -433   -371       N  
ATOM   2045  OE1AGLN A 246      11.627  18.808  -4.795  0.70 40.90           O  
ANISOU 2045  OE1AGLN A 246     4989   5153   5399    238   -571   -528       O  
ATOM   2046  OE1BGLN A 246      12.540  19.456  -1.510  0.30 33.85           O  
ANISOU 2046  OE1BGLN A 246     4073   4263   4525     94   -408   -342       O  
ATOM   2047  N   ASP A 247      11.021  23.682  -4.663  1.00 21.39           N  
ANISOU 2047  N   ASP A 247     2670   2792   2665    323   -483   -436       N  
ATOM   2048  CA AASP A 247      10.323  24.918  -4.319  0.50 20.27           C  
ANISOU 2048  CA AASP A 247     2537   2670   2496    335   -471   -421       C  
ATOM   2049  CA BASP A 247      10.337  24.919  -4.328  0.50 20.03           C  
ANISOU 2049  CA BASP A 247     2507   2640   2465    335   -471   -420       C  
ATOM   2050  C   ASP A 247      10.324  25.098  -2.816  1.00 22.58           C  
ANISOU 2050  C   ASP A 247     2788   2961   2830    266   -416   -368       C  
ATOM   2051  O   ASP A 247      10.055  24.142  -2.092  1.00 20.27           O  
ANISOU 2051  O   ASP A 247     2433   2653   2617    218   -414   -366       O  
ATOM   2052  CB AASP A 247       8.852  24.876  -4.788  0.50 23.42           C  
ANISOU 2052  CB AASP A 247     2894   3073   2932    373   -540   -486       C  
ATOM   2053  CB BASP A 247       8.895  24.869  -4.862  0.50 22.92           C  
ANISOU 2053  CB BASP A 247     2835   3010   2865    377   -542   -487       C  
ATOM   2054  CG AASP A 247       8.581  24.628  -6.260  0.50 34.61           C  
ANISOU 2054  CG AASP A 247     4342   4496   4314    452   -612   -553       C  
ATOM   2055  CG BASP A 247       8.250  26.223  -5.070  0.50 30.47           C  
ANISOU 2055  CG BASP A 247     3822   3988   3765    423   -548   -487       C  
ATOM   2056  OD1AASP A 247       9.527  24.729  -7.066  0.50 37.10           O  
ANISOU 2056  OD1AASP A 247     4726   4818   4552    490   -603   -545       O  
ATOM   2057  OD1BASP A 247       8.070  26.959  -4.071  0.50 28.34           O  
ANISOU 2057  OD1BASP A 247     3539   3726   3504    388   -504   -447       O  
ATOM   2058  OD2AASP A 247       7.406  24.379  -6.611  0.50 42.95           O1-
ANISOU 2058  OD2AASP A 247     5351   5551   5417    481   -678   -618       O1-
ATOM   2059  OD2BASP A 247       7.912  26.543  -6.225  0.50 40.45           O1-
ANISOU 2059  OD2BASP A 247     5127   5263   4977    498   -599   -529       O1-
ATOM   2060  N   PHE A 248      10.555  26.321  -2.332  1.00 17.69           N  
ANISOU 2060  N   PHE A 248     2202   2358   2160    266   -373   -328       N  
ATOM   2061  CA  PHE A 248      10.508  26.540  -0.877  1.00 18.37           C  
ANISOU 2061  CA  PHE A 248     2251   2449   2278    209   -325   -285       C  
ATOM   2062  C   PHE A 248       9.136  26.298  -0.281  1.00 18.45           C  
ANISOU 2062  C   PHE A 248     2188   2464   2358    192   -343   -306       C  
ATOM   2063  O   PHE A 248       9.037  26.035   0.935  1.00 19.20           O  
ANISOU 2063  O   PHE A 248     2240   2562   2494    142   -305   -273       O  
ATOM   2064  CB  PHE A 248      10.998  27.955  -0.529  1.00 21.27           C  
ANISOU 2064  CB  PHE A 248     2667   2832   2584    218   -282   -248       C  
ATOM   2065  CG  PHE A 248      12.490  28.007  -0.365  1.00 23.93           C  
ANISOU 2065  CG  PHE A 248     3044   3160   2887    198   -237   -208       C  
ATOM   2066  CD1 PHE A 248      13.306  28.381  -1.420  1.00 27.41           C  
ANISOU 2066  CD1 PHE A 248     3548   3593   3271    236   -233   -207       C  
ATOM   2067  CD2 PHE A 248      13.095  27.561   0.810  1.00 26.30           C  
ANISOU 2067  CD2 PHE A 248     3316   3459   3217    144   -200   -174       C  
ATOM   2068  CE1 PHE A 248      14.703  28.395  -1.277  1.00 27.89           C  
ANISOU 2068  CE1 PHE A 248     3639   3644   3313    215   -189   -174       C  
ATOM   2069  CE2 PHE A 248      14.492  27.540   0.934  1.00 28.34           C  
ANISOU 2069  CE2 PHE A 248     3607   3709   3453    128   -165   -145       C  
ATOM   2070  CZ  PHE A 248      15.282  27.962  -0.116  1.00 24.68           C  
ANISOU 2070  CZ  PHE A 248     3200   3236   2942    161   -159   -148       C  
ATOM   2071  N   SER A 249       8.064  26.318  -1.110  1.00 18.20           N  
ANISOU 2071  N   SER A 249     2139   2434   2343    236   -402   -363       N  
ATOM   2072  CA  SER A 249       6.731  26.037  -0.614  1.00 17.36           C  
ANISOU 2072  CA  SER A 249     1954   2328   2315    220   -420   -391       C  
ATOM   2073  C   SER A 249       6.715  24.596  -0.089  1.00 16.10           C  
ANISOU 2073  C   SER A 249     1730   2141   2245    165   -413   -385       C  
ATOM   2074  O   SER A 249       5.962  24.344   0.826  1.00 17.48           O  
ANISOU 2074  O   SER A 249     1840   2316   2486    127   -390   -374       O  
ATOM   2075  CB  SER A 249       5.692  26.227  -1.716  1.00 19.18           C  
ANISOU 2075  CB  SER A 249     2177   2561   2551    282   -494   -463       C  
ATOM   2076  OG  SER A 249       5.961  25.382  -2.822  1.00 19.23           O  
ANISOU 2076  OG  SER A 249     2198   2550   2560    312   -546   -506       O  
ATOM   2077  N   LYS A 250       7.556  23.686  -0.634  1.00 14.75           N  
ANISOU 2077  N   LYS A 250     1579   1948   2078    162   -427   -390       N  
ATOM   2078  CA  LYS A 250       7.612  22.299  -0.162  1.00 16.23           C  
ANISOU 2078  CA  LYS A 250     1710   2103   2356    112   -421   -381       C  
ATOM   2079  C   LYS A 250       8.542  22.153   1.050  1.00 21.77           C  
ANISOU 2079  C   LYS A 250     2420   2806   3046     59   -350   -304       C  
ATOM   2080  O   LYS A 250       8.276  21.311   1.932  1.00 23.19           O  
ANISOU 2080  O   LYS A 250     2543   2966   3301     10   -324   -276       O  
ATOM   2081  CB  LYS A 250       8.066  21.420  -1.342  1.00 18.70           C  
ANISOU 2081  CB  LYS A 250     2038   2391   2676    141   -475   -430       C  
ATOM   2082  CG  LYS A 250       8.238  19.915  -1.073  1.00 29.08           C  
ANISOU 2082  CG  LYS A 250     3301   3662   4088     96   -479   -429       C  
ATOM   2083  CD  LYS A 250       8.938  19.247  -2.267  1.00 30.91           C  
ANISOU 2083  CD  LYS A 250     3565   3877   4302    134   -528   -476       C  
ATOM   2084  CE  LYS A 250       9.533  17.882  -1.989  1.00 29.59           C  
ANISOU 2084  CE  LYS A 250     3368   3667   4209     92   -523   -464       C  
ATOM   2085  NZ  LYS A 250       8.496  16.800  -2.043  1.00 27.95           N1+
ANISOU 2085  NZ  LYS A 250     3073   3415   4134     73   -567   -513       N1+
ATOM   2086  N   VAL A 251       9.591  22.982   1.101  1.00 17.57           N  
ANISOU 2086  N   VAL A 251     1957   2295   2425     70   -320   -271       N  
ATOM   2087  CA  VAL A 251      10.649  22.907   2.109  1.00 17.42           C  
ANISOU 2087  CA  VAL A 251     1955   2278   2385     31   -263   -208       C  
ATOM   2088  C   VAL A 251      10.260  23.458   3.467  1.00 20.91           C  
ANISOU 2088  C   VAL A 251     2373   2745   2827      3   -214   -165       C  
ATOM   2089  O   VAL A 251      10.597  22.832   4.480  1.00 21.49           O  
ANISOU 2089  O   VAL A 251     2424   2813   2927    -37   -178   -119       O  
ATOM   2090  CB  VAL A 251      11.922  23.578   1.576  1.00 19.93           C  
ANISOU 2090  CB  VAL A 251     2349   2605   2620     56   -252   -199       C  
ATOM   2091  CG1 VAL A 251      13.079  23.452   2.577  1.00 20.41           C  
ANISOU 2091  CG1 VAL A 251     2424   2667   2665     20   -203   -144       C  
ATOM   2092  CG2 VAL A 251      12.345  22.993   0.219  1.00 20.98           C  
ANISOU 2092  CG2 VAL A 251     2509   2719   2744     90   -296   -241       C  
ATOM   2093  N   VAL A 252       9.552  24.613   3.517  1.00 16.25           N  
ANISOU 2093  N   VAL A 252     1787   2182   2205     27   -213   -179       N  
ATOM   2094  CA  VAL A 252       9.199  25.223   4.818  1.00 14.64           C  
ANISOU 2094  CA  VAL A 252     1562   2007   1993      6   -166   -143       C  
ATOM   2095  C   VAL A 252       7.731  25.591   4.996  1.00 17.65           C  
ANISOU 2095  C   VAL A 252     1890   2403   2411     14   -174   -169       C  
ATOM   2096  O   VAL A 252       7.437  26.645   5.546  1.00 16.72           O  
ANISOU 2096  O   VAL A 252     1780   2316   2258     26   -153   -163       O  
ATOM   2097  CB  VAL A 252      10.136  26.421   5.110  1.00 15.91           C  
ANISOU 2097  CB  VAL A 252     1783   2190   2071     21   -140   -122       C  
ATOM   2098  CG1 VAL A 252      11.574  25.948   5.368  1.00 16.07           C  
ANISOU 2098  CG1 VAL A 252     1836   2199   2071      1   -118    -87       C  
ATOM   2099  CG2 VAL A 252      10.090  27.449   3.969  1.00 16.28           C  
ANISOU 2099  CG2 VAL A 252     1877   2238   2071     70   -171   -158       C  
ATOM   2100  N   PRO A 253       6.746  24.733   4.620  1.00 16.77           N  
ANISOU 2100  N   PRO A 253     1719   2270   2382      8   -204   -202       N  
ATOM   2101  CA  PRO A 253       5.359  25.085   4.937  1.00 19.00           C  
ANISOU 2101  CA  PRO A 253     1943   2568   2710     11   -204   -226       C  
ATOM   2102  C   PRO A 253       5.174  25.082   6.461  1.00 23.33           C  
ANISOU 2102  C   PRO A 253     2456   3139   3268    -27   -134   -170       C  
ATOM   2103  O   PRO A 253       5.873  24.311   7.139  1.00 21.53           O  
ANISOU 2103  O   PRO A 253     2230   2902   3048    -62    -97   -119       O  
ATOM   2104  CB  PRO A 253       4.544  23.974   4.269  1.00 19.72           C  
ANISOU 2104  CB  PRO A 253     1971   2622   2901      5   -248   -271       C  
ATOM   2105  CG  PRO A 253       5.461  22.822   4.229  1.00 22.82           C  
ANISOU 2105  CG  PRO A 253     2373   2981   3316    -24   -243   -244       C  
ATOM   2106  CD  PRO A 253       6.868  23.355   4.126  1.00 18.98           C  
ANISOU 2106  CD  PRO A 253     1972   2509   2731    -11   -230   -214       C  
ATOM   2107  N   PRO A 254       4.356  25.972   7.051  1.00 22.31           N  
ANISOU 2107  N   PRO A 254     2303   3045   3128    -16   -112   -175       N  
ATOM   2108  CA  PRO A 254       3.426  26.939   6.453  1.00 22.75           C  
ANISOU 2108  CA  PRO A 254     2350   3114   3178     25   -151   -232       C  
ATOM   2109  C   PRO A 254       3.949  28.375   6.396  1.00 25.42           C  
ANISOU 2109  C   PRO A 254     2757   3480   3422     63   -152   -233       C  
ATOM   2110  O   PRO A 254       3.162  29.318   6.484  1.00 25.51           O  
ANISOU 2110  O   PRO A 254     2756   3514   3425     89   -159   -260       O  
ATOM   2111  CB  PRO A 254       2.218  26.812   7.392  1.00 25.38           C  
ANISOU 2111  CB  PRO A 254     2601   3465   3576      3   -111   -227       C  
ATOM   2112  CG  PRO A 254       2.860  26.675   8.753  1.00 28.78           C  
ANISOU 2112  CG  PRO A 254     3042   3920   3973    -29    -37   -155       C  
ATOM   2113  CD  PRO A 254       4.183  25.936   8.522  1.00 23.79           C  
ANISOU 2113  CD  PRO A 254     2460   3261   3317    -46    -42   -122       C  
ATOM   2114  N   LEU A 255       5.256  28.559   6.230  1.00 19.13           N  
ANISOU 2114  N   LEU A 255     2029   2677   2562     65   -147   -207       N  
ATOM   2115  CA  LEU A 255       5.851  29.871   6.160  1.00 17.79           C  
ANISOU 2115  CA  LEU A 255     1921   2522   2316     95   -144   -206       C  
ATOM   2116  C   LEU A 255       5.262  30.667   4.988  1.00 19.35           C  
ANISOU 2116  C   LEU A 255     2141   2712   2498    148   -198   -256       C  
ATOM   2117  O   LEU A 255       5.163  30.171   3.861  1.00 17.27           O  
ANISOU 2117  O   LEU A 255     1887   2426   2248    169   -245   -285       O  
ATOM   2118  CB  LEU A 255       7.374  29.744   6.101  1.00 16.77           C  
ANISOU 2118  CB  LEU A 255     1852   2381   2141     84   -129   -172       C  
ATOM   2119  CG  LEU A 255       8.180  31.023   6.293  1.00 17.10           C  
ANISOU 2119  CG  LEU A 255     1950   2433   2116    103   -112   -161       C  
ATOM   2120  CD1 LEU A 255       7.979  31.657   7.699  1.00 17.53           C  
ANISOU 2120  CD1 LEU A 255     1982   2523   2157     93    -71   -145       C  
ATOM   2121  CD2 LEU A 255       9.638  30.768   6.020  1.00 15.18           C  
ANISOU 2121  CD2 LEU A 255     1756   2168   1842     93   -103   -136       C  
ATOM   2122  N   ASP A 256       4.881  31.915   5.284  1.00 16.06           N  
ANISOU 2122  N   ASP A 256     1734   2316   2050    175   -193   -266       N  
ATOM   2123  CA  ASP A 256       4.314  32.794   4.276  1.00 15.39           C  
ANISOU 2123  CA  ASP A 256     1675   2225   1946    230   -242   -307       C  
ATOM   2124  C   ASP A 256       5.353  33.231   3.207  1.00 15.77           C  
ANISOU 2124  C   ASP A 256     1809   2250   1934    262   -260   -298       C  
ATOM   2125  O   ASP A 256       6.566  33.006   3.354  1.00 15.00           O  
ANISOU 2125  O   ASP A 256     1748   2142   1810    238   -229   -262       O  
ATOM   2126  CB  ASP A 256       3.612  33.996   4.943  1.00 16.38           C  
ANISOU 2126  CB  ASP A 256     1786   2376   2063    250   -230   -321       C  
ATOM   2127  CG  ASP A 256       4.534  35.039   5.586  1.00 17.97           C  
ANISOU 2127  CG  ASP A 256     2035   2584   2209    250   -192   -290       C  
ATOM   2128  OD1 ASP A 256       5.548  35.370   4.998  1.00 16.18           O  
ANISOU 2128  OD1 ASP A 256     1872   2334   1942    261   -194   -273       O  
ATOM   2129  OD2 ASP A 256       4.093  35.717   6.532  1.00 30.13           O1-
ANISOU 2129  OD2 ASP A 256     3548   4150   3750    250   -169   -295       O1-
ATOM   2130  N   GLU A 257       4.868  33.870   2.145  1.00 15.35           N  
ANISOU 2130  N   GLU A 257     1786   2187   1858    319   -307   -331       N  
ATOM   2131  CA  GLU A 257       5.736  34.260   1.042  1.00 14.63           C  
ANISOU 2131  CA  GLU A 257     1776   2074   1707    356   -320   -319       C  
ATOM   2132  C   GLU A 257       6.854  35.227   1.450  1.00 14.96           C  
ANISOU 2132  C   GLU A 257     1872   2108   1705    348   -271   -275       C  
ATOM   2133  O   GLU A 257       7.952  35.146   0.899  1.00 15.01           O  
ANISOU 2133  O   GLU A 257     1931   2095   1677    349   -255   -249       O  
ATOM   2134  CB  GLU A 257       4.907  34.801  -0.121  1.00 18.02           C  
ANISOU 2134  CB  GLU A 257     2231   2499   2116    428   -380   -360       C  
ATOM   2135  CG  GLU A 257       5.711  35.372  -1.275  1.00 22.78           C  
ANISOU 2135  CG  GLU A 257     2925   3082   2647    477   -387   -341       C  
ATOM   2136  CD  GLU A 257       6.851  34.553  -1.855  1.00 31.65           C  
ANISOU 2136  CD  GLU A 257     4087   4193   3747    465   -372   -318       C  
ATOM   2137  OE1 GLU A 257       6.804  33.300  -1.802  1.00 24.91           O  
ANISOU 2137  OE1 GLU A 257     3190   3343   2933    435   -385   -335       O  
ATOM   2138  OE2 GLU A 257       7.825  35.184  -2.324  1.00 31.30           O1-
ANISOU 2138  OE2 GLU A 257     4112   4133   3648    482   -343   -281       O1-
ATOM   2139  N   ASP A 258       6.562  36.128   2.387  1.00 14.02           N  
ANISOU 2139  N   ASP A 258     1735   2002   1591    341   -248   -272       N  
ATOM   2140  CA  ASP A 258       7.640  37.020   2.840  1.00 14.05           C  
ANISOU 2140  CA  ASP A 258     1781   1993   1565    331   -205   -238       C  
ATOM   2141  C   ASP A 258       8.756  36.215   3.527  1.00 14.42           C  
ANISOU 2141  C   ASP A 258     1819   2041   1617    276   -165   -207       C  
ATOM   2142  O   ASP A 258       9.933  36.440   3.253  1.00 14.06           O  
ANISOU 2142  O   ASP A 258     1821   1974   1549    271   -142   -181       O  
ATOM   2143  CB  ASP A 258       7.090  38.036   3.838  1.00 14.94           C  
ANISOU 2143  CB  ASP A 258     1867   2123   1688    333   -192   -250       C  
ATOM   2144  CG  ASP A 258       6.281  39.181   3.232  1.00 17.28           C  
ANISOU 2144  CG  ASP A 258     2185   2408   1973    391   -225   -274       C  
ATOM   2145  OD1 ASP A 258       6.598  39.599   2.117  1.00 17.91           O  
ANISOU 2145  OD1 ASP A 258     2324   2458   2021    430   -242   -264       O  
ATOM   2146  OD2 ASP A 258       5.376  39.677   3.906  1.00 19.75           O1-
ANISOU 2146  OD2 ASP A 258     2456   2742   2306    399   -231   -300       O1-
ATOM   2147  N   GLY A 259       8.372  35.255   4.367  1.00 12.52           N  
ANISOU 2147  N   GLY A 259     1521   1825   1412    239   -157   -208       N  
ATOM   2148  CA  GLY A 259       9.366  34.422   5.038  1.00 12.22           C  
ANISOU 2148  CA  GLY A 259     1475   1789   1379    193   -124   -178       C  
ATOM   2149  C   GLY A 259      10.115  33.548   4.061  1.00 13.84           C  
ANISOU 2149  C   GLY A 259     1710   1969   1579    190   -135   -168       C  
ATOM   2150  O   GLY A 259      11.345  33.388   4.167  1.00 13.04           O  
ANISOU 2150  O   GLY A 259     1636   1855   1463    170   -110   -143       O  
ATOM   2151  N   ARG A 260       9.395  32.976   3.059  1.00 13.15           N  
ANISOU 2151  N   ARG A 260     1617   1875   1504    213   -177   -195       N  
ATOM   2152  CA  ARG A 260      10.076  32.138   2.064  1.00 12.91           C  
ANISOU 2152  CA  ARG A 260     1615   1823   1465    218   -192   -194       C  
ATOM   2153  C   ARG A 260      11.034  32.985   1.217  1.00 13.10           C  
ANISOU 2153  C   ARG A 260     1714   1828   1436    250   -180   -178       C  
ATOM   2154  O   ARG A 260      12.140  32.521   0.896  1.00 13.06           O  
ANISOU 2154  O   ARG A 260     1735   1808   1417    237   -162   -159       O  
ATOM   2155  CB  ARG A 260       9.069  31.379   1.196  1.00 14.68           C  
ANISOU 2155  CB  ARG A 260     1815   2046   1717    243   -246   -235       C  
ATOM   2156  CG  ARG A 260       8.281  30.373   2.051  1.00 17.29           C  
ANISOU 2156  CG  ARG A 260     2066   2386   2118    202   -247   -244       C  
ATOM   2157  CD  ARG A 260       7.391  29.362   1.313  1.00 22.01           C  
ANISOU 2157  CD  ARG A 260     2622   2974   2767    213   -299   -289       C  
ATOM   2158  NE  ARG A 260       6.752  29.912   0.123  1.00 27.23           N  
ANISOU 2158  NE  ARG A 260     3310   3634   3402    277   -354   -334       N  
ATOM   2159  CZ  ARG A 260       5.509  30.396   0.054  1.00 33.70           C  
ANISOU 2159  CZ  ARG A 260     4097   4465   4243    306   -386   -372       C  
ATOM   2160  NH1 ARG A 260       4.751  30.475   1.145  1.00 30.04           N1+
ANISOU 2160  NH1 ARG A 260     3570   4016   3828    273   -362   -368       N1+
ATOM   2161  NH2 ARG A 260       5.028  30.840  -1.099  1.00 34.23           N  
ANISOU 2161  NH2 ARG A 260     4195   4530   4280    371   -442   -413       N  
ATOM   2162  N   SER A 261      10.630  34.221   0.848  1.00 13.03           N  
ANISOU 2162  N   SER A 261     1737   1816   1399    291   -187   -184       N  
ATOM   2163  CA  SER A 261      11.509  35.115   0.086  1.00 13.48           C  
ANISOU 2163  CA  SER A 261     1863   1848   1409    321   -166   -160       C  
ATOM   2164  C   SER A 261      12.789  35.382   0.902  1.00 13.92           C  
ANISOU 2164  C   SER A 261     1925   1893   1472    278   -112   -127       C  
ATOM   2165  O   SER A 261      13.890  35.295   0.367  1.00 13.22           O  
ANISOU 2165  O   SER A 261     1874   1784   1366    276    -86   -105       O  
ATOM   2166  CB  SER A 261      10.785  36.431  -0.171  1.00 17.89           C  
ANISOU 2166  CB  SER A 261     2447   2403   1950    367   -179   -167       C  
ATOM   2167  OG  SER A 261      11.662  37.508  -0.485  1.00 19.91           O  
ANISOU 2167  OG  SER A 261     2759   2628   2177    383   -142   -134       O  
ATOM   2168  N   LEU A 262      12.635  35.740   2.176  1.00 12.81           N  
ANISOU 2168  N   LEU A 262     1745   1766   1356    248    -96   -127       N  
ATOM   2169  CA  LEU A 262      13.803  36.012   2.994  1.00 11.59           C  
ANISOU 2169  CA  LEU A 262     1592   1603   1209    214    -54   -106       C  
ATOM   2170  C   LEU A 262      14.695  34.773   3.121  1.00 11.91           C  
ANISOU 2170  C   LEU A 262     1621   1643   1260    178    -43    -93       C  
ATOM   2171  O   LEU A 262      15.913  34.869   2.938  1.00 11.39           O  
ANISOU 2171  O   LEU A 262     1581   1556   1191    168    -15    -76       O  
ATOM   2172  CB  LEU A 262      13.359  36.520   4.361  1.00 11.21           C  
ANISOU 2172  CB  LEU A 262     1502   1579   1179    197    -47   -116       C  
ATOM   2173  CG  LEU A 262      14.500  36.690   5.375  1.00 12.56           C  
ANISOU 2173  CG  LEU A 262     1665   1747   1359    164    -15   -105       C  
ATOM   2174  CD1 LEU A 262      15.552  37.668   4.909  1.00 13.77           C  
ANISOU 2174  CD1 LEU A 262     1861   1860   1512    173     10    -94       C  
ATOM   2175  CD2 LEU A 262      13.935  37.158   6.719  1.00 13.52           C  
ANISOU 2175  CD2 LEU A 262     1747   1902   1489    158    -13   -121       C  
ATOM   2176  N   LEU A 263      14.096  33.622   3.425  1.00 11.43           N  
ANISOU 2176  N   LEU A 263     1519   1604   1219    160    -64   -102       N  
ATOM   2177  CA  LEU A 263      14.899  32.406   3.558  1.00 10.65           C  
ANISOU 2177  CA  LEU A 263     1409   1502   1136    128    -57    -90       C  
ATOM   2178  C   LEU A 263      15.653  32.093   2.287  1.00 12.35           C  
ANISOU 2178  C   LEU A 263     1668   1693   1333    146    -58    -87       C  
ATOM   2179  O   LEU A 263      16.854  31.738   2.346  1.00 12.10           O  
ANISOU 2179  O   LEU A 263     1646   1648   1303    126    -34    -72       O  
ATOM   2180  CB  LEU A 263      13.996  31.245   3.905  1.00 11.38           C  
ANISOU 2180  CB  LEU A 263     1452   1611   1260    111    -79    -98       C  
ATOM   2181  CG  LEU A 263      14.739  29.907   4.118  1.00 12.28           C  
ANISOU 2181  CG  LEU A 263     1551   1717   1398     78    -75    -83       C  
ATOM   2182  CD1 LEU A 263      15.775  29.974   5.251  1.00 12.65           C  
ANISOU 2182  CD1 LEU A 263     1594   1769   1442     49    -42    -58       C  
ATOM   2183  CD2 LEU A 263      13.768  28.771   4.345  1.00 14.81           C  
ANISOU 2183  CD2 LEU A 263     1821   2044   1762     62    -96    -90       C  
ATOM   2184  N   SER A 264      14.996  32.215   1.136  1.00 11.88           N  
ANISOU 2184  N   SER A 264     1633   1628   1251    188    -86   -104       N  
ATOM   2185  CA ASER A 264      15.678  31.907  -0.117  0.50 12.28           C  
ANISOU 2185  CA ASER A 264     1728   1662   1274    215    -86   -103       C  
ATOM   2186  CA BSER A 264      15.664  31.908  -0.122  0.50 12.27           C  
ANISOU 2186  CA BSER A 264     1727   1661   1273    215    -86   -103       C  
ATOM   2187  C   SER A 264      16.894  32.798  -0.312  1.00 13.39           C  
ANISOU 2187  C   SER A 264     1913   1781   1394    217    -37    -75       C  
ATOM   2188  O   SER A 264      17.937  32.343  -0.805  1.00 15.18           O  
ANISOU 2188  O   SER A 264     2160   1995   1614    212    -16    -65       O  
ATOM   2189  CB ASER A 264      14.721  32.085  -1.280  0.50 15.17           C  
ANISOU 2189  CB ASER A 264     2120   2032   1610    271   -126   -128       C  
ATOM   2190  CB BSER A 264      14.676  32.045  -1.274  0.50 14.85           C  
ANISOU 2190  CB BSER A 264     2078   1993   1571    271   -128   -129       C  
ATOM   2191  OG ASER A 264      15.434  31.821  -2.479  0.50 16.99           O  
ANISOU 2191  OG ASER A 264     2400   2252   1803    303   -122   -125       O  
ATOM   2192  OG BSER A 264      14.297  33.378  -1.575  0.50 15.17           O  
ANISOU 2192  OG BSER A 264     2155   2029   1582    308   -123   -122       O  
ATOM   2193  N   GLN A 265      16.815  34.071   0.098  1.00 12.10           N  
ANISOU 2193  N   GLN A 265     1760   1610   1228    222    -17    -63       N  
ATOM   2194  CA  GLN A 265      17.935  34.996  -0.036  1.00 11.60           C  
ANISOU 2194  CA  GLN A 265     1730   1517   1160    220     32    -38       C  
ATOM   2195  C   GLN A 265      19.029  34.715   0.983  1.00 12.21           C  
ANISOU 2195  C   GLN A 265     1776   1589   1274    171     60    -32       C  
ATOM   2196  O   GLN A 265      20.196  34.990   0.692  1.00 12.82           O  
ANISOU 2196  O   GLN A 265     1873   1641   1358    164     99    -16       O  
ATOM   2197  CB  GLN A 265      17.465  36.426   0.072  1.00 12.44           C  
ANISOU 2197  CB  GLN A 265     1855   1610   1263    243     40    -32       C  
ATOM   2198  CG  GLN A 265      16.524  36.797  -1.075  1.00 15.44           C  
ANISOU 2198  CG  GLN A 265     2275   1990   1600    302     14    -34       C  
ATOM   2199  CD  GLN A 265      15.950  38.172  -0.896  1.00 19.48           C  
ANISOU 2199  CD  GLN A 265     2802   2488   2114    326     15    -30       C  
ATOM   2200  NE2 GLN A 265      14.651  38.273  -0.607  1.00 19.60           N  
ANISOU 2200  NE2 GLN A 265     2791   2525   2129    343    -29    -57       N  
ATOM   2201  OE1 GLN A 265      16.663  39.159  -0.938  1.00 27.83           O  
ANISOU 2201  OE1 GLN A 265     3885   3510   3180    326     57     -5       O  
ATOM   2202  N   MET A 266      18.696  34.136   2.126  1.00 10.27           N  
ANISOU 2202  N   MET A 266     1483   1369   1052    140     41    -44       N  
ATOM   2203  CA  MET A 266      19.708  33.733   3.104  1.00  9.45           C  
ANISOU 2203  CA  MET A 266     1350   1266    976    100     59    -41       C  
ATOM   2204  C   MET A 266      20.426  32.455   2.694  1.00 11.45           C  
ANISOU 2204  C   MET A 266     1601   1515   1234     87     57    -37       C  
ATOM   2205  O   MET A 266      21.524  32.187   3.181  1.00 10.99           O  
ANISOU 2205  O   MET A 266     1531   1448   1196     62     75    -34       O  
ATOM   2206  CB  MET A 266      19.024  33.495   4.451  1.00 10.42           C  
ANISOU 2206  CB  MET A 266     1427   1420   1110     80     40    -49       C  
ATOM   2207  CG  MET A 266      18.407  34.770   5.039  1.00  9.66           C  
ANISOU 2207  CG  MET A 266     1328   1332   1013     93     42    -59       C  
ATOM   2208  SD  MET A 266      17.565  34.491   6.627  1.00 11.57           S  
ANISOU 2208  SD  MET A 266     1518   1620   1260     77     28    -69       S  
ATOM   2209  CE  MET A 266      19.001  34.476   7.752  1.00 12.05           C  
ANISOU 2209  CE  MET A 266     1565   1681   1334     52     46    -69       C  
ATOM   2210  N   LEU A 267      19.805  31.681   1.765  1.00 10.51           N  
ANISOU 2210  N   LEU A 267     1493   1401   1098    107     31    -44       N  
ATOM   2211  CA  LEU A 267      20.348  30.407   1.295  1.00 10.40           C  
ANISOU 2211  CA  LEU A 267     1476   1384   1092     99     23    -48       C  
ATOM   2212  C   LEU A 267      20.846  30.437  -0.139  1.00 12.93           C  
ANISOU 2212  C   LEU A 267     1842   1688   1382    133     36    -49       C  
ATOM   2213  O   LEU A 267      21.037  29.384  -0.745  1.00 12.12           O  
ANISOU 2213  O   LEU A 267     1739   1585   1278    139     19    -61       O  
ATOM   2214  CB  LEU A 267      19.359  29.281   1.514  1.00 10.87           C  
ANISOU 2214  CB  LEU A 267     1501   1460   1170     91    -19    -62       C  
ATOM   2215  CG  LEU A 267      18.946  29.016   2.983  1.00 11.38           C  
ANISOU 2215  CG  LEU A 267     1519   1543   1264     57    -23    -54       C  
ATOM   2216  CD1 LEU A 267      17.982  27.837   3.031  1.00 13.25           C  
ANISOU 2216  CD1 LEU A 267     1719   1786   1528     49    -57    -63       C  
ATOM   2217  CD2 LEU A 267      20.153  28.680   3.874  1.00 11.77           C  
ANISOU 2217  CD2 LEU A 267     1555   1587   1329     26     -2    -39       C  
ATOM   2218  N   HIS A 268      21.110  31.639  -0.679  1.00 12.31           N  
ANISOU 2218  N   HIS A 268     1804   1595   1280    157     68    -34       N  
ATOM   2219  CA  HIS A 268      21.707  31.705  -2.004  1.00 12.65           C  
ANISOU 2219  CA  HIS A 268     1894   1624   1288    192     94    -25       C  
ATOM   2220  C   HIS A 268      23.058  31.028  -1.940  1.00 12.00           C  
ANISOU 2220  C   HIS A 268     1800   1530   1230    165    122    -23       C  
ATOM   2221  O   HIS A 268      23.810  31.186  -0.990  1.00 12.41           O  
ANISOU 2221  O   HIS A 268     1822   1571   1321    127    143    -18       O  
ATOM   2222  CB  HIS A 268      21.920  33.156  -2.473  1.00 16.13           C  
ANISOU 2222  CB  HIS A 268     2379   2042   1709    217    137      2       C  
ATOM   2223  CG  HIS A 268      20.705  33.831  -3.053  1.00 20.63           C  
ANISOU 2223  CG  HIS A 268     2980   2620   2238    264    111      2       C  
ATOM   2224  CD2 HIS A 268      20.274  35.107  -2.882  1.00 23.49           C  
ANISOU 2224  CD2 HIS A 268     3359   2968   2599    278    123     17       C  
ATOM   2225  ND1 HIS A 268      19.898  33.211  -3.999  1.00 24.83           N  
ANISOU 2225  ND1 HIS A 268     3533   3172   2728    309     68    -18       N  
ATOM   2226  CE1 HIS A 268      18.957  34.102  -4.301  1.00 23.45           C  
ANISOU 2226  CE1 HIS A 268     3384   2998   2526    348     52    -15       C  
ATOM   2227  NE2 HIS A 268      19.155  35.260  -3.673  1.00 23.89           N  
ANISOU 2227  NE2 HIS A 268     3440   3033   2604    331     85      8       N  
ATOM   2228  N   TYR A 269      23.398  30.299  -3.006  1.00 12.24           N  
ANISOU 2228  N   TYR A 269     1854   1562   1234    191    123    -31       N  
ATOM   2229  CA  TYR A 269      24.684  29.606  -3.065  1.00 11.74           C  
ANISOU 2229  CA  TYR A 269     1779   1488   1193    172    149    -33       C  
ATOM   2230  C   TYR A 269      25.849  30.570  -3.122  1.00 12.12           C  
ANISOU 2230  C   TYR A 269     1841   1509   1254    162    218     -7       C  
ATOM   2231  O   TYR A 269      26.785  30.441  -2.339  1.00 12.39           O  
ANISOU 2231  O   TYR A 269     1840   1530   1336    123    236     -9       O  
ATOM   2232  CB  TYR A 269      24.752  28.730  -4.312  1.00 11.81           C  
ANISOU 2232  CB  TYR A 269     1815   1507   1165    211    137    -51       C  
ATOM   2233  CG  TYR A 269      24.214  27.352  -4.095  1.00 11.10           C  
ANISOU 2233  CG  TYR A 269     1690   1430   1096    202     76    -84       C  
ATOM   2234  CD1 TYR A 269      24.798  26.500  -3.164  1.00 11.95           C  
ANISOU 2234  CD1 TYR A 269     1751   1531   1258    156     67    -90       C  
ATOM   2235  CD2 TYR A 269      23.149  26.879  -4.839  1.00 11.76           C  
ANISOU 2235  CD2 TYR A 269     1787   1531   1152    242     25   -112       C  
ATOM   2236  CE1 TYR A 269      24.348  25.202  -2.994  1.00 11.28           C  
ANISOU 2236  CE1 TYR A 269     1635   1450   1201    147     16   -116       C  
ATOM   2237  CE2 TYR A 269      22.687  25.578  -4.685  1.00 11.78           C  
ANISOU 2237  CE2 TYR A 269     1751   1536   1188    231    -29   -145       C  
ATOM   2238  CZ  TYR A 269      23.299  24.745  -3.763  1.00 11.23           C  
ANISOU 2238  CZ  TYR A 269     1637   1454   1175    182    -31   -144       C  
ATOM   2239  OH  TYR A 269      22.856  23.477  -3.570  1.00 12.90           O  
ANISOU 2239  OH  TYR A 269     1812   1662   1428    170    -80   -170       O  
ATOM   2240  N   ASP A 270      25.775  31.580  -4.011  1.00 12.82           N  
ANISOU 2240  N   ASP A 270     1978   1586   1305    199    256     18       N  
ATOM   2241  CA  ASP A 270      26.887  32.509  -4.180  1.00 13.69           C  
ANISOU 2241  CA  ASP A 270     2100   1663   1437    191    330     46       C  
ATOM   2242  C   ASP A 270      26.929  33.429  -2.957  1.00 14.03           C  
ANISOU 2242  C   ASP A 270     2110   1687   1535    152    335     50       C  
ATOM   2243  O   ASP A 270      25.982  34.207  -2.727  1.00 13.55           O  
ANISOU 2243  O   ASP A 270     2060   1627   1461    164    317     56       O  
ATOM   2244  CB  ASP A 270      26.701  33.308  -5.474  1.00 15.74           C  
ANISOU 2244  CB  ASP A 270     2426   1914   1639    245    372     80       C  
ATOM   2245  CG  ASP A 270      27.827  34.264  -5.787  1.00 17.95           C  
ANISOU 2245  CG  ASP A 270     2722   2154   1946    239    460    117       C  
ATOM   2246  OD1 ASP A 270      28.710  34.456  -4.912  1.00 16.28           O  
ANISOU 2246  OD1 ASP A 270     2461   1916   1807    189    483    111       O  
ATOM   2247  OD2 ASP A 270      27.904  34.714  -6.945  1.00 21.10           O1-
ANISOU 2247  OD2 ASP A 270     3178   2546   2295    286    506    151       O1-
ATOM   2248  N   PRO A 271      28.008  33.367  -2.153  1.00 13.02           N  
ANISOU 2248  N   PRO A 271     1939   1541   1469    109    356     40       N  
ATOM   2249  CA  PRO A 271      28.051  34.204  -0.937  1.00 15.35           C  
ANISOU 2249  CA  PRO A 271     2198   1820   1813     77    351     32       C  
ATOM   2250  C   PRO A 271      27.896  35.669  -1.276  1.00 18.42           C  
ANISOU 2250  C   PRO A 271     2615   2175   2207     93    393     59       C  
ATOM   2251  O   PRO A 271      27.398  36.433  -0.451  1.00 18.69           O  
ANISOU 2251  O   PRO A 271     2633   2205   2263     83    374     51       O  
ATOM   2252  CB  PRO A 271      29.417  33.908  -0.323  1.00 17.77           C  
ANISOU 2252  CB  PRO A 271     2460   2110   2183     41    372     14       C  
ATOM   2253  CG  PRO A 271      29.920  32.696  -1.024  1.00 19.59           C  
ANISOU 2253  CG  PRO A 271     2695   2353   2395     48    374      9       C  
ATOM   2254  CD  PRO A 271      29.190  32.479  -2.277  1.00 14.93           C  
ANISOU 2254  CD  PRO A 271     2157   1778   1736     92    375     27       C  
ATOM   2255  N   ASN A 272      28.267  36.072  -2.494  1.00 16.66           N  
ANISOU 2255  N   ASN A 272     2438   1930   1963    121    449     92       N  
ATOM   2256  CA  ASN A 272      28.137  37.473  -2.884  1.00 17.78           C  
ANISOU 2256  CA  ASN A 272     2611   2032   2112    139    494    127       C  
ATOM   2257  C   ASN A 272      26.690  37.864  -3.166  1.00 19.90           C  
ANISOU 2257  C   ASN A 272     2920   2321   2322    179    454    136       C  
ATOM   2258  O   ASN A 272      26.363  39.077  -3.148  1.00 23.67           O  
ANISOU 2258  O   ASN A 272     3414   2766   2813    190    472    156       O  
ATOM   2259  CB  ASN A 272      29.036  37.730  -4.100  1.00 20.75           C  
ANISOU 2259  CB  ASN A 272     3025   2378   2481    159    577    167       C  
ATOM   2260  CG  ASN A 272      30.479  37.614  -3.697  1.00 32.05           C  
ANISOU 2260  CG  ASN A 272     4406   3779   3991    115    622    155       C  
ATOM   2261  ND2 ASN A 272      31.077  36.438  -3.903  1.00 31.68           N  
ANISOU 2261  ND2 ASN A 272     4344   3757   3934    109    618    136       N  
ATOM   2262  OD1 ASN A 272      31.016  38.495  -3.030  1.00 34.44           O  
ANISOU 2262  OD1 ASN A 272     4674   4039   4372     83    648    151       O  
ATOM   2263  N   LYS A 273      25.820  36.905  -3.454  1.00 18.30           N  
ANISOU 2263  N   LYS A 273     2729   2164   2060    203    398    119       N  
ATOM   2264  CA  LYS A 273      24.405  37.166  -3.722  1.00 19.13           C  
ANISOU 2264  CA  LYS A 273     2864   2291   2115    243    351    118       C  
ATOM   2265  C   LYS A 273      23.639  37.050  -2.421  1.00 18.70           C  
ANISOU 2265  C   LYS A 273     2758   2258   2088    213    294     83       C  
ATOM   2266  O   LYS A 273      22.555  37.591  -2.309  1.00 18.15           O  
ANISOU 2266  O   LYS A 273     2698   2197   2001    235    262     80       O  
ATOM   2267  CB  LYS A 273      23.790  36.165  -4.732  1.00 21.74           C  
ANISOU 2267  CB  LYS A 273     3227   2660   2374    288    315    108       C  
ATOM   2268  CG  LYS A 273      24.381  36.201  -6.147  1.00 21.57           C  
ANISOU 2268  CG  LYS A 273     3265   2629   2301    334    367    141       C  
ATOM   2269  CD  LYS A 273      23.668  35.247  -7.111  1.00 26.90           C  
ANISOU 2269  CD  LYS A 273     3971   3345   2903    387    319    119       C  
ATOM   2270  CE  LYS A 273      24.206  35.301  -8.521  1.00 32.56           C  
ANISOU 2270  CE  LYS A 273     4753   4061   3555    443    369    150       C  
ATOM   2271  NZ  LYS A 273      25.544  34.656  -8.637  1.00 26.42           N1+
ANISOU 2271  NZ  LYS A 273     3958   3278   2803    415    420    151       N1+
ATOM   2272  N   ARG A 274      24.154  36.270  -1.451  1.00 14.34           N  
ANISOU 2272  N   ARG A 274     2154   1720   1576    168    278     58       N  
ATOM   2273  CA  ARG A 274      23.453  36.000  -0.203  1.00 13.28           C  
ANISOU 2273  CA  ARG A 274     1974   1613   1459    143    229     30       C  
ATOM   2274  C   ARG A 274      23.155  37.309   0.526  1.00 13.18           C  
ANISOU 2274  C   ARG A 274     1951   1582   1474    139    234     28       C  
ATOM   2275  O   ARG A 274      24.024  38.185   0.600  1.00 13.96           O  
ANISOU 2275  O   ARG A 274     2050   1640   1612    128    278     38       O  
ATOM   2276  CB  ARG A 274      24.309  35.015   0.625  1.00 12.93           C  
ANISOU 2276  CB  ARG A 274     1885   1580   1450    102    222     11       C  
ATOM   2277  CG  ARG A 274      23.520  34.247   1.670  1.00 13.57           C  
ANISOU 2277  CG  ARG A 274     1926   1698   1531     85    170    -10       C  
ATOM   2278  CD  ARG A 274      24.412  33.211   2.365  1.00 12.40           C  
ANISOU 2278  CD  ARG A 274     1743   1559   1412     52    164    -20       C  
ATOM   2279  NE  ARG A 274      24.933  32.219   1.412  1.00 11.56           N  
ANISOU 2279  NE  ARG A 274     1650   1447   1294     58    170    -17       N  
ATOM   2280  CZ  ARG A 274      26.115  31.603   1.519  1.00 10.34           C  
ANISOU 2280  CZ  ARG A 274     1480   1282   1167     39    186    -22       C  
ATOM   2281  NH1 ARG A 274      26.886  31.806   2.577  1.00 10.69           N1+
ANISOU 2281  NH1 ARG A 274     1490   1320   1251     11    191    -33       N1+
ATOM   2282  NH2 ARG A 274      26.547  30.809   0.548  1.00 11.36           N  
ANISOU 2282  NH2 ARG A 274     1625   1408   1283     51    194    -22       N  
ATOM   2283  N   ILE A 275      21.916  37.474   1.011  1.00 12.00           N  
ANISOU 2283  N   ILE A 275     1792   1459   1309    151    191     13       N  
ATOM   2284  CA  ILE A 275      21.519  38.706   1.665  1.00 11.78           C  
ANISOU 2284  CA  ILE A 275     1755   1417   1303    153    191      6       C  
ATOM   2285  C   ILE A 275      22.423  39.002   2.882  1.00 11.61           C  
ANISOU 2285  C   ILE A 275     1690   1385   1337    115    203    -14       C  
ATOM   2286  O   ILE A 275      22.850  38.083   3.598  1.00 12.50           O  
ANISOU 2286  O   ILE A 275     1768   1522   1458     88    189    -30       O  
ATOM   2287  CB  ILE A 275      20.025  38.651   2.048  1.00 13.15           C  
ANISOU 2287  CB  ILE A 275     1917   1629   1452    171    142    -13       C  
ATOM   2288  CG1 ILE A 275      19.436  40.037   2.372  1.00 13.61           C  
ANISOU 2288  CG1 ILE A 275     1979   1669   1523    190    140    -19       C  
ATOM   2289  CG2 ILE A 275      19.767  37.648   3.191  1.00 13.28           C  
ANISOU 2289  CG2 ILE A 275     1882   1688   1475    141    111    -36       C  
ATOM   2290  CD1 ILE A 275      17.901  40.058   2.407  1.00 15.33           C  
ANISOU 2290  CD1 ILE A 275     2192   1920   1713    218     96    -35       C  
ATOM   2291  N   SER A 276      22.721  40.281   3.123  1.00 11.76           N  
ANISOU 2291  N   SER A 276     1708   1365   1395    116    226    -16       N  
ATOM   2292  CA  SER A 276      23.484  40.660   4.312  1.00 12.02           C  
ANISOU 2292  CA  SER A 276     1696   1388   1483     87    227    -48       C  
ATOM   2293  C   SER A 276      22.526  40.744   5.496  1.00 12.14           C  
ANISOU 2293  C   SER A 276     1680   1448   1485     91    181    -80       C  
ATOM   2294  O   SER A 276      21.297  40.870   5.324  1.00 12.12           O  
ANISOU 2294  O   SER A 276     1691   1467   1446    115    158    -77       O  
ATOM   2295  CB  SER A 276      24.147  42.019   4.115  1.00 12.62           C  
ANISOU 2295  CB  SER A 276     1777   1399   1617     87    267    -44       C  
ATOM   2296  OG  SER A 276      23.157  43.025   4.028  1.00 14.69           O  
ANISOU 2296  OG  SER A 276     2059   1650   1872    116    256    -41       O  
ATOM   2297  N   ALA A 277      23.078  40.753   6.721  1.00 11.14           N  
ANISOU 2297  N   ALA A 277     1512   1334   1388     71    168   -115       N  
ATOM   2298  CA  ALA A 277      22.215  40.914   7.895  1.00 10.98           C  
ANISOU 2298  CA  ALA A 277     1463   1358   1350     80    131   -146       C  
ATOM   2299  C   ALA A 277      21.522  42.266   7.861  1.00 12.25           C  
ANISOU 2299  C   ALA A 277     1633   1496   1526    104    129   -158       C  
ATOM   2300  O   ALA A 277      20.323  42.354   8.175  1.00 12.28           O  
ANISOU 2300  O   ALA A 277     1634   1537   1497    124    104   -167       O  
ATOM   2301  CB  ALA A 277      23.049  40.792   9.165  1.00 12.10           C  
ANISOU 2301  CB  ALA A 277     1565   1517   1517     65    117   -183       C  
ATOM   2302  N   LYS A 278      22.258  43.325   7.474  1.00 13.08           N  
ANISOU 2302  N   LYS A 278     1682   1495   1791    -47    -55     76       N  
ATOM   2303  CA  LYS A 278      21.616  44.655   7.417  1.00 13.62           C  
ANISOU 2303  CA  LYS A 278     1860   1468   1846    -76    -50     38       C  
ATOM   2304  C   LYS A 278      20.461  44.701   6.418  1.00 15.90           C  
ANISOU 2304  C   LYS A 278     2211   1704   2126     25    -28     36       C  
ATOM   2305  O   LYS A 278      19.392  45.256   6.727  1.00 16.45           O  
ANISOU 2305  O   LYS A 278     2346   1723   2180     68    -32      5       O  
ATOM   2306  CB  LYS A 278      22.673  45.718   7.089  1.00 18.30           C  
ANISOU 2306  CB  LYS A 278     2473   2038   2441   -187    -27     62       C  
ATOM   2307  CG  LYS A 278      22.139  47.127   6.848  1.00 31.80           C  
ANISOU 2307  CG  LYS A 278     4328   3609   4143   -208      8     40       C  
ATOM   2308  CD  LYS A 278      23.256  48.173   6.818  1.00 45.47           C  
ANISOU 2308  CD  LYS A 278     6095   5306   5874   -367     37     50       C  
ATOM   2309  CE  LYS A 278      23.431  48.869   8.148  1.00 60.64           C  
ANISOU 2309  CE  LYS A 278     8070   7199   7771   -500     17    -24       C  
ATOM   2310  NZ  LYS A 278      22.219  49.629   8.567  1.00 68.48           N1+
ANISOU 2310  NZ  LYS A 278     9223   8043   8755   -435     47    -82       N1+
ATOM   2311  N   ALA A 279      20.651  44.127   5.226  1.00 13.72           N  
ANISOU 2311  N   ALA A 279     1907   1458   1847     67     -2     69       N  
ATOM   2312  CA  ALA A 279      19.567  44.128   4.251  1.00 13.96           C  
ANISOU 2312  CA  ALA A 279     1980   1482   1845    148      7     68       C  
ATOM   2313  C   ALA A 279      18.405  43.244   4.699  1.00 15.66           C  
ANISOU 2313  C   ALA A 279     2171   1737   2045    194    -22     23       C  
ATOM   2314  O   ALA A 279      17.241  43.586   4.476  1.00 16.62           O  
ANISOU 2314  O   ALA A 279     2315   1869   2133    249    -34     15       O  
ATOM   2315  CB  ALA A 279      20.077  43.735   2.857  1.00 15.21           C  
ANISOU 2315  CB  ALA A 279     2124   1674   1982    163     45    102       C  
ATOM   2316  N   ALA A 280      18.699  42.140   5.394  1.00 12.65           N  
ANISOU 2316  N   ALA A 280     1739   1384   1685    174    -29      4       N  
ATOM   2317  CA  ALA A 280      17.649  41.255   5.894  1.00 12.35           C  
ANISOU 2317  CA  ALA A 280     1684   1374   1633    192    -45    -36       C  
ATOM   2318  C   ALA A 280      16.768  41.960   6.905  1.00 13.73           C  
ANISOU 2318  C   ALA A 280     1875   1544   1800    203    -74    -58       C  
ATOM   2319  O   ALA A 280      15.570  41.746   6.926  1.00 13.57           O  
ANISOU 2319  O   ALA A 280     1843   1562   1750    234    -84    -82       O  
ATOM   2320  CB  ALA A 280      18.269  40.005   6.503  1.00 13.06           C  
ANISOU 2320  CB  ALA A 280     1739   1472   1753    177    -29    -31       C  
ATOM   2321  N   LEU A 281      17.351  42.870   7.720  1.00 13.10           N  
ANISOU 2321  N   LEU A 281     1821   1422   1733    171    -81    -55       N  
ATOM   2322  CA  LEU A 281      16.530  43.592   8.707  1.00 13.49           C  
ANISOU 2322  CA  LEU A 281     1907   1452   1766    188    -89    -89       C  
ATOM   2323  C   LEU A 281      15.486  44.462   8.050  1.00 15.76           C  
ANISOU 2323  C   LEU A 281     2240   1717   2030    272    -70    -81       C  
ATOM   2324  O   LEU A 281      14.448  44.741   8.674  1.00 16.66           O  
ANISOU 2324  O   LEU A 281     2361   1845   2124    327    -65   -103       O  
ATOM   2325  CB  LEU A 281      17.422  44.458   9.598  1.00 13.95           C  
ANISOU 2325  CB  LEU A 281     2008   1463   1828    112    -90   -104       C  
ATOM   2326  CG  LEU A 281      18.279  43.680  10.587  1.00 14.91           C  
ANISOU 2326  CG  LEU A 281     2065   1652   1950     42   -121   -101       C  
ATOM   2327  CD1 LEU A 281      19.342  44.595  11.206  1.00 17.55           C  
ANISOU 2327  CD1 LEU A 281     2424   1976   2269    -69   -131   -115       C  
ATOM   2328  CD2 LEU A 281      17.401  43.051  11.685  1.00 15.55           C  
ANISOU 2328  CD2 LEU A 281     2127   1777   2005     66   -135   -128       C  
ATOM   2329  N   ALA A 282      15.739  44.885   6.816  1.00 14.58           N  
ANISOU 2329  N   ALA A 282     2114   1547   1878    297    -53    -39       N  
ATOM   2330  CA  ALA A 282      14.822  45.746   6.058  1.00 15.76           C  
ANISOU 2330  CA  ALA A 282     2302   1691   1996    400    -33     -1       C  
ATOM   2331  C   ALA A 282      13.789  44.925   5.279  1.00 16.24           C  
ANISOU 2331  C   ALA A 282     2278   1884   2008    451    -60      9       C  
ATOM   2332  O   ALA A 282      12.924  45.496   4.614  1.00 17.52           O  
ANISOU 2332  O   ALA A 282     2437   2095   2126    548    -56     55       O  
ATOM   2333  CB  ALA A 282      15.616  46.617   5.086  1.00 17.91           C  
ANISOU 2333  CB  ALA A 282     2645   1887   2274    395      1     54       C  
ATOM   2334  N   HIS A 283      13.871  43.593   5.337  1.00 14.06           N  
ANISOU 2334  N   HIS A 283     1938   1673   1731    383    -84    -31       N  
ATOM   2335  CA  HIS A 283      12.973  42.784   4.559  1.00 12.68           C  
ANISOU 2335  CA  HIS A 283     1698   1621   1499    385   -105    -41       C  
ATOM   2336  C   HIS A 283      11.511  42.962   5.013  1.00 15.10           C  
ANISOU 2336  C   HIS A 283     1944   2028   1766    446   -122    -42       C  
ATOM   2337  O   HIS A 283      11.235  43.030   6.218  1.00 14.80           O  
ANISOU 2337  O   HIS A 283     1903   1965   1755    450   -115    -65       O  
ATOM   2338  CB  HIS A 283      13.407  41.312   4.661  1.00 12.46           C  
ANISOU 2338  CB  HIS A 283     1650   1599   1487    289   -102    -92       C  
ATOM   2339  CG  HIS A 283      12.742  40.435   3.653  1.00 13.08           C  
ANISOU 2339  CG  HIS A 283     1693   1780   1497    248   -110   -122       C  
ATOM   2340  CD2 HIS A 283      13.197  39.995   2.460  1.00 14.09           C  
ANISOU 2340  CD2 HIS A 283     1844   1923   1587    215    -94   -133       C  
ATOM   2341  ND1 HIS A 283      11.448  39.986   3.836  1.00 14.36           N  
ANISOU 2341  ND1 HIS A 283     1789   2059   1610    223   -136   -152       N  
ATOM   2342  CE1 HIS A 283      11.146  39.288   2.752  1.00 14.65           C  
ANISOU 2342  CE1 HIS A 283     1811   2180   1574    158   -141   -186       C  
ATOM   2343  NE2 HIS A 283      12.177  39.235   1.913  1.00 15.02           N  
ANISOU 2343  NE2 HIS A 283     1920   2162   1624    154   -113   -181       N  
ATOM   2344  N   PRO A 284      10.539  42.927   4.073  1.00 14.34           N  
ANISOU 2344  N   PRO A 284     1780   2076   1592    484   -146    -16       N  
ATOM   2345  CA  PRO A 284       9.115  43.027   4.476  1.00 14.97           C  
ANISOU 2345  CA  PRO A 284     1765   2296   1626    544   -163     -5       C  
ATOM   2346  C   PRO A 284       8.628  41.957   5.462  1.00 15.83           C  
ANISOU 2346  C   PRO A 284     1818   2452   1747    448   -168    -72       C  
ATOM   2347  O   PRO A 284       7.636  42.213   6.161  1.00 16.56           O  
ANISOU 2347  O   PRO A 284     1843   2629   1821    504   -164    -61       O  
ATOM   2348  CB  PRO A 284       8.367  42.916   3.151  1.00 17.27           C  
ANISOU 2348  CB  PRO A 284     1973   2775   1815    561   -201     33       C  
ATOM   2349  CG  PRO A 284       9.335  43.357   2.119  1.00 20.23           C  
ANISOU 2349  CG  PRO A 284     2431   3071   2186    576   -190     71       C  
ATOM   2350  CD  PRO A 284      10.696  42.918   2.603  1.00 15.17           C  
ANISOU 2350  CD  PRO A 284     1883   2247   1635    484   -159     16       C  
ATOM   2351  N   PHE A 285       9.328  40.815   5.600  1.00 13.73           N  
ANISOU 2351  N   PHE A 285     1585   2121   1512    320   -163   -130       N  
ATOM   2352  CA  PHE A 285       8.948  39.817   6.601  1.00 13.80           C  
ANISOU 2352  CA  PHE A 285     1565   2142   1536    232   -153   -177       C  
ATOM   2353  C   PHE A 285       8.898  40.455   8.006  1.00 14.63           C  
ANISOU 2353  C   PHE A 285     1684   2191   1682    297   -134   -165       C  
ATOM   2354  O   PHE A 285       8.124  40.005   8.867  1.00 16.18           O  
ANISOU 2354  O   PHE A 285     1828   2455   1866    266   -125   -183       O  
ATOM   2355  CB  PHE A 285       9.967  38.661   6.630  1.00 13.10           C  
ANISOU 2355  CB  PHE A 285     1547   1938   1492    128   -127   -216       C  
ATOM   2356  CG  PHE A 285       9.617  37.516   7.558  1.00 12.62           C  
ANISOU 2356  CG  PHE A 285     1480   1870   1445     35   -103   -249       C  
ATOM   2357  CD1 PHE A 285       8.425  36.802   7.399  1.00 14.56           C  
ANISOU 2357  CD1 PHE A 285     1658   2242   1633    -58   -106   -286       C  
ATOM   2358  CD2 PHE A 285      10.494  37.115   8.560  1.00 12.56           C  
ANISOU 2358  CD2 PHE A 285     1530   1743   1500     30    -74   -237       C  
ATOM   2359  CE1 PHE A 285       8.139  35.690   8.191  1.00 14.39           C  
ANISOU 2359  CE1 PHE A 285     1649   2193   1625   -163    -68   -313       C  
ATOM   2360  CE2 PHE A 285      10.199  36.003   9.364  1.00 14.40           C  
ANISOU 2360  CE2 PHE A 285     1771   1958   1742    -49    -40   -249       C  
ATOM   2361  CZ  PHE A 285       9.022  35.301   9.167  1.00 14.29           C  
ANISOU 2361  CZ  PHE A 285     1712   2039   1680   -148    -31   -289       C  
ATOM   2362  N   PHE A 286       9.711  41.502   8.262  1.00 13.28           N  
ANISOU 2362  N   PHE A 286     1592   1903   1550    369   -121   -142       N  
ATOM   2363  CA  PHE A 286       9.766  42.127   9.588  1.00 12.86           C  
ANISOU 2363  CA  PHE A 286     1578   1788   1519    408    -97   -151       C  
ATOM   2364  C   PHE A 286       8.847  43.309   9.754  1.00 17.27           C  
ANISOU 2364  C   PHE A 286     2131   2382   2050    541    -71   -126       C  
ATOM   2365  O   PHE A 286       8.892  43.954  10.811  1.00 17.20           O  
ANISOU 2365  O   PHE A 286     2179   2306   2050    578    -36   -147       O  
ATOM   2366  CB  PHE A 286      11.215  42.494   9.980  1.00 13.28           C  
ANISOU 2366  CB  PHE A 286     1726   1700   1620    372    -92   -157       C  
ATOM   2367  CG  PHE A 286      12.092  41.273  10.010  1.00 11.82           C  
ANISOU 2367  CG  PHE A 286     1533   1496   1463    275   -104   -163       C  
ATOM   2368  CD1 PHE A 286      11.887  40.272  10.954  1.00 13.17           C  
ANISOU 2368  CD1 PHE A 286     1675   1695   1632    223   -100   -176       C  
ATOM   2369  CD2 PHE A 286      13.120  41.124   9.100  1.00 12.14           C  
ANISOU 2369  CD2 PHE A 286     1597   1487   1527    251   -106   -145       C  
ATOM   2370  CE1 PHE A 286      12.689  39.125  10.972  1.00 11.86           C  
ANISOU 2370  CE1 PHE A 286     1517   1494   1494    162    -93   -163       C  
ATOM   2371  CE2 PHE A 286      13.931  39.990   9.123  1.00 12.10           C  
ANISOU 2371  CE2 PHE A 286     1589   1460   1550    194    -97   -140       C  
ATOM   2372  CZ  PHE A 286      13.713  38.991  10.055  1.00 11.83           C  
ANISOU 2372  CZ  PHE A 286     1537   1439   1519    158    -88   -146       C  
ATOM   2373  N   GLN A 287       7.941  43.547   8.783  1.00 16.71           N  
ANISOU 2373  N   GLN A 287     1986   2431   1934    619    -81    -81       N  
ATOM   2374  CA  GLN A 287       7.008  44.666   8.876  1.00 19.18           C  
ANISOU 2374  CA  GLN A 287     2281   2788   2217    787    -42    -33       C  
ATOM   2375  C   GLN A 287       6.186  44.617  10.159  1.00 21.69           C  
ANISOU 2375  C   GLN A 287     2555   3163   2523    818     -6    -61       C  
ATOM   2376  O   GLN A 287       5.920  45.666  10.755  1.00 24.13           O  
ANISOU 2376  O   GLN A 287     2928   3406   2834    948     58    -51       O  
ATOM   2377  CB  GLN A 287       6.104  44.687   7.637  1.00 20.86           C  
ANISOU 2377  CB  GLN A 287     2378   3185   2363    859    -73     37       C  
ATOM   2378  CG  GLN A 287       5.264  45.968   7.479  1.00 30.99           C  
ANISOU 2378  CG  GLN A 287     3648   4510   3616   1081    -25    126       C  
ATOM   2379  CD  GLN A 287       4.827  46.220   6.054  1.00 54.03           C  
ANISOU 2379  CD  GLN A 287     6488   7574   6466   1164    -60    221       C  
ATOM   2380  NE2 GLN A 287       3.882  47.137   5.887  1.00 51.65           N  
ANISOU 2380  NE2 GLN A 287     6133   7371   6123   1377    -21    323       N  
ATOM   2381  OE1 GLN A 287       5.349  45.641   5.088  1.00 49.70           O  
ANISOU 2381  OE1 GLN A 287     5935   7055   5896   1053   -115    212       O  
ATOM   2382  N   ASP A 288       5.733  43.442  10.546  1.00 17.01           N  
ANISOU 2382  N   ASP A 288     1864   2688   1911    706    -32    -93       N  
ATOM   2383  CA  ASP A 288       4.867  43.305  11.726  1.00 17.42           C  
ANISOU 2383  CA  ASP A 288     1856   2824   1940    726      8   -111       C  
ATOM   2384  C   ASP A 288       5.589  42.655  12.919  1.00 17.27           C  
ANISOU 2384  C   ASP A 288     1909   2706   1949    604     15   -169       C  
ATOM   2385  O   ASP A 288       4.943  42.061  13.788  1.00 17.35           O  
ANISOU 2385  O   ASP A 288     1854   2805   1932    561     36   -183       O  
ATOM   2386  CB  ASP A 288       3.602  42.508  11.345  1.00 20.25           C  
ANISOU 2386  CB  ASP A 288     2028   3427   2238    686    -17    -88       C  
ATOM   2387  CG  ASP A 288       3.895  41.065  10.970  1.00 25.13           C  
ANISOU 2387  CG  ASP A 288     2621   4069   2857    478    -64   -129       C  
ATOM   2388  OD1 ASP A 288       5.099  40.710  10.866  1.00 27.42           O  
ANISOU 2388  OD1 ASP A 288     3028   4191   3198    402    -77   -158       O  
ATOM   2389  OD2 ASP A 288       2.928  40.282  10.779  1.00 25.12           O1-
ANISOU 2389  OD2 ASP A 288     2486   4255   2804    389    -79   -131       O1-
ATOM   2390  N   VAL A 289       6.918  42.766  12.960  1.00 15.37           N  
ANISOU 2390  N   VAL A 289     1787   2299   1752    551      0   -190       N  
ATOM   2391  CA  VAL A 289       7.651  42.174  14.058  1.00 13.43           C  
ANISOU 2391  CA  VAL A 289     1593   1991   1518    451     -1   -224       C  
ATOM   2392  C   VAL A 289       7.270  42.812  15.407  1.00 15.66           C  
ANISOU 2392  C   VAL A 289     1913   2273   1765    504     51   -255       C  
ATOM   2393  O   VAL A 289       7.001  44.022  15.501  1.00 16.65           O  
ANISOU 2393  O   VAL A 289     2097   2352   1878    620     98   -266       O  
ATOM   2394  CB  VAL A 289       9.183  42.190  13.814  1.00 14.37           C  
ANISOU 2394  CB  VAL A 289     1803   1975   1682    387    -32   -228       C  
ATOM   2395  CG1 VAL A 289       9.764  43.594  13.915  1.00 15.95           C  
ANISOU 2395  CG1 VAL A 289     2112   2061   1889    444    -10   -246       C  
ATOM   2396  CG2 VAL A 289       9.921  41.244  14.753  1.00 13.96           C  
ANISOU 2396  CG2 VAL A 289     1763   1908   1633    285    -45   -233       C  
ATOM   2397  N   THR A 290       7.236  41.954  16.440  1.00 13.40           N  
ANISOU 2397  N   THR A 290     1604   2032   1455    421     54   -266       N  
ATOM   2398  CA  THR A 290       6.917  42.294  17.827  1.00 13.64           C  
ANISOU 2398  CA  THR A 290     1665   2085   1431    442    103   -299       C  
ATOM   2399  C   THR A 290       7.929  41.549  18.704  1.00 15.34           C  
ANISOU 2399  C   THR A 290     1924   2268   1635    325     72   -300       C  
ATOM   2400  O   THR A 290       8.748  40.752  18.197  1.00 13.72           O  
ANISOU 2400  O   THR A 290     1714   2025   1473    251     25   -266       O  
ATOM   2401  CB  THR A 290       5.486  41.855  18.161  1.00 16.89           C  
ANISOU 2401  CB  THR A 290     1958   2658   1802    473    146   -281       C  
ATOM   2402  CG2 THR A 290       4.445  42.476  17.249  1.00 16.28           C  
ANISOU 2402  CG2 THR A 290     1795   2666   1723    599    167   -255       C  
ATOM   2403  OG1 THR A 290       5.387  40.422  18.131  1.00 16.85           O  
ANISOU 2403  OG1 THR A 290     1880   2717   1804    344    119   -251       O  
ATOM   2404  N   LYS A 291       7.831  41.732  20.017  1.00 14.99           N  
ANISOU 2404  N   LYS A 291     1916   2255   1525    317    105   -328       N  
ATOM   2405  CA  LYS A 291       8.715  41.064  20.957  1.00 15.31           C  
ANISOU 2405  CA  LYS A 291     1984   2303   1530    221     74   -312       C  
ATOM   2406  C   LYS A 291       7.873  40.316  21.991  1.00 15.78           C  
ANISOU 2406  C   LYS A 291     1993   2476   1528    199    117   -288       C  
ATOM   2407  O   LYS A 291       7.651  40.826  23.105  1.00 16.38           O  
ANISOU 2407  O   LYS A 291     2109   2595   1519    214    156   -329       O  
ATOM   2408  CB  LYS A 291       9.691  42.059  21.600  1.00 16.67           C  
ANISOU 2408  CB  LYS A 291     2262   2415   1655    196     60   -370       C  
ATOM   2409  CG  LYS A 291      10.766  41.348  22.403  1.00 20.34           C  
ANISOU 2409  CG  LYS A 291     2727   2924   2077     98      7   -330       C  
ATOM   2410  CD  LYS A 291      11.606  42.343  23.223  1.00 24.94           C  
ANISOU 2410  CD  LYS A 291     3401   3498   2577     39     -9   -403       C  
ATOM   2411  CE  LYS A 291      12.664  41.615  24.015  1.00 34.68           C  
ANISOU 2411  CE  LYS A 291     4600   4826   3749    -50    -74   -342       C  
ATOM   2412  NZ  LYS A 291      13.625  42.560  24.645  1.00 47.92           N1+
ANISOU 2412  NZ  LYS A 291     6347   6521   5338   -146   -110   -415       N1+
ATOM   2413  N   PRO A 292       7.359  39.117  21.643  1.00 14.73           N  
ANISOU 2413  N   PRO A 292     1780   2390   1427    154    121   -229       N  
ATOM   2414  CA  PRO A 292       6.564  38.350  22.597  1.00 15.72           C  
ANISOU 2414  CA  PRO A 292     1860   2619   1495    114    171   -196       C  
ATOM   2415  C   PRO A 292       7.403  37.792  23.732  1.00 18.26           C  
ANISOU 2415  C   PRO A 292     2233   2944   1760     58    158   -151       C  
ATOM   2416  O   PRO A 292       8.649  37.673  23.593  1.00 18.80           O  
ANISOU 2416  O   PRO A 292     2347   2945   1851     37    101   -124       O  
ATOM   2417  CB  PRO A 292       5.988  37.197  21.749  1.00 17.27           C  
ANISOU 2417  CB  PRO A 292     1982   2832   1749     46    178   -150       C  
ATOM   2418  CG  PRO A 292       6.215  37.555  20.317  1.00 18.69           C  
ANISOU 2418  CG  PRO A 292     2153   2949   1999     75    135   -174       C  
ATOM   2419  CD  PRO A 292       7.459  38.419  20.346  1.00 15.04           C  
ANISOU 2419  CD  PRO A 292     1780   2386   1548    122     92   -197       C  
ATOM   2420  N   VAL A 293       6.714  37.473  24.830  1.00 19.37           N  
ANISOU 2420  N   VAL A 293     2355   3186   1819     40    213   -132       N  
ATOM   2421  CA  VAL A 293       7.241  36.843  26.048  1.00 21.27           C  
ANISOU 2421  CA  VAL A 293     2631   3473   1979     -8    214    -67       C  
ATOM   2422  C   VAL A 293       7.121  35.323  25.768  1.00 26.81           C  
ANISOU 2422  C   VAL A 293     3307   4144   2736    -76    236     39       C  
ATOM   2423  O   VAL A 293       6.028  34.840  25.454  1.00 29.60           O  
ANISOU 2423  O   VAL A 293     3604   4531   3114   -114    291     42       O  
ATOM   2424  CB  VAL A 293       6.458  37.257  27.328  1.00 27.34           C  
ANISOU 2424  CB  VAL A 293     3401   4366   2623      6    280    -98       C  
ATOM   2425  CG1 VAL A 293       6.983  36.525  28.564  1.00 27.32           C  
ANISOU 2425  CG1 VAL A 293     3430   4432   2520    -46    278    -13       C  
ATOM   2426  CG2 VAL A 293       6.503  38.769  27.549  1.00 28.25           C  
ANISOU 2426  CG2 VAL A 293     3574   4475   2684     74    285   -220       C  
ATOM   2427  N   PRO A 294       8.225  34.569  25.810  1.00 21.89           N  
ANISOU 2427  N   PRO A 294     2727   3456   2134    -92    202    126       N  
ATOM   2428  CA  PRO A 294       8.146  33.125  25.525  1.00 21.86           C  
ANISOU 2428  CA  PRO A 294     2737   3381   2188   -145    248    225       C  
ATOM   2429  C   PRO A 294       7.514  32.345  26.665  1.00 27.40           C  
ANISOU 2429  C   PRO A 294     3444   4154   2812   -193    322    306       C  
ATOM   2430  O   PRO A 294       7.613  32.750  27.818  1.00 26.17           O  
ANISOU 2430  O   PRO A 294     3292   4106   2544   -171    317    320       O  
ATOM   2431  CB  PRO A 294       9.608  32.720  25.362  1.00 23.31           C  
ANISOU 2431  CB  PRO A 294     2966   3485   2405   -105    201    305       C  
ATOM   2432  CG  PRO A 294      10.373  33.694  26.215  1.00 27.00           C  
ANISOU 2432  CG  PRO A 294     3430   4055   2776    -66    133    286       C  
ATOM   2433  CD  PRO A 294       9.600  34.992  26.139  1.00 22.99           C  
ANISOU 2433  CD  PRO A 294     2903   3594   2240    -62    129    143       C  
ATOM   2434  N   HIS A 295       6.875  31.228  26.321  1.00 28.49           N  
ANISOU 2434  N   HIS A 295     3592   4230   3002   -274    395    355       N  
ATOM   2435  CA  HIS A 295       6.276  30.307  27.280  1.00 30.86           C  
ANISOU 2435  CA  HIS A 295     3913   4570   3243   -342    483    451       C  
ATOM   2436  C   HIS A 295       7.432  29.417  27.756  1.00 38.74           C  
ANISOU 2436  C   HIS A 295     5003   5479   4238   -298    489    600       C  
ATOM   2437  O   HIS A 295       7.893  28.550  27.008  1.00 39.84           O  
ANISOU 2437  O   HIS A 295     5209   5458   4471   -305    517    651       O  
ATOM   2438  CB  HIS A 295       5.140  29.506  26.612  0.50 31.83           C  
ANISOU 2438  CB  HIS A 295     4016   4654   3425   -475    563    432       C  
ATOM   2439  CG  HIS A 295       4.452  28.537  27.522  0.50 36.80           C  
ANISOU 2439  CG  HIS A 295     4670   5311   3999   -573    669    529       C  
ATOM   2440  CD2 HIS A 295       4.430  27.185  27.482  0.50 39.69           C  
ANISOU 2440  CD2 HIS A 295     5133   5539   4407   -670    759    625       C  
ATOM   2441  ND1 HIS A 295       3.666  28.967  28.577  0.50 39.50           N  
ANISOU 2441  ND1 HIS A 295     4944   5832   4232   -579    703    529       N  
ATOM   2442  CE1 HIS A 295       3.214  27.867  29.156  0.50 40.42           C  
ANISOU 2442  CE1 HIS A 295     5107   5927   4325   -684    806    635       C  
ATOM   2443  NE2 HIS A 295       3.645  26.771  28.530  0.50 40.91           N  
ANISOU 2443  NE2 HIS A 295     5277   5789   4479   -745    845    696       N  
ATOM   2444  N   LEU A 296       7.952  29.709  28.967  0.50 35.13           N  
ANISOU 2444  N   LEU A 296     4547   5137   3662   -239    461    667       N  
ATOM   2445  CA  LEU A 296       9.074  29.011  29.598  1.00 63.40           C  
ANISOU 2445  CA  LEU A 296     8185   8700   7206   -169    453    833       C  
ATOM   2446  C   LEU A 296       8.700  28.528  31.000  0.50 89.27           C  
ANISOU 2446  C   LEU A 296    11481  12088  10350   -187    514    952       C  
ATOM   2447  O   LEU A 296       9.488  27.849  31.657  0.50 46.15           O  
ANISOU 2447  O   LEU A 296     6063   6635   4837   -123    521   1120       O  
ATOM   2448  CB  LEU A 296      10.314  29.929  29.664  1.00 62.84           C  
ANISOU 2448  CB  LEU A 296     8076   8708   7093    -82    331    808       C  
ATOM   2449  CG  LEU A 296      11.153  30.059  28.385  1.00 66.59           C  
ANISOU 2449  CG  LEU A 296     8547   9060   7693    -37    280    770       C  
ATOM   2450  CD1 LEU A 296      12.105  31.227  28.479  1.00 66.19           C  
ANISOU 2450  CD1 LEU A 296     8442   9118   7588      2    164    707       C  
ATOM   2451  CD2 LEU A 296      11.951  28.798  28.111  1.00 70.27           C  
ANISOU 2451  CD2 LEU A 296     9073   9396   8228     30    330    934       C  
TER   
CONECT    1    2    3    4
CONECT    2    1
CONECT    3    1
CONECT    4    1
END



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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: April 25th, 2023.