CNRS Nantes University US2B US2B
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***  CYTOKINE 2024-10-21  ***

elNémo ID: 2608031212472344273

Job options:

ID        	=	 2608031212472344273
JOBID     	=	 CYTOKINE 2024-10-21
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    CYTOKINE                                2024-10-21
TITLE     Crystal structure of IL-17A in complex with compound 11
EXPDTA    X-RAY DIFFRACTION
REMARK   2 RESOLUTION.    2.00 ANGSTROMS
REMARK   3  R VALUE : 0.235900
REMARK   3  FREE R VALUE : 0.262200
REMARK   4 9H4O COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 200  TEMPERATURE           (KELVIN) : 100.00
REMARK 200  PH                             : 5.50
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1  1   1.000000 0.000000 0.000000   0.000000
REMARK 350   BIOMT2  1   0.000000 1.000000 0.000000   0.000000
REMARK 350   BIOMT3  1   0.000000 0.000000 1.000000   0.000000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1  1   1.000000 0.000000 0.000000   0.000000
REMARK 350   BIOMT2  1   0.000000 1.000000 0.000000   0.000000
REMARK 350   BIOMT3  1   0.000000 0.000000 1.000000   0.000000
REMARK 888
REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC)
CRYST1   61.187   59.064   71.185  90.00 101.82  90.00 P 21          8
ATOM      1  N   PRO A  42     -29.456   5.994  -6.590  1.00 62.13           N  
ANISOU    1  N   PRO A  42     7185   9367   7055    545    547    440
ATOM      2  CA  PRO A  42     -28.356   6.642  -5.855  1.00 61.71           C  
ANISOU    2  CA  PRO A  42     7324   9137   6986    610    594    299
ATOM      3  C   PRO A  42     -27.479   7.566  -6.763  1.00 61.51           C  
ANISOU    3  C   PRO A  42     7532   8835   7003    664    601    177
ATOM      4  O   PRO A  42     -27.180   7.251  -7.917  1.00 62.11           O  
ANISOU    4  O   PRO A  42     7621   8816   7162    602    565    190
ATOM      5  CB  PRO A  42     -27.514   5.483  -5.294  1.00 62.67           C  
ANISOU    5  CB  PRO A  42     7420   9192   7199    387    548    309
ATOM      6  CG  PRO A  42     -27.672   4.401  -6.355  1.00 63.34           C  
ANISOU    6  CG  PRO A  42     7405   9277   7386    205    464    407
ATOM      7  CD  PRO A  42     -29.104   4.598  -6.844  1.00 61.81           C  
ANISOU    7  CD  PRO A  42     7084   9266   7134    283    457    506
ATOM      8  H   PRO A  42     -30.369   6.108  -6.163  1.00 62.13           H  
ATOM      9  HA  PRO A  42     -28.767   7.268  -5.062  1.00 61.71           H  
ATOM     10  HB3 PRO A  42     -27.905   5.175  -4.323  1.00 62.67           H  
ATOM     11  HB2 PRO A  42     -26.465   5.737  -5.134  1.00 62.67           H  
ATOM     12  HG3 PRO A  42     -27.499   3.398  -5.968  1.00 63.34           H  
ATOM     13  HG2 PRO A  42     -26.982   4.552  -7.186  1.00 63.34           H  
ATOM     14  HD2 PRO A  42     -29.163   4.408  -7.917  1.00 61.81           H  
ATOM     15  HD3 PRO A  42     -29.794   3.909  -6.354  1.00 61.81           H  
ATOM     16  N   ARG A  43     -27.030   8.713  -6.222  1.00 60.01           N  
ANISOU   16  N   ARG A  43     7539   8518   6743    769    639     64
ATOM     17  CA  ARG A  43     -26.248   9.692  -6.980  1.00 58.59           C  
ANISOU   17  CA  ARG A  43     7601   8077   6585    790    630    -41
ATOM     18  C   ARG A  43     -24.881   9.147  -7.430  1.00 54.92           C  
ANISOU   18  C   ARG A  43     7174   7440   6254    550    581    -60
ATOM     19  O   ARG A  43     -24.495   9.338  -8.579  1.00 55.27           O  
ANISOU   19  O   ARG A  43     7260   7358   6382    480    551    -65
ATOM     20  CB  ARG A  43     -26.064  10.982  -6.148  1.00 61.73           C  
ANISOU   20  CB  ARG A  43     8225   8392   6839    961    664   -143
ATOM     21  CG  ARG A  43     -25.379  12.123  -6.936  1.00 66.94           C  
ANISOU   21  CG  ARG A  43     9168   8769   7499    950    632   -242
ATOM     22  CD  ARG A  43     -25.011  13.356  -6.099  1.00 72.23           C  
ANISOU   22  CD  ARG A  43    10100   9342   8001   1110    643   -337
ATOM     23  NE  ARG A  43     -23.827  13.097  -5.248  1.00 78.29           N  
ANISOU   23  NE  ARG A  43    10955  10018   8773    937    616   -374
ATOM     24  CZ  ARG A  43     -22.817  13.924  -4.934  1.00 82.88           C  
ANISOU   24  CZ  ARG A  43    11816  10367   9308    858    565   -449
ATOM     25  NH1 ARG A  43     -22.805  15.201  -5.324  1.00 83.18           N  
ANISOU   25  NH1 ARG A  43    12095  10221   9287    941    531   -503
ATOM     26  NH2 ARG A  43     -21.797  13.448  -4.219  1.00 83.80           N1+
ANISOU   26  NH2 ARG A  43    11977  10439   9424    685    538   -462
ATOM     27  H   ARG A  43     -27.281   8.928  -5.273  1.00 60.01           H  
ATOM     28  HA  ARG A  43     -26.823   9.939  -7.875  1.00 58.59           H  
ATOM     29  HB3 ARG A  43     -25.496  10.754  -5.244  1.00 61.73           H  
ATOM     30  HB2 ARG A  43     -27.041  11.329  -5.807  1.00 61.73           H  
ATOM     31  HG3 ARG A  43     -25.938  12.392  -7.832  1.00 66.94           H  
ATOM     32  HG2 ARG A  43     -24.438  11.728  -7.320  1.00 66.94           H  
ATOM     33  HD3 ARG A  43     -25.826  13.553  -5.400  1.00 72.23           H  
ATOM     34  HD2 ARG A  43     -24.928  14.235  -6.734  1.00 72.23           H  
ATOM     35 HH22 ARG A  43     -21.040  14.031  -3.889  1.00 83.80           H  
ATOM     36 HH21 ARG A  43     -21.731  12.461  -3.986  1.00 83.80           H  
ATOM     37 HH12 ARG A  43     -22.002  15.805  -5.190  1.00 83.18           H  
ATOM     38 HH11 ARG A  43     -23.619  15.613  -5.751  1.00 83.18           H  
ATOM     39  HE  ARG A  43     -23.765  12.126  -4.948  1.00 78.29           H  
ATOM     40  N   THR A  44     -24.148   8.569  -6.476  1.00 51.51           N  
ANISOU   40  N   THR A  44     6711   7026   5835    433    576    -60
ATOM     41  CA  THR A  44     -22.785   8.102  -6.660  1.00 48.81           C  
ANISOU   41  CA  THR A  44     6387   6561   5596    231    536    -66
ATOM     42  C   THR A  44     -22.790   6.569  -6.574  1.00 45.87           C  
ANISOU   42  C   THR A  44     5825   6294   5312    100    503     24
ATOM     43  O   THR A  44     -23.323   6.029  -5.602  1.00 45.10           O  
ANISOU   43  O   THR A  44     5594   6362   5182     97    508     83
ATOM     44  CB  THR A  44     -21.858   8.684  -5.552  1.00 50.37           C  
ANISOU   44  CB  THR A  44     6712   6683   5742    175    541   -126
ATOM     45  OG1 THR A  44     -21.911  10.114  -5.577  1.00 51.93           O  
ANISOU   45  OG1 THR A  44     7133   6761   5837    289    551   -208
ATOM     46  CG2 THR A  44     -20.380   8.269  -5.681  1.00 50.37           C  
ANISOU   46  CG2 THR A  44     6721   6589   5829    -15    504   -119
ATOM     47  H   THR A  44     -24.570   8.332  -5.593  1.00 51.51           H  
ATOM     48  HA  THR A  44     -22.404   8.407  -7.633  1.00 48.81           H  
ATOM     49  HB  THR A  44     -22.219   8.361  -4.573  1.00 50.37           H  
ATOM     50  HG1 THR A  44     -21.472  10.383  -6.391  1.00 51.93           H  
ATOM     51 HG21 THR A  44     -19.757   8.742  -4.921  1.00 50.37           H  
ATOM     52 HG22 THR A  44     -20.252   7.191  -5.558  1.00 50.37           H  
ATOM     53 HG23 THR A  44     -19.970   8.530  -6.656  1.00 50.37           H  
ATOM     54  N   VAL A  45     -22.231   5.911  -7.589  1.00 43.26           N  
ANISOU   54  N   VAL A  45     5495   5864   5078     -6    461     40
ATOM     55  CA  VAL A  45     -22.145   4.458  -7.676  1.00 41.64           C  
ANISOU   55  CA  VAL A  45     5167   5709   4944   -123    411    117
ATOM     56  C   VAL A  45     -20.678   4.061  -7.898  1.00 41.04           C  
ANISOU   56  C   VAL A  45     5152   5516   4927   -228    389     93
ATOM     57  O   VAL A  45     -19.887   4.896  -8.343  1.00 42.08           O  
ANISOU   57  O   VAL A  45     5395   5542   5050   -224    408     34
ATOM     58  CB  VAL A  45     -23.022   3.927  -8.847  1.00 40.54           C  
ANISOU   58  CB  VAL A  45     4970   5592   4843   -117    369    179
ATOM     59  CG1 VAL A  45     -24.488   4.327  -8.617  1.00 40.14           C  
ANISOU   59  CG1 VAL A  45     4832   5706   4714     -3    394    223
ATOM     60  CG2 VAL A  45     -22.557   4.312 -10.270  1.00 40.48           C  
ANISOU   60  CG2 VAL A  45     5075   5423   4883   -102    362    129
ATOM     61  H   VAL A  45     -21.817   6.416  -8.371  1.00 43.26           H  
ATOM     62  HA  VAL A  45     -22.475   3.991  -6.745  1.00 41.64           H  
ATOM     63  HB  VAL A  45     -22.986   2.838  -8.806  1.00 40.54           H  
ATOM     64 HG11 VAL A  45     -25.172   3.798  -9.276  1.00 40.14           H  
ATOM     65 HG12 VAL A  45     -24.789   4.108  -7.593  1.00 40.14           H  
ATOM     66 HG13 VAL A  45     -24.640   5.396  -8.772  1.00 40.14           H  
ATOM     67 HG21 VAL A  45     -23.227   3.896 -11.023  1.00 40.48           H  
ATOM     68 HG22 VAL A  45     -22.536   5.390 -10.414  1.00 40.48           H  
ATOM     69 HG23 VAL A  45     -21.561   3.935 -10.503  1.00 40.48           H  
ATOM     70  N   MET A  46     -20.344   2.806  -7.579  1.00 40.03           N  
ANISOU   70  N   MET A  46     4953   5412   4843   -319    343    150
ATOM     71  CA  MET A  46     -19.040   2.220  -7.869  1.00 39.25           C  
ANISOU   71  CA  MET A  46     4895   5234   4784   -386    323    142
ATOM     72  C   MET A  46     -19.096   1.503  -9.220  1.00 37.77           C  
ANISOU   72  C   MET A  46     4735   4969   4647   -385    274    163
ATOM     73  O   MET A  46     -20.038   0.748  -9.470  1.00 36.70           O  
ANISOU   73  O   MET A  46     4565   4856   4525   -393    225    215
ATOM     74  CB  MET A  46     -18.645   1.211  -6.775  1.00 40.26           C  
ANISOU   74  CB  MET A  46     4954   5429   4912   -461    298    188
ATOM     75  CG  MET A  46     -18.241   1.880  -5.459  1.00 43.34           C  
ANISOU   75  CG  MET A  46     5349   5863   5254   -482    346    153
ATOM     76  SD  MET A  46     -17.690   0.716  -4.183  1.00 45.23           S  
ANISOU   76  SD  MET A  46     5502   6191   5494   -571    319    211
ATOM     77  CE  MET A  46     -19.286   0.021  -3.674  1.00 36.56           C  
ANISOU   77  CE  MET A  46     4297   5213   4380   -573    285    282
ATOM     78  H   MET A  46     -21.078   2.159  -7.285  1.00 40.03           H  
ATOM     79  HA  MET A  46     -18.283   3.003  -7.911  1.00 39.25           H  
ATOM     80  HB3 MET A  46     -17.801   0.614  -7.124  1.00 40.26           H  
ATOM     81  HB2 MET A  46     -19.457   0.504  -6.610  1.00 40.26           H  
ATOM     82  HG3 MET A  46     -19.061   2.475  -5.062  1.00 43.34           H  
ATOM     83  HG2 MET A  46     -17.420   2.573  -5.647  1.00 43.34           H  
ATOM     84  HE1 MET A  46     -19.150  -0.642  -2.818  1.00 36.56           H  
ATOM     85  HE2 MET A  46     -19.973   0.817  -3.383  1.00 36.56           H  
ATOM     86  HE3 MET A  46     -19.743  -0.551  -4.480  1.00 36.56           H  
ATOM     87  N   VAL A  47     -18.063   1.701 -10.035  1.00 37.64           N  
ANISOU   87  N   VAL A  47     4780   4878   4644   -382    279    137
ATOM     88  CA  VAL A  47     -17.884   0.994 -11.289  1.00 38.15           C  
ANISOU   88  CA  VAL A  47     4889   4868   4739   -356    237    149
ATOM     89  C   VAL A  47     -16.517   0.297 -11.250  1.00 40.56           C  
ANISOU   89  C   VAL A  47     5212   5162   5036   -357    226    159
ATOM     90  O   VAL A  47     -15.503   0.943 -10.983  1.00 39.78           O  
ANISOU   90  O   VAL A  47     5108   5097   4911   -370    269    143
ATOM     91  CB  VAL A  47     -17.954   1.958 -12.502  1.00 37.37           C  
ANISOU   91  CB  VAL A  47     4846   4707   4644   -305    260    110
ATOM     92  CG1 VAL A  47     -17.686   1.268 -13.856  1.00 37.18           C  
ANISOU   92  CG1 VAL A  47     4874   4612   4640   -272    218    121
ATOM     93  CG2 VAL A  47     -19.317   2.680 -12.541  1.00 36.74           C  
ANISOU   93  CG2 VAL A  47     4747   4654   4558   -272    271    108
ATOM     94  H   VAL A  47     -17.323   2.350  -9.773  1.00 37.64           H  
ATOM     95  HA  VAL A  47     -18.661   0.241 -11.423  1.00 38.15           H  
ATOM     96  HB  VAL A  47     -17.185   2.724 -12.379  1.00 37.37           H  
ATOM     97 HG11 VAL A  47     -17.800   1.973 -14.680  1.00 37.18           H  
ATOM     98 HG12 VAL A  47     -16.675   0.872 -13.921  1.00 37.18           H  
ATOM     99 HG13 VAL A  47     -18.372   0.439 -14.028  1.00 37.18           H  
ATOM    100 HG21 VAL A  47     -19.437   3.269 -13.450  1.00 36.74           H  
ATOM    101 HG22 VAL A  47     -20.146   1.973 -12.497  1.00 36.74           H  
ATOM    102 HG23 VAL A  47     -19.434   3.360 -11.695  1.00 36.74           H  
ATOM    103  N   ASN A  48     -16.520  -1.015 -11.500  1.00 41.61           N  
ANISOU  103  N   ASN A  48     5377   5255   5177   -341    160    195
ATOM    104  CA  ASN A  48     -15.321  -1.808 -11.751  1.00 41.96           C  
ANISOU  104  CA  ASN A  48     5453   5296   5195   -293    148    207
ATOM    105  C   ASN A  48     -14.881  -1.569 -13.210  1.00 43.26           C  
ANISOU  105  C   ASN A  48     5680   5409   5349   -210    154    184
ATOM    106  O   ASN A  48     -15.662  -1.849 -14.127  1.00 43.71           O  
ANISOU  106  O   ASN A  48     5806   5381   5420   -183    104    183
ATOM    107  CB  ASN A  48     -15.630  -3.295 -11.480  1.00 41.85           C  
ANISOU  107  CB  ASN A  48     5490   5235   5175   -297     58    252
ATOM    108  CG  ASN A  48     -14.407  -4.205 -11.324  1.00 42.79           C  
ANISOU  108  CG  ASN A  48     5656   5355   5250   -215     43    266
ATOM    109  OD1 ASN A  48     -13.322  -3.960 -11.846  1.00 44.13           O  
ANISOU  109  OD1 ASN A  48     5841   5541   5386   -121     80    249
ATOM    110  ND2 ASN A  48     -14.576  -5.311 -10.609  1.00 43.42           N  
ANISOU  110  ND2 ASN A  48     5750   5433   5313   -239    -10    305
ATOM    111  H   ASN A  48     -17.418  -1.483 -11.622  1.00 41.61           H  
ATOM    112  HA  ASN A  48     -14.516  -1.495 -11.088  1.00 41.96           H  
ATOM    113  HB3 ASN A  48     -16.274  -3.706 -12.250  1.00 41.85           H  
ATOM    114  HB2 ASN A  48     -16.201  -3.362 -10.553  1.00 41.85           H  
ATOM    115 HD22 ASN A  48     -13.810  -5.952 -10.532  1.00 43.42           H  
ATOM    116 HD21 ASN A  48     -15.501  -5.589 -10.291  1.00 43.42           H  
ATOM    117  N   LEU A  49     -13.673  -1.026 -13.396  1.00 43.72           N  
ANISOU  117  N   LEU A  49     5709   5533   5371   -182    210    177
ATOM    118  CA  LEU A  49     -13.150  -0.612 -14.699  1.00 44.47           C  
ANISOU  118  CA  LEU A  49     5839   5616   5440   -110    225    167
ATOM    119  C   LEU A  49     -12.574  -1.770 -15.525  1.00 45.30           C  
ANISOU  119  C   LEU A  49     6006   5711   5496     22    189    185
ATOM    120  O   LEU A  49     -12.334  -1.574 -16.712  1.00 45.74           O  
ANISOU  120  O   LEU A  49     6081   5785   5513    101    207    182
ATOM    121  CB  LEU A  49     -12.077   0.494 -14.540  1.00 44.37           C  
ANISOU  121  CB  LEU A  49     5762   5710   5385   -154    286    177
ATOM    122  CG  LEU A  49     -12.579   1.866 -14.033  1.00 46.04           C  
ANISOU  122  CG  LEU A  49     5963   5914   5617   -269    314    151
ATOM    123  CD1 LEU A  49     -11.432   2.897 -14.075  1.00 46.51           C  
ANISOU  123  CD1 LEU A  49     5996   6063   5614   -340    345    177
ATOM    124  CD2 LEU A  49     -13.784   2.381 -14.842  1.00 46.08           C  
ANISOU  124  CD2 LEU A  49     6027   5815   5668   -257    304    110
ATOM    125  H   LEU A  49     -13.072  -0.862 -12.590  1.00 43.72           H  
ATOM    126  HA  LEU A  49     -13.982  -0.222 -15.285  1.00 44.47           H  
ATOM    127  HB3 LEU A  49     -11.608   0.656 -15.512  1.00 44.37           H  
ATOM    128  HB2 LEU A  49     -11.279   0.140 -13.885  1.00 44.37           H  
ATOM    129  HG  LEU A  49     -12.897   1.758 -12.994  1.00 46.04           H  
ATOM    130 HD11 LEU A  49     -11.799   3.921 -14.152  1.00 46.51           H  
ATOM    131 HD12 LEU A  49     -10.816   2.845 -13.178  1.00 46.51           H  
ATOM    132 HD13 LEU A  49     -10.764   2.736 -14.922  1.00 46.51           H  
ATOM    133 HD21 LEU A  49     -13.954   3.448 -14.708  1.00 46.08           H  
ATOM    134 HD22 LEU A  49     -13.629   2.216 -15.907  1.00 46.08           H  
ATOM    135 HD23 LEU A  49     -14.704   1.878 -14.547  1.00 46.08           H  
ATOM    136  N   ASN A  50     -12.357  -2.947 -14.923  1.00 44.80           N  
ANISOU  136  N   ASN A  50     5982   5622   5416     56    139    207
ATOM    137  CA  ASN A  50     -11.823  -4.121 -15.621  1.00 45.40           C  
ANISOU  137  CA  ASN A  50     6163   5662   5423    213     94    218
ATOM    138  C   ASN A  50     -12.930  -4.753 -16.483  1.00 44.53           C  
ANISOU  138  C   ASN A  50     6200   5385   5336    223      8    196
ATOM    139  O   ASN A  50     -13.634  -5.651 -16.006  1.00 44.08           O  
ANISOU  139  O   ASN A  50     6215   5233   5301    157    -75    212
ATOM    140  CB  ASN A  50     -11.242  -5.130 -14.598  1.00 47.41           C  
ANISOU  140  CB  ASN A  50     6432   5943   5640    249     63    251
ATOM    141  CG  ASN A  50      -9.890  -4.735 -13.998  1.00 51.53           C  
ANISOU  141  CG  ASN A  50     6819   6653   6106    279    141    287
ATOM    142  OD1 ASN A  50      -9.153  -3.926 -14.541  1.00 52.96           O  
ANISOU  142  OD1 ASN A  50     6926   6955   6241    322    204    300
ATOM    143  ND2 ASN A  50      -9.512  -5.332 -12.873  1.00 52.57           N  
ANISOU  143  ND2 ASN A  50     6911   6832   6234    243    133    317
ATOM    144  H   ASN A  50     -12.614  -3.043 -13.952  1.00 44.80           H  
ATOM    145  HA  ASN A  50     -11.012  -3.755 -16.255  1.00 45.40           H  
ATOM    146  HB3 ASN A  50     -11.061  -6.074 -15.115  1.00 47.41           H  
ATOM    147  HB2 ASN A  50     -11.965  -5.325 -13.806  1.00 47.41           H  
ATOM    148 HD22 ASN A  50      -8.588  -5.108 -12.533  1.00 52.57           H  
ATOM    149 HD21 ASN A  50     -10.074  -6.035 -12.433  1.00 52.57           H  
ATOM    150  N   ILE A  51     -13.061  -4.239 -17.713  1.00 43.46           N  
ANISOU  150  N   ILE A  51     6093   5227   5194    274     26    171
ATOM    151  CA  ILE A  51     -14.092  -4.563 -18.699  1.00 43.89           C  
ANISOU  151  CA  ILE A  51     6276   5136   5262    274    -49    154
ATOM    152  C   ILE A  51     -14.229  -6.083 -18.961  1.00 45.59           C  
ANISOU  152  C   ILE A  51     6689   5218   5417    356   -162    162
ATOM    153  O   ILE A  51     -13.225  -6.776 -19.135  1.00 46.31           O  
ANISOU  153  O   ILE A  51     6858   5321   5418    524   -164    159
ATOM    154  CB  ILE A  51     -13.840  -3.843 -20.072  1.00 42.97           C  
ANISOU  154  CB  ILE A  51     6157   5037   5133    340     -3    127
ATOM    155  CG1 ILE A  51     -13.783  -2.298 -19.944  1.00 41.89           C  
ANISOU  155  CG1 ILE A  51     5867   5004   5048    242     89    120
ATOM    156  CG2 ILE A  51     -14.857  -4.212 -21.180  1.00 43.07           C  
ANISOU  156  CG2 ILE A  51     6307   4903   5155    335    -84    112
ATOM    157  CD1 ILE A  51     -13.062  -1.592 -21.105  1.00 42.89           C  
ANISOU  157  CD1 ILE A  51     5973   5196   5127    321    141    114
ATOM    158  H   ILE A  51     -12.470  -3.448 -17.947  1.00 43.46           H  
ATOM    159  HA  ILE A  51     -15.018  -4.182 -18.277  1.00 43.89           H  
ATOM    160  HB  ILE A  51     -12.857  -4.167 -20.424  1.00 42.97           H  
ATOM    161 HG13 ILE A  51     -13.269  -2.010 -19.031  1.00 41.89           H  
ATOM    162 HG12 ILE A  51     -14.788  -1.894 -19.844  1.00 41.89           H  
ATOM    163 HG21 ILE A  51     -14.679  -3.647 -22.090  1.00 43.07           H  
ATOM    164 HG22 ILE A  51     -14.797  -5.259 -21.470  1.00 43.07           H  
ATOM    165 HG23 ILE A  51     -15.879  -4.005 -20.858  1.00 43.07           H  
ATOM    166 HD11 ILE A  51     -13.206  -0.513 -21.051  1.00 42.89           H  
ATOM    167 HD12 ILE A  51     -11.988  -1.775 -21.067  1.00 42.89           H  
ATOM    168 HD13 ILE A  51     -13.412  -1.907 -22.086  1.00 42.89           H  
ATOM    169  N   HIS A  52     -15.470  -6.572 -19.035  1.00 46.20           N  
ANISOU  169  N   HIS A  52     6859   5169   5524    241   -266    181
ATOM    170  CA  HIS A  52     -15.786  -7.871 -19.632  1.00 47.45           C  
ANISOU  170  CA  HIS A  52     7263   5156   5608    292   -406    192
ATOM    171  C   HIS A  52     -16.358  -7.637 -21.034  1.00 47.21           C  
ANISOU  171  C   HIS A  52     7330   5034   5573    296   -447    172
ATOM    172  O   HIS A  52     -17.116  -6.692 -21.232  1.00 45.94           O  
ANISOU  172  O   HIS A  52     7067   4902   5485    160   -432    186
ATOM    173  CB  HIS A  52     -16.764  -8.648 -18.728  1.00 48.33           C  
ANISOU  173  CB  HIS A  52     7429   5196   5739    118   -524    251
ATOM    174  CG  HIS A  52     -16.128  -9.298 -17.517  1.00 53.28           C  
ANISOU  174  CG  HIS A  52     8057   5849   6337    138   -536    274
ATOM    175  ND1 HIS A  52     -14.796  -9.134 -17.160  1.00 55.27           N  
ANISOU  175  ND1 HIS A  52     8399   6021   6578     -2   -665    336
ATOM    176  CD2 HIS A  52     -16.652 -10.158 -16.574  1.00 55.15           C  
ANISOU  176  CD2 HIS A  52     8197   6203   6555    260   -437    256
ATOM    177  CE1 HIS A  52     -14.575  -9.900 -16.088  1.00 56.98           C  
ANISOU  177  CE1 HIS A  52     8579   6294   6776     51   -636    344
ATOM    178  NE2 HIS A  52     -15.657 -10.544 -15.672  1.00 57.51           N  
ANISOU  178  NE2 HIS A  52     8528   6485   6838    208   -498    298
ATOM    179  H   HIS A  52     -16.255  -5.941 -18.897  1.00 46.20           H  
ATOM    180  HA  HIS A  52     -14.888  -8.480 -19.769  1.00 47.45           H  
ATOM    181  HB3 HIS A  52     -17.242  -9.451 -19.294  1.00 48.33           H  
ATOM    182  HB2 HIS A  52     -17.577  -8.004 -18.390  1.00 48.33           H  
ATOM    183  HD1 HIS A  52     -14.115  -8.549 -17.632  1.00 55.27           H  
ATOM    184  HD2 HIS A  52     -17.661 -10.531 -16.481  1.00 55.15           H  
ATOM    185  HE1 HIS A  52     -13.617  -9.980 -15.598  1.00 56.98           H  
ATOM    186  N   ASN A  53     -15.962  -8.465 -22.002  1.00 48.11           N  
ANISOU  186  N   ASN A  53     7644   5047   5590    467   -496    142
ATOM    187  CA  ASN A  53     -16.485  -8.406 -23.371  1.00 49.54           C  
ANISOU  187  CA  ASN A  53     7947   5124   5753    470   -551    125
ATOM    188  C   ASN A  53     -17.671  -9.367 -23.437  1.00 52.03           C  
ANISOU  188  C   ASN A  53     8422   5283   6064    292   -718    176
ATOM    189  O   ASN A  53     -17.523 -10.540 -23.095  1.00 51.10           O  
ANISOU  189  O   ASN A  53     8446   5072   5898    258   -827    209
ATOM    190  CB  ASN A  53     -15.376  -8.787 -24.376  1.00 49.91           C  
ANISOU  190  CB  ASN A  53     8176   5115   5674    723   -558     77
ATOM    191  CG  ASN A  53     -14.417  -7.636 -24.703  1.00 52.73           C  
ANISOU  191  CG  ASN A  53     8346   5667   6023    868   -397     50
ATOM    192  OD1 ASN A  53     -14.246  -7.237 -25.855  1.00 55.50           O  
ANISOU  192  OD1 ASN A  53     8455   6172   6459    772   -289     63
ATOM    193  ND2 ASN A  53     -13.781  -7.073 -23.683  1.00 52.54           N  
ANISOU  193  ND2 ASN A  53     8432   5647   5882   1093   -383     19
ATOM    194  H   ASN A  53     -15.458  -9.307 -21.768  1.00 48.11           H  
ATOM    195  HA  ASN A  53     -16.801  -7.384 -23.587  1.00 49.54           H  
ATOM    196  HB3 ASN A  53     -15.838  -9.083 -25.316  1.00 49.91           H  
ATOM    197  HB2 ASN A  53     -14.817  -9.661 -24.043  1.00 49.91           H  
ATOM    198 HD22 ASN A  53     -13.094  -6.352 -23.829  1.00 52.54           H  
ATOM    199 HD21 ASN A  53     -13.972  -7.389 -22.741  1.00 52.54           H  
ATOM    200  N   ARG A  54     -18.824  -8.837 -23.833  1.00 54.19           N  
ANISOU  200  N   ARG A  54     8673   5537   6381    168   -748    194
ATOM    201  CA  ARG A  54     -20.097  -9.525 -23.886  1.00 57.45           C  
ANISOU  201  CA  ARG A  54     9206   5841   6779    -37   -914    270
ATOM    202  C   ARG A  54     -20.491  -9.661 -25.355  1.00 60.63           C  
ANISOU  202  C   ARG A  54     9800   6110   7125    -28  -1006    261
ATOM    203  O   ARG A  54     -21.028  -8.723 -25.941  1.00 60.86           O  
ANISOU  203  O   ARG A  54     9701   6212   7209    -56   -940    254
ATOM    204  CB  ARG A  54     -21.109  -8.703 -23.067  1.00 58.57           C  
ANISOU  204  CB  ARG A  54     9087   6145   7023   -239   -869    336
ATOM    205  CG  ARG A  54     -22.597  -9.104 -23.195  1.00 59.80           C  
ANISOU  205  CG  ARG A  54     9299   6264   7158   -473  -1027    443
ATOM    206  CD  ARG A  54     -22.935 -10.453 -22.550  1.00 59.62           C  
ANISOU  206  CD  ARG A  54     9472   6121   7059   -577  -1197    507
ATOM    207  NE  ARG A  54     -22.765 -10.420 -21.088  1.00 59.95           N  
ANISOU  207  NE  ARG A  54     9334   6297   7146   -645  -1145    545
ATOM    208  CZ  ARG A  54     -22.675 -11.456 -20.247  1.00 60.82           C  
ANISOU  208  CZ  ARG A  54     9562   6344   7203   -760  -1278    615
ATOM    209  NH1 ARG A  54     -22.839 -12.707 -20.688  1.00 59.84           N  
ANISOU  209  NH1 ARG A  54     9761   6004   6972   -819  -1480    652
ATOM    210  NH2 ARG A  54     -22.408 -11.231 -18.966  1.00 59.50           N1+
ANISOU  210  NH2 ARG A  54     9212   6317   7079   -818  -1220    648
ATOM    211  H   ARG A  54     -18.872  -7.863 -24.141  1.00 54.19           H  
ATOM    212  HA  ARG A  54     -20.030 -10.525 -23.449  1.00 57.45           H  
ATOM    213  HB3 ARG A  54     -21.021  -7.652 -23.337  1.00 58.57           H  
ATOM    214  HB2 ARG A  54     -20.803  -8.765 -22.027  1.00 58.57           H  
ATOM    215  HG3 ARG A  54     -22.965  -9.075 -24.223  1.00 59.80           H  
ATOM    216  HG2 ARG A  54     -23.171  -8.326 -22.690  1.00 59.80           H  
ATOM    217  HD3 ARG A  54     -22.216 -11.186 -22.910  1.00 59.62           H  
ATOM    218  HD2 ARG A  54     -23.920 -10.816 -22.851  1.00 59.62           H  
ATOM    219 HH22 ARG A  54     -22.357 -11.935 -18.249  1.00 59.50           H  
ATOM    220 HH21 ARG A  54     -22.191 -10.253 -18.686  1.00 59.50           H  
ATOM    221 HH12 ARG A  54     -22.756 -13.524 -20.101  1.00 59.84           H  
ATOM    222 HH11 ARG A  54     -23.038 -12.860 -21.666  1.00 59.84           H  
ATOM    223  HE  ARG A  54     -22.684  -9.469 -20.695  1.00 59.95           H  
ATOM    224  N   ASN A  55     -20.231 -10.855 -25.901  1.00 63.42           N  
ANISOU  224  N   ASN A  55    10482   6258   7357     27  -1161    256
ATOM    225  CA  ASN A  55     -20.772 -11.360 -27.171  1.00 66.54           C  
ANISOU  225  CA  ASN A  55    11119   6491   7670     39  -1275    245
ATOM    226  C   ASN A  55     -20.226 -10.615 -28.403  1.00 68.89           C  
ANISOU  226  C   ASN A  55    11325   6864   7986    218  -1134    167
ATOM    227  O   ASN A  55     -20.771 -10.776 -29.488  1.00 69.73           O  
ANISOU  227  O   ASN A  55    11447   6945   8102    139  -1168    180
ATOM    228  CB  ASN A  55     -22.328 -11.393 -27.186  1.00 68.74           C  
ANISOU  228  CB  ASN A  55    11425   6734   7961   -261  -1427    354
ATOM    229  CG  ASN A  55     -23.014 -12.205 -26.079  1.00 73.19           C  
ANISOU  229  CG  ASN A  55    12060   7252   8495   -471  -1578    455
ATOM    230  OD1 ASN A  55     -22.421 -12.605 -25.079  1.00 74.92           O  
ANISOU  230  OD1 ASN A  55    12371   7419   8677   -391  -1595    437
ATOM    231  ND2 ASN A  55     -24.309 -12.447 -26.229  1.00 74.43           N  
ANISOU  231  ND2 ASN A  55    12163   7455   8663   -752  -1691    576
ATOM    232  H   ASN A  55     -19.731 -11.533 -25.345  1.00 63.42           H  
ATOM    233  HA  ASN A  55     -20.424 -12.389 -27.276  1.00 66.54           H  
ATOM    234  HB3 ASN A  55     -22.658 -11.817 -28.137  1.00 68.74           H  
ATOM    235  HB2 ASN A  55     -22.726 -10.377 -27.165  1.00 68.74           H  
ATOM    236 HD22 ASN A  55     -24.796 -12.987 -25.533  1.00 74.43           H  
ATOM    237 HD21 ASN A  55     -24.795 -12.145 -27.062  1.00 74.43           H  
ATOM    238  N   THR A  56     -19.121  -9.880 -28.247  1.00 69.80           N  
ANISOU  238  N   THR A  56    11338   7087   8097    447   -982     99
ATOM    239  CA  THR A  56     -18.425  -9.106 -29.279  1.00 71.81           C  
ANISOU  239  CA  THR A  56    11515   7426   8345    618   -858     38
ATOM    240  C   THR A  56     -17.748  -9.987 -30.362  1.00 73.58           C  
ANISOU  240  C   THR A  56    12055   7497   8403    848   -936    -17
ATOM    241  O   THR A  56     -17.145  -9.458 -31.296  1.00 74.06           O  
ANISOU  241  O   THR A  56    12075   7635   8431   1010   -845    -62
ATOM    242  CB  THR A  56     -17.336  -8.254 -28.571  1.00 73.11           C  
ANISOU  242  CB  THR A  56    11414   7808   8558    735   -670     12
ATOM    243  OG1 THR A  56     -16.502  -9.076 -27.770  1.00 74.53           O  
ANISOU  243  OG1 THR A  56    11694   7980   8644    909   -676     -3
ATOM    244  CG2 THR A  56     -17.932  -7.217 -27.606  1.00 72.73           C  
ANISOU  244  CG2 THR A  56    11088   7895   8650    542   -591     51
ATOM    245  H   THR A  56     -18.695  -9.792 -27.336  1.00 69.80           H  
ATOM    246  HA  THR A  56     -19.139  -8.444 -29.779  1.00 71.81           H  
ATOM    247  HB  THR A  56     -16.708  -7.739 -29.304  1.00 73.11           H  
ATOM    248  HG1 THR A  56     -15.664  -8.612 -27.668  1.00 74.53           H  
ATOM    249 HG21 THR A  56     -17.145  -6.753 -27.021  1.00 72.73           H  
ATOM    250 HG22 THR A  56     -18.464  -6.433 -28.147  1.00 72.73           H  
ATOM    251 HG23 THR A  56     -18.627  -7.657 -26.894  1.00 72.73           H  
ATOM    252  N   TYR A  66     -16.941  -1.824 -44.446  1.00 74.06           N  
ANISOU  252  N   TYR A  66    11548   8310   8281   1463   -311   -193
ATOM    253  CA  TYR A  66     -18.107  -0.977 -44.725  1.00 73.29           C  
ANISOU  253  CA  TYR A  66    11378   8150   8318   1241   -336   -166
ATOM    254  C   TYR A  66     -17.725   0.497 -44.934  1.00 72.39           C  
ANISOU  254  C   TYR A  66    11024   8220   8259   1196   -223   -130
ATOM    255  O   TYR A  66     -18.315   1.140 -45.797  1.00 71.53           O  
ANISOU  255  O   TYR A  66    10917   8108   8154   1163   -230   -123
ATOM    256  CB  TYR A  66     -19.168  -1.085 -43.604  1.00 73.07           C  
ANISOU  256  CB  TYR A  66    11312   8020   8433   1027   -388   -139
ATOM    257  CG  TYR A  66     -19.807  -2.443 -43.326  1.00 73.80           C  
ANISOU  257  CG  TYR A  66    11650   7911   8479    994   -535   -149
ATOM    258  CD1 TYR A  66     -19.837  -3.483 -44.283  1.00 74.51           C  
ANISOU  258  CD1 TYR A  66    12025   7875   8411   1142   -629   -191
ATOM    259  CD2 TYR A  66     -20.425  -2.650 -42.075  1.00 74.52           C  
ANISOU  259  CD2 TYR A  66    11706   7940   8667    812   -589   -111
ATOM    260  CE1 TYR A  66     -20.470  -4.706 -43.978  1.00 75.24           C  
ANISOU  260  CE1 TYR A  66    12384   7760   8444   1090   -788   -193
ATOM    261  CE2 TYR A  66     -21.041  -3.877 -41.766  1.00 75.36           C  
ANISOU  261  CE2 TYR A  66    12042   7871   8719    749   -741   -101
ATOM    262  CZ  TYR A  66     -21.068  -4.905 -42.723  1.00 76.33           C  
ANISOU  262  CZ  TYR A  66    12471   7845   8685    876   -849   -141
ATOM    263  OH  TYR A  66     -21.678  -6.089 -42.446  1.00 78.03           O  
ANISOU  263  OH  TYR A  66    12954   7863   8831    791  -1024   -124
ATOM    264  H   TYR A  66     -16.895  -2.224 -43.514  1.00 74.06           H  
ATOM    265  HA  TYR A  66     -18.547  -1.308 -45.667  1.00 73.29           H  
ATOM    266  HB3 TYR A  66     -19.989  -0.406 -43.836  1.00 73.07           H  
ATOM    267  HB2 TYR A  66     -18.740  -0.720 -42.670  1.00 73.07           H  
ATOM    268  HD1 TYR A  66     -19.407  -3.349 -45.264  1.00 74.51           H  
ATOM    269  HD2 TYR A  66     -20.405  -1.880 -41.317  1.00 74.52           H  
ATOM    270  HE1 TYR A  66     -20.525  -5.494 -44.713  1.00 75.24           H  
ATOM    271  HE2 TYR A  66     -21.477  -4.017 -40.785  1.00 75.36           H  
ATOM    272  HH  TYR A  66     -22.074  -6.091 -41.568  1.00 78.03           H  
ATOM    273  N   TYR A  67     -16.694   0.978 -44.223  1.00 72.43           N  
ANISOU  273  N   TYR A  67    10843   8390   8288   1200   -127   -104
ATOM    274  CA  TYR A  67     -16.158   2.329 -44.397  1.00 72.88           C  
ANISOU  274  CA  TYR A  67    10687   8623   8380   1131    -35    -56
ATOM    275  C   TYR A  67     -15.590   2.593 -45.814  1.00 71.40           C  
ANISOU  275  C   TYR A  67    10495   8551   8082   1235     -8    -42
ATOM    276  O   TYR A  67     -15.597   3.750 -46.232  1.00 71.46           O  
ANISOU  276  O   TYR A  67    10378   8637   8137   1126     28     -1
ATOM    277  CB  TYR A  67     -15.135   2.634 -43.275  1.00 73.71           C  
ANISOU  277  CB  TYR A  67    10632   8896   8477   1135     43    -21
ATOM    278  CG  TYR A  67     -13.709   2.122 -43.460  1.00 75.77           C  
ANISOU  278  CG  TYR A  67    10862   9361   8566   1346     97     -1
ATOM    279  CD1 TYR A  67     -13.412   0.744 -43.395  1.00 77.29           C  
ANISOU  279  CD1 TYR A  67    11205   9514   8649   1547     66    -42
ATOM    280  CD2 TYR A  67     -12.668   3.043 -43.699  1.00 77.44           C  
ANISOU  280  CD2 TYR A  67    10893   9822   8710   1344    173     70
ATOM    281  CE1 TYR A  67     -12.094   0.296 -43.619  1.00 78.64           C  
ANISOU  281  CE1 TYR A  67    11342   9900   8640   1781    123    -18
ATOM    282  CE2 TYR A  67     -11.352   2.598 -43.917  1.00 78.68           C  
ANISOU  282  CE2 TYR A  67    10986  10222   8689   1546    228    110
ATOM    283  CZ  TYR A  67     -11.067   1.220 -43.897  1.00 79.71           C  
ANISOU  283  CZ  TYR A  67    11261  10320   8705   1784    209     63
ATOM    284  OH  TYR A  67      -9.810   0.773 -44.175  1.00 81.00           O  
ANISOU  284  OH  TYR A  67    11358  10748   8669   2024    270    107
ATOM    285  H   TYR A  67     -16.231   0.386 -43.545  1.00 72.43           H  
ATOM    286  HA  TYR A  67     -16.993   3.022 -44.274  1.00 72.88           H  
ATOM    287  HB3 TYR A  67     -15.515   2.313 -42.305  1.00 73.71           H  
ATOM    288  HB2 TYR A  67     -15.073   3.720 -43.199  1.00 73.71           H  
ATOM    289  HD1 TYR A  67     -14.181   0.020 -43.174  1.00 77.29           H  
ATOM    290  HD2 TYR A  67     -12.874   4.099 -43.716  1.00 77.44           H  
ATOM    291  HE1 TYR A  67     -11.866  -0.762 -43.574  1.00 78.64           H  
ATOM    292  HE2 TYR A  67     -10.573   3.320 -44.113  1.00 78.68           H  
ATOM    293  HH  TYR A  67      -9.114   1.414 -44.009  1.00 81.00           H  
ATOM    294  N   ASN A  68     -15.153   1.537 -46.527  1.00 69.55           N  
ANISOU  294  N   ASN A  68    10418   8317   7692   1451    -35    -77
ATOM    295  CA  ASN A  68     -14.622   1.601 -47.896  1.00 68.74           C  
ANISOU  295  CA  ASN A  68    10333   8339   7448   1600    -10    -69
ATOM    296  C   ASN A  68     -15.707   1.281 -48.932  1.00 66.31           C  
ANISOU  296  C   ASN A  68    10229   7840   7125   1603   -101   -115
ATOM    297  O   ASN A  68     -15.786   1.975 -49.938  1.00 66.57           O  
ANISOU  297  O   ASN A  68    10225   7943   7126   1602    -84    -96
ATOM    298  CB  ASN A  68     -13.457   0.589 -48.081  1.00 71.64           C  
ANISOU  298  CB  ASN A  68    10750   8859   7612   1889     26    -78
ATOM    299  CG  ASN A  68     -12.120   1.035 -47.499  1.00 77.38           C  
ANISOU  299  CG  ASN A  68    11221   9906   8275   1926    136      5
ATOM    300  OD1 ASN A  68     -11.751   2.199 -47.601  1.00 79.85           O  
ANISOU  300  OD1 ASN A  68    11346  10373   8623   1789    184     74
ATOM    301  ND2 ASN A  68     -11.367   0.113 -46.909  1.00 78.37           N  
ANISOU  301  ND2 ASN A  68    11343  10146   8289   2109    168      9
ATOM    302  H   ASN A  68     -15.252   0.613 -46.127  1.00 69.55           H  
ATOM    303  HA  ASN A  68     -14.250   2.614 -48.054  1.00 68.74           H  
ATOM    304  HB3 ASN A  68     -13.269   0.450 -49.149  1.00 71.64           H  
ATOM    305  HB2 ASN A  68     -13.728  -0.396 -47.702  1.00 71.64           H  
ATOM    306 HD22 ASN A  68     -10.520   0.392 -46.429  1.00 78.37           H  
ATOM    307 HD21 ASN A  68     -11.638  -0.858 -46.857  1.00 78.37           H  
ATOM    308  N   ARG A  69     -16.483   0.216 -48.684  1.00 63.99           N  
ANISOU  308  N   ARG A  69    10161   7317   6835   1608   -205   -166
ATOM    309  CA  ARG A  69     -17.451  -0.348 -49.634  1.00 62.18           C  
ANISOU  309  CA  ARG A  69    10162   6894   6570   1595   -316   -202
ATOM    310  C   ARG A  69     -18.765   0.442 -49.743  1.00 58.06           C  
ANISOU  310  C   ARG A  69     9563   6284   6213   1337   -351   -168
ATOM    311  O   ARG A  69     -19.581   0.104 -50.599  1.00 57.83           O  
ANISOU  311  O   ARG A  69     9664   6151   6157   1305   -425   -176
ATOM    312  CB  ARG A  69     -17.798  -1.781 -49.192  1.00 65.11           C  
ANISOU  312  CB  ARG A  69    10817   7041   6880   1645   -440   -250
ATOM    313  CG  ARG A  69     -16.640  -2.791 -49.207  1.00 70.45           C  
ANISOU  313  CG  ARG A  69    11610   7776   7381   1928   -418   -288
ATOM    314  CD  ARG A  69     -16.901  -4.004 -48.302  1.00 75.24           C  
ANISOU  314  CD  ARG A  69    12422   8189   7978   1923   -520   -316
ATOM    315  NE  ARG A  69     -18.199  -4.671 -48.551  1.00 78.01           N  
ANISOU  315  NE  ARG A  69    13074   8259   8308   1814   -694   -338
ATOM    316  CZ  ARG A  69     -18.836  -5.513 -47.720  1.00 78.89           C  
ANISOU  316  CZ  ARG A  69    13360   8175   8441   1704   -817   -337
ATOM    317  NH1 ARG A  69     -20.026  -6.000 -48.073  1.00 78.71           N  
ANISOU  317  NH1 ARG A  69    13607   7917   8384   1571   -989   -336
ATOM    318  NH2 ARG A  69     -18.314  -5.859 -46.538  1.00 77.27           N1+
ANISOU  318  NH2 ARG A  69    13060   8018   8283   1710   -776   -327
ATOM    319  H   ARG A  69     -16.360  -0.283 -47.810  1.00 63.99           H  
ATOM    320  HA  ARG A  69     -17.014  -0.374 -50.633  1.00 62.18           H  
ATOM    321  HB3 ARG A  69     -18.564  -2.172 -49.863  1.00 65.11           H  
ATOM    322  HB2 ARG A  69     -18.249  -1.744 -48.200  1.00 65.11           H  
ATOM    323  HG3 ARG A  69     -15.756  -2.302 -48.796  1.00 70.45           H  
ATOM    324  HG2 ARG A  69     -16.351  -3.076 -50.219  1.00 70.45           H  
ATOM    325  HD3 ARG A  69     -16.794  -3.713 -47.261  1.00 75.24           H  
ATOM    326  HD2 ARG A  69     -16.131  -4.752 -48.505  1.00 75.24           H  
ATOM    327 HH22 ARG A  69     -18.793  -6.446 -45.868  1.00 77.27           H  
ATOM    328 HH21 ARG A  69     -17.370  -5.584 -46.295  1.00 77.27           H  
ATOM    329 HH12 ARG A  69     -20.563  -6.626 -47.486  1.00 78.71           H  
ATOM    330 HH11 ARG A  69     -20.460  -5.710 -48.944  1.00 78.71           H  
ATOM    331  HE  ARG A  69     -18.599  -4.465 -49.467  1.00 78.01           H  
ATOM    332  N   SER A  70     -18.999   1.388 -48.827  1.00 55.22           N  
ANISOU  332  N   SER A  70     9010   5962   6010   1166   -306   -129
ATOM    333  CA  SER A  70     -20.218   2.184 -48.773  1.00 52.85           C  
ANISOU  333  CA  SER A  70     8625   5599   5857    953   -330    -91
ATOM    334  C   SER A  70     -20.338   3.135 -49.975  1.00 51.98           C  
ANISOU  334  C   SER A  70     8432   5561   5758    920   -296    -65
ATOM    335  O   SER A  70     -19.328   3.643 -50.460  1.00 51.84           O  
ANISOU  335  O   SER A  70     8327   5699   5672   1013   -219    -56
ATOM    336  CB  SER A  70     -20.278   2.906 -47.405  1.00 51.71           C  
ANISOU  336  CB  SER A  70     8302   5502   5843    836   -274    -63
ATOM    337  OG  SER A  70     -21.325   3.855 -47.271  1.00 51.96           O  
ANISOU  337  OG  SER A  70     8244   5496   6003    667   -287    -25
ATOM    338  H   SER A  70     -18.271   1.628 -48.171  1.00 55.22           H  
ATOM    339  HA  SER A  70     -21.042   1.485 -48.821  1.00 52.85           H  
ATOM    340  HB3 SER A  70     -19.327   3.402 -47.213  1.00 51.71           H  
ATOM    341  HB2 SER A  70     -20.420   2.165 -46.618  1.00 51.71           H  
ATOM    342  HG  SER A  70     -22.058   3.442 -46.774  1.00 51.96           H  
ATOM    343  N   THR A  71     -21.582   3.424 -50.369  1.00 50.29           N  
ANISOU  343  N   THR A  71     8242   5248   5617    783   -359    -41
ATOM    344  CA  THR A  71     -21.912   4.506 -51.291  1.00 49.29           C  
ANISOU  344  CA  THR A  71     8026   5178   5524    729   -330     -9
ATOM    345  C   THR A  71     -21.720   5.890 -50.629  1.00 48.69           C  
ANISOU  345  C   THR A  71     7743   5200   5557    641   -243     29
ATOM    346  O   THR A  71     -21.664   6.891 -51.333  1.00 49.42           O  
ANISOU  346  O   THR A  71     7755   5362   5661    611   -206     59
ATOM    347  CB  THR A  71     -23.378   4.385 -51.784  1.00 50.08           C  
ANISOU  347  CB  THR A  71     8214   5158   5658    618   -427     15
ATOM    348  OG1 THR A  71     -24.312   4.508 -50.724  1.00 50.15           O  
ANISOU  348  OG1 THR A  71     8143   5126   5785    476   -450     55
ATOM    349  CG2 THR A  71     -23.670   3.075 -52.518  1.00 49.84           C  
ANISOU  349  CG2 THR A  71     8428   4999   5508    673   -539    -19
ATOM    350  H   THR A  71     -22.379   2.946 -49.954  1.00 50.29           H  
ATOM    351  HA  THR A  71     -21.242   4.445 -52.149  1.00 49.29           H  
ATOM    352  HB  THR A  71     -23.569   5.203 -52.482  1.00 50.08           H  
ATOM    353  HG1 THR A  71     -24.508   5.441 -50.617  1.00 50.15           H  
ATOM    354 HG21 THR A  71     -24.698   3.068 -52.887  1.00 49.84           H  
ATOM    355 HG22 THR A  71     -23.016   2.967 -53.387  1.00 49.84           H  
ATOM    356 HG23 THR A  71     -23.538   2.203 -51.877  1.00 49.84           H  
ATOM    357  N   SER A  72     -21.575   5.930 -49.303  1.00 47.13           N  
ANISOU  357  N   SER A  72     7480   5001   5426    601   -218     29
ATOM    358  CA  SER A  72     -21.273   7.108 -48.507  1.00 46.24           C  
ANISOU  358  CA  SER A  72     7218   4960   5391    531   -149     56
ATOM    359  C   SER A  72     -20.051   6.816 -47.614  1.00 46.84           C  
ANISOU  359  C   SER A  72     7253   5126   5418    600    -97     41
ATOM    360  O   SER A  72     -20.226   6.698 -46.399  1.00 47.00           O  
ANISOU  360  O   SER A  72     7246   5118   5494    564    -92     34
ATOM    361  CB  SER A  72     -22.544   7.475 -47.711  1.00 44.80           C  
ANISOU  361  CB  SER A  72     7000   4698   5322    426   -172     73
ATOM    362  OG  SER A  72     -23.086   6.336 -47.047  1.00 41.51           O  
ANISOU  362  OG  SER A  72     6648   4215   4909    424   -224     59
ATOM    363  H   SER A  72     -21.614   5.061 -48.776  1.00 47.13           H  
ATOM    364  HA  SER A  72     -21.005   7.949 -49.144  1.00 46.24           H  
ATOM    365  HB3 SER A  72     -23.286   7.905 -48.382  1.00 44.80           H  
ATOM    366  HB2 SER A  72     -22.323   8.253 -46.977  1.00 44.80           H  
ATOM    367  HG  SER A  72     -22.333   5.824 -46.718  1.00 41.51           H  
ATOM    368  N   PRO A  73     -18.858   6.592 -48.213  1.00 46.60           N  
ANISOU  368  N   PRO A  73     7212   5225   5268    711    -59     43
ATOM    369  CA  PRO A  73     -17.705   6.084 -47.456  1.00 46.84           C  
ANISOU  369  CA  PRO A  73     7197   5367   5234    795    -12     41
ATOM    370  C   PRO A  73     -17.151   7.118 -46.461  1.00 46.93           C  
ANISOU  370  C   PRO A  73     7060   5467   5302    682     43     83
ATOM    371  O   PRO A  73     -17.312   8.326 -46.671  1.00 46.69           O  
ANISOU  371  O   PRO A  73     6976   5430   5335    559     48    117
ATOM    372  CB  PRO A  73     -16.709   5.703 -48.559  1.00 47.58           C  
ANISOU  372  CB  PRO A  73     7305   5609   5165    959     14     49
ATOM    373  CG  PRO A  73     -16.996   6.683 -49.686  1.00 47.95           C  
ANISOU  373  CG  PRO A  73     7317   5683   5220    888     12     82
ATOM    374  CD  PRO A  73     -18.510   6.845 -49.616  1.00 46.23           C  
ANISOU  374  CD  PRO A  73     7180   5257   5128    775    -54     58
ATOM    375  HA  PRO A  73     -17.993   5.195 -46.896  1.00 46.84           H  
ATOM    376  HB3 PRO A  73     -16.922   4.685 -48.894  1.00 47.58           H  
ATOM    377  HB2 PRO A  73     -15.672   5.713 -48.227  1.00 47.58           H  
ATOM    378  HG3 PRO A  73     -16.643   6.345 -50.663  1.00 47.95           H  
ATOM    379  HG2 PRO A  73     -16.516   7.633 -49.459  1.00 47.95           H  
ATOM    380  HD2 PRO A  73     -18.831   7.827 -49.961  1.00 46.23           H  
ATOM    381  HD3 PRO A  73     -18.978   6.098 -50.251  1.00 46.23           H  
ATOM    382  N   TRP A  74     -16.509   6.636 -45.394  1.00 46.86           N  
ANISOU  382  N   TRP A  74     7011   5528   5267    723     73     82
ATOM    383  CA  TRP A  74     -15.989   7.478 -44.323  1.00 47.43           C  
ANISOU  383  CA  TRP A  74     6964   5678   5378    610    114    123
ATOM    384  C   TRP A  74     -14.562   7.089 -43.963  1.00 49.42           C  
ANISOU  384  C   TRP A  74     7130   6129   5517    693    163    158
ATOM    385  O   TRP A  74     -14.063   6.052 -44.392  1.00 49.69           O  
ANISOU  385  O   TRP A  74     7212   6216   5452    867    167    136
ATOM    386  CB  TRP A  74     -16.936   7.461 -43.104  1.00 46.45           C  
ANISOU  386  CB  TRP A  74     6866   5401   5380    525     92     90
ATOM    387  CG  TRP A  74     -17.137   6.182 -42.343  1.00 46.14           C  
ANISOU  387  CG  TRP A  74     6887   5303   5341    604     72     48
ATOM    388  CD1 TRP A  74     -16.420   5.775 -41.268  1.00 46.67           C  
ANISOU  388  CD1 TRP A  74     6907   5434   5392    624    100     50
ATOM    389  CD2 TRP A  74     -18.116   5.130 -42.588  1.00 45.72           C  
ANISOU  389  CD2 TRP A  74     6963   5102   5307    644      4      8
ATOM    390  NE1 TRP A  74     -16.921   4.573 -40.805  1.00 46.41           N  
ANISOU  390  NE1 TRP A  74     6971   5296   5365    686     56     10
ATOM    391  CE2 TRP A  74     -17.968   4.124 -41.585  1.00 46.48           C  
ANISOU  391  CE2 TRP A  74     7094   5171   5395    685    -10    -13
ATOM    392  CE3 TRP A  74     -19.133   4.932 -43.550  1.00 46.17           C  
ANISOU  392  CE3 TRP A  74     7117   5051   5373    638    -57     -3
ATOM    393  CZ2 TRP A  74     -18.792   2.986 -41.536  1.00 47.09           C  
ANISOU  393  CZ2 TRP A  74     7312   5109   5472    705    -92    -40
ATOM    394  CZ3 TRP A  74     -19.960   3.794 -43.519  1.00 46.71           C  
ANISOU  394  CZ3 TRP A  74     7315   4990   5444    645   -138    -25
ATOM    395  CH2 TRP A  74     -19.789   2.820 -42.516  1.00 47.20           C  
ANISOU  395  CH2 TRP A  74     7424   5019   5493    674   -160    -42
ATOM    396  H   TRP A  74     -16.271   5.650 -45.360  1.00 46.86           H  
ATOM    397  HA  TRP A  74     -15.923   8.503 -44.682  1.00 47.43           H  
ATOM    398  HB3 TRP A  74     -17.918   7.796 -43.433  1.00 46.45           H  
ATOM    399  HB2 TRP A  74     -16.613   8.206 -42.376  1.00 46.45           H  
ATOM    400  HD1 TRP A  74     -15.610   6.339 -40.825  1.00 46.67           H  
ATOM    401  HE1 TRP A  74     -16.572   4.104 -39.974  1.00 46.41           H  
ATOM    402  HE3 TRP A  74     -19.274   5.663 -44.329  1.00 46.17           H  
ATOM    403  HZ2 TRP A  74     -18.667   2.249 -40.756  1.00 47.09           H  
ATOM    404  HZ3 TRP A  74     -20.727   3.672 -44.271  1.00 46.71           H  
ATOM    405  HH2 TRP A  74     -20.418   1.945 -42.495  1.00 47.20           H  
ATOM    406  N   ASN A  75     -13.921   7.967 -43.196  1.00 50.01           N  
ANISOU  406  N   ASN A  75     7090   6319   5594    573    193    217
ATOM    407  CA  ASN A  75     -12.628   7.747 -42.556  1.00 50.84           C  
ANISOU  407  CA  ASN A  75     7086   6633   5596    619    238    270
ATOM    408  C   ASN A  75     -12.854   7.955 -41.058  1.00 51.28           C  
ANISOU  408  C   ASN A  75     7126   6615   5745    505    237    258
ATOM    409  O   ASN A  75     -13.698   8.780 -40.698  1.00 50.51           O  
ANISOU  409  O   ASN A  75     7073   6357   5760    372    210    235
ATOM    410  CB  ASN A  75     -11.580   8.767 -43.064  1.00 52.98           C  
ANISOU  410  CB  ASN A  75     7223   7152   5755    546    262    380
ATOM    411  CG  ASN A  75     -11.293   8.685 -44.565  1.00 58.55           C  
ANISOU  411  CG  ASN A  75     7927   7962   6358    654    267    402
ATOM    412  OD1 ASN A  75     -11.410   7.633 -45.187  1.00 61.92           O  
ANISOU  412  OD1 ASN A  75     8340   8397   6792    535    247    445
ATOM    413  ND2 ASN A  75     -10.926   9.795 -45.185  1.00 58.90           N  
ANISOU  413  ND2 ASN A  75     7999   8085   6294    889    291    373
ATOM    414  H   ASN A  75     -14.411   8.808 -42.893  1.00 50.01           H  
ATOM    415  HA  ASN A  75     -12.275   6.726 -42.722  1.00 50.84           H  
ATOM    416  HB3 ASN A  75     -10.639   8.615 -42.531  1.00 52.98           H  
ATOM    417  HB2 ASN A  75     -11.905   9.782 -42.824  1.00 52.98           H  
ATOM    418 HD22 ASN A  75     -10.715   9.771 -46.171  1.00 58.90           H  
ATOM    419 HD21 ASN A  75     -10.847  10.664 -44.677  1.00 58.90           H  
ATOM    420  N   LEU A  76     -12.104   7.234 -40.216  1.00 51.82           N  
ANISOU  420  N   LEU A  76     7134   6802   5754    572    267    275
ATOM    421  CA  LEU A  76     -12.131   7.439 -38.767  1.00 52.26           C  
ANISOU  421  CA  LEU A  76     7167   6806   5881    469    268    269
ATOM    422  C   LEU A  76     -11.009   8.419 -38.389  1.00 52.83           C  
ANISOU  422  C   LEU A  76     7118   7059   5895    315    284    366
ATOM    423  O   LEU A  76      -9.889   8.287 -38.892  1.00 52.53           O  
ANISOU  423  O   LEU A  76     6966   7273   5722    352    312    453
ATOM    424  CB  LEU A  76     -11.950   6.095 -38.026  1.00 52.67           C  
ANISOU  424  CB  LEU A  76     7244   6853   5915    616    278    228
ATOM    425  CG  LEU A  76     -13.104   5.086 -38.218  1.00 53.88           C  
ANISOU  425  CG  LEU A  76     7552   6784   6136    709    233    138
ATOM    426  CD1 LEU A  76     -12.775   3.757 -37.516  1.00 54.16           C  
ANISOU  426  CD1 LEU A  76     7629   6804   6144    824    227    110
ATOM    427  CD2 LEU A  76     -14.465   5.628 -37.734  1.00 54.04           C  
ANISOU  427  CD2 LEU A  76     7625   6601   6307    559    196    100
ATOM    428  H   LEU A  76     -11.368   6.630 -40.549  1.00 51.82           H  
ATOM    429  HA  LEU A  76     -13.088   7.864 -38.469  1.00 52.26           H  
ATOM    430  HB3 LEU A  76     -11.852   6.297 -36.959  1.00 52.67           H  
ATOM    431  HB2 LEU A  76     -11.005   5.639 -38.327  1.00 52.67           H  
ATOM    432  HG  LEU A  76     -13.192   4.866 -39.284  1.00 53.88           H  
ATOM    433 HD11 LEU A  76     -13.522   2.995 -37.738  1.00 54.16           H  
ATOM    434 HD12 LEU A  76     -11.811   3.364 -37.834  1.00 54.16           H  
ATOM    435 HD13 LEU A  76     -12.743   3.875 -36.432  1.00 54.16           H  
ATOM    436 HD21 LEU A  76     -15.054   4.863 -37.224  1.00 54.04           H  
ATOM    437 HD22 LEU A  76     -14.357   6.457 -37.034  1.00 54.04           H  
ATOM    438 HD23 LEU A  76     -15.063   5.985 -38.573  1.00 54.04           H  
ATOM    439  N   HIS A  77     -11.322   9.375 -37.514  1.00 54.01           N  
ANISOU  439  N   HIS A  77     7299   7093   6129    142    260    361
ATOM    440  CA  HIS A  77     -10.371  10.324 -36.943  1.00 55.16           C  
ANISOU  440  CA  HIS A  77     7373   7371   6215    -44    250    455
ATOM    441  C   HIS A  77     -10.371  10.197 -35.416  1.00 53.11           C  
ANISOU  441  C   HIS A  77     7110   7074   5996    -98    254    438
ATOM    442  O   HIS A  77     -11.401   9.861 -34.837  1.00 52.04           O  
ANISOU  442  O   HIS A  77     7064   6738   5972    -76    247    350
ATOM    443  CB  HIS A  77     -10.715  11.748 -37.407  1.00 58.55           C  
ANISOU  443  CB  HIS A  77     7874   7709   6662   -217    199    484
ATOM    444  CG  HIS A  77     -10.636  11.951 -38.901  1.00 66.20           C  
ANISOU  444  CG  HIS A  77     8812   8778   7564   -175    198    528
ATOM    445  ND1 HIS A  77      -9.634  11.413 -39.691  1.00 69.55           N  
ANISOU  445  ND1 HIS A  77     9093   9487   7846    -94    234    613
ATOM    446  CD2 HIS A  77     -11.474  12.608 -39.770  1.00 68.71           C  
ANISOU  446  CD2 HIS A  77     9218   8957   7932   -177    171    495
ATOM    447  CE1 HIS A  77      -9.873  11.792 -40.947  1.00 70.77           C  
ANISOU  447  CE1 HIS A  77     9257   9664   7967    -62    225    628
ATOM    448  NE2 HIS A  77     -10.969  12.535 -41.074  1.00 70.79           N  
ANISOU  448  NE2 HIS A  77     9399   9411   8088   -122    185    560
ATOM    449  H   HIS A  77     -12.279   9.447 -37.169  1.00 54.01           H  
ATOM    450  HA  HIS A  77      -9.359  10.085 -37.276  1.00 55.16           H  
ATOM    451  HB3 HIS A  77     -10.046  12.468 -36.932  1.00 58.55           H  
ATOM    452  HB2 HIS A  77     -11.721  12.007 -37.071  1.00 58.55           H  
ATOM    453  HD1 HIS A  77      -8.900  10.786 -39.390  1.00 69.55           H  
ATOM    454  HD2 HIS A  77     -12.384  13.137 -39.540  1.00 68.71           H  
ATOM    455  HE1 HIS A  77      -9.237  11.522 -41.778  1.00 70.77           H  
ATOM    456  N   ARG A  78      -9.193  10.405 -34.820  1.00 52.54           N  
ANISOU  456  N   ARG A  78     6919   7225   5821   -156    269    530
ATOM    457  CA  ARG A  78      -8.891  10.086 -33.430  1.00 52.83           C  
ANISOU  457  CA  ARG A  78     6925   7280   5867   -208    276    533
ATOM    458  C   ARG A  78      -9.094  11.333 -32.562  1.00 53.12           C  
ANISOU  458  C   ARG A  78     7054   7184   5946   -429    224    538
ATOM    459  O   ARG A  78      -8.261  12.235 -32.610  1.00 53.69           O  
ANISOU  459  O   ARG A  78     7128   7327   5943   -606    180    627
ATOM    460  CB  ARG A  78      -7.426   9.587 -33.386  1.00 54.42           C  
ANISOU  460  CB  ARG A  78     6951   7810   5916   -193    306    655
ATOM    461  CG  ARG A  78      -6.995   8.951 -32.057  1.00 57.45           C  
ANISOU  461  CG  ARG A  78     7283   8244   6302   -159    331    650
ATOM    462  CD  ARG A  78      -5.553   8.408 -32.136  1.00 60.32           C  
ANISOU  462  CD  ARG A  78     7457   8965   6498   -114    366    782
ATOM    463  NE  ARG A  78      -5.026   7.993 -30.828  1.00 63.81           N  
ANISOU  463  NE  ARG A  78     7844   9469   6933    -60    392    782
ATOM    464  CZ  ARG A  78      -4.518   8.779 -29.870  1.00 65.56           C  
ANISOU  464  CZ  ARG A  78     8002   9787   7120   -250    372    859
ATOM    465  NH1 ARG A  78      -4.149   8.224 -28.721  1.00 65.30           N  
ANISOU  465  NH1 ARG A  78     7915   9816   7081   -182    399    858
ATOM    466  NH2 ARG A  78      -4.406  10.100 -30.013  1.00 65.89           N1+
ANISOU  466  NH2 ARG A  78     8049   9860   7124   -518    314    944
ATOM    467  H   ARG A  78      -8.440  10.815 -35.346  1.00 52.54           H  
ATOM    468  HA  ARG A  78      -9.554   9.283 -33.092  1.00 52.83           H  
ATOM    469  HB3 ARG A  78      -6.748  10.406 -33.629  1.00 54.42           H  
ATOM    470  HB2 ARG A  78      -7.277   8.849 -34.169  1.00 54.42           H  
ATOM    471  HG3 ARG A  78      -7.670   8.102 -31.921  1.00 57.45           H  
ATOM    472  HG2 ARG A  78      -7.152   9.608 -31.198  1.00 57.45           H  
ATOM    473  HD3 ARG A  78      -4.873   9.052 -32.694  1.00 60.32           H  
ATOM    474  HD2 ARG A  78      -5.591   7.468 -32.686  1.00 60.32           H  
ATOM    475 HH22 ARG A  78      -4.131  10.660 -29.179  1.00 65.89           H  
ATOM    476 HH21 ARG A  78      -4.693  10.611 -30.830  1.00 65.89           H  
ATOM    477 HH12 ARG A  78      -4.075   8.828 -27.875  1.00 65.30           H  
ATOM    478 HH11 ARG A  78      -4.094   7.238 -28.539  1.00 65.30           H  
ATOM    479  HE  ARG A  78      -5.162   7.016 -30.612  1.00 63.81           H  
ATOM    480  N   ASN A  79     -10.179  11.352 -31.789  1.00 53.53           N  
ANISOU  480  N   ASN A  79     7199   7036   6104   -415    222    446
ATOM    481  CA  ASN A  79     -10.492  12.367 -30.781  1.00 55.03           C  
ANISOU  481  CA  ASN A  79     7505   7084   6319   -581    175    434
ATOM    482  C   ASN A  79      -9.887  11.857 -29.467  1.00 54.52           C  
ANISOU  482  C   ASN A  79     7380   7094   6239   -610    193    445
ATOM    483  O   ASN A  79     -10.347  10.821 -28.984  1.00 53.29           O  
ANISOU  483  O   ASN A  79     7206   6888   6155   -476    231    375
ATOM    484  CB  ASN A  79     -12.041  12.497 -30.723  1.00 57.95           C  
ANISOU  484  CB  ASN A  79     8017   7194   6809   -504    169    320
ATOM    485  CG  ASN A  79     -12.632  13.484 -29.709  1.00 65.42           C  
ANISOU  485  CG  ASN A  79     9100   7979   7779   -592    135    279
ATOM    486  OD1 ASN A  79     -12.042  13.807 -28.679  1.00 66.78           O  
ANISOU  486  OD1 ASN A  79     9290   8195   7888   -729    108    323
ATOM    487  ND2 ASN A  79     -13.860  13.922 -29.942  1.00 68.55           N  
ANISOU  487  ND2 ASN A  79     9601   8192   8254   -502    134    196
ATOM    488  H   ASN A  79     -10.783  10.532 -31.756  1.00 53.53           H  
ATOM    489  HA  ASN A  79     -10.055  13.337 -31.041  1.00 55.03           H  
ATOM    490  HB3 ASN A  79     -12.500  11.529 -30.527  1.00 57.95           H  
ATOM    491  HB2 ASN A  79     -12.395  12.802 -31.709  1.00 57.95           H  
ATOM    492 HD22 ASN A  79     -14.303  14.628 -29.386  1.00 68.55           H  
ATOM    493 HD21 ASN A  79     -14.426  13.527 -30.716  1.00 68.55           H  
ATOM    494  N   GLU A  80      -8.879  12.542 -28.915  1.00 54.69           N  
ANISOU  494  N   GLU A  80     7379   7237   6163   -801    155    542
ATOM    495  CA  GLU A  80      -8.302  12.215 -27.612  1.00 55.25           C  
ANISOU  495  CA  GLU A  80     7390   7392   6209   -849    166    566
ATOM    496  C   GLU A  80      -8.545  13.353 -26.611  1.00 54.90           C  
ANISOU  496  C   GLU A  80     7502   7191   6164  -1023    106    547
ATOM    497  O   GLU A  80      -8.481  14.523 -26.981  1.00 54.67           O  
ANISOU  497  O   GLU A  80     7587   7119   6066  -1208     31    602
ATOM    498  CB  GLU A  80      -6.814  11.858 -27.743  1.00 58.37           C  
ANISOU  498  CB  GLU A  80     7599   8114   6464   -916    174    713
ATOM    499  CG  GLU A  80      -6.193  11.377 -26.407  1.00 63.08           C  
ANISOU  499  CG  GLU A  80     8108   8824   7035   -931    196    740
ATOM    500  CD  GLU A  80      -4.849  10.694 -26.584  1.00 70.84           C  
ANISOU  500  CD  GLU A  80     8893  10163   7859  -1008    201    907
ATOM    501  OE1 GLU A  80      -4.025  11.203 -27.371  1.00 71.82           O  
ANISOU  501  OE1 GLU A  80     8917  10484   7889  -1000    203   1002
ATOM    502  OE2 GLU A  80      -4.709   9.555 -26.096  1.00 73.03           O1-
ANISOU  502  OE2 GLU A  80     9105  10546   8098  -1076    202    953
ATOM    503  H   GLU A  80      -8.558  13.410 -29.320  1.00 54.69           H  
ATOM    504  HA  GLU A  80      -8.785  11.327 -27.218  1.00 55.25           H  
ATOM    505  HB3 GLU A  80      -6.254  12.722 -28.105  1.00 58.37           H  
ATOM    506  HB2 GLU A  80      -6.704  11.081 -28.501  1.00 58.37           H  
ATOM    507  HG3 GLU A  80      -6.879  10.686 -25.916  1.00 63.08           H  
ATOM    508  HG2 GLU A  80      -6.044  12.217 -25.728  1.00 63.08           H  
ATOM    509  N   ASP A  81      -8.799  12.958 -25.360  1.00 54.58           N  
ANISOU  509  N   ASP A  81     7484   7068   6187   -966    132    475
ATOM    510  CA  ASP A  81      -9.173  13.811 -24.235  1.00 54.46           C  
ANISOU  510  CA  ASP A  81     7624   6911   6158  -1097     81    447
ATOM    511  C   ASP A  81      -8.717  13.060 -22.960  1.00 54.98           C  
ANISOU  511  C   ASP A  81     7594   7080   6216  -1105    111    459
ATOM    512  O   ASP A  81      -9.323  12.036 -22.634  1.00 55.20           O  
ANISOU  512  O   ASP A  81     7567   7076   6332   -943    168    385
ATOM    513  CB  ASP A  81     -10.700  14.071 -24.285  1.00 54.93           C  
ANISOU  513  CB  ASP A  81     7855   6707   6309   -985     82    320
ATOM    514  CG  ASP A  81     -11.355  14.923 -23.196  1.00 58.33           C  
ANISOU  514  CG  ASP A  81     8499   6966   6697  -1086     22    284
ATOM    515  OD1 ASP A  81     -10.777  15.167 -22.115  1.00 58.67           O  
ANISOU  515  OD1 ASP A  81     8565   7075   6652  -1259    -24    347
ATOM    516  OD2 ASP A  81     -12.557  15.206 -23.380  1.00 61.00           O1-
ANISOU  516  OD2 ASP A  81     8988   7113   7077   -982     17    195
ATOM    517  H   ASP A  81      -8.844  11.965 -25.158  1.00 54.58           H  
ATOM    518  HA  ASP A  81      -8.685  14.776 -24.340  1.00 54.46           H  
ATOM    519  HB3 ASP A  81     -11.207  13.109 -24.291  1.00 54.93           H  
ATOM    520  HB2 ASP A  81     -10.937  14.522 -25.251  1.00 54.93           H  
ATOM    521  N   PRO A  82      -7.637  13.513 -22.280  1.00 55.20           N  
ANISOU  521  N   PRO A  82     7605   7237   6132  -1310     61    563
ATOM    522  CA  PRO A  82      -7.111  12.814 -21.089  1.00 55.24           C  
ANISOU  522  CA  PRO A  82     7513   7353   6121  -1330     86    585
ATOM    523  C   PRO A  82      -8.003  12.902 -19.833  1.00 54.27           C  
ANISOU  523  C   PRO A  82     7535   7024   6062  -1301     84    473
ATOM    524  O   PRO A  82      -7.865  12.063 -18.935  1.00 54.02           O  
ANISOU  524  O   PRO A  82     7421   7061   6044  -1276    117    469
ATOM    525  CB  PRO A  82      -5.734  13.465 -20.867  1.00 56.42           C  
ANISOU  525  CB  PRO A  82     7621   7700   6115  -1591     15    744
ATOM    526  CG  PRO A  82      -5.878  14.870 -21.434  1.00 56.42           C  
ANISOU  526  CG  PRO A  82     7806   7571   6058  -1753    -76    770
ATOM    527  CD  PRO A  82      -6.819  14.678 -22.619  1.00 55.02           C  
ANISOU  527  CD  PRO A  82     7648   7278   5980  -1555    -30    682
ATOM    528  HA  PRO A  82      -6.979  11.756 -21.312  1.00 55.24           H  
ATOM    529  HB3 PRO A  82      -4.979  12.915 -21.429  1.00 56.42           H  
ATOM    530  HB2 PRO A  82      -5.412  13.471 -19.823  1.00 56.42           H  
ATOM    531  HG3 PRO A  82      -4.928  15.334 -21.708  1.00 56.42           H  
ATOM    532  HG2 PRO A  82      -6.358  15.506 -20.689  1.00 56.42           H  
ATOM    533  HD2 PRO A  82      -7.412  15.580 -22.777  1.00 55.02           H  
ATOM    534  HD3 PRO A  82      -6.258  14.457 -23.529  1.00 55.02           H  
ATOM    535  N   GLU A  83      -8.923  13.875 -19.805  1.00 53.15           N  
ANISOU  535  N   GLU A  83     7605   6643   5945  -1290     49    388
ATOM    536  CA  GLU A  83      -9.878  14.110 -18.724  1.00 52.40           C  
ANISOU  536  CA  GLU A  83     7645   6373   5890  -1224     54    283
ATOM    537  C   GLU A  83     -11.153  13.263 -18.865  1.00 51.54           C  
ANISOU  537  C   GLU A  83     7478   6195   5911   -979    131    181
ATOM    538  O   GLU A  83     -12.095  13.446 -18.089  1.00 51.66           O  
ANISOU  538  O   GLU A  83     7590   6083   5954   -893    142     98
ATOM    539  CB  GLU A  83     -10.168  15.626 -18.648  1.00 53.53           C  
ANISOU  539  CB  GLU A  83     8073   6303   5962  -1314    -31    249
ATOM    540  CG  GLU A  83      -8.952  16.444 -18.170  1.00 56.17           C  
ANISOU  540  CG  GLU A  83     8525   6663   6153  -1587   -133    343
ATOM    541  CD  GLU A  83      -8.545  16.075 -16.747  1.00 63.69           C  
ANISOU  541  CD  GLU A  83     9444   7680   7075  -1651   -128    350
ATOM    542  OE1 GLU A  83      -9.409  16.167 -15.851  1.00 64.38           O  
ANISOU  542  OE1 GLU A  83     9622   7638   7202  -1519    -97    243
ATOM    543  OE2 GLU A  83      -7.393  15.629 -16.565  1.00 65.11           O1-
ANISOU  543  OE2 GLU A  83     9488   8064   7185  -1823   -150    471
ATOM    544  H   GLU A  83      -9.052  14.481 -20.611  1.00 53.15           H  
ATOM    545  HA  GLU A  83      -9.441  13.793 -17.781  1.00 52.40           H  
ATOM    546  HB3 GLU A  83     -11.024  15.829 -18.003  1.00 53.53           H  
ATOM    547  HB2 GLU A  83     -10.443  15.996 -19.633  1.00 53.53           H  
ATOM    548  HG3 GLU A  83      -9.185  17.508 -18.191  1.00 56.17           H  
ATOM    549  HG2 GLU A  83      -8.111  16.307 -18.850  1.00 56.17           H  
ATOM    550  N   ARG A  84     -11.168  12.354 -19.843  1.00 50.16           N  
ANISOU  550  N   ARG A  84     7152   6111   5796   -872    176    195
ATOM    551  CA  ARG A  84     -12.302  11.524 -20.202  1.00 49.05           C  
ANISOU  551  CA  ARG A  84     6972   5904   5760   -681    223    120
ATOM    552  C   ARG A  84     -11.898  10.044 -20.175  1.00 48.43           C  
ANISOU  552  C   ARG A  84     6720   5956   5726   -590    268    141
ATOM    553  O   ARG A  84     -10.757   9.703 -20.489  1.00 48.80           O  
ANISOU  553  O   ARG A  84     6665   6156   5721   -627    272    215
ATOM    554  CB  ARG A  84     -12.741  11.980 -21.604  1.00 49.10           C  
ANISOU  554  CB  ARG A  84     7040   5833   5782   -636    209    110
ATOM    555  CG  ARG A  84     -14.046  11.398 -22.170  1.00 49.89           C  
ANISOU  555  CG  ARG A  84     7115   5867   5976   -466    241     51
ATOM    556  CD  ARG A  84     -14.337  11.921 -23.595  1.00 50.51           C  
ANISOU  556  CD  ARG A  84     7238   5895   6057   -443    223     57
ATOM    557  NE  ARG A  84     -13.391  11.412 -24.612  1.00 49.57           N  
ANISOU  557  NE  ARG A  84     7014   5911   5912   -464    228    121
ATOM    558  CZ  ARG A  84     -13.044  11.984 -25.778  1.00 50.77           C  
ANISOU  558  CZ  ARG A  84     7193   6073   6025   -507    205    159
ATOM    559  NH1 ARG A  84     -12.113  11.420 -26.535  1.00 51.17           N  
ANISOU  559  NH1 ARG A  84     7131   6280   6030   -508    216    224
ATOM    560  NH2 ARG A  84     -13.591  13.115 -26.221  1.00 47.37           N1+
ANISOU  560  NH2 ARG A  84     6905   5505   5589   -537    168    136
ATOM    561  H   ARG A  84     -10.355  12.269 -20.442  1.00 50.16           H  
ATOM    562  HA  ARG A  84     -13.113  11.690 -19.501  1.00 49.05           H  
ATOM    563  HB3 ARG A  84     -11.922  11.786 -22.296  1.00 49.10           H  
ATOM    564  HB2 ARG A  84     -12.857  13.062 -21.580  1.00 49.10           H  
ATOM    565  HG3 ARG A  84     -14.891  11.603 -21.512  1.00 49.89           H  
ATOM    566  HG2 ARG A  84     -13.960  10.313 -22.203  1.00 49.89           H  
ATOM    567  HD3 ARG A  84     -14.200  13.001 -23.566  1.00 50.51           H  
ATOM    568  HD2 ARG A  84     -15.371  11.760 -23.889  1.00 50.51           H  
ATOM    569 HH22 ARG A  84     -13.250  13.539 -27.086  1.00 47.37           H  
ATOM    570 HH21 ARG A  84     -14.189  13.677 -25.638  1.00 47.37           H  
ATOM    571 HH12 ARG A  84     -11.877  11.793 -27.451  1.00 51.17           H  
ATOM    572 HH11 ARG A  84     -11.418  10.781 -26.145  1.00 51.17           H  
ATOM    573  HE  ARG A  84     -13.015  10.484 -24.389  1.00 49.57           H  
ATOM    574  N   PRO A  86     -13.993   6.766 -22.105  1.00 46.79           N  
ANISOU  574  N   PRO A  86     6382   5690   5704   -186    305     68
ATOM    575  CA  PRO A  86     -12.755   6.451 -22.848  1.00 46.42           C  
ANISOU  575  CA  PRO A  86     6276   5772   5591   -170    314    122
ATOM    576  C   PRO A  86     -11.976   7.713 -23.254  1.00 46.92           C  
ANISOU  576  C   PRO A  86     6351   5890   5588   -281    309    167
ATOM    577  O   PRO A  86     -12.595   8.691 -23.678  1.00 46.66           O  
ANISOU  577  O   PRO A  86     6406   5751   5574   -324    291    141
ATOM    578  CB  PRO A  86     -13.256   5.674 -24.085  1.00 47.14           C  
ANISOU  578  CB  PRO A  86     6390   5818   5701    -47    301    105
ATOM    579  CG  PRO A  86     -14.644   5.174 -23.711  1.00 48.52           C  
ANISOU  579  CG  PRO A  86     6617   5860   5957    -20    278     56
ATOM    580  CD  PRO A  86     -15.170   6.305 -22.840  1.00 46.70           C  
ANISOU  580  CD  PRO A  86     6410   5585   5749   -104    288     36
ATOM    581  HA  PRO A  86     -12.148   5.788 -22.229  1.00 46.42           H  
ATOM    582  HB3 PRO A  86     -12.585   4.863 -24.371  1.00 47.14           H  
ATOM    583  HB2 PRO A  86     -13.339   6.334 -24.951  1.00 47.14           H  
ATOM    584  HG3 PRO A  86     -14.560   4.265 -23.113  1.00 48.52           H  
ATOM    585  HG2 PRO A  86     -15.273   4.953 -24.574  1.00 48.52           H  
ATOM    586  HD2 PRO A  86     -15.546   7.129 -23.451  1.00 46.70           H  
ATOM    587  HD3 PRO A  86     -15.987   5.969 -22.198  1.00 46.70           H  
ATOM    588  N   SER A  87     -10.649   7.697 -23.086  1.00 48.21           N  
ANISOU  588  N   SER A  87     6429   6224   5663   -338    317    244
ATOM    589  CA  SER A  87      -9.804   8.846 -23.402  1.00 50.68           C  
ANISOU  589  CA  SER A  87     6747   6616   5893   -486    294    314
ATOM    590  C   SER A  87      -9.717   9.087 -24.913  1.00 50.50           C  
ANISOU  590  C   SER A  87     6721   6620   5845   -439    291    336
ATOM    591  O   SER A  87      -9.792  10.236 -25.338  1.00 51.60           O  
ANISOU  591  O   SER A  87     6928   6722   5955   -554    256    360
ATOM    592  CB  SER A  87      -8.429   8.669 -22.734  1.00 53.63           C  
ANISOU  592  CB  SER A  87     7002   7211   6163   -576    299    416
ATOM    593  OG  SER A  87      -7.827   7.438 -23.112  1.00 58.14           O  
ANISOU  593  OG  SER A  87     7447   7961   6683   -430    336    462
ATOM    594  H   SER A  87     -10.140   6.885 -22.769  1.00 48.21           H  
ATOM    595  HA  SER A  87     -10.269   9.734 -22.973  1.00 50.68           H  
ATOM    596  HB3 SER A  87      -8.530   8.704 -21.648  1.00 53.63           H  
ATOM    597  HB2 SER A  87      -7.772   9.499 -23.005  1.00 53.63           H  
ATOM    598  HG  SER A  87      -6.910   7.621 -23.351  1.00 58.14           H  
ATOM    599  N   VAL A  88      -9.640   8.008 -25.699  1.00 49.88           N  
ANISOU  599  N   VAL A  88     6592   6588   5774   -268    318    323
ATOM    600  CA  VAL A  88      -9.665   8.031 -27.156  1.00 50.26           C  
ANISOU  600  CA  VAL A  88     6639   6665   5791   -201    318    339
ATOM    601  C   VAL A  88     -11.056   7.582 -27.630  1.00 50.02           C  
ANISOU  601  C   VAL A  88     6705   6440   5858    -88    309    247
ATOM    602  O   VAL A  88     -11.557   6.561 -27.157  1.00 49.52           O  
ANISOU  602  O   VAL A  88     6660   6313   5842     23    312    198
ATOM    603  CB  VAL A  88      -8.606   7.062 -27.754  1.00 51.28           C  
ANISOU  603  CB  VAL A  88     6646   7030   5810    -79    350    411
ATOM    604  CG1 VAL A  88      -8.610   6.998 -29.298  1.00 51.60           C  
ANISOU  604  CG1 VAL A  88     6692   7105   5809     18    353    420
ATOM    605  CG2 VAL A  88      -7.198   7.438 -27.273  1.00 51.60           C  
ANISOU  605  CG2 VAL A  88     6560   7312   5734   -215    353    532
ATOM    606  H   VAL A  88      -9.661   7.099 -25.266  1.00 49.88           H  
ATOM    607  HA  VAL A  88      -9.458   9.037 -27.517  1.00 50.26           H  
ATOM    608  HB  VAL A  88      -8.817   6.053 -27.391  1.00 51.28           H  
ATOM    609 HG11 VAL A  88      -7.776   6.405 -29.675  1.00 51.60           H  
ATOM    610 HG12 VAL A  88      -9.519   6.542 -29.693  1.00 51.60           H  
ATOM    611 HG13 VAL A  88      -8.533   7.998 -29.726  1.00 51.60           H  
ATOM    612 HG21 VAL A  88      -6.452   6.739 -27.648  1.00 51.60           H  
ATOM    613 HG22 VAL A  88      -6.933   8.438 -27.617  1.00 51.60           H  
ATOM    614 HG23 VAL A  88      -7.122   7.434 -26.185  1.00 51.60           H  
ATOM    615  N   ILE A  89     -11.633   8.338 -28.562  1.00 49.31           N  
ANISOU  615  N   ILE A  89     6686   6258   5793   -133    288    233
ATOM    616  CA  ILE A  89     -12.824   7.980 -29.324  1.00 49.62           C  
ANISOU  616  CA  ILE A  89     6803   6141   5910    -42    275    165
ATOM    617  C   ILE A  89     -12.462   8.159 -30.812  1.00 50.22           C  
ANISOU  617  C   ILE A  89     6876   6268   5936     -3    271    194
ATOM    618  O   ILE A  89     -11.650   9.024 -31.148  1.00 50.10           O  
ANISOU  618  O   ILE A  89     6851   6314   5869   -109    262    248
ATOM    619  CB  ILE A  89     -14.047   8.870 -28.918  1.00 50.39           C  
ANISOU  619  CB  ILE A  89     6991   6071   6085   -107    256    116
ATOM    620  CG1 ILE A  89     -14.495   8.523 -27.476  1.00 49.96           C  
ANISOU  620  CG1 ILE A  89     6932   5977   6074   -113    264     84
ATOM    621  CG2 ILE A  89     -15.264   8.804 -29.871  1.00 51.62           C  
ANISOU  621  CG2 ILE A  89     7206   6108   6300    -32    239     75
ATOM    622  CD1 ILE A  89     -15.544   9.480 -26.890  1.00 49.29           C  
ANISOU  622  CD1 ILE A  89     6929   5770   6029   -152    253     45
ATOM    623  H   ILE A  89     -11.144   9.160 -28.917  1.00 49.31           H  
ATOM    624  HA  ILE A  89     -13.067   6.926 -29.164  1.00 49.62           H  
ATOM    625  HB  ILE A  89     -13.709   9.909 -28.923  1.00 50.39           H  
ATOM    626 HG13 ILE A  89     -13.638   8.513 -26.804  1.00 49.96           H  
ATOM    627 HG12 ILE A  89     -14.889   7.506 -27.466  1.00 49.96           H  
ATOM    628 HG21 ILE A  89     -16.048   9.496 -29.562  1.00 51.62           H  
ATOM    629 HG22 ILE A  89     -15.008   9.099 -30.885  1.00 51.62           H  
ATOM    630 HG23 ILE A  89     -15.703   7.807 -29.910  1.00 51.62           H  
ATOM    631 HD11 ILE A  89     -15.519   9.454 -25.801  1.00 49.29           H  
ATOM    632 HD12 ILE A  89     -15.368  10.509 -27.205  1.00 49.29           H  
ATOM    633 HD13 ILE A  89     -16.548   9.199 -27.207  1.00 49.29           H  
ATOM    634  N   TRP A  90     -13.019   7.307 -31.675  1.00 51.16           N  
ANISOU  634  N   TRP A  90     7015   6369   6057    140    271    166
ATOM    635  CA  TRP A  90     -12.814   7.359 -33.118  1.00 53.03           C  
ANISOU  635  CA  TRP A  90     7255   6654   6239    198    269    186
ATOM    636  C   TRP A  90     -14.129   7.779 -33.772  1.00 54.31           C  
ANISOU  636  C   TRP A  90     7510   6640   6486    179    238    139
ATOM    637  O   TRP A  90     -15.103   7.034 -33.677  1.00 55.81           O  
ANISOU  637  O   TRP A  90     7759   6704   6743    232    217     87
ATOM    638  CB  TRP A  90     -12.354   5.991 -33.639  1.00 53.23           C  
ANISOU  638  CB  TRP A  90     7280   6753   6193    385    278    180
ATOM    639  CG  TRP A  90     -10.968   5.589 -33.248  1.00 54.34           C  
ANISOU  639  CG  TRP A  90     7312   7113   6223    437    316    244
ATOM    640  CD1 TRP A  90     -10.631   4.865 -32.157  1.00 55.58           C  
ANISOU  640  CD1 TRP A  90     7441   7301   6377    465    327    243
ATOM    641  CD2 TRP A  90      -9.715   5.913 -33.922  1.00 55.02           C  
ANISOU  641  CD2 TRP A  90     7284   7447   6174    456    347    335
ATOM    642  NE1 TRP A  90      -9.263   4.673 -32.142  1.00 55.85           N  
ANISOU  642  NE1 TRP A  90     7351   7587   6283    513    365    326
ATOM    643  CE2 TRP A  90      -8.647   5.288 -33.212  1.00 56.10           C  
ANISOU  643  CE2 TRP A  90     7318   7770   6226    504    379    390
ATOM    644  CE3 TRP A  90      -9.373   6.642 -35.088  1.00 55.93           C  
ANISOU  644  CE3 TRP A  90     7362   7666   6224    431    349    388
ATOM    645  CZ2 TRP A  90      -7.312   5.361 -33.651  1.00 57.38           C  
ANISOU  645  CZ2 TRP A  90     7329   8242   6230    538    415    505
ATOM    646  CZ3 TRP A  90      -8.043   6.713 -35.546  1.00 57.13           C  
ANISOU  646  CZ3 TRP A  90     7366   8121   6220    452    382    501
ATOM    647  CH2 TRP A  90      -7.012   6.073 -34.829  1.00 57.42           C  
ANISOU  647  CH2 TRP A  90     7290   8362   6164    513    416    561
ATOM    648  H   TRP A  90     -13.742   6.675 -31.367  1.00 51.16           H  
ATOM    649  HA  TRP A  90     -12.037   8.075 -33.374  1.00 53.03           H  
ATOM    650  HB3 TRP A  90     -12.378   5.998 -34.727  1.00 53.23           H  
ATOM    651  HB2 TRP A  90     -13.054   5.212 -33.336  1.00 53.23           H  
ATOM    652  HD1 TRP A  90     -11.342   4.469 -31.444  1.00 55.58           H  
ATOM    653  HE1 TRP A  90      -8.817   4.071 -31.467  1.00 55.85           H  
ATOM    654  HE3 TRP A  90     -10.151   7.137 -35.650  1.00 55.93           H  
ATOM    655  HZ2 TRP A  90      -6.528   4.850 -33.113  1.00 57.38           H  
ATOM    656  HZ3 TRP A  90      -7.815   7.258 -36.450  1.00 57.13           H  
ATOM    657  HH2 TRP A  90      -5.996   6.115 -35.191  1.00 57.42           H  
ATOM    658  N   GLU A  91     -14.135   8.956 -34.397  1.00 53.70           N  
ANISOU  658  N   GLU A  91     7446   6562   6398     91    228    168
ATOM    659  CA  GLU A  91     -15.306   9.540 -35.042  1.00 54.25           C  
ANISOU  659  CA  GLU A  91     7597   6480   6535     80    201    133
ATOM    660  C   GLU A  91     -15.190   9.411 -36.564  1.00 53.43           C  
ANISOU  660  C   GLU A  91     7503   6405   6392    140    193    146
ATOM    661  O   GLU A  91     -14.118   9.645 -37.126  1.00 53.16           O  
ANISOU  661  O   GLU A  91     7411   6520   6265    129    206    204
ATOM    662  CB  GLU A  91     -15.423  11.011 -34.606  1.00 58.20           C  
ANISOU  662  CB  GLU A  91     8148   6914   7051    -51    184    146
ATOM    663  CG  GLU A  91     -16.029  11.129 -33.186  1.00 65.34           C  
ANISOU  663  CG  GLU A  91     9090   7719   8016    -66    185    102
ATOM    664  CD  GLU A  91     -15.660  12.368 -32.367  1.00 73.57           C  
ANISOU  664  CD  GLU A  91    10190   8735   9026   -190    169    121
ATOM    665  OE1 GLU A  91     -14.926  13.251 -32.859  1.00 77.89           O  
ANISOU  665  OE1 GLU A  91    10754   9338   9502   -297    144    179
ATOM    666  OE2 GLU A  91     -16.074  12.394 -31.193  1.00 73.79           O1-
ANISOU  666  OE2 GLU A  91    10256   8692   9087   -186    172     83
ATOM    667  H   GLU A  91     -13.279   9.498 -34.465  1.00 53.70           H  
ATOM    668  HA  GLU A  91     -16.209   9.014 -34.723  1.00 54.25           H  
ATOM    669  HB3 GLU A  91     -16.033  11.587 -35.306  1.00 58.20           H  
ATOM    670  HB2 GLU A  91     -14.428  11.458 -34.637  1.00 58.20           H  
ATOM    671  HG3 GLU A  91     -15.743  10.261 -32.598  1.00 65.34           H  
ATOM    672  HG2 GLU A  91     -17.114  11.091 -33.262  1.00 65.34           H  
ATOM    673  N   ALA A  92     -16.306   9.041 -37.195  1.00 52.29           N  
ANISOU  673  N   ALA A  92     7425   6136   6307    195    168    104
ATOM    674  CA  ALA A  92     -16.459   8.928 -38.636  1.00 51.46           C  
ANISOU  674  CA  ALA A  92     7344   6042   6166    251    155    111
ATOM    675  C   ALA A  92     -16.648  10.312 -39.269  1.00 51.91           C  
ANISOU  675  C   ALA A  92     7419   6079   6227    160    143    141
ATOM    676  O   ALA A  92     -17.528  11.056 -38.843  1.00 52.83           O  
ANISOU  676  O   ALA A  92     7580   6091   6403     93    129    130
ATOM    677  CB  ALA A  92     -17.678   8.050 -38.936  1.00 50.45           C  
ANISOU  677  CB  ALA A  92     7288   5794   6086    323    119     66
ATOM    678  H   ALA A  92     -17.152   8.924 -36.641  1.00 52.29           H  
ATOM    679  HA  ALA A  92     -15.575   8.443 -39.050  1.00 51.46           H  
ATOM    680  HB1 ALA A  92     -17.849   7.958 -40.008  1.00 50.45           H  
ATOM    681  HB2 ALA A  92     -17.554   7.045 -38.537  1.00 50.45           H  
ATOM    682  HB3 ALA A  92     -18.582   8.476 -38.501  1.00 50.45           H  
ATOM    683  N   LYS A  93     -15.863  10.600 -40.306  1.00 51.22           N  
ANISOU  683  N   LYS A  93     7302   6101   6059    165    147    186
ATOM    684  CA  LYS A  93     -16.039  11.751 -41.175  1.00 51.65           C  
ANISOU  684  CA  LYS A  93     7382   6138   6104     75    124    224
ATOM    685  C   LYS A  93     -16.198  11.202 -42.596  1.00 49.87           C  
ANISOU  685  C   LYS A  93     7171   5924   5852    165    117    217
ATOM    686  O   LYS A  93     -15.340  10.443 -43.053  1.00 47.75           O  
ANISOU  686  O   LYS A  93     6855   5793   5494    254    138    235
ATOM    687  CB  LYS A  93     -14.804  12.660 -41.030  1.00 55.99           C  
ANISOU  687  CB  LYS A  93     7867   6849   6557    -44    125    312
ATOM    688  CG  LYS A  93     -14.874  13.986 -41.813  1.00 63.57           C  
ANISOU  688  CG  LYS A  93     8884   7768   7502   -169     81    359
ATOM    689  CD  LYS A  93     -13.564  14.772 -41.675  1.00 70.62           C  
ANISOU  689  CD  LYS A  93     9733   8807   8294   -342     58    463
ATOM    690  CE  LYS A  93     -13.579  16.158 -42.332  1.00 76.05           C  
ANISOU  690  CE  LYS A  93    10512   9430   8953   -497     -9    520
ATOM    691  NZ  LYS A  93     -12.278  16.835 -42.159  1.00 79.85           N1+
ANISOU  691  NZ  LYS A  93    10920  10121   9297   -678    -44    656
ATOM    692  H   LYS A  93     -15.126   9.952 -40.570  1.00 51.22           H  
ATOM    693  HA  LYS A  93     -16.933  12.317 -40.905  1.00 51.65           H  
ATOM    694  HB3 LYS A  93     -13.917  12.097 -41.328  1.00 55.99           H  
ATOM    695  HB2 LYS A  93     -14.679  12.887 -39.970  1.00 55.99           H  
ATOM    696  HG3 LYS A  93     -15.712  14.577 -41.439  1.00 63.57           H  
ATOM    697  HG2 LYS A  93     -15.074  13.787 -42.866  1.00 63.57           H  
ATOM    698  HD3 LYS A  93     -12.771  14.168 -42.118  1.00 70.62           H  
ATOM    699  HD2 LYS A  93     -13.330  14.872 -40.615  1.00 70.62           H  
ATOM    700  HE3 LYS A  93     -14.367  16.775 -41.897  1.00 76.05           H  
ATOM    701  HE2 LYS A  93     -13.796  16.070 -43.399  1.00 76.05           H  
ATOM    702  HZ1 LYS A  93     -11.553  16.273 -42.585  1.00 79.85           H  
ATOM    703  HZ2 LYS A  93     -12.292  17.748 -42.596  1.00 79.85           H  
ATOM    704  HZ3 LYS A  93     -12.075  16.938 -41.173  1.00 79.85           H  
ATOM    705  N   CYS A  94     -17.295  11.569 -43.269  1.00 50.32           N  
ANISOU  705  N   CYS A  94     7300   5844   5976    157     86    193
ATOM    706  CA  CYS A  94     -17.613  11.117 -44.627  1.00 50.86           C  
ANISOU  706  CA  CYS A  94     7396   5906   6023    228     70    187
ATOM    707  C   CYS A  94     -16.606  11.704 -45.638  1.00 51.02           C  
ANISOU  707  C   CYS A  94     7363   6086   5936    206     80    252
ATOM    708  O   CYS A  94     -16.184  12.848 -45.466  1.00 51.74           O  
ANISOU  708  O   CYS A  94     7433   6222   6005     80     72    310
ATOM    709  CB  CYS A  94     -19.058  11.516 -44.997  1.00 51.17           C  
ANISOU  709  CB  CYS A  94     7502   5792   6148    205     35    167
ATOM    710  SG  CYS A  94     -20.308  11.379 -43.669  1.00 53.53           S  
ANISOU  710  SG  CYS A  94     7827   5964   6549    224     24    121
ATOM    711  H   CYS A  94     -17.986  12.165 -42.838  1.00 50.32           H  
ATOM    712  HA  CYS A  94     -17.549  10.028 -44.643  1.00 50.86           H  
ATOM    713  HB3 CYS A  94     -19.389  10.918 -45.849  1.00 51.17           H  
ATOM    714  HB2 CYS A  94     -19.079  12.554 -45.337  1.00 51.17           H  
ATOM    715  N   ARG A  95     -16.224  10.929 -46.661  1.00 50.31           N  
ANISOU  715  N   ARG A  95     7259   6094   5761    326     93    250
ATOM    716  CA  ARG A  95     -15.227  11.355 -47.650  1.00 51.31           C  
ANISOU  716  CA  ARG A  95     7317   6410   5767    325    107    321
ATOM    717  C   ARG A  95     -15.757  12.357 -48.683  1.00 51.00           C  
ANISOU  717  C   ARG A  95     7314   6312   5753    241     72    348
ATOM    718  O   ARG A  95     -14.960  13.089 -49.268  1.00 51.61           O  
ANISOU  718  O   ARG A  95     7328   6535   5749    156     70    432
ATOM    719  CB  ARG A  95     -14.689  10.141 -48.419  1.00 52.79           C  
ANISOU  719  CB  ARG A  95     7504   6712   5840    519    130    302
ATOM    720  CG  ARG A  95     -14.046   9.077 -47.535  1.00 55.58           C  
ANISOU  720  CG  ARG A  95     7809   7184   6125    622    168    300
ATOM    721  CD  ARG A  95     -13.504   7.914 -48.368  1.00 56.56           C  
ANISOU  721  CD  ARG A  95     7948   7442   6099    843    191    290
ATOM    722  NE  ARG A  95     -13.063   6.834 -47.485  1.00 59.79           N  
ANISOU  722  NE  ARG A  95     8399   7832   6487    975    203    242
ATOM    723  CZ  ARG A  95     -12.710   5.586 -47.788  1.00 63.48           C  
ANISOU  723  CZ  ARG A  95     8974   8292   6854   1197    198    190
ATOM    724  NH1 ARG A  95     -12.662   5.136 -49.042  1.00 63.39           N  
ANISOU  724  NH1 ARG A  95     9033   8311   6741   1325    188    178
ATOM    725  NH2 ARG A  95     -12.395   4.789 -46.777  1.00 63.51           N1+
ANISOU  725  NH2 ARG A  95     9031   8258   6842   1301    198    151
ATOM    726  H   ARG A  95     -16.627   9.996 -46.771  1.00 50.31           H  
ATOM    727  HA  ARG A  95     -14.398  11.834 -47.125  1.00 51.31           H  
ATOM    728  HB3 ARG A  95     -13.962  10.473 -49.163  1.00 52.79           H  
ATOM    729  HB2 ARG A  95     -15.503   9.691 -48.985  1.00 52.79           H  
ATOM    730  HG3 ARG A  95     -14.719   8.729 -46.753  1.00 55.58           H  
ATOM    731  HG2 ARG A  95     -13.213   9.563 -47.026  1.00 55.58           H  
ATOM    732  HD3 ARG A  95     -12.607   8.247 -48.889  1.00 56.56           H  
ATOM    733  HD2 ARG A  95     -14.206   7.596 -49.140  1.00 56.56           H  
ATOM    734 HH22 ARG A  95     -12.072   3.831 -46.945  1.00 63.51           H  
ATOM    735 HH21 ARG A  95     -12.619   5.042 -45.818  1.00 63.51           H  
ATOM    736 HH12 ARG A  95     -12.366   4.187 -49.241  1.00 63.39           H  
ATOM    737 HH11 ARG A  95     -12.962   5.706 -49.818  1.00 63.39           H  
ATOM    738  HE  ARG A  95     -12.855   7.120 -46.526  1.00 59.79           H  
ATOM    739  N   HIS A  96     -17.063  12.320 -48.949  1.00 49.94           N  
ANISOU  739  N   HIS A  96     7273   5991   5710    265     41    291
ATOM    740  CA  HIS A  96     -17.715  13.080 -50.010  1.00 49.78           C  
ANISOU  740  CA  HIS A  96     7290   5917   5709    203      8    316
ATOM    741  C   HIS A  96     -18.942  13.780 -49.423  1.00 48.70           C  
ANISOU  741  C   HIS A  96     7222   5588   5692    138    -24    293
ATOM    742  O   HIS A  96     -19.459  13.346 -48.391  1.00 47.46           O  
ANISOU  742  O   HIS A  96     7086   5341   5606    160    -21    248
ATOM    743  CB  HIS A  96     -18.117  12.124 -51.160  1.00 51.77           C  
ANISOU  743  CB  HIS A  96     7583   6169   5918    318     -3    289
ATOM    744  CG  HIS A  96     -16.999  11.254 -51.686  1.00 56.12           C  
ANISOU  744  CG  HIS A  96     8088   6907   6327    442     31    301
ATOM    745  ND1 HIS A  96     -15.995  11.702 -52.531  1.00 58.58           N  
ANISOU  745  ND1 HIS A  96     8319   7416   6523    427     48    377
ATOM    746  CD2 HIS A  96     -16.719   9.925 -51.463  1.00 57.94           C  
ANISOU  746  CD2 HIS A  96     8352   7160   6501    594     46    251
ATOM    747  CE1 HIS A  96     -15.164  10.675 -52.737  1.00 59.04           C  
ANISOU  747  CE1 HIS A  96     8349   7633   6452    593     85    371
ATOM    748  NE2 HIS A  96     -15.524   9.573 -52.090  1.00 59.06           N  
ANISOU  748  NE2 HIS A  96     8434   7522   6484    705     82    291
ATOM    749  H   HIS A  96     -17.688  11.793 -48.359  1.00 49.94           H  
ATOM    750  HA  HIS A  96     -17.043  13.846 -50.399  1.00 49.78           H  
ATOM    751  HB3 HIS A  96     -18.545  12.687 -51.992  1.00 51.77           H  
ATOM    752  HB2 HIS A  96     -18.910  11.457 -50.818  1.00 51.77           H  
ATOM    753  HD1 HIS A  96     -15.890  12.626 -52.924  1.00 58.58           H  
ATOM    754  HD2 HIS A  96     -17.272   9.211 -50.878  1.00 57.94           H  
ATOM    755  HE1 HIS A  96     -14.287  10.731 -53.365  1.00 59.04           H  
ATOM    756  N   LEU A  97     -19.385  14.837 -50.114  1.00 48.48           N  
ANISOU  756  N   LEU A  97     7230   5513   5676     68    -55    328
ATOM    757  CA  LEU A  97     -20.684  15.468 -49.866  1.00 48.04           C  
ANISOU  757  CA  LEU A  97     7248   5292   5711     47    -85    312
ATOM    758  C   LEU A  97     -21.792  14.635 -50.535  1.00 47.53           C  
ANISOU  758  C   LEU A  97     7203   5167   5689    131   -100    279
ATOM    759  O   LEU A  97     -22.806  14.353 -49.903  1.00 48.18           O  
ANISOU  759  O   LEU A  97     7306   5158   5844    160   -109    255
ATOM    760  CB  LEU A  97     -20.676  16.924 -50.397  1.00 48.21           C  
ANISOU  760  CB  LEU A  97     7321   5289   5707    -54   -123    372
ATOM    761  CG  LEU A  97     -19.622  17.843 -49.728  1.00 49.91           C  
ANISOU  761  CG  LEU A  97     7561   5525   5877   -179   -140    418
ATOM    762  CD1 LEU A  97     -19.471  19.164 -50.505  1.00 51.18           C  
ANISOU  762  CD1 LEU A  97     7806   5638   6003   -286   -199    481
ATOM    763  CD2 LEU A  97     -19.938  18.101 -48.241  1.00 50.40           C  
ANISOU  763  CD2 LEU A  97     7684   5468   5999   -167   -137    373
ATOM    764  H   LEU A  97     -18.862  15.178 -50.904  1.00 48.48           H  
ATOM    765  HA  LEU A  97     -20.893  15.485 -48.793  1.00 48.04           H  
ATOM    766  HB3 LEU A  97     -21.669  17.361 -50.265  1.00 48.21           H  
ATOM    767  HB2 LEU A  97     -20.513  16.913 -51.475  1.00 48.21           H  
ATOM    768  HG  LEU A  97     -18.651  17.350 -49.776  1.00 49.91           H  
ATOM    769 HD11 LEU A  97     -18.776  19.847 -50.016  1.00 51.18           H  
ATOM    770 HD12 LEU A  97     -19.087  18.990 -51.510  1.00 51.18           H  
ATOM    771 HD13 LEU A  97     -20.423  19.685 -50.606  1.00 51.18           H  
ATOM    772 HD21 LEU A  97     -19.614  19.092 -47.918  1.00 50.40           H  
ATOM    773 HD22 LEU A  97     -21.006  18.030 -48.029  1.00 50.40           H  
ATOM    774 HD23 LEU A  97     -19.432  17.374 -47.602  1.00 50.40           H  
ATOM    775  N   GLY A  98     -21.547  14.216 -51.786  1.00 47.35           N  
ANISOU  775  N   GLY A  98     7173   5210   5608    167   -106    286
ATOM    776  CA  GLY A  98     -22.450  13.365 -52.563  1.00 48.66           C  
ANISOU  776  CA  GLY A  98     7378   5322   5791    227   -136    262
ATOM    777  C   GLY A  98     -22.261  11.883 -52.202  1.00 50.42           C  
ANISOU  777  C   GLY A  98     7619   5555   5982    306   -136    214
ATOM    778  O   GLY A  98     -21.553  11.553 -51.249  1.00 50.78           O  
ANISOU  778  O   GLY A  98     7636   5645   6012    327   -103    197
ATOM    779  H   GLY A  98     -20.664  14.426 -52.211  1.00 47.35           H  
ATOM    780  HA3 GLY A  98     -22.247  13.522 -53.621  1.00 48.66           H  
ATOM    781  HA2 GLY A  98     -23.484  13.651 -52.389  1.00 48.66           H  
ATOM    782  N   CYS A  99     -22.886  10.987 -52.972  1.00 50.93           N  
ANISOU  782  N   CYS A  99     7751   5572   6027    347   -181    197
ATOM    783  CA  CYS A  99     -22.786   9.529 -52.804  1.00 51.63           C  
ANISOU  783  CA  CYS A  99     7915   5638   6065    422   -206    153
ATOM    784  C   CYS A  99     -22.188   8.888 -54.062  1.00 54.87           C  
ANISOU  784  C   CYS A  99     8399   6097   6350    517   -219    136
ATOM    785  O   CYS A  99     -22.439   9.376 -55.159  1.00 55.51           O  
ANISOU  785  O   CYS A  99     8482   6198   6410    499   -230    161
ATOM    786  CB  CYS A  99     -24.175   8.905 -52.584  1.00 49.57           C  
ANISOU  786  CB  CYS A  99     7708   5265   5863    375   -273    153
ATOM    787  SG  CYS A  99     -25.113   9.493 -51.149  1.00 48.81           S  
ANISOU  787  SG  CYS A  99     7515   5142   5886    301   -254    179
ATOM    788  H   CYS A  99     -23.369  11.311 -53.808  1.00 50.93           H  
ATOM    789  HA  CYS A  99     -22.149   9.287 -51.954  1.00 51.63           H  
ATOM    790  HB3 CYS A  99     -24.055   7.827 -52.469  1.00 49.57           H  
ATOM    791  HB2 CYS A  99     -24.793   9.033 -53.474  1.00 49.57           H  
ATOM    792  N   ILE A 100     -21.460   7.778 -53.897  1.00 56.56           N  
ANISOU  792  N   ILE A 100     8689   6330   6471    632   -221     93
ATOM    793  CA  ILE A 100     -20.913   6.993 -55.002  1.00 60.24           C  
ANISOU  793  CA  ILE A 100     9255   6845   6790    768   -233     69
ATOM    794  C   ILE A 100     -22.045   6.177 -55.666  1.00 63.89           C  
ANISOU  794  C   ILE A 100     9890   7152   7234    755   -334     45
ATOM    795  O   ILE A 100     -22.765   5.466 -54.961  1.00 64.27           O  
ANISOU  795  O   ILE A 100    10029   7073   7316    712   -400     29
ATOM    796  CB  ILE A 100     -19.784   6.025 -54.533  1.00 61.75           C  
ANISOU  796  CB  ILE A 100     9483   7114   6865    932   -200     32
ATOM    797  CG1 ILE A 100     -18.695   6.724 -53.685  1.00 63.06           C  
ANISOU  797  CG1 ILE A 100     9467   7447   7047    917   -110     70
ATOM    798  CG2 ILE A 100     -19.126   5.262 -55.698  1.00 63.05           C  
ANISOU  798  CG2 ILE A 100     9760   7345   6849   1118   -207      5
ATOM    799  CD1 ILE A 100     -18.009   7.910 -54.382  1.00 65.46           C  
ANISOU  799  CD1 ILE A 100     9632   7923   7319    869    -59    137
ATOM    800  H   ILE A 100     -21.385   7.367 -52.968  1.00 56.56           H  
ATOM    801  HA  ILE A 100     -20.492   7.691 -55.721  1.00 60.24           H  
ATOM    802  HB  ILE A 100     -20.236   5.266 -53.899  1.00 61.75           H  
ATOM    803 HG13 ILE A 100     -17.940   5.992 -53.400  1.00 63.06           H  
ATOM    804 HG12 ILE A 100     -19.126   7.067 -52.746  1.00 63.06           H  
ATOM    805 HG21 ILE A 100     -18.294   4.646 -55.354  1.00 63.05           H  
ATOM    806 HG22 ILE A 100     -19.827   4.588 -56.193  1.00 63.05           H  
ATOM    807 HG23 ILE A 100     -18.742   5.947 -56.453  1.00 63.05           H  
ATOM    808 HD11 ILE A 100     -17.170   8.274 -53.790  1.00 65.46           H  
ATOM    809 HD12 ILE A 100     -17.613   7.641 -55.362  1.00 65.46           H  
ATOM    810 HD13 ILE A 100     -18.703   8.738 -54.515  1.00 65.46           H  
ATOM    811  N   ASN A 101     -22.187   6.320 -56.989  1.00 66.56           N  
ANISOU  811  N   ASN A 101    10274   7505   7509    775   -356     54
ATOM    812  CA  ASN A 101     -23.156   5.603 -57.820  1.00 69.84           C  
ANISOU  812  CA  ASN A 101    10864   7777   7894    741   -464     43
ATOM    813  C   ASN A 101     -22.565   4.292 -58.388  1.00 72.74           C  
ANISOU  813  C   ASN A 101    11458   8096   8084    913   -515    -21
ATOM    814  O   ASN A 101     -21.400   3.986 -58.129  1.00 72.82           O  
ANISOU  814  O   ASN A 101    11473   8194   8001   1077   -458    -56
ATOM    815  CB  ASN A 101     -23.731   6.557 -58.909  1.00 71.69           C  
ANISOU  815  CB  ASN A 101    11043   8031   8166    651   -474     91
ATOM    816  CG  ASN A 101     -22.832   6.928 -60.101  1.00 75.29           C  
ANISOU  816  CG  ASN A 101    11467   8624   8517    750   -421     94
ATOM    817  OD1 ASN A 101     -21.717   6.443 -60.258  1.00 76.02           O  
ANISOU  817  OD1 ASN A 101    11609   8805   8470    918   -387     57
ATOM    818  ND2 ASN A 101     -23.327   7.795 -60.978  1.00 75.74           N  
ANISOU  818  ND2 ASN A 101    11433   8718   8627    658   -413    146
ATOM    819  H   ASN A 101     -21.537   6.925 -57.490  1.00 66.56           H  
ATOM    820  HA  ASN A 101     -23.996   5.274 -57.207  1.00 69.84           H  
ATOM    821  HB3 ASN A 101     -24.063   7.478 -58.430  1.00 71.69           H  
ATOM    822  HB2 ASN A 101     -24.629   6.098 -59.324  1.00 71.69           H  
ATOM    823 HD22 ASN A 101     -22.816   7.977 -61.830  1.00 75.74           H  
ATOM    824 HD21 ASN A 101     -24.237   8.210 -60.845  1.00 75.74           H  
ATOM    825  N   ALA A 102     -23.370   3.550 -59.165  1.00 74.83           N  
ANISOU  825  N   ALA A 102    11923   8220   8288    882   -630    -33
ATOM    826  CA  ALA A 102     -22.997   2.285 -59.815  1.00 77.05           C  
ANISOU  826  CA  ALA A 102    12484   8411   8380   1045   -705    -99
ATOM    827  C   ALA A 102     -21.761   2.365 -60.727  1.00 78.22           C  
ANISOU  827  C   ALA A 102    12618   8726   8375   1273   -619   -129
ATOM    828  O   ALA A 102     -20.972   1.421 -60.750  1.00 78.99           O  
ANISOU  828  O   ALA A 102    12871   8831   8310   1493   -619   -187
ATOM    829  CB  ALA A 102     -24.201   1.754 -60.607  1.00 77.57           C  
ANISOU  829  CB  ALA A 102    12752   8308   8413    925   -851    -86
ATOM    830  H   ALA A 102     -24.315   3.855 -59.330  1.00 74.83           H  
ATOM    831  HA  ALA A 102     -22.760   1.569 -59.028  1.00 77.05           H  
ATOM    832  HB1 ALA A 102     -23.960   0.807 -61.097  1.00 77.57           H  
ATOM    833  HB2 ALA A 102     -25.058   1.574 -59.957  1.00 77.57           H  
ATOM    834  HB3 ALA A 102     -24.504   2.450 -61.393  1.00 77.57           H  
ATOM    835  N   GLY A 104     -19.281   4.264 -60.160  1.00 77.32           N  
ANISOU  835  N   GLY A 104    11977   9155   8247   1440   -321    -54
ATOM    836  CA  GLY A 104     -18.179   4.616 -59.269  1.00 76.40           C  
ANISOU  836  CA  GLY A 104    11664   9245   8121   1497   -216    -20
ATOM    837  C   GLY A 104     -17.940   6.132 -59.237  1.00 75.27           C  
ANISOU  837  C   GLY A 104    11264   9256   8081   1328   -149     68
ATOM    838  O   GLY A 104     -16.887   6.571 -58.775  1.00 75.61           O  
ANISOU  838  O   GLY A 104    11136   9504   8089   1350    -70    119
ATOM    839  H   GLY A 104     -20.185   4.071 -59.739  1.00 77.32           H  
ATOM    840  HA3 GLY A 104     -17.261   4.115 -59.580  1.00 76.40           H  
ATOM    841  HA2 GLY A 104     -18.409   4.261 -58.266  1.00 76.40           H  
ATOM    842  N   ASN A 105     -18.876   6.938 -59.751  1.00 73.55           N  
ANISOU  842  N   ASN A 105    11026   8938   7981   1150   -188     96
ATOM    843  CA  ASN A 105     -18.811   8.401 -59.779  1.00 72.87           C  
ANISOU  843  CA  ASN A 105    10748   8953   7987    984   -146    177
ATOM    844  C   ASN A 105     -19.576   8.943 -58.570  1.00 70.99           C  
ANISOU  844  C   ASN A 105    10456   8580   7937    810   -159    187
ATOM    845  O   ASN A 105     -20.480   8.279 -58.062  1.00 71.36           O  
ANISOU  845  O   ASN A 105    10604   8451   8058    785   -212    142
ATOM    846  CB  ASN A 105     -19.442   8.935 -61.087  1.00 74.87           C  
ANISOU  846  CB  ASN A 105    11021   9186   8242    918   -182    205
ATOM    847  CG  ASN A 105     -18.644   8.696 -62.376  1.00 79.08           C  
ANISOU  847  CG  ASN A 105    11606   9852   8587   1082   -172    199
ATOM    848  OD1 ASN A 105     -18.922   9.331 -63.384  1.00 80.33           O  
ANISOU  848  OD1 ASN A 105    11879   9920   8723   1082   -228    180
ATOM    849  ND2 ASN A 105     -17.651   7.814 -62.384  1.00 79.77           N  
ANISOU  849  ND2 ASN A 105    11606  10177   8525   1228   -102    224
ATOM    850  H   ASN A 105     -19.771   6.531 -60.019  1.00 73.55           H  
ATOM    851  HA  ASN A 105     -17.769   8.721 -59.732  1.00 72.87           H  
ATOM    852  HB3 ASN A 105     -19.559  10.017 -61.012  1.00 74.87           H  
ATOM    853  HB2 ASN A 105     -20.450   8.542 -61.214  1.00 74.87           H  
ATOM    854 HD22 ASN A 105     -17.212   7.599 -63.264  1.00 79.77           H  
ATOM    855 HD21 ASN A 105     -17.482   7.210 -61.589  1.00 79.77           H  
ATOM    856  N   VAL A 106     -19.215  10.155 -58.129  1.00 68.83           N  
ANISOU  856  N   VAL A 106    10035   8391   7725    685   -120    252
ATOM    857  CA  VAL A 106     -19.949  10.857 -57.081  1.00 67.06           C  
ANISOU  857  CA  VAL A 106     9779   8042   7658    546   -131    259
ATOM    858  C   VAL A 106     -21.207  11.479 -57.715  1.00 64.84           C  
ANISOU  858  C   VAL A 106     9539   7625   7470    452   -183    272
ATOM    859  O   VAL A 106     -21.075  12.398 -58.526  1.00 65.20           O  
ANISOU  859  O   VAL A 106     9555   7720   7499    400   -187    320
ATOM    860  CB  VAL A 106     -19.098  11.992 -56.431  1.00 67.62           C  
ANISOU  860  CB  VAL A 106     9724   8226   7742    450    -87    321
ATOM    861  CG1 VAL A 106     -19.859  12.814 -55.365  1.00 68.14           C  
ANISOU  861  CG1 VAL A 106     9795   8141   7955    331   -105    320
ATOM    862  CG2 VAL A 106     -17.797  11.457 -55.807  1.00 68.32           C  
ANISOU  862  CG2 VAL A 106     9753   8466   7739    540    -36    319
ATOM    863  H   VAL A 106     -18.551  10.701 -58.652  1.00 68.83           H  
ATOM    864  HA  VAL A 106     -20.241  10.149 -56.304  1.00 67.06           H  
ATOM    865  HB  VAL A 106     -18.811  12.684 -57.225  1.00 67.62           H  
ATOM    866 HG11 VAL A 106     -19.197  13.532 -54.880  1.00 68.14           H  
ATOM    867 HG12 VAL A 106     -20.685  13.385 -55.795  1.00 68.14           H  
ATOM    868 HG13 VAL A 106     -20.271  12.167 -54.590  1.00 68.14           H  
ATOM    869 HG21 VAL A 106     -17.163  12.277 -55.471  1.00 68.32           H  
ATOM    870 HG22 VAL A 106     -18.006  10.832 -54.941  1.00 68.32           H  
ATOM    871 HG23 VAL A 106     -17.214  10.864 -56.513  1.00 68.32           H  
ATOM    872  N   ASP A 107     -22.384  10.977 -57.333  1.00 62.07           N  
ANISOU  872  N   ASP A 107     9252   7123   7209    428   -225    241
ATOM    873  CA  ASP A 107     -23.669  11.612 -57.600  1.00 60.26           C  
ANISOU  873  CA  ASP A 107     9041   6790   7066    348   -273    266
ATOM    874  C   ASP A 107     -23.849  12.732 -56.563  1.00 58.65           C  
ANISOU  874  C   ASP A 107     8763   6558   6963    270   -248    297
ATOM    875  O   ASP A 107     -23.670  12.490 -55.365  1.00 56.93           O  
ANISOU  875  O   ASP A 107     8529   6303   6798    267   -235    277
ATOM    876  CB  ASP A 107     -24.855  10.623 -57.551  1.00 60.89           C  
ANISOU  876  CB  ASP A 107     9210   6759   7165    352   -337    239
ATOM    877  CG  ASP A 107     -26.233  11.243 -57.827  1.00 64.56           C  
ANISOU  877  CG  ASP A 107     9669   7155   7708    269   -390    284
ATOM    878  OD1 ASP A 107     -26.302  12.331 -58.449  1.00 64.61           O  
ANISOU  878  OD1 ASP A 107     9615   7179   7754    231   -374    327
ATOM    879  OD2 ASP A 107     -27.227  10.581 -57.487  1.00 65.03           O1-
ANISOU  879  OD2 ASP A 107     9784   7150   7775    238   -454    287
ATOM    880  H   ASP A 107     -22.406  10.244 -56.624  1.00 62.07           H  
ATOM    881  HA  ASP A 107     -23.633  12.050 -58.599  1.00 60.26           H  
ATOM    882  HB3 ASP A 107     -24.879  10.121 -56.582  1.00 60.89           H  
ATOM    883  HB2 ASP A 107     -24.693   9.837 -58.288  1.00 60.89           H  
ATOM    884  N   TYR A 108     -24.184  13.927 -57.047  1.00 58.68           N  
ANISOU  884  N   TYR A 108     8742   6571   6982    212   -249    345
ATOM    885  CA  TYR A 108     -24.344  15.133 -56.244  1.00 59.43           C  
ANISOU  885  CA  TYR A 108     8817   6615   7148    156   -240    371
ATOM    886  C   TYR A 108     -25.811  15.419 -55.893  1.00 58.27           C  
ANISOU  886  C   TYR A 108     8685   6372   7085    164   -268    380
ATOM    887  O   TYR A 108     -26.042  16.314 -55.081  1.00 58.84           O  
ANISOU  887  O   TYR A 108     8761   6393   7202    157   -260    393
ATOM    888  CB  TYR A 108     -23.667  16.312 -56.974  1.00 60.86           C  
ANISOU  888  CB  TYR A 108     8998   6836   7292     86   -244    426
ATOM    889  CG  TYR A 108     -24.286  16.741 -58.299  1.00 63.67           C  
ANISOU  889  CG  TYR A 108     9379   7174   7641     72   -282    462
ATOM    890  CD1 TYR A 108     -23.835  16.187 -59.516  1.00 65.11           C  
ANISOU  890  CD1 TYR A 108     9553   7441   7744     95   -287    466
ATOM    891  CD2 TYR A 108     -25.319  17.702 -58.312  1.00 65.15           C  
ANISOU  891  CD2 TYR A 108     9604   7267   7881     47   -312    496
ATOM    892  CE1 TYR A 108     -24.419  16.587 -60.734  1.00 66.42           C  
ANISOU  892  CE1 TYR A 108     9740   7597   7899     74   -322    502
ATOM    893  CE2 TYR A 108     -25.912  18.092 -59.527  1.00 66.32           C  
ANISOU  893  CE2 TYR A 108     9772   7406   8020     35   -347    535
ATOM    894  CZ  TYR A 108     -25.466  17.528 -60.738  1.00 67.89           C  
ANISOU  894  CZ  TYR A 108     9953   7689   8152     36   -352    539
ATOM    895  OH  TYR A 108     -26.063  17.871 -61.913  1.00 71.20           O  
ANISOU  895  OH  TYR A 108    10390   8102   8558     14   -388    582
ATOM    896  H   TYR A 108     -24.503  13.965 -58.009  1.00 58.68           H  
ATOM    897  HA  TYR A 108     -23.832  15.001 -55.287  1.00 59.43           H  
ATOM    898  HB3 TYR A 108     -22.618  16.072 -57.143  1.00 60.86           H  
ATOM    899  HB2 TYR A 108     -23.668  17.179 -56.312  1.00 60.86           H  
ATOM    900  HD1 TYR A 108     -23.038  15.456 -59.525  1.00 65.11           H  
ATOM    901  HD2 TYR A 108     -25.674  18.129 -57.385  1.00 65.15           H  
ATOM    902  HE1 TYR A 108     -24.079  16.152 -61.665  1.00 66.42           H  
ATOM    903  HE2 TYR A 108     -26.717  18.813 -59.517  1.00 66.32           H  
ATOM    904  HH  TYR A 108     -26.984  18.116 -61.777  1.00 71.20           H  
ATOM    905  N   HIS A 109     -26.775  14.681 -56.470  1.00 56.95           N  
ANISOU  905  N   HIS A 109     8530   6189   6920    181   -306    382
ATOM    906  CA  HIS A 109     -28.191  14.839 -56.128  1.00 56.26           C  
ANISOU  906  CA  HIS A 109     8423   6063   6891    184   -335    414
ATOM    907  C   HIS A 109     -28.534  14.191 -54.775  1.00 54.42           C  
ANISOU  907  C   HIS A 109     8159   5823   6693    200   -324    394
ATOM    908  O   HIS A 109     -29.503  14.599 -54.140  1.00 55.10           O  
ANISOU  908  O   HIS A 109     8203   5915   6819    214   -335    431
ATOM    909  CB  HIS A 109     -29.082  14.278 -57.248  1.00 58.19           C  
ANISOU  909  CB  HIS A 109     8687   6313   7109    162   -395    445
ATOM    910  CG  HIS A 109     -28.831  14.875 -58.611  1.00 62.10           C  
ANISOU  910  CG  HIS A 109     9206   6819   7570    148   -407    469
ATOM    911  ND1 HIS A 109     -28.039  14.245 -59.547  1.00 64.43           N  
ANISOU  911  ND1 HIS A 109     9486   7099   7894    148   -400    513
ATOM    912  CD2 HIS A 109     -29.257  16.038 -59.216  1.00 63.53           C  
ANISOU  912  CD2 HIS A 109     9434   7026   7679    142   -426    456
ATOM    913  CE1 HIS A 109     -28.001  15.018 -60.634  1.00 65.23           C  
ANISOU  913  CE1 HIS A 109     9614   7221   7951    122   -418    531
ATOM    914  NE2 HIS A 109     -28.723  16.130 -60.504  1.00 65.00           N  
ANISOU  914  NE2 HIS A 109     9613   7224   7858    121   -429    497
ATOM    915  H   HIS A 109     -26.552  13.952 -57.147  1.00 56.95           H  
ATOM    916  HA  HIS A 109     -28.410  15.903 -56.041  1.00 56.26           H  
ATOM    917  HB3 HIS A 109     -30.133  14.427 -56.993  1.00 58.19           H  
ATOM    918  HB2 HIS A 109     -28.942  13.197 -57.323  1.00 58.19           H  
ATOM    919  HD1 HIS A 109     -27.503  13.385 -59.364  1.00 64.43           H  
ATOM    920  HD2 HIS A 109     -29.890  16.817 -58.827  1.00 63.53           H  
ATOM    921  HE1 HIS A 109     -27.425  14.774 -61.515  1.00 65.23           H  
ATOM    922  N   MET A 110     -27.728  13.213 -54.359  1.00 52.67           N  
ANISOU  922  N   MET A 110     7951   5611   6448    207   -303    343
ATOM    923  CA  MET A 110     -27.814  12.543 -53.066  1.00 52.05           C  
ANISOU  923  CA  MET A 110     7851   5528   6397    215   -296    322
ATOM    924  C   MET A 110     -26.790  13.137 -52.085  1.00 50.29           C  
ANISOU  924  C   MET A 110     7611   5315   6183    230   -236    288
ATOM    925  O   MET A 110     -25.911  13.897 -52.495  1.00 50.74           O  
ANISOU  925  O   MET A 110     7678   5398   6203    222   -211    282
ATOM    926  CB  MET A 110     -27.581  11.042 -53.285  1.00 53.46           C  
ANISOU  926  CB  MET A 110     8090   5696   6525    210   -341    296
ATOM    927  CG  MET A 110     -28.658  10.392 -54.173  1.00 57.61           C  
ANISOU  927  CG  MET A 110     8659   6203   7028    165   -422    338
ATOM    928  SD  MET A 110     -30.324  10.400 -53.448  1.00 64.30           S  
ANISOU  928  SD  MET A 110     9418   7084   7929    106   -464    422
ATOM    929  CE  MET A 110     -30.099   9.069 -52.247  1.00 63.57           C  
ANISOU  929  CE  MET A 110     9349   6975   7829     81   -487    397
ATOM    930  H   MET A 110     -26.936  12.975 -54.939  1.00 52.67           H  
ATOM    931  HA  MET A 110     -28.804  12.690 -52.634  1.00 52.05           H  
ATOM    932  HB3 MET A 110     -27.566  10.542 -52.317  1.00 53.46           H  
ATOM    933  HB2 MET A 110     -26.597  10.875 -53.726  1.00 53.46           H  
ATOM    934  HG3 MET A 110     -28.378   9.365 -54.404  1.00 57.61           H  
ATOM    935  HG2 MET A 110     -28.712  10.898 -55.136  1.00 57.61           H  
ATOM    936  HE1 MET A 110     -31.041   8.837 -51.751  1.00 63.57           H  
ATOM    937  HE2 MET A 110     -29.748   8.178 -52.766  1.00 63.57           H  
ATOM    938  HE3 MET A 110     -29.364   9.340 -51.490  1.00 63.57           H  
ATOM    939  N   ASN A 111     -26.925  12.830 -50.788  1.00 48.56           N  
ANISOU  939  N   ASN A 111     7358   5088   6003    240   -218    278
ATOM    940  CA  ASN A 111     -26.038  13.347 -49.738  1.00 46.96           C  
ANISOU  940  CA  ASN A 111     7146   4891   5805    242   -169    249
ATOM    941  C   ASN A 111     -25.512  12.196 -48.879  1.00 45.00           C  
ANISOU  941  C   ASN A 111     6886   4665   5547    250   -156    212
ATOM    942  O   ASN A 111     -26.312  11.430 -48.339  1.00 44.26           O  
ANISOU  942  O   ASN A 111     6779   4561   5476    252   -181    215
ATOM    943  CB  ASN A 111     -26.781  14.323 -48.798  1.00 47.78           C  
ANISOU  943  CB  ASN A 111     7241   4962   5952    264   -152    263
ATOM    944  CG  ASN A 111     -27.258  15.655 -49.372  1.00 51.04           C  
ANISOU  944  CG  ASN A 111     7696   5334   6362    276   -163    295
ATOM    945  OD1 ASN A 111     -27.993  16.361 -48.689  1.00 51.32           O  
ANISOU  945  OD1 ASN A 111     7758   5371   6372    246   -183    314
ATOM    946  ND2 ASN A 111     -26.876  16.036 -50.588  1.00 50.99           N  
ANISOU  946  ND2 ASN A 111     7712   5291   6371    333   -153    303
ATOM    947  H   ASN A 111     -27.677  12.215 -50.482  1.00 48.56           H  
ATOM    948  HA  ASN A 111     -25.193  13.870 -50.180  1.00 46.96           H  
ATOM    949  HB3 ASN A 111     -26.125  14.580 -47.965  1.00 47.78           H  
ATOM    950  HB2 ASN A 111     -27.639  13.822 -48.352  1.00 47.78           H  
ATOM    951 HD22 ASN A 111     -27.203  16.912 -50.958  1.00 50.99           H  
ATOM    952 HD21 ASN A 111     -26.327  15.431 -51.199  1.00 50.99           H  
ATOM    953  N   SER A 112     -24.193  12.165 -48.675  1.00 44.55           N  
ANISOU  953  N   SER A 112     6824   4650   5452    248   -120    190
ATOM    954  CA  SER A 112     -23.559  11.429 -47.590  1.00 44.85           C  
ANISOU  954  CA  SER A 112     6846   4713   5482    267   -100    159
ATOM    955  C   SER A 112     -23.733  12.229 -46.289  1.00 45.53           C  
ANISOU  955  C   SER A 112     6903   4776   5620    244    -74    158
ATOM    956  O   SER A 112     -23.210  13.339 -46.211  1.00 46.28           O  
ANISOU  956  O   SER A 112     7010   4864   5711    211    -57    172
ATOM    957  CB  SER A 112     -22.055  11.286 -47.890  1.00 45.11           C  
ANISOU  957  CB  SER A 112     6865   4837   5438    285    -67    152
ATOM    958  OG  SER A 112     -21.808  10.301 -48.868  1.00 47.31           O  
ANISOU  958  OG  SER A 112     7182   5149   5643    350    -85    140
ATOM    959  H   SER A 112     -23.612  12.871 -49.121  1.00 44.55           H  
ATOM    960  HA  SER A 112     -24.006  10.439 -47.478  1.00 44.85           H  
ATOM    961  HB3 SER A 112     -21.504  11.007 -46.991  1.00 45.11           H  
ATOM    962  HB2 SER A 112     -21.646  12.235 -48.234  1.00 45.11           H  
ATOM    963  HG  SER A 112     -21.789  10.754 -49.734  1.00 47.31           H  
ATOM    964  N   VAL A 113     -24.444  11.683 -45.296  1.00 44.45           N  
ANISOU  964  N   VAL A 113     6745   4625   5520    257    -79    147
ATOM    965  CA  VAL A 113     -24.612  12.329 -43.994  1.00 45.31           C  
ANISOU  965  CA  VAL A 113     6831   4721   5664    255    -50    143
ATOM    966  C   VAL A 113     -24.050  11.415 -42.879  1.00 46.18           C  
ANISOU  966  C   VAL A 113     6913   4858   5775    253    -33    117
ATOM    967  O   VAL A 113     -24.232  10.193 -42.957  1.00 45.82           O  
ANISOU  967  O   VAL A 113     6867   4819   5723    261    -61    113
ATOM    968  CB  VAL A 113     -26.108  12.642 -43.713  1.00 45.01           C  
ANISOU  968  CB  VAL A 113     6772   4668   5663    288    -64    172
ATOM    969  CG1 VAL A 113     -26.622  13.757 -44.645  1.00 44.59           C  
ANISOU  969  CG1 VAL A 113     6755   4583   5603    307    -75    197
ATOM    970  CG2 VAL A 113     -27.045  11.416 -43.742  1.00 45.07           C  
ANISOU  970  CG2 VAL A 113     6738   4706   5678    278   -107    199
ATOM    971  H   VAL A 113     -24.850  10.754 -45.405  1.00 44.45           H  
ATOM    972  HA  VAL A 113     -24.076  13.275 -43.996  1.00 45.31           H  
ATOM    973  HB  VAL A 113     -26.164  13.052 -42.702  1.00 45.01           H  
ATOM    974 HG11 VAL A 113     -27.652  14.031 -44.417  1.00 44.59           H  
ATOM    975 HG12 VAL A 113     -26.023  14.663 -44.542  1.00 44.59           H  
ATOM    976 HG13 VAL A 113     -26.576  13.457 -45.693  1.00 44.59           H  
ATOM    977 HG21 VAL A 113     -28.082  11.707 -43.599  1.00 45.07           H  
ATOM    978 HG22 VAL A 113     -26.987  10.891 -44.694  1.00 45.07           H  
ATOM    979 HG23 VAL A 113     -26.814  10.703 -42.952  1.00 45.07           H  
ATOM    980  N   PRO A 114     -23.347  12.001 -41.882  1.00 46.80           N  
ANISOU  980  N   PRO A 114     6985   4944   5852    235      3    103
ATOM    981  CA  PRO A 114     -22.883  11.242 -40.714  1.00 47.17           C  
ANISOU  981  CA  PRO A 114     6999   5023   5902    233     20     83
ATOM    982  C   PRO A 114     -24.063  10.853 -39.807  1.00 47.63           C  
ANISOU  982  C   PRO A 114     7025   5072   6002    252     10     88
ATOM    983  O   PRO A 114     -24.884  11.707 -39.467  1.00 47.90           O  
ANISOU  983  O   PRO A 114     7055   5091   6053    278     13    104
ATOM    984  CB  PRO A 114     -21.896  12.197 -40.025  1.00 47.85           C  
ANISOU  984  CB  PRO A 114     7095   5121   5965    190     53     78
ATOM    985  CG  PRO A 114     -22.378  13.592 -40.385  1.00 48.02           C  
ANISOU  985  CG  PRO A 114     7180   5077   5989    181     42     91
ATOM    986  CD  PRO A 114     -22.960  13.414 -41.783  1.00 46.37           C  
ANISOU  986  CD  PRO A 114     6977   4856   5786    208     16    110
ATOM    987  HA  PRO A 114     -22.355  10.345 -41.033  1.00 47.17           H  
ATOM    988  HB3 PRO A 114     -20.898  12.030 -40.432  1.00 47.85           H  
ATOM    989  HB2 PRO A 114     -21.833  12.048 -38.948  1.00 47.85           H  
ATOM    990  HG3 PRO A 114     -21.593  14.349 -40.337  1.00 48.02           H  
ATOM    991  HG2 PRO A 114     -23.174  13.890 -39.700  1.00 48.02           H  
ATOM    992  HD2 PRO A 114     -23.793  14.102 -41.941  1.00 46.37           H  
ATOM    993  HD3 PRO A 114     -22.200  13.617 -42.540  1.00 46.37           H  
ATOM    994  N   ILE A 115     -24.129   9.571 -39.433  1.00 47.05           N  
ANISOU  994  N   ILE A 115     6929   5017   5929    247     -8     84
ATOM    995  CA  ILE A 115     -25.047   9.080 -38.417  1.00 48.70           C  
ANISOU  995  CA  ILE A 115     7091   5248   6165    241    -24    106
ATOM    996  C   ILE A 115     -24.422   9.452 -37.065  1.00 50.07           C  
ANISOU  996  C   ILE A 115     7239   5441   6346    244     25     80
ATOM    997  O   ILE A 115     -23.296   9.041 -36.778  1.00 50.28           O  
ANISOU  997  O   ILE A 115     7271   5477   6357    229     40     56
ATOM    998  CB  ILE A 115     -25.257   7.535 -38.484  1.00 50.18           C  
ANISOU  998  CB  ILE A 115     7295   5432   6338    208    -87    122
ATOM    999  CG1 ILE A 115     -25.710   7.099 -39.899  1.00 51.05           C  
ANISOU  999  CG1 ILE A 115     7467   5506   6424    198   -145    140
ATOM   1000  CG2 ILE A 115     -26.270   7.055 -37.417  1.00 50.96           C  
ANISOU 1000  CG2 ILE A 115     7327   5582   6453    173   -113    169
ATOM   1001  CD1 ILE A 115     -25.842   5.579 -40.096  1.00 52.22           C  
ANISOU 1001  CD1 ILE A 115     7698   5612   6533    165   -229    149
ATOM   1002  H   ILE A 115     -23.340   8.959 -39.649  1.00 47.05           H  
ATOM   1003  HA  ILE A 115     -26.016   9.574 -38.527  1.00 48.70           H  
ATOM   1004  HB  ILE A 115     -24.303   7.047 -38.277  1.00 50.18           H  
ATOM   1005 HG13 ILE A 115     -25.000   7.464 -40.643  1.00 51.05           H  
ATOM   1006 HG12 ILE A 115     -26.660   7.580 -40.138  1.00 51.05           H  
ATOM   1007 HG21 ILE A 115     -26.421   5.978 -37.439  1.00 50.96           H  
ATOM   1008 HG22 ILE A 115     -25.955   7.293 -36.400  1.00 50.96           H  
ATOM   1009 HG23 ILE A 115     -27.244   7.519 -37.566  1.00 50.96           H  
ATOM   1010 HD11 ILE A 115     -25.253   5.249 -40.951  1.00 52.22           H  
ATOM   1011 HD12 ILE A 115     -25.499   5.010 -39.231  1.00 52.22           H  
ATOM   1012 HD13 ILE A 115     -26.875   5.295 -40.293  1.00 52.22           H  
ATOM   1013  N   GLN A 116     -25.145  10.278 -36.306  1.00 51.60           N  
ANISOU 1013  N   GLN A 116     7415   5644   6548    276     51     86
ATOM   1014  CA  GLN A 116     -24.689  10.814 -35.032  1.00 53.72           C  
ANISOU 1014  CA  GLN A 116     7682   5919   6810    283     90     60
ATOM   1015  C   GLN A 116     -25.489  10.128 -33.926  1.00 55.94           C  
ANISOU 1015  C   GLN A 116     7885   6268   7102    293     87     83
ATOM   1016  O   GLN A 116     -26.696   9.956 -34.083  1.00 57.40           O  
ANISOU 1016  O   GLN A 116     8016   6508   7285    322     67    130
ATOM   1017  CB  GLN A 116     -24.893  12.341 -35.022  1.00 56.10           C  
ANISOU 1017  CB  GLN A 116     8052   6173   7089    333    112     47
ATOM   1018  CG  GLN A 116     -24.288  13.032 -36.271  1.00 63.01           C  
ANISOU 1018  CG  GLN A 116     9005   6987   7949    307     98     45
ATOM   1019  CD  GLN A 116     -23.556  14.335 -35.969  1.00 72.84           C  
ANISOU 1019  CD  GLN A 116    10344   8177   9154    257    103     24
ATOM   1020  OE1 GLN A 116     -23.938  15.092 -35.088  1.00 74.64           O  
ANISOU 1020  OE1 GLN A 116    10622   8378   9360    272    116      4
ATOM   1021  NE2 GLN A 116     -22.496  14.628 -36.706  1.00 76.08           N  
ANISOU 1021  NE2 GLN A 116    10788   8577   9542    187     86     39
ATOM   1022  H   GLN A 116     -26.077  10.553 -36.569  1.00 51.60           H  
ATOM   1023  HA  GLN A 116     -23.631  10.617 -34.888  1.00 53.72           H  
ATOM   1024  HB3 GLN A 116     -24.441  12.724 -34.105  1.00 56.10           H  
ATOM   1025  HB2 GLN A 116     -25.955  12.590 -34.946  1.00 56.10           H  
ATOM   1026  HG3 GLN A 116     -25.075  13.240 -36.997  1.00 63.01           H  
ATOM   1027  HG2 GLN A 116     -23.582  12.367 -36.770  1.00 63.01           H  
ATOM   1028 HE22 GLN A 116     -21.993  15.475 -36.504  1.00 76.08           H  
ATOM   1029 HE21 GLN A 116     -22.098  13.944 -37.335  1.00 76.08           H  
ATOM   1030  N   GLN A 117     -24.801   9.719 -32.859  1.00 55.79           N  
ANISOU 1030  N   GLN A 117     7848   6265   7083    261    102     62
ATOM   1031  CA  GLN A 117     -25.393   9.050 -31.711  1.00 55.52           C  
ANISOU 1031  CA  GLN A 117     7739   6302   7053    256     98     87
ATOM   1032  C   GLN A 117     -25.039   9.835 -30.447  1.00 54.43           C  
ANISOU 1032  C   GLN A 117     7608   6175   6899    287    148     54
ATOM   1033  O   GLN A 117     -23.881  10.231 -30.290  1.00 54.11           O  
ANISOU 1033  O   GLN A 117     7632   6081   6848    263    170     14
ATOM   1034  CB  GLN A 117     -24.823   7.617 -31.616  1.00 57.89           C  
ANISOU 1034  CB  GLN A 117     8031   6603   7361    190     60     93
ATOM   1035  CG  GLN A 117     -25.311   6.650 -32.719  1.00 65.19           C  
ANISOU 1035  CG  GLN A 117     8986   7501   8282    157    -10    125
ATOM   1036  CD  GLN A 117     -26.809   6.364 -32.643  1.00 75.61           C  
ANISOU 1036  CD  GLN A 117    10244   8889   9597    124    -62    201
ATOM   1037  OE1 GLN A 117     -27.445   6.588 -31.622  1.00 79.31           O  
ANISOU 1037  OE1 GLN A 117    10627   9450  10059    117    -55    241
ATOM   1038  NE2 GLN A 117     -27.412   5.839 -33.699  1.00 77.76           N  
ANISOU 1038  NE2 GLN A 117    10549   9138   9858     97   -119    235
ATOM   1039  H   GLN A 117     -23.798   9.895 -32.794  1.00 55.79           H  
ATOM   1040  HA  GLN A 117     -26.481   9.020 -31.792  1.00 55.52           H  
ATOM   1041  HB3 GLN A 117     -25.082   7.192 -30.642  1.00 57.89           H  
ATOM   1042  HB2 GLN A 117     -23.733   7.662 -31.628  1.00 57.89           H  
ATOM   1043  HG3 GLN A 117     -24.785   5.700 -32.621  1.00 65.19           H  
ATOM   1044  HG2 GLN A 117     -25.080   7.051 -33.705  1.00 65.19           H  
ATOM   1045 HE22 GLN A 117     -28.391   5.622 -33.605  1.00 77.76           H  
ATOM   1046 HE21 GLN A 117     -26.939   5.608 -34.563  1.00 77.76           H  
ATOM   1047  N   GLU A 118     -26.022  10.005 -29.555  1.00 53.79           N  
ANISOU 1047  N   GLU A 118     7459   6177   6801    332    161     81
ATOM   1048  CA  GLU A 118     -25.817  10.386 -28.164  1.00 53.45           C  
ANISOU 1048  CA  GLU A 118     7431   6148   6730    369    204     48
ATOM   1049  C   GLU A 118     -25.068   9.255 -27.437  1.00 51.64           C  
ANISOU 1049  C   GLU A 118     7151   5950   6521    287    196     49
ATOM   1050  O   GLU A 118     -25.600   8.150 -27.311  1.00 51.66           O  
ANISOU 1050  O   GLU A 118     7071   6023   6536    247    162     99
ATOM   1051  CB  GLU A 118     -27.179  10.640 -27.491  1.00 57.49           C  
ANISOU 1051  CB  GLU A 118     7887   6762   7195    485    226     81
ATOM   1052  CG  GLU A 118     -27.751  12.068 -27.661  1.00 68.04           C  
ANISOU 1052  CG  GLU A 118     9346   8028   8480    607    254     40
ATOM   1053  CD  GLU A 118     -28.981  12.331 -26.781  1.00 81.12           C  
ANISOU 1053  CD  GLU A 118    10967   9794  10060    777    286     66
ATOM   1054  OE1 GLU A 118     -29.617  11.367 -26.289  1.00 84.47           O  
ANISOU 1054  OE1 GLU A 118    11238  10386  10470    789    291    130
ATOM   1055  OE2 GLU A 118     -29.152  13.491 -26.368  1.00 84.57           O1-
ANISOU 1055  OE2 GLU A 118    11539  10157  10438    906    302     29
ATOM   1056  H   GLU A 118     -26.942   9.647 -29.763  1.00 53.79           H  
ATOM   1057  HA  GLU A 118     -25.222  11.301 -28.123  1.00 53.45           H  
ATOM   1058  HB3 GLU A 118     -27.110  10.398 -26.430  1.00 57.49           H  
ATOM   1059  HB2 GLU A 118     -27.914   9.941 -27.895  1.00 57.49           H  
ATOM   1060  HG3 GLU A 118     -27.976  12.282 -28.707  1.00 68.04           H  
ATOM   1061  HG2 GLU A 118     -26.995  12.795 -27.362  1.00 68.04           H  
ATOM   1062  N   ILE A 119     -23.853   9.556 -26.984  1.00 50.54           N  
ANISOU 1062  N   ILE A 119     7070   5757   6377    247    217      3
ATOM   1063  CA  ILE A 119     -22.977   8.650 -26.259  1.00 49.39           C  
ANISOU 1063  CA  ILE A 119     6889   5635   6243    178    215     -1
ATOM   1064  C   ILE A 119     -22.677   9.263 -24.879  1.00 47.62           C  
ANISOU 1064  C   ILE A 119     6677   5428   5988    183    251    -27
ATOM   1065  O   ILE A 119     -22.485  10.476 -24.763  1.00 46.93           O  
ANISOU 1065  O   ILE A 119     6679   5290   5863    218    270    -59
ATOM   1066  CB  ILE A 119     -21.664   8.398 -27.068  1.00 50.69           C  
ANISOU 1066  CB  ILE A 119     7100   5752   6409    130    208    -16
ATOM   1067  CG1 ILE A 119     -21.923   7.522 -28.322  1.00 51.68           C  
ANISOU 1067  CG1 ILE A 119     7220   5862   6552    133    165      7
ATOM   1068  CG2 ILE A 119     -20.456   7.851 -26.274  1.00 51.08           C  
ANISOU 1068  CG2 ILE A 119     7134   5830   6443     78    222    -25
ATOM   1069  CD1 ILE A 119     -22.385   6.078 -28.041  1.00 52.79           C  
ANISOU 1069  CD1 ILE A 119     7321   6031   6705    114    121     39
ATOM   1070  H   ILE A 119     -23.506  10.510 -27.081  1.00 50.54           H  
ATOM   1071  HA  ILE A 119     -23.478   7.695 -26.093  1.00 49.39           H  
ATOM   1072  HB  ILE A 119     -21.346   9.370 -27.446  1.00 50.69           H  
ATOM   1073 HG13 ILE A 119     -21.022   7.499 -28.932  1.00 51.68           H  
ATOM   1074 HG12 ILE A 119     -22.670   8.015 -28.945  1.00 51.68           H  
ATOM   1075 HG21 ILE A 119     -19.621   7.612 -26.937  1.00 51.08           H  
ATOM   1076 HG22 ILE A 119     -20.082   8.582 -25.555  1.00 51.08           H  
ATOM   1077 HG23 ILE A 119     -20.712   6.947 -25.722  1.00 51.08           H  
ATOM   1078 HD11 ILE A 119     -22.184   5.428 -28.896  1.00 52.79           H  
ATOM   1079 HD12 ILE A 119     -21.880   5.636 -27.181  1.00 52.79           H  
ATOM   1080 HD13 ILE A 119     -23.459   6.033 -27.856  1.00 52.79           H  
ATOM   1081  N   LEU A 120     -22.648   8.415 -23.849  1.00 46.81           N  
ANISOU 1081  N   LEU A 120     6507   5386   5893    147    251    -15
ATOM   1082  CA  LEU A 120     -22.207   8.772 -22.509  1.00 46.97           C  
ANISOU 1082  CA  LEU A 120     6539   5426   5882    140    282    -39
ATOM   1083  C   LEU A 120     -20.692   8.545 -22.408  1.00 45.47           C  
ANISOU 1083  C   LEU A 120     6373   5215   5690     55    284    -53
ATOM   1084  O   LEU A 120     -20.182   7.544 -22.906  1.00 45.87           O  
ANISOU 1084  O   LEU A 120     6383   5280   5764     23    264    -33
ATOM   1085  CB  LEU A 120     -22.942   7.902 -21.463  1.00 48.27           C  
ANISOU 1085  CB  LEU A 120     6596   5693   6049    141    279     -4
ATOM   1086  CG  LEU A 120     -24.460   8.145 -21.342  1.00 50.97           C  
ANISOU 1086  CG  LEU A 120     6875   6122   6368    223    281     36
ATOM   1087  CD1 LEU A 120     -25.105   7.079 -20.442  1.00 51.76           C  
ANISOU 1087  CD1 LEU A 120     6856   6347   6463    190    265     93
ATOM   1088  CD2 LEU A 120     -24.778   9.556 -20.819  1.00 52.32           C  
ANISOU 1088  CD2 LEU A 120     7122   6282   6475    343    326     -5
ATOM   1089  H   LEU A 120     -22.680   7.412 -24.038  1.00 46.81           H  
ATOM   1090  HA  LEU A 120     -22.425   9.821 -22.318  1.00 46.97           H  
ATOM   1091  HB3 LEU A 120     -22.478   8.060 -20.490  1.00 48.27           H  
ATOM   1092  HB2 LEU A 120     -22.783   6.855 -21.700  1.00 48.27           H  
ATOM   1093  HG  LEU A 120     -24.909   8.041 -22.330  1.00 50.97           H  
ATOM   1094 HD11 LEU A 120     -26.191   7.172 -20.424  1.00 51.76           H  
ATOM   1095 HD12 LEU A 120     -24.877   6.071 -20.786  1.00 51.76           H  
ATOM   1096 HD13 LEU A 120     -24.754   7.165 -19.413  1.00 51.76           H  
ATOM   1097 HD21 LEU A 120     -25.794   9.618 -20.430  1.00 52.32           H  
ATOM   1098 HD22 LEU A 120     -24.093   9.866 -20.028  1.00 52.32           H  
ATOM   1099 HD23 LEU A 120     -24.691  10.290 -21.617  1.00 52.32           H  
ATOM   1100  N   VAL A 121     -19.994   9.438 -21.720  1.00 43.53           N  
ANISOU 1100  N   VAL A 121     6199   4942   5400     24    300    -80
ATOM   1101  CA  VAL A 121     -18.591   9.304 -21.358  1.00 43.64           C  
ANISOU 1101  CA  VAL A 121     6215   4976   5392    -72    300    -72
ATOM   1102  C   VAL A 121     -18.453   9.665 -19.872  1.00 44.91           C  
ANISOU 1102  C   VAL A 121     6392   5156   5515   -101    315    -89
ATOM   1103  O   VAL A 121     -19.290  10.393 -19.337  1.00 44.71           O  
ANISOU 1103  O   VAL A 121     6419   5107   5462    -34    326   -117
ATOM   1104  CB  VAL A 121     -17.693  10.243 -22.217  1.00 43.62           C  
ANISOU 1104  CB  VAL A 121     6294   4930   5349   -137    284    -64
ATOM   1105  CG1 VAL A 121     -17.714   9.816 -23.692  1.00 42.54           C  
ANISOU 1105  CG1 VAL A 121     6129   4793   5242   -107    273    -46
ATOM   1106  CG2 VAL A 121     -17.997  11.754 -22.084  1.00 44.22           C  
ANISOU 1106  CG2 VAL A 121     6525   4906   5372   -136    270    -95
ATOM   1107  H   VAL A 121     -20.460  10.270 -21.354  1.00 43.53           H  
ATOM   1108  HA  VAL A 121     -18.258   8.269 -21.483  1.00 43.64           H  
ATOM   1109  HB  VAL A 121     -16.668  10.093 -21.876  1.00 43.62           H  
ATOM   1110 HG11 VAL A 121     -17.051  10.424 -24.298  1.00 42.54           H  
ATOM   1111 HG12 VAL A 121     -17.398   8.781 -23.804  1.00 42.54           H  
ATOM   1112 HG13 VAL A 121     -18.712   9.907 -24.118  1.00 42.54           H  
ATOM   1113 HG21 VAL A 121     -17.400  12.350 -22.771  1.00 44.22           H  
ATOM   1114 HG22 VAL A 121     -19.041  11.978 -22.300  1.00 44.22           H  
ATOM   1115 HG23 VAL A 121     -17.783  12.128 -21.084  1.00 44.22           H  
ATOM   1116  N   LEU A 122     -17.415   9.139 -19.221  1.00 45.68           N  
ANISOU 1116  N   LEU A 122     6453   5307   5595   -188    316    -68
ATOM   1117  CA  LEU A 122     -17.039   9.542 -17.874  1.00 47.16           C  
ANISOU 1117  CA  LEU A 122     6666   5514   5740   -236    324    -80
ATOM   1118  C   LEU A 122     -16.064  10.712 -18.019  1.00 48.52           C  
ANISOU 1118  C   LEU A 122     6961   5638   5837   -342    297    -76
ATOM   1119  O   LEU A 122     -15.034  10.524 -18.667  1.00 49.93           O  
ANISOU 1119  O   LEU A 122     7108   5862   5999   -426    283    -30
ATOM   1120  CB  LEU A 122     -16.330   8.364 -17.171  1.00 46.95           C  
ANISOU 1120  CB  LEU A 122     6519   5588   5733   -279    332    -47
ATOM   1121  CG  LEU A 122     -17.188   7.119 -16.882  1.00 48.55           C  
ANISOU 1121  CG  LEU A 122     6623   5830   5995   -210    335    -38
ATOM   1122  CD1 LEU A 122     -16.345   5.982 -16.269  1.00 49.19           C  
ANISOU 1122  CD1 LEU A 122     6620   5990   6082   -249    332     -4
ATOM   1123  CD2 LEU A 122     -18.382   7.447 -15.983  1.00 48.56           C  
ANISOU 1123  CD2 LEU A 122     6627   5835   5988   -152    349    -60
ATOM   1124  H   LEU A 122     -16.716   8.585 -19.712  1.00 45.68           H  
ATOM   1125  HA  LEU A 122     -17.907   9.863 -17.295  1.00 47.16           H  
ATOM   1126  HB3 LEU A 122     -15.913   8.715 -16.232  1.00 46.95           H  
ATOM   1127  HB2 LEU A 122     -15.483   8.072 -17.781  1.00 46.95           H  
ATOM   1128  HG  LEU A 122     -17.572   6.757 -17.837  1.00 48.55           H  
ATOM   1129 HD11 LEU A 122     -16.677   5.012 -16.639  1.00 49.19           H  
ATOM   1130 HD12 LEU A 122     -15.285   6.073 -16.507  1.00 49.19           H  
ATOM   1131 HD13 LEU A 122     -16.425   5.958 -15.180  1.00 49.19           H  
ATOM   1132 HD21 LEU A 122     -18.972   6.554 -15.785  1.00 48.56           H  
ATOM   1133 HD22 LEU A 122     -18.042   7.853 -15.031  1.00 48.56           H  
ATOM   1134 HD23 LEU A 122     -19.051   8.178 -16.431  1.00 48.56           H  
ATOM   1135  N   ARG A 123     -16.379  11.866 -17.423  1.00 48.49           N  
ANISOU 1135  N   ARG A 123     7110   5544   5770   -336    283   -116
ATOM   1136  CA  ARG A 123     -15.413  12.951 -17.252  1.00 49.31           C  
ANISOU 1136  CA  ARG A 123     7370   5582   5783   -471    232   -103
ATOM   1137  C   ARG A 123     -14.942  12.945 -15.794  1.00 49.51           C  
ANISOU 1137  C   ARG A 123     7420   5639   5753   -555    224   -102
ATOM   1138  O   ARG A 123     -15.768  12.700 -14.916  1.00 48.62           O  
ANISOU 1138  O   ARG A 123     7324   5515   5636   -458    251   -149
ATOM   1139  CB  ARG A 123     -16.032  14.304 -17.650  1.00 50.73           C  
ANISOU 1139  CB  ARG A 123     7769   5602   5905   -412    197   -149
ATOM   1140  CG  ARG A 123     -14.996  15.449 -17.516  1.00 53.65           C  
ANISOU 1140  CG  ARG A 123     8331   5887   6168   -591    116   -121
ATOM   1141  CD  ARG A 123     -15.295  16.734 -18.294  1.00 55.55           C  
ANISOU 1141  CD  ARG A 123     8750   5989   6367   -584     64   -128
ATOM   1142  NE  ARG A 123     -15.425  16.473 -19.737  1.00 57.09           N  
ANISOU 1142  NE  ARG A 123     8799   6244   6647   -536     94   -101
ATOM   1143  CZ  ARG A 123     -14.509  16.151 -20.660  1.00 55.67           C  
ANISOU 1143  CZ  ARG A 123     8539   6145   6468   -669     72    -27
ATOM   1144  NH1 ARG A 123     -13.197  16.133 -20.422  1.00 55.52           N  
ANISOU 1144  NH1 ARG A 123     8544   6183   6369   -874     19     44
ATOM   1145  NH2 ARG A 123     -14.942  15.832 -21.870  1.00 53.60           N1+
ANISOU 1145  NH2 ARG A 123     8164   5927   6273   -599    100    -14
ATOM   1146  H   ARG A 123     -17.234  11.932 -16.873  1.00 48.49           H  
ATOM   1147  HA  ARG A 123     -14.546  12.787 -17.895  1.00 49.31           H  
ATOM   1148  HB3 ARG A 123     -16.904  14.518 -17.032  1.00 50.73           H  
ATOM   1149  HB2 ARG A 123     -16.401  14.224 -18.674  1.00 50.73           H  
ATOM   1150  HG3 ARG A 123     -14.003  15.099 -17.799  1.00 53.65           H  
ATOM   1151  HG2 ARG A 123     -14.908  15.710 -16.460  1.00 53.65           H  
ATOM   1152  HD3 ARG A 123     -14.497  17.458 -18.133  1.00 55.55           H  
ATOM   1153  HD2 ARG A 123     -16.202  17.197 -17.908  1.00 55.55           H  
ATOM   1154 HH22 ARG A 123     -14.234  15.604 -22.591  1.00 53.60           H  
ATOM   1155 HH21 ARG A 123     -15.945  15.776 -22.065  1.00 53.60           H  
ATOM   1156 HH12 ARG A 123     -12.511  15.866 -21.154  1.00 55.52           H  
ATOM   1157 HH11 ARG A 123     -12.812  16.346 -19.520  1.00 55.52           H  
ATOM   1158  HE  ARG A 123     -16.414  16.431 -20.031  1.00 57.09           H  
ATOM   1159  N   ARG A 124     -13.644  13.191 -15.563  1.00 49.87           N  
ANISOU 1159  N   ARG A 124     7455   5748   5746   -736    189    -38
ATOM   1160  CA  ARG A 124     -13.050  13.313 -14.227  1.00 51.26           C  
ANISOU 1160  CA  ARG A 124     7658   5960   5858   -844    171    -24
ATOM   1161  C   ARG A 124     -13.683  14.481 -13.448  1.00 53.48           C  
ANISOU 1161  C   ARG A 124     8190   6080   6049   -827    131    -91
ATOM   1162  O   ARG A 124     -13.750  15.589 -13.981  1.00 53.80           O  
ANISOU 1162  O   ARG A 124     8437   5984   6019   -865     70   -102
ATOM   1163  CB  ARG A 124     -11.527  13.521 -14.354  1.00 51.58           C  
ANISOU 1163  CB  ARG A 124     7663   6107   5829  -1063    122     78
ATOM   1164  CG  ARG A 124     -10.803  12.369 -15.068  1.00 52.54           C  
ANISOU 1164  CG  ARG A 124     7544   6409   6009  -1044    165    147
ATOM   1165  CD  ARG A 124      -9.285  12.591 -15.184  1.00 53.35           C  
ANISOU 1165  CD  ARG A 124     7565   6681   6023  -1235    128    269
ATOM   1166  NE  ARG A 124      -8.647  11.619 -16.092  1.00 54.46           N  
ANISOU 1166  NE  ARG A 124     7502   6995   6197  -1165    172    330
ATOM   1167  CZ  ARG A 124      -8.362  10.328 -15.897  1.00 58.03           C  
ANISOU 1167  CZ  ARG A 124     7784   7574   6692  -1064    226    342
ATOM   1168  NH1 ARG A 124      -8.637   9.718 -14.741  1.00 57.70           N  
ANISOU 1168  NH1 ARG A 124     7730   7512   6681  -1038    246    303
ATOM   1169  NH2 ARG A 124      -7.793   9.652 -16.894  1.00 58.13           N1+
ANISOU 1169  NH2 ARG A 124     7653   7723   6710   -972    259    391
ATOM   1170  H   ARG A 124     -13.034  13.406 -16.345  1.00 49.87           H  
ATOM   1171  HA  ARG A 124     -13.231  12.384 -13.683  1.00 51.26           H  
ATOM   1172  HB3 ARG A 124     -11.087  13.669 -13.365  1.00 51.58           H  
ATOM   1173  HB2 ARG A 124     -11.343  14.449 -14.899  1.00 51.58           H  
ATOM   1174  HG3 ARG A 124     -11.241  12.132 -16.036  1.00 52.54           H  
ATOM   1175  HG2 ARG A 124     -10.974  11.492 -14.443  1.00 52.54           H  
ATOM   1176  HD3 ARG A 124      -8.815  12.444 -14.214  1.00 53.35           H  
ATOM   1177  HD2 ARG A 124      -9.040  13.614 -15.449  1.00 53.35           H  
ATOM   1178 HH22 ARG A 124      -7.421   8.720 -16.805  1.00 58.13           H  
ATOM   1179 HH21 ARG A 124      -7.686  10.124 -17.790  1.00 58.13           H  
ATOM   1180 HH12 ARG A 124      -8.453   8.747 -14.547  1.00 57.70           H  
ATOM   1181 HH11 ARG A 124      -9.050  10.261 -13.980  1.00 57.70           H  
ATOM   1182  HE  ARG A 124      -8.350  12.060 -16.968  1.00 54.46           H  
ATOM   1183  N   GLU A 125     -14.131  14.214 -12.216  1.00 54.54           N  
ANISOU 1183  N   GLU A 125     8319   6227   6178   -746    165   -138
ATOM   1184  CA  GLU A 125     -14.695  15.219 -11.321  1.00 57.25           C  
ANISOU 1184  CA  GLU A 125     8910   6427   6414   -688    133   -208
ATOM   1185  C   GLU A 125     -14.218  14.892  -9.890  1.00 58.89           C  
ANISOU 1185  C   GLU A 125     9102   6695   6577   -746    138   -211
ATOM   1186  O   GLU A 125     -14.636  13.855  -9.365  1.00 58.76           O  
ANISOU 1186  O   GLU A 125     8890   6802   6634   -659    206   -214
ATOM   1187  CB  GLU A 125     -16.235  15.240 -11.452  1.00 61.10           C  
ANISOU 1187  CB  GLU A 125     9419   6871   6926   -430    186   -281
ATOM   1188  CG  GLU A 125     -16.901  16.289 -10.524  1.00 68.62           C  
ANISOU 1188  CG  GLU A 125    10653   7679   7740   -318    155   -358
ATOM   1189  CD  GLU A 125     -18.392  16.480 -10.778  1.00 78.29           C  
ANISOU 1189  CD  GLU A 125    11923   8869   8956    -50    198   -414
ATOM   1190  OE1 GLU A 125     -18.770  16.759 -11.931  1.00 79.36           O  
ANISOU 1190  OE1 GLU A 125    12058   8960   9134    -17    191   -403
ATOM   1191  OE2 GLU A 125     -19.199  16.375  -9.823  1.00 82.46           O1-
ANISOU 1191  OE2 GLU A 125    12476   9433   9422    132    240   -462
ATOM   1192  H   GLU A 125     -13.981  13.297 -11.802  1.00 54.54           H  
ATOM   1193  HA  GLU A 125     -14.367  16.205 -11.639  1.00 57.25           H  
ATOM   1194  HB3 GLU A 125     -16.653  14.255 -11.240  1.00 61.10           H  
ATOM   1195  HB2 GLU A 125     -16.487  15.460 -12.491  1.00 61.10           H  
ATOM   1196  HG3 GLU A 125     -16.426  17.258 -10.674  1.00 68.62           H  
ATOM   1197  HG2 GLU A 125     -16.744  16.034  -9.477  1.00 68.62           H  
ATOM   1198  N   PRO A 126     -13.375  15.741  -9.255  1.00 60.21           N  
ANISOU 1198  N   PRO A 126     9476   6781   6620   -913     57   -200
ATOM   1199  CA  PRO A 126     -12.757  16.960  -9.816  1.00 60.76           C  
ANISOU 1199  CA  PRO A 126     9808   6702   6578  -1076    -53   -176
ATOM   1200  C   PRO A 126     -11.775  16.671 -10.979  1.00 61.20           C  
ANISOU 1200  C   PRO A 126     9715   6862   6677  -1254    -79    -67
ATOM   1201  O   PRO A 126     -11.401  15.507 -11.159  1.00 60.88           O  
ANISOU 1201  O   PRO A 126     9384   7013   6734  -1263    -14    -11
ATOM   1202  CB  PRO A 126     -12.057  17.595  -8.597  1.00 61.52           C  
ANISOU 1202  CB  PRO A 126    10095   6744   6537  -1239   -130   -170
ATOM   1203  CG  PRO A 126     -11.762  16.439  -7.656  1.00 62.11           C  
ANISOU 1203  CG  PRO A 126     9906   7012   6683  -1245    -56   -143
ATOM   1204  CD  PRO A 126     -12.956  15.516  -7.871  1.00 60.24           C  
ANISOU 1204  CD  PRO A 126     9469   6845   6574   -980     58   -200
ATOM   1205  HA  PRO A 126     -13.551  17.622 -10.152  1.00 60.76           H  
ATOM   1206  HB3 PRO A 126     -12.741  18.295  -8.115  1.00 61.52           H  
ATOM   1207  HB2 PRO A 126     -11.154  18.151  -8.852  1.00 61.52           H  
ATOM   1208  HG3 PRO A 126     -11.637  16.744  -6.616  1.00 62.11           H  
ATOM   1209  HG2 PRO A 126     -10.848  15.933  -7.972  1.00 62.11           H  
ATOM   1210  HD2 PRO A 126     -12.689  14.482  -7.663  1.00 60.24           H  
ATOM   1211  HD3 PRO A 126     -13.779  15.785  -7.209  1.00 60.24           H  
ATOM   1212  N   PRO A 127     -11.369  17.717 -11.735  1.00 60.92           N  
ANISOU 1212  N   PRO A 127     9876   6711   6560  -1386   -174    -32
ATOM   1213  CA  PRO A 127     -10.351  17.581 -12.793  1.00 60.84           C  
ANISOU 1213  CA  PRO A 127     9702   6836   6576  -1544   -193     82
ATOM   1214  C   PRO A 127      -9.064  16.890 -12.312  1.00 60.75           C  
ANISOU 1214  C   PRO A 127     9482   7053   6548  -1739   -195    198
ATOM   1215  O   PRO A 127      -8.641  17.107 -11.176  1.00 61.06           O  
ANISOU 1215  O   PRO A 127     9611   7089   6500  -1872   -243    216
ATOM   1216  CB  PRO A 127     -10.096  19.026 -13.252  1.00 61.66           C  
ANISOU 1216  CB  PRO A 127    10110   6763   6556  -1697   -323    109
ATOM   1217  CG  PRO A 127     -11.394  19.755 -12.941  1.00 61.95           C  
ANISOU 1217  CG  PRO A 127    10442   6551   6545  -1508   -339    -21
ATOM   1218  CD  PRO A 127     -11.836  19.104 -11.637  1.00 60.35           C  
ANISOU 1218  CD  PRO A 127    10195   6382   6352  -1393   -276    -88
ATOM   1219  HA  PRO A 127     -10.810  17.017 -13.605  1.00 60.84           H  
ATOM   1220  HB3 PRO A 127      -9.822  19.082 -14.306  1.00 61.66           H  
ATOM   1221  HB2 PRO A 127      -9.276  19.471 -12.683  1.00 61.66           H  
ATOM   1222  HG3 PRO A 127     -12.125  19.533 -13.721  1.00 61.95           H  
ATOM   1223  HG2 PRO A 127     -11.286  20.839 -12.878  1.00 61.95           H  
ATOM   1224  HD2 PRO A 127     -11.344  19.582 -10.789  1.00 60.35           H  
ATOM   1225  HD3 PRO A 127     -12.913  19.202 -11.512  1.00 60.35           H  
ATOM   1226  N   HIS A 128      -8.512  16.025 -13.166  1.00 60.47           N  
ANISOU 1226  N   HIS A 128     9165   7222   6588  -1730   -137    275
ATOM   1227  CA  HIS A 128      -7.315  15.209 -12.953  1.00 60.61           C  
ANISOU 1227  CA  HIS A 128     8941   7503   6587  -1861   -122    397
ATOM   1228  C   HIS A 128      -7.509  14.036 -11.966  1.00 60.31           C  
ANISOU 1228  C   HIS A 128     8730   7561   6625  -1737    -36    360
ATOM   1229  O   HIS A 128      -6.550  13.301 -11.723  1.00 61.13           O  
ANISOU 1229  O   HIS A 128     8631   7884   6711  -1810    -17    457
ATOM   1230  CB  HIS A 128      -6.072  16.072 -12.604  1.00 62.41           C  
ANISOU 1230  CB  HIS A 128     9277   7785   6649  -2181   -243    520
ATOM   1231  CG  HIS A 128      -5.887  17.339 -13.415  1.00 65.65           C  
ANISOU 1231  CG  HIS A 128     9904   8078   6962  -2346   -357    567
ATOM   1232  ND1 HIS A 128      -6.111  17.411 -14.780  1.00 67.73           N  
ANISOU 1232  ND1 HIS A 128    10046   8445   7244  -2344   -347    635
ATOM   1233  CD2 HIS A 128      -5.552  18.622 -13.037  1.00 67.25           C  
ANISOU 1233  CD2 HIS A 128    10448   8068   7034  -2519   -490    560
ATOM   1234  CE1 HIS A 128      -5.921  18.677 -15.152  1.00 68.88           C  
ANISOU 1234  CE1 HIS A 128    10448   8443   7281  -2525   -473    671
ATOM   1235  NE2 HIS A 128      -5.563  19.471 -14.148  1.00 68.93           N  
ANISOU 1235  NE2 HIS A 128    10752   8246   7191  -2637   -568    627
ATOM   1236  H   HIS A 128      -8.873  16.010 -14.130  1.00 60.47           H  
ATOM   1237  HA  HIS A 128      -7.119  14.749 -13.920  1.00 60.61           H  
ATOM   1238  HB3 HIS A 128      -5.168  15.472 -12.721  1.00 62.41           H  
ATOM   1239  HB2 HIS A 128      -6.101  16.349 -11.551  1.00 62.41           H  
ATOM   1240  HD1 HIS A 128      -6.483  16.671 -15.396  1.00 67.73           H  
ATOM   1241  HD2 HIS A 128      -5.304  18.997 -12.055  1.00 67.25           H  
ATOM   1242  HE1 HIS A 128      -6.062  19.022 -16.165  1.00 68.88           H  
ATOM   1243  N   SER A 129      -8.728  13.829 -11.434  1.00 58.78           N  
ANISOU 1243  N   SER A 129     8608   7224   6501  -1550     12    233
ATOM   1244  CA  SER A 129      -9.024  12.731 -10.509  1.00 57.49           C  
ANISOU 1244  CA  SER A 129     8284   7151   6408  -1443     85    206
ATOM   1245  C   SER A 129      -8.853  11.353 -11.191  1.00 55.92           C  
ANISOU 1245  C   SER A 129     7824   7113   6308  -1327    157    244
ATOM   1246  O   SER A 129      -9.473  11.109 -12.235  1.00 55.21           O  
ANISOU 1246  O   SER A 129     7708   6980   6289  -1196    186    211
ATOM   1247  CB  SER A 129     -10.451  12.858  -9.937  1.00 57.67           C  
ANISOU 1247  CB  SER A 129     8414   7024   6475  -1260    121     81
ATOM   1248  OG  SER A 129     -10.711  11.774  -9.053  1.00 57.83           O  
ANISOU 1248  OG  SER A 129     8273   7142   6557  -1179    182     68
ATOM   1249  H   SER A 129      -9.471  14.486 -11.633  1.00 58.78           H  
ATOM   1250  HA  SER A 129      -8.341  12.859  -9.674  1.00 57.49           H  
ATOM   1251  HB3 SER A 129     -11.198  12.865 -10.734  1.00 57.67           H  
ATOM   1252  HB2 SER A 129     -10.557  13.793  -9.384  1.00 57.67           H  
ATOM   1253  HG  SER A 129     -11.581  11.916  -8.620  1.00 57.83           H  
ATOM   1254  N   PRO A 130      -8.033  10.452 -10.608  1.00 55.23           N  
ANISOU 1254  N   PRO A 130     7562   7207   6217  -1366    180    313
ATOM   1255  CA  PRO A 130      -7.919   9.098 -11.148  1.00 53.74           C  
ANISOU 1255  CA  PRO A 130     7168   7147   6103  -1223    240    340
ATOM   1256  C   PRO A 130      -9.165   8.217 -10.912  1.00 51.15           C  
ANISOU 1256  C   PRO A 130     6809   6739   5888  -1034    291    251
ATOM   1257  O   PRO A 130      -9.323   7.245 -11.650  1.00 51.91           O  
ANISOU 1257  O   PRO A 130     6800   6879   6045   -907    321    256
ATOM   1258  CB  PRO A 130      -6.654   8.561 -10.460  1.00 55.12           C  
ANISOU 1258  CB  PRO A 130     7192   7540   6213  -1319    241    447
ATOM   1259  CG  PRO A 130      -6.635   9.247  -9.103  1.00 55.77           C  
ANISOU 1259  CG  PRO A 130     7384   7582   6225  -1486    196    447
ATOM   1260  CD  PRO A 130      -7.192  10.635  -9.419  1.00 54.76           C  
ANISOU 1260  CD  PRO A 130     7499   7232   6073  -1527    149    368
ATOM   1261  HA  PRO A 130      -7.736   9.132 -12.219  1.00 53.74           H  
ATOM   1262  HB3 PRO A 130      -5.795   8.895 -11.043  1.00 55.12           H  
ATOM   1263  HB2 PRO A 130      -6.608   7.474 -10.404  1.00 55.12           H  
ATOM   1264  HG3 PRO A 130      -5.652   9.271  -8.628  1.00 55.77           H  
ATOM   1265  HG2 PRO A 130      -7.319   8.733  -8.428  1.00 55.77           H  
ATOM   1266  HD2 PRO A 130      -7.736  11.045  -8.567  1.00 54.76           H  
ATOM   1267  HD3 PRO A 130      -6.386  11.323  -9.680  1.00 54.76           H  
ATOM   1268  N   ASN A 131      -9.993   8.533  -9.900  1.00 47.75           N  
ANISOU 1268  N   ASN A 131     6472   6202   5470  -1018    292    179
ATOM   1269  CA  ASN A 131     -10.945   7.579  -9.322  1.00 44.64           C  
ANISOU 1269  CA  ASN A 131     6012   5789   5161   -876    331    128
ATOM   1270  C   ASN A 131     -12.362   8.125  -9.065  1.00 44.44           C  
ANISOU 1270  C   ASN A 131     6093   5635   5156   -784    340     42
ATOM   1271  O   ASN A 131     -13.179   7.383  -8.513  1.00 44.64           O  
ANISOU 1271  O   ASN A 131     6058   5683   5221   -710    364     20
ATOM   1272  CB  ASN A 131     -10.340   6.909  -8.055  1.00 42.75           C  
ANISOU 1272  CB  ASN A 131     5684   5654   4905   -929    339    161
ATOM   1273  CG  ASN A 131     -10.254   7.788  -6.800  1.00 44.33           C  
ANISOU 1273  CG  ASN A 131     6000   5821   5021  -1049    314    145
ATOM   1274  OD1 ASN A 131     -10.371   9.005  -6.849  1.00 45.13           O  
ANISOU 1274  OD1 ASN A 131     6276   5808   5064  -1092    282    106
ATOM   1275  ND2 ASN A 131     -10.007   7.184  -5.643  1.00 45.19           N  
ANISOU 1275  ND2 ASN A 131     6042   6014   5114  -1096    321    168
ATOM   1276  H   ASN A 131      -9.854   9.386  -9.367  1.00 47.75           H  
ATOM   1277  HA  ASN A 131     -11.142   6.787 -10.042  1.00 44.64           H  
ATOM   1278  HB3 ASN A 131      -9.337   6.547  -8.265  1.00 42.75           H  
ATOM   1279  HB2 ASN A 131     -10.937   6.029  -7.810  1.00 42.75           H  
ATOM   1280 HD22 ASN A 131      -9.923   7.754  -4.812  1.00 45.19           H  
ATOM   1281 HD21 ASN A 131      -9.914   6.182  -5.581  1.00 45.19           H  
ATOM   1282  N   SER A 132     -12.659   9.366  -9.467  1.00 44.41           N  
ANISOU 1282  N   SER A 132     6247   5515   5110   -784    318      3
ATOM   1283  CA  SER A 132     -13.976   9.965  -9.286  1.00 45.37           C  
ANISOU 1283  CA  SER A 132     6471   5537   5230   -656    332    -73
ATOM   1284  C   SER A 132     -14.389  10.694 -10.574  1.00 44.72           C  
ANISOU 1284  C   SER A 132     6497   5348   5146   -605    316    -98
ATOM   1285  O   SER A 132     -13.647  11.550 -11.064  1.00 44.53           O  
ANISOU 1285  O   SER A 132     6570   5278   5072   -712    274    -74
ATOM   1286  CB  SER A 132     -13.987  10.822  -8.000  1.00 46.53           C  
ANISOU 1286  CB  SER A 132     6758   5639   5284   -677    320   -115
ATOM   1287  OG  SER A 132     -13.192  11.989  -8.084  1.00 49.67           O  
ANISOU 1287  OG  SER A 132     7334   5956   5584   -821    259   -106
ATOM   1288  H   SER A 132     -11.972   9.958  -9.914  1.00 44.41           H  
ATOM   1289  HA  SER A 132     -14.704   9.174  -9.117  1.00 45.37           H  
ATOM   1290  HB3 SER A 132     -13.653  10.227  -7.149  1.00 46.53           H  
ATOM   1291  HB2 SER A 132     -15.010  11.129  -7.777  1.00 46.53           H  
ATOM   1292  HG  SER A 132     -13.689  12.643  -8.617  1.00 49.67           H  
ATOM   1293  N   PHE A 133     -15.548  10.314 -11.121  1.00 44.38           N  
ANISOU 1293  N   PHE A 133     6422   5285   5155   -453    345   -130
ATOM   1294  CA  PHE A 133     -16.040  10.790 -12.411  1.00 44.25           C  
ANISOU 1294  CA  PHE A 133     6468   5189   5156   -389    335   -144
ATOM   1295  C   PHE A 133     -17.499  11.250 -12.288  1.00 44.91           C  
ANISOU 1295  C   PHE A 133     6604   5234   5227   -216    359   -193
ATOM   1296  O   PHE A 133     -18.206  10.845 -11.361  1.00 44.90           O  
ANISOU 1296  O   PHE A 133     6540   5302   5216   -136    389   -203
ATOM   1297  CB  PHE A 133     -15.966   9.642 -13.451  1.00 43.22           C  
ANISOU 1297  CB  PHE A 133     6176   5127   5120   -381    346    -99
ATOM   1298  CG  PHE A 133     -14.585   9.082 -13.752  1.00 43.50           C  
ANISOU 1298  CG  PHE A 133     6132   5240   5157   -498    334    -40
ATOM   1299  CD1 PHE A 133     -14.007   8.118 -12.900  1.00 43.94           C  
ANISOU 1299  CD1 PHE A 133     6070   5398   5226   -530    346     -7
ATOM   1300  CD2 PHE A 133     -13.809   9.603 -14.808  1.00 43.66           C  
ANISOU 1300  CD2 PHE A 133     6182   5252   5154   -561    311     -7
ATOM   1301  CE1 PHE A 133     -12.720   7.663 -13.138  1.00 43.54           C  
ANISOU 1301  CE1 PHE A 133     5939   5447   5157   -607    340     56
ATOM   1302  CE2 PHE A 133     -12.533   9.117 -15.048  1.00 43.85           C  
ANISOU 1302  CE2 PHE A 133     6108   5396   5156   -644    307     63
ATOM   1303  CZ  PHE A 133     -11.990   8.153 -14.211  1.00 43.27           C  
ANISOU 1303  CZ  PHE A 133     5920   5430   5090   -654    324     93
ATOM   1304  H   PHE A 133     -16.095   9.576 -10.689  1.00 44.38           H  
ATOM   1305  HA  PHE A 133     -15.446  11.638 -12.747  1.00 44.25           H  
ATOM   1306  HB3 PHE A 133     -16.402   9.986 -14.390  1.00 43.22           H  
ATOM   1307  HB2 PHE A 133     -16.597   8.816 -13.123  1.00 43.22           H  
ATOM   1308  HD1 PHE A 133     -14.565   7.737 -12.057  1.00 43.94           H  
ATOM   1309  HD2 PHE A 133     -14.216  10.364 -15.454  1.00 43.66           H  
ATOM   1310  HE1 PHE A 133     -12.274   6.937 -12.478  1.00 43.54           H  
ATOM   1311  HE2 PHE A 133     -11.958   9.504 -15.876  1.00 43.85           H  
ATOM   1312  HZ  PHE A 133     -10.992   7.782 -14.385  1.00 43.27           H  
ATOM   1313  N   ARG A 134     -17.961  12.015 -13.275  1.00 45.99           N  
ANISOU 1313  N   ARG A 134     6841   5279   5352   -153    345   -213
ATOM   1314  CA  ARG A 134     -19.378  12.199 -13.559  1.00 48.14           C  
ANISOU 1314  CA  ARG A 134     7131   5546   5612     33    371   -242
ATOM   1315  C   ARG A 134     -19.645  11.684 -14.972  1.00 48.68           C  
ANISOU 1315  C   ARG A 134     7113   5622   5763     57    369   -211
ATOM   1316  O   ARG A 134     -18.793  11.831 -15.852  1.00 48.34           O  
ANISOU 1316  O   ARG A 134     7107   5519   5740    -36    341   -197
ATOM   1317  CB  ARG A 134     -19.774  13.683 -13.402  1.00 50.31           C  
ANISOU 1317  CB  ARG A 134     7659   5686   5769    123    350   -302
ATOM   1318  CG  ARG A 134     -21.295  13.945 -13.561  1.00 55.39           C  
ANISOU 1318  CG  ARG A 134     8308   6357   6382    351    384   -322
ATOM   1319  CD  ARG A 134     -21.687  15.421 -13.660  1.00 59.29           C  
ANISOU 1319  CD  ARG A 134     9085   6691   6750    474    354   -383
ATOM   1320  NE  ARG A 134     -21.512  16.111 -12.377  1.00 61.74           N  
ANISOU 1320  NE  ARG A 134     9572   6948   6939    501    342   -434
ATOM   1321  CZ  ARG A 134     -22.417  16.537 -11.496  1.00 62.95           C  
ANISOU 1321  CZ  ARG A 134     9717   7191   7008    697    389   -460
ATOM   1322  NH1 ARG A 134     -23.720  16.308 -11.677  1.00 61.08           N  
ANISOU 1322  NH1 ARG A 134     9289   7126   6794    871    450   -427
ATOM   1323  NH2 ARG A 134     -21.996  17.189 -10.415  1.00 62.40           N1+
ANISOU 1323  NH2 ARG A 134     9833   7057   6819    715    370   -511
ATOM   1324  H   ARG A 134     -17.312  12.319 -14.004  1.00 45.99           H  
ATOM   1325  HA  ARG A 134     -19.980  11.595 -12.881  1.00 48.14           H  
ATOM   1326  HB3 ARG A 134     -19.217  14.281 -14.126  1.00 50.31           H  
ATOM   1327  HB2 ARG A 134     -19.453  14.033 -12.420  1.00 50.31           H  
ATOM   1328  HG3 ARG A 134     -21.770  13.529 -12.674  1.00 55.39           H  
ATOM   1329  HG2 ARG A 134     -21.757  13.407 -14.379  1.00 55.39           H  
ATOM   1330  HD3 ARG A 134     -22.658  15.563 -14.132  1.00 59.29           H  
ATOM   1331  HD2 ARG A 134     -20.977  15.921 -14.321  1.00 59.29           H  
ATOM   1332 HH22 ARG A 134     -22.519  17.899  -9.938  1.00 62.40           H  
ATOM   1333 HH21 ARG A 134     -20.971  17.150 -10.231  1.00 62.40           H  
ATOM   1334 HH12 ARG A 134     -24.445  16.724 -11.120  1.00 61.08           H  
ATOM   1335 HH11 ARG A 134     -24.006  15.717 -12.465  1.00 61.08           H  
ATOM   1336  HE  ARG A 134     -20.502  16.347 -12.213  1.00 61.74           H  
ATOM   1337  N   LEU A 135     -20.843  11.123 -15.173  1.00 50.01           N  
ANISOU 1337  N   LEU A 135     7160   5877   5965    170    395   -191
ATOM   1338  CA  LEU A 135     -21.384  10.906 -16.510  1.00 51.32           C  
ANISOU 1338  CA  LEU A 135     7262   6044   6195    194    385   -161
ATOM   1339  C   LEU A 135     -21.594  12.235 -17.246  1.00 51.34           C  
ANISOU 1339  C   LEU A 135     7429   5929   6149    269    374   -196
ATOM   1340  O   LEU A 135     -22.213  13.163 -16.719  1.00 51.31           O  
ANISOU 1340  O   LEU A 135     7550   5889   6057    390    384   -235
ATOM   1341  CB  LEU A 135     -22.734  10.161 -16.456  1.00 52.53           C  
ANISOU 1341  CB  LEU A 135     7259   6331   6370    281    400   -114
ATOM   1342  CG  LEU A 135     -22.665   8.641 -16.236  1.00 55.00           C  
ANISOU 1342  CG  LEU A 135     7413   6736   6748    187    383    -58
ATOM   1343  CD1 LEU A 135     -24.081   8.068 -16.108  1.00 56.50           C  
ANISOU 1343  CD1 LEU A 135     7470   7067   6933    248    379      7
ATOM   1344  CD2 LEU A 135     -21.929   7.892 -17.362  1.00 54.96           C  
ANISOU 1344  CD2 LEU A 135     7405   6664   6811     94    349    -45
ATOM   1345  H   LEU A 135     -21.478  10.997 -14.391  1.00 50.01           H  
ATOM   1346  HA  LEU A 135     -20.650  10.331 -17.070  1.00 51.32           H  
ATOM   1347  HB3 LEU A 135     -23.257  10.320 -17.402  1.00 52.53           H  
ATOM   1348  HB2 LEU A 135     -23.363  10.624 -15.694  1.00 52.53           H  
ATOM   1349  HG  LEU A 135     -22.136   8.465 -15.298  1.00 55.00           H  
ATOM   1350 HD11 LEU A 135     -24.047   7.006 -15.872  1.00 56.50           H  
ATOM   1351 HD12 LEU A 135     -24.666   8.565 -15.339  1.00 56.50           H  
ATOM   1352 HD13 LEU A 135     -24.639   8.178 -17.038  1.00 56.50           H  
ATOM   1353 HD21 LEU A 135     -21.714   6.874 -17.048  1.00 54.96           H  
ATOM   1354 HD22 LEU A 135     -22.545   7.830 -18.258  1.00 54.96           H  
ATOM   1355 HD23 LEU A 135     -20.980   8.338 -17.655  1.00 54.96           H  
ATOM   1356  N   GLU A 136     -21.125  12.274 -18.480  1.00 51.16           N  
ANISOU 1356  N   GLU A 136     7417   5849   6172    213    349   -182
ATOM   1357  CA  GLU A 136     -21.326  13.364 -19.397  1.00 51.54           C  
ANISOU 1357  CA  GLU A 136     7619   5782   6181    265    329   -206
ATOM   1358  C   GLU A 136     -21.866  12.782 -20.703  1.00 52.17           C  
ANISOU 1358  C   GLU A 136     7606   5884   6332    283    324   -171
ATOM   1359  O   GLU A 136     -21.420  11.712 -21.108  1.00 51.44           O  
ANISOU 1359  O   GLU A 136     7399   5839   6308    196    317   -137
ATOM   1360  CB  GLU A 136     -20.000  14.104 -19.543  1.00 54.20           C  
ANISOU 1360  CB  GLU A 136     8111   6008   6474    123    286   -219
ATOM   1361  CG  GLU A 136     -20.032  15.217 -20.595  1.00 62.49           C  
ANISOU 1361  CG  GLU A 136     9311   6936   7495    111    245   -222
ATOM   1362  CD  GLU A 136     -18.774  16.047 -20.497  1.00 70.97           C  
ANISOU 1362  CD  GLU A 136    10541   7923   8500    -64    186   -213
ATOM   1363  OE1 GLU A 136     -17.938  15.989 -21.423  1.00 73.38           O  
ANISOU 1363  OE1 GLU A 136    10820   8238   8825   -188    157   -168
ATOM   1364  OE2 GLU A 136     -18.635  16.837 -19.545  1.00 71.49           O1-
ANISOU 1364  OE2 GLU A 136    10749   7929   8483    -84    163   -242
ATOM   1365  H   GLU A 136     -20.591  11.492 -18.862  1.00 51.16           H  
ATOM   1366  HA  GLU A 136     -22.049  14.058 -18.985  1.00 51.54           H  
ATOM   1367  HB3 GLU A 136     -19.201  13.401 -19.781  1.00 54.20           H  
ATOM   1368  HB2 GLU A 136     -19.742  14.529 -18.571  1.00 54.20           H  
ATOM   1369  HG3 GLU A 136     -20.898  15.863 -20.441  1.00 62.49           H  
ATOM   1370  HG2 GLU A 136     -20.127  14.800 -21.599  1.00 62.49           H  
ATOM   1371  N   LYS A 137     -22.814  13.472 -21.334  1.00 52.40           N  
ANISOU 1371  N   LYS A 137     7689   5887   6333    414    327   -176
ATOM   1372  CA  LYS A 137     -23.377  13.054 -22.610  1.00 53.29           C  
ANISOU 1372  CA  LYS A 137     7720   6025   6502    435    318   -140
ATOM   1373  C   LYS A 137     -22.802  13.939 -23.723  1.00 52.29           C  
ANISOU 1373  C   LYS A 137     7725   5771   6371    387    285   -153
ATOM   1374  O   LYS A 137     -22.894  15.167 -23.618  1.00 52.18           O  
ANISOU 1374  O   LYS A 137     7888   5651   6286    443    270   -186
ATOM   1375  CB  LYS A 137     -24.916  13.123 -22.560  1.00 57.19           C  
ANISOU 1375  CB  LYS A 137     8161   6608   6959    609    341   -117
ATOM   1376  CG  LYS A 137     -25.542  12.278 -23.681  1.00 64.01           C  
ANISOU 1376  CG  LYS A 137     8886   7553   7883    601    327    -55
ATOM   1377  CD  LYS A 137     -27.004  12.571 -24.016  1.00 70.49           C  
ANISOU 1377  CD  LYS A 137     9623   8507   8650    760    347     -6
ATOM   1378  CE  LYS A 137     -28.081  12.259 -22.967  1.00 77.28           C  
ANISOU 1378  CE  LYS A 137    10360   9533   9468    807    375     28
ATOM   1379  NZ  LYS A 137     -29.425  12.486 -23.535  1.00 80.89           N1+
ANISOU 1379  NZ  LYS A 137    10696  10183   9855    961    395    103
ATOM   1380  H   LYS A 137     -23.097  14.371 -20.949  1.00 52.40           H  
ATOM   1381  HA  LYS A 137     -23.096  12.024 -22.823  1.00 53.29           H  
ATOM   1382  HB3 LYS A 137     -25.243  14.162 -22.618  1.00 57.19           H  
ATOM   1383  HB2 LYS A 137     -25.261  12.738 -21.604  1.00 57.19           H  
ATOM   1384  HG3 LYS A 137     -25.420  11.217 -23.464  1.00 64.01           H  
ATOM   1385  HG2 LYS A 137     -24.979  12.430 -24.604  1.00 64.01           H  
ATOM   1386  HD3 LYS A 137     -27.206  11.934 -24.868  1.00 70.49           H  
ATOM   1387  HD2 LYS A 137     -27.099  13.594 -24.382  1.00 70.49           H  
ATOM   1388  HE3 LYS A 137     -27.942  12.866 -22.071  1.00 77.28           H  
ATOM   1389  HE2 LYS A 137     -28.012  11.211 -22.672  1.00 77.28           H  
ATOM   1390  HZ1 LYS A 137     -29.564  13.455 -23.792  1.00 80.89           H  
ATOM   1391  HZ2 LYS A 137     -29.471  12.038 -24.466  1.00 80.89           H  
ATOM   1392  HZ3 LYS A 137     -30.185  12.140 -22.981  1.00 80.89           H  
ATOM   1393  N   ILE A 138     -22.254  13.298 -24.756  1.00 51.01           N  
ANISOU 1393  N   ILE A 138     7493   5618   6270    286    269   -125
ATOM   1394  CA  ILE A 138     -21.686  13.905 -25.953  1.00 50.63           C  
ANISOU 1394  CA  ILE A 138     7534   5486   6218    228    238   -121
ATOM   1395  C   ILE A 138     -22.336  13.274 -27.204  1.00 50.66           C  
ANISOU 1395  C   ILE A 138     7447   5523   6277    259    232    -91
ATOM   1396  O   ILE A 138     -23.086  12.305 -27.085  1.00 50.16           O  
ANISOU 1396  O   ILE A 138     7260   5543   6254    290    240    -67
ATOM   1397  CB  ILE A 138     -20.148  13.677 -25.997  1.00 50.67           C  
ANISOU 1397  CB  ILE A 138     7547   5494   6211     69    220   -107
ATOM   1398  CG1 ILE A 138     -19.718  12.185 -25.982  1.00 51.49           C  
ANISOU 1398  CG1 ILE A 138     7487   5706   6371     33    237    -80
ATOM   1399  CG2 ILE A 138     -19.450  14.473 -24.876  1.00 50.13           C  
ANISOU 1399  CG2 ILE A 138     7588   5384   6075      8    208   -126
ATOM   1400  CD1 ILE A 138     -18.291  11.954 -26.499  1.00 52.72           C  
ANISOU 1400  CD1 ILE A 138     7615   5910   6507    -76    226    -47
ATOM   1401  H   ILE A 138     -22.308  12.279 -24.805  1.00 51.01           H  
ATOM   1402  HA  ILE A 138     -21.904  14.974 -25.978  1.00 50.63           H  
ATOM   1403  HB  ILE A 138     -19.792  14.100 -26.938  1.00 50.67           H  
ATOM   1404 HG13 ILE A 138     -20.380  11.570 -26.591  1.00 51.49           H  
ATOM   1405 HG12 ILE A 138     -19.812  11.786 -24.970  1.00 51.49           H  
ATOM   1406 HG21 ILE A 138     -18.367  14.466 -24.993  1.00 50.13           H  
ATOM   1407 HG22 ILE A 138     -19.769  15.515 -24.875  1.00 50.13           H  
ATOM   1408 HG23 ILE A 138     -19.679  14.060 -23.892  1.00 50.13           H  
ATOM   1409 HD11 ILE A 138     -18.108  10.892 -26.648  1.00 52.72           H  
ATOM   1410 HD12 ILE A 138     -18.127  12.443 -27.461  1.00 52.72           H  
ATOM   1411 HD13 ILE A 138     -17.541  12.322 -25.802  1.00 52.72           H  
ATOM   1412  N   LEU A 139     -22.050  13.842 -28.377  1.00 50.90           N  
ANISOU 1412  N   LEU A 139     7552   5489   6301    234    208    -85
ATOM   1413  CA  LEU A 139     -22.621  13.433 -29.655  1.00 52.21           C  
ANISOU 1413  CA  LEU A 139     7655   5674   6508    257    197    -58
ATOM   1414  C   LEU A 139     -21.463  12.946 -30.541  1.00 51.20           C  
ANISOU 1414  C   LEU A 139     7495   5567   6392    154    185    -41
ATOM   1415  O   LEU A 139     -20.561  13.731 -30.815  1.00 51.73           O  
ANISOU 1415  O   LEU A 139     7632   5606   6417     75    171    -36
ATOM   1416  CB  LEU A 139     -23.348  14.663 -30.249  1.00 54.30           C  
ANISOU 1416  CB  LEU A 139     8039   5853   6741    324    180    -63
ATOM   1417  CG  LEU A 139     -24.380  14.338 -31.342  1.00 58.11           C  
ANISOU 1417  CG  LEU A 139     8464   6366   7250    411    177    -35
ATOM   1418  CD1 LEU A 139     -25.584  13.543 -30.799  1.00 59.12           C  
ANISOU 1418  CD1 LEU A 139     8461   6608   7394    483    196     -9
ATOM   1419  CD2 LEU A 139     -24.850  15.628 -32.030  1.00 59.22           C  
ANISOU 1419  CD2 LEU A 139     8740   6421   7340    506    165    -44
ATOM   1420  H   LEU A 139     -21.346  14.562 -28.447  1.00 50.90           H  
ATOM   1421  HA  LEU A 139     -23.340  12.626 -29.520  1.00 52.21           H  
ATOM   1422  HB3 LEU A 139     -22.606  15.358 -30.644  1.00 54.30           H  
ATOM   1423  HB2 LEU A 139     -23.855  15.211 -29.454  1.00 54.30           H  
ATOM   1424  HG  LEU A 139     -23.885  13.735 -32.101  1.00 58.11           H  
ATOM   1425 HD11 LEU A 139     -26.537  13.944 -31.149  1.00 59.12           H  
ATOM   1426 HD12 LEU A 139     -25.539  12.509 -31.135  1.00 59.12           H  
ATOM   1427 HD13 LEU A 139     -25.624  13.532 -29.708  1.00 59.12           H  
ATOM   1428 HD21 LEU A 139     -25.549  15.411 -32.839  1.00 59.22           H  
ATOM   1429 HD22 LEU A 139     -25.346  16.302 -31.331  1.00 59.22           H  
ATOM   1430 HD23 LEU A 139     -24.009  16.163 -32.473  1.00 59.22           H  
ATOM   1431  N   VAL A 140     -21.474  11.668 -30.931  1.00 50.10           N  
ANISOU 1431  N   VAL A 140     7261   5485   6289    158    181    -24
ATOM   1432  CA  VAL A 140     -20.394  11.018 -31.676  1.00 49.43           C  
ANISOU 1432  CA  VAL A 140     7150   5438   6193    109    175     -9
ATOM   1433  C   VAL A 140     -20.916  10.588 -33.062  1.00 48.65           C  
ANISOU 1433  C   VAL A 140     7050   5328   6109    145    151      4
ATOM   1434  O   VAL A 140     -21.995   9.995 -33.145  1.00 49.78           O  
ANISOU 1434  O   VAL A 140     7171   5460   6284    187    134     10
ATOM   1435  CB  VAL A 140     -19.902   9.758 -30.901  1.00 50.17           C  
ANISOU 1435  CB  VAL A 140     7173   5599   6290    100    184     -9
ATOM   1436  CG1 VAL A 140     -18.904   8.852 -31.656  1.00 50.87           C  
ANISOU 1436  CG1 VAL A 140     7238   5745   6347    105    181      7
ATOM   1437  CG2 VAL A 140     -19.285  10.166 -29.551  1.00 51.39           C  
ANISOU 1437  CG2 VAL A 140     7327   5775   6422     49    206    -16
ATOM   1438  H   VAL A 140     -22.260  11.073 -30.683  1.00 50.10           H  
ATOM   1439  HA  VAL A 140     -19.546  11.696 -31.813  1.00 49.43           H  
ATOM   1440  HB  VAL A 140     -20.779   9.145 -30.688  1.00 50.17           H  
ATOM   1441 HG11 VAL A 140     -18.580   8.021 -31.029  1.00 50.87           H  
ATOM   1442 HG12 VAL A 140     -19.323   8.416 -32.563  1.00 50.87           H  
ATOM   1443 HG13 VAL A 140     -18.005   9.401 -31.933  1.00 50.87           H  
ATOM   1444 HG21 VAL A 140     -18.957   9.298 -28.979  1.00 51.39           H  
ATOM   1445 HG22 VAL A 140     -18.419  10.813 -29.703  1.00 51.39           H  
ATOM   1446 HG23 VAL A 140     -19.996  10.714 -28.931  1.00 51.39           H  
ATOM   1447  N   SER A 141     -20.140  10.863 -34.119  1.00 46.93           N  
ANISOU 1447  N   SER A 141     6848   5128   5856    121    146     19
ATOM   1448  CA  SER A 141     -20.402  10.359 -35.468  1.00 46.21           C  
ANISOU 1448  CA  SER A 141     6762   5028   5767    159    123     28
ATOM   1449  C   SER A 141     -19.844   8.938 -35.603  1.00 45.48           C  
ANISOU 1449  C   SER A 141     6642   4984   5654    195    117     25
ATOM   1450  O   SER A 141     -18.627   8.769 -35.538  1.00 44.99           O  
ANISOU 1450  O   SER A 141     6552   4999   5543    190    139     33
ATOM   1451  CB  SER A 141     -19.786  11.300 -36.515  1.00 48.14           C  
ANISOU 1451  CB  SER A 141     7037   5283   5969    126    121     49
ATOM   1452  OG  SER A 141     -20.585  12.463 -36.602  1.00 53.22           O  
ANISOU 1452  OG  SER A 141     7745   5849   6626    109    110     50
ATOM   1453  H   SER A 141     -19.239  11.291 -33.955  1.00 46.93           H  
ATOM   1454  HA  SER A 141     -21.478  10.327 -35.637  1.00 46.21           H  
ATOM   1455  HB3 SER A 141     -19.773  10.820 -37.494  1.00 48.14           H  
ATOM   1456  HB2 SER A 141     -18.753  11.560 -36.272  1.00 48.14           H  
ATOM   1457  HG  SER A 141     -20.631  12.840 -35.715  1.00 53.22           H  
ATOM   1458  N   VAL A 142     -20.727   7.955 -35.779  1.00 45.45           N  
ANISOU 1458  N   VAL A 142     6655   4941   5674    229     78     21
ATOM   1459  CA  VAL A 142     -20.395   6.529 -35.726  1.00 46.63           C  
ANISOU 1459  CA  VAL A 142     6830   5095   5793    271     49     14
ATOM   1460  C   VAL A 142     -20.259   5.866 -37.115  1.00 47.76           C  
ANISOU 1460  C   VAL A 142     7045   5216   5885    330     13     11
ATOM   1461  O   VAL A 142     -19.852   4.708 -37.194  1.00 48.34           O  
ANISOU 1461  O   VAL A 142     7182   5276   5908    390    -20     -1
ATOM   1462  CB  VAL A 142     -21.475   5.772 -34.910  1.00 48.57           C  
ANISOU 1462  CB  VAL A 142     7073   5303   6078    241      6     24
ATOM   1463  CG1 VAL A 142     -21.389   6.112 -33.410  1.00 48.60           C  
ANISOU 1463  CG1 VAL A 142     7009   5344   6112    208     47     22
ATOM   1464  CG2 VAL A 142     -22.907   6.002 -35.434  1.00 50.58           C  
ANISOU 1464  CG2 VAL A 142     7329   5525   6366    212    -32     53
ATOM   1465  H   VAL A 142     -21.710   8.191 -35.893  1.00 45.45           H  
ATOM   1466  HA  VAL A 142     -19.433   6.397 -35.224  1.00 46.63           H  
ATOM   1467  HB  VAL A 142     -21.264   4.704 -34.989  1.00 48.57           H  
ATOM   1468 HG11 VAL A 142     -22.096   5.518 -32.829  1.00 48.60           H  
ATOM   1469 HG12 VAL A 142     -20.396   5.906 -33.007  1.00 48.60           H  
ATOM   1470 HG13 VAL A 142     -21.609   7.164 -33.216  1.00 48.60           H  
ATOM   1471 HG21 VAL A 142     -23.612   5.422 -34.850  1.00 50.58           H  
ATOM   1472 HG22 VAL A 142     -23.221   7.040 -35.330  1.00 50.58           H  
ATOM   1473 HG23 VAL A 142     -23.028   5.711 -36.478  1.00 50.58           H  
ATOM   1474  N   GLY A 143     -20.574   6.596 -38.184  1.00 47.69           N  
ANISOU 1474  N   GLY A 143     7044   5197   5879    322     13     20
ATOM   1475  CA  GLY A 143     -20.476   6.128 -39.562  1.00 47.76           C  
ANISOU 1475  CA  GLY A 143     7124   5188   5836    376    -20     18
ATOM   1476  C   GLY A 143     -21.333   7.057 -40.423  1.00 47.65           C  
ANISOU 1476  C   GLY A 143     7106   5144   5854    337    -28     35
ATOM   1477  O   GLY A 143     -21.937   7.995 -39.900  1.00 49.23           O  
ANISOU 1477  O   GLY A 143     7259   5342   6105    287     -3     47
ATOM   1478  H   GLY A 143     -20.948   7.529 -38.063  1.00 47.69           H  
ATOM   1479  HA3 GLY A 143     -20.816   5.102 -39.647  1.00 47.76           H  
ATOM   1480  HA2 GLY A 143     -19.443   6.160 -39.901  1.00 47.76           H  
ATOM   1481  N   CYS A 144     -21.389   6.812 -41.736  1.00 46.85           N  
ANISOU 1481  N   CYS A 144     7069   5019   5712    372    -63     36
ATOM   1482  CA  CYS A 144     -22.146   7.637 -42.683  1.00 46.66           C  
ANISOU 1482  CA  CYS A 144     7044   4969   5714    338    -76     57
ATOM   1483  C   CYS A 144     -23.145   6.779 -43.471  1.00 45.42           C  
ANISOU 1483  C   CYS A 144     6965   4742   5551    330   -155     68
ATOM   1484  O   CYS A 144     -22.929   5.579 -43.658  1.00 43.91           O  
ANISOU 1484  O   CYS A 144     6869   4511   5303    366   -206     51
ATOM   1485  CB  CYS A 144     -21.185   8.395 -43.624  1.00 48.34           C  
ANISOU 1485  CB  CYS A 144     7245   5245   5876    359    -41     64
ATOM   1486  SG  CYS A 144     -20.049   9.547 -42.793  1.00 53.43           S  
ANISOU 1486  SG  CYS A 144     7808   5980   6512    312     25     82
ATOM   1487  H   CYS A 144     -20.942   5.991 -42.124  1.00 46.85           H  
ATOM   1488  HA  CYS A 144     -22.735   8.371 -42.138  1.00 46.66           H  
ATOM   1489  HB3 CYS A 144     -21.764   8.954 -44.361  1.00 48.34           H  
ATOM   1490  HB2 CYS A 144     -20.582   7.686 -44.184  1.00 48.34           H  
ATOM   1491  N   THR A 145     -24.228   7.420 -43.912  1.00 45.04           N  
ANISOU 1491  N   THR A 145     6891   4677   5546    283   -173    102
ATOM   1492  CA  THR A 145     -25.265   6.810 -44.731  1.00 45.30           C  
ANISOU 1492  CA  THR A 145     6980   4666   5568    246   -253    134
ATOM   1493  C   THR A 145     -25.646   7.804 -45.850  1.00 47.04           C  
ANISOU 1493  C   THR A 145     7191   4891   5790    247   -246    153
ATOM   1494  O   THR A 145     -25.453   9.013 -45.689  1.00 47.26           O  
ANISOU 1494  O   THR A 145     7167   4949   5840    263   -185    149
ATOM   1495  CB  THR A 145     -26.493   6.413 -43.856  1.00 44.66           C  
ANISOU 1495  CB  THR A 145     6852   4592   5524    175   -297    182
ATOM   1496  OG1 THR A 145     -27.384   5.548 -44.546  1.00 44.01           O  
ANISOU 1496  OG1 THR A 145     6858   4466   5400    114   -402    220
ATOM   1497  CG2 THR A 145     -27.316   7.593 -43.309  1.00 44.51           C  
ANISOU 1497  CG2 THR A 145     6720   4632   5560    169   -256    223
ATOM   1498  H   THR A 145     -24.333   8.426 -43.772  1.00 45.04           H  
ATOM   1499  HA  THR A 145     -24.878   5.915 -45.219  1.00 45.30           H  
ATOM   1500  HB  THR A 145     -26.122   5.845 -43.003  1.00 44.66           H  
ATOM   1501  HG1 THR A 145     -27.207   4.641 -44.229  1.00 44.01           H  
ATOM   1502 HG21 THR A 145     -28.129   7.248 -42.678  1.00 44.51           H  
ATOM   1503 HG22 THR A 145     -26.699   8.256 -42.699  1.00 44.51           H  
ATOM   1504 HG23 THR A 145     -27.759   8.185 -44.105  1.00 44.51           H  
ATOM   1505  N   CYS A 146     -26.143   7.269 -46.967  1.00 46.28           N  
ANISOU 1505  N   CYS A 146     7163   4760   5663    220   -319    178
ATOM   1506  CA  CYS A 146     -26.529   8.028 -48.151  1.00 46.18           C  
ANISOU 1506  CA  CYS A 146     7142   4755   5651    220   -316    199
ATOM   1507  C   CYS A 146     -28.040   8.294 -48.107  1.00 45.50           C  
ANISOU 1507  C   CYS A 146     6990   4692   5607    162   -350    270
ATOM   1508  O   CYS A 146     -28.806   7.327 -48.169  1.00 45.53           O  
ANISOU 1508  O   CYS A 146     7013   4693   5595     94   -428    316
ATOM   1509  CB  CYS A 146     -26.121   7.248 -49.416  1.00 46.23           C  
ANISOU 1509  CB  CYS A 146     7266   4723   5576    245   -365    180
ATOM   1510  SG  CYS A 146     -26.558   8.079 -50.966  1.00 48.92           S  
ANISOU 1510  SG  CYS A 146     7594   5080   5914    238   -364    210
ATOM   1511  H   CYS A 146     -26.307   6.274 -46.996  1.00 46.28           H  
ATOM   1512  HA  CYS A 146     -25.986   8.971 -48.162  1.00 46.18           H  
ATOM   1513  HB3 CYS A 146     -26.568   6.255 -49.415  1.00 46.23           H  
ATOM   1514  HB2 CYS A 146     -25.046   7.083 -49.412  1.00 46.23           H  
ATOM   1515  N   VAL A 147     -28.425   9.572 -47.982  1.00 44.65           N  
ANISOU 1515  N   VAL A 147     6810   4616   5539    187   -301    290
ATOM   1516  CA  VAL A 147     -29.809  10.033 -47.918  1.00 45.49           C  
ANISOU 1516  CA  VAL A 147     6838   4777   5669    173   -321    365
ATOM   1517  C   VAL A 147     -30.151  10.952 -49.103  1.00 48.49           C  
ANISOU 1517  C   VAL A 147     7218   5159   6045    190   -326    397
ATOM   1518  O   VAL A 147     -29.265  11.593 -49.677  1.00 48.69           O  
ANISOU 1518  O   VAL A 147     7293   5144   6064    215   -296    359
ATOM   1519  CB  VAL A 147     -30.084  10.862 -46.623  1.00 44.97           C  
ANISOU 1519  CB  VAL A 147     6688   4759   5639    226   -262    371
ATOM   1520  CG1 VAL A 147     -29.977  10.019 -45.347  1.00 43.82           C  
ANISOU 1520  CG1 VAL A 147     6519   4633   5496    196   -268    361
ATOM   1521  CG2 VAL A 147     -29.239  12.149 -46.491  1.00 45.54           C  
ANISOU 1521  CG2 VAL A 147     6793   4784   5725    288   -193    318
ATOM   1522  H   VAL A 147     -27.723  10.311 -48.043  1.00 44.65           H  
ATOM   1523  HA  VAL A 147     -30.479   9.182 -47.967  1.00 45.49           H  
ATOM   1524  HB  VAL A 147     -31.126  11.187 -46.660  1.00 44.97           H  
ATOM   1525 HG11 VAL A 147     -30.208  10.608 -44.460  1.00 43.82           H  
ATOM   1526 HG12 VAL A 147     -30.670   9.181 -45.358  1.00 43.82           H  
ATOM   1527 HG13 VAL A 147     -28.972   9.621 -45.233  1.00 43.82           H  
ATOM   1528 HG21 VAL A 147     -29.405  12.636 -45.531  1.00 45.54           H  
ATOM   1529 HG22 VAL A 147     -28.176  11.932 -46.561  1.00 45.54           H  
ATOM   1530 HG23 VAL A 147     -29.475  12.880 -47.264  1.00 45.54           H  
ATOM   1531  N   THR A 148     -31.452  11.076 -49.377  1.00 50.21           N  
ANISOU 1531  N   THR A 148     7371   5447   6260    171   -365    481
ATOM   1532  CA  THR A 148     -32.011  12.127 -50.217  1.00 52.62           C  
ANISOU 1532  CA  THR A 148     7660   5772   6562    203   -366    524
ATOM   1533  C   THR A 148     -31.968  13.468 -49.424  1.00 53.39           C  
ANISOU 1533  C   THR A 148     7724   5877   6683    316   -294    514
ATOM   1534  O   THR A 148     -32.253  13.462 -48.216  1.00 53.68           O  
ANISOU 1534  O   THR A 148     7701   5970   6726    361   -266    526
ATOM   1535  CB  THR A 148     -33.490  11.757 -50.513  1.00 55.37           C  
ANISOU 1535  CB  THR A 148     7936   6221   6883    145   -437    633
ATOM   1536  OG1 THR A 148     -34.250  11.616 -49.318  1.00 58.09           O  
ANISOU 1536  OG1 THR A 148     8169   6677   7226    159   -428    689
ATOM   1537  CG2 THR A 148     -33.640  10.449 -51.311  1.00 55.22           C  
ANISOU 1537  CG2 THR A 148     8000   6160   6821     19   -532    643
ATOM   1538  H   THR A 148     -32.151  10.506 -48.911  1.00 50.21           H  
ATOM   1539  HA  THR A 148     -31.433  12.164 -51.140  1.00 52.62           H  
ATOM   1540  HB  THR A 148     -33.935  12.559 -51.107  1.00 55.37           H  
ATOM   1541  HG1 THR A 148     -34.442  12.497 -48.988  1.00 58.09           H  
ATOM   1542 HG21 THR A 148     -34.686  10.234 -51.532  1.00 55.22           H  
ATOM   1543 HG22 THR A 148     -33.124  10.512 -52.269  1.00 55.22           H  
ATOM   1544 HG23 THR A 148     -33.238   9.594 -50.768  1.00 55.22           H  
ATOM   1545  N   PRO A 149     -31.587  14.594 -50.068  1.00 53.36           N  
ANISOU 1545  N   PRO A 149     7783   5810   6682    359   -269    490
ATOM   1546  CA  PRO A 149     -31.612  15.916 -49.409  1.00 54.02           C  
ANISOU 1546  CA  PRO A 149     7895   5862   6769    463   -220    473
ATOM   1547  C   PRO A 149     -33.026  16.360 -48.976  1.00 55.27           C  
ANISOU 1547  C   PRO A 149     7986   6108   6906    580   -212    541
ATOM   1548  O   PRO A 149     -34.020  15.837 -49.479  1.00 55.91           O  
ANISOU 1548  O   PRO A 149     7994   6279   6970    576   -246    619
ATOM   1549  CB  PRO A 149     -31.011  16.863 -50.465  1.00 54.23           C  
ANISOU 1549  CB  PRO A 149     8022   5797   6787    450   -223    450
ATOM   1550  CG  PRO A 149     -31.284  16.188 -51.799  1.00 54.69           C  
ANISOU 1550  CG  PRO A 149     8070   5875   6837    373   -264    471
ATOM   1551  CD  PRO A 149     -31.151  14.707 -51.461  1.00 52.71           C  
ANISOU 1551  CD  PRO A 149     7765   5676   6585    312   -293    477
ATOM   1552  HA  PRO A 149     -30.969  15.893 -48.529  1.00 54.02           H  
ATOM   1553  HB3 PRO A 149     -29.935  16.935 -50.312  1.00 54.23           H  
ATOM   1554  HB2 PRO A 149     -31.399  17.879 -50.420  1.00 54.23           H  
ATOM   1555  HG3 PRO A 149     -30.615  16.510 -52.602  1.00 54.69           H  
ATOM   1556  HG2 PRO A 149     -32.307  16.400 -52.117  1.00 54.69           H  
ATOM   1557  HD2 PRO A 149     -31.723  14.103 -52.163  1.00 52.71           H  
ATOM   1558  HD3 PRO A 149     -30.108  14.397 -51.522  1.00 52.71           H  
ATOM   1559  N   ILE A 150     -33.092  17.315 -48.040  1.00 55.56           N  
ANISOU 1559  N   ILE A 150     8051   6128   6929    695   -168    516
ATOM   1560  CA  ILE A 150     -34.330  18.018 -47.712  1.00 56.29           C  
ANISOU 1560  CA  ILE A 150     8099   6313   6975    863   -150    577
ATOM   1561  C   ILE A 150     -34.365  19.263 -48.606  1.00 56.24           C  
ANISOU 1561  C   ILE A 150     8211   6211   6946    935   -163    579
ATOM   1562  O   ILE A 150     -33.456  20.087 -48.513  1.00 56.12           O  
ANISOU 1562  O   ILE A 150     8350   6041   6932    921   -163    513
ATOM   1563  CB  ILE A 150     -34.374  18.467 -46.220  1.00 57.11           C  
ANISOU 1563  CB  ILE A 150     8224   6427   7049    995   -101    545
ATOM   1564  CG1 ILE A 150     -34.402  17.254 -45.267  1.00 58.86           C  
ANISOU 1564  CG1 ILE A 150     8321   6758   7287    927    -90    554
ATOM   1565  CG2 ILE A 150     -35.515  19.454 -45.875  1.00 57.25           C  
ANISOU 1565  CG2 ILE A 150     8230   6532   6989   1220    -80    603
ATOM   1566  CD1 ILE A 150     -35.641  16.350 -45.390  1.00 60.86           C  
ANISOU 1566  CD1 ILE A 150     8389   7215   7519    891   -122    671
ATOM   1567  H   ILE A 150     -32.248  17.792 -47.765  1.00 55.56           H  
ATOM   1568  HA  ILE A 150     -35.204  17.398 -47.927  1.00 56.29           H  
ATOM   1569  HB  ILE A 150     -33.444  18.998 -46.011  1.00 57.11           H  
ATOM   1570 HG13 ILE A 150     -34.302  17.596 -44.235  1.00 58.86           H  
ATOM   1571 HG12 ILE A 150     -33.515  16.653 -45.448  1.00 58.86           H  
ATOM   1572 HG21 ILE A 150     -35.566  19.641 -44.800  1.00 57.25           H  
ATOM   1573 HG22 ILE A 150     -35.370  20.426 -46.346  1.00 57.25           H  
ATOM   1574 HG23 ILE A 150     -36.489  19.085 -46.198  1.00 57.25           H  
ATOM   1575 HD11 ILE A 150     -35.844  15.839 -44.448  1.00 60.86           H  
ATOM   1576 HD12 ILE A 150     -36.541  16.907 -45.646  1.00 60.86           H  
ATOM   1577 HD13 ILE A 150     -35.504  15.593 -46.163  1.00 60.86           H  
ATOM   1578  N   VAL A 151     -35.379  19.351 -49.465  1.00 56.36           N  
ANISOU 1578  N   VAL A 151     8154   6328   6932   1001   -182    665
ATOM   1579  CA  VAL A 151     -35.511  20.411 -50.452  1.00 57.01           C  
ANISOU 1579  CA  VAL A 151     8335   6337   6990   1069   -202    683
ATOM   1580  C   VAL A 151     -36.678  21.321 -50.037  1.00 57.87           C  
ANISOU 1580  C   VAL A 151     8450   6519   7020   1316   -181    737
ATOM   1581  O   VAL A 151     -37.733  20.829 -49.637  1.00 57.77           O  
ANISOU 1581  O   VAL A 151     8269   6712   6967   1403   -163    821
ATOM   1582  CB  VAL A 151     -35.802  19.813 -51.859  1.00 57.38           C  
ANISOU 1582  CB  VAL A 151     8302   6442   7058    942   -248    742
ATOM   1583  CG1 VAL A 151     -35.964  20.880 -52.964  1.00 57.87           C  
ANISOU 1583  CG1 VAL A 151     8458   6432   7096   1003   -272    766
ATOM   1584  CG2 VAL A 151     -34.706  18.809 -52.276  1.00 57.69           C  
ANISOU 1584  CG2 VAL A 151     8358   6414   7149    742   -269    685
ATOM   1585  H   VAL A 151     -36.109  18.656 -49.475  1.00 56.36           H  
ATOM   1586  HA  VAL A 151     -34.596  21.004 -50.509  1.00 57.01           H  
ATOM   1587  HB  VAL A 151     -36.744  19.261 -51.809  1.00 57.38           H  
ATOM   1588 HG11 VAL A 151     -36.119  20.415 -53.939  1.00 57.87           H  
ATOM   1589 HG12 VAL A 151     -36.823  21.531 -52.793  1.00 57.87           H  
ATOM   1590 HG13 VAL A 151     -35.080  21.514 -53.041  1.00 57.87           H  
ATOM   1591 HG21 VAL A 151     -34.897  18.405 -53.271  1.00 57.69           H  
ATOM   1592 HG22 VAL A 151     -33.724  19.283 -52.296  1.00 57.69           H  
ATOM   1593 HG23 VAL A 151     -34.648  17.958 -51.596  1.00 57.69           H  
ATOM   1594  N   HIS A 152     -36.459  22.629 -50.147  1.00 58.75           N  
ANISOU 1594  N   HIS A 152     8759   6472   7091   1431   -189    700
ATOM   1595  CA  HIS A 152     -37.443  23.687 -49.980  1.00 60.10           C  
ANISOU 1595  CA  HIS A 152     8986   6684   7165   1706   -175    743
ATOM   1596  C   HIS A 152     -36.938  24.888 -50.792  1.00 62.01           C  
ANISOU 1596  C   HIS A 152     9486   6703   7371   1765   -218    705
ATOM   1597  O   HIS A 152     -35.752  24.943 -51.129  1.00 62.51           O  
ANISOU 1597  O   HIS A 152     9729   6567   7455   1648   -246    626
ATOM   1598  CB  HIS A 152     -37.679  24.024 -48.486  1.00 61.11           C  
ANISOU 1598  CB  HIS A 152     9127   6863   7229   1893   -125    717
ATOM   1599  CG  HIS A 152     -36.452  24.270 -47.638  1.00 64.49           C  
ANISOU 1599  CG  HIS A 152     9726   7096   7682   1809   -126    604
ATOM   1600  ND1 HIS A 152     -35.618  23.247 -47.217  1.00 67.16           N  
ANISOU 1600  ND1 HIS A 152    10343   7228   7948   1939   -147    539
ATOM   1601  CD2 HIS A 152     -35.931  25.421 -47.086  1.00 65.57           C  
ANISOU 1601  CD2 HIS A 152     9801   7218   7895   1606   -118    556
ATOM   1602  CE1 HIS A 152     -34.662  23.795 -46.464  1.00 67.58           C  
ANISOU 1602  CE1 HIS A 152    10476   7164   8037   1795   -150    461
ATOM   1603  NE2 HIS A 152     -34.792  25.108 -46.336  1.00 67.17           N  
ANISOU 1603  NE2 HIS A 152    10216   7229   8076   1603   -127    468
ATOM   1604  H   HIS A 152     -35.576  22.993 -50.490  1.00 58.75           H  
ATOM   1605  HA  HIS A 152     -38.387  23.363 -50.424  1.00 60.10           H  
ATOM   1606  HB3 HIS A 152     -38.235  23.211 -48.019  1.00 61.11           H  
ATOM   1607  HB2 HIS A 152     -38.326  24.900 -48.400  1.00 61.11           H  
ATOM   1608  HD1 HIS A 152     -35.719  22.268 -47.445  1.00 67.16           H  
ATOM   1609  HD2 HIS A 152     -36.291  26.437 -47.156  1.00 65.57           H  
ATOM   1610  HE1 HIS A 152     -33.876  23.226 -45.992  1.00 67.58           H  
ATOM   1611  N   HIS A 153     -37.852  25.812 -51.100  1.00 62.79           N  
ANISOU 1611  N   HIS A 153     9615   6842   7401   1950   -230    770
ATOM   1612  CA  HIS A 153     -37.513  27.114 -51.664  1.00 64.04           C  
ANISOU 1612  CA  HIS A 153    10038   6782   7511   2015   -286    747
ATOM   1613  C   HIS A 153     -37.122  28.053 -50.511  1.00 65.52           C  
ANISOU 1613  C   HIS A 153    10513   6772   7608   2184   -298    668
ATOM   1614  O   HIS A 153     -37.550  27.825 -49.378  1.00 65.22           O  
ANISOU 1614  O   HIS A 153    10441   6829   7510   2377   -247    658
ATOM   1615  CB  HIS A 153     -38.739  27.633 -52.448  1.00 63.86           C  
ANISOU 1615  CB  HIS A 153     9955   6881   7428   2195   -292    847
ATOM   1616  CG  HIS A 153     -38.465  28.770 -53.407  1.00 64.67           C  
ANISOU 1616  CG  HIS A 153    10296   6776   7500   2204   -362    841
ATOM   1617  ND1 HIS A 153     -38.408  30.102 -53.022  1.00 66.64           N  
ANISOU 1617  ND1 HIS A 153    10848   6835   7639   2427   -397    805
ATOM   1618  CD2 HIS A 153     -38.250  28.774 -54.768  1.00 65.49           C  
ANISOU 1618  CD2 HIS A 153    10382   6842   7658   2025   -409    875
ATOM   1619  CE1 HIS A 153     -38.139  30.820 -54.114  1.00 67.51           C  
ANISOU 1619  CE1 HIS A 153    11117   6792   7743   2361   -470    822
ATOM   1620  NE2 HIS A 153     -38.019  30.077 -55.210  1.00 67.01           N  
ANISOU 1620  NE2 HIS A 153    10857   6823   7780   2117   -475    864
ATOM   1621  H   HIS A 153     -38.760  25.761 -50.665  1.00 62.79           H  
ATOM   1622  HA  HIS A 153     -36.667  27.002 -52.345  1.00 64.04           H  
ATOM   1623  HB3 HIS A 153     -39.529  27.946 -51.761  1.00 63.86           H  
ATOM   1624  HB2 HIS A 153     -39.160  26.821 -53.043  1.00 63.86           H  
ATOM   1625  HD1 HIS A 153     -38.516  30.489 -52.076  1.00 66.64           H  
ATOM   1626  HD2 HIS A 153     -38.235  27.941 -55.455  1.00 65.49           H  
ATOM   1627  HE1 HIS A 153     -38.021  31.893 -54.104  1.00 67.51           H  
ATOM   1628  N   VAL A 154     -36.335  29.090 -50.818  1.00 66.46           N  
ANISOU 1628  N   VAL A 154    10929   6619   7703   2106   -377    620
ATOM   1629  CA  VAL A 154     -36.015  30.151 -49.865  1.00 67.93           C  
ANISOU 1629  CA  VAL A 154    11446   6580   7785   2242   -418    550
ATOM   1630  C   VAL A 154     -37.278  31.004 -49.581  1.00 69.55           C  
ANISOU 1630  C   VAL A 154    11771   6810   7845   2648   -404    574
ATOM   1631  O   VAL A 154     -38.141  31.109 -50.460  1.00 69.23           O  
ANISOU 1631  O   VAL A 154    11702   6834   7769   2782   -413    644
ATOM   1632  CB  VAL A 154     -34.845  31.032 -50.402  1.00 68.81           C  
ANISOU 1632  CB  VAL A 154    11865   6396   7883   2027   -530    512
ATOM   1633  CG1 VAL A 154     -35.231  32.063 -51.486  1.00 68.59           C  
ANISOU 1633  CG1 VAL A 154    12081   6212   7767   2150   -612    549
ATOM   1634  CG2 VAL A 154     -34.074  31.728 -49.267  1.00 69.72           C  
ANISOU 1634  CG2 VAL A 154    12240   6320   7932   2015   -567    431
ATOM   1635  H   VAL A 154     -36.104  29.277 -51.779  1.00 66.46           H  
ATOM   1636  HA  VAL A 154     -35.704  29.675 -48.934  1.00 67.93           H  
ATOM   1637  HB  VAL A 154     -34.132  30.350 -50.872  1.00 68.81           H  
ATOM   1638 HG11 VAL A 154     -34.343  32.523 -51.917  1.00 68.59           H  
ATOM   1639 HG12 VAL A 154     -35.788  31.609 -52.304  1.00 68.59           H  
ATOM   1640 HG13 VAL A 154     -35.841  32.874 -51.081  1.00 68.59           H  
ATOM   1641 HG21 VAL A 154     -33.219  32.280 -49.655  1.00 69.72           H  
ATOM   1642 HG22 VAL A 154     -34.701  32.437 -48.724  1.00 69.72           H  
ATOM   1643 HG23 VAL A 154     -33.689  31.006 -48.548  1.00 69.72           H  
ATOM   1644  N   ALA A 155     -37.355  31.564 -48.374  1.00 70.34           N  
ANISOU 1644  N   ALA A 155    12003   6874   7850   2856   -379    518
ATOM   1645  CA  ALA A 155     -38.429  32.464 -47.907  1.00 71.74           C  
ANISOU 1645  CA  ALA A 155    12316   7082   7859   3285   -359    532
ATOM   1646  C   ALA A 155     -37.928  33.957 -47.700  1.00 73.34           C  
ANISOU 1646  C   ALA A 155    13023   6920   7924   3412   -469    464
ATOM   1647  O   ALA A 155     -38.827  34.817 -47.786  1.00 74.20           O  
ANISOU 1647  O   ALA A 155    13307   7001   7885   3763   -483    487
ATOM   1648  CB  ALA A 155     -39.006  31.873 -46.603  1.00 72.07           C  
ANISOU 1648  CB  ALA A 155    12206   7325   7854   3470   -265    517
ATOM   1649  OXT ALA A 155     -36.712  34.103 -47.419  1.00 74.95           O1-
ANISOU 1649  OXT ALA A 155    13459   6867   8149   3166   -549    395
ATOM   1650  H   ALA A 155     -36.537  31.586 -47.782  1.00 70.34           H  
ATOM   1651  HA  ALA A 155     -39.240  32.512 -48.636  1.00 71.74           H  
ATOM   1652  HB1 ALA A 155     -39.826  32.482 -46.228  1.00 72.07           H  
ATOM   1653  HB2 ALA A 155     -39.395  30.871 -46.765  1.00 72.07           H  
ATOM   1654  HB3 ALA A 155     -38.255  31.819 -45.816  1.00 72.07           H  
ATOM   1655  N   ASP A 103     -21.589   3.505 -61.410  1.00 78.06           N  
ANISOU 1655  N   ASP A 103    12409   8856   8395   1228   -546    -80
ATOM   1656  CA  ASP A 103     -20.440   3.783 -62.286  1.00 78.68           C  
ANISOU 1656  CA  ASP A 103    12430   9142   8324   1418   -462    -82
ATOM   1657  C   ASP A 103     -19.177   4.183 -61.493  1.00 78.82           C  
ANISOU 1657  C   ASP A 103    12242   9385   8321   1519   -338    -58
ATOM   1658  O   ASP A 103     -18.129   4.445 -62.083  1.00 79.92           O  
ANISOU 1658  O   ASP A 103    12281   9753   8334   1652   -262    -30
ATOM   1659  CB  ASP A 103     -20.720   4.856 -63.374  1.00  0.00           C  
ATOM   1660  CG  ASP A 103     -21.847   4.578 -64.373  1.00  0.00           C  
ATOM   1661  OD1 ASP A 103     -22.357   3.438 -64.429  1.00  0.00           O  
ATOM   1662  OD2 ASP A 103     -22.137   5.519 -65.141  1.00  0.00           O1-
ATOM   1663  H   ASP A 103     -22.294   4.224 -61.378  1.00 78.06           H  
ATOM   1664  HA  ASP A 103     -20.189   2.856 -62.806  1.00 78.68           H  
ATOM   1665  HB2 ASP A 103     -20.945   5.808 -62.895  1.00  0.00           H  
ATOM   1666  HB3 ASP A 103     -19.823   5.013 -63.976  1.00  0.00           H  
ATOM   1667  N   ASN A  57     -17.841 -11.317 -30.242  1.00 74.25           N  
ANISOU 1667  N   ASN A  57    12469   7372   8372    869  -1109    -10
ATOM   1668  CA  ASN A  57     -17.361 -12.303 -31.221  1.00 75.85           C  
ANISOU 1668  CA  ASN A  57    13024   7402   8392   1110  -1199    -67
ATOM   1669  C   ASN A  57     -18.587 -13.097 -31.638  1.00 77.54           C  
ANISOU 1669  C   ASN A  57    13574   7352   8536    937  -1429    -36
ATOM   1670  O   ASN A  57     -18.540 -14.279 -31.978  1.00 78.47           O  
ANISOU 1670  O   ASN A  57    14082   7243   8490   1050  -1588    -57
ATOM   1671  CB  ASN A  57     -16.233 -13.200 -30.627  1.00  0.00           C  
ATOM   1672  CG  ASN A  57     -14.987 -12.483 -30.095  1.00  0.00           C  
ATOM   1673  OD1 ASN A  57     -14.307 -13.003 -29.218  1.00  0.00           O  
ATOM   1674  ND2 ASN A  57     -14.638 -11.307 -30.605  1.00  0.00           N  
ATOM   1675  H   ASN A  57     -18.322 -11.671 -29.431  1.00 74.25           H  
ATOM   1676  HA  ASN A  57     -16.977 -11.822 -32.125  1.00 75.85           H  
ATOM   1677  HXT ASN A  57     -19.530 -12.548 -31.630  1.00 77.54           H  
ATOM   1678  HB2 ASN A  57     -16.633 -13.818 -29.820  1.00  0.00           H  
ATOM   1679  HB3 ASN A  57     -15.886 -13.895 -31.393  1.00  0.00           H  
ATOM   1680 HD22 ASN A  57     -13.802 -10.864 -30.263  1.00  0.00           H  
ATOM   1681 HD21 ASN A  57     -15.238 -10.794 -31.245  1.00  0.00           H  
ATOM   1682  N   SER A  64     -15.029  -3.982 -39.919  1.00 77.94           N  
ANISOU 1682  N   SER A  64    12088   8794   8731   1629   -317   -198
ATOM   1683  CA  SER A  64     -15.680  -4.224 -41.236  1.00 78.22           C  
ANISOU 1683  CA  SER A  64    12317   8713   8691   1684   -390   -229
ATOM   1684  C   SER A  64     -15.298  -3.127 -42.282  1.00 78.36           C  
ANISOU 1684  C   SER A  64    12165   8928   8679   1752   -282   -214
ATOM   1685  O   SER A  64     -15.450  -1.926 -42.046  1.00 79.03           O  
ANISOU 1685  O   SER A  64    11977   9201   8848   1662   -173   -170
ATOM   1686  CB  SER A  64     -17.223  -4.313 -41.086  1.00  0.00           C  
ATOM   1687  OG  SER A  64     -17.751  -3.102 -40.572  1.00  0.00           O  
ATOM   1688  H1  SER A  64     -15.063  -4.805 -39.327  1.00 77.94           H  
ATOM   1689  H2  SER A  64     -14.042  -3.786 -40.031  1.00 77.94           H  
ATOM   1690  HA  SER A  64     -15.328  -5.180 -41.633  1.00 78.22           H  
ATOM   1691  HB2 SER A  64     -17.692  -4.511 -42.050  1.00  0.00           H  
ATOM   1692  HB3 SER A  64     -17.492  -5.141 -40.426  1.00  0.00           H  
ATOM   1693  HG  SER A  64     -17.094  -2.799 -39.929  1.00  0.00           H  
ATOM   1694  N   ASP A  65     -14.923  -3.572 -43.492  1.00 77.03           N  
ANISOU 1694  N   ASP A  65    12170   8716   8382   1901   -321   -247
ATOM   1695  CA  ASP A  65     -14.646  -2.771 -44.697  1.00 76.48           C  
ANISOU 1695  CA  ASP A  65    11940   8839   8281   1949   -228   -224
ATOM   1696  C   ASP A  65     -15.834  -1.915 -45.200  1.00 75.44           C  
ANISOU 1696  C   ASP A  65    11733   8631   8298   1698   -251   -205
ATOM   1697  O   ASP A  65     -15.746  -1.339 -46.287  1.00 75.31           O  
ANISOU 1697  O   ASP A  65    11657   8709   8249   1724   -212   -193
ATOM   1698  CB  ASP A  65     -14.109  -3.602 -45.898  1.00  0.00           C  
ATOM   1699  CG  ASP A  65     -12.983  -4.605 -45.649  1.00  0.00           C  
ATOM   1700  OD1 ASP A  65     -12.398  -4.592 -44.553  1.00  0.00           O  
ATOM   1701  OD2 ASP A  65     -12.732  -5.361 -46.613  1.00  0.00           O1-
ATOM   1702  H   ASP A  65     -14.514  -4.499 -43.536  1.00 77.03           H  
ATOM   1703  HA  ASP A  65     -13.849  -2.080 -44.419  1.00 76.48           H  
ATOM   1704  HB2 ASP A  65     -14.917  -4.179 -46.335  1.00  0.00           H  
ATOM   1705  HB3 ASP A  65     -13.735  -2.929 -46.671  1.00  0.00           H  
ATOM   1706  N   TYR A  85     -12.867   9.182 -19.858  1.00 47.33           N  
ANISOU 1706  N   TYR A  85     6554   5765   5666   -467    293     85
ATOM   1707  CA  TYR A  85     -12.827   7.747 -20.108  1.00 47.60           C  
ANISOU 1707  CA  TYR A  85     6477   5871   5736   -368    314     97
ATOM   1708  C   TYR A  85     -14.106   7.388 -20.906  1.00 46.55           C  
ANISOU 1708  C   TYR A  85     6377   5639   5671   -259    309     53
ATOM   1709  O   TYR A  85     -15.201   7.669 -20.402  1.00 46.39           O  
ANISOU 1709  O   TYR A  85     6402   5533   5689   -234    307     12
ATOM   1710  CB  TYR A  85     -12.737   7.004 -18.763  1.00  0.00           C  
ATOM   1711  CG  TYR A  85     -12.670   5.495 -18.893  1.00  0.00           C  
ATOM   1712  CD1 TYR A  85     -11.421   4.844 -18.956  1.00  0.00           C  
ATOM   1713  CD2 TYR A  85     -13.855   4.734 -18.966  1.00  0.00           C  
ATOM   1714  CE1 TYR A  85     -11.361   3.443 -19.078  1.00  0.00           C  
ATOM   1715  CE2 TYR A  85     -13.793   3.337 -19.105  1.00  0.00           C  
ATOM   1716  CZ  TYR A  85     -12.545   2.684 -19.138  1.00  0.00           C  
ATOM   1717  OH  TYR A  85     -12.461   1.325 -19.216  1.00  0.00           O  
ATOM   1718  H   TYR A  85     -13.763   9.543 -19.535  1.00 47.33           H  
ATOM   1719  HA  TYR A  85     -11.917   7.488 -20.640  1.00 47.60           H  
ATOM   1720  HB2 TYR A  85     -11.847   7.341 -18.232  1.00  0.00           H  
ATOM   1721  HB3 TYR A  85     -13.571   7.256 -18.117  1.00  0.00           H  
ATOM   1722  HD1 TYR A  85     -10.502   5.410 -18.893  1.00  0.00           H  
ATOM   1723  HD2 TYR A  85     -14.818   5.223 -18.936  1.00  0.00           H  
ATOM   1724  HE1 TYR A  85     -10.402   2.948 -19.099  1.00  0.00           H  
ATOM   1725  HE2 TYR A  85     -14.714   2.784 -19.192  1.00  0.00           H  
ATOM   1726  HH  TYR A  85     -13.261   0.859 -18.957  1.00  0.00           H  
TER    1727      TYR A  85
ATOM   1728  N   PHE B  41      -4.466   3.778 -12.826  1.00 75.53           N  
ANISOU 1728  N   PHE B  41     8617  12003   8077     78    130   -550
ATOM   1729  CA  PHE B  41      -5.557   2.916 -13.297  1.00 73.92           C  
ANISOU 1729  CA  PHE B  41     8596  11433   8057    268     87   -497
ATOM   1730  C   PHE B  41      -6.136   2.068 -12.144  1.00 70.78           C  
ANISOU 1730  C   PHE B  41     8323  10795   7774    465     22   -440
ATOM   1731  O   PHE B  41      -5.796   0.888 -12.035  1.00 71.98           O  
ANISOU 1731  O   PHE B  41     8474  10976   7898    751    -61   -477
ATOM   1732  CB  PHE B  41      -5.068   2.051 -14.481  1.00 74.64           C  
ANISOU 1732  CB  PHE B  41     8608  11662   8088    470     49   -575
ATOM   1733  CG  PHE B  41      -4.637   2.868 -15.686  1.00 75.85           C  
ANISOU 1733  CG  PHE B  41     8671  12007   8141    241    118   -616
ATOM   1734  CD1 PHE B  41      -5.597   3.577 -16.437  1.00 76.90           C  
ANISOU 1734  CD1 PHE B  41     8975  11861   8382     39    163   -547
ATOM   1735  CD2 PHE B  41      -3.272   3.044 -15.988  1.00 77.09           C  
ANISOU 1735  CD2 PHE B  41     8573  12647   8071    210    136   -725
ATOM   1736  CE1 PHE B  41      -5.199   4.405 -17.474  1.00 77.87           C  
ANISOU 1736  CE1 PHE B  41     9053  12139   8393   -195    219   -578
ATOM   1737  CE2 PHE B  41      -2.891   3.864 -17.038  1.00 78.19           C  
ANISOU 1737  CE2 PHE B  41     8641  12974   8093    -52    202   -757
ATOM   1738  CZ  PHE B  41      -3.851   4.543 -17.777  1.00 77.83           C  
ANISOU 1738  CZ  PHE B  41     8806  12603   8163   -259    241   -679
ATOM   1739  H   PHE B  41      -3.629   3.304 -12.534  1.00 75.53           H  
ATOM   1740  HA  PHE B  41      -6.374   3.509 -13.703  1.00 73.92           H  
ATOM   1741  HB3 PHE B  41      -5.876   1.388 -14.801  1.00 74.64           H  
ATOM   1742  HB2 PHE B  41      -4.250   1.395 -14.176  1.00 74.64           H  
ATOM   1743  HD1 PHE B  41      -6.646   3.487 -16.201  1.00 76.90           H  
ATOM   1744  HD2 PHE B  41      -2.517   2.535 -15.408  1.00 77.09           H  
ATOM   1745  HE1 PHE B  41      -5.941   4.949 -18.044  1.00 77.87           H  
ATOM   1746  HE2 PHE B  41      -1.843   3.981 -17.279  1.00 78.19           H  
ATOM   1747  HZ  PHE B  41      -3.546   5.190 -18.586  1.00 77.83           H  
ATOM   1748  N   PRO B  42      -6.961   2.679 -11.262  1.00 66.10           N  
ANISOU 1748  N   PRO B  42     7864   9958   7293    318     53   -351
ATOM   1749  CA  PRO B  42      -7.617   1.936 -10.171  1.00 62.75           C  
ANISOU 1749  CA  PRO B  42     7562   9317   6964    463     -3   -291
ATOM   1750  C   PRO B  42      -8.650   0.925 -10.701  1.00 58.91           C  
ANISOU 1750  C   PRO B  42     7241   8548   6594    608    -58   -247
ATOM   1751  O   PRO B  42      -9.360   1.223 -11.658  1.00 58.98           O  
ANISOU 1751  O   PRO B  42     7294   8457   6659    553    -34   -239
ATOM   1752  CB  PRO B  42      -8.282   3.048  -9.334  1.00 63.58           C  
ANISOU 1752  CB  PRO B  42     7747   9273   7137    246     57   -219
ATOM   1753  CG  PRO B  42      -8.553   4.161 -10.333  1.00 64.63           C  
ANISOU 1753  CG  PRO B  42     7899   9398   7260     29    125   -221
ATOM   1754  CD  PRO B  42      -7.363   4.089 -11.267  1.00 64.51           C  
ANISOU 1754  CD  PRO B  42     7732   9665   7113     24    130   -307
ATOM   1755  HA  PRO B  42      -6.863   1.419  -9.576  1.00 62.75           H  
ATOM   1756  HB3 PRO B  42      -7.587   3.399  -8.570  1.00 63.58           H  
ATOM   1757  HB2 PRO B  42      -9.194   2.731  -8.827  1.00 63.58           H  
ATOM   1758  HG3 PRO B  42      -8.697   5.149  -9.898  1.00 64.63           H  
ATOM   1759  HG2 PRO B  42      -9.434   3.913 -10.919  1.00 64.63           H  
ATOM   1760  HD2 PRO B  42      -7.640   4.475 -12.248  1.00 64.51           H  
ATOM   1761  HD3 PRO B  42      -6.547   4.695 -10.878  1.00 64.51           H  
ATOM   1762  N   ARG B  43      -8.760  -0.238 -10.039  1.00 55.40           N  
ANISOU 1762  N   ARG B  43     6907   7972   6170    774   -136   -217
ATOM   1763  CA  ARG B  43      -9.755  -1.267 -10.369  1.00 53.76           C  
ANISOU 1763  CA  ARG B  43     6893   7491   6042    870   -200   -166
ATOM   1764  C   ARG B  43     -11.207  -0.759 -10.262  1.00 51.79           C  
ANISOU 1764  C   ARG B  43     6737   7014   5927    671   -145    -72
ATOM   1765  O   ARG B  43     -12.054  -1.182 -11.047  1.00 51.74           O  
ANISOU 1765  O   ARG B  43     6795   6875   5987    630   -136    -50
ATOM   1766  CB  ARG B  43      -9.529  -2.504  -9.456  1.00 55.67           C  
ANISOU 1766  CB  ARG B  43     7271   7659   6224   1080   -313   -159
ATOM   1767  CG  ARG B  43     -10.603  -3.621  -9.523  1.00 58.90           C  
ANISOU 1767  CG  ARG B  43     7938   7754   6686   1115   -390    -87
ATOM   1768  CD  ARG B  43     -10.284  -4.793  -8.571  1.00 62.41           C  
ANISOU 1768  CD  ARG B  43     8554   8134   7026   1317   -515    -89
ATOM   1769  NE  ARG B  43     -11.393  -5.768  -8.420  1.00 65.05           N  
ANISOU 1769  NE  ARG B  43     9185   8157   7372   1297   -601     -7
ATOM   1770  CZ  ARG B  43     -12.502  -5.643  -7.662  1.00 67.67           C  
ANISOU 1770  CZ  ARG B  43     9625   8336   7752   1113   -590     90
ATOM   1771  NH1 ARG B  43     -12.767  -4.522  -6.987  1.00 66.97           N  
ANISOU 1771  NH1 ARG B  43     9369   8354   7721    958   -493    115
ATOM   1772  NH2 ARG B  43     -13.366  -6.659  -7.581  1.00 67.02           N1+
ANISOU 1772  NH2 ARG B  43     9824   8001   7639   1066   -678    161
ATOM   1773  H   ARG B  43      -8.112  -0.431  -9.292  1.00 55.40           H  
ATOM   1774  HA  ARG B  43      -9.596  -1.564 -11.409  1.00 53.76           H  
ATOM   1775  HB3 ARG B  43      -9.474  -2.159  -8.422  1.00 55.67           H  
ATOM   1776  HB2 ARG B  43      -8.549  -2.927  -9.678  1.00 55.67           H  
ATOM   1777  HG3 ARG B  43     -10.585  -3.984 -10.552  1.00 58.90           H  
ATOM   1778  HG2 ARG B  43     -11.618  -3.256  -9.358  1.00 58.90           H  
ATOM   1779  HD3 ARG B  43      -9.875  -4.462  -7.616  1.00 62.41           H  
ATOM   1780  HD2 ARG B  43      -9.484  -5.370  -9.038  1.00 62.41           H  
ATOM   1781 HH22 ARG B  43     -14.227  -6.588  -7.050  1.00 67.02           H  
ATOM   1782 HH21 ARG B  43     -13.211  -7.558  -8.015  1.00 67.02           H  
ATOM   1783 HH12 ARG B  43     -13.559  -4.400  -6.369  1.00 66.97           H  
ATOM   1784 HH11 ARG B  43     -12.253  -3.663  -7.164  1.00 66.97           H  
ATOM   1785  HE  ARG B  43     -11.192  -6.650  -8.872  1.00 65.05           H  
ATOM   1786  N   THR B  44     -11.482   0.069  -9.253  1.00 49.57           N  
ANISOU 1786  N   THR B  44     6452   6712   5671    558   -107    -26
ATOM   1787  CA  THR B  44     -12.828   0.491  -8.893  1.00 48.55           C  
ANISOU 1787  CA  THR B  44     6390   6419   5639    406    -59     48
ATOM   1788  C   THR B  44     -12.827   2.011  -8.698  1.00 47.60           C  
ANISOU 1788  C   THR B  44     6192   6376   5518    251     29     35
ATOM   1789  O   THR B  44     -11.954   2.522  -7.994  1.00 47.56           O  
ANISOU 1789  O   THR B  44     6106   6525   5440    210     52      2
ATOM   1790  CB  THR B  44     -13.294  -0.202  -7.578  1.00 51.32           C  
ANISOU 1790  CB  THR B  44     6831   6671   5998    404    -94    112
ATOM   1791  OG1 THR B  44     -13.221  -1.613  -7.749  1.00 53.07           O  
ANISOU 1791  OG1 THR B  44     7194   6777   6192    525   -192    130
ATOM   1792  CG2 THR B  44     -14.739   0.122  -7.147  1.00 52.65           C  
ANISOU 1792  CG2 THR B  44     7032   6736   6238    263    -43    173
ATOM   1793  H   THR B  44     -10.738   0.511  -8.734  1.00 49.57           H  
ATOM   1794  HA  THR B  44     -13.526   0.251  -9.694  1.00 48.55           H  
ATOM   1795  HB  THR B  44     -12.616   0.073  -6.766  1.00 51.32           H  
ATOM   1796  HG1 THR B  44     -13.839  -1.813  -8.461  1.00 53.07           H  
ATOM   1797 HG21 THR B  44     -15.008  -0.394  -6.225  1.00 52.65           H  
ATOM   1798 HG22 THR B  44     -14.886   1.185  -6.958  1.00 52.65           H  
ATOM   1799 HG23 THR B  44     -15.461  -0.173  -7.907  1.00 52.65           H  
ATOM   1800  N   VAL B  45     -13.772   2.693  -9.346  1.00 45.60           N  
ANISOU 1800  N   VAL B  45     5983   6014   5327    163     70     58
ATOM   1801  CA  VAL B  45     -13.896   4.145  -9.330  1.00 43.80           C  
ANISOU 1801  CA  VAL B  45     5757   5807   5078     33    134     46
ATOM   1802  C   VAL B  45     -15.338   4.520  -8.974  1.00 43.24           C  
ANISOU 1802  C   VAL B  45     5761   5602   5067      7    153     95
ATOM   1803  O   VAL B  45     -16.238   3.692  -9.133  1.00 42.59           O  
ANISOU 1803  O   VAL B  45     5702   5439   5042     54    125    134
ATOM   1804  CB  VAL B  45     -13.530   4.744 -10.719  1.00 42.50           C  
ANISOU 1804  CB  VAL B  45     5587   5682   4880    -26    156      1
ATOM   1805  CG1 VAL B  45     -12.087   4.368 -11.075  1.00 42.11           C  
ANISOU 1805  CG1 VAL B  45     5423   5834   4743      9    140    -60
ATOM   1806  CG2 VAL B  45     -14.487   4.408 -11.884  1.00 41.22           C  
ANISOU 1806  CG2 VAL B  45     5486   5379   4798     16    142     21
ATOM   1807  H   VAL B  45     -14.475   2.215  -9.904  1.00 45.60           H  
ATOM   1808  HA  VAL B  45     -13.245   4.583  -8.568  1.00 43.80           H  
ATOM   1809  HB  VAL B  45     -13.550   5.829 -10.618  1.00 42.50           H  
ATOM   1810 HG11 VAL B  45     -11.716   4.903 -11.948  1.00 42.11           H  
ATOM   1811 HG12 VAL B  45     -11.427   4.589 -10.237  1.00 42.11           H  
ATOM   1812 HG13 VAL B  45     -11.997   3.301 -11.276  1.00 42.11           H  
ATOM   1813 HG21 VAL B  45     -14.132   4.854 -12.814  1.00 41.22           H  
ATOM   1814 HG22 VAL B  45     -14.573   3.334 -12.044  1.00 41.22           H  
ATOM   1815 HG23 VAL B  45     -15.493   4.797 -11.723  1.00 41.22           H  
ATOM   1816  N   MET B  46     -15.521   5.755  -8.492  1.00 42.41           N  
ANISOU 1816  N   MET B  46     5704   5487   4924    -70    194     86
ATOM   1817  CA  MET B  46     -16.831   6.338  -8.234  1.00 42.27           C  
ANISOU 1817  CA  MET B  46     5748   5382   4929    -55    209    110
ATOM   1818  C   MET B  46     -17.312   7.085  -9.481  1.00 42.44           C  
ANISOU 1818  C   MET B  46     5850   5327   4947    -54    216     88
ATOM   1819  O   MET B  46     -16.532   7.833 -10.074  1.00 42.04           O  
ANISOU 1819  O   MET B  46     5859   5275   4838   -125    224     54
ATOM   1820  CB  MET B  46     -16.749   7.303  -7.039  1.00 41.23           C  
ANISOU 1820  CB  MET B  46     5660   5270   4735    -93    235    106
ATOM   1821  CG  MET B  46     -16.507   6.584  -5.706  1.00 40.79           C  
ANISOU 1821  CG  MET B  46     5539   5270   4691    -76    228    138
ATOM   1822  SD  MET B  46     -16.381   7.686  -4.272  1.00 44.93           S  
ANISOU 1822  SD  MET B  46     6112   5825   5133   -125    256    129
ATOM   1823  CE  MET B  46     -14.729   8.383  -4.543  1.00 35.46           C  
ANISOU 1823  CE  MET B  46     4931   4702   3840   -250    262     83
ATOM   1824  H   MET B  46     -14.728   6.396  -8.462  1.00 42.41           H  
ATOM   1825  HA  MET B  46     -17.541   5.548  -7.988  1.00 42.27           H  
ATOM   1826  HB3 MET B  46     -17.682   7.862  -6.962  1.00 41.23           H  
ATOM   1827  HB2 MET B  46     -15.971   8.045  -7.214  1.00 41.23           H  
ATOM   1828  HG3 MET B  46     -15.602   5.980  -5.756  1.00 40.79           H  
ATOM   1829  HG2 MET B  46     -17.328   5.891  -5.517  1.00 40.79           H  
ATOM   1830  HE1 MET B  46     -14.448   9.022  -3.706  1.00 35.46           H  
ATOM   1831  HE2 MET B  46     -13.985   7.591  -4.635  1.00 35.46           H  
ATOM   1832  HE3 MET B  46     -14.708   8.982  -5.451  1.00 35.46           H  
ATOM   1833  N   VAL B  47     -18.585   6.911  -9.832  1.00 42.51           N  
ANISOU 1833  N   VAL B  47     5864   5291   4998     15    208    105
ATOM   1834  CA  VAL B  47     -19.231   7.648 -10.907  1.00 43.34           C  
ANISOU 1834  CA  VAL B  47     6046   5328   5093     49    202     82
ATOM   1835  C   VAL B  47     -20.488   8.329 -10.341  1.00 44.99           C  
ANISOU 1835  C   VAL B  47     6289   5537   5267    141    203     75
ATOM   1836  O   VAL B  47     -21.300   7.671  -9.689  1.00 45.46           O  
ANISOU 1836  O   VAL B  47     6248   5674   5352    178    203    101
ATOM   1837  CB  VAL B  47     -19.634   6.723 -12.086  1.00 43.17           C  
ANISOU 1837  CB  VAL B  47     5979   5286   5140     67    179     93
ATOM   1838  CG1 VAL B  47     -20.381   7.463 -13.217  1.00 43.06           C  
ANISOU 1838  CG1 VAL B  47     6055   5203   5103    111    170     66
ATOM   1839  CG2 VAL B  47     -18.404   5.993 -12.661  1.00 43.49           C  
ANISOU 1839  CG2 VAL B  47     5985   5350   5190     19    172     83
ATOM   1840  H   VAL B  47     -19.175   6.254  -9.323  1.00 42.51           H  
ATOM   1841  HA  VAL B  47     -18.563   8.414 -11.301  1.00 43.34           H  
ATOM   1842  HB  VAL B  47     -20.312   5.959 -11.703  1.00 43.17           H  
ATOM   1843 HG11 VAL B  47     -20.613   6.784 -14.037  1.00 43.06           H  
ATOM   1844 HG12 VAL B  47     -21.329   7.882 -12.886  1.00 43.06           H  
ATOM   1845 HG13 VAL B  47     -19.790   8.287 -13.619  1.00 43.06           H  
ATOM   1846 HG21 VAL B  47     -18.658   5.429 -13.557  1.00 43.49           H  
ATOM   1847 HG22 VAL B  47     -17.611   6.691 -12.926  1.00 43.49           H  
ATOM   1848 HG23 VAL B  47     -17.984   5.287 -11.943  1.00 43.49           H  
ATOM   1849  N   ASN B  48     -20.612   9.633 -10.600  1.00 45.61           N  
ANISOU 1849  N   ASN B  48     6524   5542   5263    179    197     35
ATOM   1850  CA  ASN B  48     -21.803  10.436 -10.343  1.00 47.38           C  
ANISOU 1850  CA  ASN B  48     6807   5776   5420    325    183      6
ATOM   1851  C   ASN B  48     -22.761  10.274 -11.544  1.00 48.25           C  
ANISOU 1851  C   ASN B  48     6900   5883   5550    413    157     -7
ATOM   1852  O   ASN B  48     -22.403  10.669 -12.659  1.00 48.41           O  
ANISOU 1852  O   ASN B  48     7039   5796   5558    389    137    -23
ATOM   1853  CB  ASN B  48     -21.355  11.899 -10.129  1.00 49.14           C  
ANISOU 1853  CB  ASN B  48     7272   5882   5515    336    168    -36
ATOM   1854  CG  ASN B  48     -22.420  12.864  -9.599  1.00 53.30           C  
ANISOU 1854  CG  ASN B  48     7905   6409   5938    537    138    -84
ATOM   1855  OD1 ASN B  48     -23.623  12.614  -9.637  1.00 54.15           O  
ANISOU 1855  OD1 ASN B  48     7933   6593   6048    685    121   -102
ATOM   1856  ND2 ASN B  48     -21.982  14.020  -9.111  1.00 54.94           N  
ANISOU 1856  ND2 ASN B  48     8301   6544   6030    555    127   -112
ATOM   1857  H   ASN B  48     -19.841  10.104 -11.075  1.00 45.61           H  
ATOM   1858  HA  ASN B  48     -22.303  10.093  -9.439  1.00 47.38           H  
ATOM   1859  HB3 ASN B  48     -20.951  12.310 -11.048  1.00 49.14           H  
ATOM   1860  HB2 ASN B  48     -20.527  11.907  -9.418  1.00 49.14           H  
ATOM   1861 HD22 ASN B  48     -22.641  14.723  -8.838  1.00 54.94           H  
ATOM   1862 HD21 ASN B  48     -20.999  14.278  -9.179  1.00 54.94           H  
ATOM   1863  N   LEU B  49     -23.930   9.665 -11.312  1.00 49.17           N  
ANISOU 1863  N   LEU B  49     6855   6137   5688    488    156      3
ATOM   1864  CA  LEU B  49     -24.901   9.313 -12.354  1.00 50.18           C  
ANISOU 1864  CA  LEU B  49     6931   6307   5827    558    130     -7
ATOM   1865  C   LEU B  49     -25.800  10.478 -12.801  1.00 52.23           C  
ANISOU 1865  C   LEU B  49     7309   6562   5974    760     92    -75
ATOM   1866  O   LEU B  49     -26.553  10.306 -13.756  1.00 52.29           O  
ANISOU 1866  O   LEU B  49     7255   6637   5974    841     66    -91
ATOM   1867  CB  LEU B  49     -25.782   8.123 -11.899  1.00 49.81           C  
ANISOU 1867  CB  LEU B  49     6667   6444   5816    516    139     31
ATOM   1868  CG  LEU B  49     -25.056   6.773 -11.707  1.00 50.14           C  
ANISOU 1868  CG  LEU B  49     6638   6464   5950    340    150     98
ATOM   1869  CD1 LEU B  49     -26.071   5.668 -11.367  1.00 50.33           C  
ANISOU 1869  CD1 LEU B  49     6509   6648   5966    267    143    137
ATOM   1870  CD2 LEU B  49     -24.241   6.357 -12.942  1.00 49.65           C  
ANISOU 1870  CD2 LEU B  49     6651   6254   5959    279    135    108
ATOM   1871  H   LEU B  49     -24.153   9.360 -10.364  1.00 49.17           H  
ATOM   1872  HA  LEU B  49     -24.340   9.029 -13.242  1.00 50.18           H  
ATOM   1873  HB3 LEU B  49     -26.567   7.968 -12.642  1.00 49.81           H  
ATOM   1874  HB2 LEU B  49     -26.299   8.388 -10.976  1.00 49.81           H  
ATOM   1875  HG  LEU B  49     -24.369   6.873 -10.864  1.00 50.14           H  
ATOM   1876 HD11 LEU B  49     -25.594   4.689 -11.329  1.00 50.33           H  
ATOM   1877 HD12 LEU B  49     -26.542   5.844 -10.397  1.00 50.33           H  
ATOM   1878 HD13 LEU B  49     -26.864   5.603 -12.113  1.00 50.33           H  
ATOM   1879 HD21 LEU B  49     -23.906   5.321 -12.882  1.00 49.65           H  
ATOM   1880 HD22 LEU B  49     -24.842   6.452 -13.845  1.00 49.65           H  
ATOM   1881 HD23 LEU B  49     -23.350   6.970 -13.057  1.00 49.65           H  
ATOM   1882  N   ASN B  50     -25.732  11.636 -12.132  1.00 53.38           N  
ANISOU 1882  N   ASN B  50     7638   6630   6014    854     78   -118
ATOM   1883  CA  ASN B  50     -26.479  12.840 -12.522  1.00 55.23           C  
ANISOU 1883  CA  ASN B  50     8050   6826   6108   1088     20   -192
ATOM   1884  C   ASN B  50     -25.782  13.499 -13.724  1.00 56.71           C  
ANISOU 1884  C   ASN B  50     8487   6781   6278   1032    -17   -197
ATOM   1885  O   ASN B  50     -24.986  14.425 -13.527  1.00 56.73           O  
ANISOU 1885  O   ASN B  50     8728   6608   6217    942    -26   -200
ATOM   1886  CB  ASN B  50     -26.586  13.815 -11.321  1.00 56.47           C  
ANISOU 1886  CB  ASN B  50     8350   6971   6133   1221      5   -238
ATOM   1887  CG  ASN B  50     -27.638  13.439 -10.272  1.00 62.07           C  
ANISOU 1887  CG  ASN B  50     8811   7955   6817   1329     33   -253
ATOM   1888  OD1 ASN B  50     -28.523  12.631 -10.502  1.00 64.75           O  
ANISOU 1888  OD1 ASN B  50     8911   8516   7176   1374     39   -254
ATOM   1889  ND2 ASN B  50     -27.587  14.061  -9.099  1.00 62.01           N  
ANISOU 1889  ND2 ASN B  50     8853   7958   6750   1348     50   -264
ATOM   1890  H   ASN B  50     -25.070  11.711 -11.374  1.00 53.38           H  
ATOM   1891  HA  ASN B  50     -27.482  12.508 -12.805  1.00 55.23           H  
ATOM   1892  HB3 ASN B  50     -26.894  14.791 -11.700  1.00 56.47           H  
ATOM   1893  HB2 ASN B  50     -25.612  13.956 -10.851  1.00 56.47           H  
ATOM   1894 HD22 ASN B  50     -28.337  13.865  -8.451  1.00 62.01           H  
ATOM   1895 HD21 ASN B  50     -26.905  14.770  -8.912  1.00 62.01           H  
ATOM   1896  N   ILE B  51     -26.088  12.977 -14.921  1.00 57.52           N  
ANISOU 1896  N   ILE B  51     8527   6899   6428   1048    -35   -194
ATOM   1897  CA  ILE B  51     -25.508  13.330 -16.218  1.00 59.56           C  
ANISOU 1897  CA  ILE B  51     8975   6971   6684    971    -64   -193
ATOM   1898  C   ILE B  51     -25.466  14.858 -16.486  1.00 61.98           C  
ANISOU 1898  C   ILE B  51     9654   7078   6817   1086   -135   -247
ATOM   1899  O   ILE B  51     -26.418  15.574 -16.169  1.00 62.86           O  
ANISOU 1899  O   ILE B  51     9860   7218   6804   1350   -193   -308
ATOM   1900  CB  ILE B  51     -26.272  12.651 -17.415  1.00 59.40           C  
ANISOU 1900  CB  ILE B  51     8802   7031   6737   1006    -77   -185
ATOM   1901  CG1 ILE B  51     -26.454  11.117 -17.255  1.00 60.26           C  
ANISOU 1901  CG1 ILE B  51     8598   7309   6989    877    -24   -128
ATOM   1902  CG2 ILE B  51     -25.619  12.925 -18.791  1.00 59.68           C  
ANISOU 1902  CG2 ILE B  51     9021   6883   6772    910   -101   -180
ATOM   1903  CD1 ILE B  51     -27.547  10.509 -18.156  1.00 61.24           C  
ANISOU 1903  CD1 ILE B  51     8573   7552   7144    929    -45   -128
ATOM   1904  H   ILE B  51     -26.678  12.151 -14.919  1.00 57.52           H  
ATOM   1905  HA  ILE B  51     -24.498  12.934 -16.184  1.00 59.56           H  
ATOM   1906  HB  ILE B  51     -27.278  13.083 -17.440  1.00 59.40           H  
ATOM   1907 HG13 ILE B  51     -26.722  10.866 -16.234  1.00 60.26           H  
ATOM   1908 HG12 ILE B  51     -25.509  10.610 -17.437  1.00 60.26           H  
ATOM   1909 HG21 ILE B  51     -26.112  12.385 -19.591  1.00 59.68           H  
ATOM   1910 HG22 ILE B  51     -25.670  13.972 -19.071  1.00 59.68           H  
ATOM   1911 HG23 ILE B  51     -24.570  12.622 -18.796  1.00 59.68           H  
ATOM   1912 HD11 ILE B  51     -27.523   9.420 -18.116  1.00 61.24           H  
ATOM   1913 HD12 ILE B  51     -28.539  10.821 -17.834  1.00 61.24           H  
ATOM   1914 HD13 ILE B  51     -27.446  10.778 -19.202  1.00 61.24           H  
ATOM   1915  N   HIS B  52     -24.383  15.339 -17.106  1.00 62.42           N  
ANISOU 1915  N   HIS B  52     9936   6943   6839    890   -140   -229
ATOM   1916  CA  HIS B  52     -24.326  16.661 -17.737  1.00 63.43           C  
ANISOU 1916  CA  HIS B  52    10483   6840   6778    944   -222   -270
ATOM   1917  C   HIS B  52     -24.322  16.482 -19.257  1.00 64.51           C  
ANISOU 1917  C   HIS B  52    10690   6890   6929    885   -247   -263
ATOM   1918  O   HIS B  52     -23.710  15.545 -19.758  1.00 62.78           O  
ANISOU 1918  O   HIS B  52    10360   6689   6806    642   -194   -219
ATOM   1919  CB  HIS B  52     -23.080  17.426 -17.250  1.00 64.27           C  
ANISOU 1919  CB  HIS B  52    10835   6801   6783    710   -214   -254
ATOM   1920  CG  HIS B  52     -23.231  18.062 -15.887  1.00 67.67           C  
ANISOU 1920  CG  HIS B  52    11395   7212   7106    830   -235   -285
ATOM   1921  ND1 HIS B  52     -24.327  17.863 -15.060  1.00 69.86           N  
ANISOU 1921  ND1 HIS B  52    11999   7317   7226    660   -259   -285
ATOM   1922  CD2 HIS B  52     -22.420  18.952 -15.212  1.00 68.96           C  
ANISOU 1922  CD2 HIS B  52    11395   7524   7283   1083   -233   -317
ATOM   1923  CE1 HIS B  52     -24.162  18.647 -13.990  1.00 70.13           C  
ANISOU 1923  CE1 HIS B  52    12072   7377   7197    835   -275   -316
ATOM   1924  NE2 HIS B  52     -23.023  19.325 -14.009  1.00 70.24           N  
ANISOU 1924  NE2 HIS B  52    11786   7593   7309   1098   -257   -339
ATOM   1925  H   HIS B  52     -23.622  14.708 -17.337  1.00 62.42           H  
ATOM   1926  HA  HIS B  52     -25.212  17.260 -17.506  1.00 63.43           H  
ATOM   1927  HB3 HIS B  52     -22.843  18.235 -17.943  1.00 64.27           H  
ATOM   1928  HB2 HIS B  52     -22.203  16.779 -17.241  1.00 64.27           H  
ATOM   1929  HD1 HIS B  52     -25.113  17.246 -15.242  1.00 69.86           H  
ATOM   1930  HD2 HIS B  52     -21.466  19.363 -15.506  1.00 68.96           H  
ATOM   1931  HE1 HIS B  52     -24.871  18.711 -13.181  1.00 70.13           H  
ATOM   1932  N   ASN B  53     -25.047  17.335 -19.979  1.00 66.59           N  
ANISOU 1932  N   ASN B  53    11133   7082   7088   1128   -333   -314
ATOM   1933  CA  ASN B  53     -25.116  17.281 -21.443  1.00 68.85           C  
ANISOU 1933  CA  ASN B  53    11531   7264   7365   1083   -368   -310
ATOM   1934  C   ASN B  53     -24.100  18.278 -21.995  1.00 70.84           C  
ANISOU 1934  C   ASN B  53    12179   7266   7471    836   -397   -297
ATOM   1935  O   ASN B  53     -24.003  19.388 -21.471  1.00 70.60           O  
ANISOU 1935  O   ASN B  53    12460   7090   7277    826   -441   -316
ATOM   1936  CB  ASN B  53     -26.541  17.642 -21.936  1.00 70.41           C  
ANISOU 1936  CB  ASN B  53    11829   7459   7463   1430   -464   -375
ATOM   1937  CG  ASN B  53     -27.647  16.618 -21.632  1.00 74.54           C  
ANISOU 1937  CG  ASN B  53    11926   8273   8125   1580   -429   -378
ATOM   1938  OD1 ASN B  53     -28.692  16.614 -22.272  1.00 76.28           O  
ANISOU 1938  OD1 ASN B  53    11801   8680   8503   1449   -341   -334
ATOM   1939  ND2 ASN B  53     -27.461  15.737 -20.657  1.00 74.82           N  
ANISOU 1939  ND2 ASN B  53    11989   8356   8082   1843   -505   -432
ATOM   1940  H   ASN B  53     -25.445  18.160 -19.553  1.00 66.59           H  
ATOM   1941  HA  ASN B  53     -24.875  16.280 -21.804  1.00 68.85           H  
ATOM   1942  HB3 ASN B  53     -26.522  17.748 -23.024  1.00 70.41           H  
ATOM   1943  HB2 ASN B  53     -26.841  18.617 -21.550  1.00 70.41           H  
ATOM   1944 HD22 ASN B  53     -28.232  15.149 -20.387  1.00 74.82           H  
ATOM   1945 HD21 ASN B  53     -26.611  15.755 -20.108  1.00 74.82           H  
ATOM   1946  N   ARG B  54     -23.378  17.877 -23.045  1.00 72.25           N  
ANISOU 1946  N   ARG B  54    12337   7417   7698    609   -370   -263
ATOM   1947  CA  ARG B  54     -22.345  18.675 -23.705  1.00 74.05           C  
ANISOU 1947  CA  ARG B  54    12915   7457   7763    325   -393   -250
ATOM   1948  C   ARG B  54     -22.543  18.368 -25.179  1.00 74.44           C  
ANISOU 1948  C   ARG B  54    13125   7395   7765    299   -441   -252
ATOM   1949  O   ARG B  54     -21.671  17.877 -25.897  1.00 74.53           O  
ANISOU 1949  O   ARG B  54    12854   7540   7924    191   -377   -226
ATOM   1950  CB  ARG B  54     -20.945  18.305 -23.143  1.00 76.11           C  
ANISOU 1950  CB  ARG B  54    12971   7856   8092    -21   -291   -206
ATOM   1951  CG  ARG B  54     -19.826  19.236 -23.666  1.00 80.15           C  
ANISOU 1951  CG  ARG B  54    13838   8224   8390   -355   -315   -196
ATOM   1952  CD  ARG B  54     -18.413  18.922 -23.154  1.00 83.53           C  
ANISOU 1952  CD  ARG B  54    14134   8801   8801   -667   -237   -171
ATOM   1953  NE  ARG B  54     -18.333  19.008 -21.695  1.00 85.58           N  
ANISOU 1953  NE  ARG B  54    14379   9078   9061   -580   -231   -176
ATOM   1954  CZ  ARG B  54     -18.261  20.042 -20.855  1.00 88.17           C  
ANISOU 1954  CZ  ARG B  54    15099   9226   9177   -650   -293   -187
ATOM   1955  NH1 ARG B  54     -18.150  21.290 -21.312  1.00 87.12           N  
ANISOU 1955  NH1 ARG B  54    15444   8857   8801   -804   -377   -193
ATOM   1956  NH2 ARG B  54     -18.302  19.784 -19.552  1.00 89.18           N1+
ANISOU 1956  NH2 ARG B  54    15173   9393   9319   -569   -279   -192
ATOM   1957  H   ARG B  54     -23.413  16.901 -23.344  1.00 72.25           H  
ATOM   1958  HA  ARG B  54     -22.536  19.742 -23.565  1.00 74.05           H  
ATOM   1959  HXT ARG B  54     -23.533  18.618 -25.565  1.00 74.44           H  
ATOM   1960  HB3 ARG B  54     -20.708  17.261 -23.355  1.00 76.11           H  
ATOM   1961  HB2 ARG B  54     -20.985  18.379 -22.055  1.00 76.11           H  
ATOM   1962  HG3 ARG B  54     -20.084  20.262 -23.401  1.00 80.15           H  
ATOM   1963  HG2 ARG B  54     -19.793  19.226 -24.757  1.00 80.15           H  
ATOM   1964  HD3 ARG B  54     -17.666  19.566 -23.618  1.00 83.53           H  
ATOM   1965  HD2 ARG B  54     -18.139  17.904 -23.434  1.00 83.53           H  
ATOM   1966 HH22 ARG B  54     -18.165  20.452 -18.813  1.00 89.18           H  
ATOM   1967 HH21 ARG B  54     -18.431  18.793 -19.283  1.00 89.18           H  
ATOM   1968 HH12 ARG B  54     -18.133  22.110 -20.721  1.00 87.12           H  
ATOM   1969 HH11 ARG B  54     -18.078  21.430 -22.310  1.00 87.12           H  
ATOM   1970  HE  ARG B  54     -18.326  18.054 -21.293  1.00 85.58           H  
ATOM   1971  N   SER B  64     -33.884  14.474 -38.140  1.00 77.76           N  
ANISOU 1971  N   SER B  64    12394   8692   8458   2336  -1049   -514
ATOM   1972  CA  SER B  64     -33.229  13.201 -37.701  1.00 77.64           C  
ANISOU 1972  CA  SER B  64    12087   8750   8661   1994   -919   -435
ATOM   1973  C   SER B  64     -33.696  11.977 -38.549  1.00 76.42           C  
ANISOU 1973  C   SER B  64    11617   8828   8590   1961   -914   -424
ATOM   1974  O   SER B  64     -33.176  10.870 -38.389  1.00 77.64           O  
ANISOU 1974  O   SER B  64    11447   9185   8866   1812   -841   -387
ATOM   1975  CB  SER B  64     -33.361  12.942 -36.179  1.00 79.62           C  
ANISOU 1975  CB  SER B  64    12136   9137   8981   1936   -841   -418
ATOM   1976  OG  SER B  64     -32.618  13.927 -35.472  1.00 83.08           O  
ANISOU 1976  OG  SER B  64    12864   9395   9308   2016   -864   -442
ATOM   1977  H1  SER B  64     -34.290  14.913 -37.320  1.00 77.76           H  
ATOM   1978  H2  SER B  64     -33.176  15.138 -38.424  1.00 77.76           H  
ATOM   1979  HA  SER B  64     -32.161  13.263 -37.916  1.00 77.64           H  
ATOM   1980  HB3 SER B  64     -32.974  11.956 -35.911  1.00 79.62           H  
ATOM   1981  HB2 SER B  64     -34.405  12.969 -35.865  1.00 79.62           H  
ATOM   1982  HG  SER B  64     -32.737  13.800 -34.526  1.00 83.08           H  
ATOM   1983  N   TYR B  66     -33.047  10.412 -41.080  1.00 66.05           N  
ANISOU 1983  N   TYR B  66    10279   7325   7490   1506   -856   -329
ATOM   1984  CA  TYR B  66     -32.052   9.592 -41.783  1.00 64.55           C  
ANISOU 1984  CA  TYR B  66    10093   7013   7420   1237   -791   -278
ATOM   1985  C   TYR B  66     -32.473   8.118 -41.898  1.00 63.19           C  
ANISOU 1985  C   TYR B  66     9626   7025   7358   1126   -764   -247
ATOM   1986  O   TYR B  66     -32.216   7.503 -42.927  1.00 61.95           O  
ANISOU 1986  O   TYR B  66     9487   6825   7226   1053   -781   -237
ATOM   1987  CB  TYR B  66     -30.675   9.693 -41.089  1.00 63.83           C  
ANISOU 1987  CB  TYR B  66    10068   6791   7393   1038   -701   -244
ATOM   1988  CG  TYR B  66     -29.976  11.049 -41.059  1.00 63.97           C  
ANISOU 1988  CG  TYR B  66    10426   6590   7287   1038   -721   -261
ATOM   1989  CD1 TYR B  66     -30.343  12.109 -41.920  1.00 64.49           C  
ANISOU 1989  CD1 TYR B  66    10788   6519   7198   1189   -820   -298
ATOM   1990  CD2 TYR B  66     -28.886  11.224 -40.178  1.00 64.46           C  
ANISOU 1990  CD2 TYR B  66    10541   6583   7367    871   -648   -240
ATOM   1991  CE1 TYR B  66     -29.610  13.311 -41.913  1.00 65.19           C  
ANISOU 1991  CE1 TYR B  66    11248   6380   7140   1156   -852   -308
ATOM   1992  CE2 TYR B  66     -28.159  12.429 -40.170  1.00 65.25           C  
ANISOU 1992  CE2 TYR B  66    10973   6492   7326    818   -670   -251
ATOM   1993  CZ  TYR B  66     -28.516  13.469 -41.047  1.00 65.93           C  
ANISOU 1993  CZ  TYR B  66    11386   6417   7247    950   -774   -282
ATOM   1994  OH  TYR B  66     -27.797  14.621 -41.087  1.00 66.33           O  
ANISOU 1994  OH  TYR B  66    11824   6253   7127    869   -809   -287
ATOM   1995  H   TYR B  66     -32.781  10.803 -40.179  1.00 66.05           H  
ATOM   1996  HA  TYR B  66     -31.969   9.957 -42.807  1.00 64.55           H  
ATOM   1997  HB3 TYR B  66     -29.982   9.014 -41.588  1.00 63.83           H  
ATOM   1998  HB2 TYR B  66     -30.759   9.329 -40.064  1.00 63.83           H  
ATOM   1999  HD1 TYR B  66     -31.163  12.005 -42.614  1.00 64.49           H  
ATOM   2000  HD2 TYR B  66     -28.585  10.431 -39.509  1.00 64.46           H  
ATOM   2001  HE1 TYR B  66     -29.859  14.108 -42.597  1.00 65.19           H  
ATOM   2002  HE2 TYR B  66     -27.322  12.539 -39.494  1.00 65.25           H  
ATOM   2003  HH  TYR B  66     -27.018  14.585 -40.524  1.00 66.33           H  
ATOM   2004  N   TYR B  67     -33.185   7.609 -40.886  1.00 63.13           N  
ANISOU 2004  N   TYR B  67     9369   7228   7390   1115   -735   -234
ATOM   2005  CA  TYR B  67     -33.749   6.260 -40.886  1.00 63.49           C  
ANISOU 2005  CA  TYR B  67     9165   7453   7506    972   -718   -199
ATOM   2006  C   TYR B  67     -34.792   6.018 -42.006  1.00 61.73           C  
ANISOU 2006  C   TYR B  67     8878   7345   7231   1014   -788   -215
ATOM   2007  O   TYR B  67     -34.922   4.874 -42.438  1.00 60.50           O  
ANISOU 2007  O   TYR B  67     8617   7237   7132    837   -779   -177
ATOM   2008  CB  TYR B  67     -34.289   5.939 -39.471  1.00 65.18           C  
ANISOU 2008  CB  TYR B  67     9151   7903   7711    972   -694   -192
ATOM   2009  CG  TYR B  67     -35.693   6.425 -39.125  1.00 68.08           C  
ANISOU 2009  CG  TYR B  67     9357   8568   7943   1173   -758   -246
ATOM   2010  CD1 TYR B  67     -35.982   7.801 -38.997  1.00 70.14           C  
ANISOU 2010  CD1 TYR B  67     9731   8835   8086   1455   -806   -312
ATOM   2011  CD2 TYR B  67     -36.724   5.481 -38.940  1.00 69.71           C  
ANISOU 2011  CD2 TYR B  67     9302   9071   8112   1081   -776   -235
ATOM   2012  CE1 TYR B  67     -37.305   8.222 -38.754  1.00 71.48           C  
ANISOU 2012  CE1 TYR B  67     9734   9321   8104   1689   -872   -379
ATOM   2013  CE2 TYR B  67     -38.042   5.898 -38.694  1.00 70.97           C  
ANISOU 2013  CE2 TYR B  67     9269   9579   8119   1267   -833   -297
ATOM   2014  CZ  TYR B  67     -38.338   7.271 -38.626  1.00 72.54           C  
ANISOU 2014  CZ  TYR B  67     9560   9801   8202   1596   -881   -374
ATOM   2015  OH  TYR B  67     -39.626   7.683 -38.467  1.00 74.52           O  
ANISOU 2015  OH  TYR B  67     9603  10436   8276   1828   -946   -452
ATOM   2016  H   TYR B  67     -33.398   8.194 -40.089  1.00 63.13           H  
ATOM   2017  HA  TYR B  67     -32.928   5.571 -41.092  1.00 63.49           H  
ATOM   2018  HB3 TYR B  67     -33.591   6.279 -38.707  1.00 65.18           H  
ATOM   2019  HB2 TYR B  67     -34.295   4.852 -39.378  1.00 65.18           H  
ATOM   2020  HD1 TYR B  67     -35.204   8.543 -39.092  1.00 70.14           H  
ATOM   2021  HD2 TYR B  67     -36.510   4.429 -38.992  1.00 69.71           H  
ATOM   2022  HE1 TYR B  67     -37.535   9.279 -38.673  1.00 71.48           H  
ATOM   2023  HE2 TYR B  67     -38.822   5.160 -38.579  1.00 70.97           H  
ATOM   2024  HH  TYR B  67     -40.195   7.040 -38.039  1.00 74.52           H  
ATOM   2025  N   ASN B  68     -35.473   7.080 -42.472  1.00 60.92           N  
ANISOU 2025  N   ASN B  68     8867   7278   7002   1257   -869   -275
ATOM   2026  CA  ASN B  68     -36.468   7.050 -43.554  1.00 59.87           C  
ANISOU 2026  CA  ASN B  68     8681   7277   6789   1349   -950   -304
ATOM   2027  C   ASN B  68     -35.827   7.435 -44.889  1.00 57.61           C  
ANISOU 2027  C   ASN B  68     8668   6725   6496   1363   -985   -309
ATOM   2028  O   ASN B  68     -36.069   6.757 -45.881  1.00 58.39           O  
ANISOU 2028  O   ASN B  68     8728   6853   6606   1292  -1013   -299
ATOM   2029  CB  ASN B  68     -37.622   8.050 -43.262  1.00 62.39           C  
ANISOU 2029  CB  ASN B  68     8918   7850   6939   1661  -1033   -382
ATOM   2030  CG  ASN B  68     -38.686   7.549 -42.290  1.00 68.62           C  
ANISOU 2030  CG  ASN B  68     9344   9049   7680   1635  -1028   -390
ATOM   2031  OD1 ASN B  68     -39.011   6.368 -42.275  1.00 71.09           O  
ANISOU 2031  OD1 ASN B  68     9475   9492   8046   1391  -1004   -343
ATOM   2032  ND2 ASN B  68     -39.263   8.440 -41.492  1.00 69.84           N  
ANISOU 2032  ND2 ASN B  68     9399   9430   7708   1877  -1058   -454
ATOM   2033  H   ASN B  68     -35.245   7.998 -42.111  1.00 60.92           H  
ATOM   2034  HA  ASN B  68     -36.862   6.034 -43.611  1.00 59.87           H  
ATOM   2035  HB3 ASN B  68     -38.166   8.247 -44.189  1.00 62.39           H  
ATOM   2036  HB2 ASN B  68     -37.236   9.017 -42.937  1.00 62.39           H  
ATOM   2037 HD22 ASN B  68     -39.904   8.126 -40.774  1.00 69.84           H  
ATOM   2038 HD21 ASN B  68     -39.022   9.423 -41.498  1.00 69.84           H  
ATOM   2039  N   ARG B  69     -35.059   8.533 -44.887  1.00 55.17           N  
ANISOU 2039  N   ARG B  69     8648   6170   6142   1447   -992   -326
ATOM   2040  CA  ARG B  69     -34.499   9.157 -46.092  1.00 53.79           C  
ANISOU 2040  CA  ARG B  69     8770   5742   5925   1442  -1029   -331
ATOM   2041  C   ARG B  69     -33.302   8.401 -46.697  1.00 51.72           C  
ANISOU 2041  C   ARG B  69     8549   5317   5787   1158   -948   -279
ATOM   2042  O   ARG B  69     -32.867   8.774 -47.788  1.00 51.78           O  
ANISOU 2042  O   ARG B  69     8747   5165   5762   1114   -971   -280
ATOM   2043  CB  ARG B  69     -34.035  10.583 -45.741  1.00 56.34           C  
ANISOU 2043  CB  ARG B  69     9426   5855   6127   1577  -1065   -361
ATOM   2044  CG  ARG B  69     -35.146  11.567 -45.327  1.00 59.40           C  
ANISOU 2044  CG  ARG B  69     9848   6367   6356   1918  -1163   -430
ATOM   2045  CD  ARG B  69     -34.612  12.801 -44.578  1.00 61.92           C  
ANISOU 2045  CD  ARG B  69    10463   6487   6577   1999  -1175   -447
ATOM   2046  NE  ARG B  69     -33.514  13.482 -45.300  1.00 62.57           N  
ANISOU 2046  NE  ARG B  69    10951   6233   6592   1874  -1193   -430
ATOM   2047  CZ  ARG B  69     -32.539  14.251 -44.796  1.00 63.45           C  
ANISOU 2047  CZ  ARG B  69    11336   6130   6643   1773  -1171   -417
ATOM   2048  NH1 ARG B  69     -31.553  14.641 -45.602  1.00 63.41           N  
ANISOU 2048  NH1 ARG B  69    11694   5854   6547   1613  -1189   -399
ATOM   2049  NH2 ARG B  69     -32.532  14.622 -43.510  1.00 61.98           N1+
ANISOU 2049  NH2 ARG B  69    11076   6008   6464   1819  -1137   -423
ATOM   2050  H   ARG B  69     -34.914   9.025 -44.011  1.00 55.17           H  
ATOM   2051  HA  ARG B  69     -35.265   9.205 -46.868  1.00 53.79           H  
ATOM   2052  HB3 ARG B  69     -33.532  11.006 -46.612  1.00 56.34           H  
ATOM   2053  HB2 ARG B  69     -33.280  10.521 -44.958  1.00 56.34           H  
ATOM   2054  HG3 ARG B  69     -35.795  11.042 -44.627  1.00 59.40           H  
ATOM   2055  HG2 ARG B  69     -35.798  11.835 -46.158  1.00 59.40           H  
ATOM   2056  HD3 ARG B  69     -34.336  12.537 -43.560  1.00 61.92           H  
ATOM   2057  HD2 ARG B  69     -35.423  13.525 -44.508  1.00 61.92           H  
ATOM   2058 HH22 ARG B  69     -31.797  15.177 -43.094  1.00 61.98           H  
ATOM   2059 HH21 ARG B  69     -33.339  14.435 -42.929  1.00 61.98           H  
ATOM   2060 HH12 ARG B  69     -30.752  15.176 -45.300  1.00 63.41           H  
ATOM   2061 HH11 ARG B  69     -31.567  14.349 -46.584  1.00 63.41           H  
ATOM   2062  HE  ARG B  69     -33.534  13.324 -46.307  1.00 62.57           H  
ATOM   2063  N   SER B  70     -32.726   7.442 -45.964  1.00 50.57           N  
ANISOU 2063  N   SER B  70     8237   5215   5762    982   -858   -240
ATOM   2064  CA  SER B  70     -31.591   6.648 -46.416  1.00 48.96           C  
ANISOU 2064  CA  SER B  70     8056   4893   5654    760   -785   -205
ATOM   2065  C   SER B  70     -31.980   5.718 -47.577  1.00 49.06           C  
ANISOU 2065  C   SER B  70     8003   4928   5708    677   -805   -192
ATOM   2066  O   SER B  70     -33.078   5.167 -47.600  1.00 50.09           O  
ANISOU 2066  O   SER B  70     7971   5226   5836    714   -850   -190
ATOM   2067  CB  SER B  70     -30.975   5.902 -45.209  1.00 48.28           C  
ANISOU 2067  CB  SER B  70     7817   4865   5662    650   -705   -176
ATOM   2068  OG  SER B  70     -29.922   5.016 -45.546  1.00 49.75           O  
ANISOU 2068  OG  SER B  70     8008   4973   5922    482   -642   -157
ATOM   2069  H   SER B  70     -33.140   7.171 -45.084  1.00 50.57           H  
ATOM   2070  HA  SER B  70     -30.843   7.341 -46.789  1.00 48.96           H  
ATOM   2071  HB3 SER B  70     -31.745   5.345 -44.673  1.00 48.28           H  
ATOM   2072  HB2 SER B  70     -30.555   6.629 -44.513  1.00 48.28           H  
ATOM   2073  HG  SER B  70     -29.082   5.406 -45.238  1.00 49.75           H  
ATOM   2074  N   THR B  71     -31.014   5.504 -48.469  1.00 47.66           N  
ANISOU 2074  N   THR B  71     7948   4608   5552    553   -773   -187
ATOM   2075  CA  THR B  71     -31.023   4.448 -49.485  1.00 46.82           C  
ANISOU 2075  CA  THR B  71     7787   4511   5491    464   -785   -175
ATOM   2076  C   THR B  71     -30.930   3.040 -48.857  1.00 47.17           C  
ANISOU 2076  C   THR B  71     7658   4636   5627    354   -747   -144
ATOM   2077  O   THR B  71     -31.309   2.062 -49.492  1.00 48.29           O  
ANISOU 2077  O   THR B  71     7756   4800   5792    280   -774   -129
ATOM   2078  CB  THR B  71     -29.825   4.617 -50.446  1.00 47.34           C  
ANISOU 2078  CB  THR B  71     8023   4430   5536    377   -760   -187
ATOM   2079  OG1 THR B  71     -28.620   4.771 -49.712  1.00 48.47           O  
ANISOU 2079  OG1 THR B  71     8164   4541   5711    274   -676   -187
ATOM   2080  CG2 THR B  71     -29.976   5.852 -51.334  1.00 47.59           C  
ANISOU 2080  CG2 THR B  71     8285   4348   5449    448   -805   -211
ATOM   2081  H   THR B  71     -30.150   6.022 -48.359  1.00 47.66           H  
ATOM   2082  HA  THR B  71     -31.956   4.509 -50.046  1.00 46.82           H  
ATOM   2083  HB  THR B  71     -29.731   3.740 -51.089  1.00 47.34           H  
ATOM   2084  HG1 THR B  71     -28.629   5.646 -49.304  1.00 48.47           H  
ATOM   2085 HG21 THR B  71     -29.138   5.931 -52.030  1.00 47.59           H  
ATOM   2086 HG22 THR B  71     -30.885   5.784 -51.934  1.00 47.59           H  
ATOM   2087 HG23 THR B  71     -30.035   6.772 -50.750  1.00 47.59           H  
ATOM   2088  N   SER B  72     -30.511   2.958 -47.593  1.00 46.23           N  
ANISOU 2088  N   SER B  72     7473   4545   5546    337   -695   -133
ATOM   2089  CA  SER B  72     -30.489   1.750 -46.790  1.00 45.24           C  
ANISOU 2089  CA  SER B  72     7223   4481   5485    246   -673   -101
ATOM   2090  C   SER B  72     -31.292   2.002 -45.497  1.00 45.66           C  
ANISOU 2090  C   SER B  72     7142   4682   5526    299   -678    -90
ATOM   2091  O   SER B  72     -30.673   2.131 -44.437  1.00 45.24           O  
ANISOU 2091  O   SER B  72     7064   4625   5501    296   -628    -84
ATOM   2092  CB  SER B  72     -29.007   1.391 -46.551  1.00 44.10           C  
ANISOU 2092  CB  SER B  72     7126   4251   5381    192   -605   -107
ATOM   2093  OG  SER B  72     -28.285   2.501 -46.027  1.00 45.35           O  
ANISOU 2093  OG  SER B  72     7334   4386   5512    233   -561   -126
ATOM   2094  H   SER B  72     -30.218   3.800 -47.106  1.00 46.23           H  
ATOM   2095  HA  SER B  72     -30.965   0.920 -47.311  1.00 45.24           H  
ATOM   2096  HB3 SER B  72     -28.550   1.060 -47.485  1.00 44.10           H  
ATOM   2097  HB2 SER B  72     -28.931   0.552 -45.858  1.00 44.10           H  
ATOM   2098  HG  SER B  72     -28.867   2.935 -45.387  1.00 45.35           H  
ATOM   2099  N   PRO B  73     -32.632   2.180 -45.591  1.00 46.13           N  
ANISOU 2099  N   PRO B  73     7102   4899   5524    364   -739    -96
ATOM   2100  CA  PRO B  73     -33.432   2.644 -44.446  1.00 46.05           C  
ANISOU 2100  CA  PRO B  73     6948   5075   5475    442   -744   -100
ATOM   2101  C   PRO B  73     -33.558   1.584 -43.339  1.00 45.81           C  
ANISOU 2101  C   PRO B  73     6783   5144   5480    295   -717    -58
ATOM   2102  O   PRO B  73     -33.485   0.381 -43.619  1.00 45.63           O  
ANISOU 2102  O   PRO B  73     6784   5061   5491    136   -721    -23
ATOM   2103  CB  PRO B  73     -34.777   3.004 -45.086  1.00 46.59           C  
ANISOU 2103  CB  PRO B  73     6926   5333   5443    552   -822   -129
ATOM   2104  CG  PRO B  73     -34.913   2.036 -46.249  1.00 47.06           C  
ANISOU 2104  CG  PRO B  73     7011   5353   5518    416   -854   -109
ATOM   2105  CD  PRO B  73     -33.481   1.928 -46.763  1.00 45.78           C  
ANISOU 2105  CD  PRO B  73     7052   4911   5431    370   -808   -104
ATOM   2106  HA  PRO B  73     -32.982   3.538 -44.014  1.00 46.05           H  
ATOM   2107  HB3 PRO B  73     -34.727   4.027 -45.465  1.00 46.59           H  
ATOM   2108  HB2 PRO B  73     -35.612   2.967 -44.387  1.00 46.59           H  
ATOM   2109  HG3 PRO B  73     -35.621   2.365 -47.010  1.00 47.06           H  
ATOM   2110  HG2 PRO B  73     -35.243   1.072 -45.867  1.00 47.06           H  
ATOM   2111  HD2 PRO B  73     -33.286   0.962 -47.227  1.00 45.78           H  
ATOM   2112  HD3 PRO B  73     -33.312   2.701 -47.509  1.00 45.78           H  
ATOM   2113  N   TRP B  74     -33.750   2.044 -42.099  1.00 45.89           N  
ANISOU 2113  N   TRP B  74     6682   5287   5467    352   -697    -61
ATOM   2114  CA  TRP B  74     -33.791   1.196 -40.912  1.00 46.82           C  
ANISOU 2114  CA  TRP B  74     6690   5498   5603    208   -671    -19
ATOM   2115  C   TRP B  74     -34.957   1.566 -39.998  1.00 49.20           C  
ANISOU 2115  C   TRP B  74     6789   6089   5816    263   -684    -33
ATOM   2116  O   TRP B  74     -35.591   2.602 -40.183  1.00 49.48           O  
ANISOU 2116  O   TRP B  74     6790   6225   5784    465   -707    -85
ATOM   2117  CB  TRP B  74     -32.431   1.221 -40.180  1.00 45.80           C  
ANISOU 2117  CB  TRP B  74     6658   5190   5556    194   -606     -7
ATOM   2118  CG  TRP B  74     -31.981   2.483 -39.506  1.00 44.39           C  
ANISOU 2118  CG  TRP B  74     6506   4990   5370    348   -570    -40
ATOM   2119  CD1 TRP B  74     -32.264   2.845 -38.233  1.00 45.26           C  
ANISOU 2119  CD1 TRP B  74     6520   5216   5460    391   -546    -40
ATOM   2120  CD2 TRP B  74     -31.171   3.561 -40.060  1.00 43.03           C  
ANISOU 2120  CD2 TRP B  74     6501   4650   5196    443   -556    -73
ATOM   2121  NE1 TRP B  74     -31.641   4.043 -37.944  1.00 45.18           N  
ANISOU 2121  NE1 TRP B  74     6619   5113   5436    525   -524    -74
ATOM   2122  CE2 TRP B  74     -30.945   4.528 -39.034  1.00 44.58           C  
ANISOU 2122  CE2 TRP B  74     6715   4859   5364    541   -531    -92
ATOM   2123  CE3 TRP B  74     -30.583   3.810 -41.322  1.00 42.13           C  
ANISOU 2123  CE3 TRP B  74     6539   4387   5084    439   -565    -89
ATOM   2124  CZ2 TRP B  74     -30.154   5.671 -39.245  1.00 44.73           C  
ANISOU 2124  CZ2 TRP B  74     6922   4728   5347    607   -520   -120
ATOM   2125  CZ3 TRP B  74     -29.803   4.959 -41.553  1.00 43.52           C  
ANISOU 2125  CZ3 TRP B  74     6880   4433   5221    497   -549   -117
ATOM   2126  CH2 TRP B  74     -29.584   5.885 -40.514  1.00 44.13           C  
ANISOU 2126  CH2 TRP B  74     6997   4511   5261    569   -529   -130
ATOM   2127  H   TRP B  74     -33.960   3.028 -41.965  1.00 45.89           H  
ATOM   2128  HA  TRP B  74     -33.982   0.172 -41.226  1.00 46.82           H  
ATOM   2129  HB3 TRP B  74     -31.652   0.932 -40.884  1.00 45.80           H  
ATOM   2130  HB2 TRP B  74     -32.414   0.450 -39.410  1.00 45.80           H  
ATOM   2131  HD1 TRP B  74     -32.854   2.255 -37.543  1.00 45.26           H  
ATOM   2132  HE1 TRP B  74     -31.686   4.488 -37.033  1.00 45.18           H  
ATOM   2133  HE3 TRP B  74     -30.738   3.111 -42.128  1.00 42.13           H  
ATOM   2134  HZ2 TRP B  74     -29.973   6.371 -38.442  1.00 44.73           H  
ATOM   2135  HZ3 TRP B  74     -29.371   5.127 -42.529  1.00 43.52           H  
ATOM   2136  HH2 TRP B  74     -28.970   6.756 -40.679  1.00 44.13           H  
ATOM   2137  N   ASN B  75     -35.231   0.676 -39.046  1.00 51.01           N  
ANISOU 2137  N   ASN B  75     6899   6458   6025     91   -674      9
ATOM   2138  CA  ASN B  75     -36.193   0.850 -37.958  1.00 53.39           C  
ANISOU 2138  CA  ASN B  75     6984   7072   6229    113   -672     -4
ATOM   2139  C   ASN B  75     -35.408   0.674 -36.652  1.00 54.30           C  
ANISOU 2139  C   ASN B  75     7116   7117   6399     61   -613     26
ATOM   2140  O   ASN B  75     -34.490  -0.152 -36.632  1.00 53.96           O  
ANISOU 2140  O   ASN B  75     7221   6838   6446    -49   -589     66
ATOM   2141  CB  ASN B  75     -37.293  -0.241 -38.010  1.00 57.09           C  
ANISOU 2141  CB  ASN B  75     7287   7818   6587   -106   -715     24
ATOM   2142  CG  ASN B  75     -38.106  -0.287 -39.306  1.00 63.66           C  
ANISOU 2142  CG  ASN B  75     8089   8745   7356    -81   -777     -2
ATOM   2143  OD1 ASN B  75     -38.170   0.676 -40.064  1.00 65.50           O  
ANISOU 2143  OD1 ASN B  75     8395   8907   7587   -289   -809     39
ATOM   2144  ND2 ASN B  75     -38.731  -1.418 -39.600  1.00 64.99           N  
ANISOU 2144  ND2 ASN B  75     8171   9068   7456    185   -804    -75
ATOM   2145  H   ASN B  75     -34.663  -0.167 -38.989  1.00 51.01           H  
ATOM   2146  HA  ASN B  75     -36.646   1.844 -37.973  1.00 53.39           H  
ATOM   2147  HB3 ASN B  75     -37.988  -0.099 -37.180  1.00 57.09           H  
ATOM   2148  HB2 ASN B  75     -36.840  -1.224 -37.866  1.00 57.09           H  
ATOM   2149 HD22 ASN B  75     -39.289  -1.477 -40.436  1.00 64.99           H  
ATOM   2150 HD21 ASN B  75     -38.742  -2.190 -38.947  1.00 64.99           H  
ATOM   2151  N   LEU B  76     -35.780   1.392 -35.585  1.00 55.44           N  
ANISOU 2151  N   LEU B  76     7112   7475   6480    165   -594     -2
ATOM   2152  CA  LEU B  76     -35.169   1.218 -34.265  1.00 57.10           C  
ANISOU 2152  CA  LEU B  76     7328   7634   6732    118   -541     25
ATOM   2153  C   LEU B  76     -36.010   0.220 -33.453  1.00 58.72           C  
ANISOU 2153  C   LEU B  76     7381   8072   6857   -119   -542     72
ATOM   2154  O   LEU B  76     -37.235   0.354 -33.426  1.00 58.29           O  
ANISOU 2154  O   LEU B  76     7121   8357   6670   -154   -568     53
ATOM   2155  CB  LEU B  76     -35.063   2.571 -33.524  1.00 57.93           C  
ANISOU 2155  CB  LEU B  76     7419   7773   6818    368   -516    -32
ATOM   2156  CG  LEU B  76     -34.111   3.597 -34.177  1.00 60.10           C  
ANISOU 2156  CG  LEU B  76     7915   7759   7160    539   -507    -63
ATOM   2157  CD1 LEU B  76     -34.189   4.946 -33.439  1.00 61.52           C  
ANISOU 2157  CD1 LEU B  76     8116   7967   7292    745   -493   -111
ATOM   2158  CD2 LEU B  76     -32.651   3.097 -34.238  1.00 60.73           C  
ANISOU 2158  CD2 LEU B  76     8154   7558   7364    402   -466    -18
ATOM   2159  H   LEU B  76     -36.608   1.971 -35.601  1.00 55.44           H  
ATOM   2160  HA  LEU B  76     -34.161   0.828 -34.383  1.00 57.10           H  
ATOM   2161  HB3 LEU B  76     -34.709   2.385 -32.509  1.00 57.93           H  
ATOM   2162  HB2 LEU B  76     -36.060   3.001 -33.416  1.00 57.93           H  
ATOM   2163  HG  LEU B  76     -34.451   3.776 -35.201  1.00 60.10           H  
ATOM   2164 HD11 LEU B  76     -33.547   5.695 -33.905  1.00 61.52           H  
ATOM   2165 HD12 LEU B  76     -35.202   5.348 -33.446  1.00 61.52           H  
ATOM   2166 HD13 LEU B  76     -33.877   4.853 -32.398  1.00 61.52           H  
ATOM   2167 HD21 LEU B  76     -31.937   3.875 -33.961  1.00 60.73           H  
ATOM   2168 HD22 LEU B  76     -32.469   2.260 -33.564  1.00 60.73           H  
ATOM   2169 HD23 LEU B  76     -32.390   2.766 -35.243  1.00 60.73           H  
ATOM   2170  N   HIS B  77     -35.345  -0.746 -32.813  1.00 60.28           N  
ANISOU 2170  N   HIS B  77     7687   8104   7113   -287   -519    130
ATOM   2171  CA  HIS B  77     -35.946  -1.704 -31.885  1.00 61.74           C  
ANISOU 2171  CA  HIS B  77     7793   8457   7207   -548   -526    186
ATOM   2172  C   HIS B  77     -35.424  -1.425 -30.471  1.00 60.90           C  
ANISOU 2172  C   HIS B  77     7665   8348   7125   -513   -475    194
ATOM   2173  O   HIS B  77     -34.248  -1.095 -30.318  1.00 60.17           O  
ANISOU 2173  O   HIS B  77     7722   7993   7147   -414   -444    195
ATOM   2174  CB  HIS B  77     -35.612  -3.145 -32.320  1.00 64.88           C  
ANISOU 2174  CB  HIS B  77     8390   8651   7610   -802   -572    254
ATOM   2175  CG  HIS B  77     -36.320  -3.567 -33.583  1.00 71.77           C  
ANISOU 2175  CG  HIS B  77     9248   9603   8416   -896   -628    252
ATOM   2176  ND1 HIS B  77     -35.886  -3.187 -34.839  1.00 75.04           N  
ANISOU 2176  ND1 HIS B  77     9494  10353   8663  -1122   -663    271
ATOM   2177  CD2 HIS B  77     -37.454  -4.322 -33.797  1.00 73.82           C  
ANISOU 2177  CD2 HIS B  77     9622   9683   8744   -794   -652    229
ATOM   2178  CE1 HIS B  77     -36.745  -3.695 -35.726  1.00 75.84           C  
ANISOU 2178  CE1 HIS B  77     9618  10456   8740  -1148   -710    260
ATOM   2179  NE2 HIS B  77     -37.717  -4.401 -35.167  1.00 75.53           N  
ANISOU 2179  NE2 HIS B  77     9751  10101   8845   -945   -705    235
ATOM   2180  H   HIS B  77     -34.325  -0.773 -32.870  1.00 60.28           H  
ATOM   2181  HA  HIS B  77     -37.033  -1.592 -31.866  1.00 61.74           H  
ATOM   2182  HB3 HIS B  77     -35.877  -3.851 -31.529  1.00 64.88           H  
ATOM   2183  HB2 HIS B  77     -34.535  -3.253 -32.466  1.00 64.88           H  
ATOM   2184  HD1 HIS B  77     -35.078  -2.608 -35.028  1.00 75.04           H  
ATOM   2185  HD2 HIS B  77     -38.100  -4.804 -33.081  1.00 73.82           H  
ATOM   2186  HE1 HIS B  77     -36.658  -3.557 -36.792  1.00 75.84           H  
ATOM   2187  N   ARG B  78     -36.314  -1.546 -29.481  1.00 61.11           N  
ANISOU 2187  N   ARG B  78     7486   8706   7029   -588   -463    192
ATOM   2188  CA  ARG B  78     -36.058  -1.193 -28.090  1.00 61.87           C  
ANISOU 2188  CA  ARG B  78     7526   8861   7121   -564   -415    196
ATOM   2189  C   ARG B  78     -35.604  -2.443 -27.328  1.00 62.40           C  
ANISOU 2189  C   ARG B  78     7737   8789   7185   -842   -424    280
ATOM   2190  O   ARG B  78     -36.436  -3.281 -26.994  1.00 62.59           O  
ANISOU 2190  O   ARG B  78     7743   8953   7087  -1126   -463    330
ATOM   2191  CB  ARG B  78     -37.365  -0.604 -27.511  1.00 63.68           C  
ANISOU 2191  CB  ARG B  78     7459   9551   7185   -540   -405    153
ATOM   2192  CG  ARG B  78     -37.204   0.090 -26.149  1.00 66.68           C  
ANISOU 2192  CG  ARG B  78     7761  10016   7559   -400   -353    125
ATOM   2193  CD  ARG B  78     -38.528   0.725 -25.676  1.00 69.41           C  
ANISOU 2193  CD  ARG B  78     7796  10863   7713   -354   -350     67
ATOM   2194  NE  ARG B  78     -38.479   1.204 -24.284  1.00 70.78           N  
ANISOU 2194  NE  ARG B  78     7882  11154   7858   -182   -305     26
ATOM   2195  CZ  ARG B  78     -38.608   0.461 -23.174  1.00 71.66           C  
ANISOU 2195  CZ  ARG B  78     7898  11434   7894   -375   -271     64
ATOM   2196  NH1 ARG B  78     -38.511   1.036 -21.979  1.00 71.17           N  
ANISOU 2196  NH1 ARG B  78     7753  11487   7800   -191   -232     17
ATOM   2197  NH2 ARG B  78     -38.804  -0.855 -23.232  1.00 71.35           N1+
ANISOU 2197  NH2 ARG B  78     7872  11445   7795   -761   -284    149
ATOM   2198  H   ARG B  78     -37.220  -1.945 -29.673  1.00 61.11           H  
ATOM   2199  HA  ARG B  78     -35.276  -0.429 -28.042  1.00 61.87           H  
ATOM   2200  HB3 ARG B  78     -38.126  -1.383 -27.436  1.00 63.68           H  
ATOM   2201  HB2 ARG B  78     -37.766   0.124 -28.210  1.00 63.68           H  
ATOM   2202  HG3 ARG B  78     -36.487   0.895 -26.329  1.00 66.68           H  
ATOM   2203  HG2 ARG B  78     -36.754  -0.556 -25.391  1.00 66.68           H  
ATOM   2204  HD3 ARG B  78     -39.402   0.111 -25.892  1.00 69.41           H  
ATOM   2205  HD2 ARG B  78     -38.666   1.643 -26.245  1.00 69.41           H  
ATOM   2206 HH22 ARG B  78     -38.760  -1.398 -22.341  1.00 71.35           H  
ATOM   2207 HH21 ARG B  78     -38.892  -1.380 -24.085  1.00 71.35           H  
ATOM   2208 HH12 ARG B  78     -38.253   0.439 -21.166  1.00 71.17           H  
ATOM   2209 HH11 ARG B  78     -38.470   2.026 -21.806  1.00 71.17           H  
ATOM   2210  HE  ARG B  78     -38.272   2.187 -24.179  1.00 70.78           H  
ATOM   2211  N   ASN B  79     -34.298  -2.547 -27.082  1.00 62.53           N  
ANISOU 2211  N   ASN B  79     7914   8528   7315   -764   -397    295
ATOM   2212  CA  ASN B  79     -33.632  -3.595 -26.306  1.00 63.23           C  
ANISOU 2212  CA  ASN B  79     8176   8450   7399   -958   -415    364
ATOM   2213  C   ASN B  79     -33.613  -3.092 -24.851  1.00 63.26           C  
ANISOU 2213  C   ASN B  79     8066   8588   7382   -922   -362    361
ATOM   2214  O   ASN B  79     -32.912  -2.114 -24.588  1.00 63.24           O  
ANISOU 2214  O   ASN B  79     8044   8511   7472   -689   -315    316
ATOM   2215  CB  ASN B  79     -32.231  -3.757 -26.972  1.00 64.93           C  
ANISOU 2215  CB  ASN B  79     8637   8288   7747   -842   -427    365
ATOM   2216  CG  ASN B  79     -31.183  -4.677 -26.338  1.00 69.58           C  
ANISOU 2216  CG  ASN B  79     9426   8671   8340   -924   -450    413
ATOM   2217  OD1 ASN B  79     -31.171  -4.934 -25.133  1.00 70.23           O  
ANISOU 2217  OD1 ASN B  79     9499   8847   8339  -1082   -453    456
ATOM   2218  ND2 ASN B  79     -30.216  -5.110 -27.147  1.00 71.01           N  
ANISOU 2218  ND2 ASN B  79     9798   8580   8604   -803   -470    399
ATOM   2219  H   ASN B  79     -33.681  -1.778 -27.341  1.00 62.53           H  
ATOM   2220  HA  ASN B  79     -34.188  -4.535 -26.389  1.00 63.23           H  
ATOM   2221  HB3 ASN B  79     -31.746  -2.788 -27.050  1.00 64.93           H  
ATOM   2222  HB2 ASN B  79     -32.383  -4.092 -27.999  1.00 64.93           H  
ATOM   2223 HD22 ASN B  79     -29.488  -5.732 -26.837  1.00 71.01           H  
ATOM   2224 HD21 ASN B  79     -30.148  -4.822 -28.134  1.00 71.01           H  
ATOM   2225  N   GLU B  80     -34.400  -3.691 -23.945  1.00 63.69           N  
ANISOU 2225  N   GLU B  80     8052   8849   7298  -1171   -372    408
ATOM   2226  CA  GLU B  80     -34.413  -3.330 -22.521  1.00 64.41           C  
ANISOU 2226  CA  GLU B  80     8029   9090   7354  -1156   -323    406
ATOM   2227  C   GLU B  80     -33.836  -4.467 -21.663  1.00 62.97           C  
ANISOU 2227  C   GLU B  80     8046   8732   7145  -1357   -346    482
ATOM   2228  O   GLU B  80     -33.981  -5.638 -22.011  1.00 62.96           O  
ANISOU 2228  O   GLU B  80     8187   8700   7034  -1647   -408    548
ATOM   2229  CB  GLU B  80     -35.819  -2.886 -22.066  1.00 68.92           C  
ANISOU 2229  CB  GLU B  80     8295  10135   7756  -1232   -301    378
ATOM   2230  CG  GLU B  80     -35.845  -2.322 -20.618  1.00 78.35           C  
ANISOU 2230  CG  GLU B  80     9352  11503   8915  -1154   -243    357
ATOM   2231  CD  GLU B  80     -37.097  -1.524 -20.285  1.00 90.70           C  
ANISOU 2231  CD  GLU B  80    10594  13587  10282  -1218   -220    318
ATOM   2232  OE1 GLU B  80     -38.201  -1.965 -20.665  1.00 93.19           O  
ANISOU 2232  OE1 GLU B  80    10755  14166  10486  -1282   -247    293
ATOM   2233  OE2 GLU B  80     -36.952  -0.386 -19.795  1.00 94.59           O1-
ANISOU 2233  OE2 GLU B  80    10975  14248  10716  -1199   -176    307
ATOM   2234  H   GLU B  80     -34.924  -4.520 -24.186  1.00 63.69           H  
ATOM   2235  HA  GLU B  80     -33.772  -2.467 -22.369  1.00 64.41           H  
ATOM   2236  HB3 GLU B  80     -36.510  -3.729 -22.124  1.00 68.92           H  
ATOM   2237  HB2 GLU B  80     -36.193  -2.137 -22.765  1.00 68.92           H  
ATOM   2238  HG3 GLU B  80     -34.967  -1.700 -20.446  1.00 78.35           H  
ATOM   2239  HG2 GLU B  80     -35.803  -3.138 -19.898  1.00 78.35           H  
ATOM   2240  N   ASP B  81     -33.187  -4.076 -20.562  1.00 61.18           N  
ANISOU 2240  N   ASP B  81     7857   8386   7004  -1208   -306    472
ATOM   2241  CA  ASP B  81     -32.397  -4.923 -19.672  1.00 60.35           C  
ANISOU 2241  CA  ASP B  81     7942   8117   6872  -1348   -332    535
ATOM   2242  C   ASP B  81     -32.293  -4.163 -18.326  1.00 59.28           C  
ANISOU 2242  C   ASP B  81     7659   8134   6731  -1274   -266    518
ATOM   2243  O   ASP B  81     -31.595  -3.148 -18.274  1.00 58.94           O  
ANISOU 2243  O   ASP B  81     7575   8015   6804  -1017   -218    466
ATOM   2244  CB  ASP B  81     -31.017  -5.193 -20.319  1.00 61.88           C  
ANISOU 2244  CB  ASP B  81     8403   7923   7187  -1211   -370    537
ATOM   2245  CG  ASP B  81     -30.001  -6.070 -19.588  1.00 66.20           C  
ANISOU 2245  CG  ASP B  81     9214   8261   7678  -1335   -431    599
ATOM   2246  OD1 ASP B  81     -30.160  -6.401 -18.393  1.00 68.17           O  
ANISOU 2246  OD1 ASP B  81     9449   8638   7814  -1531   -433    646
ATOM   2247  OD2 ASP B  81     -28.943  -6.304 -20.216  1.00 68.28           O1-
ANISOU 2247  OD2 ASP B  81     9704   8243   7995  -1223   -483    595
ATOM   2248  H   ASP B  81     -33.115  -3.086 -20.360  1.00 61.18           H  
ATOM   2249  HA  ASP B  81     -32.888  -5.886 -19.566  1.00 60.35           H  
ATOM   2250  HB3 ASP B  81     -30.536  -4.235 -20.497  1.00 61.88           H  
ATOM   2251  HB2 ASP B  81     -31.174  -5.617 -21.313  1.00 61.88           H  
ATOM   2252  N   PRO B  82     -33.021  -4.599 -17.270  1.00 59.01           N  
ANISOU 2252  N   PRO B  82     7554   8325   6541  -1521   -266    562
ATOM   2253  CA  PRO B  82     -33.016  -3.900 -15.968  1.00 58.64           C  
ANISOU 2253  CA  PRO B  82     7369   8435   6475  -1458   -205    546
ATOM   2254  C   PRO B  82     -31.695  -4.013 -15.178  1.00 57.61           C  
ANISOU 2254  C   PRO B  82     7439   8007   6441  -1368   -208    569
ATOM   2255  O   PRO B  82     -31.428  -3.164 -14.320  1.00 57.78           O  
ANISOU 2255  O   PRO B  82     7359   8107   6489  -1248   -153    543
ATOM   2256  CB  PRO B  82     -34.198  -4.535 -15.214  1.00 59.81           C  
ANISOU 2256  CB  PRO B  82     7413   8907   6405  -1802   -214    596
ATOM   2257  CG  PRO B  82     -34.320  -5.936 -15.795  1.00 60.38           C  
ANISOU 2257  CG  PRO B  82     7713   8839   6390  -2096   -301    669
ATOM   2258  CD  PRO B  82     -33.927  -5.748 -17.257  1.00 58.76           C  
ANISOU 2258  CD  PRO B  82     7576   8428   6323  -1897   -324    630
ATOM   2259  HA  PRO B  82     -33.209  -2.838 -16.118  1.00 58.64           H  
ATOM   2260  HB3 PRO B  82     -35.106  -3.969 -15.425  1.00 59.81           H  
ATOM   2261  HB2 PRO B  82     -34.074  -4.548 -14.129  1.00 59.81           H  
ATOM   2262  HG3 PRO B  82     -35.307  -6.386 -15.667  1.00 60.38           H  
ATOM   2263  HG2 PRO B  82     -33.592  -6.587 -15.309  1.00 60.38           H  
ATOM   2264  HD2 PRO B  82     -33.465  -6.659 -17.635  1.00 58.76           H  
ATOM   2265  HD3 PRO B  82     -34.800  -5.511 -17.868  1.00 58.76           H  
ATOM   2266  N   GLU B  83     -30.878  -5.024 -15.505  1.00 55.82           N  
ANISOU 2266  N   GLU B  83     7497   7454   6258  -1401   -278    610
ATOM   2267  CA  GLU B  83     -29.577  -5.298 -14.899  1.00 53.87           C  
ANISOU 2267  CA  GLU B  83     7436   6949   6084  -1284   -294    620
ATOM   2268  C   GLU B  83     -28.442  -4.474 -15.528  1.00 52.44           C  
ANISOU 2268  C   GLU B  83     7243   6611   6071   -972   -262    550
ATOM   2269  O   GLU B  83     -27.278  -4.688 -15.188  1.00 52.51           O  
ANISOU 2269  O   GLU B  83     7395   6423   6133   -857   -283    546
ATOM   2270  CB  GLU B  83     -29.314  -6.819 -14.969  1.00 54.91           C  
ANISOU 2270  CB  GLU B  83     7905   6823   6133  -1449   -404    687
ATOM   2271  CG  GLU B  83     -30.276  -7.641 -14.087  1.00 59.02           C  
ANISOU 2271  CG  GLU B  83     8514   7452   6458  -1798   -446    767
ATOM   2272  CD  GLU B  83     -30.107  -7.314 -12.605  1.00 64.45           C  
ANISOU 2272  CD  GLU B  83     9131   8234   7124  -1800   -401    779
ATOM   2273  OE1 GLU B  83     -28.960  -7.381 -12.114  1.00 63.51           O  
ANISOU 2273  OE1 GLU B  83     9138   7905   7087  -1609   -414    766
ATOM   2274  OE2 GLU B  83     -31.109  -6.920 -11.973  1.00 66.42           O1-
ANISOU 2274  OE2 GLU B  83     9181   8793   7265  -1982   -352    793
ATOM   2275  H   GLU B  83     -31.119  -5.649 -16.268  1.00 55.82           H  
ATOM   2276  HA  GLU B  83     -29.602  -4.998 -13.855  1.00 53.87           H  
ATOM   2277  HB3 GLU B  83     -28.284  -7.045 -14.688  1.00 54.91           H  
ATOM   2278  HB2 GLU B  83     -29.426  -7.165 -15.993  1.00 54.91           H  
ATOM   2279  HG3 GLU B  83     -30.093  -8.707 -14.225  1.00 59.02           H  
ATOM   2280  HG2 GLU B  83     -31.311  -7.479 -14.393  1.00 59.02           H  
ATOM   2281  N   ARG B  84     -28.792  -3.544 -16.420  1.00 51.24           N  
ANISOU 2281  N   ARG B  84     6930   6559   5981   -843   -218    494
ATOM   2282  CA  ARG B  84     -27.871  -2.721 -17.174  1.00 50.75           C  
ANISOU 2282  CA  ARG B  84     6882   6356   6043   -610   -195    435
ATOM   2283  C   ARG B  84     -28.202  -1.237 -16.970  1.00 51.29           C  
ANISOU 2283  C   ARG B  84     6767   6574   6147   -452   -124    373
ATOM   2284  O   ARG B  84     -29.368  -0.880 -16.794  1.00 51.56           O  
ANISOU 2284  O   ARG B  84     6645   6834   6111   -483   -105    362
ATOM   2285  CB  ARG B  84     -28.008  -3.156 -18.641  1.00 50.67           C  
ANISOU 2285  CB  ARG B  84     6968   6230   6053   -620   -245    432
ATOM   2286  CG  ARG B  84     -27.022  -2.549 -19.653  1.00 51.57           C  
ANISOU 2286  CG  ARG B  84     7102   6221   6271   -420   -226    373
ATOM   2287  CD  ARG B  84     -27.283  -3.065 -21.082  1.00 52.74           C  
ANISOU 2287  CD  ARG B  84     7318   6296   6423   -446   -270    370
ATOM   2288  NE  ARG B  84     -28.584  -2.621 -21.624  1.00 53.49           N  
ANISOU 2288  NE  ARG B  84     7263   6577   6482   -491   -255    360
ATOM   2289  CZ  ARG B  84     -29.349  -3.231 -22.548  1.00 55.24           C  
ANISOU 2289  CZ  ARG B  84     7511   6819   6657   -608   -302    380
ATOM   2290  NH1 ARG B  84     -30.481  -2.665 -22.938  1.00 54.46           N  
ANISOU 2290  NH1 ARG B  84     7245   6938   6510   -629   -289    361
ATOM   2291  NH2 ARG B  84     -29.031  -4.402 -23.101  1.00 54.65           N1+
ANISOU 2291  NH2 ARG B  84     7642   6558   6567   -691   -370    412
ATOM   2292  H   ARG B  84     -29.772  -3.399 -16.621  1.00 51.24           H  
ATOM   2293  HA  ARG B  84     -26.858  -2.911 -16.841  1.00 50.75           H  
ATOM   2294  HB3 ARG B  84     -29.030  -2.957 -18.956  1.00 50.67           H  
ATOM   2295  HB2 ARG B  84     -27.889  -4.237 -18.681  1.00 50.67           H  
ATOM   2296  HG3 ARG B  84     -25.990  -2.768 -19.367  1.00 51.57           H  
ATOM   2297  HG2 ARG B  84     -27.099  -1.462 -19.646  1.00 51.57           H  
ATOM   2298  HD3 ARG B  84     -27.274  -4.153 -21.055  1.00 52.74           H  
ATOM   2299  HD2 ARG B  84     -26.483  -2.769 -21.757  1.00 52.74           H  
ATOM   2300 HH22 ARG B  84     -29.613  -4.784 -23.848  1.00 54.65           H  
ATOM   2301 HH21 ARG B  84     -28.450  -5.055 -22.594  1.00 54.65           H  
ATOM   2302 HH12 ARG B  84     -31.047  -3.049 -23.690  1.00 54.46           H  
ATOM   2303 HH11 ARG B  84     -30.939  -1.943 -22.384  1.00 54.46           H  
ATOM   2304  HE  ARG B  84     -28.869  -1.700 -21.278  1.00 53.49           H  
ATOM   2305  N   TYR B  85     -27.173  -0.393 -17.054  1.00 51.01           N  
ANISOU 2305  N   TYR B  85     6763   6425   6195   -281    -94    329
ATOM   2306  CA  TYR B  85     -27.293   1.042 -17.281  1.00 51.06           C  
ANISOU 2306  CA  TYR B  85     6680   6505   6215   -128    -46    269
ATOM   2307  C   TYR B  85     -26.444   1.356 -18.538  1.00 48.77           C  
ANISOU 2307  C   TYR B  85     6481   6056   5994    -29    -51    231
ATOM   2308  O   TYR B  85     -25.259   1.008 -18.543  1.00 47.04           O  
ANISOU 2308  O   TYR B  85     6351   5703   5818    -15    -55    230
ATOM   2309  CB  TYR B  85     -26.823   1.803 -16.022  1.00 53.33           C  
ANISOU 2309  CB  TYR B  85     6947   6817   6498    -67     -3    255
ATOM   2310  CG  TYR B  85     -27.018   3.309 -16.093  1.00 56.62           C  
ANISOU 2310  CG  TYR B  85     7334   7278   6899     93     28    192
ATOM   2311  CD1 TYR B  85     -26.104   4.114 -16.805  1.00 58.73           C  
ANISOU 2311  CD1 TYR B  85     7707   7400   7208    181     33    154
ATOM   2312  CD2 TYR B  85     -28.125   3.907 -15.457  1.00 58.81           C  
ANISOU 2312  CD2 TYR B  85     7498   7755   7092    157     43    165
ATOM   2313  CE1 TYR B  85     -26.318   5.502 -16.907  1.00 60.78           C  
ANISOU 2313  CE1 TYR B  85     8009   7662   7424    315     42     99
ATOM   2314  CE2 TYR B  85     -28.321   5.300 -15.531  1.00 60.99           C  
ANISOU 2314  CE2 TYR B  85     7802   8045   7326    342     51     99
ATOM   2315  CZ  TYR B  85     -27.415   6.101 -16.255  1.00 63.06           C  
ANISOU 2315  CZ  TYR B  85     8219   8113   7629    414     45     70
ATOM   2316  OH  TYR B  85     -27.589   7.451 -16.331  1.00 66.81           O  
ANISOU 2316  OH  TYR B  85     8792   8558   8035    583     35      8
ATOM   2317  H   TYR B  85     -26.234  -0.775 -17.154  1.00 51.01           H  
ATOM   2318  HA  TYR B  85     -28.336   1.312 -17.412  1.00 51.06           H  
ATOM   2319  HB3 TYR B  85     -25.781   1.605 -15.799  1.00 53.33           H  
ATOM   2320  HB2 TYR B  85     -27.377   1.432 -15.161  1.00 53.33           H  
ATOM   2321  HD1 TYR B  85     -25.243   3.674 -17.288  1.00 58.73           H  
ATOM   2322  HD2 TYR B  85     -28.836   3.302 -14.913  1.00 58.81           H  
ATOM   2323  HE1 TYR B  85     -25.621   6.104 -17.472  1.00 60.78           H  
ATOM   2324  HE2 TYR B  85     -29.177   5.742 -15.038  1.00 60.99           H  
ATOM   2325  HH  TYR B  85     -28.137   7.840 -15.642  1.00 66.81           H  
ATOM   2326  N   PRO B  86     -27.010   2.027 -19.571  1.00 49.52           N  
ANISOU 2326  N   PRO B  86     6551   6182   6083     47    -54    194
ATOM   2327  CA  PRO B  86     -28.436   2.375 -19.750  1.00 49.52           C  
ANISOU 2327  CA  PRO B  86     6430   6376   6011     73    -61    177
ATOM   2328  C   PRO B  86     -29.333   1.130 -19.840  1.00 50.35           C  
ANISOU 2328  C   PRO B  86     6476   6584   6070   -105    -97    228
ATOM   2329  O   PRO B  86     -28.941   0.154 -20.479  1.00 49.71           O  
ANISOU 2329  O   PRO B  86     6502   6360   6024   -203   -133    263
ATOM   2330  CB  PRO B  86     -28.453   3.177 -21.067  1.00 50.09           C  
ANISOU 2330  CB  PRO B  86     6557   6377   6097    195    -76    130
ATOM   2331  CG  PRO B  86     -27.033   3.693 -21.228  1.00 50.81           C  
ANISOU 2331  CG  PRO B  86     6791   6262   6255    223    -60    117
ATOM   2332  CD  PRO B  86     -26.215   2.525 -20.693  1.00 49.64           C  
ANISOU 2332  CD  PRO B  86     6664   6050   6147    112    -60    163
ATOM   2333  HA  PRO B  86     -28.731   3.026 -18.925  1.00 49.52           H  
ATOM   2334  HB3 PRO B  86     -29.192   3.980 -21.062  1.00 50.09           H  
ATOM   2335  HB2 PRO B  86     -28.688   2.528 -21.914  1.00 50.09           H  
ATOM   2336  HG3 PRO B  86     -26.885   4.565 -20.588  1.00 50.81           H  
ATOM   2337  HG2 PRO B  86     -26.785   3.979 -22.250  1.00 50.81           H  
ATOM   2338  HD2 PRO B  86     -26.125   1.736 -21.444  1.00 49.64           H  
ATOM   2339  HD3 PRO B  86     -25.207   2.830 -20.413  1.00 49.64           H  
ATOM   2340  N   SER B  87     -30.490   1.155 -19.168  1.00 51.85           N  
ANISOU 2340  N   SER B  87     6508   7034   6158   -159    -92    230
ATOM   2341  CA  SER B  87     -31.398   0.013 -19.146  1.00 54.36           C  
ANISOU 2341  CA  SER B  87     6771   7491   6393   -386   -126    282
ATOM   2342  C   SER B  87     -32.035  -0.234 -20.523  1.00 55.77           C  
ANISOU 2342  C   SER B  87     6938   7692   6559   -401   -165    270
ATOM   2343  O   SER B  87     -32.142  -1.385 -20.934  1.00 55.99           O  
ANISOU 2343  O   SER B  87     7033   7685   6554   -605   -209    323
ATOM   2344  CB  SER B  87     -32.422   0.198 -18.009  1.00 56.50           C  
ANISOU 2344  CB  SER B  87     6844   8096   6527   -466   -104    281
ATOM   2345  OG  SER B  87     -33.113   1.434 -18.134  1.00 60.35           O  
ANISOU 2345  OG  SER B  87     7162   8816   6952   -263    -87    202
ATOM   2346  H   SER B  87     -30.823   1.960 -18.658  1.00 51.85           H  
ATOM   2347  HA  SER B  87     -30.807  -0.874 -18.915  1.00 54.36           H  
ATOM   2348  HB3 SER B  87     -31.917   0.160 -17.042  1.00 56.50           H  
ATOM   2349  HB2 SER B  87     -33.137  -0.628 -18.007  1.00 56.50           H  
ATOM   2350  HG  SER B  87     -34.055   1.266 -17.999  1.00 60.35           H  
ATOM   2351  N   VAL B  88     -32.370   0.840 -21.245  1.00 56.30           N  
ANISOU 2351  N   VAL B  88     6955   7795   6641   -187   -158    202
ATOM   2352  CA  VAL B  88     -32.899   0.815 -22.602  1.00 56.78           C  
ANISOU 2352  CA  VAL B  88     7000   7887   6687   -172   -196    184
ATOM   2353  C   VAL B  88     -31.775   1.190 -23.575  1.00 56.15           C  
ANISOU 2353  C   VAL B  88     7098   7513   6723    -52   -204    164
ATOM   2354  O   VAL B  88     -31.051   2.153 -23.324  1.00 56.32           O  
ANISOU 2354  O   VAL B  88     7183   7431   6786    128   -180    121
ATOM   2355  CB  VAL B  88     -34.028   1.871 -22.775  1.00 58.11           C  
ANISOU 2355  CB  VAL B  88     6968   8373   6737    -13   -199    113
ATOM   2356  CG1 VAL B  88     -34.596   1.965 -24.210  1.00 59.03           C  
ANISOU 2356  CG1 VAL B  88     7073   8519   6836     32   -244     87
ATOM   2357  CG2 VAL B  88     -35.177   1.592 -21.803  1.00 58.39           C  
ANISOU 2357  CG2 VAL B  88     6786   8773   6627   -157   -188    125
ATOM   2358  H   VAL B  88     -32.180   1.752 -20.865  1.00 56.30           H  
ATOM   2359  HA  VAL B  88     -33.288  -0.176 -22.844  1.00 56.78           H  
ATOM   2360  HB  VAL B  88     -33.619   2.851 -22.521  1.00 58.11           H  
ATOM   2361 HG11 VAL B  88     -35.471   2.613 -24.249  1.00 59.03           H  
ATOM   2362 HG12 VAL B  88     -33.873   2.373 -24.920  1.00 59.03           H  
ATOM   2363 HG13 VAL B  88     -34.892   0.980 -24.571  1.00 59.03           H  
ATOM   2364 HG21 VAL B  88     -35.944   2.362 -21.868  1.00 58.39           H  
ATOM   2365 HG22 VAL B  88     -35.633   0.630 -22.037  1.00 58.39           H  
ATOM   2366 HG23 VAL B  88     -34.845   1.557 -20.764  1.00 58.39           H  
ATOM   2367  N   ILE B  89     -31.670   0.433 -24.667  1.00 54.79           N  
ANISOU 2367  N   ILE B  89     7021   7212   6585   -169   -241    197
ATOM   2368  CA  ILE B  89     -30.812   0.725 -25.800  1.00 54.54           C  
ANISOU 2368  CA  ILE B  89     7136   6946   6642    -77   -250    176
ATOM   2369  C   ILE B  89     -31.682   0.554 -27.055  1.00 53.89           C  
ANISOU 2369  C   ILE B  89     7028   6921   6525    -98   -294    166
ATOM   2370  O   ILE B  89     -32.452  -0.405 -27.155  1.00 51.93           O  
ANISOU 2370  O   ILE B  89     6751   6760   6221   -280   -331    207
ATOM   2371  CB  ILE B  89     -29.597  -0.253 -25.848  1.00 55.00           C  
ANISOU 2371  CB  ILE B  89     7356   6770   6770   -153   -255    212
ATOM   2372  CG1 ILE B  89     -28.756  -0.075 -24.561  1.00 54.99           C  
ANISOU 2372  CG1 ILE B  89     7371   6723   6800   -101   -212    210
ATOM   2373  CG2 ILE B  89     -28.708  -0.080 -27.103  1.00 55.67           C  
ANISOU 2373  CG2 ILE B  89     7561   6675   6915    -84   -268    186
ATOM   2374  CD1 ILE B  89     -27.425  -0.838 -24.521  1.00 55.26           C  
ANISOU 2374  CD1 ILE B  89     7539   6587   6870   -147   -228    236
ATOM   2375  H   ILE B  89     -32.274  -0.375 -24.804  1.00 54.79           H  
ATOM   2376  HA  ILE B  89     -30.461   1.759 -25.755  1.00 54.54           H  
ATOM   2377  HB  ILE B  89     -29.983  -1.275 -25.862  1.00 55.00           H  
ATOM   2378 HG13 ILE B  89     -29.333  -0.379 -23.695  1.00 54.99           H  
ATOM   2379 HG12 ILE B  89     -28.605   0.986 -24.386  1.00 54.99           H  
ATOM   2380 HG21 ILE B  89     -27.932  -0.843 -27.146  1.00 55.67           H  
ATOM   2381 HG22 ILE B  89     -29.258  -0.188 -28.036  1.00 55.67           H  
ATOM   2382 HG23 ILE B  89     -28.222   0.895 -27.111  1.00 55.67           H  
ATOM   2383 HD11 ILE B  89     -27.026  -0.826 -23.507  1.00 55.26           H  
ATOM   2384 HD12 ILE B  89     -27.555  -1.878 -24.821  1.00 55.26           H  
ATOM   2385 HD13 ILE B  89     -26.674  -0.386 -25.171  1.00 55.26           H  
ATOM   2386  N   TRP B  90     -31.570   1.499 -27.984  1.00 54.86           N  
ANISOU 2386  N   TRP B  90     7179   7001   6664     74   -296    113
ATOM   2387  CA  TRP B  90     -32.210   1.436 -29.290  1.00 56.27           C  
ANISOU 2387  CA  TRP B  90     7341   7227   6812     85   -340     97
ATOM   2388  C   TRP B  90     -31.187   0.962 -30.326  1.00 56.74           C  
ANISOU 2388  C   TRP B  90     7573   7031   6954     48   -352    109
ATOM   2389  O   TRP B  90     -30.187   1.654 -30.527  1.00 57.58           O  
ANISOU 2389  O   TRP B  90     7791   6968   7117    145   -326     84
ATOM   2390  CB  TRP B  90     -32.756   2.817 -29.670  1.00 56.86           C  
ANISOU 2390  CB  TRP B  90     7380   7393   6830    318   -350     27
ATOM   2391  CG  TRP B  90     -33.863   3.312 -28.798  1.00 58.18           C  
ANISOU 2391  CG  TRP B  90     7356   7865   6884    396   -350     -4
ATOM   2392  CD1 TRP B  90     -33.715   4.084 -27.698  1.00 59.39           C  
ANISOU 2392  CD1 TRP B  90     7484   8071   7011    504   -317    -27
ATOM   2393  CD2 TRP B  90     -35.290   3.035 -28.913  1.00 59.10           C  
ANISOU 2393  CD2 TRP B  90     7263   8317   6876    370   -384    -21
ATOM   2394  NE1 TRP B  90     -34.959   4.364 -27.169  1.00 59.97           N  
ANISOU 2394  NE1 TRP B  90     7342   8494   6951    566   -328    -62
ATOM   2395  CE2 TRP B  90     -35.970   3.746 -27.878  1.00 60.15           C  
ANISOU 2395  CE2 TRP B  90     7234   8717   6904    484   -368    -61
ATOM   2396  CE3 TRP B  90     -36.089   2.279 -29.808  1.00 59.66           C  
ANISOU 2396  CE3 TRP B  90     7259   8512   6898    250   -428     -8
ATOM   2397  CZ2 TRP B  90     -37.371   3.733 -27.758  1.00 61.13           C  
ANISOU 2397  CZ2 TRP B  90     7096   9266   6864    490   -391    -97
ATOM   2398  CZ3 TRP B  90     -37.492   2.268 -29.706  1.00 60.96           C  
ANISOU 2398  CZ3 TRP B  90     7170   9088   6903    229   -452    -37
ATOM   2399  CH2 TRP B  90     -38.135   2.993 -28.683  1.00 61.08           C  
ANISOU 2399  CH2 TRP B  90     7002   9402   6805    354   -432    -84
ATOM   2400  H   TRP B  90     -30.945   2.291 -27.821  1.00 54.86           H  
ATOM   2401  HA  TRP B  90     -33.059   0.755 -29.262  1.00 56.27           H  
ATOM   2402  HB3 TRP B  90     -33.144   2.782 -30.688  1.00 56.86           H  
ATOM   2403  HB2 TRP B  90     -31.957   3.560 -29.686  1.00 56.86           H  
ATOM   2404  HD1 TRP B  90     -32.760   4.444 -27.332  1.00 59.39           H  
ATOM   2405  HE1 TRP B  90     -35.080   5.007 -26.402  1.00 59.97           H  
ATOM   2406  HE3 TRP B  90     -35.614   1.712 -30.592  1.00 59.66           H  
ATOM   2407  HZ2 TRP B  90     -37.861   4.307 -26.987  1.00 61.13           H  
ATOM   2408  HZ3 TRP B  90     -38.077   1.697 -30.413  1.00 60.96           H  
ATOM   2409  HH2 TRP B  90     -39.214   2.989 -28.613  1.00 61.08           H  
ATOM   2410  N   GLU B  91     -31.461  -0.177 -30.967  1.00 56.37           N  
ANISOU 2410  N   GLU B  91     7555   6969   6896   -106   -393    146
ATOM   2411  CA  GLU B  91     -30.666  -0.697 -32.077  1.00 56.15           C  
ANISOU 2411  CA  GLU B  91     7691   6717   6927   -128   -413    151
ATOM   2412  C   GLU B  91     -31.417  -0.566 -33.406  1.00 54.78           C  
ANISOU 2412  C   GLU B  91     7518   6567   6730   -113   -453    132
ATOM   2413  O   GLU B  91     -32.633  -0.761 -33.454  1.00 54.43           O  
ANISOU 2413  O   GLU B  91     7355   6718   6606   -183   -487    139
ATOM   2414  CB  GLU B  91     -30.334  -2.176 -31.857  1.00 59.00           C  
ANISOU 2414  CB  GLU B  91     8160   6978   7279   -297   -445    205
ATOM   2415  CG  GLU B  91     -29.265  -2.419 -30.779  1.00 65.34           C  
ANISOU 2415  CG  GLU B  91     9037   7659   8128   -254   -415    209
ATOM   2416  CD  GLU B  91     -28.746  -3.847 -30.887  1.00 73.25           C  
ANISOU 2416  CD  GLU B  91    10227   8489   9117   -332   -467    238
ATOM   2417  OE1 GLU B  91     -29.193  -4.669 -30.056  1.00 77.96           O  
ANISOU 2417  OE1 GLU B  91    10873   9099   9651   -475   -502    289
ATOM   2418  OE2 GLU B  91     -27.978  -4.079 -31.852  1.00 70.97           O1-
ANISOU 2418  OE2 GLU B  91    10050   8057   8858   -251   -481    209
ATOM   2419  H   GLU B  91     -32.308  -0.687 -30.744  1.00 56.37           H  
ATOM   2420  HA  GLU B  91     -29.729  -0.143 -32.159  1.00 56.15           H  
ATOM   2421  HB3 GLU B  91     -30.009  -2.616 -32.804  1.00 59.00           H  
ATOM   2422  HB2 GLU B  91     -31.242  -2.714 -31.583  1.00 59.00           H  
ATOM   2423  HG3 GLU B  91     -29.674  -2.225 -29.788  1.00 65.34           H  
ATOM   2424  HG2 GLU B  91     -28.428  -1.733 -30.910  1.00 65.34           H  
ATOM   2425  N   ALA B  92     -30.657  -0.282 -34.466  1.00 53.59           N  
ANISOU 2425  N   ALA B  92     7491   6237   6632    -37   -451    106
ATOM   2426  CA  ALA B  92     -31.123  -0.199 -35.841  1.00 52.34           C  
ANISOU 2426  CA  ALA B  92     7357   6073   6455    -17   -489     87
ATOM   2427  C   ALA B  92     -31.205  -1.584 -36.494  1.00 51.82           C  
ANISOU 2427  C   ALA B  92     7376   5935   6380   -171   -539    123
ATOM   2428  O   ALA B  92     -30.211  -2.303 -36.529  1.00 51.79           O  
ANISOU 2428  O   ALA B  92     7496   5776   6404   -216   -541    139
ATOM   2429  CB  ALA B  92     -30.151   0.676 -36.639  1.00 51.19           C  
ANISOU 2429  CB  ALA B  92     7322   5779   6350    112   -466     44
ATOM   2430  H   ALA B  92     -29.651  -0.202 -34.317  1.00 53.59           H  
ATOM   2431  HA  ALA B  92     -32.102   0.278 -35.847  1.00 52.34           H  
ATOM   2432  HB1 ALA B  92     -30.458   0.757 -37.680  1.00 51.19           H  
ATOM   2433  HB2 ALA B  92     -30.093   1.685 -36.234  1.00 51.19           H  
ATOM   2434  HB3 ALA B  92     -29.149   0.249 -36.635  1.00 51.19           H  
ATOM   2435  N   LYS B  93     -32.356  -1.894 -37.090  1.00 51.49           N  
ANISOU 2435  N   LYS B  93     7278   6011   6277   -242   -587    129
ATOM   2436  CA  LYS B  93     -32.502  -3.002 -38.020  1.00 52.19           C  
ANISOU 2436  CA  LYS B  93     7477   6018   6334   -400   -645    161
ATOM   2437  C   LYS B  93     -32.850  -2.428 -39.398  1.00 51.30           C  
ANISOU 2437  C   LYS B  93     7380   5886   6224   -318   -668    125
ATOM   2438  O   LYS B  93     -33.858  -1.733 -39.516  1.00 51.12           O  
ANISOU 2438  O   LYS B  93     7218   6052   6152   -260   -680    102
ATOM   2439  CB  LYS B  93     -33.584  -3.965 -37.492  1.00 55.93           C  
ANISOU 2439  CB  LYS B  93     7864   6692   6696   -627   -688    210
ATOM   2440  CG  LYS B  93     -34.042  -4.997 -38.541  1.00 63.65           C  
ANISOU 2440  CG  LYS B  93     8938   7648   7599   -817   -763    240
ATOM   2441  CD  LYS B  93     -34.460  -6.366 -37.983  1.00 70.28           C  
ANISOU 2441  CD  LYS B  93     9885   8488   8331  -1104   -816    308
ATOM   2442  CE  LYS B  93     -35.031  -7.313 -39.064  1.00 74.93           C  
ANISOU 2442  CE  LYS B  93    10636   8993   8841  -1284   -897    334
ATOM   2443  NZ  LYS B  93     -34.149  -7.444 -40.251  1.00 77.81           N1+
ANISOU 2443  NZ  LYS B  93    11162   9100   9304  -1099   -900    294
ATOM   2444  H   LYS B  93     -33.141  -1.250 -37.009  1.00 51.49           H  
ATOM   2445  HA  LYS B  93     -31.569  -3.565 -38.108  1.00 52.19           H  
ATOM   2446  HB3 LYS B  93     -34.446  -3.383 -37.176  1.00 55.93           H  
ATOM   2447  HB2 LYS B  93     -33.205  -4.455 -36.594  1.00 55.93           H  
ATOM   2448  HG3 LYS B  93     -33.226  -5.143 -39.250  1.00 63.65           H  
ATOM   2449  HG2 LYS B  93     -34.872  -4.566 -39.105  1.00 63.65           H  
ATOM   2450  HD3 LYS B  93     -35.208  -6.226 -37.199  1.00 70.28           H  
ATOM   2451  HD2 LYS B  93     -33.605  -6.828 -37.485  1.00 70.28           H  
ATOM   2452  HE3 LYS B  93     -36.003  -6.944 -39.393  1.00 74.93           H  
ATOM   2453  HE2 LYS B  93     -35.217  -8.299 -38.634  1.00 74.93           H  
ATOM   2454  HZ1 LYS B  93     -34.058  -6.547 -40.717  1.00 77.81           H  
ATOM   2455  HZ2 LYS B  93     -33.231  -7.764 -39.976  1.00 77.81           H  
ATOM   2456  HZ3 LYS B  93     -34.541  -8.103 -40.910  1.00 77.81           H  
ATOM   2457  N   CYS B  94     -32.048  -2.761 -40.418  1.00 51.01           N  
ANISOU 2457  N   CYS B  94     7509   5643   6231   -295   -678    114
ATOM   2458  CA  CYS B  94     -32.288  -2.390 -41.820  1.00 50.85           C  
ANISOU 2458  CA  CYS B  94     7522   5592   6208   -235   -702     83
ATOM   2459  C   CYS B  94     -33.600  -3.023 -42.333  1.00 50.25           C  
ANISOU 2459  C   CYS B  94     7371   5675   6044   -367   -768    105
ATOM   2460  O   CYS B  94     -33.881  -4.182 -41.995  1.00 50.26           O  
ANISOU 2460  O   CYS B  94     7406   5703   5988   -564   -808    151
ATOM   2461  CB  CYS B  94     -31.098  -2.826 -42.705  1.00 50.88           C  
ANISOU 2461  CB  CYS B  94     7707   5372   6253   -204   -700     65
ATOM   2462  SG  CYS B  94     -29.445  -2.665 -41.959  1.00 55.14           S  
ANISOU 2462  SG  CYS B  94     8299   5796   6855    -84   -625     34
ATOM   2463  H   CYS B  94     -31.186  -3.261 -40.241  1.00 51.01           H  
ATOM   2464  HA  CYS B  94     -32.362  -1.303 -41.870  1.00 50.85           H  
ATOM   2465  HB3 CYS B  94     -31.111  -2.253 -43.634  1.00 50.88           H  
ATOM   2466  HB2 CYS B  94     -31.211  -3.872 -42.998  1.00 50.88           H  
ATOM   2467  N   ARG B  95     -34.383  -2.261 -43.108  1.00 49.99           N  
ANISOU 2467  N   ARG B  95     7245   5771   5979   -266   -785     70
ATOM   2468  CA  ARG B  95     -35.680  -2.705 -43.635  1.00 51.37           C  
ANISOU 2468  CA  ARG B  95     7313   6154   6051   -386   -850     81
ATOM   2469  C   ARG B  95     -35.560  -3.737 -44.766  1.00 51.01           C  
ANISOU 2469  C   ARG B  95     7424   5960   5995   -520   -900    101
ATOM   2470  O   ARG B  95     -36.412  -4.617 -44.864  1.00 51.05           O  
ANISOU 2470  O   ARG B  95     7398   6092   5906   -724   -956    134
ATOM   2471  CB  ARG B  95     -36.488  -1.509 -44.167  1.00 53.19           C  
ANISOU 2471  CB  ARG B  95     7410   6571   6230   -198   -869     27
ATOM   2472  CG  ARG B  95     -36.792  -0.439 -43.120  1.00 57.81           C  
ANISOU 2472  CG  ARG B  95     7818   7377   6769    -74   -846      1
ATOM   2473  CD  ARG B  95     -37.607   0.729 -43.691  1.00 59.35           C  
ANISOU 2473  CD  ARG B  95     7896   7785   6871    140   -890    -62
ATOM   2474  NE  ARG B  95     -37.697   1.794 -42.688  1.00 61.79           N  
ANISOU 2474  NE  ARG B  95     8165   8143   7168    361   -861   -103
ATOM   2475  CZ  ARG B  95     -38.120   3.051 -42.800  1.00 63.43           C  
ANISOU 2475  CZ  ARG B  95     8400   8386   7315    640   -895   -169
ATOM   2476  NH1 ARG B  95     -38.610   3.554 -43.934  1.00 61.55           N  
ANISOU 2476  NH1 ARG B  95     8207   8158   7022    739   -960   -202
ATOM   2477  NH2 ARG B  95     -38.048   3.811 -41.715  1.00 64.89           N1+
ANISOU 2477  NH2 ARG B  95     8590   8588   7476    828   -876   -204
ATOM   2478  H   ARG B  95     -34.079  -1.320 -43.358  1.00 49.99           H  
ATOM   2479  HA  ARG B  95     -36.241  -3.169 -42.822  1.00 51.37           H  
ATOM   2480  HB3 ARG B  95     -37.430  -1.868 -44.589  1.00 53.19           H  
ATOM   2481  HB2 ARG B  95     -35.950  -1.054 -44.997  1.00 53.19           H  
ATOM   2482  HG3 ARG B  95     -35.890  -0.085 -42.624  1.00 57.81           H  
ATOM   2483  HG2 ARG B  95     -37.387  -0.931 -42.350  1.00 57.81           H  
ATOM   2484  HD3 ARG B  95     -38.631   0.390 -43.854  1.00 59.35           H  
ATOM   2485  HD2 ARG B  95     -37.235   1.063 -44.661  1.00 59.35           H  
ATOM   2486 HH22 ARG B  95     -38.406   4.772 -41.723  1.00 64.89           H  
ATOM   2487 HH21 ARG B  95     -37.469   3.539 -40.926  1.00 64.89           H  
ATOM   2488 HH12 ARG B  95     -38.978   4.499 -43.958  1.00 61.55           H  
ATOM   2489 HH11 ARG B  95     -38.591   3.034 -44.797  1.00 61.55           H  
ATOM   2490  HE  ARG B  95     -37.580   1.453 -41.728  1.00 61.79           H  
ATOM   2491  N   HIS B  96     -34.548  -3.572 -45.618  1.00 51.39           N  
ANISOU 2491  N   HIS B  96     7642   5764   6122   -415   -883     78
ATOM   2492  CA  HIS B  96     -34.365  -4.335 -46.846  1.00 52.14           C  
ANISOU 2492  CA  HIS B  96     7897   5712   6202   -500   -932     85
ATOM   2493  C   HIS B  96     -33.016  -5.056 -46.804  1.00 52.45           C  
ANISOU 2493  C   HIS B  96     8144   5490   6296   -485   -914     83
ATOM   2494  O   HIS B  96     -32.158  -4.720 -45.983  1.00 52.42           O  
ANISOU 2494  O   HIS B  96     8145   5421   6352   -377   -855     67
ATOM   2495  CB  HIS B  96     -34.450  -3.369 -48.051  1.00 53.53           C  
ANISOU 2495  CB  HIS B  96     8072   5878   6387   -357   -939     40
ATOM   2496  CG  HIS B  96     -35.690  -2.505 -48.064  1.00 56.43           C  
ANISOU 2496  CG  HIS B  96     8249   6509   6684   -296   -969     22
ATOM   2497  ND1 HIS B  96     -36.954  -2.964 -48.403  1.00 58.19           N  
ANISOU 2497  ND1 HIS B  96     8370   6934   6804   -436  -1036     37
ATOM   2498  CD2 HIS B  96     -35.859  -1.178 -47.744  1.00 57.80           C  
ANISOU 2498  CD2 HIS B  96     8324   6784   6853    -98   -947    -17
ATOM   2499  CE1 HIS B  96     -37.804  -1.947 -48.228  1.00 58.90           C  
ANISOU 2499  CE1 HIS B  96     8275   7274   6830   -293  -1051     -1
ATOM   2500  NE2 HIS B  96     -37.212  -0.844 -47.786  1.00 58.87           N  
ANISOU 2500  NE2 HIS B  96     8286   7200   6881    -74  -1004    -35
ATOM   2501  H   HIS B  96     -33.829  -2.891 -45.428  1.00 51.39           H  
ATOM   2502  HA  HIS B  96     -35.145  -5.091 -46.946  1.00 52.14           H  
ATOM   2503  HB3 HIS B  96     -34.390  -3.916 -48.994  1.00 53.53           H  
ATOM   2504  HB2 HIS B  96     -33.589  -2.698 -48.041  1.00 53.53           H  
ATOM   2505  HD1 HIS B  96     -37.205  -3.885 -48.732  1.00 58.19           H  
ATOM   2506  HD2 HIS B  96     -35.112  -0.461 -47.450  1.00 57.80           H  
ATOM   2507  HE1 HIS B  96     -38.864  -2.014 -48.422  1.00 58.90           H  
ATOM   2508  N   LEU B  97     -32.868  -6.030 -47.707  1.00 51.93           N  
ANISOU 2508  N   LEU B  97     8250   5290   6190   -579   -971     93
ATOM   2509  CA  LEU B  97     -31.582  -6.650 -48.024  1.00 51.72           C  
ANISOU 2509  CA  LEU B  97     8434   5033   6185   -512   -971     72
ATOM   2510  C   LEU B  97     -30.836  -5.763 -49.032  1.00 51.22           C  
ANISOU 2510  C   LEU B  97     8376   4912   6175   -341   -923     13
ATOM   2511  O   LEU B  97     -29.676  -5.436 -48.805  1.00 52.11           O  
ANISOU 2511  O   LEU B  97     8532   4945   6321   -217   -873    -26
ATOM   2512  CB  LEU B  97     -31.810  -8.073 -48.589  1.00 51.60           C  
ANISOU 2512  CB  LEU B  97     8636   4890   6077   -667  -1065     99
ATOM   2513  CG  LEU B  97     -32.504  -9.043 -47.604  1.00 53.14           C  
ANISOU 2513  CG  LEU B  97     8908   5099   6183   -881  -1124    162
ATOM   2514  CD1 LEU B  97     -33.008 -10.297 -48.338  1.00 54.06           C  
ANISOU 2514  CD1 LEU B  97     9274   5089   6177  -1073  -1232    193
ATOM   2515  CD2 LEU B  97     -31.584  -9.419 -46.429  1.00 53.56           C  
ANISOU 2515  CD2 LEU B  97     9056   5039   6257   -795  -1102    160
ATOM   2516  H   LEU B  97     -33.636  -6.268 -48.311  1.00 51.93           H  
ATOM   2517  HA  LEU B  97     -30.965  -6.719 -47.124  1.00 51.72           H  
ATOM   2518  HB3 LEU B  97     -30.852  -8.498 -48.897  1.00 51.60           H  
ATOM   2519  HB2 LEU B  97     -32.398  -8.009 -49.506  1.00 51.60           H  
ATOM   2520  HG  LEU B  97     -33.387  -8.557 -47.190  1.00 53.14           H  
ATOM   2521 HD11 LEU B  97     -33.420 -11.033 -47.648  1.00 54.06           H  
ATOM   2522 HD12 LEU B  97     -33.796 -10.045 -49.047  1.00 54.06           H  
ATOM   2523 HD13 LEU B  97     -32.206 -10.782 -48.897  1.00 54.06           H  
ATOM   2524 HD21 LEU B  97     -31.853 -10.380 -45.991  1.00 53.56           H  
ATOM   2525 HD22 LEU B  97     -30.540  -9.489 -46.740  1.00 53.56           H  
ATOM   2526 HD23 LEU B  97     -31.636  -8.674 -45.634  1.00 53.56           H  
ATOM   2527  N   GLY B  98     -31.543  -5.348 -50.096  1.00 50.32           N  
ANISOU 2527  N   GLY B  98     8210   4860   6048   -343   -941      4
ATOM   2528  CA  GLY B  98     -31.037  -4.434 -51.120  1.00 50.58           C  
ANISOU 2528  CA  GLY B  98     8269   4841   6108   -217   -905    -45
ATOM   2529  C   GLY B  98     -31.094  -2.974 -50.644  1.00 51.01           C  
ANISOU 2529  C   GLY B  98     8199   4992   6192   -114   -852    -61
ATOM   2530  O   GLY B  98     -31.383  -2.702 -49.476  1.00 50.61           O  
ANISOU 2530  O   GLY B  98     8034   5045   6152   -112   -836    -41
ATOM   2531  H   GLY B  98     -32.503  -5.623 -50.192  1.00 50.32           H  
ATOM   2532  HA3 GLY B  98     -31.632  -4.557 -52.023  1.00 50.58           H  
ATOM   2533  HA2 GLY B  98     -30.011  -4.686 -51.372  1.00 50.58           H  
ATOM   2534  N   CYS B  99     -30.828  -2.031 -51.554  1.00 51.69           N  
ANISOU 2534  N   CYS B  99     8330   5039   6271    -34   -835    -96
ATOM   2535  CA  CYS B  99     -30.875  -0.585 -51.297  1.00 53.35           C  
ANISOU 2535  CA  CYS B  99     8501   5296   6474     64   -807   -113
ATOM   2536  C   CYS B  99     -31.920   0.070 -52.203  1.00 56.59           C  
ANISOU 2536  C   CYS B  99     8913   5757   6829    113   -869   -121
ATOM   2537  O   CYS B  99     -32.125  -0.394 -53.322  1.00 57.21           O  
ANISOU 2537  O   CYS B  99     9053   5795   6887     72   -910   -124
ATOM   2538  CB  CYS B  99     -29.516   0.070 -51.594  1.00 52.70           C  
ANISOU 2538  CB  CYS B  99     8513   5121   6391     99   -739   -148
ATOM   2539  SG  CYS B  99     -28.113  -0.569 -50.650  1.00 51.17           S  
ANISOU 2539  SG  CYS B  99     8293   4915   6234     81   -670   -157
ATOM   2540  H   CYS B  99     -30.707  -2.302 -52.529  1.00 51.69           H  
ATOM   2541  HA  CYS B  99     -31.146  -0.387 -50.260  1.00 53.35           H  
ATOM   2542  HB3 CYS B  99     -29.583   1.141 -51.391  1.00 52.70           H  
ATOM   2543  HB2 CYS B  99     -29.280  -0.011 -52.657  1.00 52.70           H  
ATOM   2544  N   ILE B 100     -32.533   1.156 -51.729  1.00 58.26           N  
ANISOU 2544  N   ILE B 100     9083   6048   7004    226   -883   -132
ATOM   2545  CA  ILE B 100     -33.489   1.956 -52.485  1.00 60.82           C  
ANISOU 2545  CA  ILE B 100     9423   6433   7251    332   -955   -153
ATOM   2546  C   ILE B 100     -32.729   2.826 -53.510  1.00 63.86           C  
ANISOU 2546  C   ILE B 100    10017   6648   7600    375   -953   -179
ATOM   2547  O   ILE B 100     -31.823   3.564 -53.113  1.00 63.90           O  
ANISOU 2547  O   ILE B 100    10130   6555   7595    392   -904   -191
ATOM   2548  CB  ILE B 100     -34.339   2.871 -51.554  1.00 61.49           C  
ANISOU 2548  CB  ILE B 100     9405   6676   7280    482   -984   -169
ATOM   2549  CG1 ILE B 100     -34.993   2.093 -50.389  1.00 62.15           C  
ANISOU 2549  CG1 ILE B 100     9273   6957   7386    405   -973   -141
ATOM   2550  CG2 ILE B 100     -35.414   3.672 -52.312  1.00 62.55           C  
ANISOU 2550  CG2 ILE B 100     9552   6906   7309    639  -1077   -203
ATOM   2551  CD1 ILE B 100     -35.899   0.933 -50.833  1.00 63.39           C  
ANISOU 2551  CD1 ILE B 100     9312   7256   7517    263  -1022   -117
ATOM   2552  H   ILE B 100     -32.209   1.555 -50.848  1.00 58.26           H  
ATOM   2553  HA  ILE B 100     -34.158   1.273 -53.007  1.00 60.82           H  
ATOM   2554  HB  ILE B 100     -33.673   3.606 -51.106  1.00 61.49           H  
ATOM   2555 HG13 ILE B 100     -35.568   2.783 -49.770  1.00 62.15           H  
ATOM   2556 HG12 ILE B 100     -34.217   1.699 -49.734  1.00 62.15           H  
ATOM   2557 HG21 ILE B 100     -36.056   4.226 -51.626  1.00 62.55           H  
ATOM   2558 HG22 ILE B 100     -34.979   4.403 -52.994  1.00 62.55           H  
ATOM   2559 HG23 ILE B 100     -36.048   3.012 -52.902  1.00 62.55           H  
ATOM   2560 HD11 ILE B 100     -36.419   0.498 -49.982  1.00 63.39           H  
ATOM   2561 HD12 ILE B 100     -36.663   1.253 -51.543  1.00 63.39           H  
ATOM   2562 HD13 ILE B 100     -35.317   0.142 -51.303  1.00 63.39           H  
ATOM   2563  N   ASN B 101     -33.096   2.690 -54.787  1.00 66.18           N  
ANISOU 2563  N   ASN B 101    10374   6914   7856    370  -1006   -188
ATOM   2564  CA  ASN B 101     -32.558   3.457 -55.912  1.00 68.65           C  
ANISOU 2564  CA  ASN B 101    10899   7071   8115    386  -1010   -210
ATOM   2565  C   ASN B 101     -33.333   4.778 -56.119  1.00 70.45           C  
ANISOU 2565  C   ASN B 101    11240   7294   8232    563  -1089   -235
ATOM   2566  O   ASN B 101     -34.305   5.033 -55.406  1.00 70.37           O  
ANISOU 2566  O   ASN B 101    11121   7427   8189    700  -1134   -245
ATOM   2567  CB  ASN B 101     -32.502   2.558 -57.183  1.00 70.93           C  
ANISOU 2567  CB  ASN B 101    11229   7305   8415    286  -1023   -208
ATOM   2568  CG  ASN B 101     -33.823   2.249 -57.912  1.00 75.43           C  
ANISOU 2568  CG  ASN B 101    11729   7980   8952    312  -1114   -204
ATOM   2569  OD1 ASN B 101     -34.900   2.683 -57.521  1.00 76.85           O  
ANISOU 2569  OD1 ASN B 101    11835   8292   9072    438  -1180   -214
ATOM   2570  ND2 ASN B 101     -33.745   1.508 -59.009  1.00 75.84           N  
ANISOU 2570  ND2 ASN B 101    11798   7995   9024    201  -1123   -196
ATOM   2571  H   ASN B 101     -33.871   2.069 -55.019  1.00 66.18           H  
ATOM   2572  HA  ASN B 101     -31.535   3.769 -55.693  1.00 68.65           H  
ATOM   2573  HB3 ASN B 101     -32.012   1.616 -56.938  1.00 70.93           H  
ATOM   2574  HB2 ASN B 101     -31.854   3.043 -57.914  1.00 70.93           H  
ATOM   2575 HD22 ASN B 101     -34.548   1.473 -59.629  1.00 75.84           H  
ATOM   2576 HD21 ASN B 101     -32.867   1.128 -59.328  1.00 75.84           H  
ATOM   2577  N   ALA B 102     -32.915   5.580 -57.113  1.00 72.04           N  
ANISOU 2577  N   ALA B 102    11677   7339   8354    569  -1111   -251
ATOM   2578  CA  ALA B 102     -33.539   6.851 -57.508  1.00 74.33           C  
ANISOU 2578  CA  ALA B 102    12166   7566   8508    745  -1204   -278
ATOM   2579  C   ALA B 102     -35.044   6.760 -57.814  1.00 76.41           C  
ANISOU 2579  C   ALA B 102    12300   8008   8724    924  -1311   -299
ATOM   2580  O   ALA B 102     -35.791   7.673 -57.464  1.00 76.58           O  
ANISOU 2580  O   ALA B 102    12361   8093   8643   1147  -1388   -332
ATOM   2581  CB  ALA B 102     -32.796   7.411 -58.733  1.00 74.39           C  
ANISOU 2581  CB  ALA B 102    12449   7379   8435    660  -1213   -283
ATOM   2582  H   ALA B 102     -32.119   5.304 -57.665  1.00 72.04           H  
ATOM   2583  HA  ALA B 102     -33.421   7.549 -56.679  1.00 74.33           H  
ATOM   2584  HB1 ALA B 102     -33.206   8.377 -59.036  1.00 74.39           H  
ATOM   2585  HB2 ALA B 102     -31.735   7.556 -58.527  1.00 74.39           H  
ATOM   2586  HB3 ALA B 102     -32.886   6.745 -59.596  1.00 74.39           H  
ATOM   2587  N   ASP B 103     -35.449   5.637 -58.414  1.00 77.66           N  
ANISOU 2587  N   ASP B 103    12298   8271   8939    827  -1317   -285
ATOM   2588  CA  ASP B 103     -36.832   5.315 -58.795  1.00 79.06           C  
ANISOU 2588  CA  ASP B 103    12315   8667   9055    942  -1413   -303
ATOM   2589  C   ASP B 103     -37.703   4.914 -57.586  1.00 78.92           C  
ANISOU 2589  C   ASP B 103    12001   8935   9048    979  -1415   -304
ATOM   2590  O   ASP B 103     -38.906   4.700 -57.737  1.00 79.90           O  
ANISOU 2590  O   ASP B 103    11944   9310   9103   1038  -1487   -323
ATOM   2591  CB  ASP B 103     -36.925   4.195 -59.868  1.00 82.24           C  
ANISOU 2591  CB  ASP B 103    12683   9070   9495    781  -1422   -284
ATOM   2592  CG  ASP B 103     -35.929   4.274 -61.028  1.00 88.48           C  
ANISOU 2592  CG  ASP B 103    13735   9609  10274    714  -1407   -284
ATOM   2593  OD1 ASP B 103     -35.637   5.396 -61.493  1.00 89.21           O  
ANISOU 2593  OD1 ASP B 103    14062   9547  10286    811  -1425   -302
ATOM   2594  OD2 ASP B 103     -35.526   3.185 -61.494  1.00 91.12           O1-
ANISOU 2594  OD2 ASP B 103    14059   9902  10660    554  -1384   -267
ATOM   2595  H   ASP B 103     -34.761   4.968 -58.725  1.00 77.66           H  
ATOM   2596  HA  ASP B 103     -37.271   6.220 -59.217  1.00 79.06           H  
ATOM   2597  HB3 ASP B 103     -37.918   4.214 -60.317  1.00 82.24           H  
ATOM   2598  HB2 ASP B 103     -36.808   3.219 -59.393  1.00 82.24           H  
ATOM   2599  N   GLY B 104     -37.084   4.770 -56.405  1.00 77.25           N  
ANISOU 2599  N   GLY B 104    11728   8713   8909    922  -1335   -285
ATOM   2600  CA  GLY B 104     -37.735   4.360 -55.166  1.00 76.03           C  
ANISOU 2600  CA  GLY B 104    11301   8826   8760    922  -1327   -281
ATOM   2601  C   GLY B 104     -37.903   2.836 -55.093  1.00 74.58           C  
ANISOU 2601  C   GLY B 104    10940   8752   8647    668  -1296   -236
ATOM   2602  O   GLY B 104     -38.645   2.350 -54.240  1.00 75.04           O  
ANISOU 2602  O   GLY B 104    10765   9072   8674    620  -1305   -228
ATOM   2603  H   GLY B 104     -36.082   4.924 -56.377  1.00 77.25           H  
ATOM   2604  HA3 GLY B 104     -38.715   4.832 -55.077  1.00 76.03           H  
ATOM   2605  HA2 GLY B 104     -37.135   4.698 -54.323  1.00 76.03           H  
ATOM   2606  N   ASN B 105     -37.266   2.079 -55.992  1.00 72.81           N  
ANISOU 2606  N   ASN B 105    10841   8331   8493    498  -1266   -207
ATOM   2607  CA  ASN B 105     -37.318   0.619 -56.059  1.00 71.95           C  
ANISOU 2607  CA  ASN B 105    10649   8260   8429    261  -1253   -165
ATOM   2608  C   ASN B 105     -36.115   0.057 -55.300  1.00 69.83           C  
ANISOU 2608  C   ASN B 105    10442   7825   8265    144  -1165   -135
ATOM   2609  O   ASN B 105     -35.089   0.725 -55.178  1.00 68.83           O  
ANISOU 2609  O   ASN B 105    10440   7530   8184    213  -1107   -148
ATOM   2610  CB  ASN B 105     -37.291   0.165 -57.538  1.00 73.62           C  
ANISOU 2610  CB  ASN B 105    10980   8363   8629    176  -1292   -162
ATOM   2611  CG  ASN B 105     -38.570   0.434 -58.342  1.00 77.19           C  
ANISOU 2611  CG  ASN B 105    11389   8965   8974    285  -1386   -193
ATOM   2612  OD1 ASN B 105     -38.765  -0.155 -59.396  1.00 78.79           O  
ANISOU 2612  OD1 ASN B 105    11752   9025   9162    324  -1413   -208
ATOM   2613  ND2 ASN B 105     -39.466   1.298 -57.877  1.00 77.31           N  
ANISOU 2613  ND2 ASN B 105    11178   9298   8898    338  -1439   -207
ATOM   2614  H   ASN B 105     -36.572   2.513 -56.602  1.00 72.81           H  
ATOM   2615  HA  ASN B 105     -38.242   0.266 -55.596  1.00 71.95           H  
ATOM   2616  HB3 ASN B 105     -37.126  -0.912 -57.584  1.00 73.62           H  
ATOM   2617  HB2 ASN B 105     -36.446   0.614 -58.060  1.00 73.62           H  
ATOM   2618 HD22 ASN B 105     -40.251   1.535 -58.461  1.00 77.31           H  
ATOM   2619 HD21 ASN B 105     -39.268   1.866 -57.062  1.00 77.31           H  
ATOM   2620  N   VAL B 106     -36.254  -1.174 -54.796  1.00 68.86           N  
ANISOU 2620  N   VAL B 106    10256   7750   8158    -44  -1163    -96
ATOM   2621  CA  VAL B 106     -35.153  -1.882 -54.152  1.00 68.34           C  
ANISOU 2621  CA  VAL B 106    10270   7526   8170   -129  -1099    -74
ATOM   2622  C   VAL B 106     -34.252  -2.466 -55.254  1.00 67.92           C  
ANISOU 2622  C   VAL B 106    10411   7250   8146   -165  -1087    -84
ATOM   2623  O   VAL B 106     -34.698  -3.362 -55.973  1.00 69.32           O  
ANISOU 2623  O   VAL B 106    10648   7405   8287   -267  -1142    -74
ATOM   2624  CB  VAL B 106     -35.664  -3.046 -53.247  1.00 69.15           C  
ANISOU 2624  CB  VAL B 106    10284   7737   8251   -309  -1114    -29
ATOM   2625  CG1 VAL B 106     -34.533  -3.866 -52.589  1.00 69.82           C  
ANISOU 2625  CG1 VAL B 106    10497   7631   8401   -359  -1065    -14
ATOM   2626  CG2 VAL B 106     -36.623  -2.550 -52.149  1.00 69.54           C  
ANISOU 2626  CG2 VAL B 106    10117   8044   8259   -270  -1113    -28
ATOM   2627  H   VAL B 106     -37.068  -1.720 -55.023  1.00 68.86           H  
ATOM   2628  HA  VAL B 106     -34.576  -1.187 -53.540  1.00 68.34           H  
ATOM   2629  HB  VAL B 106     -36.232  -3.733 -53.880  1.00 69.15           H  
ATOM   2630 HG11 VAL B 106     -34.938  -4.609 -51.903  1.00 69.82           H  
ATOM   2631 HG12 VAL B 106     -33.931  -4.404 -53.323  1.00 69.82           H  
ATOM   2632 HG13 VAL B 106     -33.862  -3.221 -52.020  1.00 69.82           H  
ATOM   2633 HG21 VAL B 106     -37.063  -3.387 -51.607  1.00 69.54           H  
ATOM   2634 HG22 VAL B 106     -36.100  -1.933 -51.421  1.00 69.54           H  
ATOM   2635 HG23 VAL B 106     -37.446  -1.960 -52.555  1.00 69.54           H  
ATOM   2636  N   ASP B 107     -33.018  -1.963 -55.355  1.00 66.50           N  
ANISOU 2636  N   ASP B 107    10323   6929   8015    -87  -1018   -109
ATOM   2637  CA  ASP B 107     -31.959  -2.577 -56.147  1.00 66.20           C  
ANISOU 2637  CA  ASP B 107    10438   6729   7987    -99   -994   -133
ATOM   2638  C   ASP B 107     -31.344  -3.694 -55.291  1.00 65.20           C  
ANISOU 2638  C   ASP B 107    10346   6544   7883   -157   -978   -121
ATOM   2639  O   ASP B 107     -30.969  -3.445 -54.140  1.00 64.90           O  
ANISOU 2639  O   ASP B 107    10259   6519   7880   -117   -923   -123
ATOM   2640  CB  ASP B 107     -30.870  -1.581 -56.602  1.00 68.07           C  
ANISOU 2640  CB  ASP B 107    10733   6904   8226     -8   -926   -171
ATOM   2641  CG  ASP B 107     -29.755  -2.193 -57.464  1.00 72.18           C  
ANISOU 2641  CG  ASP B 107    11372   7324   8731    -15   -887   -210
ATOM   2642  OD1 ASP B 107     -29.957  -3.278 -58.059  1.00 72.04           O  
ANISOU 2642  OD1 ASP B 107    11414   7254   8705    -54   -919   -213
ATOM   2643  OD2 ASP B 107     -28.712  -1.526 -57.587  1.00 74.29           O1-
ANISOU 2643  OD2 ASP B 107    11678   7576   8972     11   -828   -240
ATOM   2644  H   ASP B 107     -32.710  -1.251 -54.691  1.00 66.50           H  
ATOM   2645  HA  ASP B 107     -32.408  -3.012 -57.043  1.00 66.20           H  
ATOM   2646  HB3 ASP B 107     -30.420  -1.104 -55.729  1.00 68.07           H  
ATOM   2647  HB2 ASP B 107     -31.334  -0.778 -57.174  1.00 68.07           H  
ATOM   2648  N   TYR B 108     -31.277  -4.897 -55.861  1.00 64.24           N  
ANISOU 2648  N   TYR B 108    10335   6347   7725   -245  -1035   -111
ATOM   2649  CA  TYR B 108     -30.788  -6.096 -55.195  1.00 64.54           C  
ANISOU 2649  CA  TYR B 108    10472   6295   7753   -278  -1046   -103
ATOM   2650  C   TYR B 108     -29.297  -6.350 -55.457  1.00 63.52           C  
ANISOU 2650  C   TYR B 108    10442   6067   7625   -147   -996   -163
ATOM   2651  O   TYR B 108     -28.736  -7.209 -54.779  1.00 64.18           O  
ANISOU 2651  O   TYR B 108    10609   6087   7691   -114  -1005   -171
ATOM   2652  CB  TYR B 108     -31.679  -7.293 -55.590  1.00 66.08           C  
ANISOU 2652  CB  TYR B 108    10797   6436   7876   -436  -1144    -67
ATOM   2653  CG  TYR B 108     -31.578  -7.792 -57.028  1.00 68.84           C  
ANISOU 2653  CG  TYR B 108    11311   6670   8177   -437  -1191    -95
ATOM   2654  CD1 TYR B 108     -32.444  -7.294 -58.025  1.00 70.19           C  
ANISOU 2654  CD1 TYR B 108    11429   6908   8333   -478  -1218    -91
ATOM   2655  CD2 TYR B 108     -30.620  -8.772 -57.365  1.00 70.56           C  
ANISOU 2655  CD2 TYR B 108    11752   6715   8342   -390  -1223   -125
ATOM   2656  CE1 TYR B 108     -32.351  -7.773 -59.347  1.00 71.61           C  
ANISOU 2656  CE1 TYR B 108    11763   6982   8464   -488  -1262   -115
ATOM   2657  CE2 TYR B 108     -30.516  -9.240 -58.688  1.00 71.78           C  
ANISOU 2657  CE2 TYR B 108    12067   6765   8440   -381  -1269   -155
ATOM   2658  CZ  TYR B 108     -31.381  -8.739 -59.681  1.00 73.39           C  
ANISOU 2658  CZ  TYR B 108    12207   7034   8645   -445  -1285   -146
ATOM   2659  OH  TYR B 108     -31.268  -9.171 -60.968  1.00 76.17           O  
ANISOU 2659  OH  TYR B 108    12727   7279   8936   -445  -1334   -174
ATOM   2660  H   TYR B 108     -31.415  -4.939 -56.864  1.00 64.24           H  
ATOM   2661  HA  TYR B 108     -30.876  -5.970 -54.114  1.00 64.54           H  
ATOM   2662  HB3 TYR B 108     -32.719  -7.051 -55.374  1.00 66.08           H  
ATOM   2663  HB2 TYR B 108     -31.432  -8.131 -54.937  1.00 66.08           H  
ATOM   2664  HD1 TYR B 108     -33.187  -6.546 -57.784  1.00 70.19           H  
ATOM   2665  HD2 TYR B 108     -29.951  -9.158 -56.610  1.00 70.56           H  
ATOM   2666  HE1 TYR B 108     -33.010  -7.383 -60.112  1.00 71.61           H  
ATOM   2667  HE2 TYR B 108     -29.766  -9.977 -58.933  1.00 71.78           H  
ATOM   2668  HH  TYR B 108     -30.348  -9.329 -61.202  1.00 76.17           H  
ATOM   2669  N   HIS B 109     -28.670  -5.625 -56.398  1.00 62.69           N  
ANISOU 2669  N   HIS B 109    10328   5971   7519    -70   -947   -210
ATOM   2670  CA  HIS B 109     -27.232  -5.748 -56.656  1.00 62.62           C  
ANISOU 2670  CA  HIS B 109    10365   5947   7481     43   -891   -277
ATOM   2671  C   HIS B 109     -26.387  -5.066 -55.570  1.00 62.20           C  
ANISOU 2671  C   HIS B 109    10192   5983   7456     99   -810   -292
ATOM   2672  O   HIS B 109     -25.222  -5.419 -55.407  1.00 63.09           O  
ANISOU 2672  O   HIS B 109    10312   6130   7530    192   -769   -348
ATOM   2673  CB  HIS B 109     -26.880  -5.198 -58.047  1.00 63.76           C  
ANISOU 2673  CB  HIS B 109    10542   6098   7585     60   -866   -320
ATOM   2674  CG  HIS B 109     -27.656  -5.821 -59.181  1.00 66.77           C  
ANISOU 2674  CG  HIS B 109    11046   6392   7934     11   -944   -312
ATOM   2675  ND1 HIS B 109     -28.748  -5.197 -59.746  1.00 68.72           N  
ANISOU 2675  ND1 HIS B 109    11448   6536   8128     35  -1006   -330
ATOM   2676  CD2 HIS B 109     -27.515  -7.007 -59.868  1.00 67.66           C  
ANISOU 2676  CD2 HIS B 109    11162   6501   8043    -53   -978   -289
ATOM   2677  CE1 HIS B 109     -29.219  -5.997 -60.705  1.00 68.82           C  
ANISOU 2677  CE1 HIS B 109    11546   6490   8113    -39  -1069   -314
ATOM   2678  NE2 HIS B 109     -28.515  -7.118 -60.838  1.00 68.60           N  
ANISOU 2678  NE2 HIS B 109    11417   6531   8118    -91  -1053   -290
ATOM   2679  H   HIS B 109     -29.162  -4.920 -56.946  1.00 62.69           H  
ATOM   2680  HA  HIS B 109     -26.967  -6.807 -56.648  1.00 62.62           H  
ATOM   2681  HB3 HIS B 109     -25.814  -5.333 -58.238  1.00 63.76           H  
ATOM   2682  HB2 HIS B 109     -27.053  -4.120 -58.066  1.00 63.76           H  
ATOM   2683  HD1 HIS B 109     -29.163  -4.324 -59.393  1.00 68.72           H  
ATOM   2684  HD2 HIS B 109     -26.785  -7.788 -59.739  1.00 67.66           H  
ATOM   2685  HE1 HIS B 109     -30.092  -5.763 -61.297  1.00 68.82           H  
ATOM   2686  N   MET B 110     -26.991  -4.124 -54.842  1.00 60.31           N  
ANISOU 2686  N   MET B 110     9841   5803   7271     54   -791   -246
ATOM   2687  CA  MET B 110     -26.408  -3.473 -53.676  1.00 58.99           C  
ANISOU 2687  CA  MET B 110     9571   5712   7129     88   -722   -251
ATOM   2688  C   MET B 110     -26.928  -4.135 -52.392  1.00 56.63           C  
ANISOU 2688  C   MET B 110     9227   5417   6872     62   -751   -203
ATOM   2689  O   MET B 110     -27.874  -4.922 -52.445  1.00 56.92           O  
ANISOU 2689  O   MET B 110     9286   5432   6911    -17   -819   -158
ATOM   2690  CB  MET B 110     -26.773  -1.985 -53.729  1.00 60.74           C  
ANISOU 2690  CB  MET B 110     9741   5980   7356     67   -687   -242
ATOM   2691  CG  MET B 110     -26.225  -1.265 -54.974  1.00 65.88           C  
ANISOU 2691  CG  MET B 110    10468   6619   7944     55   -664   -282
ATOM   2692  SD  MET B 110     -24.410  -1.199 -55.077  1.00 77.84           S  
ANISOU 2692  SD  MET B 110    11964   8227   9386     74   -575   -354
ATOM   2693  CE  MET B 110     -24.091  -0.001 -53.761  1.00 76.15           C  
ANISOU 2693  CE  MET B 110    11672   8083   9179     40   -515   -338
ATOM   2694  H   MET B 110     -27.963  -3.928 -55.034  1.00 60.31           H  
ATOM   2695  HA  MET B 110     -25.324  -3.574 -53.691  1.00 58.99           H  
ATOM   2696  HB3 MET B 110     -26.376  -1.505 -52.837  1.00 60.74           H  
ATOM   2697  HB2 MET B 110     -27.856  -1.864 -53.683  1.00 60.74           H  
ATOM   2698  HG3 MET B 110     -26.617  -0.249 -55.016  1.00 65.88           H  
ATOM   2699  HG2 MET B 110     -26.590  -1.749 -55.878  1.00 65.88           H  
ATOM   2700  HE1 MET B 110     -23.045   0.301 -53.761  1.00 76.15           H  
ATOM   2701  HE2 MET B 110     -24.711   0.882 -53.916  1.00 76.15           H  
ATOM   2702  HE3 MET B 110     -24.330  -0.425 -52.787  1.00 76.15           H  
ATOM   2703  N   ASN B 111     -26.295  -3.855 -51.246  1.00 54.63           N  
ANISOU 2703  N   ASN B 111     8909   5212   6635    106   -701   -212
ATOM   2704  CA  ASN B 111     -26.674  -4.431 -49.951  1.00 53.82           C  
ANISOU 2704  CA  ASN B 111     8772   5115   6562     72   -725   -165
ATOM   2705  C   ASN B 111     -26.809  -3.322 -48.907  1.00 52.41           C  
ANISOU 2705  C   ASN B 111     8457   5031   6426     68   -673   -144
ATOM   2706  O   ASN B 111     -25.869  -2.548 -48.728  1.00 52.42           O  
ANISOU 2706  O   ASN B 111     8415   5077   6424    117   -605   -178
ATOM   2707  CB  ASN B 111     -25.606  -5.431 -49.454  1.00 54.59           C  
ANISOU 2707  CB  ASN B 111     8947   5166   6628    149   -735   -192
ATOM   2708  CG  ASN B 111     -25.456  -6.753 -50.208  1.00 59.05           C  
ANISOU 2708  CG  ASN B 111     9702   5610   7125    186   -810   -216
ATOM   2709  OD1 ASN B 111     -24.544  -7.510 -49.894  1.00 58.28           O  
ANISOU 2709  OD1 ASN B 111     9686   5450   7009    115   -862   -200
ATOM   2710  ND2 ASN B 111     -26.301  -7.068 -51.185  1.00 61.84           N  
ANISOU 2710  ND2 ASN B 111    10144   5928   7424    312   -826   -260
ATOM   2711  H   ASN B 111     -25.500  -3.219 -51.240  1.00 54.63           H  
ATOM   2712  HA  ASN B 111     -27.622  -4.955 -50.038  1.00 53.82           H  
ATOM   2713  HB3 ASN B 111     -25.828  -5.708 -48.422  1.00 54.59           H  
ATOM   2714  HB2 ASN B 111     -24.632  -4.944 -49.426  1.00 54.59           H  
ATOM   2715 HD22 ASN B 111     -26.164  -7.913 -51.710  1.00 61.84           H  
ATOM   2716 HD21 ASN B 111     -27.011  -6.412 -51.517  1.00 61.84           H  
ATOM   2717  N   SER B 112     -27.923  -3.329 -48.173  1.00 51.72           N  
ANISOU 2717  N   SER B 112     8305   4990   6358      2   -705    -92
ATOM   2718  CA  SER B 112     -28.074  -2.629 -46.904  1.00 51.60           C  
ANISOU 2718  CA  SER B 112     8169   5066   6373     20   -661    -77
ATOM   2719  C   SER B 112     -27.376  -3.449 -45.808  1.00 51.33           C  
ANISOU 2719  C   SER B 112     8144   5012   6348     28   -646    -71
ATOM   2720  O   SER B 112     -27.802  -4.579 -45.564  1.00 51.28           O  
ANISOU 2720  O   SER B 112     8220   4949   6317    -31   -704    -45
ATOM   2721  CB  SER B 112     -29.574  -2.519 -46.555  1.00 51.69           C  
ANISOU 2721  CB  SER B 112     8081   5185   6375    -41   -702    -34
ATOM   2722  OG  SER B 112     -30.235  -1.516 -47.297  1.00 50.99           O  
ANISOU 2722  OG  SER B 112     7963   5147   6264      5   -718    -49
ATOM   2723  H   SER B 112     -28.625  -4.040 -48.368  1.00 51.72           H  
ATOM   2724  HA  SER B 112     -27.630  -1.633 -46.956  1.00 51.60           H  
ATOM   2725  HB3 SER B 112     -29.698  -2.272 -45.499  1.00 51.69           H  
ATOM   2726  HB2 SER B 112     -30.080  -3.473 -46.714  1.00 51.69           H  
ATOM   2727  HG  SER B 112     -30.540  -1.923 -48.131  1.00 50.99           H  
ATOM   2728  N   VAL B 113     -26.344  -2.899 -45.161  1.00 50.22           N  
ANISOU 2728  N   VAL B 113     7952   4907   6222     92   -580    -97
ATOM   2729  CA  VAL B 113     -25.660  -3.563 -44.051  1.00 51.17           C  
ANISOU 2729  CA  VAL B 113     8076   5024   6343    122   -571    -97
ATOM   2730  C   VAL B 113     -25.745  -2.666 -42.795  1.00 50.84           C  
ANISOU 2730  C   VAL B 113     7917   5067   6332    118   -522    -78
ATOM   2731  O   VAL B 113     -25.643  -1.441 -42.930  1.00 50.18           O  
ANISOU 2731  O   VAL B 113     7783   5030   6252    137   -474    -95
ATOM   2732  CB  VAL B 113     -24.174  -3.846 -44.402  1.00 51.59           C  
ANISOU 2732  CB  VAL B 113     8178   5068   6354    226   -547   -162
ATOM   2733  CG1 VAL B 113     -24.066  -4.930 -45.492  1.00 51.99           C  
ANISOU 2733  CG1 VAL B 113     8370   5025   6359    256   -608   -185
ATOM   2734  CG2 VAL B 113     -23.344  -2.600 -44.767  1.00 51.02           C  
ANISOU 2734  CG2 VAL B 113     8029   5090   6267    242   -467   -207
ATOM   2735  H   VAL B 113     -26.019  -1.962 -45.398  1.00 50.22           H  
ATOM   2736  HA  VAL B 113     -26.134  -4.522 -43.856  1.00 51.17           H  
ATOM   2737  HB  VAL B 113     -23.710  -4.277 -43.511  1.00 51.59           H  
ATOM   2738 HG11 VAL B 113     -23.028  -5.194 -45.693  1.00 51.99           H  
ATOM   2739 HG12 VAL B 113     -24.574  -5.846 -45.185  1.00 51.99           H  
ATOM   2740 HG13 VAL B 113     -24.521  -4.603 -46.428  1.00 51.99           H  
ATOM   2741 HG21 VAL B 113     -22.347  -2.877 -45.099  1.00 51.02           H  
ATOM   2742 HG22 VAL B 113     -23.802  -2.037 -45.577  1.00 51.02           H  
ATOM   2743 HG23 VAL B 113     -23.213  -1.932 -43.916  1.00 51.02           H  
ATOM   2744  N   PRO B 114     -25.997  -3.269 -41.609  1.00 51.14           N  
ANISOU 2744  N   PRO B 114     7939   5114   6378     89   -539    -42
ATOM   2745  CA  PRO B 114     -25.990  -2.522 -40.346  1.00 51.43           C  
ANISOU 2745  CA  PRO B 114     7866   5236   6440     93   -491    -28
ATOM   2746  C   PRO B 114     -24.555  -2.129 -39.969  1.00 52.39           C  
ANISOU 2746  C   PRO B 114     7967   5382   6557    169   -430    -73
ATOM   2747  O   PRO B 114     -23.664  -2.977 -39.985  1.00 53.41           O  
ANISOU 2747  O   PRO B 114     8152   5487   6656    229   -438   -108
ATOM   2748  CB  PRO B 114     -26.627  -3.492 -39.340  1.00 51.97           C  
ANISOU 2748  CB  PRO B 114     7943   5305   6499     18   -535     24
ATOM   2749  CG  PRO B 114     -26.275  -4.875 -39.864  1.00 52.36           C  
ANISOU 2749  CG  PRO B 114     8162   5228   6505     14   -601     21
ATOM   2750  CD  PRO B 114     -26.255  -4.695 -41.379  1.00 50.50           C  
ANISOU 2750  CD  PRO B 114     7976   4949   6262     42   -612    -12
ATOM   2751  HA  PRO B 114     -26.607  -1.628 -40.430  1.00 51.43           H  
ATOM   2752  HB3 PRO B 114     -27.709  -3.348 -39.343  1.00 51.97           H  
ATOM   2753  HB2 PRO B 114     -26.285  -3.341 -38.316  1.00 51.97           H  
ATOM   2754  HG3 PRO B 114     -26.954  -5.657 -39.524  1.00 52.36           H  
ATOM   2755  HG2 PRO B 114     -25.270  -5.134 -39.526  1.00 52.36           H  
ATOM   2756  HD2 PRO B 114     -25.493  -5.333 -41.827  1.00 50.50           H  
ATOM   2757  HD3 PRO B 114     -27.222  -4.957 -41.811  1.00 50.50           H  
ATOM   2758  N   ILE B 115     -24.359  -0.847 -39.646  1.00 51.09           N  
ANISOU 2758  N   ILE B 115     7731   5281   6398    172   -375    -80
ATOM   2759  CA  ILE B 115     -23.127  -0.362 -39.045  1.00 51.71           C  
ANISOU 2759  CA  ILE B 115     7778   5419   6452    199   -315   -118
ATOM   2760  C   ILE B 115     -23.195  -0.765 -37.567  1.00 53.16           C  
ANISOU 2760  C   ILE B 115     7908   5632   6658    210   -313    -91
ATOM   2761  O   ILE B 115     -24.181  -0.448 -36.893  1.00 52.74           O  
ANISOU 2761  O   ILE B 115     7810   5598   6630    180   -311    -54
ATOM   2762  CB  ILE B 115     -22.980   1.184 -39.135  1.00 52.42           C  
ANISOU 2762  CB  ILE B 115     7871   5536   6509    164   -269   -134
ATOM   2763  CG1 ILE B 115     -23.022   1.653 -40.605  1.00 53.08           C  
ANISOU 2763  CG1 ILE B 115     8038   5571   6559    143   -283   -154
ATOM   2764  CG2 ILE B 115     -21.698   1.705 -38.432  1.00 52.88           C  
ANISOU 2764  CG2 ILE B 115     7890   5686   6516    143   -208   -171
ATOM   2765  CD1 ILE B 115     -23.077   3.179 -40.731  1.00 53.85           C  
ANISOU 2765  CD1 ILE B 115     8211   5651   6598    100   -263   -164
ATOM   2766  H   ILE B 115     -25.170  -0.245 -39.516  1.00 51.09           H  
ATOM   2767  HA  ILE B 115     -22.270  -0.836 -39.530  1.00 51.71           H  
ATOM   2768  HB  ILE B 115     -23.836   1.627 -38.625  1.00 52.42           H  
ATOM   2769 HG13 ILE B 115     -23.892   1.239 -41.117  1.00 53.08           H  
ATOM   2770 HG12 ILE B 115     -22.151   1.267 -41.133  1.00 53.08           H  
ATOM   2771 HG21 ILE B 115     -21.644   2.793 -38.416  1.00 52.88           H  
ATOM   2772 HG22 ILE B 115     -21.638   1.405 -37.385  1.00 52.88           H  
ATOM   2773 HG23 ILE B 115     -20.796   1.332 -38.922  1.00 52.88           H  
ATOM   2774 HD11 ILE B 115     -23.226   3.510 -41.754  1.00 53.85           H  
ATOM   2775 HD12 ILE B 115     -23.885   3.581 -40.126  1.00 53.85           H  
ATOM   2776 HD13 ILE B 115     -22.149   3.627 -40.397  1.00 53.85           H  
ATOM   2777  N   GLN B 116     -22.170  -1.489 -37.129  1.00 54.38           N  
ANISOU 2777  N   GLN B 116     8076   5795   6790    268   -323   -113
ATOM   2778  CA  GLN B 116     -22.079  -2.015 -35.779  1.00 55.77           C  
ANISOU 2778  CA  GLN B 116     8226   5990   6975    285   -328    -90
ATOM   2779  C   GLN B 116     -20.970  -1.238 -35.073  1.00 56.27           C  
ANISOU 2779  C   GLN B 116     8198   6169   7012    310   -262   -126
ATOM   2780  O   GLN B 116     -19.922  -1.000 -35.673  1.00 57.26           O  
ANISOU 2780  O   GLN B 116     8295   6382   7079    348   -232   -187
ATOM   2781  CB  GLN B 116     -21.811  -3.529 -35.825  1.00 58.32           C  
ANISOU 2781  CB  GLN B 116     8663   6234   7262    353   -401    -91
ATOM   2782  CG  GLN B 116     -22.831  -4.268 -36.722  1.00 65.23           C  
ANISOU 2782  CG  GLN B 116     9660   6992   8133    300   -471    -61
ATOM   2783  CD  GLN B 116     -23.298  -5.585 -36.122  1.00 75.07           C  
ANISOU 2783  CD  GLN B 116    11017   8148   9359    221   -545      2
ATOM   2784  OE1 GLN B 116     -22.513  -6.495 -35.898  1.00 78.02           O  
ANISOU 2784  OE1 GLN B 116    11439   8501   9703    257   -567     11
ATOM   2785  NE2 GLN B 116     -24.586  -5.709 -35.849  1.00 76.95           N  
ANISOU 2785  NE2 GLN B 116    11306   8339   9592     95   -590     47
ATOM   2786  H   GLN B 116     -21.356  -1.633 -37.705  1.00 54.38           H  
ATOM   2787  HA  GLN B 116     -23.014  -1.865 -35.244  1.00 55.77           H  
ATOM   2788  HB3 GLN B 116     -21.865  -3.904 -34.801  1.00 58.32           H  
ATOM   2789  HB2 GLN B 116     -20.793  -3.742 -36.157  1.00 58.32           H  
ATOM   2790  HG3 GLN B 116     -22.396  -4.458 -37.705  1.00 65.23           H  
ATOM   2791  HG2 GLN B 116     -23.715  -3.654 -36.902  1.00 65.23           H  
ATOM   2792 HE22 GLN B 116     -24.901  -6.563 -35.424  1.00 76.95           H  
ATOM   2793 HE21 GLN B 116     -25.224  -4.917 -35.897  1.00 76.95           H  
ATOM   2794  N   GLN B 117     -21.241  -0.828 -33.834  1.00 54.97           N  
ANISOU 2794  N   GLN B 117     7979   6032   6874    271   -237    -93
ATOM   2795  CA  GLN B 117     -20.318  -0.076 -32.997  1.00 54.21           C  
ANISOU 2795  CA  GLN B 117     7809   6042   6748    269   -181   -119
ATOM   2796  C   GLN B 117     -20.088  -0.882 -31.715  1.00 52.62           C  
ANISOU 2796  C   GLN B 117     7586   5854   6555    314   -200    -98
ATOM   2797  O   GLN B 117     -21.042  -1.443 -31.172  1.00 50.76           O  
ANISOU 2797  O   GLN B 117     7383   5548   6357    287   -237    -43
ATOM   2798  CB  GLN B 117     -20.949   1.305 -32.689  1.00 55.89           C  
ANISOU 2798  CB  GLN B 117     8012   6255   6967    194   -142   -100
ATOM   2799  CG  GLN B 117     -20.034   2.331 -31.979  1.00 63.32           C  
ANISOU 2799  CG  GLN B 117     8911   7289   7858    154    -87   -122
ATOM   2800  CD  GLN B 117     -18.723   2.583 -32.722  1.00 71.88           C  
ANISOU 2800  CD  GLN B 117     9980   8476   8854    113    -52   -182
ATOM   2801  OE1 GLN B 117     -17.678   2.059 -32.352  1.00 73.26           O  
ANISOU 2801  OE1 GLN B 117    10220   8625   8991     54    -46   -197
ATOM   2802  NE2 GLN B 117     -18.760   3.341 -33.802  1.00 73.26           N  
ANISOU 2802  NE2 GLN B 117    10063   8796   8977    146    -33   -221
ATOM   2803  H   GLN B 117     -22.128  -1.087 -33.404  1.00 54.97           H  
ATOM   2804  HA  GLN B 117     -19.361   0.045 -33.512  1.00 54.21           H  
ATOM   2805  HB3 GLN B 117     -21.836   1.153 -32.075  1.00 55.89           H  
ATOM   2806  HB2 GLN B 117     -21.309   1.741 -33.620  1.00 55.89           H  
ATOM   2807  HG3 GLN B 117     -19.791   1.974 -30.978  1.00 63.32           H  
ATOM   2808  HG2 GLN B 117     -20.559   3.276 -31.843  1.00 63.32           H  
ATOM   2809 HE22 GLN B 117     -17.899   3.481 -34.309  1.00 73.26           H  
ATOM   2810 HE21 GLN B 117     -19.625   3.739 -34.140  1.00 73.26           H  
ATOM   2811  N   GLU B 118     -18.839  -0.897 -31.249  1.00 53.12           N  
ANISOU 2811  N   GLU B 118     7590   6028   6565    367   -175   -142
ATOM   2812  CA  GLU B 118     -18.473  -1.402 -29.934  1.00 54.26           C  
ANISOU 2812  CA  GLU B 118     7717   6194   6704    418   -192   -127
ATOM   2813  C   GLU B 118     -18.732  -0.300 -28.904  1.00 53.14           C  
ANISOU 2813  C   GLU B 118     7512   6090   6590    329   -140    -96
ATOM   2814  O   GLU B 118     -18.072   0.738 -28.961  1.00 53.46           O  
ANISOU 2814  O   GLU B 118     7502   6213   6596    268    -83   -124
ATOM   2815  CB  GLU B 118     -16.997  -1.834 -29.921  1.00 58.74           C  
ANISOU 2815  CB  GLU B 118     8234   6903   7182    542   -195   -200
ATOM   2816  CG  GLU B 118     -16.741  -3.224 -30.541  1.00 67.74           C  
ANISOU 2816  CG  GLU B 118     9496   7962   8282    698   -285   -220
ATOM   2817  CD  GLU B 118     -15.400  -3.838 -30.135  1.00 80.85           C  
ANISOU 2817  CD  GLU B 118    11108   9790   9823    886   -303   -317
ATOM   2818  OE1 GLU B 118     -14.476  -3.098 -29.732  1.00 83.97           O  
ANISOU 2818  OE1 GLU B 118    11335  10410  10159    864   -234   -371
ATOM   2819  OE2 GLU B 118     -15.331  -5.085 -30.034  1.00 84.37           O1-
ANISOU 2819  OE2 GLU B 118    11694  10153  10211   1056   -393   -343
ATOM   2820  H   GLU B 118     -18.137  -0.333 -31.712  1.00 53.12           H  
ATOM   2821  HA  GLU B 118     -19.088  -2.268 -29.681  1.00 54.26           H  
ATOM   2822  HB3 GLU B 118     -16.618  -1.785 -28.900  1.00 58.74           H  
ATOM   2823  HB2 GLU B 118     -16.398  -1.117 -30.483  1.00 58.74           H  
ATOM   2824  HG3 GLU B 118     -16.777  -3.167 -31.631  1.00 67.74           H  
ATOM   2825  HG2 GLU B 118     -17.523  -3.901 -30.207  1.00 67.74           H  
ATOM   2826  N   ILE B 119     -19.678  -0.523 -27.994  1.00 51.47           N  
ANISOU 2826  N   ILE B 119     7320   5813   6424    300   -162    -37
ATOM   2827  CA  ILE B 119     -19.970   0.420 -26.922  1.00 51.00           C  
ANISOU 2827  CA  ILE B 119     7204   5792   6380    243   -119    -12
ATOM   2828  C   ILE B 119     -19.798  -0.273 -25.570  1.00 48.50           C  
ANISOU 2828  C   ILE B 119     6875   5492   6061    263   -135     15
ATOM   2829  O   ILE B 119     -19.845  -1.504 -25.474  1.00 47.41           O  
ANISOU 2829  O   ILE B 119     6808   5296   5911    304   -195     32
ATOM   2830  CB  ILE B 119     -21.405   1.016 -27.006  1.00 52.84           C  
ANISOU 2830  CB  ILE B 119     7444   5984   6647    191   -118     24
ATOM   2831  CG1 ILE B 119     -22.550  -0.005 -26.821  1.00 54.90           C  
ANISOU 2831  CG1 ILE B 119     7724   6207   6929    162   -169     74
ATOM   2832  CG2 ILE B 119     -21.579   1.855 -28.287  1.00 53.03           C  
ANISOU 2832  CG2 ILE B 119     7508   5980   6662    182   -109     -4
ATOM   2833  CD1 ILE B 119     -23.846   0.633 -26.320  1.00 57.19           C  
ANISOU 2833  CD1 ILE B 119     7953   6556   7221    126   -157    103
ATOM   2834  H   ILE B 119     -20.119  -1.436 -27.922  1.00 51.47           H  
ATOM   2835  HA  ILE B 119     -19.266   1.253 -26.933  1.00 51.00           H  
ATOM   2836  HB  ILE B 119     -21.490   1.719 -26.173  1.00 52.84           H  
ATOM   2837 HG13 ILE B 119     -22.287  -0.754 -26.078  1.00 54.90           H  
ATOM   2838 HG12 ILE B 119     -22.714  -0.568 -27.736  1.00 54.90           H  
ATOM   2839 HG21 ILE B 119     -22.526   2.395 -28.292  1.00 53.03           H  
ATOM   2840 HG22 ILE B 119     -20.780   2.595 -28.376  1.00 53.03           H  
ATOM   2841 HG23 ILE B 119     -21.546   1.224 -29.179  1.00 53.03           H  
ATOM   2842 HD11 ILE B 119     -24.708   0.005 -26.528  1.00 57.19           H  
ATOM   2843 HD12 ILE B 119     -23.795   0.765 -25.239  1.00 57.19           H  
ATOM   2844 HD13 ILE B 119     -24.033   1.606 -26.775  1.00 57.19           H  
ATOM   2845  N   LEU B 120     -19.630   0.554 -24.544  1.00 47.41           N  
ANISOU 2845  N   LEU B 120     6678   5417   5917    234    -91     19
ATOM   2846  CA  LEU B 120     -19.626   0.128 -23.157  1.00 47.95           C  
ANISOU 2846  CA  LEU B 120     6731   5508   5981    244   -101     45
ATOM   2847  C   LEU B 120     -21.036   0.280 -22.564  1.00 47.95           C  
ANISOU 2847  C   LEU B 120     6719   5492   6009    177    -97    100
ATOM   2848  O   LEU B 120     -21.794   1.173 -22.947  1.00 48.82           O  
ANISOU 2848  O   LEU B 120     6801   5619   6127    154    -67     97
ATOM   2849  CB  LEU B 120     -18.591   0.974 -22.387  1.00 48.31           C  
ANISOU 2849  CB  LEU B 120     6706   5663   5985    246    -51      9
ATOM   2850  CG  LEU B 120     -17.120   0.748 -22.804  1.00 49.32           C  
ANISOU 2850  CG  LEU B 120     6793   5900   6047    300    -45    -58
ATOM   2851  CD1 LEU B 120     -16.193   1.778 -22.136  1.00 50.31           C  
ANISOU 2851  CD1 LEU B 120     6838   6165   6111    244      9    -88
ATOM   2852  CD2 LEU B 120     -16.633  -0.687 -22.538  1.00 48.84           C  
ANISOU 2852  CD2 LEU B 120     6764   5837   5956    433   -111    -73
ATOM   2853  H   LEU B 120     -19.627   1.556 -24.727  1.00 47.41           H  
ATOM   2854  HA  LEU B 120     -19.347  -0.922 -23.094  1.00 47.95           H  
ATOM   2855  HB3 LEU B 120     -18.703   0.793 -21.316  1.00 48.31           H  
ATOM   2856  HB2 LEU B 120     -18.827   2.020 -22.552  1.00 48.31           H  
ATOM   2857  HG  LEU B 120     -17.050   0.929 -23.877  1.00 49.32           H  
ATOM   2858 HD11 LEU B 120     -15.257   1.871 -22.687  1.00 50.31           H  
ATOM   2859 HD12 LEU B 120     -16.642   2.772 -22.101  1.00 50.31           H  
ATOM   2860 HD13 LEU B 120     -15.944   1.492 -21.114  1.00 50.31           H  
ATOM   2861 HD21 LEU B 120     -15.546  -0.751 -22.583  1.00 48.84           H  
ATOM   2862 HD22 LEU B 120     -16.953  -1.061 -21.564  1.00 48.84           H  
ATOM   2863 HD23 LEU B 120     -17.020  -1.372 -23.291  1.00 48.84           H  
ATOM   2864  N   VAL B 121     -21.359  -0.556 -21.589  1.00 45.81           N  
ANISOU 2864  N   VAL B 121     6479   5197   5729    151   -137    145
ATOM   2865  CA  VAL B 121     -22.528  -0.440 -20.736  1.00 45.02           C  
ANISOU 2865  CA  VAL B 121     6340   5140   5627     69   -131    194
ATOM   2866  C   VAL B 121     -22.081  -0.847 -19.322  1.00 45.55           C  
ANISOU 2866  C   VAL B 121     6409   5230   5670     59   -133    217
ATOM   2867  O   VAL B 121     -21.084  -1.557 -19.177  1.00 45.64           O  
ANISOU 2867  O   VAL B 121     6478   5202   5661    123   -161    202
ATOM   2868  CB  VAL B 121     -23.682  -1.365 -21.219  1.00 45.03           C  
ANISOU 2868  CB  VAL B 121     6385   5117   5609    -26   -183    239
ATOM   2869  CG1 VAL B 121     -24.192  -0.953 -22.610  1.00 44.74           C  
ANISOU 2869  CG1 VAL B 121     6331   5074   5594    -11   -181    215
ATOM   2870  CG2 VAL B 121     -23.349  -2.871 -21.202  1.00 45.10           C  
ANISOU 2870  CG2 VAL B 121     6552   5007   5576    -53   -262    269
ATOM   2871  H   VAL B 121     -20.740  -1.331 -21.355  1.00 45.81           H  
ATOM   2872  HA  VAL B 121     -22.879   0.593 -20.701  1.00 45.02           H  
ATOM   2873  HB  VAL B 121     -24.515  -1.214 -20.532  1.00 45.03           H  
ATOM   2874 HG11 VAL B 121     -25.026  -1.572 -22.923  1.00 44.74           H  
ATOM   2875 HG12 VAL B 121     -24.525   0.085 -22.631  1.00 44.74           H  
ATOM   2876 HG13 VAL B 121     -23.422  -1.068 -23.372  1.00 44.74           H  
ATOM   2877 HG21 VAL B 121     -24.167  -3.471 -21.596  1.00 45.10           H  
ATOM   2878 HG22 VAL B 121     -22.473  -3.084 -21.815  1.00 45.10           H  
ATOM   2879 HG23 VAL B 121     -23.150  -3.237 -20.195  1.00 45.10           H  
ATOM   2880  N   LEU B 122     -22.804  -0.398 -18.298  1.00 45.35           N  
ANISOU 2880  N   LEU B 122     6319   5284   5629     -7   -109    248
ATOM   2881  CA  LEU B 122     -22.604  -0.867 -16.931  1.00 45.89           C  
ANISOU 2881  CA  LEU B 122     6396   5373   5667    -37   -113    278
ATOM   2882  C   LEU B 122     -23.553  -2.043 -16.722  1.00 46.85           C  
ANISOU 2882  C   LEU B 122     6593   5474   5734   -169   -171    342
ATOM   2883  O   LEU B 122     -24.738  -1.876 -17.014  1.00 48.09           O  
ANISOU 2883  O   LEU B 122     6684   5721   5867   -264   -163    362
ATOM   2884  CB  LEU B 122     -22.980   0.251 -15.940  1.00 45.78           C  
ANISOU 2884  CB  LEU B 122     6270   5475   5649    -35    -50    269
ATOM   2885  CG  LEU B 122     -22.114   1.516 -15.988  1.00 47.73           C  
ANISOU 2885  CG  LEU B 122     6491   5728   5915     52      0    213
ATOM   2886  CD1 LEU B 122     -22.693   2.624 -15.094  1.00 49.51           C  
ANISOU 2886  CD1 LEU B 122     6658   6041   6113     64     45    204
ATOM   2887  CD2 LEU B 122     -20.660   1.222 -15.604  1.00 46.92           C  
ANISOU 2887  CD2 LEU B 122     6421   5598   5808     91     -7    194
ATOM   2888  H   LEU B 122     -23.661   0.125 -18.465  1.00 45.35           H  
ATOM   2889  HA  LEU B 122     -21.575  -1.186 -16.763  1.00 45.89           H  
ATOM   2890  HB3 LEU B 122     -22.950  -0.144 -14.931  1.00 45.78           H  
ATOM   2891  HB2 LEU B 122     -24.016   0.524 -16.113  1.00 45.78           H  
ATOM   2892  HG  LEU B 122     -22.130   1.886 -17.012  1.00 47.73           H  
ATOM   2893 HD11 LEU B 122     -22.083   3.526 -15.153  1.00 49.51           H  
ATOM   2894 HD12 LEU B 122     -23.701   2.897 -15.401  1.00 49.51           H  
ATOM   2895 HD13 LEU B 122     -22.736   2.320 -14.047  1.00 49.51           H  
ATOM   2896 HD21 LEU B 122     -20.050   2.120 -15.686  1.00 46.92           H  
ATOM   2897 HD22 LEU B 122     -20.595   0.856 -14.580  1.00 46.92           H  
ATOM   2898 HD23 LEU B 122     -20.208   0.473 -16.251  1.00 46.92           H  
ATOM   2899  N   ARG B 123     -23.058  -3.170 -16.205  1.00 46.27           N  
ANISOU 2899  N   ARG B 123     6671   5293   5614   -181   -237    370
ATOM   2900  CA  ARG B 123     -23.908  -4.244 -15.692  1.00 46.44           C  
ANISOU 2900  CA  ARG B 123     6818   5278   5547   -355   -302    441
ATOM   2901  C   ARG B 123     -23.772  -4.271 -14.168  1.00 46.73           C  
ANISOU 2901  C   ARG B 123     6851   5367   5538   -413   -292    474
ATOM   2902  O   ARG B 123     -22.661  -4.071 -13.679  1.00 45.62           O  
ANISOU 2902  O   ARG B 123     6738   5182   5413   -285   -293    449
ATOM   2903  CB  ARG B 123     -23.542  -5.596 -16.333  1.00 47.52           C  
ANISOU 2903  CB  ARG B 123     7211   5216   5627   -336   -409    454
ATOM   2904  CG  ARG B 123     -24.458  -6.735 -15.811  1.00 49.41           C  
ANISOU 2904  CG  ARG B 123     7640   5394   5740   -570   -488    536
ATOM   2905  CD  ARG B 123     -24.517  -8.008 -16.665  1.00 51.72           C  
ANISOU 2905  CD  ARG B 123     8169   5517   5964   -628   -587    556
ATOM   2906  NE  ARG B 123     -24.907  -7.715 -18.056  1.00 54.25           N  
ANISOU 2906  NE  ARG B 123     8364   5886   6362   -583   -548    516
ATOM   2907  CZ  ARG B 123     -26.084  -7.344 -18.576  1.00 56.40           C  
ANISOU 2907  CZ  ARG B 123     8517   6289   6622   -754   -520    540
ATOM   2908  NH1 ARG B 123     -27.216  -7.315 -17.868  1.00 55.12           N  
ANISOU 2908  NH1 ARG B 123     8324   6257   6361  -1001   -521    601
ATOM   2909  NH2 ARG B 123     -26.112  -6.982 -19.852  1.00 58.00           N1+
ANISOU 2909  NH2 ARG B 123     8622   6522   6894   -683   -492    499
ATOM   2910  H   ARG B 123     -22.065  -3.237 -15.976  1.00 46.27           H  
ATOM   2911  HA  ARG B 123     -24.951  -4.047 -15.934  1.00 46.44           H  
ATOM   2912  HB3 ARG B 123     -22.498  -5.839 -16.133  1.00 47.52           H  
ATOM   2913  HB2 ARG B 123     -23.625  -5.489 -17.415  1.00 47.52           H  
ATOM   2914  HG3 ARG B 123     -25.473  -6.391 -15.623  1.00 49.41           H  
ATOM   2915  HG2 ARG B 123     -24.074  -7.019 -14.830  1.00 49.41           H  
ATOM   2916  HD3 ARG B 123     -25.271  -8.675 -16.246  1.00 51.72           H  
ATOM   2917  HD2 ARG B 123     -23.575  -8.553 -16.606  1.00 51.72           H  
ATOM   2918 HH22 ARG B 123     -27.032  -6.721 -20.238  1.00 58.00           H  
ATOM   2919 HH21 ARG B 123     -25.255  -6.909 -20.400  1.00 58.00           H  
ATOM   2920 HH12 ARG B 123     -28.119  -7.029 -18.291  1.00 55.12           H  
ATOM   2921 HH11 ARG B 123     -27.250  -7.535 -16.890  1.00 55.12           H  
ATOM   2922  HE  ARG B 123     -24.083  -7.684 -18.678  1.00 54.25           H  
ATOM   2923  N   ARG B 124     -24.884  -4.494 -13.455  1.00 47.82           N  
ANISOU 2923  N   ARG B 124     6938   5627   5604   -608   -280    526
ATOM   2924  CA  ARG B 124     -24.923  -4.648 -11.998  1.00 49.43           C  
ANISOU 2924  CA  ARG B 124     7141   5891   5748   -688   -271    562
ATOM   2925  C   ARG B 124     -24.053  -5.837 -11.554  1.00 51.22           C  
ANISOU 2925  C   ARG B 124     7638   5917   5908   -688   -368    597
ATOM   2926  O   ARG B 124     -24.232  -6.937 -12.081  1.00 50.80           O  
ANISOU 2926  O   ARG B 124     7815   5716   5770   -784   -462    636
ATOM   2927  CB  ARG B 124     -26.384  -4.847 -11.540  1.00 50.23           C  
ANISOU 2927  CB  ARG B 124     7148   6193   5744   -931   -252    611
ATOM   2928  CG  ARG B 124     -27.300  -3.662 -11.882  1.00 50.82           C  
ANISOU 2928  CG  ARG B 124     6957   6499   5853   -886   -170    563
ATOM   2929  CD  ARG B 124     -28.751  -3.841 -11.402  1.00 52.21           C  
ANISOU 2929  CD  ARG B 124     6986   6956   5896  -1101   -148    593
ATOM   2930  NE  ARG B 124     -29.635  -2.817 -11.985  1.00 55.00           N  
ANISOU 2930  NE  ARG B 124     7103   7536   6259  -1008    -92    533
ATOM   2931  CZ  ARG B 124     -29.710  -1.510 -11.718  1.00 57.53           C  
ANISOU 2931  CZ  ARG B 124     7257   7987   6616   -815    -25    469
ATOM   2932  NH1 ARG B 124     -28.967  -0.954 -10.755  1.00 57.14           N  
ANISOU 2932  NH1 ARG B 124     7234   7872   6607   -721      5    461
ATOM   2933  NH2 ARG B 124     -30.547  -0.766 -12.439  1.00 57.59           N1+
ANISOU 2933  NH2 ARG B 124     7100   8168   6612   -694      3    408
ATOM   2934  H   ARG B 124     -25.753  -4.678 -13.945  1.00 47.82           H  
ATOM   2935  HA  ARG B 124     -24.537  -3.733 -11.544  1.00 49.43           H  
ATOM   2936  HB3 ARG B 124     -26.419  -5.032 -10.465  1.00 50.23           H  
ATOM   2937  HB2 ARG B 124     -26.784  -5.748 -12.008  1.00 50.23           H  
ATOM   2938  HG3 ARG B 124     -27.263  -3.393 -12.937  1.00 50.82           H  
ATOM   2939  HG2 ARG B 124     -26.871  -2.815 -11.348  1.00 50.82           H  
ATOM   2940  HD3 ARG B 124     -28.804  -3.707 -10.323  1.00 52.21           H  
ATOM   2941  HD2 ARG B 124     -29.121  -4.846 -11.573  1.00 52.21           H  
ATOM   2942 HH22 ARG B 124     -30.726   0.211 -12.273  1.00 57.59           H  
ATOM   2943 HH21 ARG B 124     -31.053  -1.219 -13.198  1.00 57.59           H  
ATOM   2944 HH12 ARG B 124     -28.948   0.029 -10.536  1.00 57.14           H  
ATOM   2945 HH11 ARG B 124     -28.349  -1.550 -10.197  1.00 57.14           H  
ATOM   2946  HE  ARG B 124     -30.263  -3.215 -12.692  1.00 55.00           H  
ATOM   2947  N   GLU B 125     -23.128  -5.599 -10.618  1.00 52.44           N  
ANISOU 2947  N   GLU B 125     7784   6056   6084   -560   -355    577
ATOM   2948  CA  GLU B 125     -22.271  -6.635 -10.052  1.00 53.97           C  
ANISOU 2948  CA  GLU B 125     8232   6074   6200   -506   -454    597
ATOM   2949  C   GLU B 125     -22.130  -6.345  -8.544  1.00 54.76           C  
ANISOU 2949  C   GLU B 125     8295   6243   6270   -532   -429    618
ATOM   2950  O   GLU B 125     -21.504  -5.335  -8.211  1.00 54.70           O  
ANISOU 2950  O   GLU B 125     8099   6341   6343   -403   -353    569
ATOM   2951  CB  GLU B 125     -20.915  -6.673 -10.790  1.00 56.84           C  
ANISOU 2951  CB  GLU B 125     8642   6342   6611   -238   -489    525
ATOM   2952  CG  GLU B 125     -19.948  -7.732 -10.204  1.00 62.44           C  
ANISOU 2952  CG  GLU B 125     9636   6878   7211   -126   -614    531
ATOM   2953  CD  GLU B 125     -18.676  -7.924 -11.019  1.00 68.71           C  
ANISOU 2953  CD  GLU B 125    10512   7592   8002    139   -676    455
ATOM   2954  OE1 GLU B 125     -18.773  -8.176 -12.232  1.00 69.25           O  
ANISOU 2954  OE1 GLU B 125    10601   7615   8094    143   -685    438
ATOM   2955  OE2 GLU B 125     -17.562  -7.843 -10.441  1.00 72.65           O1-
ANISOU 2955  OE2 GLU B 125    11044   8098   8461    351   -717    406
ATOM   2956  H   GLU B 125     -23.068  -4.688 -10.170  1.00 52.44           H  
ATOM   2957  HA  GLU B 125     -22.718  -7.609 -10.230  1.00 53.97           H  
ATOM   2958  HB3 GLU B 125     -20.438  -5.691 -10.779  1.00 56.84           H  
ATOM   2959  HB2 GLU B 125     -21.105  -6.906 -11.839  1.00 56.84           H  
ATOM   2960  HG3 GLU B 125     -20.454  -8.697 -10.171  1.00 62.44           H  
ATOM   2961  HG2 GLU B 125     -19.683  -7.493  -9.175  1.00 62.44           H  
ATOM   2962  N   PRO B 126     -22.684  -7.194  -7.645  1.00 55.27           N  
ANISOU 2962  N   PRO B 126     8547   6250   6204   -719   -493    692
ATOM   2963  CA  PRO B 126     -23.488  -8.399  -7.940  1.00 55.86           C  
ANISOU 2963  CA  PRO B 126     8896   6193   6136   -943   -595    764
ATOM   2964  C   PRO B 126     -24.847  -8.072  -8.611  1.00 56.76           C  
ANISOU 2964  C   PRO B 126     8853   6475   6240  -1170   -539    788
ATOM   2965  O   PRO B 126     -25.246  -6.903  -8.593  1.00 56.74           O  
ANISOU 2965  O   PRO B 126     8533   6700   6326  -1143   -424    751
ATOM   2966  CB  PRO B 126     -23.657  -9.055  -6.555  1.00 56.45           C  
ANISOU 2966  CB  PRO B 126     9161   6219   6068  -1100   -651    832
ATOM   2967  CG  PRO B 126     -23.560  -7.912  -5.558  1.00 56.69           C  
ANISOU 2967  CG  PRO B 126     8894   6464   6181  -1051   -533    806
ATOM   2968  CD  PRO B 126     -22.539  -6.985  -6.204  1.00 55.00           C  
ANISOU 2968  CD  PRO B 126     8474   6289   6136   -752   -466    713
ATOM   2969  HA  PRO B 126     -22.908  -9.060  -8.578  1.00 55.86           H  
ATOM   2970  HB3 PRO B 126     -22.836  -9.754  -6.389  1.00 56.45           H  
ATOM   2971  HB2 PRO B 126     -24.586  -9.615  -6.443  1.00 56.45           H  
ATOM   2972  HG3 PRO B 126     -23.277  -8.232  -4.554  1.00 56.69           H  
ATOM   2973  HG2 PRO B 126     -24.525  -7.405  -5.491  1.00 56.69           H  
ATOM   2974  HD2 PRO B 126     -22.702  -5.953  -5.898  1.00 55.00           H  
ATOM   2975  HD3 PRO B 126     -21.525  -7.260  -5.915  1.00 55.00           H  
ATOM   2976  N   PRO B 127     -25.534  -9.092  -9.178  1.00 57.51           N  
ANISOU 2976  N   PRO B 127     9168   6474   6211  -1388   -624    843
ATOM   2977  CA  PRO B 127     -26.890  -8.920  -9.730  1.00 58.04           C  
ANISOU 2977  CA  PRO B 127     9046   6749   6257  -1596   -570    856
ATOM   2978  C   PRO B 127     -27.862  -8.249  -8.748  1.00 57.78           C  
ANISOU 2978  C   PRO B 127     8736   7043   6175  -1777   -473    872
ATOM   2979  O   PRO B 127     -27.784  -8.494  -7.544  1.00 57.40           O  
ANISOU 2979  O   PRO B 127     8765   7014   6030  -1903   -486    917
ATOM   2980  CB  PRO B 127     -27.328 -10.345 -10.097  1.00 59.35           C  
ANISOU 2980  CB  PRO B 127     9564   6736   6252  -1848   -699    925
ATOM   2981  CG  PRO B 127     -26.027 -11.085 -10.356  1.00 59.60           C  
ANISOU 2981  CG  PRO B 127     9950   6418   6276  -1623   -818    913
ATOM   2982  CD  PRO B 127     -25.084 -10.480  -9.323  1.00 57.34           C  
ANISOU 2982  CD  PRO B 127     9593   6151   6043  -1445   -783    890
ATOM   2983  HA  PRO B 127     -26.791  -8.321 -10.636  1.00 58.04           H  
ATOM   2984  HB3 PRO B 127     -27.999 -10.361 -10.956  1.00 59.35           H  
ATOM   2985  HB2 PRO B 127     -27.859 -10.810  -9.264  1.00 59.35           H  
ATOM   2986  HG3 PRO B 127     -25.672 -10.841 -11.359  1.00 59.60           H  
ATOM   2987  HG2 PRO B 127     -26.119 -12.169 -10.284  1.00 59.60           H  
ATOM   2988  HD2 PRO B 127     -25.193 -10.989  -8.364  1.00 57.34           H  
ATOM   2989  HD3 PRO B 127     -24.051 -10.576  -9.652  1.00 57.34           H  
ATOM   2990  N   HIS B 128     -28.701  -7.363  -9.286  1.00 57.40           N  
ANISOU 2990  N   HIS B 128     8367   7256   6186  -1755   -380    826
ATOM   2991  CA  HIS B 128     -29.695  -6.547  -8.590  1.00 58.59           C  
ANISOU 2991  CA  HIS B 128     8208   7775   6278  -1862   -286    815
ATOM   2992  C   HIS B 128     -29.102  -5.396  -7.750  1.00 58.77           C  
ANISOU 2992  C   HIS B 128     8048   7876   6407  -1622   -201    759
ATOM   2993  O   HIS B 128     -29.873  -4.663  -7.131  1.00 59.76           O  
ANISOU 2993  O   HIS B 128     7921   8303   6483  -1649   -124    733
ATOM   2994  CB  HIS B 128     -30.694  -7.415  -7.780  1.00 60.57           C  
ANISOU 2994  CB  HIS B 128     8536   8180   6299  -2260   -321    898
ATOM   2995  CG  HIS B 128     -31.192  -8.670  -8.468  1.00 65.59           C  
ANISOU 2995  CG  HIS B 128     9429   8702   6791  -2551   -423    965
ATOM   2996  ND1 HIS B 128     -31.543  -8.719  -9.808  1.00 68.17           N  
ANISOU 2996  ND1 HIS B 128     9642   9147   7114  -2603   -419    944
ATOM   2997  CD2 HIS B 128     -31.325  -9.963  -8.010  1.00 67.80           C  
ANISOU 2997  CD2 HIS B 128    10098   8756   6908  -2808   -539   1052
ATOM   2998  CE1 HIS B 128     -31.860  -9.984 -10.088  1.00 68.94           C  
ANISOU 2998  CE1 HIS B 128    10056   9083   7055  -2896   -529   1019
ATOM   2999  NE2 HIS B 128     -31.767 -10.798  -9.041  1.00 69.30           N  
ANISOU 2999  NE2 HIS B 128    10431   8907   6993  -3028   -608   1086
ATOM   3000  H   HIS B 128     -28.763  -7.322 -10.312  1.00 57.40           H  
ATOM   3001  HA  HIS B 128     -30.261  -6.070  -9.388  1.00 58.59           H  
ATOM   3002  HB3 HIS B 128     -31.562  -6.816  -7.507  1.00 60.57           H  
ATOM   3003  HB2 HIS B 128     -30.237  -7.714  -6.836  1.00 60.57           H  
ATOM   3004  HD1 HIS B 128     -31.454  -7.971 -10.510  1.00 68.17           H  
ATOM   3005  HD2 HIS B 128     -31.134 -10.354  -7.022  1.00 67.80           H  
ATOM   3006  HE1 HIS B 128     -32.142 -10.316 -11.076  1.00 68.94           H  
ATOM   3007  N   SER B 129     -27.769  -5.200  -7.756  1.00 56.95           N  
ANISOU 3007  N   SER B 129     7942   7399   6298  -1391   -217    736
ATOM   3008  CA  SER B 129     -27.117  -4.119  -7.011  1.00 55.18           C  
ANISOU 3008  CA  SER B 129     7571   7234   6160  -1191   -143    686
ATOM   3009  C   SER B 129     -27.540  -2.728  -7.536  1.00 54.29           C  
ANISOU 3009  C   SER B 129     7201   7297   6129  -1018    -58    607
ATOM   3010  O   SER B 129     -27.356  -2.446  -8.729  1.00 53.02           O  
ANISOU 3010  O   SER B 129     7036   7058   6051   -900    -62    570
ATOM   3011  CB  SER B 129     -25.582  -4.245  -7.083  1.00 54.10           C  
ANISOU 3011  CB  SER B 129     7599   6840   6118   -991   -182    668
ATOM   3012  OG  SER B 129     -24.971  -3.176  -6.369  1.00 54.62           O  
ANISOU 3012  OG  SER B 129     7527   6968   6258   -821   -112    618
ATOM   3013  H   SER B 129     -27.176  -5.854  -8.251  1.00 56.95           H  
ATOM   3014  HA  SER B 129     -27.399  -4.263  -5.970  1.00 55.18           H  
ATOM   3015  HB3 SER B 129     -25.236  -4.240  -8.119  1.00 54.10           H  
ATOM   3016  HB2 SER B 129     -25.259  -5.187  -6.640  1.00 54.10           H  
ATOM   3017  HG  SER B 129     -24.003  -3.336  -6.335  1.00 54.62           H  
ATOM   3018  N   PRO B 130     -28.081  -1.857  -6.657  1.00 53.42           N  
ANISOU 3018  N   PRO B 130     6899   7417   5982   -986     14    577
ATOM   3019  CA  PRO B 130     -28.405  -0.493  -7.074  1.00 52.30           C  
ANISOU 3019  CA  PRO B 130     6569   7412   5889   -782     75    494
ATOM   3020  C   PRO B 130     -27.180   0.416  -7.302  1.00 50.93           C  
ANISOU 3020  C   PRO B 130     6451   7057   5845   -545     96    442
ATOM   3021  O   PRO B 130     -27.364   1.448  -7.948  1.00 51.64           O  
ANISOU 3021  O   PRO B 130     6468   7184   5970   -382    126    378
ATOM   3022  CB  PRO B 130     -29.331   0.006  -5.951  1.00 53.52           C  
ANISOU 3022  CB  PRO B 130     6532   7878   5925   -813    131    474
ATOM   3023  CG  PRO B 130     -28.853  -0.725  -4.704  1.00 54.67           C  
ANISOU 3023  CG  PRO B 130     6769   8009   5996  -1014    113    546
ATOM   3024  CD  PRO B 130     -28.433  -2.090  -5.250  1.00 53.18           C  
ANISOU 3024  CD  PRO B 130     6839   7521   5846  -1118     33    612
ATOM   3025  HA  PRO B 130     -28.971  -0.511  -8.003  1.00 52.30           H  
ATOM   3026  HB3 PRO B 130     -30.353  -0.300  -6.182  1.00 53.52           H  
ATOM   3027  HB2 PRO B 130     -29.340   1.088  -5.836  1.00 53.52           H  
ATOM   3028  HG3 PRO B 130     -29.602  -0.790  -3.913  1.00 54.67           H  
ATOM   3029  HG2 PRO B 130     -27.982  -0.213  -4.292  1.00 54.67           H  
ATOM   3030  HD2 PRO B 130     -27.610  -2.507  -4.666  1.00 53.18           H  
ATOM   3031  HD3 PRO B 130     -29.274  -2.786  -5.222  1.00 53.18           H  
ATOM   3032  N   ASN B 131     -25.991   0.064  -6.772  1.00 49.19           N  
ANISOU 3032  N   ASN B 131     6363   6655   5670   -531     76    465
ATOM   3033  CA  ASN B 131     -24.880   1.009  -6.601  1.00 47.13           C  
ANISOU 3033  CA  ASN B 131     6123   6292   5492   -352    103    414
ATOM   3034  C   ASN B 131     -23.479   0.465  -6.947  1.00 46.29           C  
ANISOU 3034  C   ASN B 131     6154   5983   5451   -304     61    419
ATOM   3035  O   ASN B 131     -22.513   1.217  -6.795  1.00 46.49           O  
ANISOU 3035  O   ASN B 131     6184   5971   5509   -209     83    385
ATOM   3036  CB  ASN B 131     -24.922   1.654  -5.186  1.00 46.46           C  
ANISOU 3036  CB  ASN B 131     5982   6307   5363   -334    147    406
ATOM   3037  CG  ASN B 131     -24.576   0.744  -4.000  1.00 48.01           C  
ANISOU 3037  CG  ASN B 131     6256   6479   5509   -471    115    471
ATOM   3038  OD1 ASN B 131     -24.362  -0.452  -4.134  1.00 48.33           O  
ANISOU 3038  OD1 ASN B 131     6426   6402   5536   -569     50    522
ATOM   3039  ND2 ASN B 131     -24.544   1.303  -2.793  1.00 48.84           N  
ANISOU 3039  ND2 ASN B 131     6312   6676   5568   -475    150    470
ATOM   3040  H   ASN B 131     -25.875  -0.833  -6.310  1.00 49.19           H  
ATOM   3041  HA  ASN B 131     -24.995   1.823  -7.316  1.00 47.13           H  
ATOM   3042  HB3 ASN B 131     -25.911   2.068  -5.001  1.00 46.46           H  
ATOM   3043  HB2 ASN B 131     -24.232   2.499  -5.166  1.00 46.46           H  
ATOM   3044 HD22 ASN B 131     -24.346   0.709  -1.999  1.00 48.84           H  
ATOM   3045 HD21 ASN B 131     -24.715   2.287  -2.659  1.00 48.84           H  
ATOM   3046  N   SER B 132     -23.366  -0.786  -7.411  1.00 45.51           N  
ANISOU 3046  N   SER B 132     6170   5773   5350   -364     -5    454
ATOM   3047  CA  SER B 132     -22.091  -1.383  -7.797  1.00 45.09           C  
ANISOU 3047  CA  SER B 132     6238   5560   5332   -271    -55    441
ATOM   3048  C   SER B 132     -22.243  -2.084  -9.155  1.00 44.55           C  
ANISOU 3048  C   SER B 132     6261   5391   5274   -278   -109    447
ATOM   3049  O   SER B 132     -23.115  -2.939  -9.320  1.00 44.13           O  
ANISOU 3049  O   SER B 132     6263   5336   5168   -416   -145    493
ATOM   3050  CB  SER B 132     -21.557  -2.273  -6.652  1.00 45.57           C  
ANISOU 3050  CB  SER B 132     6419   5558   5339   -287   -107    476
ATOM   3051  OG  SER B 132     -22.301  -3.461  -6.462  1.00 49.33           O  
ANISOU 3051  OG  SER B 132     7024   5990   5727   -449   -168    546
ATOM   3052  H   SER B 132     -24.171  -1.393  -7.497  1.00 45.51           H  
ATOM   3053  HA  SER B 132     -21.353  -0.594  -7.922  1.00 45.09           H  
ATOM   3054  HB3 SER B 132     -21.542  -1.713  -5.715  1.00 45.57           H  
ATOM   3055  HB2 SER B 132     -20.523  -2.551  -6.857  1.00 45.57           H  
ATOM   3056  HG  SER B 132     -22.033  -4.093  -7.160  1.00 49.33           H  
ATOM   3057  N   PHE B 133     -21.397  -1.695 -10.113  1.00 43.94           N  
ANISOU 3057  N   PHE B 133     6190   5253   5252   -144   -112    395
ATOM   3058  CA  PHE B 133     -21.440  -2.170 -11.490  1.00 43.59           C  
ANISOU 3058  CA  PHE B 133     6211   5124   5226   -119   -152    383
ATOM   3059  C   PHE B 133     -20.041  -2.615 -11.932  1.00 43.53           C  
ANISOU 3059  C   PHE B 133     6282   5038   5220     32   -197    339
ATOM   3060  O   PHE B 133     -19.041  -2.195 -11.346  1.00 44.26           O  
ANISOU 3060  O   PHE B 133     6334   5178   5305    120   -183    306
ATOM   3061  CB  PHE B 133     -21.900  -1.022 -12.418  1.00 43.00           C  
ANISOU 3061  CB  PHE B 133     6006   5123   5208    -99    -86    344
ATOM   3062  CG  PHE B 133     -23.273  -0.428 -12.149  1.00 43.29           C  
ANISOU 3062  CG  PHE B 133     5935   5290   5225   -186    -44    363
ATOM   3063  CD1 PHE B 133     -23.437   0.556 -11.154  1.00 44.44           C  
ANISOU 3063  CD1 PHE B 133     5987   5541   5358   -163     13    347
ATOM   3064  CD2 PHE B 133     -24.417  -0.929 -12.804  1.00 43.36           C  
ANISOU 3064  CD2 PHE B 133     5931   5338   5205   -281    -65    388
ATOM   3065  CE1 PHE B 133     -24.698   1.059 -10.878  1.00 45.09           C  
ANISOU 3065  CE1 PHE B 133     5958   5782   5393   -202     46    348
ATOM   3066  CE2 PHE B 133     -25.668  -0.404 -12.526  1.00 44.12           C  
ANISOU 3066  CE2 PHE B 133     5892   5618   5253   -339    -29    390
ATOM   3067  CZ  PHE B 133     -25.806   0.588 -11.565  1.00 44.60           C  
ANISOU 3067  CZ  PHE B 133     5854   5796   5295   -281     26    365
ATOM   3068  H   PHE B 133     -20.711  -0.971  -9.922  1.00 43.94           H  
ATOM   3069  HA  PHE B 133     -22.114  -3.021 -11.572  1.00 43.59           H  
ATOM   3070  HB3 PHE B 133     -21.881  -1.382 -13.447  1.00 43.00           H  
ATOM   3071  HB2 PHE B 133     -21.169  -0.214 -12.377  1.00 43.00           H  
ATOM   3072  HD1 PHE B 133     -22.580   0.925 -10.608  1.00 44.44           H  
ATOM   3073  HD2 PHE B 133     -24.321  -1.700 -13.551  1.00 43.36           H  
ATOM   3074  HE1 PHE B 133     -24.820   1.814 -10.119  1.00 45.09           H  
ATOM   3075  HE2 PHE B 133     -26.533  -0.779 -13.053  1.00 44.12           H  
ATOM   3076  HZ  PHE B 133     -26.777   0.999 -11.343  1.00 44.60           H  
ATOM   3077  N   ARG B 134     -19.984  -3.377 -13.024  1.00 44.69           N  
ANISOU 3077  N   ARG B 134     6526   5092   5361     67   -251    330
ATOM   3078  CA  ARG B 134     -18.789  -3.540 -13.842  1.00 45.89           C  
ANISOU 3078  CA  ARG B 134     6721   5214   5501    237   -289    268
ATOM   3079  C   ARG B 134     -19.100  -2.983 -15.234  1.00 45.23           C  
ANISOU 3079  C   ARG B 134     6576   5138   5470    241   -257    236
ATOM   3080  O   ARG B 134     -20.243  -3.083 -15.686  1.00 44.42           O  
ANISOU 3080  O   ARG B 134     6509   4985   5384    138   -265    273
ATOM   3081  CB  ARG B 134     -18.387  -5.032 -13.894  1.00 47.93           C  
ANISOU 3081  CB  ARG B 134     7220   5321   5670    313   -413    282
ATOM   3082  CG  ARG B 134     -17.087  -5.312 -14.690  1.00 50.69           C  
ANISOU 3082  CG  ARG B 134     7578   5699   5982    543   -451    197
ATOM   3083  CD  ARG B 134     -16.766  -6.794 -14.907  1.00 53.39           C  
ANISOU 3083  CD  ARG B 134     8198   5873   6213    671   -590    196
ATOM   3084  NE  ARG B 134     -16.402  -7.469 -13.654  1.00 55.35           N  
ANISOU 3084  NE  ARG B 134     8587   6067   6376    713   -659    222
ATOM   3085  CZ  ARG B 134     -15.210  -7.825 -13.174  1.00 54.88           C  
ANISOU 3085  CZ  ARG B 134     8497   6103   6252    925   -690    159
ATOM   3086  NH1 ARG B 134     -14.082  -7.504 -13.816  1.00 54.05           N  
ANISOU 3086  NH1 ARG B 134     8196   6189   6151   1090   -648     63
ATOM   3087  NH2 ARG B 134     -15.157  -8.495 -12.025  1.00 53.76           N1+
ANISOU 3087  NH2 ARG B 134     8513   5888   6024    962   -765    188
ATOM   3088  H   ARG B 134     -20.858  -3.677 -13.458  1.00 44.69           H  
ATOM   3089  HA  ARG B 134     -17.967  -2.953 -13.434  1.00 45.89           H  
ATOM   3090  HB3 ARG B 134     -19.208  -5.609 -14.320  1.00 47.93           H  
ATOM   3091  HB2 ARG B 134     -18.263  -5.395 -12.874  1.00 47.93           H  
ATOM   3092  HG3 ARG B 134     -16.265  -4.871 -14.129  1.00 50.69           H  
ATOM   3093  HG2 ARG B 134     -17.052  -4.815 -15.651  1.00 50.69           H  
ATOM   3094  HD3 ARG B 134     -16.053  -6.946 -15.715  1.00 53.39           H  
ATOM   3095  HD2 ARG B 134     -17.678  -7.301 -15.233  1.00 53.39           H  
ATOM   3096 HH22 ARG B 134     -14.517  -9.248 -11.849  1.00 53.76           H  
ATOM   3097 HH21 ARG B 134     -16.036  -8.478 -11.464  1.00 53.76           H  
ATOM   3098 HH12 ARG B 134     -13.167  -7.806 -13.533  1.00 54.05           H  
ATOM   3099 HH11 ARG B 134     -14.146  -6.885 -14.631  1.00 54.05           H  
ATOM   3100  HE  ARG B 134     -17.264  -7.758 -13.127  1.00 55.35           H  
ATOM   3101  N   LEU B 135     -18.077  -2.431 -15.897  1.00 45.70           N  
ANISOU 3101  N   LEU B 135     6543   5283   5539    346   -222    165
ATOM   3102  CA  LEU B 135     -18.116  -2.157 -17.332  1.00 46.00           C  
ANISOU 3102  CA  LEU B 135     6539   5329   5609    354   -196    129
ATOM   3103  C   LEU B 135     -18.205  -3.454 -18.149  1.00 46.64           C  
ANISOU 3103  C   LEU B 135     6774   5291   5656    425   -284    127
ATOM   3104  O   LEU B 135     -17.372  -4.352 -17.988  1.00 47.11           O  
ANISOU 3104  O   LEU B 135     6941   5316   5644    556   -359    105
ATOM   3105  CB  LEU B 135     -16.846  -1.409 -17.778  1.00 45.70           C  
ANISOU 3105  CB  LEU B 135     6382   5435   5547    420   -147     52
ATOM   3106  CG  LEU B 135     -16.755   0.083 -17.419  1.00 46.30           C  
ANISOU 3106  CG  LEU B 135     6351   5600   5641    320    -60     42
ATOM   3107  CD1 LEU B 135     -15.359   0.598 -17.770  1.00 45.10           C  
ANISOU 3107  CD1 LEU B 135     6107   5606   5421    342    -27    -29
ATOM   3108  CD2 LEU B 135     -17.814   0.947 -18.127  1.00 46.82           C  
ANISOU 3108  CD2 LEU B 135     6433   5595   5762    234    -29     68
ATOM   3109  H   LEU B 135     -17.185  -2.311 -15.429  1.00 45.70           H  
ATOM   3110  HA  LEU B 135     -19.000  -1.559 -17.543  1.00 46.00           H  
ATOM   3111  HB3 LEU B 135     -16.769  -1.478 -18.865  1.00 45.70           H  
ATOM   3112  HB2 LEU B 135     -15.978  -1.940 -17.385  1.00 45.70           H  
ATOM   3113  HG  LEU B 135     -16.893   0.176 -16.341  1.00 46.30           H  
ATOM   3114 HD11 LEU B 135     -15.197   1.575 -17.319  1.00 45.10           H  
ATOM   3115 HD12 LEU B 135     -14.576  -0.077 -17.429  1.00 45.10           H  
ATOM   3116 HD13 LEU B 135     -15.256   0.692 -18.850  1.00 45.10           H  
ATOM   3117 HD21 LEU B 135     -17.853   1.946 -17.690  1.00 46.82           H  
ATOM   3118 HD22 LEU B 135     -17.590   1.070 -19.186  1.00 46.82           H  
ATOM   3119 HD23 LEU B 135     -18.820   0.535 -18.066  1.00 46.82           H  
ATOM   3120  N   GLU B 136     -19.155  -3.493 -19.070  1.00 46.80           N  
ANISOU 3120  N   GLU B 136     6823   5246   5713    352   -285    146
ATOM   3121  CA  GLU B 136     -19.302  -4.547 -20.049  1.00 47.76           C  
ANISOU 3121  CA  GLU B 136     7108   5240   5798    393   -368    148
ATOM   3122  C   GLU B 136     -19.170  -3.897 -21.434  1.00 47.48           C  
ANISOU 3122  C   GLU B 136     7001   5237   5803    411   -330    103
ATOM   3123  O   GLU B 136     -19.740  -2.828 -21.633  1.00 47.43           O  
ANISOU 3123  O   GLU B 136     6880   5287   5854    319   -260    112
ATOM   3124  CB  GLU B 136     -20.676  -5.202 -19.821  1.00 51.85           C  
ANISOU 3124  CB  GLU B 136     7742   5654   6303    222   -411    231
ATOM   3125  CG  GLU B 136     -20.574  -6.718 -19.976  1.00 60.51           C  
ANISOU 3125  CG  GLU B 136     9113   6576   7303    235   -534    259
ATOM   3126  CD  GLU B 136     -21.880  -7.437 -19.679  1.00 66.70           C  
ANISOU 3126  CD  GLU B 136    10014   7288   8041     -3   -575    348
ATOM   3127  OE1 GLU B 136     -22.920  -7.148 -20.310  1.00 74.03           O  
ANISOU 3127  OE1 GLU B 136    10840   8279   9009   -138   -534    368
ATOM   3128  OE2 GLU B 136     -21.856  -8.381 -18.870  1.00 63.16           O1-
ANISOU 3128  OE2 GLU B 136     9764   6737   7496    -62   -653    394
ATOM   3129  H   GLU B 136     -19.817  -2.721 -19.163  1.00 46.80           H  
ATOM   3130  HA  GLU B 136     -18.518  -5.284 -19.917  1.00 47.76           H  
ATOM   3131  HB3 GLU B 136     -21.414  -4.823 -20.528  1.00 51.85           H  
ATOM   3132  HB2 GLU B 136     -21.072  -4.968 -18.828  1.00 51.85           H  
ATOM   3133  HG3 GLU B 136     -19.809  -7.091 -19.294  1.00 60.51           H  
ATOM   3134  HG2 GLU B 136     -20.233  -6.949 -20.983  1.00 60.51           H  
ATOM   3135  N   LYS B 137     -18.422  -4.510 -22.359  1.00 47.03           N  
ANISOU 3135  N   LYS B 137     7023   5147   5698    544   -380     51
ATOM   3136  CA  LYS B 137     -18.383  -4.072 -23.758  1.00 47.68           C  
ANISOU 3136  CA  LYS B 137     7049   5261   5805    556   -348      9
ATOM   3137  C   LYS B 137     -19.356  -4.956 -24.549  1.00 47.41           C  
ANISOU 3137  C   LYS B 137     7171   5069   5773    499   -413     48
ATOM   3138  O   LYS B 137     -19.214  -6.179 -24.483  1.00 46.95           O  
ANISOU 3138  O   LYS B 137     7311   4884   5645    566   -511     54
ATOM   3139  CB  LYS B 137     -16.958  -4.181 -24.348  1.00 50.72           C  
ANISOU 3139  CB  LYS B 137     7390   5766   6116    738   -355    -87
ATOM   3140  CG  LYS B 137     -16.760  -3.323 -25.616  1.00 54.82           C  
ANISOU 3140  CG  LYS B 137     7803   6377   6648    709   -293   -135
ATOM   3141  CD  LYS B 137     -15.821  -3.931 -26.660  1.00 61.25           C  
ANISOU 3141  CD  LYS B 137     8611   7297   7365    888   -325   -227
ATOM   3142  CE  LYS B 137     -14.323  -3.945 -26.323  1.00 67.21           C  
ANISOU 3142  CE  LYS B 137     9238   8276   8022   1014   -312   -301
ATOM   3143  NZ  LYS B 137     -13.536  -4.523 -27.429  1.00 70.73           N1+
ANISOU 3143  NZ  LYS B 137     9646   8881   8348   1203   -340   -406
ATOM   3144  H   LYS B 137     -17.993  -5.404 -22.125  1.00 47.03           H  
ATOM   3145  HA  LYS B 137     -18.698  -3.034 -23.837  1.00 47.68           H  
ATOM   3146  HB3 LYS B 137     -16.724  -5.227 -24.554  1.00 50.72           H  
ATOM   3147  HB2 LYS B 137     -16.232  -3.845 -23.617  1.00 50.72           H  
ATOM   3148  HG3 LYS B 137     -16.388  -2.336 -25.342  1.00 54.82           H  
ATOM   3149  HG2 LYS B 137     -17.715  -3.128 -26.108  1.00 54.82           H  
ATOM   3150  HD3 LYS B 137     -15.971  -3.342 -27.555  1.00 61.25           H  
ATOM   3151  HD2 LYS B 137     -16.146  -4.934 -26.919  1.00 61.25           H  
ATOM   3152  HE3 LYS B 137     -14.142  -4.499 -25.402  1.00 67.21           H  
ATOM   3153  HE2 LYS B 137     -13.976  -2.923 -26.177  1.00 67.21           H  
ATOM   3154  HZ1 LYS B 137     -13.783  -3.985 -28.282  1.00 70.73           H  
ATOM   3155  HZ2 LYS B 137     -12.543  -4.474 -27.299  1.00 70.73           H  
ATOM   3156  HZ3 LYS B 137     -13.818  -5.474 -27.635  1.00 70.73           H  
ATOM   3157  N   ILE B 138     -20.280  -4.335 -25.280  1.00 46.68           N  
ANISOU 3157  N   ILE B 138     7013   4979   5744    373   -370     74
ATOM   3158  CA  ILE B 138     -21.224  -4.994 -26.178  1.00 47.41           C  
ANISOU 3158  CA  ILE B 138     7220   4962   5834    293   -423    109
ATOM   3159  C   ILE B 138     -21.087  -4.389 -27.588  1.00 48.62           C  
ANISOU 3159  C   ILE B 138     7314   5141   6018    321   -389     64
ATOM   3160  O   ILE B 138     -20.444  -3.353 -27.759  1.00 47.37           O  
ANISOU 3160  O   ILE B 138     7032   5086   5881    361   -320     17
ATOM   3161  CB  ILE B 138     -22.696  -4.843 -25.681  1.00 47.85           C  
ANISOU 3161  CB  ILE B 138     7251   5027   5905    105   -420    186
ATOM   3162  CG1 ILE B 138     -23.187  -3.384 -25.547  1.00 49.32           C  
ANISOU 3162  CG1 ILE B 138     7238   5347   6153     74   -328    176
ATOM   3163  CG2 ILE B 138     -22.922  -5.629 -24.379  1.00 47.93           C  
ANISOU 3163  CG2 ILE B 138     7347   5004   5860     43   -461    236
ATOM   3164  CD1 ILE B 138     -24.703  -3.251 -25.352  1.00 51.32           C  
ANISOU 3164  CD1 ILE B 138     7426   5671   6404    -63   -324    224
ATOM   3165  H   ILE B 138     -20.244  -3.320 -25.379  1.00 46.68           H  
ATOM   3166  HA  ILE B 138     -20.978  -6.053 -26.268  1.00 47.41           H  
ATOM   3167  HB  ILE B 138     -23.334  -5.314 -26.433  1.00 47.85           H  
ATOM   3168 HG13 ILE B 138     -22.936  -2.826 -26.447  1.00 49.32           H  
ATOM   3169 HG12 ILE B 138     -22.671  -2.890 -24.724  1.00 49.32           H  
ATOM   3170 HG21 ILE B 138     -23.975  -5.660 -24.101  1.00 47.93           H  
ATOM   3171 HG22 ILE B 138     -22.603  -6.658 -24.516  1.00 47.93           H  
ATOM   3172 HG23 ILE B 138     -22.361  -5.204 -23.545  1.00 47.93           H  
ATOM   3173 HD11 ILE B 138     -25.010  -2.211 -25.446  1.00 51.32           H  
ATOM   3174 HD12 ILE B 138     -25.252  -3.819 -26.104  1.00 51.32           H  
ATOM   3175 HD13 ILE B 138     -25.020  -3.590 -24.367  1.00 51.32           H  
ATOM   3176  N   LEU B 139     -21.682  -5.065 -28.571  1.00 50.71           N  
ANISOU 3176  N   LEU B 139     7690   5308   6271    280   -443     80
ATOM   3177  CA  LEU B 139     -21.720  -4.657 -29.967  1.00 52.61           C  
ANISOU 3177  CA  LEU B 139     7900   5556   6533    297   -423     44
ATOM   3178  C   LEU B 139     -23.181  -4.288 -30.257  1.00 53.11           C  
ANISOU 3178  C   LEU B 139     7913   5632   6635    151   -412     94
ATOM   3179  O   LEU B 139     -24.055  -5.083 -29.915  1.00 54.63           O  
ANISOU 3179  O   LEU B 139     8181   5779   6798     36   -466    150
ATOM   3180  CB  LEU B 139     -21.237  -5.863 -30.806  1.00 54.48           C  
ANISOU 3180  CB  LEU B 139     8326   5670   6705    381   -510     20
ATOM   3181  CG  LEU B 139     -20.868  -5.551 -32.269  1.00 59.07           C  
ANISOU 3181  CG  LEU B 139     8891   6278   7274    482   -495    -51
ATOM   3182  CD1 LEU B 139     -19.656  -4.612 -32.377  1.00 60.85           C  
ANISOU 3182  CD1 LEU B 139     8949   6677   7496    567   -413   -119
ATOM   3183  CD2 LEU B 139     -20.590  -6.854 -33.030  1.00 60.14           C  
ANISOU 3183  CD2 LEU B 139     9241   6293   7318    617   -596    -85
ATOM   3184  H   LEU B 139     -22.304  -5.829 -28.355  1.00 50.71           H  
ATOM   3185  HA  LEU B 139     -21.070  -3.801 -30.142  1.00 52.61           H  
ATOM   3186  HB3 LEU B 139     -22.007  -6.636 -30.790  1.00 54.48           H  
ATOM   3187  HB2 LEU B 139     -20.370  -6.314 -30.322  1.00 54.48           H  
ATOM   3188  HG  LEU B 139     -21.720  -5.069 -32.748  1.00 59.07           H  
ATOM   3189 HD11 LEU B 139     -18.943  -4.925 -33.142  1.00 60.85           H  
ATOM   3190 HD12 LEU B 139     -19.959  -3.596 -32.624  1.00 60.85           H  
ATOM   3191 HD13 LEU B 139     -19.112  -4.579 -31.439  1.00 60.85           H  
ATOM   3192 HD21 LEU B 139     -20.274  -6.659 -34.056  1.00 60.14           H  
ATOM   3193 HD22 LEU B 139     -19.806  -7.437 -32.546  1.00 60.14           H  
ATOM   3194 HD23 LEU B 139     -21.487  -7.471 -33.083  1.00 60.14           H  
ATOM   3195  N   VAL B 140     -23.428  -3.100 -30.818  1.00 52.32           N  
ANISOU 3195  N   VAL B 140     7695   5608   6576    148   -350     73
ATOM   3196  CA  VAL B 140     -24.772  -2.583 -31.089  1.00 52.67           C  
ANISOU 3196  CA  VAL B 140     7681   5696   6636     63   -348    103
ATOM   3197  C   VAL B 140     -24.860  -2.014 -32.514  1.00 51.76           C  
ANISOU 3197  C   VAL B 140     7580   5557   6530     90   -347     70
ATOM   3198  O   VAL B 140     -23.896  -1.404 -32.987  1.00 52.42           O  
ANISOU 3198  O   VAL B 140     7670   5632   6614    157   -312     22
ATOM   3199  CB  VAL B 140     -25.142  -1.436 -30.108  1.00 53.75           C  
ANISOU 3199  CB  VAL B 140     7692   5946   6786     58   -295    110
ATOM   3200  CG1 VAL B 140     -25.388  -1.978 -28.694  1.00 54.49           C  
ANISOU 3200  CG1 VAL B 140     7766   6074   6864     12   -298    148
ATOM   3201  CG2 VAL B 140     -24.141  -0.256 -30.091  1.00 55.16           C  
ANISOU 3201  CG2 VAL B 140     7847   6137   6974    136   -236     61
ATOM   3202  H   VAL B 140     -22.666  -2.472 -31.057  1.00 52.32           H  
ATOM   3203  HA  VAL B 140     -25.507  -3.386 -31.000  1.00 52.67           H  
ATOM   3204  HB  VAL B 140     -26.099  -1.022 -30.434  1.00 53.75           H  
ATOM   3205 HG11 VAL B 140     -25.778  -1.199 -28.043  1.00 54.49           H  
ATOM   3206 HG12 VAL B 140     -26.125  -2.784 -28.706  1.00 54.49           H  
ATOM   3207 HG13 VAL B 140     -24.472  -2.370 -28.252  1.00 54.49           H  
ATOM   3208 HG21 VAL B 140     -24.389   0.459 -29.310  1.00 55.16           H  
ATOM   3209 HG22 VAL B 140     -23.122  -0.590 -29.905  1.00 55.16           H  
ATOM   3210 HG23 VAL B 140     -24.129   0.297 -31.029  1.00 55.16           H  
ATOM   3211  N   SER B 141     -26.015  -2.206 -33.161  1.00 49.76           N  
ANISOU 3211  N   SER B 141     7326   5315   6267     23   -384     94
ATOM   3212  CA  SER B 141     -26.309  -1.694 -34.501  1.00 49.23           C  
ANISOU 3212  CA  SER B 141     7275   5226   6204     52   -387     66
ATOM   3213  C   SER B 141     -26.817  -0.233 -34.440  1.00 48.09           C  
ANISOU 3213  C   SER B 141     7045   5168   6058     97   -351     51
ATOM   3214  O   SER B 141     -27.919   0.003 -33.944  1.00 47.62           O  
ANISOU 3214  O   SER B 141     6897   5218   5979     77   -360     72
ATOM   3215  CB  SER B 141     -27.346  -2.625 -35.161  1.00 51.36           C  
ANISOU 3215  CB  SER B 141     7590   5477   6446    -38   -453     95
ATOM   3216  OG  SER B 141     -26.839  -3.951 -35.239  1.00 56.31           O  
ANISOU 3216  OG  SER B 141     8363   5980   7052    -52   -499     99
ATOM   3217  H   SER B 141     -26.736  -2.768 -32.701  1.00 49.76           H  
ATOM   3218  HA  SER B 141     -25.395  -1.730 -35.092  1.00 49.23           H  
ATOM   3219  HB3 SER B 141     -27.593  -2.273 -36.163  1.00 51.36           H  
ATOM   3220  HB2 SER B 141     -28.279  -2.634 -34.591  1.00 51.36           H  
ATOM   3221  HG  SER B 141     -27.022  -4.344 -34.369  1.00 56.31           H  
ATOM   3222  N   VAL B 142     -26.038   0.724 -34.964  1.00 48.08           N  
ANISOU 3222  N   VAL B 142     7084   5128   6054    158   -317     10
ATOM   3223  CA  VAL B 142     -26.279   2.168 -34.820  1.00 49.31           C  
ANISOU 3223  CA  VAL B 142     7239   5317   6182    217   -298    -11
ATOM   3224  C   VAL B 142     -26.993   2.826 -36.026  1.00 49.27           C  
ANISOU 3224  C   VAL B 142     7296   5282   6141    262   -331    -32
ATOM   3225  O   VAL B 142     -27.329   4.008 -35.958  1.00 49.94           O  
ANISOU 3225  O   VAL B 142     7435   5364   6176    337   -336    -55
ATOM   3226  CB  VAL B 142     -24.942   2.927 -34.586  1.00 51.80           C  
ANISOU 3226  CB  VAL B 142     7603   5600   6479    218   -244    -38
ATOM   3227  CG1 VAL B 142     -24.325   2.591 -33.222  1.00 51.60           C  
ANISOU 3227  CG1 VAL B 142     7508   5621   6477    199   -217    -21
ATOM   3228  CG2 VAL B 142     -23.897   2.726 -35.706  1.00 53.54           C  
ANISOU 3228  CG2 VAL B 142     7892   5768   6683    184   -229    -69
ATOM   3229  H   VAL B 142     -25.192   0.445 -35.453  1.00 48.08           H  
ATOM   3230  HA  VAL B 142     -26.918   2.345 -33.948  1.00 49.31           H  
ATOM   3231  HB  VAL B 142     -25.185   3.989 -34.549  1.00 51.80           H  
ATOM   3232 HG11 VAL B 142     -23.466   3.228 -33.007  1.00 51.60           H  
ATOM   3233 HG12 VAL B 142     -25.043   2.739 -32.417  1.00 51.60           H  
ATOM   3234 HG13 VAL B 142     -23.997   1.551 -33.182  1.00 51.60           H  
ATOM   3235 HG21 VAL B 142     -22.979   3.272 -35.501  1.00 53.54           H  
ATOM   3236 HG22 VAL B 142     -23.603   1.682 -35.788  1.00 53.54           H  
ATOM   3237 HG23 VAL B 142     -24.254   3.055 -36.682  1.00 53.54           H  
ATOM   3238  N   GLY B 143     -27.209   2.084 -37.107  1.00 48.88           N  
ANISOU 3238  N   GLY B 143     7269   5199   6106    225   -363    -27
ATOM   3239  CA  GLY B 143     -27.799   2.589 -38.340  1.00 49.20           C  
ANISOU 3239  CA  GLY B 143     7368   5210   6114    261   -400    -45
ATOM   3240  C   GLY B 143     -27.342   1.654 -39.453  1.00 48.96           C  
ANISOU 3240  C   GLY B 143     7391   5107   6105    202   -416    -46
ATOM   3241  O   GLY B 143     -26.609   0.698 -39.200  1.00 50.56           O  
ANISOU 3241  O   GLY B 143     7587   5287   6335    154   -411    -33
ATOM   3242  H   GLY B 143     -26.853   1.135 -37.148  1.00 48.88           H  
ATOM   3243  HA3 GLY B 143     -27.474   3.606 -38.557  1.00 49.20           H  
ATOM   3244  HA2 GLY B 143     -28.886   2.589 -38.278  1.00 49.20           H  
ATOM   3245  N   CYS B 144     -27.766   1.917 -40.693  1.00 47.14           N  
ANISOU 3245  N   CYS B 144     7228   4836   5848    222   -445    -63
ATOM   3246  CA  CYS B 144     -27.394   1.104 -41.849  1.00 46.20           C  
ANISOU 3246  CA  CYS B 144     7168   4649   5738    176   -464    -69
ATOM   3247  C   CYS B 144     -26.807   1.998 -42.941  1.00 44.07           C  
ANISOU 3247  C   CYS B 144     7009   4308   5427    188   -446   -106
ATOM   3248  O   CYS B 144     -27.110   3.196 -43.000  1.00 43.00           O  
ANISOU 3248  O   CYS B 144     6937   4157   5244    228   -448   -119
ATOM   3249  CB  CYS B 144     -28.613   0.304 -42.355  1.00 47.98           C  
ANISOU 3249  CB  CYS B 144     7361   4910   5959    140   -530    -43
ATOM   3250  SG  CYS B 144     -29.369  -0.800 -41.123  1.00 52.72           S  
ANISOU 3250  SG  CYS B 144     7859   5607   6565     45   -557      8
ATOM   3251  H   CYS B 144     -28.301   2.751 -40.899  1.00 47.14           H  
ATOM   3252  HA  CYS B 144     -26.606   0.404 -41.577  1.00 46.20           H  
ATOM   3253  HB3 CYS B 144     -28.322  -0.288 -43.223  1.00 47.98           H  
ATOM   3254  HB2 CYS B 144     -29.386   0.988 -42.692  1.00 47.98           H  
ATOM   3255  N   THR B 145     -25.976   1.387 -43.780  1.00 43.93           N  
ANISOU 3255  N   THR B 145     7035   4250   5407    155   -434   -127
ATOM   3256  CA  THR B 145     -25.371   2.027 -44.931  1.00 45.32           C  
ANISOU 3256  CA  THR B 145     7309   4386   5526    132   -415   -163
ATOM   3257  C   THR B 145     -25.470   1.045 -46.113  1.00 47.32           C  
ANISOU 3257  C   THR B 145     7602   4597   5783    126   -454   -171
ATOM   3258  O   THR B 145     -25.562  -0.170 -45.893  1.00 47.41           O  
ANISOU 3258  O   THR B 145     7583   4599   5831    130   -492   -151
ATOM   3259  CB  THR B 145     -23.904   2.430 -44.617  1.00 45.92           C  
ANISOU 3259  CB  THR B 145     7381   4513   5553     88   -345   -198
ATOM   3260  OG1 THR B 145     -23.411   3.355 -45.569  1.00 45.21           O  
ANISOU 3260  OG1 THR B 145     7403   4402   5373     20   -327   -223
ATOM   3261  CG2 THR B 145     -22.904   1.265 -44.492  1.00 46.54           C  
ANISOU 3261  CG2 THR B 145     7398   4648   5636    110   -327   -227
ATOM   3262  H   THR B 145     -25.812   0.382 -43.717  1.00 43.93           H  
ATOM   3263  HA  THR B 145     -25.924   2.927 -45.202  1.00 45.32           H  
ATOM   3264  HB  THR B 145     -23.916   2.965 -43.673  1.00 45.92           H  
ATOM   3265  HG1 THR B 145     -23.575   4.249 -45.223  1.00 45.21           H  
ATOM   3266 HG21 THR B 145     -21.922   1.618 -44.191  1.00 46.54           H  
ATOM   3267 HG22 THR B 145     -23.227   0.543 -43.740  1.00 46.54           H  
ATOM   3268 HG23 THR B 145     -22.781   0.733 -45.433  1.00 46.54           H  
ATOM   3269  N   CYS B 146     -25.491   1.593 -47.328  1.00 47.92           N  
ANISOU 3269  N   CYS B 146     7771   4633   5804    104   -455   -196
ATOM   3270  CA  CYS B 146     -25.562   0.837 -48.570  1.00 49.23           C  
ANISOU 3270  CA  CYS B 146     7983   4757   5966    101   -492   -207
ATOM   3271  C   CYS B 146     -24.128   0.548 -49.025  1.00 50.63           C  
ANISOU 3271  C   CYS B 146     8173   4973   6091     88   -444   -259
ATOM   3272  O   CYS B 146     -23.373   1.506 -49.189  1.00 49.80           O  
ANISOU 3272  O   CYS B 146     8091   4918   5914     32   -393   -288
ATOM   3273  CB  CYS B 146     -26.332   1.643 -49.635  1.00 48.34           C  
ANISOU 3273  CB  CYS B 146     7961   4588   5819     98   -536   -202
ATOM   3274  SG  CYS B 146     -26.623   0.714 -51.158  1.00 51.71           S  
ANISOU 3274  SG  CYS B 146     8446   4962   6240     86   -587   -212
ATOM   3275  H   CYS B 146     -25.368   2.591 -47.426  1.00 47.92           H  
ATOM   3276  HA  CYS B 146     -26.101  -0.092 -48.390  1.00 49.23           H  
ATOM   3277  HB3 CYS B 146     -25.780   2.544 -49.897  1.00 48.34           H  
ATOM   3278  HB2 CYS B 146     -27.295   1.977 -49.248  1.00 48.34           H  
ATOM   3279  N   VAL B 147     -23.772  -0.730 -49.197  1.00 52.04           N  
ANISOU 3279  N   VAL B 147     8347   5147   6280    137   -467   -277
ATOM   3280  CA  VAL B 147     -22.469  -1.162 -49.690  1.00 54.51           C  
ANISOU 3280  CA  VAL B 147     8652   5542   6519    176   -429   -345
ATOM   3281  C   VAL B 147     -22.621  -2.003 -50.961  1.00 57.90           C  
ANISOU 3281  C   VAL B 147     9168   5915   6915    213   -474   -373
ATOM   3282  O   VAL B 147     -23.639  -2.678 -51.148  1.00 58.15           O  
ANISOU 3282  O   VAL B 147     9273   5831   6992    210   -544   -334
ATOM   3283  CB  VAL B 147     -21.705  -2.049 -48.658  1.00 54.64           C  
ANISOU 3283  CB  VAL B 147     8600   5629   6531    267   -417   -369
ATOM   3284  CG1 VAL B 147     -21.301  -1.273 -47.398  1.00 54.10           C  
ANISOU 3284  CG1 VAL B 147     8438   5636   6480    226   -364   -351
ATOM   3285  CG2 VAL B 147     -22.419  -3.364 -48.282  1.00 55.51           C  
ANISOU 3285  CG2 VAL B 147     8786   5617   6689    326   -499   -335
ATOM   3286  H   VAL B 147     -24.477  -1.463 -49.112  1.00 52.04           H  
ATOM   3287  HA  VAL B 147     -21.870  -0.294 -49.946  1.00 54.51           H  
ATOM   3288  HB  VAL B 147     -20.764  -2.346 -49.124  1.00 54.64           H  
ATOM   3289 HG11 VAL B 147     -20.755  -1.906 -46.700  1.00 54.10           H  
ATOM   3290 HG12 VAL B 147     -20.654  -0.434 -47.638  1.00 54.10           H  
ATOM   3291 HG13 VAL B 147     -22.180  -0.884 -46.888  1.00 54.10           H  
ATOM   3292 HG21 VAL B 147     -21.907  -3.873 -47.468  1.00 55.51           H  
ATOM   3293 HG22 VAL B 147     -23.439  -3.175 -47.952  1.00 55.51           H  
ATOM   3294 HG23 VAL B 147     -22.466  -4.063 -49.117  1.00 55.51           H  
ATOM   3295  N   THR B 148     -21.559  -2.011 -51.771  1.00 60.27           N  
ANISOU 3295  N   THR B 148     9457   6322   7120    235   -432   -444
ATOM   3296  CA  THR B 148     -21.359  -2.998 -52.824  1.00 64.12           C  
ANISOU 3296  CA  THR B 148    10025   6783   7555    300   -469   -489
ATOM   3297  C   THR B 148     -21.004  -4.363 -52.156  1.00 66.71           C  
ANISOU 3297  C   THR B 148    10378   7104   7865    462   -513   -523
ATOM   3298  O   THR B 148     -20.211  -4.381 -51.198  1.00 67.16           O  
ANISOU 3298  O   THR B 148    10343   7290   7885    538   -476   -561
ATOM   3299  CB  THR B 148     -20.166  -2.537 -53.703  1.00 66.87           C  
ANISOU 3299  CB  THR B 148    10334   7291   7781    261   -403   -559
ATOM   3300  OG1 THR B 148     -19.000  -2.310 -52.922  1.00 69.22           O  
ANISOU 3300  OG1 THR B 148    10497   7799   8006    266   -331   -607
ATOM   3301  CG2 THR B 148     -20.462  -1.242 -54.480  1.00 67.40           C  
ANISOU 3301  CG2 THR B 148    10458   7310   7841    102   -386   -522
ATOM   3302  H   THR B 148     -20.762  -1.403 -51.599  1.00 60.27           H  
ATOM   3303  HA  THR B 148     -22.270  -3.037 -53.423  1.00 64.12           H  
ATOM   3304  HB  THR B 148     -19.946  -3.323 -54.429  1.00 66.87           H  
ATOM   3305  HG1 THR B 148     -18.720  -3.152 -52.555  1.00 69.22           H  
ATOM   3306 HG21 THR B 148     -19.617  -0.943 -55.103  1.00 67.40           H  
ATOM   3307 HG22 THR B 148     -21.316  -1.372 -55.143  1.00 67.40           H  
ATOM   3308 HG23 THR B 148     -20.678  -0.409 -53.811  1.00 67.40           H  
ATOM   3309  N   PRO B 149     -21.623  -5.477 -52.606  1.00 68.58           N  
ANISOU 3309  N   PRO B 149    10763   7176   8118    509   -603   -504
ATOM   3310  CA  PRO B 149     -21.331  -6.811 -52.050  1.00 70.52           C  
ANISOU 3310  CA  PRO B 149    11108   7356   8330    653   -670   -523
ATOM   3311  C   PRO B 149     -19.881  -7.270 -52.291  1.00 73.52           C  
ANISOU 3311  C   PRO B 149    11490   7866   8577    869   -666   -637
ATOM   3312  O   PRO B 149     -19.266  -6.873 -53.279  1.00 74.03           O  
ANISOU 3312  O   PRO B 149    11541   8029   8559    915   -642   -706
ATOM   3313  CB  PRO B 149     -22.340  -7.736 -52.754  1.00 70.59           C  
ANISOU 3313  CB  PRO B 149    11315   7150   8355    599   -774   -471
ATOM   3314  CG  PRO B 149     -22.678  -7.034 -54.059  1.00 70.31           C  
ANISOU 3314  CG  PRO B 149    11266   7117   8333    504   -756   -466
ATOM   3315  CD  PRO B 149     -22.614  -5.558 -53.681  1.00 68.16           C  
ANISOU 3315  CD  PRO B 149    10815   6981   8100    417   -659   -457
ATOM   3316  HA  PRO B 149     -21.525  -6.806 -50.978  1.00 70.52           H  
ATOM   3317  HB3 PRO B 149     -23.236  -7.819 -52.142  1.00 70.59           H  
ATOM   3318  HB2 PRO B 149     -21.972  -8.749 -52.911  1.00 70.59           H  
ATOM   3319  HG3 PRO B 149     -23.642  -7.326 -54.479  1.00 70.31           H  
ATOM   3320  HG2 PRO B 149     -21.912  -7.250 -54.806  1.00 70.31           H  
ATOM   3321  HD2 PRO B 149     -22.368  -4.959 -54.555  1.00 68.16           H  
ATOM   3322  HD3 PRO B 149     -23.578  -5.218 -53.302  1.00 68.16           H  
ATOM   3323  N   VAL B 151     -18.058 -10.332 -53.544  1.00 80.86           N  
ANISOU 3323  N   VAL B 151    12769   8825   9131   1548   -843   -897
ATOM   3324  CA  VAL B 151     -18.327 -11.497 -54.375  1.00 83.10           C  
ANISOU 3324  CA  VAL B 151    13340   8918   9318   1691   -960   -935
ATOM   3325  C   VAL B 151     -17.038 -12.334 -54.459  1.00 85.67           C  
ANISOU 3325  C   VAL B 151    13755   9359   9437   2076  -1021  -1083
ATOM   3326  O   VAL B 151     -15.950 -11.767 -54.567  1.00 86.22           O  
ANISOU 3326  O   VAL B 151    13581   9769   9409   2212   -937  -1191
ATOM   3327  CB  VAL B 151     -18.736 -11.042 -55.807  1.00 83.58           C  
ANISOU 3327  CB  VAL B 151    13373   8980   9403   1545   -922   -926
ATOM   3328  CG1 VAL B 151     -18.953 -12.197 -56.811  1.00 83.87           C  
ANISOU 3328  CG1 VAL B 151    13705   8833   9328   1688  -1038   -973
ATOM   3329  CG2 VAL B 151     -19.995 -10.152 -55.771  1.00 83.78           C  
ANISOU 3329  CG2 VAL B 151    13344   8885   9604   1221   -889   -791
ATOM   3330  H   VAL B 151     -17.455  -9.640 -53.962  1.00 80.86           H  
ATOM   3331  HA  VAL B 151     -19.126 -12.104 -53.944  1.00 83.10           H  
ATOM   3332  HB  VAL B 151     -17.927 -10.428 -56.214  1.00 83.58           H  
ATOM   3333 HG11 VAL B 151     -19.311 -11.820 -57.771  1.00 83.87           H  
ATOM   3334 HG12 VAL B 151     -18.032 -12.743 -57.022  1.00 83.87           H  
ATOM   3335 HG13 VAL B 151     -19.691 -12.914 -56.449  1.00 83.87           H  
ATOM   3336 HG21 VAL B 151     -20.285  -9.831 -56.773  1.00 83.78           H  
ATOM   3337 HG22 VAL B 151     -20.844 -10.682 -55.338  1.00 83.78           H  
ATOM   3338 HG23 VAL B 151     -19.838  -9.245 -55.186  1.00 83.78           H  
ATOM   3339  N   HIS B 152     -17.182 -13.661 -54.411  1.00 86.92           N  
ANISOU 3339  N   HIS B 152    14276   9249   9501   2250  -1174  -1094
ATOM   3340  CA  HIS B 152     -16.113 -14.639 -54.589  1.00 88.59           C  
ANISOU 3340  CA  HIS B 152    14643   9528   9488   2669  -1264  -1244
ATOM   3341  C   HIS B 152     -16.759 -15.996 -54.911  1.00 90.08           C  
ANISOU 3341  C   HIS B 152    15330   9327   9571   2786  -1451  -1234
ATOM   3342  O   HIS B 152     -17.933 -16.199 -54.598  1.00 89.50           O  
ANISOU 3342  O   HIS B 152    15488   8950   9567   2590  -1529  -1113
ATOM   3343  CB  HIS B 152     -15.188 -14.707 -53.347  1.00 89.61           C  
ANISOU 3343  CB  HIS B 152    14643   9851   9553   2882  -1255  -1303
ATOM   3344  CG  HIS B 152     -15.855 -14.983 -52.019  1.00 92.09           C  
ANISOU 3344  CG  HIS B 152    15080   9928   9982   2719  -1299  -1178
ATOM   3345  ND1 HIS B 152     -16.656 -14.054 -51.374  1.00 94.07           N  
ANISOU 3345  ND1 HIS B 152    15713   9912  10118   2909  -1462  -1181
ATOM   3346  CD2 HIS B 152     -15.825 -16.082 -51.191  1.00 93.27           C  
ANISOU 3346  CD2 HIS B 152    15035  10075  10329   2386  -1207  -1051
ATOM   3347  CE1 HIS B 152     -17.072 -14.612 -50.235  1.00 94.61           C  
ANISOU 3347  CE1 HIS B 152    15784   9844  10321   2663  -1453  -1053
ATOM   3348  NE2 HIS B 152     -16.603 -15.841 -50.056  1.00 94.55           N  
ANISOU 3348  NE2 HIS B 152    15424   9996  10504   2358  -1301   -976
ATOM   3349  H   HIS B 152     -18.092 -14.100 -54.321  1.00 86.92           H  
ATOM   3350  HA  HIS B 152     -15.521 -14.337 -55.456  1.00 88.59           H  
ATOM   3351  HB3 HIS B 152     -14.643 -13.769 -53.249  1.00 89.61           H  
ATOM   3352  HB2 HIS B 152     -14.420 -15.469 -53.501  1.00 89.61           H  
ATOM   3353  HD1 HIS B 152     -16.894 -13.134 -51.717  1.00 94.07           H  
ATOM   3354  HD2 HIS B 152     -15.300 -17.015 -51.319  1.00 93.27           H  
ATOM   3355  HE1 HIS B 152     -17.715 -14.111 -49.525  1.00 94.61           H  
ATOM   3356  N   HIS B 153     -15.972 -16.881 -55.525  1.00 91.88           N  
ANISOU 3356  N   HIS B 153    15735   9571   9603   3098  -1528  -1364
ATOM   3357  CA  HIS B 153     -16.279 -18.297 -55.683  1.00 93.92           C  
ANISOU 3357  CA  HIS B 153    16532   9451   9703   3269  -1729  -1379
ATOM   3358  C   HIS B 153     -15.463 -18.997 -54.587  1.00 96.22           C  
ANISOU 3358  C   HIS B 153    17011   9711   9837   3616  -1838  -1450
ATOM   3359  O   HIS B 153     -14.305 -18.629 -54.381  1.00 96.76           O  
ANISOU 3359  O   HIS B 153    16778  10154   9831   3887  -1767  -1570
ATOM   3360  CB  HIS B 153     -15.835 -18.742 -57.097  1.00 94.43           C  
ANISOU 3360  CB  HIS B 153    16691   9596   9595   3537  -1765  -1517
ATOM   3361  CG  HIS B 153     -16.418 -20.041 -57.617  1.00 96.20           C  
ANISOU 3361  CG  HIS B 153    17484   9395   9671   3622  -1961  -1514
ATOM   3362  ND1 HIS B 153     -16.248 -21.276 -57.004  1.00 97.98           N  
ANISOU 3362  ND1 HIS B 153    18179   9350   9698   3910  -2153  -1556
ATOM   3363  CD2 HIS B 153     -17.176 -20.299 -58.740  1.00 97.23           C  
ANISOU 3363  CD2 HIS B 153    17796   9347   9799   3476  -1997  -1485
ATOM   3364  CE1 HIS B 153     -16.903 -22.178 -57.737  1.00 98.47           C  
ANISOU 3364  CE1 HIS B 153    18713   9058   9645   3896  -2300  -1543
ATOM   3365  NE2 HIS B 153     -17.491 -21.656 -58.807  1.00 98.37           N  
ANISOU 3365  NE2 HIS B 153    18531   9097   9747   3638  -2210  -1501
ATOM   3366  H   HIS B 153     -14.989 -16.674 -55.627  1.00 91.88           H  
ATOM   3367  HA  HIS B 153     -17.349 -18.477 -55.553  1.00 93.92           H  
ATOM   3368  HB3 HIS B 153     -14.747 -18.818 -57.156  1.00 94.43           H  
ATOM   3369  HB2 HIS B 153     -16.115 -17.972 -57.816  1.00 94.43           H  
ATOM   3370  HD1 HIS B 153     -15.734 -21.517 -56.153  1.00 97.98           H  
ATOM   3371  HD2 HIS B 153     -17.512 -19.614 -59.505  1.00 97.23           H  
ATOM   3372  HE1 HIS B 153     -16.942 -23.226 -57.480  1.00 98.47           H  
ATOM   3373  N   ALA B 155     -13.980 -22.764 -52.873  1.00100.86           N  
ANISOU 3373  N   ALA B 155    18911   9721   9689   4851  -2425  -1705
ATOM   3374  CA  ALA B 155     -13.438 -24.077 -53.294  1.00102.29           C  
ANISOU 3374  CA  ALA B 155    19594   9730   9540   5380  -2640  -1859
ATOM   3375  C   ALA B 155     -14.206 -25.319 -52.668  1.00102.77           C  
ANISOU 3375  C   ALA B 155    20388   9192   9466   5321  -2878  -1764
ATOM   3376  O   ALA B 155     -14.656 -25.160 -51.507  1.00103.04           O  
ANISOU 3376  O   ALA B 155    20448   9056   9645   4952  -2863  -1604
ATOM   3377  CB  ALA B 155     -11.946 -24.115 -52.899  1.00102.87           C  
ANISOU 3377  CB  ALA B 155    19421  10231   9436   5932  -2634  -2054
ATOM   3378  OXT ALA B 155     -14.157 -26.360 -53.356  1.00103.08           O1-
ANISOU 3378  OXT ALA B 155    20991   8938   9236   5636  -3083  -1850
ATOM   3379  H   ALA B 155     -13.707 -22.494 -51.941  1.00100.86           H  
ATOM   3380  HA  ALA B 155     -13.493 -24.178 -54.380  1.00102.29           H  
ATOM   3381  HB1 ALA B 155     -11.483 -25.050 -53.213  1.00102.87           H  
ATOM   3382  HB2 ALA B 155     -11.383 -23.309 -53.361  1.00102.87           H  
ATOM   3383  HB3 ALA B 155     -11.823 -24.044 -51.820  1.00102.87           H  
ATOM   3384  N   ILE B 150     -19.367  -8.108 -51.384  1.00 75.17           N  
ANISOU 3384  N   ILE B 150    11726   8087   8749   1018   -699   -661
ATOM   3385  CA  ILE B 150     -18.126  -8.847 -51.605  1.00 77.52           C  
ANISOU 3385  CA  ILE B 150    12037   8523   8896   1285   -718   -781
ATOM   3386  C   ILE B 150     -18.512 -10.162 -52.301  1.00 79.42           C  
ANISOU 3386  C   ILE B 150    12569   8553   9055   1433   -845   -808
ATOM   3387  O   ILE B 150     -19.222 -10.969 -51.703  1.00 79.25           O  
ANISOU 3387  O   ILE B 150    12769   8294   9050   1430   -946   -749
ATOM   3388  CB  ILE B 150     -17.380  -9.162 -50.269  1.00  0.00           C  
ATOM   3389  CG1 ILE B 150     -16.818  -7.859 -49.662  1.00  0.00           C  
ATOM   3390  CG2 ILE B 150     -16.251 -10.214 -50.402  1.00  0.00           C  
ATOM   3391  CD1 ILE B 150     -16.271  -8.020 -48.236  1.00  0.00           C  
ATOM   3392  H   ILE B 150     -19.970  -8.488 -50.671  1.00 75.17           H  
ATOM   3393  HA  ILE B 150     -17.450  -8.288 -52.258  1.00 77.52           H  
ATOM   3394  HB  ILE B 150     -18.111  -9.567 -49.569  1.00  0.00           H  
ATOM   3395 HG13 ILE B 150     -17.592  -7.096 -49.655  1.00  0.00           H  
ATOM   3396 HG12 ILE B 150     -16.021  -7.472 -50.301  1.00  0.00           H  
ATOM   3397 HG21 ILE B 150     -16.619 -11.182 -50.738  1.00  0.00           H  
ATOM   3398 HG22 ILE B 150     -15.485  -9.892 -51.107  1.00  0.00           H  
ATOM   3399 HG23 ILE B 150     -15.762 -10.416 -49.447  1.00  0.00           H  
ATOM   3400 HD11 ILE B 150     -16.016  -7.054 -47.805  1.00  0.00           H  
ATOM   3401 HD12 ILE B 150     -16.991  -8.512 -47.581  1.00  0.00           H  
ATOM   3402 HD13 ILE B 150     -15.349  -8.598 -48.237  1.00  0.00           H  
ATOM   3403  N   VAL B 154     -16.071 -19.957 -53.893  1.00 97.38           N  
ANISOU 3403  N   VAL B 154    17640   9441   9917   3589  -2009  -1376
ATOM   3404  CA  VAL B 154     -15.418 -20.759 -52.859  1.00 99.30           C  
ANISOU 3404  CA  VAL B 154    18092   9639   9997   3932  -2124  -1444
ATOM   3405  C   VAL B 154     -14.945 -22.087 -53.502  1.00100.14           C  
ANISOU 3405  C   VAL B 154    18716   9537   9795   4393  -2334  -1580
ATOM   3406  O   VAL B 154     -15.413 -22.416 -54.595  1.00100.10           O  
ANISOU 3406  O   VAL B 154    19002   9314   9717   4363  -2413  -1582
ATOM   3407  CB  VAL B 154     -16.418 -20.997 -51.690  1.00  0.00           C  
ATOM   3408  CG1 VAL B 154     -15.902 -21.886 -50.546  1.00  0.00           C  
ATOM   3409  CG2 VAL B 154     -16.861 -19.658 -51.063  1.00  0.00           C  
ATOM   3410  H   VAL B 154     -16.988 -20.283 -54.155  1.00 97.38           H  
ATOM   3411  HA  VAL B 154     -14.539 -20.245 -52.469  1.00 99.30           H  
ATOM   3412  HB  VAL B 154     -17.312 -21.474 -52.095  1.00  0.00           H  
ATOM   3413 HG11 VAL B 154     -15.798 -22.923 -50.844  1.00  0.00           H  
ATOM   3414 HG12 VAL B 154     -14.940 -21.545 -50.165  1.00  0.00           H  
ATOM   3415 HG13 VAL B 154     -16.606 -21.888 -49.712  1.00  0.00           H  
ATOM   3416 HG21 VAL B 154     -17.286 -18.971 -51.797  1.00  0.00           H  
ATOM   3417 HG22 VAL B 154     -17.626 -19.806 -50.299  1.00  0.00           H  
ATOM   3418 HG23 VAL B 154     -16.015 -19.161 -50.587  1.00  0.00           H  
ATOM   3419  N   ASN B  40      -2.619   6.579 -13.563  1.00 77.18           N  
ANISOU 3419  N   ASN B  40     8588  12914   7822   -767    289   -634
ATOM   3420  CA  ASN B  40      -3.205   5.873 -12.393  1.00 77.56           C  
ANISOU 3420  CA  ASN B  40     8731  12682   8055   -496    237   -581
ATOM   3421  C   ASN B  40      -4.499   5.122 -12.840  1.00 77.14           C  
ANISOU 3421  C   ASN B  40     8862  12221   8228   -271    202   -524
ATOM   3422  O   ASN B  40      -5.498   5.766 -13.176  1.00 77.79           O  
ANISOU 3422  O   ASN B  40     9136  12005   8414   -410    232   -460
ATOM   3423  CB  ASN B  40      -3.506   6.868 -11.238  1.00  0.00           C  
ATOM   3424  CG  ASN B  40      -2.293   7.336 -10.430  1.00  0.00           C  
ATOM   3425  OD1 ASN B  40      -1.247   6.699 -10.409  1.00  0.00           O  
ATOM   3426  ND2 ASN B  40      -2.423   8.448  -9.713  1.00  0.00           N  
ATOM   3427  H1  ASN B  40      -1.762   7.044 -13.299  1.00 77.18           H  
ATOM   3428  H2  ASN B  40      -2.354   5.926 -14.287  1.00 77.18           H  
ATOM   3429  HA  ASN B  40      -2.505   5.117 -12.028  1.00 77.56           H  
ATOM   3430  HB2 ASN B  40      -3.999   7.746 -11.656  1.00  0.00           H  
ATOM   3431  HB3 ASN B  40      -4.202   6.427 -10.521  1.00  0.00           H  
ATOM   3432 HD22 ASN B  40      -1.632   8.769  -9.177  1.00  0.00           H  
ATOM   3433 HD21 ASN B  40      -3.267   8.998  -9.746  1.00  0.00           H  
ATOM   3434  N   ASP B  65     -34.606  12.222 -39.503  1.00 73.91           N  
ANISOU 3434  N   ASP B  65    11421   8471   8189   2088  -1000   -455
ATOM   3435  CA  ASP B  65     -35.270  11.346 -40.485  1.00 71.95           C  
ANISOU 3435  CA  ASP B  65    10910   8431   7997   2045  -1007   -447
ATOM   3436  C   ASP B  65     -34.346  10.507 -41.391  1.00 68.74           C  
ANISOU 3436  C   ASP B  65    10513   7864   7742   1729   -940   -377
ATOM   3437  O   ASP B  65     -34.815   9.929 -42.373  1.00 68.50           O  
ANISOU 3437  O   ASP B  65    10376   7915   7735   1691   -964   -371
ATOM   3438  CB  ASP B  65     -36.256  12.130 -41.394  1.00  0.00           C  
ATOM   3439  CG  ASP B  65     -37.409  12.849 -40.705  1.00  0.00           C  
ATOM   3440  OD1 ASP B  65     -37.802  12.404 -39.610  1.00  0.00           O  
ATOM   3441  OD2 ASP B  65     -37.972  13.726 -41.394  1.00  0.00           O1-
ATOM   3442  H   ASP B  65     -35.016  13.145 -39.393  1.00 73.91           H  
ATOM   3443  HA  ASP B  65     -35.850  10.637 -39.895  1.00 71.95           H  
ATOM   3444  HB2 ASP B  65     -35.705  12.893 -41.938  1.00  0.00           H  
ATOM   3445  HB3 ASP B  65     -36.723  11.473 -42.129  1.00  0.00           H  
TER    3446      ASP B  65
HETATM 3447  C1  UNK B 201     -22.007   4.081 -20.638  1.00 61.97           C  
ANISOU 3447  C1  UNK B 201    10216   6387   6942   1788  -1272    113
HETATM 3448  C2  UNK B 201     -21.954   4.493 -19.158  1.00 62.94           C  
ANISOU 3448  C2  UNK B 201    10532   6560   6823   1752  -1532    -68
HETATM 3449  C3  UNK B 201     -20.596   4.155 -18.531  1.00 63.86           C  
ANISOU 3449  C3  UNK B 201    10968   6735   6560   1862  -1302    -67
HETATM 3450  C14 UNK B 201     -24.455   3.858 -24.282  1.00 65.54           C  
ANISOU 3450  C14 UNK B 201    10442   7172   7290   1603   -884   -163
HETATM 3451  C16 UNK B 201     -26.608   4.454 -25.314  1.00 68.80           C  
ANISOU 3451  C16 UNK B 201    10360   7953   7827   1593  -1274    -68
HETATM 3452  C17 UNK B 201     -26.460   3.116 -25.035  1.00 67.47           C  
ANISOU 3452  C17 UNK B 201    10268   7692   7674   1410  -1055   -398
HETATM 3453  C19 UNK B 201     -27.749   5.134 -25.999  1.00 71.27           C  
ANISOU 3453  C19 UNK B 201    10283   8527   8272   1687  -1632    170
HETATM 3454  C21 UNK B 201     -26.811   4.742 -28.323  1.00 74.63           C  
ANISOU 3454  C21 UNK B 201    11030   9738   7588   1496  -2001    339
HETATM 3455  C22 UNK B 201     -27.363   3.991 -29.541  1.00 76.01           C  
ANISOU 3455  C22 UNK B 201    11167  10577   7138   1236  -2372     62
HETATM 3456  C24 UNK B 201     -28.996   4.070 -27.889  1.00 73.40           C  
ANISOU 3456  C24 UNK B 201    10215   9689   7986   1289  -2292   -135
HETATM 3457  C26 UNK B 201     -26.652   2.658 -29.834  1.00 78.30           C  
ANISOU 3457  C26 UNK B 201    11833  10812   7107    985  -1974   -529
HETATM 3458  C30 UNK B 201     -19.153   4.501 -24.764  1.00 61.77           C  
ANISOU 3458  C30 UNK B 201     9907   6556   7009   1674   -722    349
HETATM 3459  C4  UNK B 201     -19.454   4.797 -19.327  1.00 63.20           C  
ANISOU 3459  C4  UNK B 201    10888   6518   6608   1855   -943   -172
HETATM 3460  C5  UNK B 201     -19.500   4.352 -20.795  1.00 62.30           C  
ANISOU 3460  C5  UNK B 201    10525   6370   6777   1818   -881    -78
HETATM 3461  C6  UNK B 201     -20.852   4.699 -21.472  1.00 61.83           C  
ANISOU 3461  C6  UNK B 201    10279   6323   6890   1768  -1061     23
HETATM 3462  F7  UNK B 201     -20.556   4.592 -17.273  1.00 64.39           F  
ANISOU 3462  F7  UNK B 201    11298   6939   6226   1834  -1447   -262
HETATM 3463  F8  UNK B 201     -20.439   2.832 -18.519  1.00 64.88           F  
ANISOU 3463  F8  UNK B 201    11106   6903   6641   1996  -1240    237
HETATM 3464  C9  UNK B 201     -20.869   4.254 -22.969  1.00 61.26           C  
ANISOU 3464  C9  UNK B 201    10086   6348   6841   1736   -911    102
HETATM 3465  C10 UNK B 201     -22.208   4.640 -23.630  1.00 61.62           C  
ANISOU 3465  C10 UNK B 201    10110   6480   6825   1707   -899     58
HETATM 3466  N11 UNK B 201     -19.800   4.963 -23.683  1.00 61.13           N  
ANISOU 3466  N11 UNK B 201     9914   6349   6965   1683   -938    275
HETATM 3467  N12 UNK B 201     -23.155   3.693 -23.739  1.00 63.07           N  
ANISOU 3467  N12 UNK B 201    10294   6713   6959   1657   -791   -111
HETATM 3468  O13 UNK B 201     -22.371   5.788 -24.029  1.00 61.71           O  
ANISOU 3468  O13 UNK B 201    10039   6486   6922   1724  -1005    220
HETATM 3469  S15 UNK B 201     -25.205   5.362 -24.823  1.00 67.28           S  
ANISOU 3469  S15 UNK B 201    10466   7514   7584   1716  -1151    139
HETATM 3470  N18 UNK B 201     -25.244   2.793 -24.426  1.00 66.34           N  
ANISOU 3470  N18 UNK B 201    10445   7310   7451   1470   -815   -380
HETATM 3471  N20 UNK B 201     -27.917   4.679 -27.377  1.00 73.23           N  
ANISOU 3471  N20 UNK B 201    10519   9311   7994   1507  -1982    141
HETATM 3472  N23 UNK B 201     -28.749   3.790 -29.168  1.00 74.69           N  
ANISOU 3472  N23 UNK B 201    10540  10400   7437   1114  -2601   -222
HETATM 3473  O25 UNK B 201     -30.040   3.800 -27.298  1.00 72.53           O  
ANISOU 3473  O25 UNK B 201     9702   9452   8405   1225  -2270   -311
HETATM 3474  F27 UNK B 201     -26.788   1.797 -28.829  1.00 78.77           F  
ANISOU 3474  F27 UNK B 201    11964  11418   6546    691  -2219   -985
HETATM 3475  F28 UNK B 201     -27.163   2.111 -30.937  1.00 79.22           F  
ANISOU 3475  F28 UNK B 201    12241  10821   7040   1132  -1635   -240
HETATM 3476  F29 UNK B 201     -25.355   2.891 -30.029  1.00 78.67           F  
ANISOU 3476  F29 UNK B 201    11833  10319   7741    918  -1650   -879
HETATM 3477  C31 UNK B 201     -18.177   5.453 -25.273  1.00 63.60           C  
ANISOU 3477  C31 UNK B 201     9941   6782   7444   1597   -629    600
HETATM 3478  O32 UNK B 201     -19.392   3.392 -25.232  1.00 60.83           O  
ANISOU 3478  O32 UNK B 201     9861   6495   6758   1707   -532    182
HETATM 3479  C33 UNK B 201     -17.447   5.262 -26.391  1.00 64.28           C  
ANISOU 3479  C33 UNK B 201     9932   7017   7476   1570   -286    742
HETATM 3480  F34 UNK B 201     -17.978   6.592 -24.596  1.00 64.62           F  
ANISOU 3480  F34 UNK B 201     9966   6692   7894   1508   -836    678
HETATM 3481  C35 UNK B 201     -17.449   4.106 -27.332  1.00 65.51           C  
ANISOU 3481  C35 UNK B 201    10219   7411   7260   1613     86    549
HETATM 3482  C36 UNK B 201     -18.478   3.991 -28.434  1.00 65.68           C  
ANISOU 3482  C36 UNK B 201    10414   7803   6738   1521    307    762
HETATM 3483  C37 UNK B 201     -17.046   4.300 -28.779  1.00 65.90           C  
ANISOU 3483  C37 UNK B 201    10112   7593   7333   1595    620    702
HETATM 3484 H1_1 UNK B 201     -22.980   4.381 -21.028  1.00 61.97           H  
HETATM 3485 H1_2 UNK B 201     -21.969   2.993 -20.713  1.00 61.97           H  
HETATM 3486 H2_1 UNK B 201     -22.138   5.565 -19.076  1.00 62.94           H  
HETATM 3487 H2_2 UNK B 201     -22.753   4.000 -18.603  1.00 62.94           H  
HETATM 3488 HC17 UNK B 201     -27.164   2.324 -25.250  1.00 67.47           H  
HETATM 3489 H191 UNK B 201     -28.662   4.974 -25.422  1.00 71.27           H  
HETATM 3490 H192 UNK B 201     -27.587   6.214 -26.013  1.00 71.27           H  
HETATM 3491 H211 UNK B 201     -26.590   5.784 -28.561  1.00 74.63           H  
HETATM 3492 H212 UNK B 201     -25.907   4.279 -27.927  1.00 74.63           H  
HETATM 3493 HC22 UNK B 201     -27.321   4.605 -30.432  1.00 76.01           H  
HETATM 3494 H4_1 UNK B 201     -19.524   5.883 -19.266  1.00 63.20           H  
HETATM 3495 H4_2 UNK B 201     -18.495   4.523 -18.886  1.00 63.20           H  
HETATM 3496 H5_1 UNK B 201     -19.331   3.275 -20.830  1.00 62.30           H  
HETATM 3497 H5_2 UNK B 201     -18.668   4.815 -21.327  1.00 62.30           H  
HETATM 3498  HC6 UNK B 201     -20.959   5.785 -21.438  1.00 61.83           H  
HETATM 3499  HC9 UNK B 201     -20.716   3.179 -23.039  1.00 61.26           H  
HETATM 3500 HC33 UNK B 201     -16.755   6.048 -26.657  1.00 64.28           H  
HETATM 3501 HC35 UNK B 201     -17.127   3.179 -26.856  1.00 65.51           H  
HETATM 3502 H361 UNK B 201     -18.840   2.993 -28.683  1.00 65.68           H  
HETATM 3503 H362 UNK B 201     -19.211   4.791 -28.528  1.00 65.68           H  
HETATM 3504 H371 UNK B 201     -16.824   5.310 -29.121  1.00 65.90           H  
HETATM 3505 H372 UNK B 201     -16.467   3.510 -29.254  1.00 65.90           H  
HETATM 3506 HN11 UNK B 201     -19.641   5.930 -23.408  1.00 61.13           H  
HETATM 3507 HN12 UNK B 201     -22.902   2.761 -23.429  1.00 63.07           H  
HETATM 3508 HN23 UNK B 201     -29.381   3.249 -29.749  1.00 74.69           H  
CONECT  240 1667
CONECT  252 1696
CONECT  552 1706
CONECT  574 1708
CONECT  710 1486
CONECT  787 1510
CONECT  827 1655
CONECT  835 1657
CONECT 1486  710
CONECT 1510  787
CONECT 1728 3421
CONECT 1948 1959
CONECT 1973 3434
CONECT 1983 3436
CONECT 2462 3250
CONECT 2539 3274
CONECT 3250 2462
CONECT 3274 2539
CONECT 3311 3384
CONECT 3323 3386
CONECT 3358 3403
CONECT 3373 3405
CONECT 1959 1948
CONECT 1655  827
CONECT 1657  835
CONECT 1667  240
CONECT 1669 1677
CONECT 1696  252
CONECT 1706  552
CONECT 1708  574
CONECT 3384 3311
CONECT 3386 3323
CONECT 3403 3358
CONECT 3405 3373
CONECT 3421 1728
CONECT 3434 1973
CONECT 3436 1983
CONECT 1677 1669
CONECT 3447 3448 3461 3484 3485
CONECT 3448 3447 3449 3486 3487
CONECT 3449 3448 3459 3462 3463
CONECT 3450 3467 3469 3470
CONECT 3450 3470
CONECT 3451 3452 3453 3469
CONECT 3451 3452
CONECT 3452 3451 3470 3488
CONECT 3452 3451
CONECT 3453 3451 3471 3489 3490
CONECT 3454 3455 3471 3491 3492
CONECT 3455 3454 3457 3472 3493
CONECT 3456 3471 3472 3473
CONECT 3456 3473
CONECT 3457 3455 3474 3475 3476
CONECT 3458 3466 3477 3478
CONECT 3458 3478
CONECT 3459 3449 3460 3494 3495
CONECT 3460 3459 3461 3496 3497
CONECT 3461 3447 3460 3464 3498
CONECT 3462 3449
CONECT 3463 3449
CONECT 3464 3461 3465 3466 3499
CONECT 3465 3464 3467 3468
CONECT 3465 3468
CONECT 3466 3458 3464 3506
CONECT 3467 3450 3465 3507
CONECT 3468 3465
CONECT 3468 3465
CONECT 3469 3450 3451
CONECT 3470 3450 3452
CONECT 3470 3450
CONECT 3471 3453 3454 3456
CONECT 3472 3455 3456 3508
CONECT 3473 3456
CONECT 3473 3456
CONECT 3474 3457
CONECT 3475 3457
CONECT 3476 3457
CONECT 3477 3458 3479 3480
CONECT 3477 3479
CONECT 3478 3458
CONECT 3478 3458
CONECT 3479 3477 3481 3500
CONECT 3479 3477
CONECT 3480 3477
CONECT 3481 3479 3482 3483 3501
CONECT 3482 3481 3483 3502 3503
CONECT 3483 3481 3482 3504 3505
CONECT 3484 3447
CONECT 3485 3447
CONECT 3486 3448
CONECT 3487 3448
CONECT 3488 3452
CONECT 3489 3453
CONECT 3490 3453
CONECT 3491 3454
CONECT 3492 3454
CONECT 3493 3455
CONECT 3494 3459
CONECT 3495 3459
CONECT 3496 3460
CONECT 3497 3460
CONECT 3498 3461
CONECT 3499 3464
CONECT 3500 3479
CONECT 3501 3481
CONECT 3502 3482
CONECT 3503 3482
CONECT 3504 3483
CONECT 3505 3483
CONECT 3506 3466
CONECT 3507 3467
CONECT 3508 3472
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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.